data_8R1Q
# 
_entry.id   8R1Q 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8R1Q         pdb_00008r1q 10.2210/pdb8r1q/pdb 
WWPDB D_1292134430 ?            ?                   
# 
_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       2024-11-13 
# 
_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                        8R1Q 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rolf.hilgenfeld@uni-luebeck.de 
_pdbx_contact_author.name_first         Hilgenfeld 
_pdbx_contact_author.name_last          Rolf 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8850-2977 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sun, X.'        1 0000-0002-2761-2862 
'Ibrahim, M.'    2 0000-0002-1431-9755 
'Hilgenfeld, R.' 3 0000-0001-8850-2977 
# 
_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                     'SARS-CoV-2 Omicron (P132H+T169S) complex with alpha-ketoamide 13b-K' 
_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 'Sun, X.'        1 0000-0002-2761-2862 
primary 'Hilgenfeld, R.' 2 0000-0001-8850-2977 
primary 'Ibrahim, M.'    3 0000-0002-1431-9755 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase nsp5' 33852.551 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
;~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate
;
595.687   2   ?         ? ? ? 
3 water       nat water 18.015    475 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPSGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRHNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPSGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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 
;~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate
;
O6K 
3 water HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 HIS n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 SER n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 
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 
O6K non-polymer         . 
;~{tert}-butyl ~{N}-[1-[(2~{S})-3-cyclopropyl-1-oxidanylidene-1-[[(2~{S},3~{R})-3-oxidanyl-4-oxidanylidene-1-[(3~{S})-2-oxidanylidenepyrrolidin-3-yl]-4-[(phenylmethyl)amino]butan-2-yl]amino]propan-2-yl]-2-oxidanylidene-pyridin-3-yl]carbamate
;
'(S,S,S)-13b; 13b-K; ketoamide inhibitor 13b (bound)' 'C31 H41 N5 O7'  595.687 
PHE 'L-peptide linking' y PHENYLALANINE ?                                                     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                                                     'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                                                     'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                                                     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN ?                                                     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE ?                                                     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE ?                                                     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER B . n 
A 1 2   GLY 2   2   2   GLY GLY B . n 
A 1 3   PHE 3   3   3   PHE PHE B . n 
A 1 4   ARG 4   4   4   ARG ARG B . n 
A 1 5   LYS 5   5   5   LYS LYS B . n 
A 1 6   MET 6   6   6   MET MET B . n 
A 1 7   ALA 7   7   7   ALA ALA B . n 
A 1 8   PHE 8   8   8   PHE PHE B . n 
A 1 9   PRO 9   9   9   PRO PRO B . n 
A 1 10  SER 10  10  10  SER SER B . n 
A 1 11  GLY 11  11  11  GLY GLY B . n 
A 1 12  LYS 12  12  12  LYS LYS B . n 
A 1 13  VAL 13  13  13  VAL VAL B . n 
A 1 14  GLU 14  14  14  GLU GLU B . n 
A 1 15  GLY 15  15  15  GLY GLY B . n 
A 1 16  CYS 16  16  16  CYS CYS B . n 
A 1 17  MET 17  17  17  MET MET B . n 
A 1 18  VAL 18  18  18  VAL VAL B . n 
A 1 19  GLN 19  19  19  GLN GLN B . n 
A 1 20  VAL 20  20  20  VAL VAL B . n 
A 1 21  THR 21  21  21  THR THR B . n 
A 1 22  CYS 22  22  22  CYS CYS B . n 
A 1 23  GLY 23  23  23  GLY GLY B . n 
A 1 24  THR 24  24  24  THR THR B . n 
A 1 25  THR 25  25  25  THR THR B . n 
A 1 26  THR 26  26  26  THR THR B . n 
A 1 27  LEU 27  27  27  LEU LEU B . n 
A 1 28  ASN 28  28  28  ASN ASN B . n 
A 1 29  GLY 29  29  29  GLY GLY B . n 
A 1 30  LEU 30  30  30  LEU LEU B . n 
A 1 31  TRP 31  31  31  TRP TRP B . n 
A 1 32  LEU 32  32  32  LEU LEU B . n 
A 1 33  ASP 33  33  33  ASP ASP B . n 
A 1 34  ASP 34  34  34  ASP ASP B . n 
A 1 35  VAL 35  35  35  VAL VAL B . n 
A 1 36  VAL 36  36  36  VAL VAL B . n 
A 1 37  TYR 37  37  37  TYR TYR B . n 
A 1 38  CYS 38  38  38  CYS CYS B . n 
A 1 39  PRO 39  39  39  PRO PRO B . n 
A 1 40  ARG 40  40  40  ARG ARG B . n 
A 1 41  HIS 41  41  41  HIS HIS B . n 
A 1 42  VAL 42  42  42  VAL VAL B . n 
A 1 43  ILE 43  43  43  ILE ILE B . n 
A 1 44  CYS 44  44  44  CYS CYS B . n 
A 1 45  THR 45  45  45  THR THR B . n 
A 1 46  SER 46  46  46  SER SER B . n 
A 1 47  GLU 47  47  47  GLU GLU B . n 
A 1 48  ASP 48  48  48  ASP ASP B . n 
A 1 49  MET 49  49  49  MET MET B . n 
A 1 50  LEU 50  50  50  LEU LEU B . n 
A 1 51  ASN 51  51  51  ASN ASN B . n 
A 1 52  PRO 52  52  52  PRO PRO B . n 
A 1 53  ASN 53  53  53  ASN ASN B . n 
A 1 54  TYR 54  54  54  TYR TYR B . n 
A 1 55  GLU 55  55  55  GLU GLU B . n 
A 1 56  ASP 56  56  56  ASP ASP B . n 
A 1 57  LEU 57  57  57  LEU LEU B . n 
A 1 58  LEU 58  58  58  LEU LEU B . n 
A 1 59  ILE 59  59  59  ILE ILE B . n 
A 1 60  ARG 60  60  60  ARG ARG B . n 
A 1 61  LYS 61  61  61  LYS LYS B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  HIS 64  64  64  HIS HIS B . n 
A 1 65  ASN 65  65  65  ASN ASN B . n 
A 1 66  PHE 66  66  66  PHE PHE B . n 
A 1 67  LEU 67  67  67  LEU LEU B . n 
A 1 68  VAL 68  68  68  VAL VAL B . n 
A 1 69  GLN 69  69  69  GLN GLN B . n 
A 1 70  ALA 70  70  70  ALA ALA B . n 
A 1 71  GLY 71  71  71  GLY GLY B . n 
A 1 72  ASN 72  72  72  ASN ASN B . n 
A 1 73  VAL 73  73  73  VAL VAL B . n 
A 1 74  GLN 74  74  74  GLN GLN B . n 
A 1 75  LEU 75  75  75  LEU LEU B . n 
A 1 76  ARG 76  76  76  ARG ARG B . n 
A 1 77  VAL 77  77  77  VAL VAL B . n 
A 1 78  ILE 78  78  78  ILE ILE B . n 
A 1 79  GLY 79  79  79  GLY GLY B . n 
A 1 80  HIS 80  80  80  HIS HIS B . n 
A 1 81  SER 81  81  81  SER SER B . n 
A 1 82  MET 82  82  82  MET MET B . n 
A 1 83  GLN 83  83  83  GLN GLN B . n 
A 1 84  ASN 84  84  84  ASN ASN B . n 
A 1 85  CYS 85  85  85  CYS CYS B . n 
A 1 86  VAL 86  86  86  VAL VAL B . n 
A 1 87  LEU 87  87  87  LEU LEU B . n 
A 1 88  LYS 88  88  88  LYS LYS B . n 
A 1 89  LEU 89  89  89  LEU LEU B . n 
A 1 90  LYS 90  90  90  LYS LYS B . n 
A 1 91  VAL 91  91  91  VAL VAL B . n 
A 1 92  ASP 92  92  92  ASP ASP B . n 
A 1 93  THR 93  93  93  THR THR B . n 
A 1 94  ALA 94  94  94  ALA ALA B . n 
A 1 95  ASN 95  95  95  ASN ASN B . n 
A 1 96  PRO 96  96  96  PRO PRO B . n 
A 1 97  LYS 97  97  97  LYS LYS B . n 
A 1 98  THR 98  98  98  THR THR B . n 
A 1 99  PRO 99  99  99  PRO PRO B . n 
A 1 100 LYS 100 100 100 LYS LYS B . n 
A 1 101 TYR 101 101 101 TYR TYR B . n 
A 1 102 LYS 102 102 102 LYS LYS B . n 
A 1 103 PHE 103 103 103 PHE PHE B . n 
A 1 104 VAL 104 104 104 VAL VAL B . n 
A 1 105 ARG 105 105 105 ARG ARG B . n 
A 1 106 ILE 106 106 106 ILE ILE B . n 
A 1 107 GLN 107 107 107 GLN GLN B . n 
A 1 108 PRO 108 108 108 PRO PRO B . n 
A 1 109 GLY 109 109 109 GLY GLY B . n 
A 1 110 GLN 110 110 110 GLN GLN B . n 
A 1 111 THR 111 111 111 THR THR B . n 
A 1 112 PHE 112 112 112 PHE PHE B . n 
A 1 113 SER 113 113 113 SER SER B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 LEU 115 115 115 LEU LEU B . n 
A 1 116 ALA 116 116 116 ALA ALA B . n 
A 1 117 CYS 117 117 117 CYS CYS B . n 
A 1 118 TYR 118 118 118 TYR TYR B . n 
A 1 119 ASN 119 119 119 ASN ASN B . n 
A 1 120 GLY 120 120 120 GLY GLY B . n 
A 1 121 SER 121 121 121 SER SER B . n 
A 1 122 PRO 122 122 122 PRO PRO B . n 
A 1 123 SER 123 123 123 SER SER B . n 
A 1 124 GLY 124 124 124 GLY GLY B . n 
A 1 125 VAL 125 125 125 VAL VAL B . n 
A 1 126 TYR 126 126 126 TYR TYR B . n 
A 1 127 GLN 127 127 127 GLN GLN B . n 
A 1 128 CYS 128 128 128 CYS CYS B . n 
A 1 129 ALA 129 129 129 ALA ALA B . n 
A 1 130 MET 130 130 130 MET MET B . n 
A 1 131 ARG 131 131 131 ARG ARG B . n 
A 1 132 HIS 132 132 132 HIS HIS B . n 
A 1 133 ASN 133 133 133 ASN ASN B . n 
A 1 134 PHE 134 134 134 PHE PHE B . n 
A 1 135 THR 135 135 135 THR THR B . n 
A 1 136 ILE 136 136 136 ILE ILE B . n 
A 1 137 LYS 137 137 137 LYS LYS B . n 
A 1 138 GLY 138 138 138 GLY GLY B . n 
A 1 139 SER 139 139 139 SER SER B . n 
A 1 140 PHE 140 140 140 PHE PHE B . n 
A 1 141 LEU 141 141 141 LEU LEU B . n 
A 1 142 ASN 142 142 142 ASN ASN B . n 
A 1 143 GLY 143 143 143 GLY GLY B . n 
A 1 144 SER 144 144 144 SER SER B . n 
A 1 145 CYS 145 145 145 CYS CYS B . n 
A 1 146 GLY 146 146 146 GLY GLY B . n 
A 1 147 SER 147 147 147 SER SER B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 GLY 149 149 149 GLY GLY B . n 
A 1 150 PHE 150 150 150 PHE PHE B . n 
A 1 151 ASN 151 151 151 ASN ASN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 ASP 153 153 153 ASP ASP B . n 
A 1 154 TYR 154 154 154 TYR TYR B . n 
A 1 155 ASP 155 155 155 ASP ASP B . n 
A 1 156 CYS 156 156 156 CYS CYS B . n 
A 1 157 VAL 157 157 157 VAL VAL B . n 
A 1 158 SER 158 158 158 SER SER B . n 
A 1 159 PHE 159 159 159 PHE PHE B . n 
A 1 160 CYS 160 160 160 CYS CYS B . n 
A 1 161 TYR 161 161 161 TYR TYR B . n 
A 1 162 MET 162 162 162 MET MET B . n 
A 1 163 HIS 163 163 163 HIS HIS B . n 
A 1 164 HIS 164 164 164 HIS HIS B . n 
A 1 165 MET 165 165 165 MET MET B . n 
A 1 166 GLU 166 166 166 GLU GLU B . n 
A 1 167 LEU 167 167 167 LEU LEU B . n 
A 1 168 PRO 168 168 168 PRO PRO B . n 
A 1 169 SER 169 169 169 SER SER B . n 
A 1 170 GLY 170 170 170 GLY GLY B . n 
A 1 171 VAL 171 171 171 VAL VAL B . n 
A 1 172 HIS 172 172 172 HIS HIS B . n 
A 1 173 ALA 173 173 173 ALA ALA B . n 
A 1 174 GLY 174 174 174 GLY GLY B . n 
A 1 175 THR 175 175 175 THR THR B . n 
A 1 176 ASP 176 176 176 ASP ASP B . n 
A 1 177 LEU 177 177 177 LEU LEU B . n 
A 1 178 GLU 178 178 178 GLU GLU B . n 
A 1 179 GLY 179 179 179 GLY GLY B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 TYR 182 182 182 TYR TYR B . n 
A 1 183 GLY 183 183 183 GLY GLY B . n 
A 1 184 PRO 184 184 184 PRO PRO B . n 
A 1 185 PHE 185 185 185 PHE PHE B . n 
A 1 186 VAL 186 186 186 VAL VAL B . n 
A 1 187 ASP 187 187 187 ASP ASP B . n 
A 1 188 ARG 188 188 188 ARG ARG B . n 
A 1 189 GLN 189 189 189 GLN GLN B . n 
A 1 190 THR 190 190 190 THR THR B . n 
A 1 191 ALA 191 191 191 ALA ALA B . n 
A 1 192 GLN 192 192 192 GLN GLN B . n 
A 1 193 ALA 193 193 193 ALA ALA B . n 
A 1 194 ALA 194 194 194 ALA ALA B . n 
A 1 195 GLY 195 195 195 GLY GLY B . n 
A 1 196 THR 196 196 196 THR THR B . n 
A 1 197 ASP 197 197 197 ASP ASP B . n 
A 1 198 THR 198 198 198 THR THR B . n 
A 1 199 THR 199 199 199 THR THR B . n 
A 1 200 ILE 200 200 200 ILE ILE B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 ASN 203 203 203 ASN ASN B . n 
A 1 204 VAL 204 204 204 VAL VAL B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 ALA 206 206 206 ALA ALA B . n 
A 1 207 TRP 207 207 207 TRP TRP B . n 
A 1 208 LEU 208 208 208 LEU LEU B . n 
A 1 209 TYR 209 209 209 TYR TYR B . n 
A 1 210 ALA 210 210 210 ALA ALA B . n 
A 1 211 ALA 211 211 211 ALA ALA B . n 
A 1 212 VAL 212 212 212 VAL VAL B . n 
A 1 213 ILE 213 213 213 ILE ILE B . n 
A 1 214 ASN 214 214 214 ASN ASN B . n 
A 1 215 GLY 215 215 215 GLY GLY B . n 
A 1 216 ASP 216 216 216 ASP ASP B . n 
A 1 217 ARG 217 217 217 ARG ARG B . n 
A 1 218 TRP 218 218 218 TRP TRP B . n 
A 1 219 PHE 219 219 219 PHE PHE B . n 
A 1 220 LEU 220 220 220 LEU LEU B . n 
A 1 221 ASN 221 221 221 ASN ASN B . n 
A 1 222 ARG 222 222 222 ARG ARG B . n 
A 1 223 PHE 223 223 223 PHE PHE B . n 
A 1 224 THR 224 224 224 THR THR B . n 
A 1 225 THR 225 225 225 THR THR B . n 
A 1 226 THR 226 226 226 THR THR B . n 
A 1 227 LEU 227 227 227 LEU LEU B . n 
A 1 228 ASN 228 228 228 ASN ASN B . n 
A 1 229 ASP 229 229 229 ASP ASP B . n 
A 1 230 PHE 230 230 230 PHE PHE B . n 
A 1 231 ASN 231 231 231 ASN ASN B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 VAL 233 233 233 VAL VAL B . n 
A 1 234 ALA 234 234 234 ALA ALA B . n 
A 1 235 MET 235 235 235 MET MET B . n 
A 1 236 LYS 236 236 236 LYS LYS B . n 
A 1 237 TYR 237 237 237 TYR TYR B . n 
A 1 238 ASN 238 238 238 ASN ASN B . n 
A 1 239 TYR 239 239 239 TYR TYR B . n 
A 1 240 GLU 240 240 240 GLU GLU B . n 
A 1 241 PRO 241 241 241 PRO PRO B . n 
A 1 242 LEU 242 242 242 LEU LEU B . n 
A 1 243 THR 243 243 243 THR THR B . n 
A 1 244 GLN 244 244 244 GLN GLN B . n 
A 1 245 ASP 245 245 245 ASP ASP B . n 
A 1 246 HIS 246 246 246 HIS HIS B . n 
A 1 247 VAL 247 247 247 VAL VAL B . n 
A 1 248 ASP 248 248 248 ASP ASP B . n 
A 1 249 ILE 249 249 249 ILE ILE B . n 
A 1 250 LEU 250 250 250 LEU LEU B . n 
A 1 251 GLY 251 251 251 GLY GLY B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 SER 254 254 254 SER SER B . n 
A 1 255 ALA 255 255 255 ALA ALA B . n 
A 1 256 GLN 256 256 256 GLN GLN B . n 
A 1 257 THR 257 257 257 THR THR B . n 
A 1 258 GLY 258 258 258 GLY GLY B . n 
A 1 259 ILE 259 259 259 ILE ILE B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 VAL 261 261 261 VAL VAL B . n 
A 1 262 LEU 262 262 262 LEU LEU B . n 
A 1 263 ASP 263 263 263 ASP ASP B . n 
A 1 264 MET 264 264 264 MET MET B . n 
A 1 265 CYS 265 265 265 CYS CYS B . n 
A 1 266 ALA 266 266 266 ALA ALA B . n 
A 1 267 SER 267 267 267 SER SER B . n 
A 1 268 LEU 268 268 268 LEU LEU B . n 
A 1 269 LYS 269 269 269 LYS LYS B . n 
A 1 270 GLU 270 270 270 GLU GLU B . n 
A 1 271 LEU 271 271 271 LEU LEU B . n 
A 1 272 LEU 272 272 272 LEU LEU B . n 
A 1 273 GLN 273 273 273 GLN GLN B . n 
A 1 274 ASN 274 274 274 ASN ASN B . n 
A 1 275 GLY 275 275 275 GLY GLY B . n 
A 1 276 MET 276 276 276 MET MET B . n 
A 1 277 ASN 277 277 277 ASN ASN B . n 
A 1 278 GLY 278 278 278 GLY GLY B . n 
A 1 279 ARG 279 279 279 ARG ARG B . n 
A 1 280 THR 280 280 280 THR THR B . n 
A 1 281 ILE 281 281 281 ILE ILE B . n 
A 1 282 LEU 282 282 282 LEU LEU B . n 
A 1 283 GLY 283 283 283 GLY GLY B . n 
A 1 284 SER 284 284 284 SER SER B . n 
A 1 285 ALA 285 285 285 ALA ALA B . n 
A 1 286 LEU 286 286 286 LEU LEU B . n 
A 1 287 LEU 287 287 287 LEU LEU B . n 
A 1 288 GLU 288 288 288 GLU GLU B . n 
A 1 289 ASP 289 289 289 ASP ASP B . n 
A 1 290 GLU 290 290 290 GLU GLU B . n 
A 1 291 PHE 291 291 291 PHE PHE B . n 
A 1 292 THR 292 292 292 THR THR B . n 
A 1 293 PRO 293 293 293 PRO PRO B . n 
A 1 294 PHE 294 294 294 PHE PHE B . n 
A 1 295 ASP 295 295 295 ASP ASP B . n 
A 1 296 VAL 296 296 296 VAL VAL B . n 
A 1 297 VAL 297 297 297 VAL VAL B . n 
A 1 298 ARG 298 298 298 ARG ARG B . n 
A 1 299 GLN 299 299 299 GLN GLN B . n 
A 1 300 CYS 300 300 300 CYS CYS B . n 
A 1 301 SER 301 301 301 SER SER B . n 
A 1 302 GLY 302 302 302 GLY GLY B . n 
A 1 303 VAL 303 303 303 VAL VAL B . n 
A 1 304 THR 304 304 304 THR THR B . n 
A 1 305 PHE 305 305 305 PHE PHE B . n 
A 1 306 GLN 306 306 306 GLN GLN B . n 
B 1 1   SER 1   1   1   SER SER A . n 
B 1 2   GLY 2   2   2   GLY GLY A . n 
B 1 3   PHE 3   3   3   PHE PHE A . n 
B 1 4   ARG 4   4   4   ARG ARG A . n 
B 1 5   LYS 5   5   5   LYS LYS A . n 
B 1 6   MET 6   6   6   MET MET A . n 
B 1 7   ALA 7   7   7   ALA ALA A . n 
B 1 8   PHE 8   8   8   PHE PHE A . n 
B 1 9   PRO 9   9   9   PRO PRO A . n 
B 1 10  SER 10  10  10  SER SER A . n 
B 1 11  GLY 11  11  11  GLY GLY A . n 
B 1 12  LYS 12  12  12  LYS LYS A . n 
B 1 13  VAL 13  13  13  VAL VAL A . n 
B 1 14  GLU 14  14  14  GLU GLU A . n 
B 1 15  GLY 15  15  15  GLY GLY A . n 
B 1 16  CYS 16  16  16  CYS CYS A . n 
B 1 17  MET 17  17  17  MET MET A . n 
B 1 18  VAL 18  18  18  VAL VAL A . n 
B 1 19  GLN 19  19  19  GLN GLN A . n 
B 1 20  VAL 20  20  20  VAL VAL A . n 
B 1 21  THR 21  21  21  THR THR A . n 
B 1 22  CYS 22  22  22  CYS CYS A . n 
B 1 23  GLY 23  23  23  GLY GLY A . n 
B 1 24  THR 24  24  24  THR THR A . n 
B 1 25  THR 25  25  25  THR THR A . n 
B 1 26  THR 26  26  26  THR THR A . n 
B 1 27  LEU 27  27  27  LEU LEU A . n 
B 1 28  ASN 28  28  28  ASN ASN A . n 
B 1 29  GLY 29  29  29  GLY GLY A . n 
B 1 30  LEU 30  30  30  LEU LEU A . n 
B 1 31  TRP 31  31  31  TRP TRP A . n 
B 1 32  LEU 32  32  32  LEU LEU A . n 
B 1 33  ASP 33  33  33  ASP ASP A . n 
B 1 34  ASP 34  34  34  ASP ASP A . n 
B 1 35  VAL 35  35  35  VAL VAL A . n 
B 1 36  VAL 36  36  36  VAL VAL A . n 
B 1 37  TYR 37  37  37  TYR TYR A . n 
B 1 38  CYS 38  38  38  CYS CYS A . n 
B 1 39  PRO 39  39  39  PRO PRO A . n 
B 1 40  ARG 40  40  40  ARG ARG A . n 
B 1 41  HIS 41  41  41  HIS HIS A . n 
B 1 42  VAL 42  42  42  VAL VAL A . n 
B 1 43  ILE 43  43  43  ILE ILE A . n 
B 1 44  CYS 44  44  44  CYS CYS A . n 
B 1 45  THR 45  45  45  THR THR A . n 
B 1 46  SER 46  46  46  SER SER A . n 
B 1 47  GLU 47  47  47  GLU GLU A . n 
B 1 48  ASP 48  48  48  ASP ASP A . n 
B 1 49  MET 49  49  49  MET MET A . n 
B 1 50  LEU 50  50  50  LEU LEU A . n 
B 1 51  ASN 51  51  51  ASN ASN A . n 
B 1 52  PRO 52  52  52  PRO PRO A . n 
B 1 53  ASN 53  53  53  ASN ASN A . n 
B 1 54  TYR 54  54  54  TYR TYR A . n 
B 1 55  GLU 55  55  55  GLU GLU A . n 
B 1 56  ASP 56  56  56  ASP ASP A . n 
B 1 57  LEU 57  57  57  LEU LEU A . n 
B 1 58  LEU 58  58  58  LEU LEU A . n 
B 1 59  ILE 59  59  59  ILE ILE A . n 
B 1 60  ARG 60  60  60  ARG ARG A . n 
B 1 61  LYS 61  61  61  LYS LYS A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  HIS 64  64  64  HIS HIS A . n 
B 1 65  ASN 65  65  65  ASN ASN A . n 
B 1 66  PHE 66  66  66  PHE PHE A . n 
B 1 67  LEU 67  67  67  LEU LEU A . n 
B 1 68  VAL 68  68  68  VAL VAL A . n 
B 1 69  GLN 69  69  69  GLN GLN A . n 
B 1 70  ALA 70  70  70  ALA ALA A . n 
B 1 71  GLY 71  71  71  GLY GLY A . n 
B 1 72  ASN 72  72  72  ASN ASN A . n 
B 1 73  VAL 73  73  73  VAL VAL A . n 
B 1 74  GLN 74  74  74  GLN GLN A . n 
B 1 75  LEU 75  75  75  LEU LEU A . n 
B 1 76  ARG 76  76  76  ARG ARG A . n 
B 1 77  VAL 77  77  77  VAL VAL A . n 
B 1 78  ILE 78  78  78  ILE ILE A . n 
B 1 79  GLY 79  79  79  GLY GLY A . n 
B 1 80  HIS 80  80  80  HIS HIS A . n 
B 1 81  SER 81  81  81  SER SER A . n 
B 1 82  MET 82  82  82  MET MET A . n 
B 1 83  GLN 83  83  83  GLN GLN A . n 
B 1 84  ASN 84  84  84  ASN ASN A . n 
B 1 85  CYS 85  85  85  CYS CYS A . n 
B 1 86  VAL 86  86  86  VAL VAL A . n 
B 1 87  LEU 87  87  87  LEU LEU A . n 
B 1 88  LYS 88  88  88  LYS LYS A . n 
B 1 89  LEU 89  89  89  LEU LEU A . n 
B 1 90  LYS 90  90  90  LYS LYS A . n 
B 1 91  VAL 91  91  91  VAL VAL A . n 
B 1 92  ASP 92  92  92  ASP ASP A . n 
B 1 93  THR 93  93  93  THR THR A . n 
B 1 94  ALA 94  94  94  ALA ALA A . n 
B 1 95  ASN 95  95  95  ASN ASN A . n 
B 1 96  PRO 96  96  96  PRO PRO A . n 
B 1 97  LYS 97  97  97  LYS LYS A . n 
B 1 98  THR 98  98  98  THR THR A . n 
B 1 99  PRO 99  99  99  PRO PRO A . n 
B 1 100 LYS 100 100 100 LYS LYS A . n 
B 1 101 TYR 101 101 101 TYR TYR A . n 
B 1 102 LYS 102 102 102 LYS LYS A . n 
B 1 103 PHE 103 103 103 PHE PHE A . n 
B 1 104 VAL 104 104 104 VAL VAL A . n 
B 1 105 ARG 105 105 105 ARG ARG A . n 
B 1 106 ILE 106 106 106 ILE ILE A . n 
B 1 107 GLN 107 107 107 GLN GLN A . n 
B 1 108 PRO 108 108 108 PRO PRO A . n 
B 1 109 GLY 109 109 109 GLY GLY A . n 
B 1 110 GLN 110 110 110 GLN GLN A . n 
B 1 111 THR 111 111 111 THR THR A . n 
B 1 112 PHE 112 112 112 PHE PHE A . n 
B 1 113 SER 113 113 113 SER SER A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 LEU 115 115 115 LEU LEU A . n 
B 1 116 ALA 116 116 116 ALA ALA A . n 
B 1 117 CYS 117 117 117 CYS CYS A . n 
B 1 118 TYR 118 118 118 TYR TYR A . n 
B 1 119 ASN 119 119 119 ASN ASN A . n 
B 1 120 GLY 120 120 120 GLY GLY A . n 
B 1 121 SER 121 121 121 SER SER A . n 
B 1 122 PRO 122 122 122 PRO PRO A . n 
B 1 123 SER 123 123 123 SER SER A . n 
B 1 124 GLY 124 124 124 GLY GLY A . n 
B 1 125 VAL 125 125 125 VAL VAL A . n 
B 1 126 TYR 126 126 126 TYR TYR A . n 
B 1 127 GLN 127 127 127 GLN GLN A . n 
B 1 128 CYS 128 128 128 CYS CYS A . n 
B 1 129 ALA 129 129 129 ALA ALA A . n 
B 1 130 MET 130 130 130 MET MET A . n 
B 1 131 ARG 131 131 131 ARG ARG A . n 
B 1 132 HIS 132 132 132 HIS HIS A . n 
B 1 133 ASN 133 133 133 ASN ASN A . n 
B 1 134 PHE 134 134 134 PHE PHE A . n 
B 1 135 THR 135 135 135 THR THR A . n 
B 1 136 ILE 136 136 136 ILE ILE A . n 
B 1 137 LYS 137 137 137 LYS LYS A . n 
B 1 138 GLY 138 138 138 GLY GLY A . n 
B 1 139 SER 139 139 139 SER SER A . n 
B 1 140 PHE 140 140 140 PHE PHE A . n 
B 1 141 LEU 141 141 141 LEU LEU A . n 
B 1 142 ASN 142 142 142 ASN ASN A . n 
B 1 143 GLY 143 143 143 GLY GLY A . n 
B 1 144 SER 144 144 144 SER SER A . n 
B 1 145 CYS 145 145 145 CYS CYS A . n 
B 1 146 GLY 146 146 146 GLY GLY A . n 
B 1 147 SER 147 147 147 SER SER A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 GLY 149 149 149 GLY GLY A . n 
B 1 150 PHE 150 150 150 PHE PHE A . n 
B 1 151 ASN 151 151 151 ASN ASN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 ASP 153 153 153 ASP ASP A . n 
B 1 154 TYR 154 154 154 TYR TYR A . n 
B 1 155 ASP 155 155 155 ASP ASP A . n 
B 1 156 CYS 156 156 156 CYS CYS A . n 
B 1 157 VAL 157 157 157 VAL VAL A . n 
B 1 158 SER 158 158 158 SER SER A . n 
B 1 159 PHE 159 159 159 PHE PHE A . n 
B 1 160 CYS 160 160 160 CYS CYS A . n 
B 1 161 TYR 161 161 161 TYR TYR A . n 
B 1 162 MET 162 162 162 MET MET A . n 
B 1 163 HIS 163 163 163 HIS HIS A . n 
B 1 164 HIS 164 164 164 HIS HIS A . n 
B 1 165 MET 165 165 165 MET MET A . n 
B 1 166 GLU 166 166 166 GLU GLU A . n 
B 1 167 LEU 167 167 167 LEU LEU A . n 
B 1 168 PRO 168 168 168 PRO PRO A . n 
B 1 169 SER 169 169 169 SER SER A . n 
B 1 170 GLY 170 170 170 GLY GLY A . n 
B 1 171 VAL 171 171 171 VAL VAL A . n 
B 1 172 HIS 172 172 172 HIS HIS A . n 
B 1 173 ALA 173 173 173 ALA ALA A . n 
B 1 174 GLY 174 174 174 GLY GLY A . n 
B 1 175 THR 175 175 175 THR THR A . n 
B 1 176 ASP 176 176 176 ASP ASP A . n 
B 1 177 LEU 177 177 177 LEU LEU A . n 
B 1 178 GLU 178 178 178 GLU GLU A . n 
B 1 179 GLY 179 179 179 GLY GLY A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 TYR 182 182 182 TYR TYR A . n 
B 1 183 GLY 183 183 183 GLY GLY A . n 
B 1 184 PRO 184 184 184 PRO PRO A . n 
B 1 185 PHE 185 185 185 PHE PHE A . n 
B 1 186 VAL 186 186 186 VAL VAL A . n 
B 1 187 ASP 187 187 187 ASP ASP A . n 
B 1 188 ARG 188 188 188 ARG ARG A . n 
B 1 189 GLN 189 189 189 GLN GLN A . n 
B 1 190 THR 190 190 190 THR THR A . n 
B 1 191 ALA 191 191 191 ALA ALA A . n 
B 1 192 GLN 192 192 192 GLN GLN A . n 
B 1 193 ALA 193 193 193 ALA ALA A . n 
B 1 194 ALA 194 194 194 ALA ALA A . n 
B 1 195 GLY 195 195 195 GLY GLY A . n 
B 1 196 THR 196 196 196 THR THR A . n 
B 1 197 ASP 197 197 197 ASP ASP A . n 
B 1 198 THR 198 198 198 THR THR A . n 
B 1 199 THR 199 199 199 THR THR A . n 
B 1 200 ILE 200 200 200 ILE ILE A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 ASN 203 203 203 ASN ASN A . n 
B 1 204 VAL 204 204 204 VAL VAL A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 ALA 206 206 206 ALA ALA A . n 
B 1 207 TRP 207 207 207 TRP TRP A . n 
B 1 208 LEU 208 208 208 LEU LEU A . n 
B 1 209 TYR 209 209 209 TYR TYR A . n 
B 1 210 ALA 210 210 210 ALA ALA A . n 
B 1 211 ALA 211 211 211 ALA ALA A . n 
B 1 212 VAL 212 212 212 VAL VAL A . n 
B 1 213 ILE 213 213 213 ILE ILE A . n 
B 1 214 ASN 214 214 214 ASN ASN A . n 
B 1 215 GLY 215 215 215 GLY GLY A . n 
B 1 216 ASP 216 216 216 ASP ASP A . n 
B 1 217 ARG 217 217 217 ARG ARG A . n 
B 1 218 TRP 218 218 218 TRP TRP A . n 
B 1 219 PHE 219 219 219 PHE PHE A . n 
B 1 220 LEU 220 220 220 LEU LEU A . n 
B 1 221 ASN 221 221 221 ASN ASN A . n 
B 1 222 ARG 222 222 222 ARG ARG A . n 
B 1 223 PHE 223 223 223 PHE PHE A . n 
B 1 224 THR 224 224 224 THR THR A . n 
B 1 225 THR 225 225 225 THR THR A . n 
B 1 226 THR 226 226 226 THR THR A . n 
B 1 227 LEU 227 227 227 LEU LEU A . n 
B 1 228 ASN 228 228 228 ASN ASN A . n 
B 1 229 ASP 229 229 229 ASP ASP A . n 
B 1 230 PHE 230 230 230 PHE PHE A . n 
B 1 231 ASN 231 231 231 ASN ASN A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 VAL 233 233 233 VAL VAL A . n 
B 1 234 ALA 234 234 234 ALA ALA A . n 
B 1 235 MET 235 235 235 MET MET A . n 
B 1 236 LYS 236 236 236 LYS LYS A . n 
B 1 237 TYR 237 237 237 TYR TYR A . n 
B 1 238 ASN 238 238 238 ASN ASN A . n 
B 1 239 TYR 239 239 239 TYR TYR A . n 
B 1 240 GLU 240 240 240 GLU GLU A . n 
B 1 241 PRO 241 241 241 PRO PRO A . n 
B 1 242 LEU 242 242 242 LEU LEU A . n 
B 1 243 THR 243 243 243 THR THR A . n 
B 1 244 GLN 244 244 244 GLN GLN A . n 
B 1 245 ASP 245 245 245 ASP ASP A . n 
B 1 246 HIS 246 246 246 HIS HIS A . n 
B 1 247 VAL 247 247 247 VAL VAL A . n 
B 1 248 ASP 248 248 248 ASP ASP A . n 
B 1 249 ILE 249 249 249 ILE ILE A . n 
B 1 250 LEU 250 250 250 LEU LEU A . n 
B 1 251 GLY 251 251 251 GLY GLY A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 SER 254 254 254 SER SER A . n 
B 1 255 ALA 255 255 255 ALA ALA A . n 
B 1 256 GLN 256 256 256 GLN GLN A . n 
B 1 257 THR 257 257 257 THR THR A . n 
B 1 258 GLY 258 258 258 GLY GLY A . n 
B 1 259 ILE 259 259 259 ILE ILE A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 VAL 261 261 261 VAL VAL A . n 
B 1 262 LEU 262 262 262 LEU LEU A . n 
B 1 263 ASP 263 263 263 ASP ASP A . n 
B 1 264 MET 264 264 264 MET MET A . n 
B 1 265 CYS 265 265 265 CYS CYS A . n 
B 1 266 ALA 266 266 266 ALA ALA A . n 
B 1 267 SER 267 267 267 SER SER A . n 
B 1 268 LEU 268 268 268 LEU LEU A . n 
B 1 269 LYS 269 269 269 LYS LYS A . n 
B 1 270 GLU 270 270 270 GLU GLU A . n 
B 1 271 LEU 271 271 271 LEU LEU A . n 
B 1 272 LEU 272 272 272 LEU LEU A . n 
B 1 273 GLN 273 273 273 GLN GLN A . n 
B 1 274 ASN 274 274 274 ASN ASN A . n 
B 1 275 GLY 275 275 275 GLY GLY A . n 
B 1 276 MET 276 276 276 MET MET A . n 
B 1 277 ASN 277 277 277 ASN ASN A . n 
B 1 278 GLY 278 278 278 GLY GLY A . n 
B 1 279 ARG 279 279 279 ARG ARG A . n 
B 1 280 THR 280 280 280 THR THR A . n 
B 1 281 ILE 281 281 281 ILE ILE A . n 
B 1 282 LEU 282 282 282 LEU LEU A . n 
B 1 283 GLY 283 283 283 GLY GLY A . n 
B 1 284 SER 284 284 284 SER SER A . n 
B 1 285 ALA 285 285 285 ALA ALA A . n 
B 1 286 LEU 286 286 286 LEU LEU A . n 
B 1 287 LEU 287 287 287 LEU LEU A . n 
B 1 288 GLU 288 288 288 GLU GLU A . n 
B 1 289 ASP 289 289 289 ASP ASP A . n 
B 1 290 GLU 290 290 290 GLU GLU A . n 
B 1 291 PHE 291 291 291 PHE PHE A . n 
B 1 292 THR 292 292 292 THR THR A . n 
B 1 293 PRO 293 293 293 PRO PRO A . n 
B 1 294 PHE 294 294 294 PHE PHE A . n 
B 1 295 ASP 295 295 295 ASP ASP A . n 
B 1 296 VAL 296 296 296 VAL VAL A . n 
B 1 297 VAL 297 297 297 VAL VAL A . n 
B 1 298 ARG 298 298 298 ARG ARG A . n 
B 1 299 GLN 299 299 299 GLN GLN A . n 
B 1 300 CYS 300 300 300 CYS CYS A . n 
B 1 301 SER 301 301 301 SER SER A . n 
B 1 302 GLY 302 302 302 GLY GLY A . n 
B 1 303 VAL 303 303 303 VAL VAL A . n 
B 1 304 THR 304 304 304 THR THR A . n 
B 1 305 PHE 305 305 305 PHE PHE A . n 
B 1 306 GLN 306 306 306 GLN GLN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        O6K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   O6K 
_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 O6K 1   401 2   O6K O6K B . 
D 2 O6K 1   401 1   O6K O6K A . 
E 3 HOH 1   501 390 HOH HOH B . 
E 3 HOH 2   502 112 HOH HOH B . 
E 3 HOH 3   503 286 HOH HOH B . 
E 3 HOH 4   504 245 HOH HOH B . 
E 3 HOH 5   505 181 HOH HOH B . 
E 3 HOH 6   506 264 HOH HOH B . 
E 3 HOH 7   507 465 HOH HOH B . 
E 3 HOH 8   508 315 HOH HOH B . 
E 3 HOH 9   509 431 HOH HOH B . 
E 3 HOH 10  510 284 HOH HOH B . 
E 3 HOH 11  511 31  HOH HOH B . 
E 3 HOH 12  512 176 HOH HOH B . 
E 3 HOH 13  513 15  HOH HOH B . 
E 3 HOH 14  514 80  HOH HOH B . 
E 3 HOH 15  515 462 HOH HOH B . 
E 3 HOH 16  516 157 HOH HOH B . 
E 3 HOH 17  517 317 HOH HOH B . 
E 3 HOH 18  518 32  HOH HOH B . 
E 3 HOH 19  519 159 HOH HOH B . 
E 3 HOH 20  520 229 HOH HOH B . 
E 3 HOH 21  521 261 HOH HOH B . 
E 3 HOH 22  522 360 HOH HOH B . 
E 3 HOH 23  523 427 HOH HOH B . 
E 3 HOH 24  524 370 HOH HOH B . 
E 3 HOH 25  525 26  HOH HOH B . 
E 3 HOH 26  526 33  HOH HOH B . 
E 3 HOH 27  527 206 HOH HOH B . 
E 3 HOH 28  528 240 HOH HOH B . 
E 3 HOH 29  529 318 HOH HOH B . 
E 3 HOH 30  530 404 HOH HOH B . 
E 3 HOH 31  531 137 HOH HOH B . 
E 3 HOH 32  532 396 HOH HOH B . 
E 3 HOH 33  533 441 HOH HOH B . 
E 3 HOH 34  534 89  HOH HOH B . 
E 3 HOH 35  535 30  HOH HOH B . 
E 3 HOH 36  536 84  HOH HOH B . 
E 3 HOH 37  537 55  HOH HOH B . 
E 3 HOH 38  538 185 HOH HOH B . 
E 3 HOH 39  539 235 HOH HOH B . 
E 3 HOH 40  540 73  HOH HOH B . 
E 3 HOH 41  541 452 HOH HOH B . 
E 3 HOH 42  542 239 HOH HOH B . 
E 3 HOH 43  543 454 HOH HOH B . 
E 3 HOH 44  544 98  HOH HOH B . 
E 3 HOH 45  545 403 HOH HOH B . 
E 3 HOH 46  546 222 HOH HOH B . 
E 3 HOH 47  547 184 HOH HOH B . 
E 3 HOH 48  548 88  HOH HOH B . 
E 3 HOH 49  549 428 HOH HOH B . 
E 3 HOH 50  550 357 HOH HOH B . 
E 3 HOH 51  551 12  HOH HOH B . 
E 3 HOH 52  552 6   HOH HOH B . 
E 3 HOH 53  553 133 HOH HOH B . 
E 3 HOH 54  554 146 HOH HOH B . 
E 3 HOH 55  555 101 HOH HOH B . 
E 3 HOH 56  556 394 HOH HOH B . 
E 3 HOH 57  557 50  HOH HOH B . 
E 3 HOH 58  558 57  HOH HOH B . 
E 3 HOH 59  559 92  HOH HOH B . 
E 3 HOH 60  560 14  HOH HOH B . 
E 3 HOH 61  561 470 HOH HOH B . 
E 3 HOH 62  562 266 HOH HOH B . 
E 3 HOH 63  563 2   HOH HOH B . 
E 3 HOH 64  564 242 HOH HOH B . 
E 3 HOH 65  565 29  HOH HOH B . 
E 3 HOH 66  566 17  HOH HOH B . 
E 3 HOH 67  567 333 HOH HOH B . 
E 3 HOH 68  568 299 HOH HOH B . 
E 3 HOH 69  569 205 HOH HOH B . 
E 3 HOH 70  570 220 HOH HOH B . 
E 3 HOH 71  571 319 HOH HOH B . 
E 3 HOH 72  572 161 HOH HOH B . 
E 3 HOH 73  573 100 HOH HOH B . 
E 3 HOH 74  574 210 HOH HOH B . 
E 3 HOH 75  575 138 HOH HOH B . 
E 3 HOH 76  576 411 HOH HOH B . 
E 3 HOH 77  577 400 HOH HOH B . 
E 3 HOH 78  578 378 HOH HOH B . 
E 3 HOH 79  579 177 HOH HOH B . 
E 3 HOH 80  580 224 HOH HOH B . 
E 3 HOH 81  581 43  HOH HOH B . 
E 3 HOH 82  582 53  HOH HOH B . 
E 3 HOH 83  583 123 HOH HOH B . 
E 3 HOH 84  584 149 HOH HOH B . 
E 3 HOH 85  585 361 HOH HOH B . 
E 3 HOH 86  586 397 HOH HOH B . 
E 3 HOH 87  587 191 HOH HOH B . 
E 3 HOH 88  588 448 HOH HOH B . 
E 3 HOH 89  589 166 HOH HOH B . 
E 3 HOH 90  590 141 HOH HOH B . 
E 3 HOH 91  591 151 HOH HOH B . 
E 3 HOH 92  592 54  HOH HOH B . 
E 3 HOH 93  593 154 HOH HOH B . 
E 3 HOH 94  594 352 HOH HOH B . 
E 3 HOH 95  595 311 HOH HOH B . 
E 3 HOH 96  596 334 HOH HOH B . 
E 3 HOH 97  597 464 HOH HOH B . 
E 3 HOH 98  598 134 HOH HOH B . 
E 3 HOH 99  599 430 HOH HOH B . 
E 3 HOH 100 600 380 HOH HOH B . 
E 3 HOH 101 601 192 HOH HOH B . 
E 3 HOH 102 602 163 HOH HOH B . 
E 3 HOH 103 603 401 HOH HOH B . 
E 3 HOH 104 604 271 HOH HOH B . 
E 3 HOH 105 605 438 HOH HOH B . 
E 3 HOH 106 606 175 HOH HOH B . 
E 3 HOH 107 607 74  HOH HOH B . 
E 3 HOH 108 608 383 HOH HOH B . 
E 3 HOH 109 609 10  HOH HOH B . 
E 3 HOH 110 610 35  HOH HOH B . 
E 3 HOH 111 611 140 HOH HOH B . 
E 3 HOH 112 612 429 HOH HOH B . 
E 3 HOH 113 613 328 HOH HOH B . 
E 3 HOH 114 614 59  HOH HOH B . 
E 3 HOH 115 615 265 HOH HOH B . 
E 3 HOH 116 616 126 HOH HOH B . 
E 3 HOH 117 617 421 HOH HOH B . 
E 3 HOH 118 618 122 HOH HOH B . 
E 3 HOH 119 619 198 HOH HOH B . 
E 3 HOH 120 620 237 HOH HOH B . 
E 3 HOH 121 621 25  HOH HOH B . 
E 3 HOH 122 622 341 HOH HOH B . 
E 3 HOH 123 623 93  HOH HOH B . 
E 3 HOH 124 624 202 HOH HOH B . 
E 3 HOH 125 625 94  HOH HOH B . 
E 3 HOH 126 626 49  HOH HOH B . 
E 3 HOH 127 627 413 HOH HOH B . 
E 3 HOH 128 628 293 HOH HOH B . 
E 3 HOH 129 629 162 HOH HOH B . 
E 3 HOH 130 630 168 HOH HOH B . 
E 3 HOH 131 631 189 HOH HOH B . 
E 3 HOH 132 632 186 HOH HOH B . 
E 3 HOH 133 633 351 HOH HOH B . 
E 3 HOH 134 634 34  HOH HOH B . 
E 3 HOH 135 635 373 HOH HOH B . 
E 3 HOH 136 636 169 HOH HOH B . 
E 3 HOH 137 637 473 HOH HOH B . 
E 3 HOH 138 638 131 HOH HOH B . 
E 3 HOH 139 639 219 HOH HOH B . 
E 3 HOH 140 640 27  HOH HOH B . 
E 3 HOH 141 641 472 HOH HOH B . 
E 3 HOH 142 642 381 HOH HOH B . 
E 3 HOH 143 643 467 HOH HOH B . 
E 3 HOH 144 644 279 HOH HOH B . 
E 3 HOH 145 645 221 HOH HOH B . 
E 3 HOH 146 646 102 HOH HOH B . 
E 3 HOH 147 647 408 HOH HOH B . 
E 3 HOH 148 648 75  HOH HOH B . 
E 3 HOH 149 649 309 HOH HOH B . 
E 3 HOH 150 650 270 HOH HOH B . 
E 3 HOH 151 651 399 HOH HOH B . 
E 3 HOH 152 652 155 HOH HOH B . 
E 3 HOH 153 653 172 HOH HOH B . 
E 3 HOH 154 654 347 HOH HOH B . 
E 3 HOH 155 655 45  HOH HOH B . 
E 3 HOH 156 656 1   HOH HOH B . 
E 3 HOH 157 657 364 HOH HOH B . 
E 3 HOH 158 658 193 HOH HOH B . 
E 3 HOH 159 659 386 HOH HOH B . 
E 3 HOH 160 660 460 HOH HOH B . 
E 3 HOH 161 661 275 HOH HOH B . 
E 3 HOH 162 662 436 HOH HOH B . 
E 3 HOH 163 663 307 HOH HOH B . 
E 3 HOH 164 664 392 HOH HOH B . 
E 3 HOH 165 665 13  HOH HOH B . 
E 3 HOH 166 666 225 HOH HOH B . 
E 3 HOH 167 667 152 HOH HOH B . 
E 3 HOH 168 668 442 HOH HOH B . 
E 3 HOH 169 669 267 HOH HOH B . 
E 3 HOH 170 670 336 HOH HOH B . 
E 3 HOH 171 671 269 HOH HOH B . 
E 3 HOH 172 672 468 HOH HOH B . 
E 3 HOH 173 673 144 HOH HOH B . 
E 3 HOH 174 674 426 HOH HOH B . 
E 3 HOH 175 675 268 HOH HOH B . 
E 3 HOH 176 676 228 HOH HOH B . 
E 3 HOH 177 677 306 HOH HOH B . 
E 3 HOH 178 678 234 HOH HOH B . 
E 3 HOH 179 679 139 HOH HOH B . 
E 3 HOH 180 680 348 HOH HOH B . 
E 3 HOH 181 681 273 HOH HOH B . 
E 3 HOH 182 682 323 HOH HOH B . 
E 3 HOH 183 683 165 HOH HOH B . 
E 3 HOH 184 684 227 HOH HOH B . 
E 3 HOH 185 685 388 HOH HOH B . 
E 3 HOH 186 686 453 HOH HOH B . 
E 3 HOH 187 687 359 HOH HOH B . 
E 3 HOH 188 688 457 HOH HOH B . 
E 3 HOH 189 689 439 HOH HOH B . 
E 3 HOH 190 690 295 HOH HOH B . 
E 3 HOH 191 691 47  HOH HOH B . 
E 3 HOH 192 692 324 HOH HOH B . 
E 3 HOH 193 693 305 HOH HOH B . 
E 3 HOH 194 694 443 HOH HOH B . 
E 3 HOH 195 695 355 HOH HOH B . 
E 3 HOH 196 696 367 HOH HOH B . 
E 3 HOH 197 697 338 HOH HOH B . 
E 3 HOH 198 698 320 HOH HOH B . 
E 3 HOH 199 699 188 HOH HOH B . 
E 3 HOH 200 700 474 HOH HOH B . 
E 3 HOH 201 701 316 HOH HOH B . 
E 3 HOH 202 702 458 HOH HOH B . 
E 3 HOH 203 703 304 HOH HOH B . 
E 3 HOH 204 704 208 HOH HOH B . 
E 3 HOH 205 705 366 HOH HOH B . 
E 3 HOH 206 706 281 HOH HOH B . 
E 3 HOH 207 707 118 HOH HOH B . 
E 3 HOH 208 708 382 HOH HOH B . 
E 3 HOH 209 709 90  HOH HOH B . 
E 3 HOH 210 710 48  HOH HOH B . 
E 3 HOH 211 711 425 HOH HOH B . 
E 3 HOH 212 712 340 HOH HOH B . 
E 3 HOH 213 713 72  HOH HOH B . 
E 3 HOH 214 714 247 HOH HOH B . 
E 3 HOH 215 715 371 HOH HOH B . 
E 3 HOH 216 716 288 HOH HOH B . 
E 3 HOH 217 717 256 HOH HOH B . 
E 3 HOH 218 718 63  HOH HOH B . 
E 3 HOH 219 719 363 HOH HOH B . 
E 3 HOH 220 720 314 HOH HOH B . 
E 3 HOH 221 721 475 HOH HOH B . 
E 3 HOH 222 722 463 HOH HOH B . 
F 3 HOH 1   501 416 HOH HOH A . 
F 3 HOH 2   502 108 HOH HOH A . 
F 3 HOH 3   503 40  HOH HOH A . 
F 3 HOH 4   504 303 HOH HOH A . 
F 3 HOH 5   505 405 HOH HOH A . 
F 3 HOH 6   506 44  HOH HOH A . 
F 3 HOH 7   507 285 HOH HOH A . 
F 3 HOH 8   508 418 HOH HOH A . 
F 3 HOH 9   509 195 HOH HOH A . 
F 3 HOH 10  510 164 HOH HOH A . 
F 3 HOH 11  511 287 HOH HOH A . 
F 3 HOH 12  512 142 HOH HOH A . 
F 3 HOH 13  513 87  HOH HOH A . 
F 3 HOH 14  514 115 HOH HOH A . 
F 3 HOH 15  515 412 HOH HOH A . 
F 3 HOH 16  516 69  HOH HOH A . 
F 3 HOH 17  517 450 HOH HOH A . 
F 3 HOH 18  518 130 HOH HOH A . 
F 3 HOH 19  519 203 HOH HOH A . 
F 3 HOH 20  520 120 HOH HOH A . 
F 3 HOH 21  521 41  HOH HOH A . 
F 3 HOH 22  522 282 HOH HOH A . 
F 3 HOH 23  523 28  HOH HOH A . 
F 3 HOH 24  524 368 HOH HOH A . 
F 3 HOH 25  525 143 HOH HOH A . 
F 3 HOH 26  526 232 HOH HOH A . 
F 3 HOH 27  527 395 HOH HOH A . 
F 3 HOH 28  528 11  HOH HOH A . 
F 3 HOH 29  529 160 HOH HOH A . 
F 3 HOH 30  530 342 HOH HOH A . 
F 3 HOH 31  531 127 HOH HOH A . 
F 3 HOH 32  532 379 HOH HOH A . 
F 3 HOH 33  533 398 HOH HOH A . 
F 3 HOH 34  534 156 HOH HOH A . 
F 3 HOH 35  535 337 HOH HOH A . 
F 3 HOH 36  536 105 HOH HOH A . 
F 3 HOH 37  537 387 HOH HOH A . 
F 3 HOH 38  538 22  HOH HOH A . 
F 3 HOH 39  539 76  HOH HOH A . 
F 3 HOH 40  540 214 HOH HOH A . 
F 3 HOH 41  541 223 HOH HOH A . 
F 3 HOH 42  542 18  HOH HOH A . 
F 3 HOH 43  543 81  HOH HOH A . 
F 3 HOH 44  544 260 HOH HOH A . 
F 3 HOH 45  545 78  HOH HOH A . 
F 3 HOH 46  546 407 HOH HOH A . 
F 3 HOH 47  547 211 HOH HOH A . 
F 3 HOH 48  548 296 HOH HOH A . 
F 3 HOH 49  549 310 HOH HOH A . 
F 3 HOH 50  550 277 HOH HOH A . 
F 3 HOH 51  551 66  HOH HOH A . 
F 3 HOH 52  552 197 HOH HOH A . 
F 3 HOH 53  553 150 HOH HOH A . 
F 3 HOH 54  554 42  HOH HOH A . 
F 3 HOH 55  555 248 HOH HOH A . 
F 3 HOH 56  556 451 HOH HOH A . 
F 3 HOH 57  557 109 HOH HOH A . 
F 3 HOH 58  558 19  HOH HOH A . 
F 3 HOH 59  559 71  HOH HOH A . 
F 3 HOH 60  560 419 HOH HOH A . 
F 3 HOH 61  561 294 HOH HOH A . 
F 3 HOH 62  562 385 HOH HOH A . 
F 3 HOH 63  563 95  HOH HOH A . 
F 3 HOH 64  564 302 HOH HOH A . 
F 3 HOH 65  565 68  HOH HOH A . 
F 3 HOH 66  566 148 HOH HOH A . 
F 3 HOH 67  567 437 HOH HOH A . 
F 3 HOH 68  568 283 HOH HOH A . 
F 3 HOH 69  569 217 HOH HOH A . 
F 3 HOH 70  570 124 HOH HOH A . 
F 3 HOH 71  571 4   HOH HOH A . 
F 3 HOH 72  572 231 HOH HOH A . 
F 3 HOH 73  573 128 HOH HOH A . 
F 3 HOH 74  574 230 HOH HOH A . 
F 3 HOH 75  575 114 HOH HOH A . 
F 3 HOH 76  576 8   HOH HOH A . 
F 3 HOH 77  577 136 HOH HOH A . 
F 3 HOH 78  578 276 HOH HOH A . 
F 3 HOH 79  579 9   HOH HOH A . 
F 3 HOH 80  580 326 HOH HOH A . 
F 3 HOH 81  581 308 HOH HOH A . 
F 3 HOH 82  582 313 HOH HOH A . 
F 3 HOH 83  583 132 HOH HOH A . 
F 3 HOH 84  584 414 HOH HOH A . 
F 3 HOH 85  585 39  HOH HOH A . 
F 3 HOH 86  586 5   HOH HOH A . 
F 3 HOH 87  587 104 HOH HOH A . 
F 3 HOH 88  588 7   HOH HOH A . 
F 3 HOH 89  589 329 HOH HOH A . 
F 3 HOH 90  590 312 HOH HOH A . 
F 3 HOH 91  591 97  HOH HOH A . 
F 3 HOH 92  592 204 HOH HOH A . 
F 3 HOH 93  593 301 HOH HOH A . 
F 3 HOH 94  594 77  HOH HOH A . 
F 3 HOH 95  595 459 HOH HOH A . 
F 3 HOH 96  596 46  HOH HOH A . 
F 3 HOH 97  597 61  HOH HOH A . 
F 3 HOH 98  598 125 HOH HOH A . 
F 3 HOH 99  599 461 HOH HOH A . 
F 3 HOH 100 600 290 HOH HOH A . 
F 3 HOH 101 601 96  HOH HOH A . 
F 3 HOH 102 602 409 HOH HOH A . 
F 3 HOH 103 603 153 HOH HOH A . 
F 3 HOH 104 604 215 HOH HOH A . 
F 3 HOH 105 605 106 HOH HOH A . 
F 3 HOH 106 606 257 HOH HOH A . 
F 3 HOH 107 607 117 HOH HOH A . 
F 3 HOH 108 608 415 HOH HOH A . 
F 3 HOH 109 609 174 HOH HOH A . 
F 3 HOH 110 610 51  HOH HOH A . 
F 3 HOH 111 611 16  HOH HOH A . 
F 3 HOH 112 612 423 HOH HOH A . 
F 3 HOH 113 613 38  HOH HOH A . 
F 3 HOH 114 614 3   HOH HOH A . 
F 3 HOH 115 615 263 HOH HOH A . 
F 3 HOH 116 616 58  HOH HOH A . 
F 3 HOH 117 617 82  HOH HOH A . 
F 3 HOH 118 618 79  HOH HOH A . 
F 3 HOH 119 619 52  HOH HOH A . 
F 3 HOH 120 620 20  HOH HOH A . 
F 3 HOH 121 621 167 HOH HOH A . 
F 3 HOH 122 622 455 HOH HOH A . 
F 3 HOH 123 623 253 HOH HOH A . 
F 3 HOH 124 624 209 HOH HOH A . 
F 3 HOH 125 625 110 HOH HOH A . 
F 3 HOH 126 626 297 HOH HOH A . 
F 3 HOH 127 627 65  HOH HOH A . 
F 3 HOH 128 628 200 HOH HOH A . 
F 3 HOH 129 629 158 HOH HOH A . 
F 3 HOH 130 630 103 HOH HOH A . 
F 3 HOH 131 631 420 HOH HOH A . 
F 3 HOH 132 632 86  HOH HOH A . 
F 3 HOH 133 633 178 HOH HOH A . 
F 3 HOH 134 634 322 HOH HOH A . 
F 3 HOH 135 635 332 HOH HOH A . 
F 3 HOH 136 636 23  HOH HOH A . 
F 3 HOH 137 637 91  HOH HOH A . 
F 3 HOH 138 638 60  HOH HOH A . 
F 3 HOH 139 639 21  HOH HOH A . 
F 3 HOH 140 640 252 HOH HOH A . 
F 3 HOH 141 641 346 HOH HOH A . 
F 3 HOH 142 642 147 HOH HOH A . 
F 3 HOH 143 643 216 HOH HOH A . 
F 3 HOH 144 644 24  HOH HOH A . 
F 3 HOH 145 645 226 HOH HOH A . 
F 3 HOH 146 646 190 HOH HOH A . 
F 3 HOH 147 647 83  HOH HOH A . 
F 3 HOH 148 648 254 HOH HOH A . 
F 3 HOH 149 649 56  HOH HOH A . 
F 3 HOH 150 650 417 HOH HOH A . 
F 3 HOH 151 651 354 HOH HOH A . 
F 3 HOH 152 652 272 HOH HOH A . 
F 3 HOH 153 653 350 HOH HOH A . 
F 3 HOH 154 654 238 HOH HOH A . 
F 3 HOH 155 655 179 HOH HOH A . 
F 3 HOH 156 656 64  HOH HOH A . 
F 3 HOH 157 657 37  HOH HOH A . 
F 3 HOH 158 658 440 HOH HOH A . 
F 3 HOH 159 659 372 HOH HOH A . 
F 3 HOH 160 660 67  HOH HOH A . 
F 3 HOH 161 661 471 HOH HOH A . 
F 3 HOH 162 662 107 HOH HOH A . 
F 3 HOH 163 663 116 HOH HOH A . 
F 3 HOH 164 664 298 HOH HOH A . 
F 3 HOH 165 665 393 HOH HOH A . 
F 3 HOH 166 666 365 HOH HOH A . 
F 3 HOH 167 667 422 HOH HOH A . 
F 3 HOH 168 668 432 HOH HOH A . 
F 3 HOH 169 669 353 HOH HOH A . 
F 3 HOH 170 670 62  HOH HOH A . 
F 3 HOH 171 671 466 HOH HOH A . 
F 3 HOH 172 672 113 HOH HOH A . 
F 3 HOH 173 673 236 HOH HOH A . 
F 3 HOH 174 674 171 HOH HOH A . 
F 3 HOH 175 675 36  HOH HOH A . 
F 3 HOH 176 676 289 HOH HOH A . 
F 3 HOH 177 677 345 HOH HOH A . 
F 3 HOH 178 678 300 HOH HOH A . 
F 3 HOH 179 679 356 HOH HOH A . 
F 3 HOH 180 680 321 HOH HOH A . 
F 3 HOH 181 681 255 HOH HOH A . 
F 3 HOH 182 682 212 HOH HOH A . 
F 3 HOH 183 683 374 HOH HOH A . 
F 3 HOH 184 684 85  HOH HOH A . 
F 3 HOH 185 685 433 HOH HOH A . 
F 3 HOH 186 686 249 HOH HOH A . 
F 3 HOH 187 687 402 HOH HOH A . 
F 3 HOH 188 688 274 HOH HOH A . 
F 3 HOH 189 689 251 HOH HOH A . 
F 3 HOH 190 690 449 HOH HOH A . 
F 3 HOH 191 691 389 HOH HOH A . 
F 3 HOH 192 692 410 HOH HOH A . 
F 3 HOH 193 693 292 HOH HOH A . 
F 3 HOH 194 694 377 HOH HOH A . 
F 3 HOH 195 695 358 HOH HOH A . 
F 3 HOH 196 696 330 HOH HOH A . 
F 3 HOH 197 697 424 HOH HOH A . 
F 3 HOH 198 698 135 HOH HOH A . 
F 3 HOH 199 699 291 HOH HOH A . 
F 3 HOH 200 700 187 HOH HOH A . 
F 3 HOH 201 701 327 HOH HOH A . 
F 3 HOH 202 702 375 HOH HOH A . 
F 3 HOH 203 703 199 HOH HOH A . 
F 3 HOH 204 704 343 HOH HOH A . 
F 3 HOH 205 705 244 HOH HOH A . 
F 3 HOH 206 706 119 HOH HOH A . 
F 3 HOH 207 707 218 HOH HOH A . 
F 3 HOH 208 708 250 HOH HOH A . 
F 3 HOH 209 709 246 HOH HOH A . 
F 3 HOH 210 710 262 HOH HOH A . 
F 3 HOH 211 711 121 HOH HOH A . 
F 3 HOH 212 712 331 HOH HOH A . 
F 3 HOH 213 713 444 HOH HOH A . 
F 3 HOH 214 714 99  HOH HOH A . 
F 3 HOH 215 715 447 HOH HOH A . 
F 3 HOH 216 716 111 HOH HOH A . 
F 3 HOH 217 717 145 HOH HOH A . 
F 3 HOH 218 718 445 HOH HOH A . 
F 3 HOH 219 719 194 HOH HOH A . 
F 3 HOH 220 720 170 HOH HOH A . 
F 3 HOH 221 721 213 HOH HOH A . 
F 3 HOH 222 722 258 HOH HOH A . 
F 3 HOH 223 723 446 HOH HOH A . 
F 3 HOH 224 724 233 HOH HOH A . 
F 3 HOH 225 725 173 HOH HOH A . 
F 3 HOH 226 726 243 HOH HOH A . 
F 3 HOH 227 727 391 HOH HOH A . 
F 3 HOH 228 728 259 HOH HOH A . 
F 3 HOH 229 729 339 HOH HOH A . 
F 3 HOH 230 730 369 HOH HOH A . 
F 3 HOH 231 731 325 HOH HOH A . 
F 3 HOH 232 732 129 HOH HOH A . 
F 3 HOH 233 733 182 HOH HOH A . 
F 3 HOH 234 734 376 HOH HOH A . 
F 3 HOH 235 735 335 HOH HOH A . 
F 3 HOH 236 736 362 HOH HOH A . 
F 3 HOH 237 737 435 HOH HOH A . 
F 3 HOH 238 738 280 HOH HOH A . 
F 3 HOH 239 739 469 HOH HOH A . 
F 3 HOH 240 740 434 HOH HOH A . 
F 3 HOH 241 741 183 HOH HOH A . 
F 3 HOH 242 742 406 HOH HOH A . 
F 3 HOH 243 743 241 HOH HOH A . 
F 3 HOH 244 744 349 HOH HOH A . 
F 3 HOH 245 745 207 HOH HOH A . 
F 3 HOH 246 746 180 HOH HOH A . 
F 3 HOH 247 747 201 HOH HOH A . 
F 3 HOH 248 748 344 HOH HOH A . 
F 3 HOH 249 749 70  HOH HOH A . 
F 3 HOH 250 750 384 HOH HOH A . 
F 3 HOH 251 751 456 HOH HOH A . 
F 3 HOH 252 752 278 HOH HOH A . 
F 3 HOH 253 753 196 HOH HOH A . 
# 
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 ? ? ? 1.19.2_4158 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .           5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.96 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8R1Q 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.541 
_cell.length_a_esd                 ? 
_cell.length_b                     64.032 
_cell.length_b_esd                 ? 
_cell.length_c                     103.692 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8R1Q 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8R1Q 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.91 
_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, SITTING 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    'PEG3350 25%' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033 
_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                        'PETRA III, DESY BEAMLINE P11' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   P11 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R1Q 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.70 
_reflns.d_resolution_low                               41.44 
_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                                     64655 
_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                           98.37 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.92 
_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                                   0.998 
_reflns.pdbx_CC_star                                   1 
_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                                    1.70 
_reflns_shell.d_res_low                                     1.76 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.28 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6414 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.6 
_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                                  0.635 
_reflns_shell.pdbx_CC_star                                  0.881 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.27 
_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                                 8R1Q 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             41.44 
_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                     64640 
_refine.ls_number_reflns_R_free                  3318 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.37 
_refine.ls_percent_reflns_R_free                 5.13 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1958 
_refine.ls_R_factor_R_free                       0.2230 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1943 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.51 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4738 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         86 
_refine_hist.number_atoms_solvent             475 
_refine_hist.number_atoms_total               5299 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        41.44 
# 
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' ? 0.008  ? 4936 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.040  ? 6710 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.306 ? 672  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 750  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 868  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.70 1.72  . . 136 2508 99.00 . . . . 0.3419 . . . . . . . . . . . 0.3844 
'X-RAY DIFFRACTION' 1.72 1.75  . . 139 2573 98.00 . . . . 0.3210 . . . . . . . . . . . 0.3454 
'X-RAY DIFFRACTION' 1.75 1.78  . . 127 2534 98.00 . . . . 0.2968 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 1.78 1.81  . . 126 2528 98.00 . . . . 0.2855 . . . . . . . . . . . 0.2803 
'X-RAY DIFFRACTION' 1.81 1.84  . . 150 2565 99.00 . . . . 0.2599 . . . . . . . . . . . 0.2975 
'X-RAY DIFFRACTION' 1.84 1.87  . . 142 2538 98.00 . . . . 0.2462 . . . . . . . . . . . 0.2752 
'X-RAY DIFFRACTION' 1.87 1.91  . . 147 2528 99.00 . . . . 0.2315 . . . . . . . . . . . 0.2820 
'X-RAY DIFFRACTION' 1.91 1.95  . . 143 2515 99.00 . . . . 0.2307 . . . . . . . . . . . 0.2582 
'X-RAY DIFFRACTION' 1.95 1.99  . . 138 2604 98.00 . . . . 0.2171 . . . . . . . . . . . 0.2825 
'X-RAY DIFFRACTION' 1.99 2.03  . . 139 2419 96.00 . . . . 0.2269 . . . . . . . . . . . 0.2564 
'X-RAY DIFFRACTION' 2.03 2.09  . . 135 2576 99.00 . . . . 0.2276 . . . . . . . . . . . 0.2915 
'X-RAY DIFFRACTION' 2.09 2.14  . . 145 2558 99.00 . . . . 0.2141 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 2.14 2.20  . . 113 2567 99.00 . . . . 0.2017 . . . . . . . . . . . 0.2466 
'X-RAY DIFFRACTION' 2.20 2.28  . . 151 2587 99.00 . . . . 0.1984 . . . . . . . . . . . 0.2365 
'X-RAY DIFFRACTION' 2.28 2.36  . . 112 2573 99.00 . . . . 0.2021 . . . . . . . . . . . 0.2266 
'X-RAY DIFFRACTION' 2.36 2.45  . . 124 2577 99.00 . . . . 0.1987 . . . . . . . . . . . 0.2487 
'X-RAY DIFFRACTION' 2.45 2.56  . . 123 2608 99.00 . . . . 0.2034 . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.56 2.70  . . 130 2575 98.00 . . . . 0.2119 . . . . . . . . . . . 0.2385 
'X-RAY DIFFRACTION' 2.70 2.87  . . 147 2457 96.00 . . . . 0.2096 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 2.87 3.09  . . 127 2580 98.00 . . . . 0.1992 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 3.09 3.40  . . 158 2581 99.00 . . . . 0.1898 . . . . . . . . . . . 0.2174 
'X-RAY DIFFRACTION' 3.40 3.89  . . 144 2579 99.00 . . . . 0.1620 . . . . . . . . . . . 0.1918 
'X-RAY DIFFRACTION' 3.89 4.90  . . 176 2584 99.00 . . . . 0.1403 . . . . . . . . . . . 0.1634 
'X-RAY DIFFRACTION' 4.90 41.44 . . 146 2608 97.00 . . . . 0.1534 . . . . . . . . . . . 0.1550 
# 
_struct.entry_id                     8R1Q 
_struct.title                        'SARS-CoV-2 Mpro (Omicron, P132H+T169S) in complex with alpha-ketoamide 13b-K' 
_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        8R1Q 
_struct_keywords.text            
'SARS-CoV-2; main protease; Omicron; Molecular Dynamics; Pro>His mutant; double mutant, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 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                    R1A_SARS2 
_struct_ref.pdbx_db_accession          P0DTC1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8R1Q B 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
2 1 8R1Q A 1 ? 306 ? P0DTC1 3264 ? 3569 ? 1 306 
# 
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 8R1Q HIS B 132 ? UNP P0DTC1 PRO 3395 variant               132 1 
1 8R1Q SER B 169 ? UNP P0DTC1 THR 3432 'engineered mutation' 169 2 
2 8R1Q HIS A 132 ? UNP P0DTC1 PRO 3395 variant               132 3 
2 8R1Q SER A 169 ? UNP P0DTC1 THR 3432 'engineered mutation' 169 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3220  ? 
1 MORE         -15   ? 
1 'SSA (A^2)'  24970 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? GLY A 302 ? THR B 292 GLY B 302 1 ? 11 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P14 AB5 GLU B 47  ? ASN B 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? HIS B 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? GLY B 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale none ? A CYS 145 SG ? ? ? 1_555 C O6K . C57 ? ? B CYS 145 B O6K 401 1_555 ? ? ? ? ? ? ? 1.762 ? ? 
covale2 covale none ? B CYS 145 SG ? ? ? 1_555 D O6K . C57 ? ? A CYS 145 A O6K 401 1_555 ? ? ? ? ? ? ? 1.762 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 O6K C . ? CYS A 145 ? O6K B 401 ? 1_555 CYS B 145 ? 1_555 C57 SG CYS 1 O6K None 'Covalent chemical modification' 
2 O6K D . ? CYS B 145 ? O6K A 401 ? 1_555 CYS A 145 ? 1_555 C57 SG CYS 1 O6K None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL B 73  LEU B 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE B 66  ALA B 70  
AA1 3 MET A 17  ? CYS A 22  ? MET B 17  CYS B 22  
AA1 4 THR A 25  ? LEU A 32  ? THR B 25  LEU B 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL B 35  PRO B 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL B 86  VAL B 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL B 77  GLN B 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS B 100 PHE B 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS B 156 GLU B 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL B 148 ASP B 153 
AA2 4 THR A 111 ? TYR A 118 ? THR B 111 TYR B 118 
AA2 5 SER A 121 ? ALA A 129 ? SER B 121 ALA B 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS B 100 PHE B 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS B 156 GLU B 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS B 172 THR B 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL A 73  LEU A 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE A 66  ALA A 70  
AA4 3 MET B 17  ? CYS B 22  ? MET A 17  CYS A 22  
AA4 4 THR B 25  ? LEU B 32  ? THR A 25  LEU A 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL A 35  PRO A 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL A 86  VAL A 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL A 77  GLN A 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR A 101 PHE A 103 
AA5 2 CYS B 156 ? LEU B 167 ? CYS A 156 LEU A 167 
AA5 3 VAL B 148 ? ASP B 153 ? VAL A 148 ASP A 153 
AA5 4 THR B 111 ? TYR B 118 ? THR A 111 TYR A 118 
AA5 5 SER B 121 ? ALA B 129 ? SER A 121 ALA A 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR A 101 PHE A 103 
AA6 2 CYS B 156 ? LEU B 167 ? CYS A 156 LEU A 167 
AA6 3 VAL B 171 ? THR B 175 ? VAL A 171 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL B 73  N ALA A 70  ? N ALA B 70  
AA1 2 3 O LEU A 67  ? O LEU B 67  N THR A 21  ? N THR B 21  
AA1 3 4 N VAL A 20  ? N VAL B 20  O LEU A 27  ? O LEU B 27  
AA1 4 5 N LEU A 30  ? N LEU B 30  O TYR A 37  ? O TYR B 37  
AA1 5 6 N CYS A 38  ? N CYS B 38  O LEU A 87  ? O LEU B 87  
AA1 6 7 O LYS A 88  ? O LYS B 88  N SER A 81  ? N SER B 81  
AA2 1 2 N LYS A 100 ? N LYS B 100 O VAL A 157 ? O VAL B 157 
AA2 2 3 O SER A 158 ? O SER B 158 N ASN A 151 ? N ASN B 151 
AA2 3 4 O PHE A 150 ? O PHE B 150 N SER A 113 ? N SER B 113 
AA2 4 5 N VAL A 114 ? N VAL B 114 O TYR A 126 ? O TYR B 126 
AA3 1 2 N LYS A 100 ? N LYS B 100 O VAL A 157 ? O VAL B 157 
AA3 2 3 N MET A 165 ? N MET B 165 O ALA A 173 ? O ALA B 173 
AA4 1 2 O VAL B 73  ? O VAL A 73  N ALA B 70  ? N ALA A 70  
AA4 2 3 O LEU B 67  ? O LEU A 67  N THR B 21  ? N THR A 21  
AA4 3 4 N VAL B 20  ? N VAL A 20  O LEU B 27  ? O LEU A 27  
AA4 4 5 N LEU B 30  ? N LEU A 30  O TYR B 37  ? O TYR A 37  
AA4 5 6 N VAL B 36  ? N VAL A 36  O LEU B 89  ? O LEU A 89  
AA4 6 7 O VAL B 86  ? O VAL A 86  N GLN B 83  ? N GLN A 83  
AA5 1 2 N LYS B 102 ? N LYS A 102 O PHE B 159 ? O PHE A 159 
AA5 2 3 O CYS B 156 ? O CYS A 156 N ASP B 153 ? N ASP A 153 
AA5 3 4 O PHE B 150 ? O PHE A 150 N SER B 113 ? N SER A 113 
AA5 4 5 N PHE B 112 ? N PHE A 112 O CYS B 128 ? O CYS A 128 
AA6 1 2 N LYS B 102 ? N LYS A 102 O PHE B 159 ? O PHE A 159 
AA6 2 3 N LEU B 167 ? N LEU A 167 O VAL B 171 ? O VAL A 171 
# 
_pdbx_entry_details.entry_id                   8R1Q 
_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   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    532 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    712 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.67 
# 
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 33  ? ? 57.81   -132.94 
2 1 ASN B 84  ? ? 51.43   -122.01 
3 1 TYR B 154 ? ? 58.46   -98.01  
4 1 PRO B 168 ? ? -79.20  40.22   
5 1 ASP A 33  ? ? 52.45   -129.00 
6 1 ASN A 51  ? ? -159.59 75.63   
7 1 ASN A 84  ? ? 51.18   -118.15 
8 1 TYR A 154 ? ? 68.24   -99.42  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
O6K O26  O N N 250 
O6K C24  C N N 251 
O6K O25  O N N 252 
O6K C27  C N N 253 
O6K C31  C N N 254 
O6K C32  C N N 255 
O6K C33  C N N 256 
O6K N23  N N N 257 
O6K C19  C N N 258 
O6K C21  C N N 259 
O6K O22  O N N 260 
O6K C18  C N N 261 
O6K C17  C N N 262 
O6K C16  C N N 263 
O6K N15  N N N 264 
O6K C20  C N S 265 
O6K C22  C N N 266 
O6K C29  C N N 267 
O6K C34  C N N 268 
O6K C30  C N N 269 
O6K C36  C N N 270 
O6K O37  O N N 271 
O6K N38  N N N 272 
O6K C40  C N S 273 
O6K C42  C N N 274 
O6K C45  C N S 275 
O6K C47  C N N 276 
O6K O48  O N N 277 
O6K N49  N N N 278 
O6K C51  C N N 279 
O6K C54  C N N 280 
O6K C57  C N R 281 
O6K O40  O N N 282 
O6K C35  C N N 283 
O6K O41  O N N 284 
O6K N36  N N N 285 
O6K C13  C N N 286 
O6K C14  C Y N 287 
O6K C28  C Y N 288 
O6K C26  C Y N 289 
O6K C25  C Y N 290 
O6K C23  C Y N 291 
O6K C15  C Y N 292 
O6K H1   H N N 293 
O6K H2   H N N 294 
O6K H3   H N N 295 
O6K H4   H N N 296 
O6K H5   H N N 297 
O6K H6   H N N 298 
O6K H7   H N N 299 
O6K H8   H N N 300 
O6K H9   H N N 301 
O6K H10  H N N 302 
O6K H11  H N N 303 
O6K H12  H N N 304 
O6K H13  H N N 305 
O6K H14  H N N 306 
O6K H15  H N N 307 
O6K H16  H N N 308 
O6K H17  H N N 309 
O6K H18  H N N 310 
O6K H19  H N N 311 
O6K H20  H N N 312 
O6K H21  H N N 313 
O6K H22  H N N 314 
O6K H23  H N N 315 
O6K H24  H N N 316 
O6K H25  H N N 317 
O6K H26  H N N 318 
O6K H27  H N N 319 
O6K H28  H N N 320 
O6K H29  H N N 321 
O6K H30  H N N 322 
O6K H31  H N N 323 
O6K H34  H N N 324 
O6K H35  H N N 325 
O6K H36  H N N 326 
O6K H37  H N N 327 
O6K H38  H N N 328 
O6K H39  H N N 329 
O6K H40  H N N 330 
O6K H41  H N N 331 
O6K H32  H N N 332 
O6K H33  H N N 333 
PHE N    N N N 334 
PHE CA   C N S 335 
PHE C    C N N 336 
PHE O    O N N 337 
PHE CB   C N N 338 
PHE CG   C Y N 339 
PHE CD1  C Y N 340 
PHE CD2  C Y N 341 
PHE CE1  C Y N 342 
PHE CE2  C Y N 343 
PHE CZ   C Y N 344 
PHE OXT  O N N 345 
PHE H    H N N 346 
PHE H2   H N N 347 
PHE HA   H N N 348 
PHE HB2  H N N 349 
PHE HB3  H N N 350 
PHE HD1  H N N 351 
PHE HD2  H N N 352 
PHE HE1  H N N 353 
PHE HE2  H N N 354 
PHE HZ   H N N 355 
PHE HXT  H N N 356 
PRO N    N N N 357 
PRO CA   C N S 358 
PRO C    C N N 359 
PRO O    O N N 360 
PRO CB   C N N 361 
PRO CG   C N N 362 
PRO CD   C N N 363 
PRO OXT  O N N 364 
PRO H    H N N 365 
PRO HA   H N N 366 
PRO HB2  H N N 367 
PRO HB3  H N N 368 
PRO HG2  H N N 369 
PRO HG3  H N N 370 
PRO HD2  H N N 371 
PRO HD3  H N N 372 
PRO HXT  H N N 373 
SER N    N N N 374 
SER CA   C N S 375 
SER C    C N N 376 
SER O    O N N 377 
SER CB   C N N 378 
SER OG   O N N 379 
SER OXT  O N N 380 
SER H    H N N 381 
SER H2   H N N 382 
SER HA   H N N 383 
SER HB2  H N N 384 
SER HB3  H N N 385 
SER HG   H N N 386 
SER HXT  H N N 387 
THR N    N N N 388 
THR CA   C N S 389 
THR C    C N N 390 
THR O    O N N 391 
THR CB   C N R 392 
THR OG1  O N N 393 
THR CG2  C N N 394 
THR OXT  O N N 395 
THR H    H N N 396 
THR H2   H N N 397 
THR HA   H N N 398 
THR HB   H N N 399 
THR HG1  H N N 400 
THR HG21 H N N 401 
THR HG22 H N N 402 
THR HG23 H N N 403 
THR HXT  H N N 404 
TRP N    N N N 405 
TRP CA   C N S 406 
TRP C    C N N 407 
TRP O    O N N 408 
TRP CB   C N N 409 
TRP CG   C Y N 410 
TRP CD1  C Y N 411 
TRP CD2  C Y N 412 
TRP NE1  N Y N 413 
TRP CE2  C Y N 414 
TRP CE3  C Y N 415 
TRP CZ2  C Y N 416 
TRP CZ3  C Y N 417 
TRP CH2  C Y N 418 
TRP OXT  O N N 419 
TRP H    H N N 420 
TRP H2   H N N 421 
TRP HA   H N N 422 
TRP HB2  H N N 423 
TRP HB3  H N N 424 
TRP HD1  H N N 425 
TRP HE1  H N N 426 
TRP HE3  H N N 427 
TRP HZ2  H N N 428 
TRP HZ3  H N N 429 
TRP HH2  H N N 430 
TRP HXT  H N N 431 
TYR N    N N N 432 
TYR CA   C N S 433 
TYR C    C N N 434 
TYR O    O N N 435 
TYR CB   C N N 436 
TYR CG   C Y N 437 
TYR CD1  C Y N 438 
TYR CD2  C Y N 439 
TYR CE1  C Y N 440 
TYR CE2  C Y N 441 
TYR CZ   C Y N 442 
TYR OH   O N N 443 
TYR OXT  O N N 444 
TYR H    H N N 445 
TYR H2   H N N 446 
TYR HA   H N N 447 
TYR HB2  H N N 448 
TYR HB3  H N N 449 
TYR HD1  H N N 450 
TYR HD2  H N N 451 
TYR HE1  H N N 452 
TYR HE2  H N N 453 
TYR HH   H N N 454 
TYR HXT  H N N 455 
VAL N    N N N 456 
VAL CA   C N S 457 
VAL C    C N N 458 
VAL O    O N N 459 
VAL CB   C N N 460 
VAL CG1  C N N 461 
VAL CG2  C N N 462 
VAL OXT  O N N 463 
VAL H    H N N 464 
VAL H2   H N N 465 
VAL HA   H N N 466 
VAL HB   H N N 467 
VAL HG11 H N N 468 
VAL HG12 H N N 469 
VAL HG13 H N N 470 
VAL HG21 H N N 471 
VAL HG22 H N N 472 
VAL HG23 H N N 473 
VAL HXT  H N N 474 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
O6K N49 C47  sing N N 237 
O6K N49 C51  sing N N 238 
O6K O48 C47  doub N N 239 
O6K C47 C45  sing N N 240 
O6K C51 C54  sing N N 241 
O6K O41 C35  doub N N 242 
O6K C54 C45  sing N N 243 
O6K C45 C42  sing N N 244 
O6K C42 C40  sing N N 245 
O6K C23 C15  doub Y N 246 
O6K C23 C25  sing Y N 247 
O6K C15 C14  sing Y N 248 
O6K C25 C26  doub Y N 249 
O6K C35 N36  sing N N 250 
O6K C35 C57  sing N N 251 
O6K C14 C13  sing N N 252 
O6K C14 C28  doub Y N 253 
O6K C13 N36  sing N N 254 
O6K C26 C28  sing Y N 255 
O6K C40 C57  sing N N 256 
O6K C40 N38  sing N N 257 
O6K C57 O40  sing N N 258 
O6K C32 C27  sing N N 259 
O6K N38 C36  sing N N 260 
O6K C33 C27  sing N N 261 
O6K C27 O25  sing N N 262 
O6K C27 C31  sing N N 263 
O6K O25 C24  sing N N 264 
O6K O37 C36  doub N N 265 
O6K O22 C21  doub N N 266 
O6K C36 C20  sing N N 267 
O6K N23 C24  sing N N 268 
O6K N23 C19  sing N N 269 
O6K C24 O26  doub N N 270 
O6K C21 C19  sing N N 271 
O6K C21 N15  sing N N 272 
O6K C20 N15  sing N N 273 
O6K C20 C22  sing N N 274 
O6K C19 C18  doub N N 275 
O6K N15 C16  sing N N 276 
O6K C22 C29  sing N N 277 
O6K C18 C17  sing N N 278 
O6K C16 C17  doub N N 279 
O6K C30 C29  sing N N 280 
O6K C30 C34  sing N N 281 
O6K C29 C34  sing N N 282 
O6K C31 H1   sing N N 283 
O6K C31 H2   sing N N 284 
O6K C31 H3   sing N N 285 
O6K C32 H4   sing N N 286 
O6K C32 H5   sing N N 287 
O6K C32 H6   sing N N 288 
O6K C33 H7   sing N N 289 
O6K C33 H8   sing N N 290 
O6K C33 H9   sing N N 291 
O6K N23 H10  sing N N 292 
O6K C18 H11  sing N N 293 
O6K C17 H12  sing N N 294 
O6K C16 H13  sing N N 295 
O6K C20 H14  sing N N 296 
O6K C22 H15  sing N N 297 
O6K C22 H16  sing N N 298 
O6K C29 H17  sing N N 299 
O6K C34 H18  sing N N 300 
O6K C34 H19  sing N N 301 
O6K C30 H20  sing N N 302 
O6K C30 H21  sing N N 303 
O6K N38 H22  sing N N 304 
O6K C40 H23  sing N N 305 
O6K C42 H24  sing N N 306 
O6K C42 H25  sing N N 307 
O6K C45 H26  sing N N 308 
O6K N49 H27  sing N N 309 
O6K C51 H28  sing N N 310 
O6K C51 H29  sing N N 311 
O6K C54 H30  sing N N 312 
O6K C54 H31  sing N N 313 
O6K N36 H34  sing N N 314 
O6K C13 H35  sing N N 315 
O6K C13 H36  sing N N 316 
O6K C28 H37  sing N N 317 
O6K C26 H38  sing N N 318 
O6K C25 H39  sing N N 319 
O6K C23 H40  sing N N 320 
O6K C15 H41  sing N N 321 
O6K C57 H32  sing N N 322 
O6K O40 H33  sing N N 323 
PHE N   CA   sing N N 324 
PHE N   H    sing N N 325 
PHE N   H2   sing N N 326 
PHE CA  C    sing N N 327 
PHE CA  CB   sing N N 328 
PHE CA  HA   sing N N 329 
PHE C   O    doub N N 330 
PHE C   OXT  sing N N 331 
PHE CB  CG   sing N N 332 
PHE CB  HB2  sing N N 333 
PHE CB  HB3  sing N N 334 
PHE CG  CD1  doub Y N 335 
PHE CG  CD2  sing Y N 336 
PHE CD1 CE1  sing Y N 337 
PHE CD1 HD1  sing N N 338 
PHE CD2 CE2  doub Y N 339 
PHE CD2 HD2  sing N N 340 
PHE CE1 CZ   doub Y N 341 
PHE CE1 HE1  sing N N 342 
PHE CE2 CZ   sing Y N 343 
PHE CE2 HE2  sing N N 344 
PHE CZ  HZ   sing N N 345 
PHE OXT HXT  sing N N 346 
PRO N   CA   sing N N 347 
PRO N   CD   sing N N 348 
PRO N   H    sing N N 349 
PRO CA  C    sing N N 350 
PRO CA  CB   sing N N 351 
PRO CA  HA   sing N N 352 
PRO C   O    doub N N 353 
PRO C   OXT  sing N N 354 
PRO CB  CG   sing N N 355 
PRO CB  HB2  sing N N 356 
PRO CB  HB3  sing N N 357 
PRO CG  CD   sing N N 358 
PRO CG  HG2  sing N N 359 
PRO CG  HG3  sing N N 360 
PRO CD  HD2  sing N N 361 
PRO CD  HD3  sing N N 362 
PRO OXT HXT  sing N N 363 
SER N   CA   sing N N 364 
SER N   H    sing N N 365 
SER N   H2   sing N N 366 
SER CA  C    sing N N 367 
SER CA  CB   sing N N 368 
SER CA  HA   sing N N 369 
SER C   O    doub N N 370 
SER C   OXT  sing N N 371 
SER CB  OG   sing N N 372 
SER CB  HB2  sing N N 373 
SER CB  HB3  sing N N 374 
SER OG  HG   sing N N 375 
SER OXT HXT  sing N N 376 
THR N   CA   sing N N 377 
THR N   H    sing N N 378 
THR N   H2   sing N N 379 
THR CA  C    sing N N 380 
THR CA  CB   sing N N 381 
THR CA  HA   sing N N 382 
THR C   O    doub N N 383 
THR C   OXT  sing N N 384 
THR CB  OG1  sing N N 385 
THR CB  CG2  sing N N 386 
THR CB  HB   sing N N 387 
THR OG1 HG1  sing N N 388 
THR CG2 HG21 sing N N 389 
THR CG2 HG22 sing N N 390 
THR CG2 HG23 sing N N 391 
THR OXT HXT  sing N N 392 
TRP N   CA   sing N N 393 
TRP N   H    sing N N 394 
TRP N   H2   sing N N 395 
TRP CA  C    sing N N 396 
TRP CA  CB   sing N N 397 
TRP CA  HA   sing N N 398 
TRP C   O    doub N N 399 
TRP C   OXT  sing N N 400 
TRP CB  CG   sing N N 401 
TRP CB  HB2  sing N N 402 
TRP CB  HB3  sing N N 403 
TRP CG  CD1  doub Y N 404 
TRP CG  CD2  sing Y N 405 
TRP CD1 NE1  sing Y N 406 
TRP CD1 HD1  sing N N 407 
TRP CD2 CE2  doub Y N 408 
TRP CD2 CE3  sing Y N 409 
TRP NE1 CE2  sing Y N 410 
TRP NE1 HE1  sing N N 411 
TRP CE2 CZ2  sing Y N 412 
TRP CE3 CZ3  doub Y N 413 
TRP CE3 HE3  sing N N 414 
TRP CZ2 CH2  doub Y N 415 
TRP CZ2 HZ2  sing N N 416 
TRP CZ3 CH2  sing Y N 417 
TRP CZ3 HZ3  sing N N 418 
TRP CH2 HH2  sing N N 419 
TRP OXT HXT  sing N N 420 
TYR N   CA   sing N N 421 
TYR N   H    sing N N 422 
TYR N   H2   sing N N 423 
TYR CA  C    sing N N 424 
TYR CA  CB   sing N N 425 
TYR CA  HA   sing N N 426 
TYR C   O    doub N N 427 
TYR C   OXT  sing N N 428 
TYR CB  CG   sing N N 429 
TYR CB  HB2  sing N N 430 
TYR CB  HB3  sing N N 431 
TYR CG  CD1  doub Y N 432 
TYR CG  CD2  sing Y N 433 
TYR CD1 CE1  sing Y N 434 
TYR CD1 HD1  sing N N 435 
TYR CD2 CE2  doub Y N 436 
TYR CD2 HD2  sing N N 437 
TYR CE1 CZ   doub Y N 438 
TYR CE1 HE1  sing N N 439 
TYR CE2 CZ   sing Y N 440 
TYR CE2 HE2  sing N N 441 
TYR CZ  OH   sing N N 442 
TYR OH  HH   sing N N 443 
TYR OXT HXT  sing N N 444 
VAL N   CA   sing N N 445 
VAL N   H    sing N N 446 
VAL N   H2   sing N N 447 
VAL CA  C    sing N N 448 
VAL CA  CB   sing N N 449 
VAL CA  HA   sing N N 450 
VAL C   O    doub N N 451 
VAL C   OXT  sing N N 452 
VAL CB  CG1  sing N N 453 
VAL CB  CG2  sing N N 454 
VAL CB  HB   sing N N 455 
VAL CG1 HG11 sing N N 456 
VAL CG1 HG12 sing N N 457 
VAL CG1 HG13 sing N N 458 
VAL CG2 HG21 sing N N 459 
VAL CG2 HG22 sing N N 460 
VAL CG2 HG23 sing N N 461 
VAL OXT HXT  sing N N 462 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                Germany 
_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   6Y2E 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R1Q 
_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]   0.021958 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000368 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015617 
_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]   0.009645 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER A 1 1   ? 26.617  9.592   32.150 1.00 26.65 ? 1   SER B N   1 
ATOM   2    C CA  . SER A 1 1   ? 26.123  8.553   33.043 1.00 25.75 ? 1   SER B CA  1 
ATOM   3    C C   . SER A 1 1   ? 24.605  8.568   33.142 1.00 25.73 ? 1   SER B C   1 
ATOM   4    O O   . SER A 1 1   ? 23.930  9.271   32.392 1.00 20.06 ? 1   SER B O   1 
ATOM   5    C CB  . SER A 1 1   ? 26.743  8.714   34.431 1.00 26.90 ? 1   SER B CB  1 
ATOM   6    O OG  . SER A 1 1   ? 26.049  9.688   35.193 1.00 29.89 ? 1   SER B OG  1 
ATOM   7    N N   . GLY A 1 2   ? 24.077  7.798   34.082 1.00 23.69 ? 2   GLY B N   1 
ATOM   8    C CA  . GLY A 1 2   ? 22.648  7.598   34.200 1.00 23.31 ? 2   GLY B CA  1 
ATOM   9    C C   . GLY A 1 2   ? 22.220  6.294   33.556 1.00 20.95 ? 2   GLY B C   1 
ATOM   10   O O   . GLY A 1 2   ? 22.833  5.810   32.603 1.00 23.68 ? 2   GLY B O   1 
ATOM   11   N N   . PHE A 1 3   ? 21.140  5.712   34.071 1.00 23.52 ? 3   PHE B N   1 
ATOM   12   C CA  . PHE A 1 3   ? 20.718  4.405   33.584 1.00 24.87 ? 3   PHE B CA  1 
ATOM   13   C C   . PHE A 1 3   ? 19.204  4.384   33.525 1.00 21.28 ? 3   PHE B C   1 
ATOM   14   O O   . PHE A 1 3   ? 18.542  4.584   34.547 1.00 23.49 ? 3   PHE B O   1 
ATOM   15   C CB  . PHE A 1 3   ? 21.248  3.281   34.475 1.00 24.30 ? 3   PHE B CB  1 
ATOM   16   C CG  . PHE A 1 3   ? 21.110  1.917   33.863 1.00 23.36 ? 3   PHE B CG  1 
ATOM   17   C CD1 . PHE A 1 3   ? 22.019  1.472   32.914 1.00 24.34 ? 3   PHE B CD1 1 
ATOM   18   C CD2 . PHE A 1 3   ? 20.057  1.098   34.218 1.00 24.59 ? 3   PHE B CD2 1 
ATOM   19   C CE1 . PHE A 1 3   ? 21.889  0.200   32.343 1.00 25.89 ? 3   PHE B CE1 1 
ATOM   20   C CE2 . PHE A 1 3   ? 19.911  -0.163  33.651 1.00 26.30 ? 3   PHE B CE2 1 
ATOM   21   C CZ  . PHE A 1 3   ? 20.821  -0.613  32.712 1.00 23.11 ? 3   PHE B CZ  1 
ATOM   22   N N   . ARG A 1 4   ? 18.664  4.159   32.326 1.00 21.04 ? 4   ARG B N   1 
ATOM   23   C CA  . ARG A 1 4   ? 17.233  4.217   32.079 1.00 21.74 ? 4   ARG B CA  1 
ATOM   24   C C   . ARG A 1 4   ? 16.805  2.972   31.317 1.00 21.50 ? 4   ARG B C   1 
ATOM   25   O O   . ARG A 1 4   ? 17.564  2.448   30.504 1.00 25.10 ? 4   ARG B O   1 
ATOM   26   C CB  . ARG A 1 4   ? 16.871  5.464   31.264 1.00 23.52 ? 4   ARG B CB  1 
ATOM   27   C CG  . ARG A 1 4   ? 17.239  6.725   32.017 1.00 21.58 ? 4   ARG B CG  1 
ATOM   28   C CD  . ARG A 1 4   ? 16.296  6.890   33.204 1.00 28.55 ? 4   ARG B CD  1 
ATOM   29   N NE  . ARG A 1 4   ? 14.908  6.619   32.855 1.00 24.24 ? 4   ARG B NE  1 
ATOM   30   C CZ  . ARG A 1 4   ? 14.166  7.400   32.082 1.00 30.14 ? 4   ARG B CZ  1 
ATOM   31   N NH1 . ARG A 1 4   ? 14.590  8.598   31.699 1.00 22.71 ? 4   ARG B NH1 1 
ATOM   32   N NH2 . ARG A 1 4   ? 12.953  6.989   31.717 1.00 25.86 ? 4   ARG B NH2 1 
ATOM   33   N N   . LYS A 1 5   ? 15.587  2.506   31.575 1.00 20.85 ? 5   LYS B N   1 
ATOM   34   C CA  . LYS A 1 5   ? 15.006  1.510   30.689 1.00 22.80 ? 5   LYS B CA  1 
ATOM   35   C C   . LYS A 1 5   ? 14.821  2.122   29.308 1.00 20.62 ? 5   LYS B C   1 
ATOM   36   O O   . LYS A 1 5   ? 14.138  3.137   29.156 1.00 20.72 ? 5   LYS B O   1 
ATOM   37   C CB  . LYS A 1 5   ? 13.673  1.002   31.237 1.00 23.12 ? 5   LYS B CB  1 
ATOM   38   C CG  . LYS A 1 5   ? 13.169  -0.191  30.487 1.00 25.63 ? 5   LYS B CG  1 
ATOM   39   C CD  . LYS A 1 5   ? 12.101  -0.901  31.282 1.00 27.48 ? 5   LYS B CD  1 
ATOM   40   C CE  . LYS A 1 5   ? 12.724  -1.712  32.415 1.00 29.65 ? 5   LYS B CE  1 
ATOM   41   N NZ  . LYS A 1 5   ? 11.665  -2.337  33.235 1.00 27.87 ? 5   LYS B NZ  1 
ATOM   42   N N   . MET A 1 6   ? 15.433  1.503   28.305 1.00 23.75 ? 6   MET B N   1 
ATOM   43   C CA  . MET A 1 6   ? 15.650  2.122   27.006 1.00 23.29 ? 6   MET B CA  1 
ATOM   44   C C   . MET A 1 6   ? 15.210  1.178   25.899 1.00 24.54 ? 6   MET B C   1 
ATOM   45   O O   . MET A 1 6   ? 15.744  0.071   25.787 1.00 25.27 ? 6   MET B O   1 
ATOM   46   C CB  . MET A 1 6   ? 17.136  2.440   26.832 1.00 26.24 ? 6   MET B CB  1 
ATOM   47   C CG  . MET A 1 6   ? 17.463  3.303   25.669 1.00 28.74 ? 6   MET B CG  1 
ATOM   48   S SD  . MET A 1 6   ? 19.121  3.911   26.006 1.00 33.07 ? 6   MET B SD  1 
ATOM   49   C CE  . MET A 1 6   ? 20.066  2.467   25.568 1.00 32.75 ? 6   MET B CE  1 
ATOM   50   N N   . ALA A 1 7   ? 14.312  1.633   25.036 1.00 19.71 ? 7   ALA B N   1 
ATOM   51   C CA  . ALA A 1 7   ? 13.954  0.812   23.883 1.00 21.00 ? 7   ALA B CA  1 
ATOM   52   C C   . ALA A 1 7   ? 14.844  1.133   22.681 1.00 23.29 ? 7   ALA B C   1 
ATOM   53   O O   . ALA A 1 7   ? 15.472  2.189   22.610 1.00 22.19 ? 7   ALA B O   1 
ATOM   54   C CB  . ALA A 1 7   ? 12.492  1.021   23.504 1.00 20.58 ? 7   ALA B CB  1 
ATOM   55   N N   . PHE A 1 8   ? 14.872  0.214   21.717 1.00 21.34 ? 8   PHE B N   1 
ATOM   56   C CA  . PHE A 1 8   ? 15.543  0.504   20.456 1.00 22.36 ? 8   PHE B CA  1 
ATOM   57   C C   . PHE A 1 8   ? 14.789  1.569   19.658 1.00 21.38 ? 8   PHE B C   1 
ATOM   58   O O   . PHE A 1 8   ? 13.565  1.701   19.768 1.00 20.28 ? 8   PHE B O   1 
ATOM   59   C CB  . PHE A 1 8   ? 15.686  -0.756  19.604 1.00 25.78 ? 8   PHE B CB  1 
ATOM   60   C CG  . PHE A 1 8   ? 16.658  -1.756  20.154 1.00 26.87 ? 8   PHE B CG  1 
ATOM   61   C CD1 . PHE A 1 8   ? 18.011  -1.631  19.903 1.00 30.58 ? 8   PHE B CD1 1 
ATOM   62   C CD2 . PHE A 1 8   ? 16.221  -2.836  20.900 1.00 25.94 ? 8   PHE B CD2 1 
ATOM   63   C CE1 . PHE A 1 8   ? 18.903  -2.551  20.402 1.00 32.18 ? 8   PHE B CE1 1 
ATOM   64   C CE2 . PHE A 1 8   ? 17.119  -3.760  21.398 1.00 27.99 ? 8   PHE B CE2 1 
ATOM   65   C CZ  . PHE A 1 8   ? 18.461  -3.612  21.145 1.00 29.20 ? 8   PHE B CZ  1 
ATOM   66   N N   . PRO A 1 9   ? 15.504  2.352   18.847 1.00 24.79 ? 9   PRO B N   1 
ATOM   67   C CA  . PRO A 1 9   ? 14.816  3.288   17.947 1.00 21.05 ? 9   PRO B CA  1 
ATOM   68   C C   . PRO A 1 9   ? 13.914  2.485   17.023 1.00 24.86 ? 9   PRO B C   1 
ATOM   69   O O   . PRO A 1 9   ? 14.316  1.445   16.494 1.00 26.37 ? 9   PRO B O   1 
ATOM   70   C CB  . PRO A 1 9   ? 15.962  3.972   17.185 1.00 24.32 ? 9   PRO B CB  1 
ATOM   71   C CG  . PRO A 1 9   ? 17.213  3.725   18.026 1.00 26.45 ? 9   PRO B CG  1 
ATOM   72   C CD  . PRO A 1 9   ? 16.968  2.374   18.683 1.00 23.28 ? 9   PRO B CD  1 
ATOM   73   N N   . SER A 1 10  ? 12.681  2.950   16.865 1.00 23.88 ? 10  SER B N   1 
ATOM   74   C CA  . SER A 1 10  ? 11.611  2.146   16.290 1.00 25.39 ? 10  SER B CA  1 
ATOM   75   C C   . SER A 1 10  ? 11.352  2.417   14.813 1.00 25.53 ? 10  SER B C   1 
ATOM   76   O O   . SER A 1 10  ? 10.496  1.751   14.222 1.00 25.64 ? 10  SER B O   1 
ATOM   77   C CB  . SER A 1 10  ? 10.323  2.381   17.076 1.00 22.48 ? 10  SER B CB  1 
ATOM   78   O OG  . SER A 1 10  ? 9.953   3.760   17.026 1.00 24.09 ? 10  SER B OG  1 
ATOM   79   N N   . GLY A 1 11  ? 12.069  3.362   14.193 1.00 25.04 ? 11  GLY B N   1 
ATOM   80   C CA  . GLY A 1 11  ? 11.674  3.802   12.859 1.00 23.17 ? 11  GLY B CA  1 
ATOM   81   C C   . GLY A 1 11  ? 11.735  2.701   11.817 1.00 21.66 ? 11  GLY B C   1 
ATOM   82   O O   . GLY A 1 11  ? 10.917  2.665   10.893 1.00 24.04 ? 11  GLY B O   1 
ATOM   83   N N   . LYS A 1 12  ? 12.720  1.814   11.932 1.00 23.66 ? 12  LYS B N   1 
ATOM   84   C CA  . LYS A 1 12  ? 12.840  0.696   11.000 1.00 24.76 ? 12  LYS B CA  1 
ATOM   85   C C   . LYS A 1 12  ? 11.599  -0.184  11.040 1.00 26.07 ? 12  LYS B C   1 
ATOM   86   O O   . LYS A 1 12  ? 11.198  -0.749  10.014 1.00 26.16 ? 12  LYS B O   1 
ATOM   87   C CB  . LYS A 1 12  ? 14.085  -0.126  11.333 1.00 27.52 ? 12  LYS B CB  1 
ATOM   88   C CG  . LYS A 1 12  ? 15.375  0.397   10.694 1.00 28.94 ? 12  LYS B CG  1 
ATOM   89   C CD  . LYS A 1 12  ? 16.559  -0.494  11.020 1.00 32.61 ? 12  LYS B CD  1 
ATOM   90   C CE  . LYS A 1 12  ? 17.783  -0.073  10.229 1.00 41.09 ? 12  LYS B CE  1 
ATOM   91   N NZ  . LYS A 1 12  ? 17.645  1.358   9.819  1.00 40.07 ? 12  LYS B NZ  1 
ATOM   92   N N   . VAL A 1 13  ? 10.969  -0.291  12.205 1.00 22.04 ? 13  VAL B N   1 
ATOM   93   C CA  . VAL A 1 13  ? 9.763   -1.107  12.325 1.00 21.78 ? 13  VAL B CA  1 
ATOM   94   C C   . VAL A 1 13  ? 8.521   -0.307  11.949 1.00 24.36 ? 13  VAL B C   1 
ATOM   95   O O   . VAL A 1 13  ? 7.589   -0.842  11.331 1.00 21.99 ? 13  VAL B O   1 
ATOM   96   C CB  . VAL A 1 13  ? 9.661   -1.680  13.748 1.00 22.11 ? 13  VAL B CB  1 
ATOM   97   C CG1 . VAL A 1 13  ? 8.351   -2.475  13.918 1.00 24.61 ? 13  VAL B CG1 1 
ATOM   98   C CG2 . VAL A 1 13  ? 10.869  -2.548  14.059 1.00 25.59 ? 13  VAL B CG2 1 
ATOM   99   N N   . GLU A 1 14  ? 8.482   0.983   12.320 1.00 24.06 ? 14  GLU B N   1 
ATOM   100  C CA  . GLU A 1 14  ? 7.366   1.846   11.948 1.00 21.91 ? 14  GLU B CA  1 
ATOM   101  C C   . GLU A 1 14  ? 7.077   1.772   10.456 1.00 23.04 ? 14  GLU B C   1 
ATOM   102  O O   . GLU A 1 14  ? 5.916   1.735   10.043 1.00 25.45 ? 14  GLU B O   1 
ATOM   103  C CB  . GLU A 1 14  ? 7.674   3.293   12.346 1.00 25.28 ? 14  GLU B CB  1 
ATOM   104  C CG  . GLU A 1 14  ? 7.740   3.507   13.840 1.00 23.59 ? 14  GLU B CG  1 
ATOM   105  C CD  . GLU A 1 14  ? 8.246   4.889   14.193 1.00 25.54 ? 14  GLU B CD  1 
ATOM   106  O OE1 . GLU A 1 14  ? 7.684   5.872   13.678 1.00 22.63 ? 14  GLU B OE1 1 
ATOM   107  O OE2 . GLU A 1 14  ? 9.198   4.977   14.986 1.00 25.23 ? 14  GLU B OE2 1 
ATOM   108  N N   . GLY A 1 15  ? 8.122   1.730   9.633  1.00 28.18 ? 15  GLY B N   1 
ATOM   109  C CA  . GLY A 1 15  ? 7.931   1.669   8.195  1.00 25.26 ? 15  GLY B CA  1 
ATOM   110  C C   . GLY A 1 15  ? 7.386   0.357   7.691  1.00 29.62 ? 15  GLY B C   1 
ATOM   111  O O   . GLY A 1 15  ? 7.198   0.204   6.482  1.00 31.60 ? 15  GLY B O   1 
ATOM   112  N N   . CYS A 1 16  ? 7.131   -0.593  8.590  1.00 24.13 ? 16  CYS B N   1 
ATOM   113  C CA  . CYS A 1 16  ? 6.570   -1.888  8.243  1.00 25.68 ? 16  CYS B CA  1 
ATOM   114  C C   . CYS A 1 16  ? 5.156   -2.093  8.762  1.00 25.13 ? 16  CYS B C   1 
ATOM   115  O O   . CYS A 1 16  ? 4.527   -3.101  8.420  1.00 24.94 ? 16  CYS B O   1 
ATOM   116  C CB  . CYS A 1 16  ? 7.469   -3.007  8.787  1.00 25.06 ? 16  CYS B CB  1 
ATOM   117  S SG  . CYS A 1 16  ? 9.157   -2.991  8.119  1.00 27.91 ? 16  CYS B SG  1 
ATOM   118  N N   . MET A 1 17  ? 4.638   -1.189  9.582  1.00 25.37 ? 17  MET B N   1 
ATOM   119  C CA  . MET A 1 17  ? 3.324   -1.396  10.176 1.00 24.58 ? 17  MET B CA  1 
ATOM   120  C C   . MET A 1 17  ? 2.206   -0.982  9.232  1.00 25.13 ? 17  MET B C   1 
ATOM   121  O O   . MET A 1 17  ? 2.229   0.113   8.658  1.00 26.68 ? 17  MET B O   1 
ATOM   122  C CB  . MET A 1 17  ? 3.203   -0.644  11.500 1.00 24.85 ? 17  MET B CB  1 
ATOM   123  C CG  . MET A 1 17  ? 4.284   -0.993  12.492 1.00 23.78 ? 17  MET B CG  1 
ATOM   124  S SD  . MET A 1 17  ? 4.389   -2.777  12.779 1.00 24.17 ? 17  MET B SD  1 
ATOM   125  C CE  . MET A 1 17  ? 2.681   -3.209  13.164 1.00 21.20 ? 17  MET B CE  1 
ATOM   126  N N   . VAL A 1 18  ? 1.216   -1.867  9.093  1.00 24.25 ? 18  VAL B N   1 
ATOM   127  C CA  . VAL A 1 18  ? 0.035   -1.645  8.276  1.00 25.23 ? 18  VAL B CA  1 
ATOM   128  C C   . VAL A 1 18  ? -1.194  -2.046  9.079  1.00 25.22 ? 18  VAL B C   1 
ATOM   129  O O   . VAL A 1 18  ? -1.108  -2.650  10.150 1.00 24.62 ? 18  VAL B O   1 
ATOM   130  C CB  . VAL A 1 18  ? 0.077   -2.427  6.946  1.00 24.20 ? 18  VAL B CB  1 
ATOM   131  C CG1 . VAL A 1 18  ? 1.227   -1.940  6.077  1.00 24.75 ? 18  VAL B CG1 1 
ATOM   132  C CG2 . VAL A 1 18  ? 0.149   -3.942  7.207  1.00 25.84 ? 18  VAL B CG2 1 
ATOM   133  N N   . GLN A 1 19  ? -2.353  -1.686  8.546  1.00 22.07 ? 19  GLN B N   1 
ATOM   134  C CA  . GLN A 1 19  ? -3.632  -2.016  9.150  1.00 27.76 ? 19  GLN B CA  1 
ATOM   135  C C   . GLN A 1 19  ? -4.300  -3.112  8.326  1.00 29.38 ? 19  GLN B C   1 
ATOM   136  O O   . GLN A 1 19  ? -4.330  -3.036  7.094  1.00 30.04 ? 19  GLN B O   1 
ATOM   137  C CB  . GLN A 1 19  ? -4.496  -0.760  9.230  1.00 28.66 ? 19  GLN B CB  1 
ATOM   138  C CG  . GLN A 1 19  ? -5.891  -0.975  9.720  1.00 30.51 ? 19  GLN B CG  1 
ATOM   139  C CD  . GLN A 1 19  ? -6.732  0.271   9.575  1.00 35.97 ? 19  GLN B CD  1 
ATOM   140  O OE1 . GLN A 1 19  ? -7.411  0.684   10.511 1.00 40.89 ? 19  GLN B OE1 1 
ATOM   141  N NE2 . GLN A 1 19  ? -6.687  0.883   8.399  1.00 44.02 ? 19  GLN B NE2 1 
ATOM   142  N N   . VAL A 1 20  ? -4.826  -4.131  9.000  1.00 25.26 ? 20  VAL B N   1 
ATOM   143  C CA  . VAL A 1 20  ? -5.487  -5.249  8.338  1.00 26.00 ? 20  VAL B CA  1 
ATOM   144  C C   . VAL A 1 20  ? -6.914  -5.319  8.850  1.00 28.08 ? 20  VAL B C   1 
ATOM   145  O O   . VAL A 1 20  ? -7.142  -5.436  10.061 1.00 27.55 ? 20  VAL B O   1 
ATOM   146  C CB  . VAL A 1 20  ? -4.761  -6.577  8.582  1.00 25.70 ? 20  VAL B CB  1 
ATOM   147  C CG1 . VAL A 1 20  ? -5.475  -7.710  7.848  1.00 28.33 ? 20  VAL B CG1 1 
ATOM   148  C CG2 . VAL A 1 20  ? -3.315  -6.479  8.142  1.00 27.49 ? 20  VAL B CG2 1 
ATOM   149  N N   . THR A 1 21  ? -7.871  -5.245  7.937  1.00 28.73 ? 21  THR B N   1 
ATOM   150  C CA  . THR A 1 21  ? -9.275  -5.385  8.278  1.00 30.81 ? 21  THR B CA  1 
ATOM   151  C C   . THR A 1 21  ? -9.837  -6.602  7.566  1.00 30.58 ? 21  THR B C   1 
ATOM   152  O O   . THR A 1 21  ? -9.584  -6.804  6.374  1.00 31.97 ? 21  THR B O   1 
ATOM   153  C CB  . THR A 1 21  ? -10.067 -4.136  7.899  1.00 29.52 ? 21  THR B CB  1 
ATOM   154  O OG1 . THR A 1 21  ? -9.516  -3.004  8.583  1.00 34.13 ? 21  THR B OG1 1 
ATOM   155  C CG2 . THR A 1 21  ? -11.526 -4.304  8.286  1.00 32.39 ? 21  THR B CG2 1 
ATOM   156  N N   . CYS A 1 22  ? -10.575 -7.418  8.309  1.00 31.78 ? 22  CYS B N   1 
ATOM   157  C CA  . CYS A 1 22  ? -11.292 -8.546  7.739  1.00 31.08 ? 22  CYS B CA  1 
ATOM   158  C C   . CYS A 1 22  ? -12.660 -8.589  8.397  1.00 33.80 ? 22  CYS B C   1 
ATOM   159  O O   . CYS A 1 22  ? -12.763 -8.742  9.620  1.00 30.85 ? 22  CYS B O   1 
ATOM   160  C CB  . CYS A 1 22  ? -10.522 -9.848  7.954  1.00 34.17 ? 22  CYS B CB  1 
ATOM   161  S SG  . CYS A 1 22  ? -11.279 -11.298 7.197  1.00 35.92 ? 22  CYS B SG  1 
ATOM   162  N N   . GLY A 1 23  ? -13.699 -8.434  7.596  1.00 35.58 ? 23  GLY B N   1 
ATOM   163  C CA  . GLY A 1 23  ? -15.023 -8.240  8.160  1.00 37.30 ? 23  GLY B CA  1 
ATOM   164  C C   . GLY A 1 23  ? -15.031 -7.041  9.093  1.00 34.00 ? 23  GLY B C   1 
ATOM   165  O O   . GLY A 1 23  ? -14.674 -5.915  8.718  1.00 35.47 ? 23  GLY B O   1 
ATOM   166  N N   . THR A 1 24  ? -15.417 -7.290  10.341 1.00 34.84 ? 24  THR B N   1 
ATOM   167  C CA  . THR A 1 24  ? -15.539 -6.261  11.363 1.00 38.84 ? 24  THR B CA  1 
ATOM   168  C C   . THR A 1 24  ? -14.317 -6.167  12.273 1.00 39.39 ? 24  THR B C   1 
ATOM   169  O O   . THR A 1 24  ? -14.312 -5.353  13.200 1.00 39.73 ? 24  THR B O   1 
ATOM   170  C CB  . THR A 1 24  ? -16.794 -6.525  12.197 1.00 42.17 ? 24  THR B CB  1 
ATOM   171  O OG1 . THR A 1 24  ? -16.710 -7.830  12.783 1.00 42.41 ? 24  THR B OG1 1 
ATOM   172  C CG2 . THR A 1 24  ? -18.029 -6.459  11.315 1.00 44.25 ? 24  THR B CG2 1 
ATOM   173  N N   . THR A 1 25  ? -13.287 -6.967  12.026 1.00 34.92 ? 25  THR B N   1 
ATOM   174  C CA  . THR A 1 25  ? -12.093 -7.000  12.858 1.00 34.46 ? 25  THR B CA  1 
ATOM   175  C C   . THR A 1 25  ? -10.963 -6.258  12.161 1.00 31.85 ? 25  THR B C   1 
ATOM   176  O O   . THR A 1 25  ? -10.637 -6.549  11.005 1.00 28.38 ? 25  THR B O   1 
ATOM   177  C CB  . THR A 1 25  ? -11.677 -8.441  13.165 1.00 32.48 ? 25  THR B CB  1 
ATOM   178  O OG1 . THR A 1 25  ? -12.805 -9.178  13.665 1.00 34.77 ? 25  THR B OG1 1 
ATOM   179  C CG2 . THR A 1 25  ? -10.530 -8.486  14.175 1.00 34.09 ? 25  THR B CG2 1 
ATOM   180  N N   . THR A 1 26  ? -10.380 -5.295  12.865 1.00 28.79 ? 26  THR B N   1 
ATOM   181  C CA  . THR A 1 26  ? -9.237  -4.538  12.384 1.00 28.71 ? 26  THR B CA  1 
ATOM   182  C C   . THR A 1 26  ? -8.113  -4.704  13.392 1.00 28.80 ? 26  THR B C   1 
ATOM   183  O O   . THR A 1 26  ? -8.343  -4.605  14.600 1.00 30.18 ? 26  THR B O   1 
ATOM   184  C CB  . THR A 1 26  ? -9.592  -3.059  12.216 1.00 32.78 ? 26  THR B CB  1 
ATOM   185  O OG1 . THR A 1 26  ? -10.520 -2.909  11.134 1.00 35.55 ? 26  THR B OG1 1 
ATOM   186  C CG2 . THR A 1 26  ? -8.348  -2.240  11.922 1.00 31.21 ? 26  THR B CG2 1 
ATOM   187  N N   . LEU A 1 27  ? -6.910  -4.977  12.903 1.00 28.07 ? 27  LEU B N   1 
ATOM   188  C CA  . LEU A 1 27  ? -5.745  -5.035  13.770 1.00 24.31 ? 27  LEU B CA  1 
ATOM   189  C C   . LEU A 1 27  ? -4.538  -4.668  12.919 1.00 20.31 ? 27  LEU B C   1 
ATOM   190  O O   . LEU A 1 27  ? -4.684  -4.167  11.802 1.00 21.41 ? 27  LEU B O   1 
ATOM   191  C CB  . LEU A 1 27  ? -5.614  -6.410  14.449 1.00 23.55 ? 27  LEU B CB  1 
ATOM   192  C CG  . LEU A 1 27  ? -5.903  -7.695  13.679 1.00 21.91 ? 27  LEU B CG  1 
ATOM   193  C CD1 . LEU A 1 27  ? -4.845  -7.857  12.576 1.00 23.15 ? 27  LEU B CD1 1 
ATOM   194  C CD2 . LEU A 1 27  ? -5.862  -8.881  14.617 1.00 23.37 ? 27  LEU B CD2 1 
ATOM   195  N N   . ASN A 1 28  ? -3.350  -4.924  13.446 1.00 20.92 ? 28  ASN B N   1 
ATOM   196  C CA  . ASN A 1 28  ? -2.105  -4.512  12.824 1.00 23.04 ? 28  ASN B CA  1 
ATOM   197  C C   . ASN A 1 28  ? -1.463  -5.682  12.097 1.00 20.89 ? 28  ASN B C   1 
ATOM   198  O O   . ASN A 1 28  ? -1.620  -6.842  12.486 1.00 21.15 ? 28  ASN B O   1 
ATOM   199  C CB  . ASN A 1 28  ? -1.132  -3.974  13.869 1.00 22.88 ? 28  ASN B CB  1 
ATOM   200  C CG  . ASN A 1 28  ? -1.732  -2.868  14.685 1.00 23.14 ? 28  ASN B CG  1 
ATOM   201  O OD1 . ASN A 1 28  ? -1.900  -1.755  14.198 1.00 24.57 ? 28  ASN B OD1 1 
ATOM   202  N ND2 . ASN A 1 28  ? -2.089  -3.172  15.925 1.00 22.62 ? 28  ASN B ND2 1 
ATOM   203  N N   . GLY A 1 29  ? -0.722  -5.355  11.038 1.00 22.69 ? 29  GLY B N   1 
ATOM   204  C CA  . GLY A 1 29  ? 0.087   -6.332  10.345 1.00 22.47 ? 29  GLY B CA  1 
ATOM   205  C C   . GLY A 1 29  ? 1.492   -5.795  10.151 1.00 23.94 ? 29  GLY B C   1 
ATOM   206  O O   . GLY A 1 29  ? 1.753   -4.613  10.331 1.00 23.37 ? 29  GLY B O   1 
ATOM   207  N N   . LEU A 1 30  ? 2.399   -6.698  9.781  1.00 23.07 ? 30  LEU B N   1 
ATOM   208  C CA  . LEU A 1 30  ? 3.808   -6.385  9.577  1.00 23.87 ? 30  LEU B CA  1 
ATOM   209  C C   . LEU A 1 30  ? 4.131   -6.628  8.110  1.00 25.14 ? 30  LEU B C   1 
ATOM   210  O O   . LEU A 1 30  ? 4.016   -7.760  7.629  1.00 25.41 ? 30  LEU B O   1 
ATOM   211  C CB  . LEU A 1 30  ? 4.700   -7.239  10.479 1.00 24.11 ? 30  LEU B CB  1 
ATOM   212  C CG  . LEU A 1 30  ? 6.209   -7.002  10.403 1.00 21.49 ? 30  LEU B CG  1 
ATOM   213  C CD1 . LEU A 1 30  ? 6.583   -5.682  11.078 1.00 21.66 ? 30  LEU B CD1 1 
ATOM   214  C CD2 . LEU A 1 30  ? 6.986   -8.155  11.018 1.00 24.56 ? 30  LEU B CD2 1 
ATOM   215  N N   . TRP A 1 31  ? 4.511   -5.569  7.397  1.00 23.43 ? 31  TRP B N   1 
ATOM   216  C CA  . TRP A 1 31  ? 4.634   -5.609  5.940  1.00 26.01 ? 31  TRP B CA  1 
ATOM   217  C C   . TRP A 1 31  ? 6.116   -5.698  5.586  1.00 26.72 ? 31  TRP B C   1 
ATOM   218  O O   . TRP A 1 31  ? 6.856   -4.720  5.739  1.00 29.95 ? 31  TRP B O   1 
ATOM   219  C CB  . TRP A 1 31  ? 3.978   -4.373  5.324  1.00 26.63 ? 31  TRP B CB  1 
ATOM   220  C CG  . TRP A 1 31  ? 4.034   -4.259  3.812  1.00 30.78 ? 31  TRP B CG  1 
ATOM   221  C CD1 . TRP A 1 31  ? 4.141   -5.282  2.904  1.00 29.51 ? 31  TRP B CD1 1 
ATOM   222  C CD2 . TRP A 1 31  ? 3.934   -3.051  3.042  1.00 30.16 ? 31  TRP B CD2 1 
ATOM   223  N NE1 . TRP A 1 31  ? 4.116   -4.777  1.624  1.00 29.77 ? 31  TRP B NE1 1 
ATOM   224  C CE2 . TRP A 1 31  ? 3.994   -3.413  1.682  1.00 32.00 ? 31  TRP B CE2 1 
ATOM   225  C CE3 . TRP A 1 31  ? 3.794   -1.701  3.375  1.00 28.03 ? 31  TRP B CE3 1 
ATOM   226  C CZ2 . TRP A 1 31  ? 3.929   -2.470  0.654  1.00 31.30 ? 31  TRP B CZ2 1 
ATOM   227  C CZ3 . TRP A 1 31  ? 3.729   -0.766  2.352  1.00 35.69 ? 31  TRP B CZ3 1 
ATOM   228  C CH2 . TRP A 1 31  ? 3.804   -1.158  1.009  1.00 37.58 ? 31  TRP B CH2 1 
ATOM   229  N N   . LEU A 1 32  ? 6.560   -6.874  5.141  1.00 25.96 ? 32  LEU B N   1 
ATOM   230  C CA  . LEU A 1 32  ? 7.951   -7.075  4.734  1.00 27.84 ? 32  LEU B CA  1 
ATOM   231  C C   . LEU A 1 32  ? 7.967   -7.683  3.339  1.00 31.41 ? 32  LEU B C   1 
ATOM   232  O O   . LEU A 1 32  ? 7.425   -8.774  3.129  1.00 26.43 ? 32  LEU B O   1 
ATOM   233  C CB  . LEU A 1 32  ? 8.706   -7.976  5.717  1.00 26.03 ? 32  LEU B CB  1 
ATOM   234  C CG  . LEU A 1 32  ? 8.639   -7.630  7.205  1.00 25.50 ? 32  LEU B CG  1 
ATOM   235  C CD1 . LEU A 1 32  ? 9.038   -8.849  8.022  1.00 22.18 ? 32  LEU B CD1 1 
ATOM   236  C CD2 . LEU A 1 32  ? 9.557   -6.463  7.518  1.00 24.08 ? 32  LEU B CD2 1 
ATOM   237  N N   . ASP A 1 33  ? 8.605   -6.987  2.396  1.00 33.22 ? 33  ASP B N   1 
ATOM   238  C CA  . ASP A 1 33  ? 8.574   -7.352  0.968  1.00 30.65 ? 33  ASP B CA  1 
ATOM   239  C C   . ASP A 1 33  ? 7.107   -7.366  0.547  1.00 31.23 ? 33  ASP B C   1 
ATOM   240  O O   . ASP A 1 33  ? 6.365   -6.426  0.880  1.00 31.27 ? 33  ASP B O   1 
ATOM   241  C CB  . ASP A 1 33  ? 9.331   -8.652  0.722  1.00 33.12 ? 33  ASP B CB  1 
ATOM   242  C CG  . ASP A 1 33  ? 10.797  -8.550  1.065  1.00 36.30 ? 33  ASP B CG  1 
ATOM   243  O OD1 . ASP A 1 33  ? 11.373  -7.472  0.851  1.00 36.19 ? 33  ASP B OD1 1 
ATOM   244  O OD2 . ASP A 1 33  ? 11.377  -9.555  1.524  1.00 39.62 ? 33  ASP B OD2 1 
ATOM   245  N N   . ASP A 1 34  ? 6.635   -8.395  -0.157 1.00 30.77 ? 34  ASP B N   1 
ATOM   246  C CA  . ASP A 1 34  ? 5.250   -8.460  -0.597 1.00 32.39 ? 34  ASP B CA  1 
ATOM   247  C C   . ASP A 1 34  ? 4.402   -9.361  0.294  1.00 30.38 ? 34  ASP B C   1 
ATOM   248  O O   . ASP A 1 34  ? 3.400   -9.917  -0.164 1.00 31.91 ? 34  ASP B O   1 
ATOM   249  C CB  . ASP A 1 34  ? 5.175   -8.918  -2.056 1.00 34.11 ? 34  ASP B CB  1 
ATOM   250  C CG  . ASP A 1 34  ? 5.814   -10.271 -2.277 1.00 36.52 ? 34  ASP B CG  1 
ATOM   251  O OD1 . ASP A 1 34  ? 6.579   -10.724 -1.402 1.00 37.87 ? 34  ASP B OD1 1 
ATOM   252  O OD2 . ASP A 1 34  ? 5.546   -10.891 -3.329 1.00 42.36 ? 34  ASP B OD2 1 
ATOM   253  N N   . VAL A 1 35  ? 4.769   -9.512  1.565  1.00 29.99 ? 35  VAL B N   1 
ATOM   254  C CA  . VAL A 1 35  ? 3.986   -10.309 2.502  1.00 28.04 ? 35  VAL B CA  1 
ATOM   255  C C   . VAL A 1 35  ? 3.639   -9.450  3.708  1.00 26.18 ? 35  VAL B C   1 
ATOM   256  O O   . VAL A 1 35  ? 4.497   -8.731  4.230  1.00 24.90 ? 35  VAL B O   1 
ATOM   257  C CB  . VAL A 1 35  ? 4.732   -11.578 2.957  1.00 27.41 ? 35  VAL B CB  1 
ATOM   258  C CG1 . VAL A 1 35  ? 3.890   -12.337 3.986  1.00 28.94 ? 35  VAL B CG1 1 
ATOM   259  C CG2 . VAL A 1 35  ? 5.072   -12.463 1.760  1.00 31.73 ? 35  VAL B CG2 1 
ATOM   260  N N   . VAL A 1 36  ? 2.385   -9.542  4.153  1.00 25.28 ? 36  VAL B N   1 
ATOM   261  C CA  . VAL A 1 36  ? 1.921   -8.919  5.388  1.00 23.62 ? 36  VAL B CA  1 
ATOM   262  C C   . VAL A 1 36  ? 1.617   -10.028 6.390  1.00 25.91 ? 36  VAL B C   1 
ATOM   263  O O   . VAL A 1 36  ? 0.817   -10.929 6.104  1.00 27.08 ? 36  VAL B O   1 
ATOM   264  C CB  . VAL A 1 36  ? 0.689   -8.035  5.153  1.00 25.52 ? 36  VAL B CB  1 
ATOM   265  C CG1 . VAL A 1 36  ? 0.038   -7.682  6.478  1.00 25.52 ? 36  VAL B CG1 1 
ATOM   266  C CG2 . VAL A 1 36  ? 1.068   -6.771  4.381  1.00 25.39 ? 36  VAL B CG2 1 
ATOM   267  N N   . TYR A 1 37  ? 2.255   -9.962  7.556  1.00 23.45 ? 37  TYR B N   1 
ATOM   268  C CA  . TYR A 1 37  ? 2.083   -10.937 8.628  1.00 23.42 ? 37  TYR B CA  1 
ATOM   269  C C   . TYR A 1 37  ? 1.140   -10.360 9.674  1.00 25.15 ? 37  TYR B C   1 
ATOM   270  O O   . TYR A 1 37  ? 1.305   -9.212  10.078 1.00 22.60 ? 37  TYR B O   1 
ATOM   271  C CB  . TYR A 1 37  ? 3.429   -11.267 9.272  1.00 22.64 ? 37  TYR B CB  1 
ATOM   272  C CG  . TYR A 1 37  ? 4.469   -11.776 8.301  1.00 27.71 ? 37  TYR B CG  1 
ATOM   273  C CD1 . TYR A 1 37  ? 5.224   -10.899 7.530  1.00 24.34 ? 37  TYR B CD1 1 
ATOM   274  C CD2 . TYR A 1 37  ? 4.709   -13.133 8.174  1.00 28.47 ? 37  TYR B CD2 1 
ATOM   275  C CE1 . TYR A 1 37  ? 6.189   -11.372 6.636  1.00 28.43 ? 37  TYR B CE1 1 
ATOM   276  C CE2 . TYR A 1 37  ? 5.666   -13.609 7.291  1.00 29.27 ? 37  TYR B CE2 1 
ATOM   277  C CZ  . TYR A 1 37  ? 6.394   -12.730 6.523  1.00 28.92 ? 37  TYR B CZ  1 
ATOM   278  O OH  . TYR A 1 37  ? 7.345   -13.213 5.640  1.00 31.35 ? 37  TYR B OH  1 
ATOM   279  N N   . CYS A 1 38  ? 0.163   -11.145 10.126 1.00 22.25 ? 38  CYS B N   1 
ATOM   280  C CA  . CYS A 1 38  ? -0.744  -10.658 11.160 1.00 22.38 ? 38  CYS B CA  1 
ATOM   281  C C   . CYS A 1 38  ? -1.312  -11.860 11.901 1.00 23.08 ? 38  CYS B C   1 
ATOM   282  O O   . CYS A 1 38  ? -1.141  -13.009 11.460 1.00 21.50 ? 38  CYS B O   1 
ATOM   283  C CB  . CYS A 1 38  ? -1.861  -9.781  10.560 1.00 21.99 ? 38  CYS B CB  1 
ATOM   284  S SG  . CYS A 1 38  ? -3.122  -10.678 9.637  1.00 26.08 ? 38  CYS B SG  1 
ATOM   285  N N   . PRO A 1 39  ? -1.949  -11.642 13.056 1.00 22.30 ? 39  PRO B N   1 
ATOM   286  C CA  . PRO A 1 39  ? -2.552  -12.772 13.782 1.00 20.48 ? 39  PRO B CA  1 
ATOM   287  C C   . PRO A 1 39  ? -3.704  -13.379 12.996 1.00 21.78 ? 39  PRO B C   1 
ATOM   288  O O   . PRO A 1 39  ? -4.528  -12.667 12.415 1.00 21.50 ? 39  PRO B O   1 
ATOM   289  C CB  . PRO A 1 39  ? -3.044  -12.142 15.091 1.00 20.07 ? 39  PRO B CB  1 
ATOM   290  C CG  . PRO A 1 39  ? -2.265  -10.852 15.219 1.00 21.78 ? 39  PRO B CG  1 
ATOM   291  C CD  . PRO A 1 39  ? -2.062  -10.377 13.818 1.00 23.30 ? 39  PRO B CD  1 
ATOM   292  N N   . ARG A 1 40  ? -3.759  -14.716 12.976 1.00 24.26 ? 40  ARG B N   1 
ATOM   293  C CA  . ARG A 1 40  ? -4.794  -15.366 12.183 1.00 23.37 ? 40  ARG B CA  1 
ATOM   294  C C   . ARG A 1 40  ? -6.194  -15.075 12.705 1.00 22.53 ? 40  ARG B C   1 
ATOM   295  O O   . ARG A 1 40  ? -7.157  -15.163 11.938 1.00 22.84 ? 40  ARG B O   1 
ATOM   296  C CB  . ARG A 1 40  ? -4.567  -16.884 12.124 1.00 21.24 ? 40  ARG B CB  1 
ATOM   297  C CG  . ARG A 1 40  ? -4.745  -17.625 13.428 1.00 22.38 ? 40  ARG B CG  1 
ATOM   298  C CD  . ARG A 1 40  ? -4.552  -19.135 13.194 1.00 24.18 ? 40  ARG B CD  1 
ATOM   299  N NE  . ARG A 1 40  ? -4.507  -19.875 14.447 1.00 26.32 ? 40  ARG B NE  1 
ATOM   300  C CZ  . ARG A 1 40  ? -4.537  -21.200 14.528 1.00 29.20 ? 40  ARG B CZ  1 
ATOM   301  N NH1 . ARG A 1 40  ? -4.561  -21.959 13.440 1.00 25.27 ? 40  ARG B NH1 1 
ATOM   302  N NH2 . ARG A 1 40  ? -4.551  -21.776 15.727 1.00 24.41 ? 40  ARG B NH2 1 
ATOM   303  N N   . HIS A 1 41  ? -6.342  -14.681 13.971 1.00 20.21 ? 41  HIS B N   1 
ATOM   304  C CA  . HIS A 1 41  ? -7.708  -14.480 14.449 1.00 24.99 ? 41  HIS B CA  1 
ATOM   305  C C   . HIS A 1 41  ? -8.362  -13.241 13.864 1.00 25.98 ? 41  HIS B C   1 
ATOM   306  O O   . HIS A 1 41  ? -9.518  -12.969 14.203 1.00 25.30 ? 41  HIS B O   1 
ATOM   307  C CB  . HIS A 1 41  ? -7.781  -14.447 15.989 1.00 24.60 ? 41  HIS B CB  1 
ATOM   308  C CG  . HIS A 1 41  ? -7.041  -13.310 16.640 1.00 25.61 ? 41  HIS B CG  1 
ATOM   309  N ND1 . HIS A 1 41  ? -5.708  -13.385 16.983 1.00 22.40 ? 41  HIS B ND1 1 
ATOM   310  C CD2 . HIS A 1 41  ? -7.467  -12.091 17.054 1.00 28.79 ? 41  HIS B CD2 1 
ATOM   311  C CE1 . HIS A 1 41  ? -5.339  -12.255 17.563 1.00 25.59 ? 41  HIS B CE1 1 
ATOM   312  N NE2 . HIS A 1 41  ? -6.387  -11.450 17.612 1.00 25.38 ? 41  HIS B NE2 1 
ATOM   313  N N   . VAL A 1 42  ? -7.678  -12.513 12.975 1.00 22.48 ? 42  VAL B N   1 
ATOM   314  C CA  . VAL A 1 42  ? -8.322  -11.430 12.237 1.00 25.78 ? 42  VAL B CA  1 
ATOM   315  C C   . VAL A 1 42  ? -9.509  -11.937 11.419 1.00 27.09 ? 42  VAL B C   1 
ATOM   316  O O   . VAL A 1 42  ? -10.439 -11.173 11.129 1.00 25.13 ? 42  VAL B O   1 
ATOM   317  C CB  . VAL A 1 42  ? -7.273  -10.706 11.356 1.00 22.70 ? 42  VAL B CB  1 
ATOM   318  C CG1 . VAL A 1 42  ? -6.883  -11.539 10.141 1.00 25.29 ? 42  VAL B CG1 1 
ATOM   319  C CG2 . VAL A 1 42  ? -7.777  -9.309  10.937 1.00 25.13 ? 42  VAL B CG2 1 
ATOM   320  N N   . ILE A 1 43  ? -9.523  -13.225 11.065 1.00 27.70 ? 43  ILE B N   1 
ATOM   321  C CA  . ILE A 1 43  ? -10.627 -13.767 10.274 1.00 29.32 ? 43  ILE B CA  1 
ATOM   322  C C   . ILE A 1 43  ? -11.827 -14.186 11.108 1.00 33.20 ? 43  ILE B C   1 
ATOM   323  O O   . ILE A 1 43  ? -12.863 -14.539 10.534 1.00 32.20 ? 43  ILE B O   1 
ATOM   324  C CB  . ILE A 1 43  ? -10.171 -14.971 9.427  1.00 27.44 ? 43  ILE B CB  1 
ATOM   325  C CG1 . ILE A 1 43  ? -9.906  -16.194 10.307 1.00 22.62 ? 43  ILE B CG1 1 
ATOM   326  C CG2 . ILE A 1 43  ? -8.934  -14.617 8.590  1.00 25.02 ? 43  ILE B CG2 1 
ATOM   327  C CD1 . ILE A 1 43  ? -9.244  -17.334 9.566  1.00 29.52 ? 43  ILE B CD1 1 
ATOM   328  N N   . CYS A 1 44  ? -11.733 -14.131 12.434 1.00 30.83 ? 44  CYS B N   1 
ATOM   329  C CA  . CYS A 1 44  ? -12.792 -14.621 13.312 1.00 34.07 ? 44  CYS B CA  1 
ATOM   330  C C   . CYS A 1 44  ? -13.808 -13.544 13.672 1.00 40.15 ? 44  CYS B C   1 
ATOM   331  O O   . CYS A 1 44  ? -13.454 -12.382 13.882 1.00 36.90 ? 44  CYS B O   1 
ATOM   332  C CB  . CYS A 1 44  ? -12.197 -15.153 14.610 1.00 35.49 ? 44  CYS B CB  1 
ATOM   333  S SG  . CYS A 1 44  ? -11.161 -16.557 14.399 1.00 35.07 ? 44  CYS B SG  1 
ATOM   334  N N   . THR A 1 45  ? -15.072 -13.954 13.768 1.00 43.40 ? 45  THR B N   1 
ATOM   335  C CA  . THR A 1 45  ? -16.075 -13.206 14.508 1.00 48.25 ? 45  THR B CA  1 
ATOM   336  C C   . THR A 1 45  ? -15.933 -13.533 15.995 1.00 48.03 ? 45  THR B C   1 
ATOM   337  O O   . THR A 1 45  ? -15.284 -14.513 16.375 1.00 45.87 ? 45  THR B O   1 
ATOM   338  C CB  . THR A 1 45  ? -17.482 -13.568 14.027 1.00 49.06 ? 45  THR B CB  1 
ATOM   339  O OG1 . THR A 1 45  ? -17.497 -13.655 12.599 1.00 50.58 ? 45  THR B OG1 1 
ATOM   340  C CG2 . THR A 1 45  ? -18.494 -12.508 14.459 1.00 54.71 ? 45  THR B CG2 1 
ATOM   341  N N   . SER A 1 46  ? -16.550 -12.710 16.850 1.00 51.65 ? 46  SER B N   1 
ATOM   342  C CA  . SER A 1 46  ? -16.615 -13.059 18.267 1.00 52.15 ? 46  SER B CA  1 
ATOM   343  C C   . SER A 1 46  ? -17.244 -14.434 18.454 1.00 49.78 ? 46  SER B C   1 
ATOM   344  O O   . SER A 1 46  ? -16.800 -15.221 19.299 1.00 50.04 ? 46  SER B O   1 
ATOM   345  C CB  . SER A 1 46  ? -17.395 -11.998 19.046 1.00 51.11 ? 46  SER B CB  1 
ATOM   346  O OG  . SER A 1 46  ? -18.726 -11.901 18.573 1.00 53.73 ? 46  SER B OG  1 
ATOM   347  N N   . GLU A 1 47  ? -18.262 -14.750 17.647 1.00 50.56 ? 47  GLU B N   1 
ATOM   348  C CA  . GLU A 1 47  ? -18.852 -16.084 17.667 1.00 50.96 ? 47  GLU B CA  1 
ATOM   349  C C   . GLU A 1 47  ? -17.840 -17.158 17.270 1.00 50.57 ? 47  GLU B C   1 
ATOM   350  O O   . GLU A 1 47  ? -17.888 -18.279 17.793 1.00 47.93 ? 47  GLU B O   1 
ATOM   351  C CB  . GLU A 1 47  ? -20.074 -16.114 16.746 1.00 53.87 ? 47  GLU B CB  1 
ATOM   352  C CG  . GLU A 1 47  ? -19.739 -15.965 15.265 1.00 54.96 ? 47  GLU B CG  1 
ATOM   353  C CD  . GLU A 1 47  ? -20.901 -15.447 14.430 1.00 60.43 ? 47  GLU B CD  1 
ATOM   354  O OE1 . GLU A 1 47  ? -22.062 -15.820 14.708 1.00 64.75 ? 47  GLU B OE1 1 
ATOM   355  O OE2 . GLU A 1 47  ? -20.647 -14.664 13.486 1.00 61.88 ? 47  GLU B OE2 1 
ATOM   356  N N   . ASP A 1 48  ? -16.911 -16.834 16.360 1.00 46.69 ? 48  ASP B N   1 
ATOM   357  C CA  . ASP A 1 48  ? -15.889 -17.801 15.962 1.00 47.38 ? 48  ASP B CA  1 
ATOM   358  C C   . ASP A 1 48  ? -14.898 -18.077 17.088 1.00 43.28 ? 48  ASP B C   1 
ATOM   359  O O   . ASP A 1 48  ? -14.337 -19.178 17.159 1.00 41.47 ? 48  ASP B O   1 
ATOM   360  C CB  . ASP A 1 48  ? -15.128 -17.300 14.730 1.00 42.89 ? 48  ASP B CB  1 
ATOM   361  C CG  . ASP A 1 48  ? -15.957 -17.352 13.462 1.00 46.64 ? 48  ASP B CG  1 
ATOM   362  O OD1 . ASP A 1 48  ? -16.736 -18.317 13.294 1.00 48.44 ? 48  ASP B OD1 1 
ATOM   363  O OD2 . ASP A 1 48  ? -15.831 -16.424 12.635 1.00 44.89 ? 48  ASP B OD2 1 
ATOM   364  N N   . MET A 1 49  ? -14.683 -17.096 17.972 1.00 43.16 ? 49  MET B N   1 
ATOM   365  C CA  . MET A 1 49  ? -13.619 -17.153 18.973 1.00 41.77 ? 49  MET B CA  1 
ATOM   366  C C   . MET A 1 49  ? -13.748 -18.300 19.968 1.00 39.66 ? 49  MET B C   1 
ATOM   367  O O   . MET A 1 49  ? -12.754 -18.635 20.619 1.00 40.84 ? 49  MET B O   1 
ATOM   368  C CB  . MET A 1 49  ? -13.554 -15.824 19.734 1.00 41.16 ? 49  MET B CB  1 
ATOM   369  C CG  . MET A 1 49  ? -12.897 -14.679 18.982 1.00 42.49 ? 49  MET B CG  1 
ATOM   370  S SD  . MET A 1 49  ? -11.497 -15.227 17.963 1.00 52.57 ? 49  MET B SD  1 
ATOM   371  C CE  . MET A 1 49  ? -10.322 -13.936 18.383 1.00 39.14 ? 49  MET B CE  1 
ATOM   372  N N   . LEU A 1 50  ? -14.924 -18.909 20.119 1.00 41.81 ? 50  LEU B N   1 
ATOM   373  C CA  . LEU A 1 50  ? -15.075 -19.919 21.163 1.00 41.11 ? 50  LEU B CA  1 
ATOM   374  C C   . LEU A 1 50  ? -14.246 -21.165 20.860 1.00 40.38 ? 50  LEU B C   1 
ATOM   375  O O   . LEU A 1 50  ? -13.461 -21.622 21.700 1.00 41.66 ? 50  LEU B O   1 
ATOM   376  C CB  . LEU A 1 50  ? -16.553 -20.257 21.351 1.00 45.12 ? 50  LEU B CB  1 
ATOM   377  C CG  . LEU A 1 50  ? -17.249 -19.238 22.261 1.00 47.38 ? 50  LEU B CG  1 
ATOM   378  C CD1 . LEU A 1 50  ? -17.898 -18.109 21.450 1.00 49.83 ? 50  LEU B CD1 1 
ATOM   379  C CD2 . LEU A 1 50  ? -18.284 -19.926 23.145 1.00 51.84 ? 50  LEU B CD2 1 
ATOM   380  N N   . ASN A 1 51  ? -14.402 -21.732 19.666 1.00 38.68 ? 51  ASN B N   1 
ATOM   381  C CA  . ASN A 1 51  ? -13.517 -22.794 19.183 1.00 37.68 ? 51  ASN B CA  1 
ATOM   382  C C   . ASN A 1 51  ? -13.400 -22.647 17.678 1.00 37.58 ? 51  ASN B C   1 
ATOM   383  O O   . ASN A 1 51  ? -14.117 -23.291 16.904 1.00 36.93 ? 51  ASN B O   1 
ATOM   384  C CB  . ASN A 1 51  ? -14.016 -24.187 19.578 1.00 41.28 ? 51  ASN B CB  1 
ATOM   385  C CG  . ASN A 1 51  ? -13.334 -24.719 20.843 1.00 36.10 ? 51  ASN B CG  1 
ATOM   386  O OD1 . ASN A 1 51  ? -12.144 -25.049 20.833 1.00 37.30 ? 51  ASN B OD1 1 
ATOM   387  N ND2 . ASN A 1 51  ? -14.088 -24.799 21.934 1.00 33.23 ? 51  ASN B ND2 1 
ATOM   388  N N   . PRO A 1 52  ? -12.502 -21.780 17.219 1.00 31.63 ? 52  PRO B N   1 
ATOM   389  C CA  . PRO A 1 52  ? -12.434 -21.472 15.788 1.00 30.55 ? 52  PRO B CA  1 
ATOM   390  C C   . PRO A 1 52  ? -11.719 -22.574 15.021 1.00 29.44 ? 52  PRO B C   1 
ATOM   391  O O   . PRO A 1 52  ? -10.636 -23.022 15.412 1.00 31.51 ? 52  PRO B O   1 
ATOM   392  C CB  . PRO A 1 52  ? -11.642 -20.158 15.747 1.00 29.04 ? 52  PRO B CB  1 
ATOM   393  C CG  . PRO A 1 52  ? -10.791 -20.198 16.984 1.00 32.31 ? 52  PRO B CG  1 
ATOM   394  C CD  . PRO A 1 52  ? -11.521 -21.025 18.015 1.00 33.62 ? 52  PRO B CD  1 
ATOM   395  N N   . ASN A 1 53  ? -12.326 -23.000 13.914 1.00 28.87 ? 53  ASN B N   1 
ATOM   396  C CA  . ASN A 1 53  ? -11.688 -23.942 12.993 1.00 33.16 ? 53  ASN B CA  1 
ATOM   397  C C   . ASN A 1 53  ? -11.008 -23.102 11.918 1.00 31.72 ? 53  ASN B C   1 
ATOM   398  O O   . ASN A 1 53  ? -11.585 -22.798 10.870 1.00 28.36 ? 53  ASN B O   1 
ATOM   399  C CB  . ASN A 1 53  ? -12.707 -24.914 12.402 1.00 32.62 ? 53  ASN B CB  1 
ATOM   400  C CG  . ASN A 1 53  ? -12.053 -26.040 11.610 1.00 35.48 ? 53  ASN B CG  1 
ATOM   401  O OD1 . ASN A 1 53  ? -11.111 -25.820 10.849 1.00 32.46 ? 53  ASN B OD1 1 
ATOM   402  N ND2 . ASN A 1 53  ? -12.564 -27.259 11.781 1.00 32.82 ? 53  ASN B ND2 1 
ATOM   403  N N   . TYR A 1 54  ? -9.759  -22.722 12.186 1.00 29.61 ? 54  TYR B N   1 
ATOM   404  C CA  . TYR A 1 54  ? -9.100  -21.719 11.356 1.00 31.89 ? 54  TYR B CA  1 
ATOM   405  C C   . TYR A 1 54  ? -8.957  -22.195 9.913  1.00 33.18 ? 54  TYR B C   1 
ATOM   406  O O   . TYR A 1 54  ? -9.158  -21.415 8.972  1.00 31.49 ? 54  TYR B O   1 
ATOM   407  C CB  . TYR A 1 54  ? -7.744  -21.361 11.971 1.00 28.21 ? 54  TYR B CB  1 
ATOM   408  C CG  . TYR A 1 54  ? -7.853  -20.414 13.162 1.00 29.11 ? 54  TYR B CG  1 
ATOM   409  C CD1 . TYR A 1 54  ? -8.194  -19.079 12.987 1.00 28.97 ? 54  TYR B CD1 1 
ATOM   410  C CD2 . TYR A 1 54  ? -7.655  -20.872 14.464 1.00 28.18 ? 54  TYR B CD2 1 
ATOM   411  C CE1 . TYR A 1 54  ? -8.303  -18.223 14.074 1.00 27.96 ? 54  TYR B CE1 1 
ATOM   412  C CE2 . TYR A 1 54  ? -7.747  -20.013 15.556 1.00 23.62 ? 54  TYR B CE2 1 
ATOM   413  C CZ  . TYR A 1 54  ? -8.074  -18.688 15.348 1.00 25.95 ? 54  TYR B CZ  1 
ATOM   414  O OH  . TYR A 1 54  ? -8.178  -17.828 16.425 1.00 28.59 ? 54  TYR B OH  1 
ATOM   415  N N   . GLU A 1 55  ? -8.649  -23.480 9.715  1.00 32.03 ? 55  GLU B N   1 
ATOM   416  C CA  . GLU A 1 55  ? -8.542  -24.010 8.359  1.00 33.77 ? 55  GLU B CA  1 
ATOM   417  C C   . GLU A 1 55  ? -9.843  -23.798 7.586  1.00 35.00 ? 55  GLU B C   1 
ATOM   418  O O   . GLU A 1 55  ? -9.833  -23.269 6.470  1.00 33.06 ? 55  GLU B O   1 
ATOM   419  C CB  . GLU A 1 55  ? -8.167  -25.496 8.398  1.00 32.98 ? 55  GLU B CB  1 
ATOM   420  C CG  . GLU A 1 55  ? -7.232  -25.896 9.549  1.00 39.73 ? 55  GLU B CG  1 
ATOM   421  C CD  . GLU A 1 55  ? -7.973  -26.222 10.862 1.00 41.93 ? 55  GLU B CD  1 
ATOM   422  O OE1 . GLU A 1 55  ? -8.171  -25.300 11.691 1.00 39.29 ? 55  GLU B OE1 1 
ATOM   423  O OE2 . GLU A 1 55  ? -8.316  -27.417 11.078 1.00 46.22 ? 55  GLU B OE2 1 
ATOM   424  N N   . ASP A 1 56  ? -10.980 -24.190 8.178  1.00 31.97 ? 56  ASP B N   1 
ATOM   425  C CA  . ASP A 1 56  ? -12.267 -24.037 7.497  1.00 35.40 ? 56  ASP B CA  1 
ATOM   426  C C   . ASP A 1 56  ? -12.651 -22.574 7.330  1.00 35.35 ? 56  ASP B C   1 
ATOM   427  O O   . ASP A 1 56  ? -13.203 -22.188 6.292  1.00 36.56 ? 56  ASP B O   1 
ATOM   428  C CB  . ASP A 1 56  ? -13.371 -24.765 8.258  1.00 35.41 ? 56  ASP B CB  1 
ATOM   429  C CG  . ASP A 1 56  ? -13.345 -26.258 8.051  1.00 41.17 ? 56  ASP B CG  1 
ATOM   430  O OD1 . ASP A 1 56  ? -12.485 -26.759 7.294  1.00 40.55 ? 56  ASP B OD1 1 
ATOM   431  O OD2 . ASP A 1 56  ? -14.202 -26.933 8.655  1.00 42.44 ? 56  ASP B OD2 1 
ATOM   432  N N   . LEU A 1 57  ? -12.388 -21.750 8.349  1.00 33.06 ? 57  LEU B N   1 
ATOM   433  C CA  . LEU A 1 57  ? -12.747 -20.337 8.265  1.00 33.23 ? 57  LEU B CA  1 
ATOM   434  C C   . LEU A 1 57  ? -11.995 -19.657 7.131  1.00 31.10 ? 57  LEU B C   1 
ATOM   435  O O   . LEU A 1 57  ? -12.565 -18.835 6.402  1.00 30.70 ? 57  LEU B O   1 
ATOM   436  C CB  . LEU A 1 57  ? -12.449 -19.646 9.594  1.00 30.43 ? 57  LEU B CB  1 
ATOM   437  C CG  . LEU A 1 57  ? -13.399 -19.976 10.743 1.00 33.85 ? 57  LEU B CG  1 
ATOM   438  C CD1 . LEU A 1 57  ? -12.972 -19.230 11.990 1.00 30.05 ? 57  LEU B CD1 1 
ATOM   439  C CD2 . LEU A 1 57  ? -14.860 -19.671 10.375 1.00 36.11 ? 57  LEU B CD2 1 
ATOM   440  N N   . LEU A 1 58  ? -10.720 -20.015 6.953  1.00 31.52 ? 58  LEU B N   1 
ATOM   441  C CA  . LEU A 1 58  ? -9.878  -19.377 5.946  1.00 34.43 ? 58  LEU B CA  1 
ATOM   442  C C   . LEU A 1 58  ? -10.302 -19.770 4.534  1.00 35.25 ? 58  LEU B C   1 
ATOM   443  O O   . LEU A 1 58  ? -10.298 -18.929 3.625  1.00 33.91 ? 58  LEU B O   1 
ATOM   444  C CB  . LEU A 1 58  ? -8.416  -19.749 6.185  1.00 31.06 ? 58  LEU B CB  1 
ATOM   445  C CG  . LEU A 1 58  ? -7.383  -18.890 5.458  1.00 32.74 ? 58  LEU B CG  1 
ATOM   446  C CD1 . LEU A 1 58  ? -7.647  -17.397 5.700  1.00 31.40 ? 58  LEU B CD1 1 
ATOM   447  C CD2 . LEU A 1 58  ? -5.959  -19.278 5.842  1.00 31.22 ? 58  LEU B CD2 1 
ATOM   448  N N   . ILE A 1 59  ? -10.673 -21.043 4.335  1.00 34.36 ? 59  ILE B N   1 
ATOM   449  C CA  . ILE A 1 59  ? -11.144 -21.506 3.027  1.00 34.04 ? 59  ILE B CA  1 
ATOM   450  C C   . ILE A 1 59  ? -12.280 -20.633 2.514  1.00 33.45 ? 59  ILE B C   1 
ATOM   451  O O   . ILE A 1 59  ? -12.345 -20.309 1.323  1.00 37.70 ? 59  ILE B O   1 
ATOM   452  C CB  . ILE A 1 59  ? -11.556 -22.992 3.100  1.00 34.26 ? 59  ILE B CB  1 
ATOM   453  C CG1 . ILE A 1 59  ? -10.319 -23.880 3.291  1.00 37.30 ? 59  ILE B CG1 1 
ATOM   454  C CG2 . ILE A 1 59  ? -12.384 -23.400 1.888  1.00 38.85 ? 59  ILE B CG2 1 
ATOM   455  C CD1 . ILE A 1 59  ? -10.581 -25.165 4.055  1.00 40.69 ? 59  ILE B CD1 1 
ATOM   456  N N   . ARG A 1 60  ? -13.171 -20.211 3.403  1.00 31.97 ? 60  ARG B N   1 
ATOM   457  C CA  . ARG A 1 60  ? -14.297 -19.373 3.010  1.00 35.70 ? 60  ARG B CA  1 
ATOM   458  C C   . ARG A 1 60  ? -13.919 -17.917 2.755  1.00 36.78 ? 60  ARG B C   1 
ATOM   459  O O   . ARG A 1 60  ? -14.787 -17.139 2.343  1.00 35.95 ? 60  ARG B O   1 
ATOM   460  C CB  . ARG A 1 60  ? -15.393 -19.444 4.078  1.00 39.18 ? 60  ARG B CB  1 
ATOM   461  C CG  . ARG A 1 60  ? -16.190 -20.727 4.016  1.00 41.76 ? 60  ARG B CG  1 
ATOM   462  C CD  . ARG A 1 60  ? -17.219 -20.829 5.122  1.00 45.45 ? 60  ARG B CD  1 
ATOM   463  N NE  . ARG A 1 60  ? -16.701 -21.625 6.227  1.00 50.46 ? 60  ARG B NE  1 
ATOM   464  C CZ  . ARG A 1 60  ? -16.819 -22.944 6.320  1.00 51.35 ? 60  ARG B CZ  1 
ATOM   465  N NH1 . ARG A 1 60  ? -17.422 -23.652 5.377  1.00 51.40 ? 60  ARG B NH1 1 
ATOM   466  N NH2 . ARG A 1 60  ? -16.302 -23.570 7.376  1.00 48.37 ? 60  ARG B NH2 1 
ATOM   467  N N   . LYS A 1 61  ? -12.666 -17.525 2.977  1.00 36.58 ? 61  LYS B N   1 
ATOM   468  C CA  . LYS A 1 61  ? -12.266 -16.130 2.845  1.00 36.03 ? 61  LYS B CA  1 
ATOM   469  C C   . LYS A 1 61  ? -11.750 -15.855 1.438  1.00 37.73 ? 61  LYS B C   1 
ATOM   470  O O   . LYS A 1 61  ? -11.014 -16.661 0.861  1.00 36.32 ? 61  LYS B O   1 
ATOM   471  C CB  . LYS A 1 61  ? -11.178 -15.769 3.861  1.00 34.97 ? 61  LYS B CB  1 
ATOM   472  C CG  . LYS A 1 61  ? -11.674 -15.534 5.287  1.00 33.53 ? 61  LYS B CG  1 
ATOM   473  C CD  . LYS A 1 61  ? -12.732 -14.449 5.371  1.00 35.73 ? 61  LYS B CD  1 
ATOM   474  C CE  . LYS A 1 61  ? -13.329 -14.391 6.772  1.00 39.07 ? 61  LYS B CE  1 
ATOM   475  N NZ  . LYS A 1 61  ? -14.569 -13.566 6.835  1.00 44.15 ? 61  LYS B NZ  1 
ATOM   476  N N   . SER A 1 62  ? -12.140 -14.709 0.895  1.00 36.15 ? 62  SER B N   1 
ATOM   477  C CA  . SER A 1 62  ? -11.591 -14.205 -0.355 1.00 37.21 ? 62  SER B CA  1 
ATOM   478  C C   . SER A 1 62  ? -10.394 -13.303 -0.079 1.00 36.78 ? 62  SER B C   1 
ATOM   479  O O   . SER A 1 62  ? -10.336 -12.630 0.954  1.00 36.66 ? 62  SER B O   1 
ATOM   480  C CB  . SER A 1 62  ? -12.659 -13.425 -1.127 1.00 32.91 ? 62  SER B CB  1 
ATOM   481  O OG  . SER A 1 62  ? -12.278 -13.216 -2.475 1.00 40.49 ? 62  SER B OG  1 
ATOM   482  N N   . ASN A 1 63  ? -9.431  -13.299 -1.012 1.00 34.52 ? 63  ASN B N   1 
ATOM   483  C CA  . ASN A 1 63  ? -8.416  -12.250 -1.007 1.00 35.82 ? 63  ASN B CA  1 
ATOM   484  C C   . ASN A 1 63  ? -9.052  -10.877 -0.884 1.00 35.86 ? 63  ASN B C   1 
ATOM   485  O O   . ASN A 1 63  ? -8.489  -9.981  -0.240 1.00 33.19 ? 63  ASN B O   1 
ATOM   486  C CB  . ASN A 1 63  ? -7.567  -12.297 -2.282 1.00 38.03 ? 63  ASN B CB  1 
ATOM   487  C CG  . ASN A 1 63  ? -6.753  -13.570 -2.406 1.00 40.46 ? 63  ASN B CG  1 
ATOM   488  O OD1 . ASN A 1 63  ? -5.840  -13.818 -1.618 1.00 37.34 ? 63  ASN B OD1 1 
ATOM   489  N ND2 . ASN A 1 63  ? -7.074  -14.381 -3.408 1.00 44.56 ? 63  ASN B ND2 1 
ATOM   490  N N   . HIS A 1 64  ? -10.233 -10.699 -1.479 1.00 36.71 ? 64  HIS B N   1 
ATOM   491  C CA  . HIS A 1 64  ? -10.933 -9.423  -1.430 1.00 35.97 ? 64  HIS B CA  1 
ATOM   492  C C   . HIS A 1 64  ? -11.446 -9.084  -0.033 1.00 33.77 ? 64  HIS B C   1 
ATOM   493  O O   . HIS A 1 64  ? -11.676 -7.907  0.253  1.00 37.52 ? 64  HIS B O   1 
ATOM   494  C CB  . HIS A 1 64  ? -12.085 -9.437  -2.440 1.00 37.42 ? 64  HIS B CB  1 
ATOM   495  C CG  . HIS A 1 64  ? -12.675 -8.088  -2.711 1.00 40.25 ? 64  HIS B CG  1 
ATOM   496  N ND1 . HIS A 1 64  ? -13.758 -7.596  -2.016 1.00 38.67 ? 64  HIS B ND1 1 
ATOM   497  C CD2 . HIS A 1 64  ? -12.328 -7.125  -3.599 1.00 46.15 ? 64  HIS B CD2 1 
ATOM   498  C CE1 . HIS A 1 64  ? -14.055 -6.389  -2.463 1.00 44.48 ? 64  HIS B CE1 1 
ATOM   499  N NE2 . HIS A 1 64  ? -13.203 -6.080  -3.424 1.00 48.45 ? 64  HIS B NE2 1 
ATOM   500  N N   . ASN A 1 65  ? -11.632 -10.083 0.837  1.00 34.33 ? 65  ASN B N   1 
ATOM   501  C CA  . ASN A 1 65  ? -12.081 -9.844  2.209  1.00 35.03 ? 65  ASN B CA  1 
ATOM   502  C C   . ASN A 1 65  ? -11.023 -9.155  3.065  1.00 33.62 ? 65  ASN B C   1 
ATOM   503  O O   . ASN A 1 65  ? -11.354 -8.625  4.129  1.00 34.36 ? 65  ASN B O   1 
ATOM   504  C CB  . ASN A 1 65  ? -12.454 -11.168 2.883  1.00 35.95 ? 65  ASN B CB  1 
ATOM   505  C CG  . ASN A 1 65  ? -13.769 -11.741 2.392  1.00 36.89 ? 65  ASN B CG  1 
ATOM   506  O OD1 . ASN A 1 65  ? -13.976 -12.951 2.449  1.00 38.94 ? 65  ASN B OD1 1 
ATOM   507  N ND2 . ASN A 1 65  ? -14.677 -10.880 1.949  1.00 38.50 ? 65  ASN B ND2 1 
ATOM   508  N N   . PHE A 1 66  ? -9.763  -9.184  2.649  1.00 31.11 ? 66  PHE B N   1 
ATOM   509  C CA  . PHE A 1 66  ? -8.653  -8.648  3.431  1.00 31.95 ? 66  PHE B CA  1 
ATOM   510  C C   . PHE A 1 66  ? -8.327  -7.252  2.936  1.00 34.15 ? 66  PHE B C   1 
ATOM   511  O O   . PHE A 1 66  ? -7.751  -7.092  1.853  1.00 32.79 ? 66  PHE B O   1 
ATOM   512  C CB  . PHE A 1 66  ? -7.441  -9.562  3.325  1.00 32.62 ? 66  PHE B CB  1 
ATOM   513  C CG  . PHE A 1 66  ? -7.643  -10.877 3.986  1.00 30.92 ? 66  PHE B CG  1 
ATOM   514  C CD1 . PHE A 1 66  ? -7.670  -10.972 5.367  1.00 32.72 ? 66  PHE B CD1 1 
ATOM   515  C CD2 . PHE A 1 66  ? -7.882  -12.013 3.231  1.00 32.59 ? 66  PHE B CD2 1 
ATOM   516  C CE1 . PHE A 1 66  ? -7.877  -12.194 5.986  1.00 30.98 ? 66  PHE B CE1 1 
ATOM   517  C CE2 . PHE A 1 66  ? -8.097  -13.235 3.843  1.00 35.58 ? 66  PHE B CE2 1 
ATOM   518  C CZ  . PHE A 1 66  ? -8.093  -13.327 5.222  1.00 32.21 ? 66  PHE B CZ  1 
ATOM   519  N N   . LEU A 1 67  ? -8.668  -6.245  3.740  1.00 30.66 ? 67  LEU B N   1 
ATOM   520  C CA  . LEU A 1 67  ? -8.429  -4.855  3.385  1.00 32.41 ? 67  LEU B CA  1 
ATOM   521  C C   . LEU A 1 67  ? -7.182  -4.400  4.151  1.00 32.31 ? 67  LEU B C   1 
ATOM   522  O O   . LEU A 1 67  ? -7.195  -4.322  5.385  1.00 30.55 ? 67  LEU B O   1 
ATOM   523  C CB  . LEU A 1 67  ? -9.666  -4.018  3.703  1.00 33.28 ? 67  LEU B CB  1 
ATOM   524  C CG  . LEU A 1 67  ? -9.756  -2.520  3.402  1.00 36.92 ? 67  LEU B CG  1 
ATOM   525  C CD1 . LEU A 1 67  ? -8.926  -1.667  4.328  1.00 39.15 ? 67  LEU B CD1 1 
ATOM   526  C CD2 . LEU A 1 67  ? -9.392  -2.275  1.932  1.00 40.33 ? 67  LEU B CD2 1 
ATOM   527  N N   . VAL A 1 68  ? -6.111  -4.116  3.417  1.00 30.91 ? 68  VAL B N   1 
ATOM   528  C CA  . VAL A 1 68  ? -4.813  -3.753  3.978  1.00 27.68 ? 68  VAL B CA  1 
ATOM   529  C C   . VAL A 1 68  ? -4.505  -2.321  3.566  1.00 31.57 ? 68  VAL B C   1 
ATOM   530  O O   . VAL A 1 68  ? -4.479  -2.009  2.367  1.00 32.29 ? 68  VAL B O   1 
ATOM   531  C CB  . VAL A 1 68  ? -3.705  -4.711  3.511  1.00 31.38 ? 68  VAL B CB  1 
ATOM   532  C CG1 . VAL A 1 68  ? -2.363  -4.309  4.095  1.00 28.63 ? 68  VAL B CG1 1 
ATOM   533  C CG2 . VAL A 1 68  ? -4.051  -6.139  3.908  1.00 27.44 ? 68  VAL B CG2 1 
ATOM   534  N N   . GLN A 1 69  ? -4.280  -1.453  4.553  1.00 30.59 ? 69  GLN B N   1 
ATOM   535  C CA  . GLN A 1 69  ? -3.928  -0.057  4.307  1.00 30.16 ? 69  GLN B CA  1 
ATOM   536  C C   . GLN A 1 69  ? -2.558  0.257   4.887  1.00 33.36 ? 69  GLN B C   1 
ATOM   537  O O   . GLN A 1 69  ? -2.301  0.001   6.071  1.00 29.83 ? 69  GLN B O   1 
ATOM   538  C CB  . GLN A 1 69  ? -4.926  0.919   4.920  1.00 34.12 ? 69  GLN B CB  1 
ATOM   539  C CG  . GLN A 1 69  ? -5.953  1.475   3.969  1.00 43.52 ? 69  GLN B CG  1 
ATOM   540  C CD  . GLN A 1 69  ? -7.235  1.820   4.692  1.00 47.44 ? 69  GLN B CD  1 
ATOM   541  O OE1 . GLN A 1 69  ? -7.870  0.961   5.300  1.00 48.59 ? 69  GLN B OE1 1 
ATOM   542  N NE2 . GLN A 1 69  ? -7.608  3.095   4.656  1.00 48.90 ? 69  GLN B NE2 1 
ATOM   543  N N   . ALA A 1 70  ? -1.708  0.860   4.068  1.00 34.00 ? 70  ALA B N   1 
ATOM   544  C CA  . ALA A 1 70  ? -0.426  1.403   4.499  1.00 33.01 ? 70  ALA B CA  1 
ATOM   545  C C   . ALA A 1 70  ? -0.549  2.920   4.388  1.00 39.35 ? 70  ALA B C   1 
ATOM   546  O O   . ALA A 1 70  ? -0.436  3.481   3.295  1.00 39.35 ? 70  ALA B O   1 
ATOM   547  C CB  . ALA A 1 70  ? 0.715   0.854   3.649  1.00 32.80 ? 70  ALA B CB  1 
ATOM   548  N N   . GLY A 1 71  ? -0.797  3.580   5.515  1.00 40.92 ? 71  GLY B N   1 
ATOM   549  C CA  . GLY A 1 71  ? -1.170  4.985   5.449  1.00 44.01 ? 71  GLY B CA  1 
ATOM   550  C C   . GLY A 1 71  ? -2.536  5.088   4.803  1.00 44.03 ? 71  GLY B C   1 
ATOM   551  O O   . GLY A 1 71  ? -3.462  4.352   5.155  1.00 42.76 ? 71  GLY B O   1 
ATOM   552  N N   . ASN A 1 72  ? -2.672  5.991   3.831  1.00 48.34 ? 72  ASN B N   1 
ATOM   553  C CA  . ASN A 1 72  ? -3.889  6.101   3.034  1.00 49.92 ? 72  ASN B CA  1 
ATOM   554  C C   . ASN A 1 72  ? -3.760  5.399   1.683  1.00 51.47 ? 72  ASN B C   1 
ATOM   555  O O   . ASN A 1 72  ? -4.503  5.720   0.748  1.00 53.03 ? 72  ASN B O   1 
ATOM   556  C CB  . ASN A 1 72  ? -4.271  7.571   2.839  1.00 49.09 ? 72  ASN B CB  1 
ATOM   557  C CG  . ASN A 1 72  ? -3.068  8.461   2.592  1.00 54.85 ? 72  ASN B CG  1 
ATOM   558  O OD1 . ASN A 1 72  ? -2.235  8.179   1.727  1.00 56.57 ? 72  ASN B OD1 1 
ATOM   559  N ND2 . ASN A 1 72  ? -2.968  9.544   3.355  1.00 55.99 ? 72  ASN B ND2 1 
ATOM   560  N N   . VAL A 1 73  ? -2.831  4.452   1.567  1.00 48.30 ? 73  VAL B N   1 
ATOM   561  C CA  . VAL A 1 73  ? -2.618  3.676   0.351  1.00 46.87 ? 73  VAL B CA  1 
ATOM   562  C C   . VAL A 1 73  ? -3.083  2.247   0.614  1.00 43.99 ? 73  VAL B C   1 
ATOM   563  O O   . VAL A 1 73  ? -2.543  1.560   1.492  1.00 40.07 ? 73  VAL B O   1 
ATOM   564  C CB  . VAL A 1 73  ? -1.144  3.704   -0.085 1.00 43.26 ? 73  VAL B CB  1 
ATOM   565  C CG1 . VAL A 1 73  ? -0.927  2.793   -1.278 1.00 44.68 ? 73  VAL B CG1 1 
ATOM   566  C CG2 . VAL A 1 73  ? -0.718  5.124   -0.406 1.00 48.39 ? 73  VAL B CG2 1 
ATOM   567  N N   . GLN A 1 74  ? -4.083  1.799   -0.139 1.00 42.12 ? 74  GLN B N   1 
ATOM   568  C CA  . GLN A 1 74  ? -4.561  0.430   -0.005 1.00 38.57 ? 74  GLN B CA  1 
ATOM   569  C C   . GLN A 1 74  ? -3.645  -0.525  -0.759 1.00 41.43 ? 74  GLN B C   1 
ATOM   570  O O   . GLN A 1 74  ? -3.221  -0.241  -1.884 1.00 41.31 ? 74  GLN B O   1 
ATOM   571  C CB  . GLN A 1 74  ? -5.991  0.305   -0.525 1.00 40.74 ? 74  GLN B CB  1 
ATOM   572  C CG  . GLN A 1 74  ? -6.666  -0.978  -0.089 1.00 41.35 ? 74  GLN B CG  1 
ATOM   573  C CD  . GLN A 1 74  ? -7.694  -1.469  -1.081 1.00 47.23 ? 74  GLN B CD  1 
ATOM   574  O OE1 . GLN A 1 74  ? -7.551  -2.550  -1.658 1.00 52.44 ? 74  GLN B OE1 1 
ATOM   575  N NE2 . GLN A 1 74  ? -8.750  -0.687  -1.275 1.00 48.89 ? 74  GLN B NE2 1 
ATOM   576  N N   . LEU A 1 75  ? -3.323  -1.654  -0.121 1.00 36.77 ? 75  LEU B N   1 
ATOM   577  C CA  . LEU A 1 75  ? -2.539  -2.715  -0.736 1.00 35.75 ? 75  LEU B CA  1 
ATOM   578  C C   . LEU A 1 75  ? -3.475  -3.815  -1.203 1.00 37.49 ? 75  LEU B C   1 
ATOM   579  O O   . LEU A 1 75  ? -4.373  -4.234  -0.466 1.00 39.02 ? 75  LEU B O   1 
ATOM   580  C CB  . LEU A 1 75  ? -1.515  -3.302  0.236  1.00 33.65 ? 75  LEU B CB  1 
ATOM   581  C CG  . LEU A 1 75  ? -0.485  -2.372  0.875  1.00 37.93 ? 75  LEU B CG  1 
ATOM   582  C CD1 . LEU A 1 75  ? 0.439   -3.177  1.774  1.00 32.51 ? 75  LEU B CD1 1 
ATOM   583  C CD2 . LEU A 1 75  ? 0.313   -1.594  -0.172 1.00 38.27 ? 75  LEU B CD2 1 
ATOM   584  N N   . ARG A 1 76  ? -3.266  -4.285  -2.425 1.00 38.70 ? 76  ARG B N   1 
ATOM   585  C CA  . ARG A 1 76  ? -4.129  -5.308  -2.997 1.00 42.60 ? 76  ARG B CA  1 
ATOM   586  C C   . ARG A 1 76  ? -3.622  -6.674  -2.553 1.00 36.45 ? 76  ARG B C   1 
ATOM   587  O O   . ARG A 1 76  ? -2.458  -7.013  -2.787 1.00 40.17 ? 76  ARG B O   1 
ATOM   588  C CB  . ARG A 1 76  ? -4.163  -5.192  -4.520 1.00 45.71 ? 76  ARG B CB  1 
ATOM   589  C CG  . ARG A 1 76  ? -5.455  -5.700  -5.140 1.00 50.35 ? 76  ARG B CG  1 
ATOM   590  C CD  . ARG A 1 76  ? -5.214  -6.568  -6.364 1.00 51.68 ? 76  ARG B CD  1 
ATOM   591  N NE  . ARG A 1 76  ? -6.462  -7.168  -6.826 1.00 56.66 ? 76  ARG B NE  1 
ATOM   592  C CZ  . ARG A 1 76  ? -6.720  -7.480  -8.089 1.00 60.37 ? 76  ARG B CZ  1 
ATOM   593  N NH1 . ARG A 1 76  ? -5.830  -7.273  -9.047 1.00 61.02 ? 76  ARG B NH1 1 
ATOM   594  N NH2 . ARG A 1 76  ? -7.904  -8.007  -8.400 1.00 55.48 ? 76  ARG B NH2 1 
ATOM   595  N N   . VAL A 1 77  ? -4.481  -7.443  -1.892 1.00 35.95 ? 77  VAL B N   1 
ATOM   596  C CA  . VAL A 1 77  ? -4.120  -8.793  -1.477 1.00 35.19 ? 77  VAL B CA  1 
ATOM   597  C C   . VAL A 1 77  ? -4.340  -9.736  -2.651 1.00 37.25 ? 77  VAL B C   1 
ATOM   598  O O   . VAL A 1 77  ? -5.434  -9.783  -3.227 1.00 39.60 ? 77  VAL B O   1 
ATOM   599  C CB  . VAL A 1 77  ? -4.937  -9.222  -0.247 1.00 31.06 ? 77  VAL B CB  1 
ATOM   600  C CG1 . VAL A 1 77  ? -4.682  -10.690 0.097  1.00 35.18 ? 77  VAL B CG1 1 
ATOM   601  C CG2 . VAL A 1 77  ? -4.607  -8.320  0.934  1.00 31.55 ? 77  VAL B CG2 1 
ATOM   602  N N   . ILE A 1 78  ? -3.296  -10.484 -3.015 1.00 37.81 ? 78  ILE B N   1 
ATOM   603  C CA  . ILE A 1 78  ? -3.316  -11.382 -4.162 1.00 38.67 ? 78  ILE B CA  1 
ATOM   604  C C   . ILE A 1 78  ? -3.106  -12.837 -3.761 1.00 38.75 ? 78  ILE B C   1 
ATOM   605  O O   . ILE A 1 78  ? -2.971  -13.699 -4.626 1.00 39.56 ? 78  ILE B O   1 
ATOM   606  C CB  . ILE A 1 78  ? -2.278  -10.960 -5.222 1.00 37.58 ? 78  ILE B CB  1 
ATOM   607  C CG1 . ILE A 1 78  ? -0.856  -11.191 -4.703 1.00 36.52 ? 78  ILE B CG1 1 
ATOM   608  C CG2 . ILE A 1 78  ? -2.489  -9.520  -5.638 1.00 41.60 ? 78  ILE B CG2 1 
ATOM   609  C CD1 . ILE A 1 78  ? 0.242   -10.803 -5.669 1.00 39.61 ? 78  ILE B CD1 1 
ATOM   610  N N   . GLY A 1 79  ? -3.076  -13.129 -2.466 1.00 35.95 ? 79  GLY B N   1 
ATOM   611  C CA  . GLY A 1 79  ? -2.844  -14.485 -2.005 1.00 36.98 ? 79  GLY B CA  1 
ATOM   612  C C   . GLY A 1 79  ? -2.786  -14.524 -0.496 1.00 35.95 ? 79  GLY B C   1 
ATOM   613  O O   . GLY A 1 79  ? -2.372  -13.543 0.130  1.00 36.84 ? 79  GLY B O   1 
ATOM   614  N N   . HIS A 1 80  ? -3.214  -15.625 0.113  1.00 38.98 ? 80  HIS B N   1 
ATOM   615  C CA  . HIS A 1 80  ? -3.126  -15.729 1.558  1.00 36.73 ? 80  HIS B CA  1 
ATOM   616  C C   . HIS A 1 80  ? -2.767  -17.153 1.942  1.00 35.04 ? 80  HIS B C   1 
ATOM   617  O O   . HIS A 1 80  ? -2.944  -18.100 1.170  1.00 40.10 ? 80  HIS B O   1 
ATOM   618  C CB  . HIS A 1 80  ? -4.421  -15.291 2.253  1.00 35.33 ? 80  HIS B CB  1 
ATOM   619  C CG  . HIS A 1 80  ? -5.642  -16.010 1.778  1.00 37.96 ? 80  HIS B CG  1 
ATOM   620  N ND1 . HIS A 1 80  ? -6.058  -17.204 2.327  1.00 40.47 ? 80  HIS B ND1 1 
ATOM   621  C CD2 . HIS A 1 80  ? -6.537  -15.711 0.806  1.00 40.97 ? 80  HIS B CD2 1 
ATOM   622  C CE1 . HIS A 1 80  ? -7.158  -17.608 1.719  1.00 37.85 ? 80  HIS B CE1 1 
ATOM   623  N NE2 . HIS A 1 80  ? -7.472  -16.719 0.794  1.00 43.15 ? 80  HIS B NE2 1 
ATOM   624  N N   . SER A 1 81  ? -2.252  -17.286 3.157  1.00 30.25 ? 81  SER B N   1 
ATOM   625  C CA  . SER A 1 81  ? -1.742  -18.551 3.646  1.00 31.62 ? 81  SER B CA  1 
ATOM   626  C C   . SER A 1 81  ? -1.649  -18.459 5.163  1.00 33.46 ? 81  SER B C   1 
ATOM   627  O O   . SER A 1 81  ? -1.530  -17.368 5.723  1.00 33.08 ? 81  SER B O   1 
ATOM   628  C CB  . SER A 1 81  ? -0.386  -18.874 3.008  1.00 31.48 ? 81  SER B CB  1 
ATOM   629  O OG  . SER A 1 81  ? 0.407   -19.679 3.851  1.00 40.33 ? 81  SER B OG  1 
ATOM   630  N N   . MET A 1 82  ? -1.733  -19.615 5.810  1.00 30.70 ? 82  MET B N   1 
ATOM   631  C CA  . MET A 1 82  ? -1.715  -19.766 7.263  1.00 28.76 ? 82  MET B CA  1 
ATOM   632  C C   . MET A 1 82  ? -0.450  -20.485 7.698  1.00 28.71 ? 82  MET B C   1 
ATOM   633  O O   . MET A 1 82  ? -0.130  -21.553 7.168  1.00 27.39 ? 82  MET B O   1 
ATOM   634  C CB  . MET A 1 82  ? -2.904  -20.602 7.733  1.00 33.10 ? 82  MET B CB  1 
ATOM   635  C CG  . MET A 1 82  ? -2.999  -20.780 9.232  1.00 32.20 ? 82  MET B CG  1 
ATOM   636  S SD  . MET A 1 82  ? -4.675  -20.563 9.836  1.00 31.56 ? 82  MET B SD  1 
ATOM   637  C CE  . MET A 1 82  ? -5.226  -22.267 9.680  1.00 31.93 ? 82  MET B CE  1 
ATOM   638  N N   . GLN A 1 83  ? 0.238   -19.939 8.693  1.00 28.79 ? 83  GLN B N   1 
ATOM   639  C CA  . GLN A 1 83  ? 1.385   -20.615 9.291  1.00 25.35 ? 83  GLN B CA  1 
ATOM   640  C C   . GLN A 1 83  ? 1.239   -20.586 10.807 1.00 27.94 ? 83  GLN B C   1 
ATOM   641  O O   . GLN A 1 83  ? 1.455   -19.539 11.432 1.00 26.26 ? 83  GLN B O   1 
ATOM   642  C CB  . GLN A 1 83  ? 2.702   -19.969 8.858  1.00 26.22 ? 83  GLN B CB  1 
ATOM   643  C CG  . GLN A 1 83  ? 3.914   -20.655 9.447  1.00 27.95 ? 83  GLN B CG  1 
ATOM   644  C CD  . GLN A 1 83  ? 5.201   -20.029 8.988  1.00 31.48 ? 83  GLN B CD  1 
ATOM   645  O OE1 . GLN A 1 83  ? 5.193   -18.990 8.325  1.00 32.76 ? 83  GLN B OE1 1 
ATOM   646  N NE2 . GLN A 1 83  ? 6.325   -20.649 9.342  1.00 35.05 ? 83  GLN B NE2 1 
ATOM   647  N N   . ASN A 1 84  ? 0.896   -21.739 11.396 1.00 24.90 ? 84  ASN B N   1 
ATOM   648  C CA  . ASN A 1 84  ? 0.602   -21.805 12.823 1.00 24.05 ? 84  ASN B CA  1 
ATOM   649  C C   . ASN A 1 84  ? -0.426  -20.728 13.158 1.00 25.42 ? 84  ASN B C   1 
ATOM   650  O O   . ASN A 1 84  ? -1.488  -20.701 12.535 1.00 25.32 ? 84  ASN B O   1 
ATOM   651  C CB  . ASN A 1 84  ? 1.889   -21.685 13.635 1.00 22.71 ? 84  ASN B CB  1 
ATOM   652  C CG  . ASN A 1 84  ? 2.879   -22.789 13.292 1.00 30.09 ? 84  ASN B CG  1 
ATOM   653  O OD1 . ASN A 1 84  ? 2.570   -23.978 13.427 1.00 28.55 ? 84  ASN B OD1 1 
ATOM   654  N ND2 . ASN A 1 84  ? 4.051   -22.409 12.814 1.00 24.40 ? 84  ASN B ND2 1 
ATOM   655  N N   . CYS A 1 85  ? -0.127  -19.803 14.073 1.00 22.44 ? 85  CYS B N   1 
ATOM   656  C CA  . CYS A 1 85  ? -1.114  -18.792 14.427 1.00 23.40 ? 85  CYS B CA  1 
ATOM   657  C C   . CYS A 1 85  ? -0.947  -17.462 13.695 1.00 24.25 ? 85  CYS B C   1 
ATOM   658  O O   . CYS A 1 85  ? -1.600  -16.490 14.075 1.00 21.61 ? 85  CYS B O   1 
ATOM   659  C CB  . CYS A 1 85  ? -1.117  -18.545 15.938 1.00 23.89 ? 85  CYS B CB  1 
ATOM   660  S SG  . CYS A 1 85  ? -1.448  -20.032 16.891 1.00 27.11 ? 85  CYS B SG  1 
ATOM   661  N N   . VAL A 1 86  ? -0.133  -17.386 12.649 1.00 24.55 ? 86  VAL B N   1 
ATOM   662  C CA  . VAL A 1 86  ? -0.051  -16.151 11.875 1.00 24.89 ? 86  VAL B CA  1 
ATOM   663  C C   . VAL A 1 86  ? -0.621  -16.385 10.487 1.00 26.05 ? 86  VAL B C   1 
ATOM   664  O O   . VAL A 1 86  ? -0.546  -17.484 9.918  1.00 29.37 ? 86  VAL B O   1 
ATOM   665  C CB  . VAL A 1 86  ? 1.373   -15.561 11.776 1.00 27.79 ? 86  VAL B CB  1 
ATOM   666  C CG1 . VAL A 1 86  ? 1.833   -15.035 13.143 1.00 27.76 ? 86  VAL B CG1 1 
ATOM   667  C CG2 . VAL A 1 86  ? 2.344   -16.569 11.215 1.00 29.17 ? 86  VAL B CG2 1 
ATOM   668  N N   . LEU A 1 87  ? -1.223  -15.333 9.961  1.00 22.75 ? 87  LEU B N   1 
ATOM   669  C CA  . LEU A 1 87  ? -1.726  -15.281 8.599  1.00 23.41 ? 87  LEU B CA  1 
ATOM   670  C C   . LEU A 1 87  ? -0.705  -14.526 7.754  1.00 27.23 ? 87  LEU B C   1 
ATOM   671  O O   . LEU A 1 87  ? -0.175  -13.502 8.193  1.00 29.29 ? 87  LEU B O   1 
ATOM   672  C CB  . LEU A 1 87  ? -3.087  -14.589 8.584  1.00 26.32 ? 87  LEU B CB  1 
ATOM   673  C CG  . LEU A 1 87  ? -3.952  -14.540 7.332  1.00 27.91 ? 87  LEU B CG  1 
ATOM   674  C CD1 . LEU A 1 87  ? -4.228  -15.941 6.837  1.00 31.05 ? 87  LEU B CD1 1 
ATOM   675  C CD2 . LEU A 1 87  ? -5.252  -13.860 7.689  1.00 28.53 ? 87  LEU B CD2 1 
ATOM   676  N N   . LYS A 1 88  ? -0.401  -15.045 6.564  1.00 25.79 ? 88  LYS B N   1 
ATOM   677  C CA  . LYS A 1 88  ? 0.502   -14.378 5.628  1.00 26.14 ? 88  LYS B CA  1 
ATOM   678  C C   . LYS A 1 88  ? -0.324  -13.937 4.427  1.00 30.64 ? 88  LYS B C   1 
ATOM   679  O O   . LYS A 1 88  ? -0.897  -14.771 3.713  1.00 32.15 ? 88  LYS B O   1 
ATOM   680  C CB  . LYS A 1 88  ? 1.660   -15.288 5.222  1.00 29.54 ? 88  LYS B CB  1 
ATOM   681  C CG  . LYS A 1 88  ? 2.469   -15.773 6.413  1.00 27.66 ? 88  LYS B CG  1 
ATOM   682  C CD  . LYS A 1 88  ? 3.753   -16.451 5.988  1.00 33.63 ? 88  LYS B CD  1 
ATOM   683  C CE  . LYS A 1 88  ? 3.519   -17.872 5.545  1.00 33.60 ? 88  LYS B CE  1 
ATOM   684  N NZ  . LYS A 1 88  ? 4.827   -18.577 5.441  1.00 35.21 ? 88  LYS B NZ  1 
ATOM   685  N N   . LEU A 1 89  ? -0.425  -12.622 4.243  1.00 25.89 ? 89  LEU B N   1 
ATOM   686  C CA  . LEU A 1 89  ? -1.159  -12.022 3.142  1.00 25.55 ? 89  LEU B CA  1 
ATOM   687  C C   . LEU A 1 89  ? -0.152  -11.587 2.089  1.00 32.13 ? 89  LEU B C   1 
ATOM   688  O O   . LEU A 1 89  ? 0.677   -10.707 2.342  1.00 29.65 ? 89  LEU B O   1 
ATOM   689  C CB  . LEU A 1 89  ? -1.991  -10.838 3.626  1.00 27.18 ? 89  LEU B CB  1 
ATOM   690  C CG  . LEU A 1 89  ? -3.089  -11.147 4.649  1.00 26.68 ? 89  LEU B CG  1 
ATOM   691  C CD1 . LEU A 1 89  ? -3.871  -9.882  5.005  1.00 29.22 ? 89  LEU B CD1 1 
ATOM   692  C CD2 . LEU A 1 89  ? -4.015  -12.180 4.077  1.00 31.00 ? 89  LEU B CD2 1 
ATOM   693  N N   . LYS A 1 90  ? -0.207  -12.212 0.920  1.00 29.13 ? 90  LYS B N   1 
ATOM   694  C CA  . LYS A 1 90  ? 0.636   -11.777 -0.179 1.00 33.19 ? 90  LYS B CA  1 
ATOM   695  C C   . LYS A 1 90  ? -0.020  -10.562 -0.820 1.00 32.81 ? 90  LYS B C   1 
ATOM   696  O O   . LYS A 1 90  ? -1.227  -10.566 -1.087 1.00 33.13 ? 90  LYS B O   1 
ATOM   697  C CB  . LYS A 1 90  ? 0.819   -12.900 -1.194 1.00 36.25 ? 90  LYS B CB  1 
ATOM   698  C CG  . LYS A 1 90  ? 1.476   -12.453 -2.479 1.00 39.81 ? 90  LYS B CG  1 
ATOM   699  C CD  . LYS A 1 90  ? 2.982   -12.511 -2.335 1.00 39.14 ? 90  LYS B CD  1 
ATOM   700  C CE  . LYS A 1 90  ? 3.491   -13.921 -2.568 1.00 38.88 ? 90  LYS B CE  1 
ATOM   701  N NZ  . LYS A 1 90  ? 2.820   -14.563 -3.734 1.00 47.87 ? 90  LYS B NZ  1 
ATOM   702  N N   . VAL A 1 91  ? 0.760   -9.505  -1.031 1.00 31.30 ? 91  VAL B N   1 
ATOM   703  C CA  . VAL A 1 91  ? 0.210   -8.271  -1.570 1.00 33.39 ? 91  VAL B CA  1 
ATOM   704  C C   . VAL A 1 91  ? 0.891   -7.945  -2.893 1.00 32.59 ? 91  VAL B C   1 
ATOM   705  O O   . VAL A 1 91  ? 1.954   -8.473  -3.229 1.00 33.93 ? 91  VAL B O   1 
ATOM   706  C CB  . VAL A 1 91  ? 0.332   -7.091  -0.586 1.00 34.53 ? 91  VAL B CB  1 
ATOM   707  C CG1 . VAL A 1 91  ? -0.767  -7.176  0.464  1.00 32.15 ? 91  VAL B CG1 1 
ATOM   708  C CG2 . VAL A 1 91  ? 1.703   -7.075  0.058  1.00 33.04 ? 91  VAL B CG2 1 
ATOM   709  N N   . ASP A 1 92  ? 0.244   -7.054  -3.648 1.00 38.37 ? 92  ASP B N   1 
ATOM   710  C CA  . ASP A 1 92  ? 0.719   -6.672  -4.972 1.00 42.74 ? 92  ASP B CA  1 
ATOM   711  C C   . ASP A 1 92  ? 1.996   -5.850  -4.927 1.00 43.08 ? 92  ASP B C   1 
ATOM   712  O O   . ASP A 1 92  ? 2.721   -5.801  -5.929 1.00 47.46 ? 92  ASP B O   1 
ATOM   713  C CB  . ASP A 1 92  ? -0.370  -5.885  -5.703 1.00 43.76 ? 92  ASP B CB  1 
ATOM   714  C CG  . ASP A 1 92  ? -0.619  -6.404  -7.106 1.00 54.09 ? 92  ASP B CG  1 
ATOM   715  O OD1 . ASP A 1 92  ? -0.065  -7.477  -7.449 1.00 53.32 ? 92  ASP B OD1 1 
ATOM   716  O OD2 . ASP A 1 92  ? -1.387  -5.752  -7.854 1.00 57.33 ? 92  ASP B OD2 1 
ATOM   717  N N   . THR A 1 93  ? 2.294   -5.215  -3.799 1.00 41.15 ? 93  THR B N   1 
ATOM   718  C CA  . THR A 1 93  ? 3.366   -4.236  -3.716 1.00 39.31 ? 93  THR B CA  1 
ATOM   719  C C   . THR A 1 93  ? 4.345   -4.654  -2.629 1.00 38.38 ? 93  THR B C   1 
ATOM   720  O O   . THR A 1 93  ? 3.941   -4.928  -1.494 1.00 37.30 ? 93  THR B O   1 
ATOM   721  C CB  . THR A 1 93  ? 2.804   -2.843  -3.425 1.00 40.01 ? 93  THR B CB  1 
ATOM   722  O OG1 . THR A 1 93  ? 2.183   -2.325  -4.607 1.00 43.25 ? 93  THR B OG1 1 
ATOM   723  C CG2 . THR A 1 93  ? 3.922   -1.893  -3.012 1.00 40.73 ? 93  THR B CG2 1 
ATOM   724  N N   . ALA A 1 94  ? 5.625   -4.719  -2.975 1.00 37.62 ? 94  ALA B N   1 
ATOM   725  C CA  . ALA A 1 94  ? 6.640   -5.010  -1.976 1.00 33.96 ? 94  ALA B CA  1 
ATOM   726  C C   . ALA A 1 94  ? 6.968   -3.745  -1.198 1.00 35.54 ? 94  ALA B C   1 
ATOM   727  O O   . ALA A 1 94  ? 7.081   -2.657  -1.773 1.00 34.24 ? 94  ALA B O   1 
ATOM   728  C CB  . ALA A 1 94  ? 7.902   -5.571  -2.623 1.00 33.64 ? 94  ALA B CB  1 
ATOM   729  N N   . ASN A 1 95  ? 7.111   -3.892  0.121  1.00 33.65 ? 95  ASN B N   1 
ATOM   730  C CA  . ASN A 1 95  ? 7.413   -2.752  0.980  1.00 32.34 ? 95  ASN B CA  1 
ATOM   731  C C   . ASN A 1 95  ? 8.759   -2.136  0.615  1.00 31.34 ? 95  ASN B C   1 
ATOM   732  O O   . ASN A 1 95  ? 9.804   -2.762  0.826  1.00 29.89 ? 95  ASN B O   1 
ATOM   733  C CB  . ASN A 1 95  ? 7.403   -3.171  2.453  1.00 33.33 ? 95  ASN B CB  1 
ATOM   734  C CG  . ASN A 1 95  ? 7.361   -1.980  3.393  1.00 35.19 ? 95  ASN B CG  1 
ATOM   735  O OD1 . ASN A 1 95  ? 7.514   -0.832  2.963  1.00 35.43 ? 95  ASN B OD1 1 
ATOM   736  N ND2 . ASN A 1 95  ? 7.134   -2.243  4.680  1.00 32.78 ? 95  ASN B ND2 1 
ATOM   737  N N   . PRO A 1 96  ? 8.773   -0.907  0.084  1.00 28.53 ? 96  PRO B N   1 
ATOM   738  C CA  . PRO A 1 96  ? 10.055  -0.260  -0.237 1.00 33.37 ? 96  PRO B CA  1 
ATOM   739  C C   . PRO A 1 96  ? 10.904  0.025   0.985  1.00 33.96 ? 96  PRO B C   1 
ATOM   740  O O   . PRO A 1 96  ? 12.124  0.176   0.848  1.00 32.63 ? 96  PRO B O   1 
ATOM   741  C CB  . PRO A 1 96  ? 9.623   1.041   -0.930 1.00 31.58 ? 96  PRO B CB  1 
ATOM   742  C CG  . PRO A 1 96  ? 8.288   1.340   -0.327 1.00 34.45 ? 96  PRO B CG  1 
ATOM   743  C CD  . PRO A 1 96  ? 7.631   -0.017  -0.182 1.00 29.06 ? 96  PRO B CD  1 
ATOM   744  N N   . LYS A 1 97  ? 10.300  0.107   2.173  1.00 32.32 ? 97  LYS B N   1 
ATOM   745  C CA  . LYS A 1 97  ? 11.028  0.367   3.407  1.00 33.03 ? 97  LYS B CA  1 
ATOM   746  C C   . LYS A 1 97  ? 11.319  -0.907  4.198  1.00 32.69 ? 97  LYS B C   1 
ATOM   747  O O   . LYS A 1 97  ? 11.497  -0.838  5.418  1.00 33.31 ? 97  LYS B O   1 
ATOM   748  C CB  . LYS A 1 97  ? 10.264  1.358   4.292  1.00 34.00 ? 97  LYS B CB  1 
ATOM   749  C CG  . LYS A 1 97  ? 10.237  2.800   3.811  1.00 39.27 ? 97  LYS B CG  1 
ATOM   750  C CD  . LYS A 1 97  ? 8.884   3.442   4.102  1.00 34.72 ? 97  LYS B CD  1 
ATOM   751  C CE  . LYS A 1 97  ? 8.447   4.389   2.989  1.00 42.71 ? 97  LYS B CE  1 
ATOM   752  N NZ  . LYS A 1 97  ? 7.114   4.015   2.407  1.00 46.10 ? 97  LYS B NZ  1 
ATOM   753  N N   . THR A 1 98  ? 11.399  -2.055  3.534  1.00 32.18 ? 98  THR B N   1 
ATOM   754  C CA  . THR A 1 98  ? 11.739  -3.285  4.230  1.00 31.47 ? 98  THR B CA  1 
ATOM   755  C C   . THR A 1 98  ? 13.174  -3.210  4.732  1.00 33.09 ? 98  THR B C   1 
ATOM   756  O O   . THR A 1 98  ? 14.101  -3.089  3.918  1.00 30.27 ? 98  THR B O   1 
ATOM   757  C CB  . THR A 1 98  ? 11.562  -4.499  3.318  1.00 31.05 ? 98  THR B CB  1 
ATOM   758  O OG1 . THR A 1 98  ? 10.234  -4.503  2.789  1.00 32.68 ? 98  THR B OG1 1 
ATOM   759  C CG2 . THR A 1 98  ? 11.777  -5.785  4.090  1.00 30.67 ? 98  THR B CG2 1 
ATOM   760  N N   . PRO A 1 99  ? 13.408  -3.283  6.038  1.00 31.03 ? 99  PRO B N   1 
ATOM   761  C CA  . PRO A 1 99  ? 14.777  -3.325  6.552  1.00 32.59 ? 99  PRO B CA  1 
ATOM   762  C C   . PRO A 1 99  ? 15.349  -4.725  6.402  1.00 33.29 ? 99  PRO B C   1 
ATOM   763  O O   . PRO A 1 99  ? 14.629  -5.701  6.174  1.00 33.56 ? 99  PRO B O   1 
ATOM   764  C CB  . PRO A 1 99  ? 14.600  -2.971  8.029  1.00 33.28 ? 99  PRO B CB  1 
ATOM   765  C CG  . PRO A 1 99  ? 13.264  -3.610  8.367  1.00 29.93 ? 99  PRO B CG  1 
ATOM   766  C CD  . PRO A 1 99  ? 12.414  -3.489  7.112  1.00 31.15 ? 99  PRO B CD  1 
ATOM   767  N N   . LYS A 1 100 ? 16.670  -4.814  6.541  1.00 33.08 ? 100 LYS B N   1 
ATOM   768  C CA  . LYS A 1 100 ? 17.277  -6.116  6.772  1.00 32.96 ? 100 LYS B CA  1 
ATOM   769  C C   . LYS A 1 100 ? 16.716  -6.704  8.058  1.00 30.83 ? 100 LYS B C   1 
ATOM   770  O O   . LYS A 1 100 ? 16.734  -6.055  9.110  1.00 30.73 ? 100 LYS B O   1 
ATOM   771  C CB  . LYS A 1 100 ? 18.797  -6.010  6.860  1.00 34.38 ? 100 LYS B CB  1 
ATOM   772  C CG  . LYS A 1 100 ? 19.425  -4.998  5.921  1.00 40.33 ? 100 LYS B CG  1 
ATOM   773  C CD  . LYS A 1 100 ? 20.863  -4.745  6.325  1.00 46.72 ? 100 LYS B CD  1 
ATOM   774  C CE  . LYS A 1 100 ? 21.823  -4.711  5.137  1.00 49.71 ? 100 LYS B CE  1 
ATOM   775  N NZ  . LYS A 1 100 ? 23.188  -5.243  5.495  1.00 48.90 ? 100 LYS B NZ  1 
ATOM   776  N N   . TYR A 1 101 ? 16.211  -7.932  7.979  1.00 30.19 ? 101 TYR B N   1 
ATOM   777  C CA  . TYR A 1 101 ? 15.481  -8.483  9.108  1.00 30.13 ? 101 TYR B CA  1 
ATOM   778  C C   . TYR A 1 101 ? 15.722  -9.978  9.222  1.00 30.14 ? 101 TYR B C   1 
ATOM   779  O O   . TYR A 1 101 ? 16.142  -10.637 8.267  1.00 29.32 ? 101 TYR B O   1 
ATOM   780  C CB  . TYR A 1 101 ? 13.980  -8.190  8.992  1.00 27.41 ? 101 TYR B CB  1 
ATOM   781  C CG  . TYR A 1 101 ? 13.269  -8.999  7.937  1.00 26.06 ? 101 TYR B CG  1 
ATOM   782  C CD1 . TYR A 1 101 ? 13.170  -8.530  6.635  1.00 28.97 ? 101 TYR B CD1 1 
ATOM   783  C CD2 . TYR A 1 101 ? 12.682  -10.228 8.240  1.00 25.93 ? 101 TYR B CD2 1 
ATOM   784  C CE1 . TYR A 1 101 ? 12.512  -9.250  5.662  1.00 30.44 ? 101 TYR B CE1 1 
ATOM   785  C CE2 . TYR A 1 101 ? 12.024  -10.960 7.266  1.00 29.05 ? 101 TYR B CE2 1 
ATOM   786  C CZ  . TYR A 1 101 ? 11.945  -10.460 5.979  1.00 28.82 ? 101 TYR B CZ  1 
ATOM   787  O OH  . TYR A 1 101 ? 11.293  -11.179 4.999  1.00 37.72 ? 101 TYR B OH  1 
ATOM   788  N N   . LYS A 1 102 ? 15.462  -10.496 10.424 1.00 26.01 ? 102 LYS B N   1 
ATOM   789  C CA  . LYS A 1 102 ? 15.420  -11.920 10.713 1.00 29.98 ? 102 LYS B CA  1 
ATOM   790  C C   . LYS A 1 102 ? 14.200  -12.182 11.583 1.00 27.92 ? 102 LYS B C   1 
ATOM   791  O O   . LYS A 1 102 ? 13.696  -11.278 12.252 1.00 25.17 ? 102 LYS B O   1 
ATOM   792  C CB  . LYS A 1 102 ? 16.666  -12.414 11.469 1.00 30.43 ? 102 LYS B CB  1 
ATOM   793  C CG  . LYS A 1 102 ? 17.998  -11.897 10.976 1.00 40.46 ? 102 LYS B CG  1 
ATOM   794  C CD  . LYS A 1 102 ? 19.128  -12.778 11.493 1.00 39.85 ? 102 LYS B CD  1 
ATOM   795  C CE  . LYS A 1 102 ? 19.174  -12.742 13.018 1.00 42.24 ? 102 LYS B CE  1 
ATOM   796  N NZ  . LYS A 1 102 ? 20.002  -11.606 13.523 1.00 45.19 ? 102 LYS B NZ  1 
ATOM   797  N N   . PHE A 1 103 ? 13.731  -13.430 11.566 1.00 27.50 ? 103 PHE B N   1 
ATOM   798  C CA  . PHE A 1 103 ? 12.746  -13.920 12.527 1.00 24.99 ? 103 PHE B CA  1 
ATOM   799  C C   . PHE A 1 103 ? 13.479  -14.784 13.548 1.00 24.16 ? 103 PHE B C   1 
ATOM   800  O O   . PHE A 1 103 ? 14.106  -15.788 13.182 1.00 28.24 ? 103 PHE B O   1 
ATOM   801  C CB  . PHE A 1 103 ? 11.647  -14.737 11.838 1.00 22.40 ? 103 PHE B CB  1 
ATOM   802  C CG  . PHE A 1 103 ? 10.682  -13.923 11.019 1.00 21.59 ? 103 PHE B CG  1 
ATOM   803  C CD1 . PHE A 1 103 ? 10.675  -12.542 11.074 1.00 22.88 ? 103 PHE B CD1 1 
ATOM   804  C CD2 . PHE A 1 103 ? 9.777   -14.557 10.177 1.00 22.97 ? 103 PHE B CD2 1 
ATOM   805  C CE1 . PHE A 1 103 ? 9.773   -11.800 10.305 1.00 25.25 ? 103 PHE B CE1 1 
ATOM   806  C CE2 . PHE A 1 103 ? 8.870   -13.830 9.417  1.00 25.91 ? 103 PHE B CE2 1 
ATOM   807  C CZ  . PHE A 1 103 ? 8.878   -12.444 9.474  1.00 27.57 ? 103 PHE B CZ  1 
ATOM   808  N N   . VAL A 1 104 ? 13.418  -14.402 14.824 1.00 24.44 ? 104 VAL B N   1 
ATOM   809  C CA  . VAL A 1 104 ? 14.095  -15.164 15.865 1.00 22.29 ? 104 VAL B CA  1 
ATOM   810  C C   . VAL A 1 104 ? 13.102  -15.487 16.972 1.00 24.30 ? 104 VAL B C   1 
ATOM   811  O O   . VAL A 1 104 ? 12.115  -14.775 17.185 1.00 29.29 ? 104 VAL B O   1 
ATOM   812  C CB  . VAL A 1 104 ? 15.331  -14.428 16.441 1.00 27.75 ? 104 VAL B CB  1 
ATOM   813  C CG1 . VAL A 1 104 ? 16.265  -13.980 15.322 1.00 30.64 ? 104 VAL B CG1 1 
ATOM   814  C CG2 . VAL A 1 104 ? 14.916  -13.254 17.304 1.00 28.66 ? 104 VAL B CG2 1 
ATOM   815  N N   . ARG A 1 105 ? 13.356  -16.585 17.664 1.00 23.16 ? 105 ARG B N   1 
ATOM   816  C CA  . ARG A 1 105 ? 12.563  -16.977 18.820 1.00 24.96 ? 105 ARG B CA  1 
ATOM   817  C C   . ARG A 1 105 ? 13.412  -16.684 20.045 1.00 28.28 ? 105 ARG B C   1 
ATOM   818  O O   . ARG A 1 105 ? 14.420  -17.355 20.283 1.00 28.39 ? 105 ARG B O   1 
ATOM   819  C CB  . ARG A 1 105 ? 12.152  -18.445 18.751 1.00 25.41 ? 105 ARG B CB  1 
ATOM   820  C CG  . ARG A 1 105 ? 11.047  -18.771 19.731 1.00 24.73 ? 105 ARG B CG  1 
ATOM   821  C CD  . ARG A 1 105 ? 10.506  -20.164 19.580 1.00 28.71 ? 105 ARG B CD  1 
ATOM   822  N NE  . ARG A 1 105 ? 9.684   -20.550 20.723 1.00 26.10 ? 105 ARG B NE  1 
ATOM   823  C CZ  . ARG A 1 105 ? 8.388   -20.291 20.843 1.00 26.63 ? 105 ARG B CZ  1 
ATOM   824  N NH1 . ARG A 1 105 ? 7.735   -19.583 19.934 1.00 27.89 ? 105 ARG B NH1 1 
ATOM   825  N NH2 . ARG A 1 105 ? 7.728   -20.770 21.893 1.00 25.45 ? 105 ARG B NH2 1 
ATOM   826  N N   . ILE A 1 106 ? 13.031  -15.654 20.805 1.00 23.68 ? 106 ILE B N   1 
ATOM   827  C CA  . ILE A 1 106 ? 13.822  -15.282 21.971 1.00 26.71 ? 106 ILE B CA  1 
ATOM   828  C C   . ILE A 1 106 ? 13.603  -16.264 23.113 1.00 28.02 ? 106 ILE B C   1 
ATOM   829  O O   . ILE A 1 106 ? 12.593  -16.961 23.198 1.00 25.60 ? 106 ILE B O   1 
ATOM   830  C CB  . ILE A 1 106 ? 13.540  -13.832 22.402 1.00 27.16 ? 106 ILE B CB  1 
ATOM   831  C CG1 . ILE A 1 106 ? 12.038  -13.623 22.568 1.00 27.30 ? 106 ILE B CG1 1 
ATOM   832  C CG2 . ILE A 1 106 ? 14.261  -12.826 21.496 1.00 34.23 ? 106 ILE B CG2 1 
ATOM   833  C CD1 . ILE A 1 106 ? 11.508  -14.019 23.857 1.00 27.58 ? 106 ILE B CD1 1 
ATOM   834  N N   . GLN A 1 107 ? 14.571  -16.298 24.006 1.00 30.20 ? 107 GLN B N   1 
ATOM   835  C CA  . GLN A 1 107 ? 14.655  -17.142 25.184 1.00 29.31 ? 107 GLN B CA  1 
ATOM   836  C C   . GLN A 1 107 ? 14.141  -16.403 26.409 1.00 27.86 ? 107 GLN B C   1 
ATOM   837  O O   . GLN A 1 107 ? 14.309  -15.176 26.514 1.00 26.39 ? 107 GLN B O   1 
ATOM   838  C CB  . GLN A 1 107 ? 16.101  -17.586 25.423 1.00 31.64 ? 107 GLN B CB  1 
ATOM   839  C CG  . GLN A 1 107 ? 16.616  -18.494 24.334 1.00 37.55 ? 107 GLN B CG  1 
ATOM   840  C CD  . GLN A 1 107 ? 15.977  -19.858 24.426 1.00 38.28 ? 107 GLN B CD  1 
ATOM   841  O OE1 . GLN A 1 107 ? 15.397  -20.362 23.459 1.00 44.12 ? 107 GLN B OE1 1 
ATOM   842  N NE2 . GLN A 1 107 ? 16.069  -20.466 25.603 1.00 42.29 ? 107 GLN B NE2 1 
ATOM   843  N N   . PRO A 1 108 ? 13.495  -17.122 27.325 1.00 27.78 ? 108 PRO B N   1 
ATOM   844  C CA  . PRO A 1 108 ? 13.047  -16.486 28.563 1.00 23.64 ? 108 PRO B CA  1 
ATOM   845  C C   . PRO A 1 108 ? 14.223  -15.851 29.290 1.00 27.20 ? 108 PRO B C   1 
ATOM   846  O O   . PRO A 1 108 ? 15.343  -16.375 29.295 1.00 28.80 ? 108 PRO B O   1 
ATOM   847  C CB  . PRO A 1 108 ? 12.417  -17.644 29.353 1.00 27.43 ? 108 PRO B CB  1 
ATOM   848  C CG  . PRO A 1 108 ? 13.019  -18.878 28.748 1.00 33.96 ? 108 PRO B CG  1 
ATOM   849  C CD  . PRO A 1 108 ? 13.146  -18.552 27.295 1.00 30.07 ? 108 PRO B CD  1 
ATOM   850  N N   . GLY A 1 109 ? 13.966  -14.674 29.847 1.00 22.95 ? 109 GLY B N   1 
ATOM   851  C CA  . GLY A 1 109 ? 14.976  -13.864 30.458 1.00 23.12 ? 109 GLY B CA  1 
ATOM   852  C C   . GLY A 1 109 ? 15.540  -12.788 29.560 1.00 22.96 ? 109 GLY B C   1 
ATOM   853  O O   . GLY A 1 109 ? 16.134  -11.838 30.070 1.00 27.63 ? 109 GLY B O   1 
ATOM   854  N N   . GLN A 1 110 ? 15.358  -12.896 28.246 1.00 19.90 ? 110 GLN B N   1 
ATOM   855  C CA  . GLN A 1 110 ? 15.860  -11.910 27.294 1.00 22.42 ? 110 GLN B CA  1 
ATOM   856  C C   . GLN A 1 110 ? 14.833  -10.798 27.062 1.00 22.11 ? 110 GLN B C   1 
ATOM   857  O O   . GLN A 1 110 ? 13.642  -10.954 27.329 1.00 19.13 ? 110 GLN B O   1 
ATOM   858  C CB  . GLN A 1 110 ? 16.217  -12.590 25.967 1.00 22.31 ? 110 GLN B CB  1 
ATOM   859  C CG  . GLN A 1 110 ? 17.294  -13.650 26.130 1.00 27.02 ? 110 GLN B CG  1 
ATOM   860  C CD  . GLN A 1 110 ? 18.575  -13.049 26.679 1.00 29.21 ? 110 GLN B CD  1 
ATOM   861  O OE1 . GLN A 1 110 ? 19.224  -12.237 26.019 1.00 35.55 ? 110 GLN B OE1 1 
ATOM   862  N NE2 . GLN A 1 110 ? 18.941  -13.437 27.898 1.00 31.08 ? 110 GLN B NE2 1 
ATOM   863  N N   . THR A 1 111 ? 15.309  -9.660  26.561 1.00 17.94 ? 111 THR B N   1 
ATOM   864  C CA  . THR A 1 111 ? 14.469  -8.485  26.387 1.00 18.86 ? 111 THR B CA  1 
ATOM   865  C C   . THR A 1 111 ? 14.297  -8.138  24.914 1.00 21.92 ? 111 THR B C   1 
ATOM   866  O O   . THR A 1 111 ? 15.040  -8.603  24.037 1.00 20.57 ? 111 THR B O   1 
ATOM   867  C CB  . THR A 1 111 ? 15.064  -7.282  27.122 1.00 20.72 ? 111 THR B CB  1 
ATOM   868  O OG1 . THR A 1 111 ? 16.433  -7.119  26.706 1.00 22.47 ? 111 THR B OG1 1 
ATOM   869  C CG2 . THR A 1 111 ? 15.009  -7.514  28.618 1.00 19.65 ? 111 THR B CG2 1 
ATOM   870  N N   . PHE A 1 112 ? 13.313  -7.279  24.665 1.00 18.68 ? 112 PHE B N   1 
ATOM   871  C CA  . PHE A 1 112 ? 13.031  -6.754  23.337 1.00 19.23 ? 112 PHE B CA  1 
ATOM   872  C C   . PHE A 1 112 ? 12.165  -5.507  23.470 1.00 17.18 ? 112 PHE B C   1 
ATOM   873  O O   . PHE A 1 112 ? 11.587  -5.233  24.524 1.00 18.48 ? 112 PHE B O   1 
ATOM   874  C CB  . PHE A 1 112 ? 12.343  -7.791  22.437 1.00 18.58 ? 112 PHE B CB  1 
ATOM   875  C CG  . PHE A 1 112 ? 11.048  -8.363  23.001 1.00 19.05 ? 112 PHE B CG  1 
ATOM   876  C CD1 . PHE A 1 112 ? 11.064  -9.463  23.840 1.00 20.07 ? 112 PHE B CD1 1 
ATOM   877  C CD2 . PHE A 1 112 ? 9.824   -7.804  22.661 1.00 19.23 ? 112 PHE B CD2 1 
ATOM   878  C CE1 . PHE A 1 112 ? 9.865   -9.998  24.348 1.00 22.02 ? 112 PHE B CE1 1 
ATOM   879  C CE2 . PHE A 1 112 ? 8.617   -8.336  23.156 1.00 18.35 ? 112 PHE B CE2 1 
ATOM   880  C CZ  . PHE A 1 112 ? 8.645   -9.431  24.000 1.00 18.53 ? 112 PHE B CZ  1 
ATOM   881  N N   . SER A 1 113 ? 12.116  -4.734  22.398 1.00 17.08 ? 113 SER B N   1 
ATOM   882  C CA  . SER A 1 113 ? 11.300  -3.528  22.357 1.00 19.77 ? 113 SER B CA  1 
ATOM   883  C C   . SER A 1 113 ? 9.963   -3.849  21.720 1.00 18.50 ? 113 SER B C   1 
ATOM   884  O O   . SER A 1 113 ? 9.905   -4.561  20.716 1.00 19.40 ? 113 SER B O   1 
ATOM   885  C CB  . SER A 1 113 ? 11.996  -2.413  21.574 1.00 20.19 ? 113 SER B CB  1 
ATOM   886  O OG  . SER A 1 113 ? 13.219  -2.088  22.181 1.00 19.64 ? 113 SER B OG  1 
ATOM   887  N N   . VAL A 1 114 ? 8.892   -3.339  22.316 1.00 18.27 ? 114 VAL B N   1 
ATOM   888  C CA  . VAL A 1 114 ? 7.557   -3.435  21.747 1.00 19.44 ? 114 VAL B CA  1 
ATOM   889  C C   . VAL A 1 114 ? 7.205   -2.095  21.110 1.00 18.17 ? 114 VAL B C   1 
ATOM   890  O O   . VAL A 1 114 ? 7.347   -1.038  21.741 1.00 20.57 ? 114 VAL B O   1 
ATOM   891  C CB  . VAL A 1 114 ? 6.533   -3.838  22.824 1.00 17.17 ? 114 VAL B CB  1 
ATOM   892  C CG1 . VAL A 1 114 ? 5.098   -3.708  22.308 1.00 21.64 ? 114 VAL B CG1 1 
ATOM   893  C CG2 . VAL A 1 114 ? 6.807   -5.250  23.298 1.00 22.76 ? 114 VAL B CG2 1 
ATOM   894  N N   . LEU A 1 115 ? 6.762   -2.133  19.850 1.00 17.21 ? 115 LEU B N   1 
ATOM   895  C CA  . LEU A 1 115 ? 6.135   -0.986  19.191 1.00 21.07 ? 115 LEU B CA  1 
ATOM   896  C C   . LEU A 1 115 ? 4.623   -1.190  19.223 1.00 18.35 ? 115 LEU B C   1 
ATOM   897  O O   . LEU A 1 115 ? 4.063   -1.882  18.371 1.00 19.06 ? 115 LEU B O   1 
ATOM   898  C CB  . LEU A 1 115 ? 6.631   -0.822  17.757 1.00 21.16 ? 115 LEU B CB  1 
ATOM   899  C CG  . LEU A 1 115 ? 6.015   0.387   17.037 1.00 22.63 ? 115 LEU B CG  1 
ATOM   900  C CD1 . LEU A 1 115 ? 6.430   1.706   17.695 1.00 25.88 ? 115 LEU B CD1 1 
ATOM   901  C CD2 . LEU A 1 115 ? 6.337   0.371   15.549 1.00 24.31 ? 115 LEU B CD2 1 
ATOM   902  N N   . ALA A 1 116 ? 3.965   -0.584  20.206 1.00 19.26 ? 116 ALA B N   1 
ATOM   903  C CA  . ALA A 1 116 ? 2.510   -0.655  20.300 1.00 18.82 ? 116 ALA B CA  1 
ATOM   904  C C   . ALA A 1 116 ? 1.843   0.149   19.187 1.00 24.76 ? 116 ALA B C   1 
ATOM   905  O O   . ALA A 1 116 ? 2.103   1.347   19.028 1.00 25.87 ? 116 ALA B O   1 
ATOM   906  C CB  . ALA A 1 116 ? 2.055   -0.150  21.668 1.00 23.32 ? 116 ALA B CB  1 
ATOM   907  N N   . CYS A 1 117 ? 0.962   -0.504  18.425 1.00 21.77 ? 117 CYS B N   1 
ATOM   908  C CA  . CYS A 1 117 ? 0.264   0.121   17.309 1.00 23.90 ? 117 CYS B CA  1 
ATOM   909  C C   . CYS A 1 117 ? -1.236  -0.096  17.403 1.00 22.60 ? 117 CYS B C   1 
ATOM   910  O O   . CYS A 1 117 ? -1.707  -1.099  17.947 1.00 22.14 ? 117 CYS B O   1 
ATOM   911  C CB  . CYS A 1 117 ? 0.716   -0.411  15.947 1.00 24.49 ? 117 CYS B CB  1 
ATOM   912  S SG  . CYS A 1 117 ? 2.442   -0.275  15.656 1.00 27.95 ? 117 CYS B SG  1 
ATOM   913  N N   . TYR A 1 118 ? -1.972  0.857   16.833 1.00 19.45 ? 118 TYR B N   1 
ATOM   914  C CA  . TYR A 1 118 ? -3.421  0.812   16.701 1.00 26.40 ? 118 TYR B CA  1 
ATOM   915  C C   . TYR A 1 118 ? -3.759  1.301   15.301 1.00 27.23 ? 118 TYR B C   1 
ATOM   916  O O   . TYR A 1 118 ? -3.216  2.318   14.856 1.00 27.10 ? 118 TYR B O   1 
ATOM   917  C CB  . TYR A 1 118 ? -4.103  1.684   17.779 1.00 24.10 ? 118 TYR B CB  1 
ATOM   918  C CG  . TYR A 1 118 ? -3.763  1.164   19.154 1.00 23.03 ? 118 TYR B CG  1 
ATOM   919  C CD1 . TYR A 1 118 ? -4.508  0.146   19.730 1.00 20.79 ? 118 TYR B CD1 1 
ATOM   920  C CD2 . TYR A 1 118 ? -2.646  1.633   19.835 1.00 24.89 ? 118 TYR B CD2 1 
ATOM   921  C CE1 . TYR A 1 118 ? -4.164  -0.383  20.961 1.00 22.76 ? 118 TYR B CE1 1 
ATOM   922  C CE2 . TYR A 1 118 ? -2.297  1.122   21.064 1.00 22.88 ? 118 TYR B CE2 1 
ATOM   923  C CZ  . TYR A 1 118 ? -3.058  0.106   21.620 1.00 22.17 ? 118 TYR B CZ  1 
ATOM   924  O OH  . TYR A 1 118 ? -2.707  -0.400  22.849 1.00 22.42 ? 118 TYR B OH  1 
ATOM   925  N N   . ASN A 1 119 ? -4.628  0.561   14.604 1.00 25.19 ? 119 ASN B N   1 
ATOM   926  C CA  . ASN A 1 119 ? -5.026  0.881   13.231 1.00 29.78 ? 119 ASN B CA  1 
ATOM   927  C C   . ASN A 1 119 ? -3.813  1.086   12.325 1.00 28.89 ? 119 ASN B C   1 
ATOM   928  O O   . ASN A 1 119 ? -3.807  1.939   11.436 1.00 29.91 ? 119 ASN B O   1 
ATOM   929  C CB  . ASN A 1 119 ? -5.958  2.095   13.214 1.00 31.57 ? 119 ASN B CB  1 
ATOM   930  C CG  . ASN A 1 119 ? -7.118  1.928   14.176 1.00 34.26 ? 119 ASN B CG  1 
ATOM   931  O OD1 . ASN A 1 119 ? -7.264  2.686   15.136 1.00 39.66 ? 119 ASN B OD1 1 
ATOM   932  N ND2 . ASN A 1 119 ? -7.933  0.908   13.941 1.00 40.47 ? 119 ASN B ND2 1 
ATOM   933  N N   . GLY A 1 120 ? -2.777  0.274   12.548 1.00 25.76 ? 120 GLY B N   1 
ATOM   934  C CA  . GLY A 1 120 ? -1.562  0.333   11.756 1.00 27.27 ? 120 GLY B CA  1 
ATOM   935  C C   . GLY A 1 120 ? -0.709  1.564   11.969 1.00 29.76 ? 120 GLY B C   1 
ATOM   936  O O   . GLY A 1 120 ? 0.208   1.813   11.176 1.00 26.77 ? 120 GLY B O   1 
ATOM   937  N N   . SER A 1 121 ? -0.980  2.351   13.007 1.00 30.06 ? 121 SER B N   1 
ATOM   938  C CA  . SER A 1 121 ? -0.194  3.552   13.271 1.00 32.80 ? 121 SER B CA  1 
ATOM   939  C C   . SER A 1 121 ? 0.554   3.404   14.587 1.00 31.37 ? 121 SER B C   1 
ATOM   940  O O   . SER A 1 121 ? -0.073  3.151   15.628 1.00 30.85 ? 121 SER B O   1 
ATOM   941  C CB  . SER A 1 121 ? -1.084  4.797   13.299 1.00 41.41 ? 121 SER B CB  1 
ATOM   942  O OG  . SER A 1 121 ? -1.967  4.812   12.194 1.00 43.69 ? 121 SER B OG  1 
ATOM   943  N N   . PRO A 1 122 ? 1.880   3.546   14.580 1.00 32.81 ? 122 PRO B N   1 
ATOM   944  C CA  . PRO A 1 122 ? 2.648   3.394   15.819 1.00 33.04 ? 122 PRO B CA  1 
ATOM   945  C C   . PRO A 1 122 ? 2.214   4.408   16.859 1.00 34.78 ? 122 PRO B C   1 
ATOM   946  O O   . PRO A 1 122 ? 2.019   5.586   16.559 1.00 41.11 ? 122 PRO B O   1 
ATOM   947  C CB  . PRO A 1 122 ? 4.087   3.643   15.367 1.00 32.34 ? 122 PRO B CB  1 
ATOM   948  C CG  . PRO A 1 122 ? 4.096   3.176   13.938 1.00 33.58 ? 122 PRO B CG  1 
ATOM   949  C CD  . PRO A 1 122 ? 2.760   3.661   13.405 1.00 31.95 ? 122 PRO B CD  1 
ATOM   950  N N   . SER A 1 123 ? 2.084   3.942   18.095 1.00 28.50 ? 123 SER B N   1 
ATOM   951  C CA  . SER A 1 123 ? 1.655   4.798   19.188 1.00 33.14 ? 123 SER B CA  1 
ATOM   952  C C   . SER A 1 123 ? 2.674   4.933   20.311 1.00 30.49 ? 123 SER B C   1 
ATOM   953  O O   . SER A 1 123 ? 2.703   5.975   20.970 1.00 29.54 ? 123 SER B O   1 
ATOM   954  C CB  . SER A 1 123 ? 0.320   4.296   19.755 1.00 33.34 ? 123 SER B CB  1 
ATOM   955  O OG  . SER A 1 123 ? 0.517   3.489   20.893 1.00 38.09 ? 123 SER B OG  1 
ATOM   956  N N   . GLY A 1 124 ? 3.533   3.943   20.528 1.00 26.07 ? 124 GLY B N   1 
ATOM   957  C CA  . GLY A 1 124 ? 4.518   4.069   21.587 1.00 23.46 ? 124 GLY B CA  1 
ATOM   958  C C   . GLY A 1 124 ? 5.482   2.911   21.575 1.00 25.70 ? 124 GLY B C   1 
ATOM   959  O O   . GLY A 1 124 ? 5.254   1.883   20.925 1.00 23.63 ? 124 GLY B O   1 
ATOM   960  N N   . VAL A 1 125 ? 6.576   3.088   22.311 1.00 21.85 ? 125 VAL B N   1 
ATOM   961  C CA  . VAL A 1 125 ? 7.619   2.076   22.382 1.00 20.45 ? 125 VAL B CA  1 
ATOM   962  C C   . VAL A 1 125 ? 8.050   1.879   23.834 1.00 21.83 ? 125 VAL B C   1 
ATOM   963  O O   . VAL A 1 125 ? 8.065   2.832   24.628 1.00 21.55 ? 125 VAL B O   1 
ATOM   964  C CB  . VAL A 1 125 ? 8.799   2.458   21.457 1.00 22.43 ? 125 VAL B CB  1 
ATOM   965  C CG1 . VAL A 1 125 ? 9.596   3.553   22.069 1.00 26.53 ? 125 VAL B CG1 1 
ATOM   966  C CG2 . VAL A 1 125 ? 9.657   1.265   21.167 1.00 22.39 ? 125 VAL B CG2 1 
ATOM   967  N N   . TYR A 1 126 ? 8.324   0.623   24.198 1.00 17.43 ? 126 TYR B N   1 
ATOM   968  C CA  . TYR A 1 126 ? 8.811   0.283   25.530 1.00 18.65 ? 126 TYR B CA  1 
ATOM   969  C C   . TYR A 1 126 ? 9.478   -1.084  25.503 1.00 19.13 ? 126 TYR B C   1 
ATOM   970  O O   . TYR A 1 126 ? 9.244   -1.891  24.598 1.00 20.38 ? 126 TYR B O   1 
ATOM   971  C CB  . TYR A 1 126 ? 7.686   0.273   26.563 1.00 20.14 ? 126 TYR B CB  1 
ATOM   972  C CG  . TYR A 1 126 ? 6.483   -0.549  26.165 1.00 18.88 ? 126 TYR B CG  1 
ATOM   973  C CD1 . TYR A 1 126 ? 6.413   -1.914  26.452 1.00 16.72 ? 126 TYR B CD1 1 
ATOM   974  C CD2 . TYR A 1 126 ? 5.406   0.038   25.524 1.00 18.10 ? 126 TYR B CD2 1 
ATOM   975  C CE1 . TYR A 1 126 ? 5.295   -2.662  26.095 1.00 16.06 ? 126 TYR B CE1 1 
ATOM   976  C CE2 . TYR A 1 126 ? 4.273   -0.697  25.187 1.00 22.61 ? 126 TYR B CE2 1 
ATOM   977  C CZ  . TYR A 1 126 ? 4.232   -2.047  25.461 1.00 20.41 ? 126 TYR B CZ  1 
ATOM   978  O OH  . TYR A 1 126 ? 3.115   -2.779  25.122 1.00 21.18 ? 126 TYR B OH  1 
ATOM   979  N N   . GLN A 1 127 ? 10.267  -1.349  26.550 1.00 19.93 ? 127 GLN B N   1 
ATOM   980  C CA  . GLN A 1 127 ? 11.045  -2.579  26.690 1.00 21.35 ? 127 GLN B CA  1 
ATOM   981  C C   . GLN A 1 127 ? 10.267  -3.615  27.494 1.00 19.79 ? 127 GLN B C   1 
ATOM   982  O O   . GLN A 1 127 ? 9.656   -3.281  28.513 1.00 22.08 ? 127 GLN B O   1 
ATOM   983  C CB  . GLN A 1 127 ? 12.360  -2.330  27.429 1.00 23.30 ? 127 GLN B CB  1 
ATOM   984  C CG  . GLN A 1 127 ? 13.462  -1.775  26.596 1.00 22.85 ? 127 GLN B CG  1 
ATOM   985  C CD  . GLN A 1 127 ? 13.950  -2.716  25.555 1.00 25.13 ? 127 GLN B CD  1 
ATOM   986  O OE1 . GLN A 1 127 ? 13.500  -2.625  24.422 1.00 26.39 ? 127 GLN B OE1 1 
ATOM   987  N NE2 . GLN A 1 127 ? 14.891  -3.602  25.902 1.00 25.80 ? 127 GLN B NE2 1 
ATOM   988  N N   . CYS A 1 128 ? 10.355  -4.880  27.069 1.00 18.93 ? 128 CYS B N   1 
ATOM   989  C CA  . CYS A 1 128 ? 9.782   -6.012  27.790 1.00 19.16 ? 128 CYS B CA  1 
ATOM   990  C C   . CYS A 1 128 ? 10.794  -7.143  27.893 1.00 20.71 ? 128 CYS B C   1 
ATOM   991  O O   . CYS A 1 128 ? 11.636  -7.342  27.011 1.00 21.09 ? 128 CYS B O   1 
ATOM   992  C CB  . CYS A 1 128 ? 8.533   -6.559  27.083 1.00 17.79 ? 128 CYS B CB  1 
ATOM   993  S SG  . CYS A 1 128 ? 7.108   -5.505  27.319 1.00 23.96 ? 128 CYS B SG  1 
ATOM   994  N N   . ALA A 1 129 ? 10.696  -7.904  28.968 1.00 17.67 ? 129 ALA B N   1 
ATOM   995  C CA  . ALA A 1 129 ? 11.397  -9.172  29.063 1.00 17.14 ? 129 ALA B CA  1 
ATOM   996  C C   . ALA A 1 129 ? 10.400  -10.296 28.837 1.00 18.15 ? 129 ALA B C   1 
ATOM   997  O O   . ALA A 1 129 ? 9.283   -10.248 29.354 1.00 20.72 ? 129 ALA B O   1 
ATOM   998  C CB  . ALA A 1 129 ? 12.054  -9.346  30.432 1.00 19.47 ? 129 ALA B CB  1 
ATOM   999  N N   . MET A 1 130 ? 10.787  -11.282 28.031 1.00 19.89 ? 130 MET B N   1 
ATOM   1000 C CA  . MET A 1 130 ? 10.158  -12.603 28.114 1.00 17.34 ? 130 MET B CA  1 
ATOM   1001 C C   . MET A 1 130 ? 10.343  -13.253 29.472 1.00 20.67 ? 130 MET B C   1 
ATOM   1002 O O   . MET A 1 130 ? 11.445  -13.706 29.773 1.00 21.80 ? 130 MET B O   1 
ATOM   1003 C CB  . MET A 1 130 ? 10.729  -13.542 27.056 1.00 18.98 ? 130 MET B CB  1 
ATOM   1004 C CG  . MET A 1 130 ? 9.860   -14.772 26.687 1.00 22.13 ? 130 MET B CG  1 
ATOM   1005 S SD  . MET A 1 130 ? 8.080   -14.618 26.554 1.00 21.96 ? 130 MET B SD  1 
ATOM   1006 C CE  . MET A 1 130 ? 7.922   -13.741 25.010 1.00 19.63 ? 130 MET B CE  1 
ATOM   1007 N N   . ARG A 1 131 ? 9.282   -13.321 30.278 1.00 16.77 ? 131 ARG B N   1 
ATOM   1008 C CA  . ARG A 1 131 ? 9.378   -13.931 31.597 1.00 18.92 ? 131 ARG B CA  1 
ATOM   1009 C C   . ARG A 1 131 ? 9.532   -15.440 31.468 1.00 19.63 ? 131 ARG B C   1 
ATOM   1010 O O   . ARG A 1 131 ? 9.246   -16.031 30.426 1.00 18.89 ? 131 ARG B O   1 
ATOM   1011 C CB  . ARG A 1 131 ? 8.136   -13.649 32.454 1.00 21.47 ? 131 ARG B CB  1 
ATOM   1012 C CG  . ARG A 1 131 ? 7.593   -12.248 32.389 1.00 27.39 ? 131 ARG B CG  1 
ATOM   1013 C CD  . ARG A 1 131 ? 8.377   -11.283 33.213 1.00 21.15 ? 131 ARG B CD  1 
ATOM   1014 N NE  . ARG A 1 131 ? 8.767   -11.775 34.531 1.00 22.61 ? 131 ARG B NE  1 
ATOM   1015 C CZ  . ARG A 1 131 ? 9.732   -11.207 35.244 1.00 26.71 ? 131 ARG B CZ  1 
ATOM   1016 N NH1 . ARG A 1 131 ? 10.310  -10.090 34.835 1.00 21.22 ? 131 ARG B NH1 1 
ATOM   1017 N NH2 . ARG A 1 131 ? 10.133  -11.775 36.381 1.00 20.07 ? 131 ARG B NH2 1 
ATOM   1018 N N   . HIS A 1 132 ? 9.971   -16.065 32.563 1.00 22.88 ? 132 HIS B N   1 
ATOM   1019 C CA  . HIS A 1 132 ? 10.090  -17.521 32.598 1.00 26.06 ? 132 HIS B CA  1 
ATOM   1020 C C   . HIS A 1 132 ? 8.746   -18.231 32.484 1.00 23.73 ? 132 HIS B C   1 
ATOM   1021 O O   . HIS A 1 132 ? 8.717   -19.415 32.125 1.00 22.42 ? 132 HIS B O   1 
ATOM   1022 C CB  . HIS A 1 132 ? 10.827  -17.939 33.868 1.00 28.34 ? 132 HIS B CB  1 
ATOM   1023 C CG  . HIS A 1 132 ? 12.298  -17.685 33.794 1.00 28.80 ? 132 HIS B CG  1 
ATOM   1024 N ND1 . HIS A 1 132 ? 13.117  -18.366 32.917 1.00 31.94 ? 132 HIS B ND1 1 
ATOM   1025 C CD2 . HIS A 1 132 ? 13.093  -16.802 34.445 1.00 31.01 ? 132 HIS B CD2 1 
ATOM   1026 C CE1 . HIS A 1 132 ? 14.356  -17.926 33.045 1.00 35.25 ? 132 HIS B CE1 1 
ATOM   1027 N NE2 . HIS A 1 132 ? 14.370  -16.976 33.964 1.00 31.99 ? 132 HIS B NE2 1 
ATOM   1028 N N   . ASN A 1 133 ? 7.638   -17.545 32.748 1.00 21.68 ? 133 ASN B N   1 
ATOM   1029 C CA  . ASN A 1 133 ? 6.324   -18.114 32.492 1.00 23.07 ? 133 ASN B CA  1 
ATOM   1030 C C   . ASN A 1 133 ? 5.784   -17.736 31.112 1.00 24.68 ? 133 ASN B C   1 
ATOM   1031 O O   . ASN A 1 133 ? 4.598   -17.951 30.836 1.00 21.28 ? 133 ASN B O   1 
ATOM   1032 C CB  . ASN A 1 133 ? 5.337   -17.718 33.596 1.00 24.11 ? 133 ASN B CB  1 
ATOM   1033 C CG  . ASN A 1 133 ? 4.978   -16.242 33.584 1.00 24.21 ? 133 ASN B CG  1 
ATOM   1034 O OD1 . ASN A 1 133 ? 5.480   -15.469 32.765 1.00 21.88 ? 133 ASN B OD1 1 
ATOM   1035 N ND2 . ASN A 1 133 ? 4.092   -15.843 34.500 1.00 23.99 ? 133 ASN B ND2 1 
ATOM   1036 N N   . PHE A 1 134 ? 6.639   -17.181 30.251 1.00 20.47 ? 134 PHE B N   1 
ATOM   1037 C CA  . PHE A 1 134 ? 6.342   -16.964 28.842 1.00 20.22 ? 134 PHE B CA  1 
ATOM   1038 C C   . PHE A 1 134 ? 5.274   -15.901 28.638 1.00 19.06 ? 134 PHE B C   1 
ATOM   1039 O O   . PHE A 1 134 ? 4.542   -15.937 27.645 1.00 21.09 ? 134 PHE B O   1 
ATOM   1040 C CB  . PHE A 1 134 ? 5.928   -18.262 28.155 1.00 22.75 ? 134 PHE B CB  1 
ATOM   1041 C CG  . PHE A 1 134 ? 6.961   -19.341 28.250 1.00 28.10 ? 134 PHE B CG  1 
ATOM   1042 C CD1 . PHE A 1 134 ? 8.170   -19.213 27.594 1.00 30.16 ? 134 PHE B CD1 1 
ATOM   1043 C CD2 . PHE A 1 134 ? 6.728   -20.474 29.009 1.00 31.01 ? 134 PHE B CD2 1 
ATOM   1044 C CE1 . PHE A 1 134 ? 9.135   -20.203 27.680 1.00 34.17 ? 134 PHE B CE1 1 
ATOM   1045 C CE2 . PHE A 1 134 ? 7.690   -21.472 29.100 1.00 34.45 ? 134 PHE B CE2 1 
ATOM   1046 C CZ  . PHE A 1 134 ? 8.897   -21.325 28.432 1.00 31.49 ? 134 PHE B CZ  1 
ATOM   1047 N N   . THR A 1 135 ? 5.175   -14.965 29.576 1.00 17.43 ? 135 THR B N   1 
ATOM   1048 C CA  . THR A 1 135 ? 4.363   -13.765 29.432 1.00 17.60 ? 135 THR B CA  1 
ATOM   1049 C C   . THR A 1 135 ? 5.280   -12.545 29.402 1.00 15.61 ? 135 THR B C   1 
ATOM   1050 O O   . THR A 1 135 ? 6.473   -12.639 29.685 1.00 18.43 ? 135 THR B O   1 
ATOM   1051 C CB  . THR A 1 135 ? 3.357   -13.629 30.581 1.00 19.13 ? 135 THR B CB  1 
ATOM   1052 O OG1 . THR A 1 135 ? 4.061   -13.398 31.807 1.00 20.29 ? 135 THR B OG1 1 
ATOM   1053 C CG2 . THR A 1 135 ? 2.500   -14.918 30.703 1.00 20.67 ? 135 THR B CG2 1 
ATOM   1054 N N   . ILE A 1 136 ? 4.715   -11.406 29.014 1.00 16.70 ? 136 ILE B N   1 
ATOM   1055 C CA  . ILE A 1 136 ? 5.423   -10.131 29.050 1.00 16.13 ? 136 ILE B CA  1 
ATOM   1056 C C   . ILE A 1 136 ? 4.536   -9.109  29.745 1.00 19.00 ? 136 ILE B C   1 
ATOM   1057 O O   . ILE A 1 136 ? 3.299   -9.195  29.715 1.00 18.76 ? 136 ILE B O   1 
ATOM   1058 C CB  . ILE A 1 136 ? 5.832   -9.640  27.641 1.00 17.68 ? 136 ILE B CB  1 
ATOM   1059 C CG1 . ILE A 1 136 ? 4.603   -9.382  26.769 1.00 18.79 ? 136 ILE B CG1 1 
ATOM   1060 C CG2 . ILE A 1 136 ? 6.832   -10.615 26.970 1.00 16.96 ? 136 ILE B CG2 1 
ATOM   1061 C CD1 . ILE A 1 136 ? 4.893   -8.487  25.577 1.00 18.71 ? 136 ILE B CD1 1 
ATOM   1062 N N   . LYS A 1 137 ? 5.176   -8.143  30.397 1.00 19.20 ? 137 LYS B N   1 
ATOM   1063 C CA  . LYS A 1 137 ? 4.450   -7.106  31.128 1.00 19.76 ? 137 LYS B CA  1 
ATOM   1064 C C   . LYS A 1 137 ? 4.317   -5.908  30.196 1.00 20.53 ? 137 LYS B C   1 
ATOM   1065 O O   . LYS A 1 137 ? 5.099   -4.954  30.234 1.00 25.06 ? 137 LYS B O   1 
ATOM   1066 C CB  . LYS A 1 137 ? 5.157   -6.742  32.433 1.00 21.64 ? 137 LYS B CB  1 
ATOM   1067 C CG  . LYS A 1 137 ? 5.218   -7.870  33.443 1.00 22.17 ? 137 LYS B CG  1 
ATOM   1068 C CD  . LYS A 1 137 ? 6.200   -7.568  34.574 1.00 29.62 ? 137 LYS B CD  1 
ATOM   1069 C CE  . LYS A 1 137 ? 5.956   -8.493  35.769 1.00 32.99 ? 137 LYS B CE  1 
ATOM   1070 N NZ  . LYS A 1 137 ? 4.936   -8.020  36.749 1.00 46.48 ? 137 LYS B NZ  1 
ATOM   1071 N N   . GLY A 1 138 ? 3.321   -5.982  29.316 1.00 19.03 ? 138 GLY B N   1 
ATOM   1072 C CA  . GLY A 1 138 ? 3.142   -5.002  28.269 1.00 19.76 ? 138 GLY B CA  1 
ATOM   1073 C C   . GLY A 1 138 ? 2.079   -3.982  28.627 1.00 22.76 ? 138 GLY B C   1 
ATOM   1074 O O   . GLY A 1 138 ? 1.570   -3.938  29.747 1.00 22.99 ? 138 GLY B O   1 
ATOM   1075 N N   . SER A 1 139 ? 1.766   -3.132  27.652 1.00 18.56 ? 139 SER B N   1 
ATOM   1076 C CA  . SER A 1 139 ? 0.668   -2.164  27.743 1.00 19.02 ? 139 SER B CA  1 
ATOM   1077 C C   . SER A 1 139 ? -0.043  -2.215  26.396 1.00 19.31 ? 139 SER B C   1 
ATOM   1078 O O   . SER A 1 139 ? 0.465   -1.690  25.403 1.00 21.52 ? 139 SER B O   1 
ATOM   1079 C CB  . SER A 1 139 ? 1.170   -0.757  28.060 1.00 16.17 ? 139 SER B CB  1 
ATOM   1080 O OG  . SER A 1 139 ? 0.087   0.149   28.145 1.00 20.02 ? 139 SER B OG  1 
ATOM   1081 N N   . PHE A 1 140 ? -1.207  -2.863  26.365 1.00 18.71 ? 140 PHE B N   1 
ATOM   1082 C CA  . PHE A 1 140 ? -1.882  -3.207  25.118 1.00 19.27 ? 140 PHE B CA  1 
ATOM   1083 C C   . PHE A 1 140 ? -3.377  -3.018  25.309 1.00 20.99 ? 140 PHE B C   1 
ATOM   1084 O O   . PHE A 1 140 ? -3.943  -3.510  26.291 1.00 22.03 ? 140 PHE B O   1 
ATOM   1085 C CB  . PHE A 1 140 ? -1.626  -4.671  24.718 1.00 18.49 ? 140 PHE B CB  1 
ATOM   1086 C CG  . PHE A 1 140 ? -0.223  -4.972  24.289 1.00 20.76 ? 140 PHE B CG  1 
ATOM   1087 C CD1 . PHE A 1 140 ? 0.285   -4.484  23.098 1.00 22.35 ? 140 PHE B CD1 1 
ATOM   1088 C CD2 . PHE A 1 140 ? 0.576   -5.775  25.074 1.00 19.12 ? 140 PHE B CD2 1 
ATOM   1089 C CE1 . PHE A 1 140 ? 1.591   -4.804  22.707 1.00 22.16 ? 140 PHE B CE1 1 
ATOM   1090 C CE2 . PHE A 1 140 ? 1.868   -6.090  24.702 1.00 21.36 ? 140 PHE B CE2 1 
ATOM   1091 C CZ  . PHE A 1 140 ? 2.371   -5.609  23.514 1.00 20.90 ? 140 PHE B CZ  1 
ATOM   1092 N N   . LEU A 1 141 ? -4.016  -2.344  24.359 1.00 22.11 ? 141 LEU B N   1 
ATOM   1093 C CA  . LEU A 1 141 ? -5.446  -2.074  24.395 1.00 23.24 ? 141 LEU B CA  1 
ATOM   1094 C C   . LEU A 1 141 ? -6.112  -2.765  23.215 1.00 26.68 ? 141 LEU B C   1 
ATOM   1095 O O   . LEU A 1 141 ? -5.444  -3.348  22.360 1.00 22.37 ? 141 LEU B O   1 
ATOM   1096 C CB  . LEU A 1 141 ? -5.711  -0.570  24.346 1.00 28.55 ? 141 LEU B CB  1 
ATOM   1097 C CG  . LEU A 1 141 ? -5.494  0.212   25.643 1.00 31.64 ? 141 LEU B CG  1 
ATOM   1098 C CD1 . LEU A 1 141 ? -5.828  1.669   25.398 1.00 35.66 ? 141 LEU B CD1 1 
ATOM   1099 C CD2 . LEU A 1 141 ? -6.334  -0.351  26.783 1.00 30.88 ? 141 LEU B CD2 1 
ATOM   1100 N N   . ASN A 1 142 ? -7.446  -2.722  23.195 1.00 23.89 ? 142 ASN B N   1 
ATOM   1101 C CA  . ASN A 1 142 ? -8.202  -3.141  22.020 1.00 27.28 ? 142 ASN B CA  1 
ATOM   1102 C C   . ASN A 1 142 ? -7.608  -2.544  20.751 1.00 25.39 ? 142 ASN B C   1 
ATOM   1103 O O   . ASN A 1 142 ? -7.416  -1.323  20.649 1.00 26.46 ? 142 ASN B O   1 
ATOM   1104 C CB  . ASN A 1 142 ? -9.667  -2.713  22.167 1.00 26.16 ? 142 ASN B CB  1 
ATOM   1105 C CG  . ASN A 1 142 ? -10.433 -3.611  23.094 1.00 29.08 ? 142 ASN B CG  1 
ATOM   1106 O OD1 . ASN A 1 142 ? -9.919  -4.642  23.536 1.00 29.82 ? 142 ASN B OD1 1 
ATOM   1107 N ND2 . ASN A 1 142 ? -11.673 -3.239  23.395 1.00 32.00 ? 142 ASN B ND2 1 
ATOM   1108 N N   . GLY A 1 143 ? -7.293  -3.419  19.789 1.00 24.23 ? 143 GLY B N   1 
ATOM   1109 C CA  . GLY A 1 143 ? -6.689  -3.011  18.538 1.00 21.25 ? 143 GLY B CA  1 
ATOM   1110 C C   . GLY A 1 143 ? -5.180  -3.119  18.479 1.00 24.27 ? 143 GLY B C   1 
ATOM   1111 O O   . GLY A 1 143 ? -4.593  -2.777  17.441 1.00 22.65 ? 143 GLY B O   1 
ATOM   1112 N N   . SER A 1 144 ? -4.531  -3.573  19.556 1.00 21.15 ? 144 SER B N   1 
ATOM   1113 C CA  . SER A 1 144 ? -3.076  -3.680  19.563 1.00 19.90 ? 144 SER B CA  1 
ATOM   1114 C C   . SER A 1 144 ? -2.564  -4.973  18.951 1.00 21.94 ? 144 SER B C   1 
ATOM   1115 O O   . SER A 1 144 ? -1.366  -5.063  18.675 1.00 19.61 ? 144 SER B O   1 
ATOM   1116 C CB  . SER A 1 144 ? -2.531  -3.566  20.993 1.00 20.03 ? 144 SER B CB  1 
ATOM   1117 O OG  . SER A 1 144 ? -3.097  -4.568  21.825 1.00 21.70 ? 144 SER B OG  1 
ATOM   1118 N N   . CYS A 1 145 ? -3.420  -5.976  18.737 1.00 21.82 ? 145 CYS B N   1 
ATOM   1119 C CA  . CYS A 1 145 ? -2.927  -7.238  18.196 1.00 19.81 ? 145 CYS B CA  1 
ATOM   1120 C C   . CYS A 1 145 ? -2.233  -7.010  16.859 1.00 18.92 ? 145 CYS B C   1 
ATOM   1121 O O   . CYS A 1 145 ? -2.644  -6.158  16.065 1.00 20.44 ? 145 CYS B O   1 
ATOM   1122 C CB  . CYS A 1 145 ? -4.079  -8.224  18.029 1.00 22.89 ? 145 CYS B CB  1 
ATOM   1123 S SG  . CYS A 1 145 ? -4.602  -8.851  19.588 1.00 24.09 ? 145 CYS B SG  1 
ATOM   1124 N N   . GLY A 1 146 ? -1.158  -7.771  16.614 1.00 19.21 ? 146 GLY B N   1 
ATOM   1125 C CA  . GLY A 1 146 ? -0.305  -7.527  15.473 1.00 21.15 ? 146 GLY B CA  1 
ATOM   1126 C C   . GLY A 1 146 ? 0.856   -6.584  15.724 1.00 18.50 ? 146 GLY B C   1 
ATOM   1127 O O   . GLY A 1 146 ? 1.785   -6.546  14.911 1.00 19.89 ? 146 GLY B O   1 
ATOM   1128 N N   . SER A 1 147 ? 0.829   -5.807  16.807 1.00 20.35 ? 147 SER B N   1 
ATOM   1129 C CA  . SER A 1 147 ? 2.033   -5.095  17.230 1.00 20.24 ? 147 SER B CA  1 
ATOM   1130 C C   . SER A 1 147 ? 3.170   -6.084  17.462 1.00 20.65 ? 147 SER B C   1 
ATOM   1131 O O   . SER A 1 147 ? 2.951   -7.205  17.936 1.00 19.43 ? 147 SER B O   1 
ATOM   1132 C CB  . SER A 1 147 ? 1.776   -4.319  18.517 1.00 18.48 ? 147 SER B CB  1 
ATOM   1133 O OG  . SER A 1 147 ? 0.746   -3.368  18.344 1.00 22.10 ? 147 SER B OG  1 
ATOM   1134 N N   . VAL A 1 148 ? 4.403   -5.669  17.159 1.00 18.91 ? 148 VAL B N   1 
ATOM   1135 C CA  . VAL A 1 148 ? 5.498   -6.625  17.198 1.00 19.41 ? 148 VAL B CA  1 
ATOM   1136 C C   . VAL A 1 148 ? 6.551   -6.208  18.220 1.00 20.73 ? 148 VAL B C   1 
ATOM   1137 O O   . VAL A 1 148 ? 6.657   -5.046  18.628 1.00 18.72 ? 148 VAL B O   1 
ATOM   1138 C CB  . VAL A 1 148 ? 6.155   -6.843  15.815 1.00 19.53 ? 148 VAL B CB  1 
ATOM   1139 C CG1 . VAL A 1 148 ? 5.136   -7.451  14.841 1.00 22.85 ? 148 VAL B CG1 1 
ATOM   1140 C CG2 . VAL A 1 148 ? 6.800   -5.580  15.271 1.00 20.49 ? 148 VAL B CG2 1 
ATOM   1141 N N   . GLY A 1 149 ? 7.342   -7.197  18.632 1.00 18.03 ? 149 GLY B N   1 
ATOM   1142 C CA  . GLY A 1 149 ? 8.499   -6.978  19.476 1.00 17.53 ? 149 GLY B CA  1 
ATOM   1143 C C   . GLY A 1 149 ? 9.755   -7.295  18.687 1.00 19.13 ? 149 GLY B C   1 
ATOM   1144 O O   . GLY A 1 149 ? 9.743   -8.171  17.812 1.00 20.56 ? 149 GLY B O   1 
ATOM   1145 N N   . PHE A 1 150 ? 10.843  -6.577  18.994 1.00 18.32 ? 150 PHE B N   1 
ATOM   1146 C CA  . PHE A 1 150 ? 12.049  -6.695  18.174 1.00 20.96 ? 150 PHE B CA  1 
ATOM   1147 C C   . PHE A 1 150 ? 13.300  -6.269  18.937 1.00 20.37 ? 150 PHE B C   1 
ATOM   1148 O O   . PHE A 1 150 ? 13.249  -5.500  19.901 1.00 19.12 ? 150 PHE B O   1 
ATOM   1149 C CB  . PHE A 1 150 ? 11.935  -5.852  16.895 1.00 20.67 ? 150 PHE B CB  1 
ATOM   1150 C CG  . PHE A 1 150 ? 11.754  -4.371  17.150 1.00 22.00 ? 150 PHE B CG  1 
ATOM   1151 C CD1 . PHE A 1 150 ? 10.514  -3.847  17.481 1.00 22.08 ? 150 PHE B CD1 1 
ATOM   1152 C CD2 . PHE A 1 150 ? 12.834  -3.504  17.041 1.00 24.33 ? 150 PHE B CD2 1 
ATOM   1153 C CE1 . PHE A 1 150 ? 10.355  -2.489  17.716 1.00 21.62 ? 150 PHE B CE1 1 
ATOM   1154 C CE2 . PHE A 1 150 ? 12.680  -2.146  17.276 1.00 23.56 ? 150 PHE B CE2 1 
ATOM   1155 C CZ  . PHE A 1 150 ? 11.444  -1.638  17.604 1.00 23.00 ? 150 PHE B CZ  1 
ATOM   1156 N N   . ASN A 1 151 ? 14.438  -6.765  18.458 1.00 22.37 ? 151 ASN B N   1 
ATOM   1157 C CA  . ASN A 1 151 ? 15.745  -6.214  18.788 1.00 26.88 ? 151 ASN B CA  1 
ATOM   1158 C C   . ASN A 1 151 ? 16.411  -5.713  17.515 1.00 26.85 ? 151 ASN B C   1 
ATOM   1159 O O   . ASN A 1 151 ? 16.094  -6.146  16.401 1.00 24.39 ? 151 ASN B O   1 
ATOM   1160 C CB  . ASN A 1 151 ? 16.648  -7.255  19.461 1.00 23.74 ? 151 ASN B CB  1 
ATOM   1161 C CG  . ASN A 1 151 ? 16.299  -7.490  20.929 1.00 29.60 ? 151 ASN B CG  1 
ATOM   1162 O OD1 . ASN A 1 151 ? 16.825  -6.822  21.822 1.00 29.74 ? 151 ASN B OD1 1 
ATOM   1163 N ND2 . ASN A 1 151 ? 15.433  -8.459  21.183 1.00 22.81 ? 151 ASN B ND2 1 
ATOM   1164 N N   . ILE A 1 152 ? 17.348  -4.789  17.671 1.00 27.43 ? 152 ILE B N   1 
ATOM   1165 C CA  . ILE A 1 152 ? 18.100  -4.293  16.530 1.00 31.55 ? 152 ILE B CA  1 
ATOM   1166 C C   . ILE A 1 152 ? 19.567  -4.597  16.780 1.00 35.59 ? 152 ILE B C   1 
ATOM   1167 O O   . ILE A 1 152 ? 20.090  -4.321  17.865 1.00 34.76 ? 152 ILE B O   1 
ATOM   1168 C CB  . ILE A 1 152 ? 17.871  -2.794  16.290 1.00 29.89 ? 152 ILE B CB  1 
ATOM   1169 C CG1 . ILE A 1 152 ? 16.407  -2.550  15.927 1.00 28.69 ? 152 ILE B CG1 1 
ATOM   1170 C CG2 . ILE A 1 152 ? 18.757  -2.322  15.139 1.00 35.77 ? 152 ILE B CG2 1 
ATOM   1171 C CD1 . ILE A 1 152 ? 16.100  -1.136  15.535 1.00 32.72 ? 152 ILE B CD1 1 
ATOM   1172 N N   . ASP A 1 153 ? 20.213  -5.207  15.800 1.00 38.61 ? 153 ASP B N   1 
ATOM   1173 C CA  . ASP A 1 153 ? 21.646  -5.454  15.860 1.00 43.61 ? 153 ASP B CA  1 
ATOM   1174 C C   . ASP A 1 153 ? 22.253  -4.765  14.651 1.00 47.86 ? 153 ASP B C   1 
ATOM   1175 O O   . ASP A 1 153 ? 22.007  -5.180  13.511 1.00 44.09 ? 153 ASP B O   1 
ATOM   1176 C CB  . ASP A 1 153 ? 21.959  -6.946  15.869 1.00 46.96 ? 153 ASP B CB  1 
ATOM   1177 C CG  . ASP A 1 153 ? 23.441  -7.223  15.745 1.00 61.33 ? 153 ASP B CG  1 
ATOM   1178 O OD1 . ASP A 1 153 ? 24.208  -6.713  16.595 1.00 63.72 ? 153 ASP B OD1 1 
ATOM   1179 O OD2 . ASP A 1 153 ? 23.843  -7.934  14.797 1.00 65.54 ? 153 ASP B OD2 1 
ATOM   1180 N N   . TYR A 1 154 ? 23.017  -3.701  14.907 1.00 50.00 ? 154 TYR B N   1 
ATOM   1181 C CA  . TYR A 1 154 ? 23.587  -2.874  13.853 1.00 52.02 ? 154 TYR B CA  1 
ATOM   1182 C C   . TYR A 1 154 ? 22.466  -2.315  12.989 1.00 48.83 ? 154 TYR B C   1 
ATOM   1183 O O   . TYR A 1 154 ? 21.818  -1.331  13.359 1.00 50.02 ? 154 TYR B O   1 
ATOM   1184 C CB  . TYR A 1 154 ? 24.598  -3.692  13.043 1.00 52.40 ? 154 TYR B CB  1 
ATOM   1185 C CG  . TYR A 1 154 ? 25.722  -4.199  13.922 1.00 60.01 ? 154 TYR B CG  1 
ATOM   1186 C CD1 . TYR A 1 154 ? 26.596  -3.315  14.547 1.00 67.60 ? 154 TYR B CD1 1 
ATOM   1187 C CD2 . TYR A 1 154 ? 25.850  -5.554  14.206 1.00 61.23 ? 154 TYR B CD2 1 
ATOM   1188 C CE1 . TYR A 1 154 ? 27.611  -3.774  15.380 1.00 69.42 ? 154 TYR B CE1 1 
ATOM   1189 C CE2 . TYR A 1 154 ? 26.856  -6.021  15.044 1.00 62.96 ? 154 TYR B CE2 1 
ATOM   1190 C CZ  . TYR A 1 154 ? 27.733  -5.127  15.625 1.00 65.54 ? 154 TYR B CZ  1 
ATOM   1191 O OH  . TYR A 1 154 ? 28.729  -5.593  16.454 1.00 67.67 ? 154 TYR B OH  1 
ATOM   1192 N N   . ASP A 1 155 ? 22.205  -2.955  11.856 1.00 46.38 ? 155 ASP B N   1 
ATOM   1193 C CA  . ASP A 1 155 ? 21.168  -2.509  10.938 1.00 44.87 ? 155 ASP B CA  1 
ATOM   1194 C C   . ASP A 1 155 ? 20.141  -3.601  10.670 1.00 40.95 ? 155 ASP B C   1 
ATOM   1195 O O   . ASP A 1 155 ? 19.292  -3.444  9.785  1.00 38.51 ? 155 ASP B O   1 
ATOM   1196 C CB  . ASP A 1 155 ? 21.827  -2.028  9.647  1.00 48.47 ? 155 ASP B CB  1 
ATOM   1197 C CG  . ASP A 1 155 ? 22.654  -3.112  8.990  1.00 51.05 ? 155 ASP B CG  1 
ATOM   1198 O OD1 . ASP A 1 155 ? 23.069  -4.046  9.709  1.00 51.36 ? 155 ASP B OD1 1 
ATOM   1199 O OD2 . ASP A 1 155 ? 22.831  -3.067  7.752  1.00 53.26 ? 155 ASP B OD2 1 
ATOM   1200 N N   . CYS A 1 156 ? 20.193  -4.690  11.431 1.00 40.19 ? 156 CYS B N   1 
ATOM   1201 C CA  . CYS A 1 156 ? 19.323  -5.843  11.256 1.00 34.10 ? 156 CYS B CA  1 
ATOM   1202 C C   . CYS A 1 156 ? 18.270  -5.863  12.355 1.00 34.08 ? 156 CYS B C   1 
ATOM   1203 O O   . CYS A 1 156 ? 18.610  -5.891  13.542 1.00 29.19 ? 156 CYS B O   1 
ATOM   1204 C CB  . CYS A 1 156 ? 20.129  -7.136  11.297 1.00 37.64 ? 156 CYS B CB  1 
ATOM   1205 S SG  . CYS A 1 156 ? 19.168  -8.579  10.852 1.00 36.16 ? 156 CYS B SG  1 
ATOM   1206 N N   . VAL A 1 157 ? 17.004  -5.879  11.958 1.00 29.70 ? 157 VAL B N   1 
ATOM   1207 C CA  . VAL A 1 157 ? 15.893  -5.996  12.897 1.00 26.03 ? 157 VAL B CA  1 
ATOM   1208 C C   . VAL A 1 157 ? 15.595  -7.477  13.090 1.00 23.66 ? 157 VAL B C   1 
ATOM   1209 O O   . VAL A 1 157 ? 15.269  -8.182  12.131 1.00 25.83 ? 157 VAL B O   1 
ATOM   1210 C CB  . VAL A 1 157 ? 14.651  -5.254  12.383 1.00 26.19 ? 157 VAL B CB  1 
ATOM   1211 C CG1 . VAL A 1 157 ? 13.506  -5.373  13.387 1.00 24.60 ? 157 VAL B CG1 1 
ATOM   1212 C CG2 . VAL A 1 157 ? 14.960  -3.800  12.102 1.00 26.20 ? 157 VAL B CG2 1 
ATOM   1213 N N   . SER A 1 158 ? 15.699  -7.952  14.326 1.00 22.32 ? 158 SER B N   1 
ATOM   1214 C CA  . SER A 1 158 ? 15.335  -9.323  14.681 1.00 23.62 ? 158 SER B CA  1 
ATOM   1215 C C   . SER A 1 158 ? 13.949  -9.279  15.313 1.00 23.98 ? 158 SER B C   1 
ATOM   1216 O O   . SER A 1 158 ? 13.814  -8.910  16.479 1.00 22.69 ? 158 SER B O   1 
ATOM   1217 C CB  . SER A 1 158 ? 16.355  -9.933  15.637 1.00 24.91 ? 158 SER B CB  1 
ATOM   1218 O OG  . SER A 1 158 ? 17.528  -10.346 14.945 1.00 30.30 ? 158 SER B OG  1 
ATOM   1219 N N   . PHE A 1 159 ? 12.925  -9.649  14.540 1.00 20.15 ? 159 PHE B N   1 
ATOM   1220 C CA  . PHE A 1 159 ? 11.548  -9.687  15.037 1.00 21.43 ? 159 PHE B CA  1 
ATOM   1221 C C   . PHE A 1 159 ? 11.379  -10.949 15.875 1.00 23.55 ? 159 PHE B C   1 
ATOM   1222 O O   . PHE A 1 159 ? 11.770  -12.037 15.446 1.00 22.45 ? 159 PHE B O   1 
ATOM   1223 C CB  . PHE A 1 159 ? 10.554  -9.688  13.871 1.00 20.22 ? 159 PHE B CB  1 
ATOM   1224 C CG  . PHE A 1 159 ? 10.498  -8.393  13.099 1.00 22.07 ? 159 PHE B CG  1 
ATOM   1225 C CD1 . PHE A 1 159 ? 9.861   -7.265  13.609 1.00 16.72 ? 159 PHE B CD1 1 
ATOM   1226 C CD2 . PHE A 1 159 ? 11.110  -8.307  11.859 1.00 23.61 ? 159 PHE B CD2 1 
ATOM   1227 C CE1 . PHE A 1 159 ? 9.812   -6.092  12.878 1.00 24.51 ? 159 PHE B CE1 1 
ATOM   1228 C CE2 . PHE A 1 159 ? 11.097  -7.134  11.133 1.00 22.01 ? 159 PHE B CE2 1 
ATOM   1229 C CZ  . PHE A 1 159 ? 10.449  -6.022  11.636 1.00 23.86 ? 159 PHE B CZ  1 
ATOM   1230 N N   . CYS A 1 160 ? 10.838  -10.813 17.083 1.00 21.08 ? 160 CYS B N   1 
ATOM   1231 C CA  . CYS A 1 160 ? 10.703  -11.950 17.980 1.00 19.92 ? 160 CYS B CA  1 
ATOM   1232 C C   . CYS A 1 160 ? 9.306   -12.117 18.566 1.00 18.76 ? 160 CYS B C   1 
ATOM   1233 O O   . CYS A 1 160 ? 9.019   -13.187 19.127 1.00 20.63 ? 160 CYS B O   1 
ATOM   1234 C CB  . CYS A 1 160 ? 11.728  -11.858 19.122 1.00 20.71 ? 160 CYS B CB  1 
ATOM   1235 S SG  . CYS A 1 160 ? 11.543  -10.409 20.223 1.00 22.26 ? 160 CYS B SG  1 
ATOM   1236 N N   . TYR A 1 161 ? 8.421   -11.130 18.431 1.00 15.67 ? 161 TYR B N   1 
ATOM   1237 C CA  . TYR A 1 161 ? 7.133   -11.223 19.113 1.00 19.57 ? 161 TYR B CA  1 
ATOM   1238 C C   . TYR A 1 161 ? 6.041   -10.576 18.276 1.00 19.26 ? 161 TYR B C   1 
ATOM   1239 O O   . TYR A 1 161 ? 6.259   -9.541  17.640 1.00 18.25 ? 161 TYR B O   1 
ATOM   1240 C CB  . TYR A 1 161 ? 7.209   -10.575 20.514 1.00 17.58 ? 161 TYR B CB  1 
ATOM   1241 C CG  . TYR A 1 161 ? 5.907   -10.547 21.307 1.00 16.97 ? 161 TYR B CG  1 
ATOM   1242 C CD1 . TYR A 1 161 ? 5.530   -11.637 22.091 1.00 18.96 ? 161 TYR B CD1 1 
ATOM   1243 C CD2 . TYR A 1 161 ? 5.088   -9.416  21.305 1.00 16.88 ? 161 TYR B CD2 1 
ATOM   1244 C CE1 . TYR A 1 161 ? 4.363   -11.612 22.828 1.00 17.48 ? 161 TYR B CE1 1 
ATOM   1245 C CE2 . TYR A 1 161 ? 3.922   -9.377  22.043 1.00 18.50 ? 161 TYR B CE2 1 
ATOM   1246 C CZ  . TYR A 1 161 ? 3.565   -10.485 22.801 1.00 17.49 ? 161 TYR B CZ  1 
ATOM   1247 O OH  . TYR A 1 161 ? 2.403   -10.466 23.539 1.00 17.42 ? 161 TYR B OH  1 
ATOM   1248 N N   . MET A 1 162 ? 4.863   -11.205 18.255 1.00 17.07 ? 162 MET B N   1 
ATOM   1249 C CA  . MET A 1 162 ? 3.673   -10.565 17.702 1.00 19.19 ? 162 MET B CA  1 
ATOM   1250 C C   . MET A 1 162 ? 2.561   -10.717 18.720 1.00 21.13 ? 162 MET B C   1 
ATOM   1251 O O   . MET A 1 162 ? 2.352   -11.814 19.244 1.00 18.84 ? 162 MET B O   1 
ATOM   1252 C CB  . MET A 1 162 ? 3.247   -11.164 16.349 1.00 17.31 ? 162 MET B CB  1 
ATOM   1253 C CG  . MET A 1 162 ? 1.950   -10.534 15.805 1.00 17.42 ? 162 MET B CG  1 
ATOM   1254 S SD  . MET A 1 162 ? 1.568   -10.971 14.094 1.00 27.79 ? 162 MET B SD  1 
ATOM   1255 C CE  . MET A 1 162 ? 2.704   -9.859  13.235 1.00 24.85 ? 162 MET B CE  1 
ATOM   1256 N N   . HIS A 1 163 ? 1.859   -9.621  19.008 1.00 17.76 ? 163 HIS B N   1 
ATOM   1257 C CA  . HIS A 1 163 ? 0.921   -9.615  20.125 1.00 17.58 ? 163 HIS B CA  1 
ATOM   1258 C C   . HIS A 1 163 ? -0.414  -10.267 19.774 1.00 18.08 ? 163 HIS B C   1 
ATOM   1259 O O   . HIS A 1 163 ? -0.998  -10.009 18.716 1.00 19.06 ? 163 HIS B O   1 
ATOM   1260 C CB  . HIS A 1 163 ? 0.681   -8.189  20.615 1.00 18.83 ? 163 HIS B CB  1 
ATOM   1261 C CG  . HIS A 1 163 ? -0.233  -8.138  21.793 1.00 19.73 ? 163 HIS B CG  1 
ATOM   1262 N ND1 . HIS A 1 163 ? 0.048   -8.812  22.962 1.00 19.25 ? 163 HIS B ND1 1 
ATOM   1263 C CD2 . HIS A 1 163 ? -1.447  -7.567  21.967 1.00 20.37 ? 163 HIS B CD2 1 
ATOM   1264 C CE1 . HIS A 1 163 ? -0.937  -8.624  23.822 1.00 17.87 ? 163 HIS B CE1 1 
ATOM   1265 N NE2 . HIS A 1 163 ? -1.859  -7.880  23.242 1.00 17.27 ? 163 HIS B NE2 1 
ATOM   1266 N N   . HIS A 1 164 ? -0.916  -11.095 20.698 1.00 19.37 ? 164 HIS B N   1 
ATOM   1267 C CA  . HIS A 1 164 ? -2.169  -11.820 20.489 1.00 17.66 ? 164 HIS B CA  1 
ATOM   1268 C C   . HIS A 1 164 ? -3.211  -11.653 21.593 1.00 19.88 ? 164 HIS B C   1 
ATOM   1269 O O   . HIS A 1 164 ? -4.412  -11.674 21.299 1.00 21.80 ? 164 HIS B O   1 
ATOM   1270 C CB  . HIS A 1 164 ? -1.909  -13.320 20.329 1.00 19.83 ? 164 HIS B CB  1 
ATOM   1271 C CG  . HIS A 1 164 ? -1.487  -13.718 18.951 1.00 22.43 ? 164 HIS B CG  1 
ATOM   1272 N ND1 . HIS A 1 164 ? -0.263  -13.371 18.419 1.00 21.21 ? 164 HIS B ND1 1 
ATOM   1273 C CD2 . HIS A 1 164 ? -2.118  -14.452 18.005 1.00 18.88 ? 164 HIS B CD2 1 
ATOM   1274 C CE1 . HIS A 1 164 ? -0.166  -13.864 17.195 1.00 22.21 ? 164 HIS B CE1 1 
ATOM   1275 N NE2 . HIS A 1 164 ? -1.278  -14.526 16.922 1.00 23.02 ? 164 HIS B NE2 1 
ATOM   1276 N N   . MET A 1 165 ? -2.803  -11.536 22.857 1.00 19.72 ? 165 MET B N   1 
ATOM   1277 C CA  . MET A 1 165 ? -3.817  -11.691 23.893 1.00 21.93 ? 165 MET B CA  1 
ATOM   1278 C C   . MET A 1 165 ? -3.370  -11.130 25.241 1.00 22.71 ? 165 MET B C   1 
ATOM   1279 O O   . MET A 1 165 ? -2.178  -10.927 25.503 1.00 20.92 ? 165 MET B O   1 
ATOM   1280 C CB  . MET A 1 165 ? -4.211  -13.169 24.036 1.00 22.39 ? 165 MET B CB  1 
ATOM   1281 C CG  . MET A 1 165 ? -3.212  -13.999 24.783 1.00 25.45 ? 165 MET B CG  1 
ATOM   1282 S SD  . MET A 1 165 ? -3.743  -15.727 24.794 1.00 34.71 ? 165 MET B SD  1 
ATOM   1283 C CE  . MET A 1 165 ? -4.224  -15.862 26.503 1.00 31.91 ? 165 MET B CE  1 
ATOM   1284 N N   . GLU A 1 166 ? -4.365  -10.886 26.097 1.00 19.50 ? 166 GLU B N   1 
ATOM   1285 C CA  . GLU A 1 166 ? -4.164  -10.449 27.474 1.00 21.77 ? 166 GLU B CA  1 
ATOM   1286 C C   . GLU A 1 166 ? -4.676  -11.515 28.436 1.00 22.46 ? 166 GLU B C   1 
ATOM   1287 O O   . GLU A 1 166 ? -5.627  -12.238 28.132 1.00 23.24 ? 166 GLU B O   1 
ATOM   1288 C CB  . GLU A 1 166 ? -4.878  -9.121  27.761 1.00 24.40 ? 166 GLU B CB  1 
ATOM   1289 C CG  . GLU A 1 166 ? -6.333  -9.048  27.250 1.00 24.84 ? 166 GLU B CG  1 
ATOM   1290 C CD  . GLU A 1 166 ? -7.146  -7.903  27.872 1.00 31.80 ? 166 GLU B CD  1 
ATOM   1291 O OE1 . GLU A 1 166 ? -8.386  -7.872  27.684 1.00 32.49 ? 166 GLU B OE1 1 
ATOM   1292 O OE2 . GLU A 1 166 ? -6.541  -7.029  28.539 1.00 30.72 ? 166 GLU B OE2 1 
ATOM   1293 N N   . LEU A 1 167 ? -4.076  -11.563 29.622 1.00 21.77 ? 167 LEU B N   1 
ATOM   1294 C CA  . LEU A 1 167 ? -4.358  -12.582 30.620 1.00 28.33 ? 167 LEU B CA  1 
ATOM   1295 C C   . LEU A 1 167 ? -4.895  -11.958 31.905 1.00 28.56 ? 167 LEU B C   1 
ATOM   1296 O O   . LEU A 1 167 ? -4.707  -10.759 32.155 1.00 27.31 ? 167 LEU B O   1 
ATOM   1297 C CB  . LEU A 1 167 ? -3.095  -13.404 30.920 1.00 25.95 ? 167 LEU B CB  1 
ATOM   1298 C CG  . LEU A 1 167 ? -2.705  -14.394 29.819 1.00 28.45 ? 167 LEU B CG  1 
ATOM   1299 C CD1 . LEU A 1 167 ? -1.207  -14.619 29.792 1.00 24.28 ? 167 LEU B CD1 1 
ATOM   1300 C CD2 . LEU A 1 167 ? -3.431  -15.713 30.006 1.00 32.85 ? 167 LEU B CD2 1 
ATOM   1301 N N   . PRO A 1 168 ? -5.583  -12.756 32.749 1.00 36.23 ? 168 PRO B N   1 
ATOM   1302 C CA  . PRO A 1 168 ? -6.196  -12.208 33.967 1.00 36.88 ? 168 PRO B CA  1 
ATOM   1303 C C   . PRO A 1 168 ? -5.204  -12.004 35.099 1.00 44.91 ? 168 PRO B C   1 
ATOM   1304 O O   . PRO A 1 168 ? -5.513  -12.317 36.256 1.00 51.03 ? 168 PRO B O   1 
ATOM   1305 C CB  . PRO A 1 168 ? -7.240  -13.268 34.351 1.00 40.30 ? 168 PRO B CB  1 
ATOM   1306 C CG  . PRO A 1 168 ? -7.277  -14.255 33.216 1.00 45.67 ? 168 PRO B CG  1 
ATOM   1307 C CD  . PRO A 1 168 ? -5.947  -14.167 32.552 1.00 41.62 ? 168 PRO B CD  1 
ATOM   1308 N N   . SER A 1 169 ? -3.999  -11.527 34.784 1.00 36.81 ? 169 SER B N   1 
ATOM   1309 C CA  . SER A 1 169 ? -3.143  -10.913 35.789 1.00 35.70 ? 169 SER B CA  1 
ATOM   1310 C C   . SER A 1 169 ? -2.621  -9.574  35.302 1.00 30.86 ? 169 SER B C   1 
ATOM   1311 O O   . SER A 1 169 ? -1.791  -8.969  35.982 1.00 36.06 ? 169 SER B O   1 
ATOM   1312 C CB  . SER A 1 169 ? -1.951  -11.801 36.178 1.00 32.82 ? 169 SER B CB  1 
ATOM   1313 O OG  . SER A 1 169 ? -1.451  -12.539 35.078 1.00 31.52 ? 169 SER B OG  1 
ATOM   1314 N N   . GLY A 1 170 ? -3.082  -9.104  34.147 1.00 29.44 ? 170 GLY B N   1 
ATOM   1315 C CA  . GLY A 1 170 ? -2.597  -7.868  33.572 1.00 28.90 ? 170 GLY B CA  1 
ATOM   1316 C C   . GLY A 1 170 ? -1.384  -8.008  32.678 1.00 25.56 ? 170 GLY B C   1 
ATOM   1317 O O   . GLY A 1 170 ? -0.785  -6.988  32.312 1.00 26.30 ? 170 GLY B O   1 
ATOM   1318 N N   . VAL A 1 171 ? -1.005  -9.231  32.320 1.00 22.72 ? 171 VAL B N   1 
ATOM   1319 C CA  . VAL A 1 171 ? 0.149   -9.488  31.461 1.00 20.55 ? 171 VAL B CA  1 
ATOM   1320 C C   . VAL A 1 171 ? -0.330  -10.002 30.104 1.00 19.67 ? 171 VAL B C   1 
ATOM   1321 O O   . VAL A 1 171 ? -1.533  -10.111 29.856 1.00 20.69 ? 171 VAL B O   1 
ATOM   1322 C CB  . VAL A 1 171 ? 1.123   -10.485 32.118 1.00 25.15 ? 171 VAL B CB  1 
ATOM   1323 C CG1 . VAL A 1 171 ? 1.552   -9.971  33.497 1.00 27.17 ? 171 VAL B CG1 1 
ATOM   1324 C CG2 . VAL A 1 171 ? 0.507   -11.889 32.198 1.00 21.64 ? 171 VAL B CG2 1 
ATOM   1325 N N   . HIS A 1 172 ? 0.605   -10.314 29.211 1.00 19.00 ? 172 HIS B N   1 
ATOM   1326 C CA  . HIS A 1 172 ? 0.285   -10.478 27.801 1.00 15.94 ? 172 HIS B CA  1 
ATOM   1327 C C   . HIS A 1 172 ? 1.027   -11.675 27.228 1.00 17.14 ? 172 HIS B C   1 
ATOM   1328 O O   . HIS A 1 172 ? 2.068   -12.089 27.739 1.00 18.08 ? 172 HIS B O   1 
ATOM   1329 C CB  . HIS A 1 172 ? 0.621   -9.198  27.028 1.00 18.49 ? 172 HIS B CB  1 
ATOM   1330 C CG  . HIS A 1 172 ? -0.079  -8.001  27.578 1.00 19.01 ? 172 HIS B CG  1 
ATOM   1331 N ND1 . HIS A 1 172 ? 0.519   -7.118  28.457 1.00 17.33 ? 172 HIS B ND1 1 
ATOM   1332 C CD2 . HIS A 1 172 ? -1.366  -7.602  27.456 1.00 19.80 ? 172 HIS B CD2 1 
ATOM   1333 C CE1 . HIS A 1 172 ? -0.360  -6.192  28.802 1.00 19.10 ? 172 HIS B CE1 1 
ATOM   1334 N NE2 . HIS A 1 172 ? -1.515  -6.469  28.218 1.00 21.46 ? 172 HIS B NE2 1 
ATOM   1335 N N   . ALA A 1 173 ? 0.471   -12.222 26.147 1.00 16.98 ? 173 ALA B N   1 
ATOM   1336 C CA  . ALA A 1 173 ? 1.032   -13.390 25.487 1.00 16.05 ? 173 ALA B CA  1 
ATOM   1337 C C   . ALA A 1 173 ? 0.916   -13.242 23.981 1.00 17.06 ? 173 ALA B C   1 
ATOM   1338 O O   . ALA A 1 173 ? -0.015  -12.621 23.469 1.00 18.30 ? 173 ALA B O   1 
ATOM   1339 C CB  . ALA A 1 173 ? 0.322   -14.680 25.937 1.00 20.87 ? 173 ALA B CB  1 
ATOM   1340 N N   . GLY A 1 174 ? 1.850   -13.856 23.271 1.00 16.86 ? 174 GLY B N   1 
ATOM   1341 C CA  . GLY A 1 174 ? 1.828   -13.768 21.827 1.00 18.84 ? 174 GLY B CA  1 
ATOM   1342 C C   . GLY A 1 174 ? 2.736   -14.813 21.236 1.00 18.04 ? 174 GLY B C   1 
ATOM   1343 O O   . GLY A 1 174 ? 3.158   -15.745 21.921 1.00 20.52 ? 174 GLY B O   1 
ATOM   1344 N N   . THR A 1 175 ? 3.038   -14.640 19.951 1.00 18.08 ? 175 THR B N   1 
ATOM   1345 C CA  . THR A 1 175 ? 3.777   -15.639 19.186 1.00 18.99 ? 175 THR B CA  1 
ATOM   1346 C C   . THR A 1 175 ? 5.111   -15.097 18.699 1.00 17.28 ? 175 THR B C   1 
ATOM   1347 O O   . THR A 1 175 ? 5.403   -13.900 18.781 1.00 18.42 ? 175 THR B O   1 
ATOM   1348 C CB  . THR A 1 175 ? 2.965   -16.117 17.975 1.00 18.30 ? 175 THR B CB  1 
ATOM   1349 O OG1 . THR A 1 175 ? 2.790   -15.024 17.058 1.00 17.70 ? 175 THR B OG1 1 
ATOM   1350 C CG2 . THR A 1 175 ? 1.604   -16.640 18.418 1.00 21.87 ? 175 THR B CG2 1 
ATOM   1351 N N   . ASP A 1 176 ? 5.938   -16.004 18.178 1.00 16.97 ? 176 ASP B N   1 
ATOM   1352 C CA  . ASP A 1 176 ? 7.039   -15.545 17.348 1.00 19.73 ? 176 ASP B CA  1 
ATOM   1353 C C   . ASP A 1 176 ? 6.481   -15.256 15.950 1.00 19.87 ? 176 ASP B C   1 
ATOM   1354 O O   . ASP A 1 176 ? 5.282   -15.419 15.694 1.00 21.18 ? 176 ASP B O   1 
ATOM   1355 C CB  . ASP A 1 176 ? 8.185   -16.562 17.369 1.00 21.25 ? 176 ASP B CB  1 
ATOM   1356 C CG  . ASP A 1 176 ? 7.803   -17.924 16.798 1.00 24.47 ? 176 ASP B CG  1 
ATOM   1357 O OD1 . ASP A 1 176 ? 6.849   -18.030 16.005 1.00 24.48 ? 176 ASP B OD1 1 
ATOM   1358 O OD2 . ASP A 1 176 ? 8.505   -18.900 17.125 1.00 24.49 ? 176 ASP B OD2 1 
ATOM   1359 N N   . LEU A 1 177 ? 7.327   -14.821 15.024 1.00 20.38 ? 177 LEU B N   1 
ATOM   1360 C CA  . LEU A 1 177 ? 6.789   -14.460 13.715 1.00 19.96 ? 177 LEU B CA  1 
ATOM   1361 C C   . LEU A 1 177 ? 6.578   -15.669 12.811 1.00 23.01 ? 177 LEU B C   1 
ATOM   1362 O O   . LEU A 1 177 ? 6.092   -15.506 11.688 1.00 27.39 ? 177 LEU B O   1 
ATOM   1363 C CB  . LEU A 1 177 ? 7.684   -13.420 13.024 1.00 20.19 ? 177 LEU B CB  1 
ATOM   1364 C CG  . LEU A 1 177 ? 7.328   -11.944 13.223 1.00 21.14 ? 177 LEU B CG  1 
ATOM   1365 C CD1 . LEU A 1 177 ? 6.056   -11.593 12.472 1.00 24.69 ? 177 LEU B CD1 1 
ATOM   1366 C CD2 . LEU A 1 177 ? 7.160   -11.602 14.691 1.00 24.61 ? 177 LEU B CD2 1 
ATOM   1367 N N   . GLU A 1 178 ? 6.926   -16.868 13.262 1.00 22.54 ? 178 GLU B N   1 
ATOM   1368 C CA  . GLU A 1 178 ? 6.463   -18.085 12.611 1.00 25.01 ? 178 GLU B CA  1 
ATOM   1369 C C   . GLU A 1 178 ? 5.123   -18.545 13.163 1.00 24.63 ? 178 GLU B C   1 
ATOM   1370 O O   . GLU A 1 178 ? 4.647   -19.625 12.797 1.00 26.96 ? 178 GLU B O   1 
ATOM   1371 C CB  . GLU A 1 178 ? 7.500   -19.195 12.757 1.00 25.62 ? 178 GLU B CB  1 
ATOM   1372 C CG  . GLU A 1 178 ? 8.682   -19.041 11.829 1.00 27.00 ? 178 GLU B CG  1 
ATOM   1373 C CD  . GLU A 1 178 ? 9.577   -20.255 11.885 1.00 36.97 ? 178 GLU B CD  1 
ATOM   1374 O OE1 . GLU A 1 178 ? 9.934   -20.791 10.811 1.00 40.63 ? 178 GLU B OE1 1 
ATOM   1375 O OE2 . GLU A 1 178 ? 9.897   -20.688 13.013 1.00 36.03 ? 178 GLU B OE2 1 
ATOM   1376 N N   . GLY A 1 179 ? 4.508   -17.753 14.040 1.00 21.38 ? 179 GLY B N   1 
ATOM   1377 C CA  . GLY A 1 179 ? 3.168   -18.050 14.508 1.00 23.21 ? 179 GLY B CA  1 
ATOM   1378 C C   . GLY A 1 179 ? 3.074   -19.014 15.667 1.00 22.70 ? 179 GLY B C   1 
ATOM   1379 O O   . GLY A 1 179 ? 1.959   -19.416 16.022 1.00 23.14 ? 179 GLY B O   1 
ATOM   1380 N N   . ASN A 1 180 ? 4.192   -19.384 16.281 1.00 20.95 ? 180 ASN B N   1 
ATOM   1381 C CA  . ASN A 1 180 ? 4.187   -20.293 17.421 1.00 23.77 ? 180 ASN B CA  1 
ATOM   1382 C C   . ASN A 1 180 ? 4.142   -19.488 18.705 1.00 22.82 ? 180 ASN B C   1 
ATOM   1383 O O   . ASN A 1 180 ? 5.021   -18.656 18.940 1.00 23.72 ? 180 ASN B O   1 
ATOM   1384 C CB  . ASN A 1 180 ? 5.415   -21.193 17.417 1.00 24.12 ? 180 ASN B CB  1 
ATOM   1385 C CG  . ASN A 1 180 ? 5.415   -22.145 16.253 1.00 31.37 ? 180 ASN B CG  1 
ATOM   1386 O OD1 . ASN A 1 180 ? 4.442   -22.863 16.046 1.00 33.49 ? 180 ASN B OD1 1 
ATOM   1387 N ND2 . ASN A 1 180 ? 6.497   -22.155 15.485 1.00 29.42 ? 180 ASN B ND2 1 
ATOM   1388 N N   . PHE A 1 181 ? 3.127   -19.750 19.528 1.00 23.49 ? 181 PHE B N   1 
ATOM   1389 C CA  . PHE A 1 181 ? 2.996   -19.073 20.812 1.00 23.79 ? 181 PHE B CA  1 
ATOM   1390 C C   . PHE A 1 181 ? 4.224   -19.311 21.683 1.00 23.01 ? 181 PHE B C   1 
ATOM   1391 O O   . PHE A 1 181 ? 4.800   -20.406 21.708 1.00 23.51 ? 181 PHE B O   1 
ATOM   1392 C CB  . PHE A 1 181 ? 1.739   -19.552 21.560 1.00 23.82 ? 181 PHE B CB  1 
ATOM   1393 C CG  . PHE A 1 181 ? 0.546   -18.644 21.381 1.00 23.16 ? 181 PHE B CG  1 
ATOM   1394 C CD1 . PHE A 1 181 ? 0.403   -17.489 22.142 1.00 21.64 ? 181 PHE B CD1 1 
ATOM   1395 C CD2 . PHE A 1 181 ? -0.406  -18.928 20.419 1.00 21.85 ? 181 PHE B CD2 1 
ATOM   1396 C CE1 . PHE A 1 181 ? -0.683  -16.646 21.956 1.00 22.90 ? 181 PHE B CE1 1 
ATOM   1397 C CE2 . PHE A 1 181 ? -1.494  -18.096 20.217 1.00 24.11 ? 181 PHE B CE2 1 
ATOM   1398 C CZ  . PHE A 1 181 ? -1.644  -16.953 20.994 1.00 21.36 ? 181 PHE B CZ  1 
ATOM   1399 N N   . TYR A 1 182 ? 4.632   -18.265 22.395 1.00 20.28 ? 182 TYR B N   1 
ATOM   1400 C CA  . TYR A 1 182 ? 5.449   -18.461 23.580 1.00 20.62 ? 182 TYR B CA  1 
ATOM   1401 C C   . TYR A 1 182 ? 4.549   -18.975 24.690 1.00 21.74 ? 182 TYR B C   1 
ATOM   1402 O O   . TYR A 1 182 ? 3.478   -18.414 24.933 1.00 23.69 ? 182 TYR B O   1 
ATOM   1403 C CB  . TYR A 1 182 ? 6.122   -17.154 24.004 1.00 23.40 ? 182 TYR B CB  1 
ATOM   1404 C CG  . TYR A 1 182 ? 7.153   -16.642 23.021 1.00 20.47 ? 182 TYR B CG  1 
ATOM   1405 C CD1 . TYR A 1 182 ? 8.458   -17.127 23.026 1.00 23.15 ? 182 TYR B CD1 1 
ATOM   1406 C CD2 . TYR A 1 182 ? 6.814   -15.682 22.072 1.00 18.68 ? 182 TYR B CD2 1 
ATOM   1407 C CE1 . TYR A 1 182 ? 9.405   -16.645 22.126 1.00 22.90 ? 182 TYR B CE1 1 
ATOM   1408 C CE2 . TYR A 1 182 ? 7.746   -15.208 21.157 1.00 19.09 ? 182 TYR B CE2 1 
ATOM   1409 C CZ  . TYR A 1 182 ? 9.030   -15.693 21.183 1.00 18.78 ? 182 TYR B CZ  1 
ATOM   1410 O OH  . TYR A 1 182 ? 9.931   -15.194 20.273 1.00 19.17 ? 182 TYR B OH  1 
ATOM   1411 N N   . GLY A 1 183 ? 4.966   -20.053 25.344 1.00 22.80 ? 183 GLY B N   1 
ATOM   1412 C CA  . GLY A 1 183 ? 4.187   -20.611 26.419 1.00 25.78 ? 183 GLY B CA  1 
ATOM   1413 C C   . GLY A 1 183 ? 3.078   -21.506 25.920 1.00 26.73 ? 183 GLY B C   1 
ATOM   1414 O O   . GLY A 1 183 ? 2.981   -21.806 24.724 1.00 28.52 ? 183 GLY B O   1 
ATOM   1415 N N   . PRO A 1 184 ? 2.217   -21.945 26.837 1.00 24.82 ? 184 PRO B N   1 
ATOM   1416 C CA  . PRO A 1 184 ? 1.189   -22.939 26.490 1.00 27.25 ? 184 PRO B CA  1 
ATOM   1417 C C   . PRO A 1 184 ? -0.131  -22.340 26.021 1.00 32.46 ? 184 PRO B C   1 
ATOM   1418 O O   . PRO A 1 184 ? -1.166  -23.015 26.054 1.00 30.48 ? 184 PRO B O   1 
ATOM   1419 C CB  . PRO A 1 184 ? 1.007   -23.697 27.810 1.00 29.90 ? 184 PRO B CB  1 
ATOM   1420 C CG  . PRO A 1 184 ? 1.230   -22.623 28.844 1.00 29.67 ? 184 PRO B CG  1 
ATOM   1421 C CD  . PRO A 1 184 ? 2.378   -21.809 28.296 1.00 27.58 ? 184 PRO B CD  1 
ATOM   1422 N N   . PHE A 1 185 ? -0.112  -21.094 25.563 1.00 27.73 ? 185 PHE B N   1 
ATOM   1423 C CA  . PHE A 1 185 ? -1.338  -20.367 25.279 1.00 27.16 ? 185 PHE B CA  1 
ATOM   1424 C C   . PHE A 1 185 ? -1.867  -20.696 23.881 1.00 25.74 ? 185 PHE B C   1 
ATOM   1425 O O   . PHE A 1 185 ? -1.145  -21.197 23.013 1.00 26.95 ? 185 PHE B O   1 
ATOM   1426 C CB  . PHE A 1 185 ? -1.082  -18.867 25.467 1.00 26.20 ? 185 PHE B CB  1 
ATOM   1427 C CG  . PHE A 1 185 ? -0.428  -18.550 26.790 1.00 27.03 ? 185 PHE B CG  1 
ATOM   1428 C CD1 . PHE A 1 185 ? -1.142  -18.698 27.971 1.00 29.08 ? 185 PHE B CD1 1 
ATOM   1429 C CD2 . PHE A 1 185 ? 0.906   -18.155 26.860 1.00 24.61 ? 185 PHE B CD2 1 
ATOM   1430 C CE1 . PHE A 1 185 ? -0.558  -18.435 29.196 1.00 26.49 ? 185 PHE B CE1 1 
ATOM   1431 C CE2 . PHE A 1 185 ? 1.504   -17.899 28.084 1.00 22.37 ? 185 PHE B CE2 1 
ATOM   1432 C CZ  . PHE A 1 185 ? 0.769   -18.035 29.257 1.00 25.96 ? 185 PHE B CZ  1 
ATOM   1433 N N   . VAL A 1 186 ? -3.164  -20.445 23.684 1.00 25.29 ? 186 VAL B N   1 
ATOM   1434 C CA  . VAL A 1 186 ? -3.850  -20.782 22.440 1.00 25.96 ? 186 VAL B CA  1 
ATOM   1435 C C   . VAL A 1 186 ? -4.688  -19.591 21.993 1.00 25.04 ? 186 VAL B C   1 
ATOM   1436 O O   . VAL A 1 186 ? -5.171  -18.809 22.819 1.00 27.00 ? 186 VAL B O   1 
ATOM   1437 C CB  . VAL A 1 186 ? -4.730  -22.047 22.599 1.00 25.60 ? 186 VAL B CB  1 
ATOM   1438 C CG1 . VAL A 1 186 ? -3.853  -23.275 22.747 1.00 29.58 ? 186 VAL B CG1 1 
ATOM   1439 C CG2 . VAL A 1 186 ? -5.676  -21.906 23.795 1.00 29.92 ? 186 VAL B CG2 1 
ATOM   1440 N N   . ASP A 1 187 ? -4.872  -19.451 20.673 1.00 24.39 ? 187 ASP B N   1 
ATOM   1441 C CA  . ASP A 1 187 ? -5.574  -18.272 20.154 1.00 28.90 ? 187 ASP B CA  1 
ATOM   1442 C C   . ASP A 1 187 ? -7.061  -18.584 19.981 1.00 26.61 ? 187 ASP B C   1 
ATOM   1443 O O   . ASP A 1 187 ? -7.612  -18.674 18.882 1.00 27.11 ? 187 ASP B O   1 
ATOM   1444 C CB  . ASP A 1 187 ? -4.949  -17.750 18.863 1.00 24.99 ? 187 ASP B CB  1 
ATOM   1445 C CG  . ASP A 1 187 ? -4.865  -18.780 17.743 1.00 27.81 ? 187 ASP B CG  1 
ATOM   1446 O OD1 . ASP A 1 187 ? -5.031  -20.003 17.964 1.00 25.68 ? 187 ASP B OD1 1 
ATOM   1447 O OD2 . ASP A 1 187 ? -4.636  -18.324 16.599 1.00 24.88 ? 187 ASP B OD2 1 
ATOM   1448 N N   . ARG A 1 188 ? -7.720  -18.704 21.124 1.00 27.32 ? 188 ARG B N   1 
ATOM   1449 C CA  . ARG A 1 188 ? -9.162  -18.843 21.153 1.00 32.27 ? 188 ARG B CA  1 
ATOM   1450 C C   . ARG A 1 188 ? -9.653  -18.293 22.479 1.00 33.70 ? 188 ARG B C   1 
ATOM   1451 O O   . ARG A 1 188 ? -8.871  -18.076 23.410 1.00 30.82 ? 188 ARG B O   1 
ATOM   1452 C CB  . ARG A 1 188 ? -9.574  -20.301 20.908 1.00 31.85 ? 188 ARG B CB  1 
ATOM   1453 C CG  . ARG A 1 188 ? -9.416  -21.239 22.090 1.00 34.32 ? 188 ARG B CG  1 
ATOM   1454 C CD  . ARG A 1 188 ? -9.518  -22.689 21.617 1.00 36.21 ? 188 ARG B CD  1 
ATOM   1455 N NE  . ARG A 1 188 ? -9.012  -23.630 22.609 1.00 37.89 ? 188 ARG B NE  1 
ATOM   1456 C CZ  . ARG A 1 188 ? -7.986  -24.449 22.414 1.00 37.18 ? 188 ARG B CZ  1 
ATOM   1457 N NH1 . ARG A 1 188 ? -7.298  -24.442 21.282 1.00 38.73 ? 188 ARG B NH1 1 
ATOM   1458 N NH2 . ARG A 1 188 ? -7.631  -25.287 23.385 1.00 38.85 ? 188 ARG B NH2 1 
ATOM   1459 N N   . GLN A 1 189 ? -10.954 -18.034 22.540 1.00 35.88 ? 189 GLN B N   1 
ATOM   1460 C CA  . GLN A 1 189 ? -11.568 -17.428 23.718 1.00 37.50 ? 189 GLN B CA  1 
ATOM   1461 C C   . GLN A 1 189 ? -11.868 -18.543 24.709 1.00 38.78 ? 189 GLN B C   1 
ATOM   1462 O O   . GLN A 1 189 ? -12.941 -19.151 24.701 1.00 40.56 ? 189 GLN B O   1 
ATOM   1463 C CB  . GLN A 1 189 ? -12.815 -16.647 23.330 1.00 37.49 ? 189 GLN B CB  1 
ATOM   1464 C CG  . GLN A 1 189 ? -13.444 -15.857 24.468 1.00 40.41 ? 189 GLN B CG  1 
ATOM   1465 C CD  . GLN A 1 189 ? -14.629 -15.044 23.992 1.00 44.18 ? 189 GLN B CD  1 
ATOM   1466 O OE1 . GLN A 1 189 ? -14.864 -13.934 24.468 1.00 50.91 ? 189 GLN B OE1 1 
ATOM   1467 N NE2 . GLN A 1 189 ? -15.377 -15.588 23.031 1.00 45.74 ? 189 GLN B NE2 1 
ATOM   1468 N N   . THR A 1 190 ? -10.878 -18.834 25.549 1.00 36.49 ? 190 THR B N   1 
ATOM   1469 C CA  . THR A 1 190 ? -10.987 -19.807 26.619 1.00 36.70 ? 190 THR B CA  1 
ATOM   1470 C C   . THR A 1 190 ? -10.279 -19.250 27.846 1.00 37.82 ? 190 THR B C   1 
ATOM   1471 O O   . THR A 1 190 ? -9.475  -18.318 27.752 1.00 39.30 ? 190 THR B O   1 
ATOM   1472 C CB  . THR A 1 190 ? -10.384 -21.156 26.214 1.00 39.13 ? 190 THR B CB  1 
ATOM   1473 O OG1 . THR A 1 190 ? -10.906 -22.186 27.054 1.00 43.78 ? 190 THR B OG1 1 
ATOM   1474 C CG2 . THR A 1 190 ? -8.869  -21.123 26.338 1.00 35.66 ? 190 THR B CG2 1 
ATOM   1475 N N   . ALA A 1 191 ? -10.589 -19.827 29.003 1.00 37.98 ? 191 ALA B N   1 
ATOM   1476 C CA  . ALA A 1 191 ? -9.958  -19.403 30.249 1.00 40.06 ? 191 ALA B CA  1 
ATOM   1477 C C   . ALA A 1 191 ? -8.484  -19.784 30.238 1.00 40.34 ? 191 ALA B C   1 
ATOM   1478 O O   . ALA A 1 191 ? -8.143  -20.965 30.111 1.00 38.70 ? 191 ALA B O   1 
ATOM   1479 C CB  . ALA A 1 191 ? -10.665 -20.035 31.446 1.00 39.80 ? 191 ALA B CB  1 
ATOM   1480 N N   . GLN A 1 192 ? -7.608  -18.788 30.371 1.00 33.42 ? 192 GLN B N   1 
ATOM   1481 C CA  . GLN A 1 192 ? -6.172  -19.031 30.356 1.00 35.58 ? 192 GLN B CA  1 
ATOM   1482 C C   . GLN A 1 192 ? -5.519  -18.248 31.482 1.00 31.49 ? 192 GLN B C   1 
ATOM   1483 O O   . GLN A 1 192 ? -5.985  -17.168 31.850 1.00 32.65 ? 192 GLN B O   1 
ATOM   1484 C CB  . GLN A 1 192 ? -5.567  -18.650 28.998 1.00 35.42 ? 192 GLN B CB  1 
ATOM   1485 C CG  . GLN A 1 192 ? -6.104  -19.503 27.874 1.00 34.04 ? 192 GLN B CG  1 
ATOM   1486 C CD  . GLN A 1 192 ? -5.430  -19.260 26.545 1.00 29.16 ? 192 GLN B CD  1 
ATOM   1487 O OE1 . GLN A 1 192 ? -4.339  -19.754 26.298 1.00 28.81 ? 192 GLN B OE1 1 
ATOM   1488 N NE2 . GLN A 1 192 ? -6.110  -18.547 25.658 1.00 31.87 ? 192 GLN B NE2 1 
ATOM   1489 N N   . ALA A 1 193 ? -4.435  -18.803 32.032 1.00 34.18 ? 193 ALA B N   1 
ATOM   1490 C CA  . ALA A 1 193 ? -3.762  -18.204 33.177 1.00 30.63 ? 193 ALA B CA  1 
ATOM   1491 C C   . ALA A 1 193 ? -2.251  -18.324 33.037 1.00 28.59 ? 193 ALA B C   1 
ATOM   1492 O O   . ALA A 1 193 ? -1.739  -19.343 32.568 1.00 34.37 ? 193 ALA B O   1 
ATOM   1493 C CB  . ALA A 1 193 ? -4.198  -18.857 34.496 1.00 35.68 ? 193 ALA B CB  1 
ATOM   1494 N N   . ALA A 1 194 ? -1.547  -17.281 33.464 1.00 30.91 ? 194 ALA B N   1 
ATOM   1495 C CA  . ALA A 1 194 ? -0.092  -17.329 33.521 1.00 28.55 ? 194 ALA B CA  1 
ATOM   1496 C C   . ALA A 1 194 ? 0.351   -18.262 34.638 1.00 30.40 ? 194 ALA B C   1 
ATOM   1497 O O   . ALA A 1 194 ? -0.192  -18.220 35.748 1.00 32.75 ? 194 ALA B O   1 
ATOM   1498 C CB  . ALA A 1 194 ? 0.475   -15.929 33.749 1.00 29.78 ? 194 ALA B CB  1 
ATOM   1499 N N   . GLY A 1 195 ? 1.315   -19.121 34.337 1.00 27.18 ? 195 GLY B N   1 
ATOM   1500 C CA  . GLY A 1 195 ? 1.930   -19.939 35.361 1.00 33.30 ? 195 GLY B CA  1 
ATOM   1501 C C   . GLY A 1 195 ? 2.667   -19.104 36.393 1.00 31.49 ? 195 GLY B C   1 
ATOM   1502 O O   . GLY A 1 195 ? 2.815   -17.883 36.294 1.00 30.57 ? 195 GLY B O   1 
ATOM   1503 N N   . THR A 1 196 ? 3.102   -19.794 37.438 1.00 30.59 ? 196 THR B N   1 
ATOM   1504 C CA  . THR A 1 196 ? 3.982   -19.180 38.413 1.00 30.75 ? 196 THR B CA  1 
ATOM   1505 C C   . THR A 1 196 ? 5.223   -18.640 37.717 1.00 33.72 ? 196 THR B C   1 
ATOM   1506 O O   . THR A 1 196 ? 5.738   -19.241 36.771 1.00 29.61 ? 196 THR B O   1 
ATOM   1507 C CB  . THR A 1 196 ? 4.381   -20.197 39.477 1.00 35.86 ? 196 THR B CB  1 
ATOM   1508 O OG1 . THR A 1 196 ? 5.187   -21.220 38.875 1.00 38.74 ? 196 THR B OG1 1 
ATOM   1509 C CG2 . THR A 1 196 ? 3.136   -20.821 40.102 1.00 32.03 ? 196 THR B CG2 1 
ATOM   1510 N N   . ASP A 1 197 ? 5.687   -17.495 38.185 1.00 30.88 ? 197 ASP B N   1 
ATOM   1511 C CA  . ASP A 1 197 ? 6.824   -16.812 37.594 1.00 33.05 ? 197 ASP B CA  1 
ATOM   1512 C C   . ASP A 1 197 ? 7.921   -16.643 38.633 1.00 35.98 ? 197 ASP B C   1 
ATOM   1513 O O   . ASP A 1 197 ? 7.643   -16.441 39.819 1.00 39.14 ? 197 ASP B O   1 
ATOM   1514 C CB  . ASP A 1 197 ? 6.406   -15.461 37.054 1.00 27.45 ? 197 ASP B CB  1 
ATOM   1515 C CG  . ASP A 1 197 ? 7.440   -14.857 36.123 1.00 26.51 ? 197 ASP B CG  1 
ATOM   1516 O OD1 . ASP A 1 197 ? 8.155   -15.618 35.424 1.00 26.17 ? 197 ASP B OD1 1 
ATOM   1517 O OD2 . ASP A 1 197 ? 7.523   -13.612 36.112 1.00 24.82 ? 197 ASP B OD2 1 
ATOM   1518 N N   . THR A 1 198 ? 9.170   -16.722 38.174 1.00 32.18 ? 198 THR B N   1 
ATOM   1519 C CA  . THR A 1 198 ? 10.344  -16.596 39.024 1.00 26.93 ? 198 THR B CA  1 
ATOM   1520 C C   . THR A 1 198 ? 11.100  -15.324 38.662 1.00 24.61 ? 198 THR B C   1 
ATOM   1521 O O   . THR A 1 198 ? 11.024  -14.847 37.529 1.00 30.77 ? 198 THR B O   1 
ATOM   1522 C CB  . THR A 1 198 ? 11.276  -17.802 38.875 1.00 30.81 ? 198 THR B CB  1 
ATOM   1523 O OG1 . THR A 1 198 ? 11.786  -17.868 37.539 1.00 35.93 ? 198 THR B OG1 1 
ATOM   1524 C CG2 . THR A 1 198 ? 10.514  -19.102 39.164 1.00 32.39 ? 198 THR B CG2 1 
ATOM   1525 N N   . THR A 1 199 ? 11.824  -14.776 39.634 1.00 20.92 ? 199 THR B N   1 
ATOM   1526 C CA  . THR A 1 199 ? 12.636  -13.584 39.393 1.00 20.10 ? 199 THR B CA  1 
ATOM   1527 C C   . THR A 1 199 ? 13.909  -13.960 38.644 1.00 21.85 ? 199 THR B C   1 
ATOM   1528 O O   . THR A 1 199 ? 14.552  -14.960 38.958 1.00 18.95 ? 199 THR B O   1 
ATOM   1529 C CB  . THR A 1 199 ? 12.978  -12.900 40.716 1.00 19.07 ? 199 THR B CB  1 
ATOM   1530 O OG1 . THR A 1 199 ? 11.757  -12.589 41.422 1.00 21.66 ? 199 THR B OG1 1 
ATOM   1531 C CG2 . THR A 1 199 ? 13.792  -11.599 40.471 1.00 21.63 ? 199 THR B CG2 1 
ATOM   1532 N N   . ILE A 1 200 ? 14.275  -13.145 37.649 1.00 19.40 ? 200 ILE B N   1 
ATOM   1533 C CA  . ILE A 1 200 ? 15.407  -13.453 36.775 1.00 17.91 ? 200 ILE B CA  1 
ATOM   1534 C C   . ILE A 1 200 ? 16.707  -12.987 37.426 1.00 18.13 ? 200 ILE B C   1 
ATOM   1535 O O   . ILE A 1 200 ? 17.154  -11.851 37.228 1.00 17.94 ? 200 ILE B O   1 
ATOM   1536 C CB  . ILE A 1 200 ? 15.199  -12.828 35.381 1.00 16.23 ? 200 ILE B CB  1 
ATOM   1537 C CG1 . ILE A 1 200 ? 13.811  -13.221 34.842 1.00 21.63 ? 200 ILE B CG1 1 
ATOM   1538 C CG2 . ILE A 1 200 ? 16.360  -13.193 34.437 1.00 19.60 ? 200 ILE B CG2 1 
ATOM   1539 C CD1 . ILE A 1 200 ? 13.349  -12.345 33.664 1.00 23.05 ? 200 ILE B CD1 1 
ATOM   1540 N N   . THR A 1 201 ? 17.307  -13.879 38.208 1.00 16.55 ? 201 THR B N   1 
ATOM   1541 C CA  . THR A 1 201 ? 18.443  -13.561 39.068 1.00 15.50 ? 201 THR B CA  1 
ATOM   1542 C C   . THR A 1 201 ? 19.603  -12.929 38.307 1.00 14.36 ? 201 THR B C   1 
ATOM   1543 O O   . THR A 1 201 ? 20.183  -11.940 38.763 1.00 16.80 ? 201 THR B O   1 
ATOM   1544 C CB  . THR A 1 201 ? 18.932  -14.836 39.755 1.00 19.26 ? 201 THR B CB  1 
ATOM   1545 O OG1 . THR A 1 201 ? 17.806  -15.514 40.336 1.00 17.50 ? 201 THR B OG1 1 
ATOM   1546 C CG2 . THR A 1 201 ? 19.953  -14.514 40.828 1.00 18.22 ? 201 THR B CG2 1 
ATOM   1547 N N   . VAL A 1 202 ? 19.969  -13.502 37.159 1.00 14.40 ? 202 VAL B N   1 
ATOM   1548 C CA  . VAL A 1 202 ? 21.115  -12.954 36.423 1.00 14.88 ? 202 VAL B CA  1 
ATOM   1549 C C   . VAL A 1 202 ? 20.862  -11.502 36.025 1.00 15.78 ? 202 VAL B C   1 
ATOM   1550 O O   . VAL A 1 202 ? 21.795  -10.682 36.009 1.00 14.49 ? 202 VAL B O   1 
ATOM   1551 C CB  . VAL A 1 202 ? 21.458  -13.849 35.210 1.00 17.48 ? 202 VAL B CB  1 
ATOM   1552 C CG1 . VAL A 1 202 ? 20.384  -13.788 34.140 1.00 21.74 ? 202 VAL B CG1 1 
ATOM   1553 C CG2 . VAL A 1 202 ? 22.824  -13.466 34.623 1.00 18.84 ? 202 VAL B CG2 1 
ATOM   1554 N N   . ASN A 1 203 ? 19.600  -11.153 35.746 1.00 15.00 ? 203 ASN B N   1 
ATOM   1555 C CA  . ASN A 1 203 ? 19.261  -9.783  35.386 1.00 16.01 ? 203 ASN B CA  1 
ATOM   1556 C C   . ASN A 1 203 ? 19.309  -8.870  36.604 1.00 16.66 ? 203 ASN B C   1 
ATOM   1557 O O   . ASN A 1 203 ? 19.716  -7.720  36.493 1.00 16.41 ? 203 ASN B O   1 
ATOM   1558 C CB  . ASN A 1 203 ? 17.876  -9.726  34.739 1.00 17.68 ? 203 ASN B CB  1 
ATOM   1559 C CG  . ASN A 1 203 ? 17.849  -10.282 33.324 1.00 15.95 ? 203 ASN B CG  1 
ATOM   1560 O OD1 . ASN A 1 203 ? 18.853  -10.789 32.803 1.00 18.40 ? 203 ASN B OD1 1 
ATOM   1561 N ND2 . ASN A 1 203 ? 16.695  -10.189 32.689 1.00 17.60 ? 203 ASN B ND2 1 
ATOM   1562 N N   . VAL A 1 204 ? 18.879  -9.354  37.772 1.00 14.56 ? 204 VAL B N   1 
ATOM   1563 C CA  . VAL A 1 204 ? 19.009  -8.538  38.977 1.00 15.08 ? 204 VAL B CA  1 
ATOM   1564 C C   . VAL A 1 204 ? 20.476  -8.209  39.226 1.00 15.00 ? 204 VAL B C   1 
ATOM   1565 O O   . VAL A 1 204 ? 20.828  -7.066  39.528 1.00 15.64 ? 204 VAL B O   1 
ATOM   1566 C CB  . VAL A 1 204 ? 18.374  -9.238  40.189 1.00 15.49 ? 204 VAL B CB  1 
ATOM   1567 C CG1 . VAL A 1 204 ? 18.565  -8.421  41.443 1.00 18.22 ? 204 VAL B CG1 1 
ATOM   1568 C CG2 . VAL A 1 204 ? 16.900  -9.498  39.947 1.00 15.24 ? 204 VAL B CG2 1 
ATOM   1569 N N   . LEU A 1 205 ? 21.351  -9.211  39.114 1.00 15.20 ? 205 LEU B N   1 
ATOM   1570 C CA  . LEU A 1 205 ? 22.781  -8.972  39.288 1.00 14.16 ? 205 LEU B CA  1 
ATOM   1571 C C   . LEU A 1 205 ? 23.297  -7.976  38.256 1.00 16.38 ? 205 LEU B C   1 
ATOM   1572 O O   . LEU A 1 205 ? 24.076  -7.077  38.588 1.00 15.50 ? 205 LEU B O   1 
ATOM   1573 C CB  . LEU A 1 205 ? 23.530  -10.302 39.192 1.00 12.68 ? 205 LEU B CB  1 
ATOM   1574 C CG  . LEU A 1 205 ? 23.283  -11.205 40.399 1.00 17.37 ? 205 LEU B CG  1 
ATOM   1575 C CD1 . LEU A 1 205 ? 23.801  -12.631 40.153 1.00 16.17 ? 205 LEU B CD1 1 
ATOM   1576 C CD2 . LEU A 1 205 ? 23.959  -10.615 41.617 1.00 15.52 ? 205 LEU B CD2 1 
ATOM   1577 N N   . ALA A 1 206 ? 22.840  -8.089  37.009 1.00 15.19 ? 206 ALA B N   1 
ATOM   1578 C CA  . ALA A 1 206 ? 23.318  -7.164  35.983 1.00 17.10 ? 206 ALA B CA  1 
ATOM   1579 C C   . ALA A 1 206 ? 22.911  -5.730  36.302 1.00 16.58 ? 206 ALA B C   1 
ATOM   1580 O O   . ALA A 1 206 ? 23.676  -4.780  36.061 1.00 14.79 ? 206 ALA B O   1 
ATOM   1581 C CB  . ALA A 1 206 ? 22.783  -7.588  34.611 1.00 14.95 ? 206 ALA B CB  1 
ATOM   1582 N N   . TRP A 1 207 ? 21.735  -5.563  36.889 1.00 15.08 ? 207 TRP B N   1 
ATOM   1583 C CA  . TRP A 1 207 ? 21.247  -4.238  37.236 1.00 14.90 ? 207 TRP B CA  1 
ATOM   1584 C C   . TRP A 1 207 ? 21.990  -3.678  38.446 1.00 15.38 ? 207 TRP B C   1 
ATOM   1585 O O   . TRP A 1 207 ? 22.280  -2.481  38.495 1.00 17.23 ? 207 TRP B O   1 
ATOM   1586 C CB  . TRP A 1 207 ? 19.733  -4.341  37.443 1.00 14.20 ? 207 TRP B CB  1 
ATOM   1587 C CG  . TRP A 1 207 ? 19.047  -3.198  38.077 1.00 16.87 ? 207 TRP B CG  1 
ATOM   1588 C CD1 . TRP A 1 207 ? 18.615  -2.059  37.466 1.00 20.09 ? 207 TRP B CD1 1 
ATOM   1589 C CD2 . TRP A 1 207 ? 18.611  -3.124  39.437 1.00 17.41 ? 207 TRP B CD2 1 
ATOM   1590 N NE1 . TRP A 1 207 ? 17.983  -1.252  38.383 1.00 19.80 ? 207 TRP B NE1 1 
ATOM   1591 C CE2 . TRP A 1 207 ? 17.964  -1.883  39.598 1.00 19.34 ? 207 TRP B CE2 1 
ATOM   1592 C CE3 . TRP A 1 207 ? 18.725  -3.972  40.543 1.00 18.13 ? 207 TRP B CE3 1 
ATOM   1593 C CZ2 . TRP A 1 207 ? 17.418  -1.475  40.826 1.00 23.42 ? 207 TRP B CZ2 1 
ATOM   1594 C CZ3 . TRP A 1 207 ? 18.199  -3.557  41.766 1.00 20.05 ? 207 TRP B CZ3 1 
ATOM   1595 C CH2 . TRP A 1 207 ? 17.551  -2.324  41.890 1.00 18.65 ? 207 TRP B CH2 1 
ATOM   1596 N N   . LEU A 1 208 ? 22.333  -4.529  39.421 1.00 15.38 ? 208 LEU B N   1 
ATOM   1597 C CA  . LEU A 1 208 ? 23.219  -4.099  40.498 1.00 14.98 ? 208 LEU B CA  1 
ATOM   1598 C C   . LEU A 1 208 ? 24.587  -3.661  39.964 1.00 16.11 ? 208 LEU B C   1 
ATOM   1599 O O   . LEU A 1 208 ? 25.188  -2.714  40.489 1.00 16.87 ? 208 LEU B O   1 
ATOM   1600 C CB  . LEU A 1 208 ? 23.388  -5.216  41.532 1.00 12.23 ? 208 LEU B CB  1 
ATOM   1601 C CG  . LEU A 1 208 ? 22.141  -5.579  42.346 1.00 14.26 ? 208 LEU B CG  1 
ATOM   1602 C CD1 . LEU A 1 208 ? 22.411  -6.744  43.316 1.00 17.46 ? 208 LEU B CD1 1 
ATOM   1603 C CD2 . LEU A 1 208 ? 21.594  -4.364  43.064 1.00 14.92 ? 208 LEU B CD2 1 
ATOM   1604 N N   . TYR A 1 209 ? 25.094  -4.328  38.923 1.00 15.05 ? 209 TYR B N   1 
ATOM   1605 C CA  . TYR A 1 209 ? 26.339  -3.874  38.301 1.00 13.20 ? 209 TYR B CA  1 
ATOM   1606 C C   . TYR A 1 209 ? 26.141  -2.526  37.607 1.00 16.02 ? 209 TYR B C   1 
ATOM   1607 O O   . TYR A 1 209 ? 26.996  -1.635  37.718 1.00 16.65 ? 209 TYR B O   1 
ATOM   1608 C CB  . TYR A 1 209 ? 26.862  -4.913  37.307 1.00 11.69 ? 209 TYR B CB  1 
ATOM   1609 C CG  . TYR A 1 209 ? 27.638  -6.039  37.966 1.00 14.96 ? 209 TYR B CG  1 
ATOM   1610 C CD1 . TYR A 1 209 ? 28.891  -5.816  38.525 1.00 16.16 ? 209 TYR B CD1 1 
ATOM   1611 C CD2 . TYR A 1 209 ? 27.133  -7.337  37.996 1.00 15.05 ? 209 TYR B CD2 1 
ATOM   1612 C CE1 . TYR A 1 209 ? 29.612  -6.836  39.126 1.00 17.43 ? 209 TYR B CE1 1 
ATOM   1613 C CE2 . TYR A 1 209 ? 27.849  -8.382  38.598 1.00 17.10 ? 209 TYR B CE2 1 
ATOM   1614 C CZ  . TYR A 1 209 ? 29.084  -8.129  39.167 1.00 18.70 ? 209 TYR B CZ  1 
ATOM   1615 O OH  . TYR A 1 209 ? 29.811  -9.166  39.751 1.00 15.75 ? 209 TYR B OH  1 
ATOM   1616 N N   . ALA A 1 210 ? 25.018  -2.365  36.893 1.00 15.07 ? 210 ALA B N   1 
ATOM   1617 C CA  . ALA A 1 210 ? 24.656  -1.066  36.328 1.00 17.18 ? 210 ALA B CA  1 
ATOM   1618 C C   . ALA A 1 210 ? 24.658  0.027   37.390 1.00 18.58 ? 210 ALA B C   1 
ATOM   1619 O O   . ALA A 1 210 ? 25.161  1.132   37.154 1.00 16.08 ? 210 ALA B O   1 
ATOM   1620 C CB  . ALA A 1 210 ? 23.286  -1.160  35.644 1.00 15.79 ? 210 ALA B CB  1 
ATOM   1621 N N   . ALA A 1 211 ? 24.110  -0.272  38.569 1.00 16.93 ? 211 ALA B N   1 
ATOM   1622 C CA  . ALA A 1 211 ? 24.072  0.699   39.657 1.00 19.73 ? 211 ALA B CA  1 
ATOM   1623 C C   . ALA A 1 211 ? 25.477  1.120   40.073 1.00 19.07 ? 211 ALA B C   1 
ATOM   1624 O O   . ALA A 1 211 ? 25.777  2.317   40.186 1.00 19.72 ? 211 ALA B O   1 
ATOM   1625 C CB  . ALA A 1 211 ? 23.317  0.103   40.837 1.00 17.59 ? 211 ALA B CB  1 
ATOM   1626 N N   . VAL A 1 212 ? 26.357  0.141   40.310 1.00 15.52 ? 212 VAL B N   1 
ATOM   1627 C CA  . VAL A 1 212 ? 27.735  0.459   40.673 1.00 16.67 ? 212 VAL B CA  1 
ATOM   1628 C C   . VAL A 1 212 ? 28.404  1.313   39.597 1.00 19.52 ? 212 VAL B C   1 
ATOM   1629 O O   . VAL A 1 212 ? 29.088  2.297   39.907 1.00 20.16 ? 212 VAL B O   1 
ATOM   1630 C CB  . VAL A 1 212 ? 28.517  -0.839  40.940 1.00 15.65 ? 212 VAL B CB  1 
ATOM   1631 C CG1 . VAL A 1 212 ? 30.008  -0.533  41.146 1.00 20.06 ? 212 VAL B CG1 1 
ATOM   1632 C CG2 . VAL A 1 212 ? 27.972  -1.521  42.173 1.00 15.91 ? 212 VAL B CG2 1 
ATOM   1633 N N   . ILE A 1 213 ? 28.229  0.954   38.322 1.00 17.64 ? 213 ILE B N   1 
ATOM   1634 C CA  . ILE A 1 213 ? 28.906  1.687   37.253 1.00 20.29 ? 213 ILE B CA  1 
ATOM   1635 C C   . ILE A 1 213 ? 28.484  3.143   37.267 1.00 22.99 ? 213 ILE B C   1 
ATOM   1636 O O   . ILE A 1 213 ? 29.293  4.045   36.999 1.00 23.39 ? 213 ILE B O   1 
ATOM   1637 C CB  . ILE A 1 213 ? 28.626  1.033   35.885 1.00 18.79 ? 213 ILE B CB  1 
ATOM   1638 C CG1 . ILE A 1 213 ? 29.346  -0.318  35.782 1.00 19.49 ? 213 ILE B CG1 1 
ATOM   1639 C CG2 . ILE A 1 213 ? 29.067  1.954   34.730 1.00 20.68 ? 213 ILE B CG2 1 
ATOM   1640 C CD1 . ILE A 1 213 ? 28.756  -1.238  34.733 1.00 21.92 ? 213 ILE B CD1 1 
ATOM   1641 N N   . ASN A 1 214 ? 27.239  3.399   37.623 1.00 18.15 ? 214 ASN B N   1 
ATOM   1642 C CA  . ASN A 1 214 ? 26.712  4.754   37.663 1.00 21.47 ? 214 ASN B CA  1 
ATOM   1643 C C   . ASN A 1 214 ? 26.900  5.426   39.012 1.00 21.23 ? 214 ASN B C   1 
ATOM   1644 O O   . ASN A 1 214 ? 26.477  6.575   39.180 1.00 25.64 ? 214 ASN B O   1 
ATOM   1645 C CB  . ASN A 1 214 ? 25.246  4.734   37.242 1.00 23.01 ? 214 ASN B CB  1 
ATOM   1646 C CG  . ASN A 1 214 ? 25.103  4.579   35.736 1.00 26.41 ? 214 ASN B CG  1 
ATOM   1647 O OD1 . ASN A 1 214 ? 25.258  5.552   34.996 1.00 30.54 ? 214 ASN B OD1 1 
ATOM   1648 N ND2 . ASN A 1 214 ? 24.910  3.351   35.270 1.00 23.47 ? 214 ASN B ND2 1 
ATOM   1649 N N   . GLY A 1 215 ? 27.562  4.764   39.956 1.00 22.10 ? 215 GLY B N   1 
ATOM   1650 C CA  . GLY A 1 215 ? 27.954  5.383   41.205 1.00 23.83 ? 215 GLY B CA  1 
ATOM   1651 C C   . GLY A 1 215 ? 27.005  5.163   42.359 1.00 24.95 ? 215 GLY B C   1 
ATOM   1652 O O   . GLY A 1 215 ? 27.253  5.692   43.449 1.00 24.77 ? 215 GLY B O   1 
ATOM   1653 N N   . ASP A 1 216 ? 25.923  4.413   42.155 1.00 23.06 ? 216 ASP B N   1 
ATOM   1654 C CA  . ASP A 1 216 ? 24.978  4.062   43.214 1.00 23.97 ? 216 ASP B CA  1 
ATOM   1655 C C   . ASP A 1 216 ? 25.515  2.778   43.837 1.00 24.94 ? 216 ASP B C   1 
ATOM   1656 O O   . ASP A 1 216 ? 25.249  1.681   43.347 1.00 23.11 ? 216 ASP B O   1 
ATOM   1657 C CB  . ASP A 1 216 ? 23.580  3.874   42.623 1.00 22.58 ? 216 ASP B CB  1 
ATOM   1658 C CG  . ASP A 1 216 ? 22.459  4.242   43.579 1.00 26.46 ? 216 ASP B CG  1 
ATOM   1659 O OD1 . ASP A 1 216 ? 22.707  4.519   44.771 1.00 26.81 ? 216 ASP B OD1 1 
ATOM   1660 O OD2 . ASP A 1 216 ? 21.300  4.277   43.113 1.00 27.40 ? 216 ASP B OD2 1 
ATOM   1661 N N   . ARG A 1 217 ? 26.294  2.906   44.925 1.00 20.91 ? 217 ARG B N   1 
ATOM   1662 C CA  . ARG A 1 217 ? 27.105  1.788   45.410 1.00 21.73 ? 217 ARG B CA  1 
ATOM   1663 C C   . ARG A 1 217 ? 26.895  1.454   46.887 1.00 18.59 ? 217 ARG B C   1 
ATOM   1664 O O   . ARG A 1 217 ? 27.686  0.689   47.455 1.00 19.84 ? 217 ARG B O   1 
ATOM   1665 C CB  . ARG A 1 217 ? 28.596  2.073   45.171 1.00 24.37 ? 217 ARG B CB  1 
ATOM   1666 C CG  . ARG A 1 217 ? 29.018  3.470   45.514 1.00 31.04 ? 217 ARG B CG  1 
ATOM   1667 C CD  . ARG A 1 217 ? 30.412  3.796   44.958 1.00 33.09 ? 217 ARG B CD  1 
ATOM   1668 N NE  . ARG A 1 217 ? 30.719  5.209   45.125 1.00 36.98 ? 217 ARG B NE  1 
ATOM   1669 C CZ  . ARG A 1 217 ? 31.340  5.737   46.172 1.00 39.20 ? 217 ARG B CZ  1 
ATOM   1670 N NH1 . ARG A 1 217 ? 31.803  4.984   47.160 1.00 43.88 ? 217 ARG B NH1 1 
ATOM   1671 N NH2 . ARG A 1 217 ? 31.507  7.057   46.226 1.00 43.39 ? 217 ARG B NH2 1 
ATOM   1672 N N   . TRP A 1 218 ? 25.855  1.987   47.526 1.00 20.95 ? 218 TRP B N   1 
ATOM   1673 C CA  . TRP A 1 218 ? 25.731  1.861   48.977 1.00 19.46 ? 218 TRP B CA  1 
ATOM   1674 C C   . TRP A 1 218 ? 25.535  0.419   49.434 1.00 20.07 ? 218 TRP B C   1 
ATOM   1675 O O   . TRP A 1 218 ? 25.856  0.096   50.581 1.00 20.85 ? 218 TRP B O   1 
ATOM   1676 C CB  . TRP A 1 218 ? 24.564  2.726   49.478 1.00 21.02 ? 218 TRP B CB  1 
ATOM   1677 C CG  . TRP A 1 218 ? 23.220  2.332   48.913 1.00 23.01 ? 218 TRP B CG  1 
ATOM   1678 C CD1 . TRP A 1 218 ? 22.573  2.892   47.840 1.00 20.81 ? 218 TRP B CD1 1 
ATOM   1679 C CD2 . TRP A 1 218 ? 22.349  1.306   49.415 1.00 20.27 ? 218 TRP B CD2 1 
ATOM   1680 N NE1 . TRP A 1 218 ? 21.363  2.258   47.637 1.00 18.78 ? 218 TRP B NE1 1 
ATOM   1681 C CE2 . TRP A 1 218 ? 21.205  1.283   48.588 1.00 20.73 ? 218 TRP B CE2 1 
ATOM   1682 C CE3 . TRP A 1 218 ? 22.427  0.403   50.482 1.00 22.26 ? 218 TRP B CE3 1 
ATOM   1683 C CZ2 . TRP A 1 218 ? 20.150  0.398   48.799 1.00 21.30 ? 218 TRP B CZ2 1 
ATOM   1684 C CZ3 . TRP A 1 218 ? 21.394  -0.483  50.677 1.00 24.20 ? 218 TRP B CZ3 1 
ATOM   1685 C CH2 . TRP A 1 218 ? 20.261  -0.476  49.843 1.00 24.02 ? 218 TRP B CH2 1 
ATOM   1686 N N   . PHE A 1 219 ? 24.994  -0.443  48.581 1.00 18.69 ? 219 PHE B N   1 
ATOM   1687 C CA  . PHE A 1 219 ? 24.651  -1.815  48.949 1.00 19.37 ? 219 PHE B CA  1 
ATOM   1688 C C   . PHE A 1 219 ? 25.830  -2.770  48.836 1.00 19.35 ? 219 PHE B C   1 
ATOM   1689 O O   . PHE A 1 219 ? 25.681  -3.948  49.171 1.00 19.02 ? 219 PHE B O   1 
ATOM   1690 C CB  . PHE A 1 219 ? 23.523  -2.334  48.058 1.00 20.10 ? 219 PHE B CB  1 
ATOM   1691 C CG  . PHE A 1 219 ? 23.788  -2.124  46.606 1.00 21.46 ? 219 PHE B CG  1 
ATOM   1692 C CD1 . PHE A 1 219 ? 24.562  -3.026  45.895 1.00 20.79 ? 219 PHE B CD1 1 
ATOM   1693 C CD2 . PHE A 1 219 ? 23.302  -0.998  45.954 1.00 20.00 ? 219 PHE B CD2 1 
ATOM   1694 C CE1 . PHE A 1 219 ? 24.848  -2.816  44.547 1.00 19.60 ? 219 PHE B CE1 1 
ATOM   1695 C CE2 . PHE A 1 219 ? 23.579  -0.786  44.619 1.00 19.26 ? 219 PHE B CE2 1 
ATOM   1696 C CZ  . PHE A 1 219 ? 24.350  -1.710  43.904 1.00 17.65 ? 219 PHE B CZ  1 
ATOM   1697 N N   . LEU A 1 220 ? 26.965  -2.308  48.333 1.00 19.73 ? 220 LEU B N   1 
ATOM   1698 C CA  . LEU A 1 220 ? 28.151  -3.147  48.270 1.00 16.98 ? 220 LEU B CA  1 
ATOM   1699 C C   . LEU A 1 220 ? 28.644  -3.445  49.679 1.00 20.46 ? 220 LEU B C   1 
ATOM   1700 O O   . LEU A 1 220 ? 28.530  -2.626  50.589 1.00 20.07 ? 220 LEU B O   1 
ATOM   1701 C CB  . LEU A 1 220 ? 29.240  -2.434  47.480 1.00 16.47 ? 220 LEU B CB  1 
ATOM   1702 C CG  . LEU A 1 220 ? 28.999  -2.300  45.976 1.00 17.42 ? 220 LEU B CG  1 
ATOM   1703 C CD1 . LEU A 1 220 ? 30.123  -1.508  45.361 1.00 16.74 ? 220 LEU B CD1 1 
ATOM   1704 C CD2 . LEU A 1 220 ? 28.878  -3.669  45.303 1.00 18.95 ? 220 LEU B CD2 1 
ATOM   1705 N N   . ASN A 1 221 ? 29.233  -4.615  49.858 1.00 20.88 ? 221 ASN B N   1 
ATOM   1706 C CA  . ASN A 1 221 ? 29.762  -4.953  51.168 1.00 21.75 ? 221 ASN B CA  1 
ATOM   1707 C C   . ASN A 1 221 ? 31.001  -5.806  50.980 1.00 18.87 ? 221 ASN B C   1 
ATOM   1708 O O   . ASN A 1 221 ? 31.283  -6.299  49.885 1.00 18.92 ? 221 ASN B O   1 
ATOM   1709 C CB  . ASN A 1 221 ? 28.730  -5.670  52.053 1.00 20.88 ? 221 ASN B CB  1 
ATOM   1710 C CG  . ASN A 1 221 ? 28.188  -6.950  51.433 1.00 23.41 ? 221 ASN B CG  1 
ATOM   1711 O OD1 . ASN A 1 221 ? 28.930  -7.762  50.887 1.00 22.06 ? 221 ASN B OD1 1 
ATOM   1712 N ND2 . ASN A 1 221 ? 26.873  -7.144  51.542 1.00 24.07 ? 221 ASN B ND2 1 
ATOM   1713 N N   . ARG A 1 222 ? 31.732  -5.984  52.072 1.00 20.65 ? 222 ARG B N   1 
ATOM   1714 C CA  . ARG A 1 222 ? 33.006  -6.694  52.010 1.00 22.09 ? 222 ARG B CA  1 
ATOM   1715 C C   . ARG A 1 222 ? 32.851  -8.206  51.995 1.00 23.87 ? 222 ARG B C   1 
ATOM   1716 O O   . ARG A 1 222 ? 33.864  -8.910  51.917 1.00 20.68 ? 222 ARG B O   1 
ATOM   1717 C CB  . ARG A 1 222 ? 33.892  -6.296  53.193 1.00 24.12 ? 222 ARG B CB  1 
ATOM   1718 C CG  . ARG A 1 222 ? 33.340  -6.724  54.545 1.00 25.62 ? 222 ARG B CG  1 
ATOM   1719 C CD  . ARG A 1 222 ? 34.028  -5.962  55.676 1.00 27.07 ? 222 ARG B CD  1 
ATOM   1720 N NE  . ARG A 1 222 ? 33.617  -6.463  56.984 1.00 31.21 ? 222 ARG B NE  1 
ATOM   1721 C CZ  . ARG A 1 222 ? 32.593  -5.982  57.680 1.00 34.98 ? 222 ARG B CZ  1 
ATOM   1722 N NH1 . ARG A 1 222 ? 31.827  -5.011  57.206 1.00 34.20 ? 222 ARG B NH1 1 
ATOM   1723 N NH2 . ARG A 1 222 ? 32.324  -6.492  58.879 1.00 34.24 ? 222 ARG B NH2 1 
ATOM   1724 N N   . PHE A 1 223 ? 31.632  -8.725  52.059 1.00 21.31 ? 223 PHE B N   1 
ATOM   1725 C CA  . PHE A 1 223 ? 31.422  -10.151 52.222 1.00 20.98 ? 223 PHE B CA  1 
ATOM   1726 C C   . PHE A 1 223 ? 31.293  -10.851 50.875 1.00 20.34 ? 223 PHE B C   1 
ATOM   1727 O O   . PHE A 1 223 ? 31.012  -10.242 49.848 1.00 19.46 ? 223 PHE B O   1 
ATOM   1728 C CB  . PHE A 1 223 ? 30.177  -10.406 53.079 1.00 20.51 ? 223 PHE B CB  1 
ATOM   1729 C CG  . PHE A 1 223 ? 30.129  -9.572  54.322 1.00 21.23 ? 223 PHE B CG  1 
ATOM   1730 C CD1 . PHE A 1 223 ? 31.026  -9.805  55.355 1.00 25.63 ? 223 PHE B CD1 1 
ATOM   1731 C CD2 . PHE A 1 223 ? 29.209  -8.537  54.457 1.00 26.74 ? 223 PHE B CD2 1 
ATOM   1732 C CE1 . PHE A 1 223 ? 30.997  -9.048  56.502 1.00 23.91 ? 223 PHE B CE1 1 
ATOM   1733 C CE2 . PHE A 1 223 ? 29.177  -7.761  55.610 1.00 24.06 ? 223 PHE B CE2 1 
ATOM   1734 C CZ  . PHE A 1 223 ? 30.063  -8.015  56.634 1.00 26.63 ? 223 PHE B CZ  1 
ATOM   1735 N N   . THR A 1 224 ? 31.540  -12.146 50.885 1.00 20.52 ? 224 THR B N   1 
ATOM   1736 C CA  . THR A 1 224 ? 31.364  -12.963 49.700 1.00 17.41 ? 224 THR B CA  1 
ATOM   1737 C C   . THR A 1 224 ? 30.538  -14.178 50.089 1.00 17.78 ? 224 THR B C   1 
ATOM   1738 O O   . THR A 1 224 ? 30.413  -14.509 51.268 1.00 24.35 ? 224 THR B O   1 
ATOM   1739 C CB  . THR A 1 224 ? 32.684  -13.431 49.121 1.00 20.16 ? 224 THR B CB  1 
ATOM   1740 O OG1 . THR A 1 224 ? 33.368  -14.198 50.121 1.00 23.30 ? 224 THR B OG1 1 
ATOM   1741 C CG2 . THR A 1 224 ? 33.546  -12.234 48.731 1.00 20.38 ? 224 THR B CG2 1 
ATOM   1742 N N   . THR A 1 225 ? 29.989  -14.848 49.090 1.00 17.12 ? 225 THR B N   1 
ATOM   1743 C CA  . THR A 1 225 ? 29.233  -16.067 49.333 1.00 24.95 ? 225 THR B CA  1 
ATOM   1744 C C   . THR A 1 225 ? 29.677  -17.137 48.350 1.00 21.65 ? 225 THR B C   1 
ATOM   1745 O O   . THR A 1 225 ? 30.181  -16.840 47.268 1.00 24.47 ? 225 THR B O   1 
ATOM   1746 C CB  . THR A 1 225 ? 27.714  -15.818 49.215 1.00 23.42 ? 225 THR B CB  1 
ATOM   1747 O OG1 . THR A 1 225 ? 26.987  -17.025 49.462 1.00 23.37 ? 225 THR B OG1 1 
ATOM   1748 C CG2 . THR A 1 225 ? 27.356  -15.336 47.817 1.00 23.31 ? 225 THR B CG2 1 
ATOM   1749 N N   . THR A 1 226 ? 29.477  -18.402 48.725 1.00 21.81 ? 226 THR B N   1 
ATOM   1750 C CA  . THR A 1 226 ? 29.609  -19.432 47.712 1.00 21.34 ? 226 THR B CA  1 
ATOM   1751 C C   . THR A 1 226 ? 28.384  -19.442 46.802 1.00 19.07 ? 226 THR B C   1 
ATOM   1752 O O   . THR A 1 226 ? 27.315  -18.893 47.124 1.00 20.84 ? 226 THR B O   1 
ATOM   1753 C CB  . THR A 1 226 ? 29.780  -20.813 48.343 1.00 23.49 ? 226 THR B CB  1 
ATOM   1754 O OG1 . THR A 1 226 ? 28.529  -21.203 48.941 1.00 24.05 ? 226 THR B OG1 1 
ATOM   1755 C CG2 . THR A 1 226 ? 30.857  -20.789 49.393 1.00 24.57 ? 226 THR B CG2 1 
ATOM   1756 N N   . LEU A 1 227 ? 28.543  -20.085 45.646 1.00 19.44 ? 227 LEU B N   1 
ATOM   1757 C CA  . LEU A 1 227 ? 27.441  -20.196 44.701 1.00 18.79 ? 227 LEU B CA  1 
ATOM   1758 C C   . LEU A 1 227 ? 26.299  -21.012 45.293 1.00 24.25 ? 227 LEU B C   1 
ATOM   1759 O O   . LEU A 1 227 ? 25.125  -20.644 45.160 1.00 21.98 ? 227 LEU B O   1 
ATOM   1760 C CB  . LEU A 1 227 ? 27.916  -20.822 43.395 1.00 19.08 ? 227 LEU B CB  1 
ATOM   1761 C CG  . LEU A 1 227 ? 26.832  -20.752 42.311 1.00 21.74 ? 227 LEU B CG  1 
ATOM   1762 C CD1 . LEU A 1 227 ? 26.353  -19.302 42.069 1.00 25.12 ? 227 LEU B CD1 1 
ATOM   1763 C CD2 . LEU A 1 227 ? 27.254  -21.425 41.026 1.00 25.81 ? 227 LEU B CD2 1 
ATOM   1764 N N   . ASN A 1 228 ? 26.629  -22.128 45.952 1.00 23.01 ? 228 ASN B N   1 
ATOM   1765 C CA  . ASN A 1 228 ? 25.583  -22.968 46.538 1.00 22.67 ? 228 ASN B CA  1 
ATOM   1766 C C   . ASN A 1 228 ? 24.848  -22.255 47.660 1.00 24.66 ? 228 ASN B C   1 
ATOM   1767 O O   . ASN A 1 228 ? 23.620  -22.356 47.758 1.00 27.27 ? 228 ASN B O   1 
ATOM   1768 C CB  . ASN A 1 228 ? 26.164  -24.291 47.056 1.00 26.88 ? 228 ASN B CB  1 
ATOM   1769 C CG  . ASN A 1 228 ? 26.654  -25.197 45.950 1.00 26.53 ? 228 ASN B CG  1 
ATOM   1770 O OD1 . ASN A 1 228 ? 26.234  -25.082 44.794 1.00 31.46 ? 228 ASN B OD1 1 
ATOM   1771 N ND2 . ASN A 1 228 ? 27.502  -26.158 46.312 1.00 33.91 ? 228 ASN B ND2 1 
ATOM   1772 N N   . ASP A 1 229 ? 25.578  -21.558 48.535 1.00 21.44 ? 229 ASP B N   1 
ATOM   1773 C CA  . ASP A 1 229 ? 24.918  -20.840 49.623 1.00 23.34 ? 229 ASP B CA  1 
ATOM   1774 C C   . ASP A 1 229 ? 24.060  -19.698 49.097 1.00 22.67 ? 229 ASP B C   1 
ATOM   1775 O O   . ASP A 1 229 ? 22.979  -19.442 49.634 1.00 23.43 ? 229 ASP B O   1 
ATOM   1776 C CB  . ASP A 1 229 ? 25.945  -20.317 50.625 1.00 26.62 ? 229 ASP B CB  1 
ATOM   1777 C CG  . ASP A 1 229 ? 26.591  -21.424 51.433 1.00 32.31 ? 229 ASP B CG  1 
ATOM   1778 O OD1 . ASP A 1 229 ? 26.130  -22.587 51.340 1.00 33.53 ? 229 ASP B OD1 1 
ATOM   1779 O OD2 . ASP A 1 229 ? 27.576  -21.129 52.137 1.00 24.95 ? 229 ASP B OD2 1 
ATOM   1780 N N   . PHE A 1 230 ? 24.523  -18.983 48.060 1.00 19.50 ? 230 PHE B N   1 
ATOM   1781 C CA  . PHE A 1 230 ? 23.651  -17.979 47.455 1.00 24.07 ? 230 PHE B CA  1 
ATOM   1782 C C   . PHE A 1 230 ? 22.358  -18.620 46.960 1.00 21.19 ? 230 PHE B C   1 
ATOM   1783 O O   . PHE A 1 230 ? 21.252  -18.126 47.236 1.00 22.80 ? 230 PHE B O   1 
ATOM   1784 C CB  . PHE A 1 230 ? 24.350  -17.253 46.304 1.00 19.01 ? 230 PHE B CB  1 
ATOM   1785 C CG  . PHE A 1 230 ? 23.409  -16.381 45.514 1.00 16.40 ? 230 PHE B CG  1 
ATOM   1786 C CD1 . PHE A 1 230 ? 22.990  -15.163 46.029 1.00 18.66 ? 230 PHE B CD1 1 
ATOM   1787 C CD2 . PHE A 1 230 ? 22.894  -16.812 44.290 1.00 18.50 ? 230 PHE B CD2 1 
ATOM   1788 C CE1 . PHE A 1 230 ? 22.088  -14.365 45.329 1.00 16.91 ? 230 PHE B CE1 1 
ATOM   1789 C CE2 . PHE A 1 230 ? 21.984  -16.025 43.579 1.00 19.33 ? 230 PHE B CE2 1 
ATOM   1790 C CZ  . PHE A 1 230 ? 21.595  -14.789 44.094 1.00 18.06 ? 230 PHE B CZ  1 
ATOM   1791 N N   . ASN A 1 231 ? 22.478  -19.748 46.254 1.00 21.55 ? 231 ASN B N   1 
ATOM   1792 C CA  . ASN A 1 231 ? 21.301  -20.383 45.680 1.00 22.39 ? 231 ASN B CA  1 
ATOM   1793 C C   . ASN A 1 231 ? 20.369  -20.950 46.745 1.00 23.10 ? 231 ASN B C   1 
ATOM   1794 O O   . ASN A 1 231 ? 19.146  -20.951 46.543 1.00 24.48 ? 231 ASN B O   1 
ATOM   1795 C CB  . ASN A 1 231 ? 21.722  -21.447 44.674 1.00 24.02 ? 231 ASN B CB  1 
ATOM   1796 C CG  . ASN A 1 231 ? 22.000  -20.847 43.310 1.00 26.78 ? 231 ASN B CG  1 
ATOM   1797 O OD1 . ASN A 1 231 ? 21.367  -19.857 42.933 1.00 24.34 ? 231 ASN B OD1 1 
ATOM   1798 N ND2 . ASN A 1 231 ? 22.944  -21.439 42.560 1.00 24.96 ? 231 ASN B ND2 1 
ATOM   1799 N N   . LEU A 1 232 ? 20.898  -21.360 47.903 1.00 22.43 ? 232 LEU B N   1 
ATOM   1800 C CA  . LEU A 1 232 ? 20.007  -21.767 48.991 1.00 24.53 ? 232 LEU B CA  1 
ATOM   1801 C C   . LEU A 1 232 ? 19.080  -20.623 49.387 1.00 26.18 ? 232 LEU B C   1 
ATOM   1802 O O   . LEU A 1 232 ? 17.867  -20.818 49.543 1.00 23.79 ? 232 LEU B O   1 
ATOM   1803 C CB  . LEU A 1 232 ? 20.817  -22.240 50.200 1.00 22.82 ? 232 LEU B CB  1 
ATOM   1804 C CG  . LEU A 1 232 ? 21.487  -23.609 50.013 1.00 27.78 ? 232 LEU B CG  1 
ATOM   1805 C CD1 . LEU A 1 232 ? 22.355  -23.990 51.199 1.00 31.45 ? 232 LEU B CD1 1 
ATOM   1806 C CD2 . LEU A 1 232 ? 20.451  -24.676 49.734 1.00 28.26 ? 232 LEU B CD2 1 
ATOM   1807 N N   . VAL A 1 233 ? 19.634  -19.417 49.524 1.00 22.22 ? 233 VAL B N   1 
ATOM   1808 C CA  . VAL A 1 233 ? 18.840  -18.247 49.894 1.00 25.63 ? 233 VAL B CA  1 
ATOM   1809 C C   . VAL A 1 233 ? 17.952  -17.825 48.738 1.00 23.66 ? 233 VAL B C   1 
ATOM   1810 O O   . VAL A 1 233 ? 16.766  -17.506 48.926 1.00 25.34 ? 233 VAL B O   1 
ATOM   1811 C CB  . VAL A 1 233 ? 19.761  -17.101 50.358 1.00 22.07 ? 233 VAL B CB  1 
ATOM   1812 C CG1 . VAL A 1 233 ? 18.962  -15.809 50.570 1.00 28.19 ? 233 VAL B CG1 1 
ATOM   1813 C CG2 . VAL A 1 233 ? 20.483  -17.482 51.648 1.00 28.27 ? 233 VAL B CG2 1 
ATOM   1814 N N   . ALA A 1 234 ? 18.494  -17.858 47.522 1.00 23.64 ? 234 ALA B N   1 
ATOM   1815 C CA  . ALA A 1 234 ? 17.759  -17.389 46.348 1.00 30.62 ? 234 ALA B CA  1 
ATOM   1816 C C   . ALA A 1 234 ? 16.492  -18.197 46.131 1.00 25.15 ? 234 ALA B C   1 
ATOM   1817 O O   . ALA A 1 234 ? 15.411  -17.631 45.929 1.00 26.89 ? 234 ALA B O   1 
ATOM   1818 C CB  . ALA A 1 234 ? 18.644  -17.471 45.103 1.00 30.33 ? 234 ALA B CB  1 
ATOM   1819 N N   . MET A 1 235 ? 16.614  -19.526 46.178 1.00 25.76 ? 235 MET B N   1 
ATOM   1820 C CA  . MET A 1 235 ? 15.493  -20.412 45.922 1.00 27.67 ? 235 MET B CA  1 
ATOM   1821 C C   . MET A 1 235 ? 14.331  -20.130 46.864 1.00 24.69 ? 235 MET B C   1 
ATOM   1822 O O   . MET A 1 235 ? 13.177  -20.222 46.451 1.00 26.68 ? 235 MET B O   1 
ATOM   1823 C CB  . MET A 1 235 ? 15.965  -21.875 46.014 1.00 31.70 ? 235 MET B CB  1 
ATOM   1824 C CG  . MET A 1 235 ? 14.883  -22.939 46.249 1.00 40.08 ? 235 MET B CG  1 
ATOM   1825 S SD  . MET A 1 235 ? 14.377  -23.171 47.992 1.00 53.88 ? 235 MET B SD  1 
ATOM   1826 C CE  . MET A 1 235 ? 15.987  -23.231 48.803 1.00 42.89 ? 235 MET B CE  1 
ATOM   1827 N N   . LYS A 1 236 ? 14.616  -19.758 48.113 1.00 23.35 ? 236 LYS B N   1 
ATOM   1828 C CA  . LYS A 1 236 ? 13.552  -19.481 49.080 1.00 20.30 ? 236 LYS B CA  1 
ATOM   1829 C C   . LYS A 1 236 ? 12.710  -18.288 48.668 1.00 22.46 ? 236 LYS B C   1 
ATOM   1830 O O   . LYS A 1 236 ? 11.532  -18.201 49.045 1.00 22.64 ? 236 LYS B O   1 
ATOM   1831 C CB  . LYS A 1 236 ? 14.160  -19.225 50.456 1.00 22.85 ? 236 LYS B CB  1 
ATOM   1832 C CG  . LYS A 1 236 ? 14.879  -20.440 51.046 1.00 23.89 ? 236 LYS B CG  1 
ATOM   1833 C CD  . LYS A 1 236 ? 15.453  -20.103 52.423 1.00 29.43 ? 236 LYS B CD  1 
ATOM   1834 C CE  . LYS A 1 236 ? 14.349  -19.980 53.465 1.00 29.92 ? 236 LYS B CE  1 
ATOM   1835 N NZ  . LYS A 1 236 ? 14.643  -20.721 54.726 1.00 35.26 ? 236 LYS B NZ  1 
ATOM   1836 N N   . TYR A 1 237 ? 13.299  -17.360 47.913 1.00 19.62 ? 237 TYR B N   1 
ATOM   1837 C CA  . TYR A 1 237 ? 12.652  -16.129 47.485 1.00 20.64 ? 237 TYR B CA  1 
ATOM   1838 C C   . TYR A 1 237 ? 12.112  -16.235 46.066 1.00 23.45 ? 237 TYR B C   1 
ATOM   1839 O O   . TYR A 1 237 ? 11.757  -15.218 45.464 1.00 24.72 ? 237 TYR B O   1 
ATOM   1840 C CB  . TYR A 1 237 ? 13.646  -14.971 47.606 1.00 22.07 ? 237 TYR B CB  1 
ATOM   1841 C CG  . TYR A 1 237 ? 13.869  -14.524 49.041 1.00 21.59 ? 237 TYR B CG  1 
ATOM   1842 C CD1 . TYR A 1 237 ? 13.005  -13.622 49.657 1.00 25.46 ? 237 TYR B CD1 1 
ATOM   1843 C CD2 . TYR A 1 237 ? 14.915  -15.045 49.791 1.00 24.52 ? 237 TYR B CD2 1 
ATOM   1844 C CE1 . TYR A 1 237 ? 13.203  -13.229 50.966 1.00 25.08 ? 237 TYR B CE1 1 
ATOM   1845 C CE2 . TYR A 1 237 ? 15.111  -14.666 51.111 1.00 23.75 ? 237 TYR B CE2 1 
ATOM   1846 C CZ  . TYR A 1 237 ? 14.247  -13.759 51.689 1.00 25.10 ? 237 TYR B CZ  1 
ATOM   1847 O OH  . TYR A 1 237 ? 14.443  -13.371 52.992 1.00 24.04 ? 237 TYR B OH  1 
ATOM   1848 N N   . ASN A 1 238 ? 12.046  -17.453 45.526 1.00 23.54 ? 238 ASN B N   1 
ATOM   1849 C CA  . ASN A 1 238 ? 11.546  -17.707 44.174 1.00 23.15 ? 238 ASN B CA  1 
ATOM   1850 C C   . ASN A 1 238 ? 12.386  -16.996 43.117 1.00 22.27 ? 238 ASN B C   1 
ATOM   1851 O O   . ASN A 1 238 ? 11.868  -16.497 42.115 1.00 23.62 ? 238 ASN B O   1 
ATOM   1852 C CB  . ASN A 1 238 ? 10.070  -17.330 44.041 1.00 22.83 ? 238 ASN B CB  1 
ATOM   1853 C CG  . ASN A 1 238 ? 9.445   -17.926 42.811 1.00 27.51 ? 238 ASN B CG  1 
ATOM   1854 O OD1 . ASN A 1 238 ? 9.610   -19.119 42.533 1.00 28.66 ? 238 ASN B OD1 1 
ATOM   1855 N ND2 . ASN A 1 238 ? 8.715   -17.105 42.064 1.00 32.50 ? 238 ASN B ND2 1 
ATOM   1856 N N   . TYR A 1 239 ? 13.689  -16.949 43.348 1.00 19.89 ? 239 TYR B N   1 
ATOM   1857 C CA  . TYR A 1 239 ? 14.644  -16.530 42.335 1.00 20.55 ? 239 TYR B CA  1 
ATOM   1858 C C   . TYR A 1 239 ? 15.098  -17.736 41.528 1.00 21.79 ? 239 TYR B C   1 
ATOM   1859 O O   . TYR A 1 239 ? 15.280  -18.833 42.071 1.00 19.61 ? 239 TYR B O   1 
ATOM   1860 C CB  . TYR A 1 239 ? 15.860  -15.862 42.978 1.00 20.69 ? 239 TYR B CB  1 
ATOM   1861 C CG  . TYR A 1 239 ? 15.709  -14.372 43.177 1.00 18.39 ? 239 TYR B CG  1 
ATOM   1862 C CD1 . TYR A 1 239 ? 14.634  -13.846 43.889 1.00 21.97 ? 239 TYR B CD1 1 
ATOM   1863 C CD2 . TYR A 1 239 ? 16.653  -13.495 42.656 1.00 17.79 ? 239 TYR B CD2 1 
ATOM   1864 C CE1 . TYR A 1 239 ? 14.495  -12.479 44.074 1.00 21.93 ? 239 TYR B CE1 1 
ATOM   1865 C CE2 . TYR A 1 239 ? 16.523  -12.125 42.838 1.00 19.19 ? 239 TYR B CE2 1 
ATOM   1866 C CZ  . TYR A 1 239 ? 15.449  -11.626 43.536 1.00 21.46 ? 239 TYR B CZ  1 
ATOM   1867 O OH  . TYR A 1 239 ? 15.345  -10.261 43.704 1.00 22.03 ? 239 TYR B OH  1 
ATOM   1868 N N   . GLU A 1 240 ? 15.297  -17.517 40.235 1.00 22.21 ? 240 GLU B N   1 
ATOM   1869 C CA  . GLU A 1 240 ? 15.865  -18.551 39.376 1.00 24.42 ? 240 GLU B CA  1 
ATOM   1870 C C   . GLU A 1 240 ? 17.258  -18.960 39.859 1.00 22.90 ? 240 GLU B C   1 
ATOM   1871 O O   . GLU A 1 240 ? 18.043  -18.102 40.278 1.00 23.97 ? 240 GLU B O   1 
ATOM   1872 C CB  . GLU A 1 240 ? 15.904  -18.043 37.932 1.00 27.35 ? 240 GLU B CB  1 
ATOM   1873 C CG  . GLU A 1 240 ? 16.394  -19.099 36.989 1.00 33.94 ? 240 GLU B CG  1 
ATOM   1874 C CD  . GLU A 1 240 ? 15.277  -20.009 36.549 1.00 34.10 ? 240 GLU B CD  1 
ATOM   1875 O OE1 . GLU A 1 240 ? 14.097  -19.649 36.771 1.00 36.75 ? 240 GLU B OE1 1 
ATOM   1876 O OE2 . GLU A 1 240 ? 15.586  -21.117 36.060 1.00 41.61 ? 240 GLU B OE2 1 
ATOM   1877 N N   . PRO A 1 241 ? 17.585  -20.261 39.867 1.00 21.44 ? 241 PRO B N   1 
ATOM   1878 C CA  . PRO A 1 241 ? 18.940  -20.676 40.251 1.00 21.49 ? 241 PRO B CA  1 
ATOM   1879 C C   . PRO A 1 241 ? 19.984  -20.005 39.376 1.00 20.69 ? 241 PRO B C   1 
ATOM   1880 O O   . PRO A 1 241 ? 19.818  -19.884 38.161 1.00 23.31 ? 241 PRO B O   1 
ATOM   1881 C CB  . PRO A 1 241 ? 18.931  -22.193 40.038 1.00 21.64 ? 241 PRO B CB  1 
ATOM   1882 C CG  . PRO A 1 241 ? 17.484  -22.572 40.158 1.00 24.38 ? 241 PRO B CG  1 
ATOM   1883 C CD  . PRO A 1 241 ? 16.721  -21.419 39.569 1.00 25.04 ? 241 PRO B CD  1 
ATOM   1884 N N   . LEU A 1 242 ? 21.039  -19.535 40.017 1.00 17.28 ? 242 LEU B N   1 
ATOM   1885 C CA  . LEU A 1 242 ? 22.163  -18.939 39.311 1.00 21.63 ? 242 LEU B CA  1 
ATOM   1886 C C   . LEU A 1 242 ? 23.109  -20.061 38.912 1.00 22.00 ? 242 LEU B C   1 
ATOM   1887 O O   . LEU A 1 242 ? 23.639  -20.766 39.778 1.00 21.20 ? 242 LEU B O   1 
ATOM   1888 C CB  . LEU A 1 242 ? 22.868  -17.906 40.187 1.00 19.96 ? 242 LEU B CB  1 
ATOM   1889 C CG  . LEU A 1 242 ? 23.890  -16.988 39.511 1.00 19.55 ? 242 LEU B CG  1 
ATOM   1890 C CD1 . LEU A 1 242 ? 23.192  -15.995 38.609 1.00 18.69 ? 242 LEU B CD1 1 
ATOM   1891 C CD2 . LEU A 1 242 ? 24.677  -16.255 40.587 1.00 20.59 ? 242 LEU B CD2 1 
ATOM   1892 N N   . THR A 1 243 ? 23.304  -20.232 37.609 1.00 22.26 ? 243 THR B N   1 
ATOM   1893 C CA  . THR A 1 243 ? 24.193  -21.254 37.072 1.00 21.02 ? 243 THR B CA  1 
ATOM   1894 C C   . THR A 1 243 ? 25.587  -20.684 36.816 1.00 25.55 ? 243 THR B C   1 
ATOM   1895 O O   . THR A 1 243 ? 25.801  -19.469 36.785 1.00 25.28 ? 243 THR B O   1 
ATOM   1896 C CB  . THR A 1 243 ? 23.639  -21.820 35.765 1.00 26.50 ? 243 THR B CB  1 
ATOM   1897 O OG1 . THR A 1 243 ? 23.636  -20.793 34.768 1.00 26.18 ? 243 THR B OG1 1 
ATOM   1898 C CG2 . THR A 1 243 ? 22.205  -22.298 35.955 1.00 28.37 ? 243 THR B CG2 1 
ATOM   1899 N N   . GLN A 1 244 ? 26.549  -21.591 36.616 1.00 24.66 ? 244 GLN B N   1 
ATOM   1900 C CA  . GLN A 1 244 ? 27.895  -21.169 36.247 1.00 22.87 ? 244 GLN B CA  1 
ATOM   1901 C C   . GLN A 1 244 ? 27.891  -20.414 34.924 1.00 25.21 ? 244 GLN B C   1 
ATOM   1902 O O   . GLN A 1 244 ? 28.690  -19.484 34.735 1.00 25.57 ? 244 GLN B O   1 
ATOM   1903 C CB  . GLN A 1 244 ? 28.820  -22.383 36.185 1.00 24.88 ? 244 GLN B CB  1 
ATOM   1904 C CG  . GLN A 1 244 ? 30.272  -22.018 35.927 1.00 26.91 ? 244 GLN B CG  1 
ATOM   1905 C CD  . GLN A 1 244 ? 30.824  -21.038 36.938 1.00 27.56 ? 244 GLN B CD  1 
ATOM   1906 O OE1 . GLN A 1 244 ? 30.683  -21.225 38.151 1.00 31.52 ? 244 GLN B OE1 1 
ATOM   1907 N NE2 . GLN A 1 244 ? 31.474  -19.987 36.446 1.00 26.22 ? 244 GLN B NE2 1 
ATOM   1908 N N   . ASP A 1 245 ? 26.985  -20.771 34.008 1.00 23.15 ? 245 ASP B N   1 
ATOM   1909 C CA  . ASP A 1 245 ? 26.885  -20.014 32.767 1.00 25.76 ? 245 ASP B CA  1 
ATOM   1910 C C   . ASP A 1 245 ? 26.430  -18.579 33.027 1.00 26.49 ? 245 ASP B C   1 
ATOM   1911 O O   . ASP A 1 245 ? 26.909  -17.648 32.372 1.00 21.32 ? 245 ASP B O   1 
ATOM   1912 C CB  . ASP A 1 245 ? 25.939  -20.698 31.784 1.00 27.65 ? 245 ASP B CB  1 
ATOM   1913 C CG  . ASP A 1 245 ? 25.992  -20.069 30.391 1.00 37.26 ? 245 ASP B CG  1 
ATOM   1914 O OD1 . ASP A 1 245 ? 27.096  -20.024 29.796 1.00 35.89 ? 245 ASP B OD1 1 
ATOM   1915 O OD2 . ASP A 1 245 ? 24.934  -19.625 29.883 1.00 38.93 ? 245 ASP B OD2 1 
ATOM   1916 N N   . HIS A 1 246 ? 25.500  -18.383 33.968 1.00 24.07 ? 246 HIS B N   1 
ATOM   1917 C CA  . HIS A 1 246 ? 25.135  -17.021 34.371 1.00 22.81 ? 246 HIS B CA  1 
ATOM   1918 C C   . HIS A 1 246 ? 26.334  -16.252 34.926 1.00 22.17 ? 246 HIS B C   1 
ATOM   1919 O O   . HIS A 1 246 ? 26.534  -15.066 34.606 1.00 19.72 ? 246 HIS B O   1 
ATOM   1920 C CB  . HIS A 1 246 ? 24.014  -17.057 35.411 1.00 23.64 ? 246 HIS B CB  1 
ATOM   1921 C CG  . HIS A 1 246 ? 22.710  -17.556 34.884 1.00 23.42 ? 246 HIS B CG  1 
ATOM   1922 N ND1 . HIS A 1 246 ? 21.838  -18.314 35.639 1.00 23.99 ? 246 HIS B ND1 1 
ATOM   1923 C CD2 . HIS A 1 246 ? 22.099  -17.351 33.692 1.00 25.44 ? 246 HIS B CD2 1 
ATOM   1924 C CE1 . HIS A 1 246 ? 20.764  -18.589 34.918 1.00 26.45 ? 246 HIS B CE1 1 
ATOM   1925 N NE2 . HIS A 1 246 ? 20.893  -18.009 33.738 1.00 27.61 ? 246 HIS B NE2 1 
ATOM   1926 N N   . VAL A 1 247 ? 27.106  -16.888 35.812 1.00 21.01 ? 247 VAL B N   1 
ATOM   1927 C CA  . VAL A 1 247 ? 28.294  -16.245 36.363 1.00 21.23 ? 247 VAL B CA  1 
ATOM   1928 C C   . VAL A 1 247 ? 29.239  -15.840 35.236 1.00 22.46 ? 247 VAL B C   1 
ATOM   1929 O O   . VAL A 1 247 ? 29.780  -14.726 35.226 1.00 20.52 ? 247 VAL B O   1 
ATOM   1930 C CB  . VAL A 1 247 ? 28.984  -17.180 37.377 1.00 25.11 ? 247 VAL B CB  1 
ATOM   1931 C CG1 . VAL A 1 247 ? 30.289  -16.582 37.831 1.00 22.92 ? 247 VAL B CG1 1 
ATOM   1932 C CG2 . VAL A 1 247 ? 28.081  -17.436 38.576 1.00 24.06 ? 247 VAL B CG2 1 
ATOM   1933 N N   . ASP A 1 248 ? 29.414  -16.730 34.251 1.00 21.89 ? 248 ASP B N   1 
ATOM   1934 C CA  . ASP A 1 248 ? 30.245  -16.443 33.086 1.00 22.13 ? 248 ASP B CA  1 
ATOM   1935 C C   . ASP A 1 248 ? 29.696  -15.271 32.283 1.00 24.65 ? 248 ASP B C   1 
ATOM   1936 O O   . ASP A 1 248 ? 30.460  -14.407 31.833 1.00 22.27 ? 248 ASP B O   1 
ATOM   1937 C CB  . ASP A 1 248 ? 30.342  -17.681 32.186 1.00 26.06 ? 248 ASP B CB  1 
ATOM   1938 C CG  . ASP A 1 248 ? 31.105  -18.827 32.827 1.00 25.61 ? 248 ASP B CG  1 
ATOM   1939 O OD1 . ASP A 1 248 ? 31.812  -18.623 33.839 1.00 27.47 ? 248 ASP B OD1 1 
ATOM   1940 O OD2 . ASP A 1 248 ? 31.003  -19.949 32.293 1.00 32.10 ? 248 ASP B OD2 1 
ATOM   1941 N N   . ILE A 1 249 ? 28.375  -15.246 32.066 1.00 21.18 ? 249 ILE B N   1 
ATOM   1942 C CA  . ILE A 1 249 ? 27.746  -14.201 31.267 1.00 19.71 ? 249 ILE B CA  1 
ATOM   1943 C C   . ILE A 1 249 ? 27.921  -12.851 31.938 1.00 19.13 ? 249 ILE B C   1 
ATOM   1944 O O   . ILE A 1 249 ? 27.989  -11.816 31.264 1.00 18.61 ? 249 ILE B O   1 
ATOM   1945 C CB  . ILE A 1 249 ? 26.255  -14.539 31.037 1.00 23.70 ? 249 ILE B CB  1 
ATOM   1946 C CG1 . ILE A 1 249 ? 26.098  -15.670 30.022 1.00 24.11 ? 249 ILE B CG1 1 
ATOM   1947 C CG2 . ILE A 1 249 ? 25.456  -13.333 30.576 1.00 22.11 ? 249 ILE B CG2 1 
ATOM   1948 C CD1 . ILE A 1 249 ? 24.678  -16.260 30.024 1.00 27.55 ? 249 ILE B CD1 1 
ATOM   1949 N N   . LEU A 1 250 ? 28.023  -12.839 33.266 1.00 17.22 ? 250 LEU B N   1 
ATOM   1950 C CA  . LEU A 1 250 ? 28.258  -11.608 34.008 1.00 16.47 ? 250 LEU B CA  1 
ATOM   1951 C C   . LEU A 1 250 ? 29.725  -11.197 34.009 1.00 21.05 ? 250 LEU B C   1 
ATOM   1952 O O   . LEU A 1 250 ? 30.044  -10.145 34.559 1.00 20.58 ? 250 LEU B O   1 
ATOM   1953 C CB  . LEU A 1 250 ? 27.760  -11.762 35.450 1.00 19.16 ? 250 LEU B CB  1 
ATOM   1954 C CG  . LEU A 1 250 ? 26.239  -11.710 35.663 1.00 17.29 ? 250 LEU B CG  1 
ATOM   1955 C CD1 . LEU A 1 250 ? 25.863  -12.168 37.060 1.00 17.18 ? 250 LEU B CD1 1 
ATOM   1956 C CD2 . LEU A 1 250 ? 25.722  -10.288 35.419 1.00 19.85 ? 250 LEU B CD2 1 
ATOM   1957 N N   . GLY A 1 251 ? 30.613  -12.002 33.422 1.00 21.41 ? 251 GLY B N   1 
ATOM   1958 C CA  . GLY A 1 251 ? 32.038  -11.737 33.417 1.00 20.98 ? 251 GLY B CA  1 
ATOM   1959 C C   . GLY A 1 251 ? 32.446  -10.347 32.959 1.00 20.69 ? 251 GLY B C   1 
ATOM   1960 O O   . GLY A 1 251 ? 33.263  -9.690  33.614 1.00 19.84 ? 251 GLY B O   1 
ATOM   1961 N N   . PRO A 1 252 ? 31.904  -9.864  31.829 1.00 22.80 ? 252 PRO B N   1 
ATOM   1962 C CA  . PRO A 1 252 ? 32.238  -8.486  31.405 1.00 20.70 ? 252 PRO B CA  1 
ATOM   1963 C C   . PRO A 1 252 ? 31.869  -7.409  32.416 1.00 19.67 ? 252 PRO B C   1 
ATOM   1964 O O   . PRO A 1 252 ? 32.666  -6.493  32.643 1.00 18.46 ? 252 PRO B O   1 
ATOM   1965 C CB  . PRO A 1 252 ? 31.461  -8.321  30.092 1.00 26.66 ? 252 PRO B CB  1 
ATOM   1966 C CG  . PRO A 1 252 ? 31.310  -9.724  29.572 1.00 23.64 ? 252 PRO B CG  1 
ATOM   1967 C CD  . PRO A 1 252 ? 31.124  -10.575 30.801 1.00 22.92 ? 252 PRO B CD  1 
ATOM   1968 N N   . LEU A 1 253 ? 30.698  -7.498  33.054 1.00 19.15 ? 253 LEU B N   1 
ATOM   1969 C CA  . LEU A 1 253 ? 30.327  -6.493  34.045 1.00 17.75 ? 253 LEU B CA  1 
ATOM   1970 C C   . LEU A 1 253 ? 31.155  -6.638  35.309 1.00 16.07 ? 253 LEU B C   1 
ATOM   1971 O O   . LEU A 1 253 ? 31.514  -5.642  35.943 1.00 17.39 ? 253 LEU B O   1 
ATOM   1972 C CB  . LEU A 1 253 ? 28.833  -6.594  34.363 1.00 15.58 ? 253 LEU B CB  1 
ATOM   1973 C CG  . LEU A 1 253 ? 27.927  -6.107  33.227 1.00 15.67 ? 253 LEU B CG  1 
ATOM   1974 C CD1 . LEU A 1 253 ? 26.476  -6.471  33.551 1.00 19.78 ? 253 LEU B CD1 1 
ATOM   1975 C CD2 . LEU A 1 253 ? 28.045  -4.598  32.994 1.00 18.97 ? 253 LEU B CD2 1 
ATOM   1976 N N   . SER A 1 254 ? 31.470  -7.876  35.690 1.00 16.56 ? 254 SER B N   1 
ATOM   1977 C CA  . SER A 1 254 ? 32.330  -8.111  36.844 1.00 17.55 ? 254 SER B CA  1 
ATOM   1978 C C   . SER A 1 254 ? 33.718  -7.537  36.611 1.00 18.33 ? 254 SER B C   1 
ATOM   1979 O O   . SER A 1 254 ? 34.317  -6.929  37.507 1.00 19.59 ? 254 SER B O   1 
ATOM   1980 C CB  . SER A 1 254 ? 32.449  -9.615  37.101 1.00 19.77 ? 254 SER B CB  1 
ATOM   1981 O OG  . SER A 1 254 ? 33.198  -9.860  38.271 1.00 26.29 ? 254 SER B OG  1 
ATOM   1982 N N   . ALA A 1 255 ? 34.246  -7.742  35.415 1.00 19.46 ? 255 ALA B N   1 
ATOM   1983 C CA  . ALA A 1 255 ? 35.561  -7.202  35.096 1.00 20.22 ? 255 ALA B CA  1 
ATOM   1984 C C   . ALA A 1 255 ? 35.537  -5.683  35.045 1.00 20.22 ? 255 ALA B C   1 
ATOM   1985 O O   . ALA A 1 255 ? 36.483  -5.027  35.496 1.00 21.72 ? 255 ALA B O   1 
ATOM   1986 C CB  . ALA A 1 255 ? 36.056  -7.778  33.769 1.00 21.48 ? 255 ALA B CB  1 
ATOM   1987 N N   . GLN A 1 256 ? 34.469  -5.103  34.500 1.00 20.72 ? 256 GLN B N   1 
ATOM   1988 C CA  . GLN A 1 256 ? 34.410  -3.648  34.395 1.00 20.85 ? 256 GLN B CA  1 
ATOM   1989 C C   . GLN A 1 256 ? 34.429  -2.995  35.771 1.00 22.23 ? 256 GLN B C   1 
ATOM   1990 O O   . GLN A 1 256 ? 35.109  -1.982  35.980 1.00 23.02 ? 256 GLN B O   1 
ATOM   1991 C CB  . GLN A 1 256 ? 33.169  -3.230  33.611 1.00 24.25 ? 256 GLN B CB  1 
ATOM   1992 C CG  . GLN A 1 256 ? 33.052  -1.720  33.441 1.00 28.20 ? 256 GLN B CG  1 
ATOM   1993 C CD  . GLN A 1 256 ? 31.885  -1.324  32.576 1.00 27.93 ? 256 GLN B CD  1 
ATOM   1994 O OE1 . GLN A 1 256 ? 31.323  -2.156  31.859 1.00 34.31 ? 256 GLN B OE1 1 
ATOM   1995 N NE2 . GLN A 1 256 ? 31.503  -0.054  32.638 1.00 31.43 ? 256 GLN B NE2 1 
ATOM   1996 N N   . THR A 1 257 ? 33.713  -3.575  36.730 1.00 17.73 ? 257 THR B N   1 
ATOM   1997 C CA  . THR A 1 257 ? 33.597  -2.992  38.057 1.00 18.88 ? 257 THR B CA  1 
ATOM   1998 C C   . THR A 1 257 ? 34.667  -3.472  39.016 1.00 19.22 ? 257 THR B C   1 
ATOM   1999 O O   . THR A 1 257 ? 34.894  -2.815  40.041 1.00 20.36 ? 257 THR B O   1 
ATOM   2000 C CB  . THR A 1 257 ? 32.219  -3.296  38.663 1.00 18.43 ? 257 THR B CB  1 
ATOM   2001 O OG1 . THR A 1 257 ? 31.998  -4.722  38.727 1.00 16.99 ? 257 THR B OG1 1 
ATOM   2002 C CG2 . THR A 1 257 ? 31.142  -2.643  37.834 1.00 17.65 ? 257 THR B CG2 1 
ATOM   2003 N N   . GLY A 1 258 ? 35.310  -4.596  38.714 1.00 16.71 ? 258 GLY B N   1 
ATOM   2004 C CA  . GLY A 1 258 ? 36.214  -5.238  39.641 1.00 21.59 ? 258 GLY B CA  1 
ATOM   2005 C C   . GLY A 1 258 ? 35.538  -6.013  40.745 1.00 23.70 ? 258 GLY B C   1 
ATOM   2006 O O   . GLY A 1 258 ? 36.223  -6.477  41.661 1.00 24.63 ? 258 GLY B O   1 
ATOM   2007 N N   . ILE A 1 259 ? 34.216  -6.169  40.697 1.00 18.38 ? 259 ILE B N   1 
ATOM   2008 C CA  . ILE A 1 259 ? 33.466  -6.819  41.767 1.00 21.42 ? 259 ILE B CA  1 
ATOM   2009 C C   . ILE A 1 259 ? 33.086  -8.207  41.278 1.00 17.50 ? 259 ILE B C   1 
ATOM   2010 O O   . ILE A 1 259 ? 32.323  -8.350  40.314 1.00 16.80 ? 259 ILE B O   1 
ATOM   2011 C CB  . ILE A 1 259 ? 32.229  -6.005  42.166 1.00 19.24 ? 259 ILE B CB  1 
ATOM   2012 C CG1 . ILE A 1 259 ? 32.656  -4.642  42.727 1.00 21.34 ? 259 ILE B CG1 1 
ATOM   2013 C CG2 . ILE A 1 259 ? 31.340  -6.806  43.173 1.00 20.03 ? 259 ILE B CG2 1 
ATOM   2014 C CD1 . ILE A 1 259 ? 31.617  -3.582  42.538 1.00 22.72 ? 259 ILE B CD1 1 
ATOM   2015 N N   . ALA A 1 260 ? 33.664  -9.224  41.914 1.00 18.29 ? 260 ALA B N   1 
ATOM   2016 C CA  . ALA A 1 260 ? 33.404  -10.607 41.532 1.00 18.39 ? 260 ALA B CA  1 
ATOM   2017 C C   . ALA A 1 260 ? 31.924  -10.931 41.702 1.00 17.12 ? 260 ALA B C   1 
ATOM   2018 O O   . ALA A 1 260 ? 31.244  -10.376 42.565 1.00 18.33 ? 260 ALA B O   1 
ATOM   2019 C CB  . ALA A 1 260 ? 34.239  -11.554 42.387 1.00 20.19 ? 260 ALA B CB  1 
ATOM   2020 N N   . VAL A 1 261 ? 31.426  -11.858 40.876 1.00 16.93 ? 261 VAL B N   1 
ATOM   2021 C CA  . VAL A 1 261 ? 30.002  -12.199 40.938 1.00 15.65 ? 261 VAL B CA  1 
ATOM   2022 C C   . VAL A 1 261 ? 29.622  -12.684 42.330 1.00 18.22 ? 261 VAL B C   1 
ATOM   2023 O O   . VAL A 1 261 ? 28.621  -12.236 42.899 1.00 16.97 ? 261 VAL B O   1 
ATOM   2024 C CB  . VAL A 1 261 ? 29.642  -13.227 39.852 1.00 16.93 ? 261 VAL B CB  1 
ATOM   2025 C CG1 . VAL A 1 261 ? 28.200  -13.797 40.088 1.00 18.69 ? 261 VAL B CG1 1 
ATOM   2026 C CG2 . VAL A 1 261 ? 29.789  -12.587 38.471 1.00 17.77 ? 261 VAL B CG2 1 
ATOM   2027 N N   . LEU A 1 262 ? 30.440  -13.552 42.933 1.00 19.11 ? 262 LEU B N   1 
ATOM   2028 C CA  . LEU A 1 262 ? 30.102  -14.086 44.251 1.00 17.77 ? 262 LEU B CA  1 
ATOM   2029 C C   . LEU A 1 262 ? 30.250  -13.046 45.353 1.00 19.95 ? 262 LEU B C   1 
ATOM   2030 O O   . LEU A 1 262 ? 29.719  -13.228 46.451 1.00 18.91 ? 262 LEU B O   1 
ATOM   2031 C CB  . LEU A 1 262 ? 30.969  -15.318 44.537 1.00 21.44 ? 262 LEU B CB  1 
ATOM   2032 C CG  . LEU A 1 262 ? 30.572  -16.491 43.648 1.00 22.73 ? 262 LEU B CG  1 
ATOM   2033 C CD1 . LEU A 1 262 ? 31.381  -17.712 44.038 1.00 26.17 ? 262 LEU B CD1 1 
ATOM   2034 C CD2 . LEU A 1 262 ? 29.060  -16.780 43.733 1.00 24.17 ? 262 LEU B CD2 1 
ATOM   2035 N N   . ASP A 1 263 ? 30.945  -11.945 45.073 1.00 17.82 ? 263 ASP B N   1 
ATOM   2036 C CA  . ASP A 1 263 ? 30.952  -10.788 45.958 1.00 18.90 ? 263 ASP B CA  1 
ATOM   2037 C C   . ASP A 1 263 ? 29.631  -10.020 45.833 1.00 16.22 ? 263 ASP B C   1 
ATOM   2038 O O   . ASP A 1 263 ? 28.949  -9.743  46.835 1.00 17.67 ? 263 ASP B O   1 
ATOM   2039 C CB  . ASP A 1 263 ? 32.202  -9.955  45.578 1.00 17.50 ? 263 ASP B CB  1 
ATOM   2040 C CG  . ASP A 1 263 ? 32.374  -8.659  46.356 1.00 21.64 ? 263 ASP B CG  1 
ATOM   2041 O OD1 . ASP A 1 263 ? 31.486  -8.212  47.085 1.00 21.46 ? 263 ASP B OD1 1 
ATOM   2042 O OD2 . ASP A 1 263 ? 33.463  -8.056  46.211 1.00 21.85 ? 263 ASP B OD2 1 
ATOM   2043 N N   . MET A 1 264 ? 29.229  -9.717  44.599 1.00 16.24 ? 264 MET B N   1 
ATOM   2044 C CA  . MET A 1 264 ? 27.928  -9.099  44.358 1.00 16.32 ? 264 MET B CA  1 
ATOM   2045 C C   . MET A 1 264 ? 26.778  -9.951  44.891 1.00 16.09 ? 264 MET B C   1 
ATOM   2046 O O   . MET A 1 264 ? 25.789  -9.403  45.385 1.00 19.24 ? 264 MET B O   1 
ATOM   2047 C CB  . MET A 1 264 ? 27.751  -8.805  42.858 1.00 16.10 ? 264 MET B CB  1 
ATOM   2048 C CG  . MET A 1 264 ? 26.515  -7.915  42.580 1.00 16.44 ? 264 MET B CG  1 
ATOM   2049 S SD  . MET A 1 264 ? 26.664  -6.258  43.254 1.00 19.47 ? 264 MET B SD  1 
ATOM   2050 C CE  . MET A 1 264 ? 27.505  -5.423  41.897 1.00 16.75 ? 264 MET B CE  1 
ATOM   2051 N N   . CYS A 1 265 ? 26.883  -11.286 44.803 1.00 16.82 ? 265 CYS B N   1 
ATOM   2052 C CA  . CYS A 1 265 ? 25.797  -12.124 45.320 1.00 17.81 ? 265 CYS B CA  1 
ATOM   2053 C C   . CYS A 1 265 ? 25.588  -11.915 46.811 1.00 19.15 ? 265 CYS B C   1 
ATOM   2054 O O   . CYS A 1 265 ? 24.469  -12.108 47.318 1.00 18.47 ? 265 CYS B O   1 
ATOM   2055 C CB  . CYS A 1 265 ? 26.056  -13.599 44.998 1.00 14.93 ? 265 CYS B CB  1 
ATOM   2056 S SG  . CYS A 1 265 ? 25.799  -14.080 43.280 1.00 19.12 ? 265 CYS B SG  1 
ATOM   2057 N N   . ALA A 1 266 ? 26.636  -11.514 47.540 1.00 19.89 ? 266 ALA B N   1 
ATOM   2058 C CA  . ALA A 1 266 ? 26.457  -11.280 48.969 1.00 20.18 ? 266 ALA B CA  1 
ATOM   2059 C C   . ALA A 1 266 ? 25.655  -10.010 49.215 1.00 22.33 ? 266 ALA B C   1 
ATOM   2060 O O   . ALA A 1 266 ? 24.887  -9.940  50.183 1.00 22.08 ? 266 ALA B O   1 
ATOM   2061 C CB  . ALA A 1 266 ? 27.800  -11.212 49.690 1.00 20.66 ? 266 ALA B CB  1 
ATOM   2062 N N   . SER A 1 267 ? 25.819  -9.007  48.347 1.00 16.95 ? 267 SER B N   1 
ATOM   2063 C CA  . SER A 1 267 ? 24.925  -7.851  48.370 1.00 19.35 ? 267 SER B CA  1 
ATOM   2064 C C   . SER A 1 267 ? 23.491  -8.279  48.119 1.00 19.18 ? 267 SER B C   1 
ATOM   2065 O O   . SER A 1 267 ? 22.564  -7.855  48.829 1.00 19.85 ? 267 SER B O   1 
ATOM   2066 C CB  . SER A 1 267 ? 25.346  -6.826  47.308 1.00 19.03 ? 267 SER B CB  1 
ATOM   2067 O OG  . SER A 1 267 ? 26.533  -6.142  47.660 1.00 23.25 ? 267 SER B OG  1 
ATOM   2068 N N   . LEU A 1 268 ? 23.281  -9.099  47.085 1.00 19.60 ? 268 LEU B N   1 
ATOM   2069 C CA  . LEU A 1 268 ? 21.922  -9.469  46.717 1.00 19.40 ? 268 LEU B CA  1 
ATOM   2070 C C   . LEU A 1 268 ? 21.282  -10.314 47.807 1.00 21.85 ? 268 LEU B C   1 
ATOM   2071 O O   . LEU A 1 268 ? 20.098  -10.135 48.123 1.00 18.99 ? 268 LEU B O   1 
ATOM   2072 C CB  . LEU A 1 268 ? 21.914  -10.195 45.372 1.00 17.81 ? 268 LEU B CB  1 
ATOM   2073 C CG  . LEU A 1 268 ? 20.573  -10.733 44.836 1.00 18.55 ? 268 LEU B CG  1 
ATOM   2074 C CD1 . LEU A 1 268 ? 19.475  -9.653  44.850 1.00 18.72 ? 268 LEU B CD1 1 
ATOM   2075 C CD2 . LEU A 1 268 ? 20.759  -11.285 43.429 1.00 18.38 ? 268 LEU B CD2 1 
ATOM   2076 N N   . LYS A 1 269 ? 22.060  -11.210 48.422 1.00 20.31 ? 269 LYS B N   1 
ATOM   2077 C CA  . LYS A 1 269 ? 21.512  -11.990 49.528 1.00 19.64 ? 269 LYS B CA  1 
ATOM   2078 C C   . LYS A 1 269 ? 21.073  -11.082 50.677 1.00 22.06 ? 269 LYS B C   1 
ATOM   2079 O O   . LYS A 1 269 ? 19.989  -11.269 51.241 1.00 21.22 ? 269 LYS B O   1 
ATOM   2080 C CB  . LYS A 1 269 ? 22.528  -13.041 49.994 1.00 23.55 ? 269 LYS B CB  1 
ATOM   2081 C CG  . LYS A 1 269 ? 22.123  -13.716 51.302 1.00 28.89 ? 269 LYS B CG  1 
ATOM   2082 C CD  . LYS A 1 269 ? 23.240  -14.579 51.899 1.00 29.73 ? 269 LYS B CD  1 
ATOM   2083 C CE  . LYS A 1 269 ? 23.920  -15.424 50.836 1.00 26.08 ? 269 LYS B CE  1 
ATOM   2084 N NZ  . LYS A 1 269 ? 24.970  -16.325 51.412 1.00 26.83 ? 269 LYS B NZ  1 
ATOM   2085 N N   . GLU A 1 270 ? 21.882  -10.065 51.010 1.00 23.93 ? 270 GLU B N   1 
ATOM   2086 C CA  . GLU A 1 270 ? 21.523  -9.137  52.080 1.00 22.66 ? 270 GLU B CA  1 
ATOM   2087 C C   . GLU A 1 270 ? 20.291  -8.316  51.710 1.00 23.64 ? 270 GLU B C   1 
ATOM   2088 O O   . GLU A 1 270 ? 19.436  -8.041  52.562 1.00 22.78 ? 270 GLU B O   1 
ATOM   2089 C CB  . GLU A 1 270 ? 22.708  -8.214  52.385 1.00 24.61 ? 270 GLU B CB  1 
ATOM   2090 C CG  . GLU A 1 270 ? 22.475  -7.164  53.452 1.00 34.18 ? 270 GLU B CG  1 
ATOM   2091 C CD  . GLU A 1 270 ? 23.775  -6.721  54.130 1.00 39.09 ? 270 GLU B CD  1 
ATOM   2092 O OE1 . GLU A 1 270 ? 24.858  -7.217  53.745 1.00 35.98 ? 270 GLU B OE1 1 
ATOM   2093 O OE2 . GLU A 1 270 ? 23.715  -5.844  55.021 1.00 42.36 ? 270 GLU B OE2 1 
ATOM   2094 N N   . LEU A 1 271 ? 20.178  -7.915  50.443 1.00 17.59 ? 271 LEU B N   1 
ATOM   2095 C CA  . LEU A 1 271 ? 19.010  -7.138  50.040 1.00 19.97 ? 271 LEU B CA  1 
ATOM   2096 C C   . LEU A 1 271 ? 17.748  -7.988  50.095 1.00 20.45 ? 271 LEU B C   1 
ATOM   2097 O O   . LEU A 1 271 ? 16.677  -7.494  50.458 1.00 20.96 ? 271 LEU B O   1 
ATOM   2098 C CB  . LEU A 1 271 ? 19.213  -6.579  48.636 1.00 20.48 ? 271 LEU B CB  1 
ATOM   2099 C CG  . LEU A 1 271 ? 20.283  -5.485  48.587 1.00 18.72 ? 271 LEU B CG  1 
ATOM   2100 C CD1 . LEU A 1 271 ? 20.752  -5.287  47.166 1.00 21.29 ? 271 LEU B CD1 1 
ATOM   2101 C CD2 . LEU A 1 271 ? 19.768  -4.194  49.196 1.00 25.69 ? 271 LEU B CD2 1 
ATOM   2102 N N   . LEU A 1 272 ? 17.855  -9.269  49.735 1.00 19.45 ? 272 LEU B N   1 
ATOM   2103 C CA  . LEU A 1 272 ? 16.688  -10.146 49.802 1.00 21.41 ? 272 LEU B CA  1 
ATOM   2104 C C   . LEU A 1 272 ? 16.234  -10.350 51.242 1.00 25.36 ? 272 LEU B C   1 
ATOM   2105 O O   . LEU A 1 272 ? 15.027  -10.329 51.527 1.00 23.57 ? 272 LEU B O   1 
ATOM   2106 C CB  . LEU A 1 272 ? 17.004  -11.489 49.149 1.00 19.93 ? 272 LEU B CB  1 
ATOM   2107 C CG  . LEU A 1 272 ? 17.080  -11.473 47.624 1.00 20.42 ? 272 LEU B CG  1 
ATOM   2108 C CD1 . LEU A 1 272 ? 17.473  -12.830 47.109 1.00 22.51 ? 272 LEU B CD1 1 
ATOM   2109 C CD2 . LEU A 1 272 ? 15.752  -11.063 47.034 1.00 24.33 ? 272 LEU B CD2 1 
ATOM   2110 N N   . GLN A 1 273 ? 17.189  -10.519 52.163 1.00 24.02 ? 273 GLN B N   1 
ATOM   2111 C CA  . GLN A 1 273 ? 16.875  -10.889 53.541 1.00 25.62 ? 273 GLN B CA  1 
ATOM   2112 C C   . GLN A 1 273 ? 16.498  -9.688  54.400 1.00 28.35 ? 273 GLN B C   1 
ATOM   2113 O O   . GLN A 1 273 ? 15.641  -9.813  55.281 1.00 27.10 ? 273 GLN B O   1 
ATOM   2114 C CB  . GLN A 1 273 ? 18.050  -11.645 54.171 1.00 27.40 ? 273 GLN B CB  1 
ATOM   2115 C CG  . GLN A 1 273 ? 18.276  -13.008 53.527 1.00 26.52 ? 273 GLN B CG  1 
ATOM   2116 C CD  . GLN A 1 273 ? 19.571  -13.705 53.950 1.00 30.63 ? 273 GLN B CD  1 
ATOM   2117 O OE1 . GLN A 1 273 ? 20.566  -13.064 54.283 1.00 33.25 ? 273 GLN B OE1 1 
ATOM   2118 N NE2 . GLN A 1 273 ? 19.565  -15.028 53.897 1.00 33.06 ? 273 GLN B NE2 1 
ATOM   2119 N N   . ASN A 1 274 ? 17.113  -8.522  54.168 1.00 25.51 ? 274 ASN B N   1 
ATOM   2120 C CA  . ASN A 1 274 ? 16.883  -7.352  55.010 1.00 25.84 ? 274 ASN B CA  1 
ATOM   2121 C C   . ASN A 1 274 ? 16.222  -6.187  54.282 1.00 28.07 ? 274 ASN B C   1 
ATOM   2122 O O   . ASN A 1 274 ? 15.930  -5.166  54.919 1.00 30.24 ? 274 ASN B O   1 
ATOM   2123 C CB  . ASN A 1 274 ? 18.208  -6.862  55.615 1.00 30.60 ? 274 ASN B CB  1 
ATOM   2124 C CG  . ASN A 1 274 ? 18.901  -7.925  56.479 1.00 31.37 ? 274 ASN B CG  1 
ATOM   2125 O OD1 . ASN A 1 274 ? 20.104  -8.158  56.336 1.00 40.15 ? 274 ASN B OD1 1 
ATOM   2126 N ND2 . ASN A 1 274 ? 18.146  -8.586  57.344 1.00 32.35 ? 274 ASN B ND2 1 
ATOM   2127 N N   . GLY A 1 275 ? 16.006  -6.286  52.977 1.00 26.30 ? 275 GLY B N   1 
ATOM   2128 C CA  . GLY A 1 275 ? 15.359  -5.209  52.256 1.00 22.74 ? 275 GLY B CA  1 
ATOM   2129 C C   . GLY A 1 275 ? 16.288  -4.033  52.043 1.00 27.33 ? 275 GLY B C   1 
ATOM   2130 O O   . GLY A 1 275 ? 17.490  -4.113  52.273 1.00 25.48 ? 275 GLY B O   1 
ATOM   2131 N N   . MET A 1 276 ? 15.709  -2.912  51.616 1.00 26.14 ? 276 MET B N   1 
ATOM   2132 C CA  . MET A 1 276 ? 16.512  -1.755  51.239 1.00 31.52 ? 276 MET B CA  1 
ATOM   2133 C C   . MET A 1 276 ? 16.586  -0.679  52.316 1.00 29.76 ? 276 MET B C   1 
ATOM   2134 O O   . MET A 1 276 ? 17.324  0.298   52.138 1.00 34.17 ? 276 MET B O   1 
ATOM   2135 C CB  . MET A 1 276 ? 15.968  -1.141  49.948 1.00 32.44 ? 276 MET B CB  1 
ATOM   2136 C CG  . MET A 1 276 ? 16.547  -1.760  48.701 1.00 29.80 ? 276 MET B CG  1 
ATOM   2137 S SD  . MET A 1 276 ? 16.119  -0.879  47.180 1.00 36.69 ? 276 MET B SD  1 
ATOM   2138 C CE  . MET A 1 276 ? 15.706  -2.329  46.203 1.00 24.62 ? 276 MET B CE  1 
ATOM   2139 N N   . ASN A 1 277 ? 15.856  -0.828  53.422 1.00 37.24 ? 277 ASN B N   1 
ATOM   2140 C CA  . ASN A 1 277 ? 15.829  0.180   54.488 1.00 36.90 ? 277 ASN B CA  1 
ATOM   2141 C C   . ASN A 1 277 ? 15.496  1.562   53.929 1.00 37.83 ? 277 ASN B C   1 
ATOM   2142 O O   . ASN A 1 277 ? 16.170  2.556   54.217 1.00 33.60 ? 277 ASN B O   1 
ATOM   2143 C CB  . ASN A 1 277 ? 17.155  0.217   55.250 1.00 40.50 ? 277 ASN B CB  1 
ATOM   2144 C CG  . ASN A 1 277 ? 17.308  -0.941  56.214 1.00 46.06 ? 277 ASN B CG  1 
ATOM   2145 O OD1 . ASN A 1 277 ? 16.572  -1.048  57.202 1.00 47.16 ? 277 ASN B OD1 1 
ATOM   2146 N ND2 . ASN A 1 277 ? 18.273  -1.814  55.937 1.00 45.35 ? 277 ASN B ND2 1 
ATOM   2147 N N   . GLY A 1 278 ? 14.455  1.617   53.099 1.00 33.69 ? 278 GLY B N   1 
ATOM   2148 C CA  . GLY A 1 278 ? 13.987  2.885   52.568 1.00 32.42 ? 278 GLY B CA  1 
ATOM   2149 C C   . GLY A 1 278 ? 14.919  3.590   51.613 1.00 35.11 ? 278 GLY B C   1 
ATOM   2150 O O   . GLY A 1 278 ? 14.675  4.756   51.280 1.00 30.91 ? 278 GLY B O   1 
ATOM   2151 N N   . ARG A 1 279 ? 15.990  2.940   51.167 1.00 31.06 ? 279 ARG B N   1 
ATOM   2152 C CA  . ARG A 1 279 ? 16.839  3.506   50.133 1.00 23.71 ? 279 ARG B CA  1 
ATOM   2153 C C   . ARG A 1 279 ? 16.392  2.988   48.777 1.00 22.60 ? 279 ARG B C   1 
ATOM   2154 O O   . ARG A 1 279 ? 15.595  2.053   48.670 1.00 27.66 ? 279 ARG B O   1 
ATOM   2155 C CB  . ARG A 1 279 ? 18.312  3.176   50.385 1.00 27.75 ? 279 ARG B CB  1 
ATOM   2156 C CG  . ARG A 1 279 ? 18.752  3.427   51.824 1.00 30.44 ? 279 ARG B CG  1 
ATOM   2157 C CD  . ARG A 1 279 ? 20.266  3.414   51.986 1.00 27.98 ? 279 ARG B CD  1 
ATOM   2158 N NE  . ARG A 1 279 ? 20.939  4.413   51.162 1.00 30.25 ? 279 ARG B NE  1 
ATOM   2159 C CZ  . ARG A 1 279 ? 22.238  4.680   51.232 1.00 25.86 ? 279 ARG B CZ  1 
ATOM   2160 N NH1 . ARG A 1 279 ? 23.019  4.079   52.117 1.00 32.98 ? 279 ARG B NH1 1 
ATOM   2161 N NH2 . ARG A 1 279 ? 22.765  5.565   50.393 1.00 28.24 ? 279 ARG B NH2 1 
ATOM   2162 N N   . THR A 1 280 ? 16.920  3.605   47.732 1.00 22.09 ? 280 THR B N   1 
ATOM   2163 C CA  . THR A 1 280 ? 16.660  3.180   46.368 1.00 17.90 ? 280 THR B CA  1 
ATOM   2164 C C   . THR A 1 280 ? 17.956  2.776   45.686 1.00 18.14 ? 280 THR B C   1 
ATOM   2165 O O   . THR A 1 280 ? 19.063  3.116   46.117 1.00 20.97 ? 280 THR B O   1 
ATOM   2166 C CB  . THR A 1 280 ? 15.981  4.287   45.541 1.00 18.48 ? 280 THR B CB  1 
ATOM   2167 O OG1 . THR A 1 280 ? 16.828  5.435   45.508 1.00 20.63 ? 280 THR B OG1 1 
ATOM   2168 C CG2 . THR A 1 280 ? 14.604  4.652   46.126 1.00 21.22 ? 280 THR B CG2 1 
ATOM   2169 N N   . ILE A 1 281 ? 17.798  2.050   44.591 1.00 17.97 ? 281 ILE B N   1 
ATOM   2170 C CA  . ILE A 1 281 ? 18.908  1.669   43.725 1.00 16.64 ? 281 ILE B CA  1 
ATOM   2171 C C   . ILE A 1 281 ? 18.495  2.042   42.317 1.00 15.86 ? 281 ILE B C   1 
ATOM   2172 O O   . ILE A 1 281 ? 17.496  1.521   41.808 1.00 16.86 ? 281 ILE B O   1 
ATOM   2173 C CB  . ILE A 1 281 ? 19.236  0.168   43.822 1.00 16.82 ? 281 ILE B CB  1 
ATOM   2174 C CG1 . ILE A 1 281 ? 19.697  -0.191  45.242 1.00 16.27 ? 281 ILE B CG1 1 
ATOM   2175 C CG2 . ILE A 1 281 ? 20.268  -0.235  42.754 1.00 19.98 ? 281 ILE B CG2 1 
ATOM   2176 C CD1 . ILE A 1 281 ? 19.888  -1.686  45.472 1.00 19.58 ? 281 ILE B CD1 1 
ATOM   2177 N N   . LEU A 1 282 ? 19.250  2.945   41.686 1.00 17.02 ? 282 LEU B N   1 
ATOM   2178 C CA  . LEU A 1 282 ? 18.882  3.456   40.369 1.00 18.04 ? 282 LEU B CA  1 
ATOM   2179 C C   . LEU A 1 282 ? 17.417  3.912   40.365 1.00 19.82 ? 282 LEU B C   1 
ATOM   2180 O O   . LEU A 1 282 ? 16.654  3.665   39.423 1.00 19.07 ? 282 LEU B O   1 
ATOM   2181 C CB  . LEU A 1 282 ? 19.156  2.409   39.287 1.00 15.35 ? 282 LEU B CB  1 
ATOM   2182 C CG  . LEU A 1 282 ? 20.654  2.228   38.978 1.00 19.70 ? 282 LEU B CG  1 
ATOM   2183 C CD1 . LEU A 1 282 ? 20.869  1.101   38.004 1.00 19.59 ? 282 LEU B CD1 1 
ATOM   2184 C CD2 . LEU A 1 282 ? 21.257  3.508   38.399 1.00 21.94 ? 282 LEU B CD2 1 
ATOM   2185 N N   . GLY A 1 283 ? 17.007  4.540   41.463 1.00 19.89 ? 283 GLY B N   1 
ATOM   2186 C CA  . GLY A 1 283 ? 15.682  5.119   41.554 1.00 23.33 ? 283 GLY B CA  1 
ATOM   2187 C C   . GLY A 1 283 ? 14.563  4.142   41.821 1.00 22.26 ? 283 GLY B C   1 
ATOM   2188 O O   . GLY A 1 283 ? 13.391  4.559   41.869 1.00 22.84 ? 283 GLY B O   1 
ATOM   2189 N N   . SER A 1 284 ? 14.869  2.865   42.005 1.00 18.38 ? 284 SER B N   1 
ATOM   2190 C CA  . SER A 1 284 ? 13.845  1.869   42.288 1.00 19.77 ? 284 SER B CA  1 
ATOM   2191 C C   . SER A 1 284 ? 13.895  1.455   43.753 1.00 19.87 ? 284 SER B C   1 
ATOM   2192 O O   . SER A 1 284 ? 14.974  1.347   44.346 1.00 16.26 ? 284 SER B O   1 
ATOM   2193 C CB  . SER A 1 284 ? 14.016  0.638   41.393 1.00 18.73 ? 284 SER B CB  1 
ATOM   2194 O OG  . SER A 1 284 ? 12.991  -0.293  41.686 1.00 25.46 ? 284 SER B OG  1 
ATOM   2195 N N   . ALA A 1 285 ? 12.720  1.224   44.342 1.00 19.54 ? 285 ALA B N   1 
ATOM   2196 C CA  . ALA A 1 285 ? 12.638  0.717   45.705 1.00 20.34 ? 285 ALA B CA  1 
ATOM   2197 C C   . ALA A 1 285 ? 12.448  -0.789  45.736 1.00 21.97 ? 285 ALA B C   1 
ATOM   2198 O O   . ALA A 1 285 ? 12.250  -1.361  46.816 1.00 24.02 ? 285 ALA B O   1 
ATOM   2199 C CB  . ALA A 1 285 ? 11.503  1.410   46.482 1.00 21.07 ? 285 ALA B CB  1 
ATOM   2200 N N   . LEU A 1 286 ? 12.510  -1.442  44.581 1.00 20.05 ? 286 LEU B N   1 
ATOM   2201 C CA  . LEU A 1 286 ? 12.506  -2.894  44.509 1.00 18.00 ? 286 LEU B CA  1 
ATOM   2202 C C   . LEU A 1 286 ? 13.614  -3.355  43.564 1.00 19.07 ? 286 LEU B C   1 
ATOM   2203 O O   . LEU A 1 286 ? 14.238  -2.557  42.865 1.00 18.34 ? 286 LEU B O   1 
ATOM   2204 C CB  . LEU A 1 286 ? 11.136  -3.408  44.072 1.00 25.19 ? 286 LEU B CB  1 
ATOM   2205 C CG  . LEU A 1 286 ? 10.394  -2.766  42.902 1.00 24.99 ? 286 LEU B CG  1 
ATOM   2206 C CD1 . LEU A 1 286 ? 11.081  -3.072  41.594 1.00 28.93 ? 286 LEU B CD1 1 
ATOM   2207 C CD2 . LEU A 1 286 ? 8.921   -3.152  42.880 1.00 23.55 ? 286 LEU B CD2 1 
ATOM   2208 N N   . LEU A 1 287 ? 13.861  -4.664  43.541 1.00 19.43 ? 287 LEU B N   1 
ATOM   2209 C CA  . LEU A 1 287 ? 14.959  -5.211  42.754 1.00 17.24 ? 287 LEU B CA  1 
ATOM   2210 C C   . LEU A 1 287 ? 14.463  -5.474  41.337 1.00 20.87 ? 287 LEU B C   1 
ATOM   2211 O O   . LEU A 1 287 ? 13.541  -6.277  41.137 1.00 22.34 ? 287 LEU B O   1 
ATOM   2212 C CB  . LEU A 1 287 ? 15.479  -6.483  43.408 1.00 19.69 ? 287 LEU B CB  1 
ATOM   2213 C CG  . LEU A 1 287 ? 15.991  -6.281  44.839 1.00 21.32 ? 287 LEU B CG  1 
ATOM   2214 C CD1 . LEU A 1 287 ? 16.336  -7.640  45.444 1.00 22.02 ? 287 LEU B CD1 1 
ATOM   2215 C CD2 . LEU A 1 287 ? 17.201  -5.374  44.860 1.00 23.99 ? 287 LEU B CD2 1 
ATOM   2216 N N   . GLU A 1 288 ? 15.061  -4.789  40.364 1.00 19.22 ? 288 GLU B N   1 
ATOM   2217 C CA  . GLU A 1 288 ? 14.618  -4.848  38.976 1.00 21.60 ? 288 GLU B CA  1 
ATOM   2218 C C   . GLU A 1 288 ? 15.243  -6.036  38.266 1.00 18.65 ? 288 GLU B C   1 
ATOM   2219 O O   . GLU A 1 288 ? 16.451  -6.269  38.387 1.00 16.49 ? 288 GLU B O   1 
ATOM   2220 C CB  . GLU A 1 288 ? 14.980  -3.549  38.254 1.00 20.53 ? 288 GLU B CB  1 
ATOM   2221 C CG  . GLU A 1 288 ? 14.354  -2.316  38.903 1.00 23.36 ? 288 GLU B CG  1 
ATOM   2222 C CD  . GLU A 1 288 ? 12.838  -2.250  38.693 1.00 32.35 ? 288 GLU B CD  1 
ATOM   2223 O OE1 . GLU A 1 288 ? 12.297  -3.118  37.971 1.00 30.81 ? 288 GLU B OE1 1 
ATOM   2224 O OE2 . GLU A 1 288 ? 12.186  -1.342  39.269 1.00 35.07 ? 288 GLU B OE2 1 
ATOM   2225 N N   . ASP A 1 289 ? 14.427  -6.791  37.517 1.00 19.83 ? 289 ASP B N   1 
ATOM   2226 C CA  . ASP A 1 289 ? 14.930  -7.996  36.863 1.00 19.74 ? 289 ASP B CA  1 
ATOM   2227 C C   . ASP A 1 289 ? 14.690  -8.012  35.354 1.00 17.35 ? 289 ASP B C   1 
ATOM   2228 O O   . ASP A 1 289 ? 14.816  -9.066  34.732 1.00 19.36 ? 289 ASP B O   1 
ATOM   2229 C CB  . ASP A 1 289 ? 14.355  -9.262  37.524 1.00 19.90 ? 289 ASP B CB  1 
ATOM   2230 C CG  . ASP A 1 289 ? 12.924  -9.596  37.091 1.00 21.70 ? 289 ASP B CG  1 
ATOM   2231 O OD1 . ASP A 1 289 ? 12.190  -8.708  36.624 1.00 19.25 ? 289 ASP B OD1 1 
ATOM   2232 O OD2 . ASP A 1 289 ? 12.522  -10.776 37.252 1.00 21.40 ? 289 ASP B OD2 1 
ATOM   2233 N N   . GLU A 1 290 ? 14.390  -6.871  34.735 1.00 18.35 ? 290 GLU B N   1 
ATOM   2234 C CA  . GLU A 1 290 ? 14.158  -6.847  33.294 1.00 19.72 ? 290 GLU B CA  1 
ATOM   2235 C C   . GLU A 1 290 ? 15.269  -6.123  32.514 1.00 19.60 ? 290 GLU B C   1 
ATOM   2236 O O   . GLU A 1 290 ? 15.031  -5.673  31.389 1.00 21.10 ? 290 GLU B O   1 
ATOM   2237 C CB  . GLU A 1 290 ? 12.786  -6.237  33.013 1.00 19.91 ? 290 GLU B CB  1 
ATOM   2238 C CG  . GLU A 1 290 ? 11.642  -7.081  33.612 1.00 20.67 ? 290 GLU B CG  1 
ATOM   2239 C CD  . GLU A 1 290 ? 10.421  -7.215  32.711 1.00 22.37 ? 290 GLU B CD  1 
ATOM   2240 O OE1 . GLU A 1 290 ? 10.317  -6.476  31.723 1.00 21.71 ? 290 GLU B OE1 1 
ATOM   2241 O OE2 . GLU A 1 290 ? 9.528   -8.041  33.003 1.00 20.38 ? 290 GLU B OE2 1 
ATOM   2242 N N   . PHE A 1 291 ? 16.476  -6.018  33.077 1.00 18.95 ? 291 PHE B N   1 
ATOM   2243 C CA  . PHE A 1 291 ? 17.680  -5.604  32.344 1.00 19.55 ? 291 PHE B CA  1 
ATOM   2244 C C   . PHE A 1 291 ? 18.615  -6.790  32.187 1.00 18.21 ? 291 PHE B C   1 
ATOM   2245 O O   . PHE A 1 291 ? 19.070  -7.348  33.190 1.00 18.05 ? 291 PHE B O   1 
ATOM   2246 C CB  . PHE A 1 291 ? 18.440  -4.510  33.083 1.00 21.35 ? 291 PHE B CB  1 
ATOM   2247 C CG  . PHE A 1 291 ? 17.701  -3.239  33.175 1.00 19.71 ? 291 PHE B CG  1 
ATOM   2248 C CD1 . PHE A 1 291 ? 17.678  -2.366  32.104 1.00 23.70 ? 291 PHE B CD1 1 
ATOM   2249 C CD2 . PHE A 1 291 ? 17.011  -2.923  34.325 1.00 21.67 ? 291 PHE B CD2 1 
ATOM   2250 C CE1 . PHE A 1 291 ? 16.966  -1.166  32.197 1.00 27.77 ? 291 PHE B CE1 1 
ATOM   2251 C CE2 . PHE A 1 291 ? 16.294  -1.734  34.423 1.00 25.84 ? 291 PHE B CE2 1 
ATOM   2252 C CZ  . PHE A 1 291 ? 16.278  -0.855  33.355 1.00 27.60 ? 291 PHE B CZ  1 
ATOM   2253 N N   . THR A 1 292 ? 18.955  -7.141  30.953 1.00 19.08 ? 292 THR B N   1 
ATOM   2254 C CA  . THR A 1 292 ? 19.911  -8.218  30.767 1.00 19.53 ? 292 THR B CA  1 
ATOM   2255 C C   . THR A 1 292 ? 21.331  -7.695  30.931 1.00 20.15 ? 292 THR B C   1 
ATOM   2256 O O   . THR A 1 292 ? 21.568  -6.489  30.865 1.00 21.53 ? 292 THR B O   1 
ATOM   2257 C CB  . THR A 1 292 ? 19.774  -8.843  29.383 1.00 23.72 ? 292 THR B CB  1 
ATOM   2258 O OG1 . THR A 1 292 ? 20.083  -7.859  28.394 1.00 21.86 ? 292 THR B OG1 1 
ATOM   2259 C CG2 . THR A 1 292 ? 18.362  -9.386  29.152 1.00 21.66 ? 292 THR B CG2 1 
ATOM   2260 N N   . PRO A 1 293 ? 22.298  -8.591  31.145 1.00 17.14 ? 293 PRO B N   1 
ATOM   2261 C CA  . PRO A 1 293 ? 23.703  -8.167  31.085 1.00 19.63 ? 293 PRO B CA  1 
ATOM   2262 C C   . PRO A 1 293 ? 24.032  -7.398  29.817 1.00 21.18 ? 293 PRO B C   1 
ATOM   2263 O O   . PRO A 1 293 ? 24.698  -6.357  29.884 1.00 21.63 ? 293 PRO B O   1 
ATOM   2264 C CB  . PRO A 1 293 ? 24.447  -9.507  31.169 1.00 18.37 ? 293 PRO B CB  1 
ATOM   2265 C CG  . PRO A 1 293 ? 23.554  -10.348 32.053 1.00 18.32 ? 293 PRO B CG  1 
ATOM   2266 C CD  . PRO A 1 293 ? 22.161  -9.981  31.623 1.00 19.90 ? 293 PRO B CD  1 
ATOM   2267 N N   . PHE A 1 294 ? 23.555  -7.861  28.658 1.00 23.06 ? 294 PHE B N   1 
ATOM   2268 C CA  . PHE A 1 294 ? 23.815  -7.137  27.416 1.00 27.73 ? 294 PHE B CA  1 
ATOM   2269 C C   . PHE A 1 294 ? 23.154  -5.763  27.413 1.00 26.02 ? 294 PHE B C   1 
ATOM   2270 O O   . PHE A 1 294 ? 23.731  -4.797  26.895 1.00 25.31 ? 294 PHE B O   1 
ATOM   2271 C CB  . PHE A 1 294 ? 23.350  -7.949  26.207 1.00 31.23 ? 294 PHE B CB  1 
ATOM   2272 C CG  . PHE A 1 294 ? 23.584  -7.248  24.890 1.00 38.18 ? 294 PHE B CG  1 
ATOM   2273 C CD1 . PHE A 1 294 ? 24.855  -7.198  24.330 1.00 41.29 ? 294 PHE B CD1 1 
ATOM   2274 C CD2 . PHE A 1 294 ? 22.542  -6.615  24.226 1.00 40.85 ? 294 PHE B CD2 1 
ATOM   2275 C CE1 . PHE A 1 294 ? 25.077  -6.542  23.122 1.00 44.02 ? 294 PHE B CE1 1 
ATOM   2276 C CE2 . PHE A 1 294 ? 22.760  -5.957  23.017 1.00 40.20 ? 294 PHE B CE2 1 
ATOM   2277 C CZ  . PHE A 1 294 ? 24.023  -5.919  22.469 1.00 40.01 ? 294 PHE B CZ  1 
ATOM   2278 N N   . ASP A 1 295 ? 21.935  -5.650  27.967 1.00 22.20 ? 295 ASP B N   1 
ATOM   2279 C CA  . ASP A 1 295 ? 21.290  -4.341  28.046 1.00 23.13 ? 295 ASP B CA  1 
ATOM   2280 C C   . ASP A 1 295 ? 22.145  -3.353  28.816 1.00 23.74 ? 295 ASP B C   1 
ATOM   2281 O O   . ASP A 1 295 ? 22.232  -2.180  28.440 1.00 24.83 ? 295 ASP B O   1 
ATOM   2282 C CB  . ASP A 1 295 ? 19.905  -4.426  28.710 1.00 21.36 ? 295 ASP B CB  1 
ATOM   2283 C CG  . ASP A 1 295 ? 18.897  -5.222  27.900 1.00 25.66 ? 295 ASP B CG  1 
ATOM   2284 O OD1 . ASP A 1 295 ? 19.120  -5.437  26.684 1.00 27.92 ? 295 ASP B OD1 1 
ATOM   2285 O OD2 . ASP A 1 295 ? 17.864  -5.619  28.493 1.00 22.65 ? 295 ASP B OD2 1 
ATOM   2286 N N   . VAL A 1 296 ? 22.760  -3.807  29.910 1.00 20.41 ? 296 VAL B N   1 
ATOM   2287 C CA  . VAL A 1 296 ? 23.598  -2.943  30.731 1.00 19.67 ? 296 VAL B CA  1 
ATOM   2288 C C   . VAL A 1 296 ? 24.860  -2.552  29.967 1.00 25.66 ? 296 VAL B C   1 
ATOM   2289 O O   . VAL A 1 296 ? 25.222  -1.367  29.892 1.00 25.00 ? 296 VAL B O   1 
ATOM   2290 C CB  . VAL A 1 296 ? 23.923  -3.649  32.062 1.00 19.74 ? 296 VAL B CB  1 
ATOM   2291 C CG1 . VAL A 1 296 ? 24.923  -2.832  32.886 1.00 18.58 ? 296 VAL B CG1 1 
ATOM   2292 C CG2 . VAL A 1 296 ? 22.638  -3.908  32.865 1.00 17.52 ? 296 VAL B CG2 1 
ATOM   2293 N N   . VAL A 1 297 ? 25.527  -3.542  29.364 1.00 21.64 ? 297 VAL B N   1 
ATOM   2294 C CA  . VAL A 1 297 ? 26.724  -3.268  28.572 1.00 24.43 ? 297 VAL B CA  1 
ATOM   2295 C C   . VAL A 1 297 ? 26.391  -2.327  27.422 1.00 30.13 ? 297 VAL B C   1 
ATOM   2296 O O   . VAL A 1 297 ? 27.110  -1.352  27.168 1.00 29.48 ? 297 VAL B O   1 
ATOM   2297 C CB  . VAL A 1 297 ? 27.342  -4.578  28.057 1.00 26.54 ? 297 VAL B CB  1 
ATOM   2298 C CG1 . VAL A 1 297 ? 28.414  -4.266  27.014 1.00 26.39 ? 297 VAL B CG1 1 
ATOM   2299 C CG2 . VAL A 1 297 ? 27.903  -5.402  29.207 1.00 23.92 ? 297 VAL B CG2 1 
ATOM   2300 N N   . ARG A 1 298 ? 25.286  -2.599  26.715 1.00 29.79 ? 298 ARG B N   1 
ATOM   2301 C CA  . ARG A 1 298 ? 24.897  -1.744  25.596 1.00 31.59 ? 298 ARG B CA  1 
ATOM   2302 C C   . ARG A 1 298 ? 24.678  -0.309  26.050 1.00 33.77 ? 298 ARG B C   1 
ATOM   2303 O O   . ARG A 1 298 ? 25.171  0.636   25.418 1.00 35.54 ? 298 ARG B O   1 
ATOM   2304 C CB  . ARG A 1 298 ? 23.631  -2.279  24.914 1.00 36.88 ? 298 ARG B CB  1 
ATOM   2305 C CG  . ARG A 1 298 ? 23.167  -1.397  23.743 1.00 43.51 ? 298 ARG B CG  1 
ATOM   2306 C CD  . ARG A 1 298 ? 21.645  -1.247  23.566 1.00 42.74 ? 298 ARG B CD  1 
ATOM   2307 N NE  . ARG A 1 298 ? 20.860  -2.357  24.098 1.00 46.20 ? 298 ARG B NE  1 
ATOM   2308 C CZ  . ARG A 1 298 ? 19.565  -2.290  24.387 1.00 41.36 ? 298 ARG B CZ  1 
ATOM   2309 N NH1 . ARG A 1 298 ? 18.873  -1.170  24.220 1.00 43.37 ? 298 ARG B NH1 1 
ATOM   2310 N NH2 . ARG A 1 298 ? 18.945  -3.375  24.848 1.00 34.59 ? 298 ARG B NH2 1 
ATOM   2311 N N   . GLN A 1 299 ? 23.950  -0.124  27.151 1.00 28.86 ? 299 GLN B N   1 
ATOM   2312 C CA  . GLN A 1 299 ? 23.639  1.225   27.600 1.00 30.86 ? 299 GLN B CA  1 
ATOM   2313 C C   . GLN A 1 299 ? 24.864  1.924   28.161 1.00 33.63 ? 299 GLN B C   1 
ATOM   2314 O O   . GLN A 1 299 ? 25.040  3.126   27.946 1.00 31.82 ? 299 GLN B O   1 
ATOM   2315 C CB  . GLN A 1 299 ? 22.547  1.206   28.660 1.00 28.45 ? 299 GLN B CB  1 
ATOM   2316 C CG  . GLN A 1 299 ? 22.220  2.590   29.131 1.00 26.18 ? 299 GLN B CG  1 
ATOM   2317 C CD  . GLN A 1 299 ? 20.830  2.731   29.666 1.00 25.44 ? 299 GLN B CD  1 
ATOM   2318 O OE1 . GLN A 1 299 ? 20.520  3.729   30.312 1.00 23.36 ? 299 GLN B OE1 1 
ATOM   2319 N NE2 . GLN A 1 299 ? 19.978  1.717   29.434 1.00 25.94 ? 299 GLN B NE2 1 
ATOM   2320 N N   . CYS A 1 300 ? 25.709  1.200   28.902 1.00 30.70 ? 300 CYS B N   1 
ATOM   2321 C CA  . CYS A 1 300 ? 26.817  1.845   29.596 1.00 34.23 ? 300 CYS B CA  1 
ATOM   2322 C C   . CYS A 1 300 ? 28.029  2.066   28.694 1.00 33.50 ? 300 CYS B C   1 
ATOM   2323 O O   . CYS A 1 300 ? 28.898  2.879   29.038 1.00 32.11 ? 300 CYS B O   1 
ATOM   2324 C CB  . CYS A 1 300 ? 27.196  1.032   30.837 1.00 30.69 ? 300 CYS B CB  1 
ATOM   2325 S SG  . CYS A 1 300 ? 25.920  1.079   32.160 1.00 39.73 ? 300 CYS B SG  1 
ATOM   2326 N N   . SER A 1 301 ? 28.085  1.390   27.540 1.00 34.89 ? 301 SER B N   1 
ATOM   2327 C CA  . SER A 1 301 ? 29.126  1.584   26.535 1.00 37.44 ? 301 SER B CA  1 
ATOM   2328 C C   . SER A 1 301 ? 28.657  2.382   25.325 1.00 42.76 ? 301 SER B C   1 
ATOM   2329 O O   . SER A 1 301 ? 29.498  2.829   24.536 1.00 42.34 ? 301 SER B O   1 
ATOM   2330 C CB  . SER A 1 301 ? 29.655  0.230   26.040 1.00 42.24 ? 301 SER B CB  1 
ATOM   2331 O OG  . SER A 1 301 ? 28.805  -0.297  25.021 1.00 37.79 ? 301 SER B OG  1 
ATOM   2332 N N   . GLY A 1 302 ? 27.345  2.530   25.140 1.00 39.87 ? 302 GLY B N   1 
ATOM   2333 C CA  . GLY A 1 302 ? 26.802  3.431   24.139 1.00 41.39 ? 302 GLY B CA  1 
ATOM   2334 C C   . GLY A 1 302 ? 26.806  2.945   22.705 1.00 46.76 ? 302 GLY B C   1 
ATOM   2335 O O   . GLY A 1 302 ? 27.028  3.751   21.789 1.00 46.40 ? 302 GLY B O   1 
ATOM   2336 N N   . VAL A 1 303 ? 26.546  1.651   22.470 1.00 45.70 ? 303 VAL B N   1 
ATOM   2337 C CA  . VAL A 1 303 ? 26.560  1.160   21.087 1.00 51.48 ? 303 VAL B CA  1 
ATOM   2338 C C   . VAL A 1 303 ? 25.337  1.692   20.340 1.00 48.72 ? 303 VAL B C   1 
ATOM   2339 O O   . VAL A 1 303 ? 24.295  2.019   20.928 1.00 44.79 ? 303 VAL B O   1 
ATOM   2340 C CB  . VAL A 1 303 ? 26.635  -0.376  21.010 1.00 54.10 ? 303 VAL B CB  1 
ATOM   2341 C CG1 . VAL A 1 303 ? 25.246  -0.997  21.018 1.00 49.25 ? 303 VAL B CG1 1 
ATOM   2342 C CG2 . VAL A 1 303 ? 27.424  -0.820  19.771 1.00 52.17 ? 303 VAL B CG2 1 
ATOM   2343 N N   . THR A 1 304 ? 25.471  1.775   19.018 1.00 46.79 ? 304 THR B N   1 
ATOM   2344 C CA  . THR A 1 304 ? 24.548  2.528   18.184 1.00 46.63 ? 304 THR B CA  1 
ATOM   2345 C C   . THR A 1 304 ? 24.105  1.674   16.998 1.00 50.63 ? 304 THR B C   1 
ATOM   2346 O O   . THR A 1 304 ? 24.770  0.703   16.622 1.00 51.05 ? 304 THR B O   1 
ATOM   2347 C CB  . THR A 1 304 ? 25.208  3.841   17.713 1.00 44.74 ? 304 THR B CB  1 
ATOM   2348 O OG1 . THR A 1 304 ? 24.199  4.810   17.422 1.00 41.63 ? 304 THR B OG1 1 
ATOM   2349 C CG2 . THR A 1 304 ? 26.075  3.606   16.477 1.00 44.47 ? 304 THR B CG2 1 
ATOM   2350 N N   . PHE A 1 305 ? 22.960  2.043   16.414 1.00 47.20 ? 305 PHE B N   1 
ATOM   2351 C CA  . PHE A 1 305 ? 22.319  1.249   15.371 1.00 51.04 ? 305 PHE B CA  1 
ATOM   2352 C C   . PHE A 1 305 ? 21.959  2.127   14.177 1.00 55.03 ? 305 PHE B C   1 
ATOM   2353 O O   . PHE A 1 305 ? 21.832  3.351   14.287 1.00 50.59 ? 305 PHE B O   1 
ATOM   2354 C CB  . PHE A 1 305 ? 21.059  0.540   15.903 1.00 46.26 ? 305 PHE B CB  1 
ATOM   2355 C CG  . PHE A 1 305 ? 21.255  -0.069  17.258 1.00 46.70 ? 305 PHE B CG  1 
ATOM   2356 C CD1 . PHE A 1 305 ? 21.798  -1.342  17.387 1.00 44.17 ? 305 PHE B CD1 1 
ATOM   2357 C CD2 . PHE A 1 305 ? 20.931  0.645   18.408 1.00 41.15 ? 305 PHE B CD2 1 
ATOM   2358 C CE1 . PHE A 1 305 ? 22.007  -1.898  18.633 1.00 45.30 ? 305 PHE B CE1 1 
ATOM   2359 C CE2 . PHE A 1 305 ? 21.134  0.096   19.662 1.00 40.87 ? 305 PHE B CE2 1 
ATOM   2360 C CZ  . PHE A 1 305 ? 21.682  -1.175  19.775 1.00 45.31 ? 305 PHE B CZ  1 
ATOM   2361 N N   . GLN A 1 306 ? 21.786  1.472   13.031 1.00 59.07 ? 306 GLN B N   1 
ATOM   2362 C CA  . GLN A 1 306 ? 21.451  2.143   11.779 1.00 59.56 ? 306 GLN B CA  1 
ATOM   2363 C C   . GLN A 1 306 ? 21.226  1.105   10.683 1.00 52.94 ? 306 GLN B C   1 
ATOM   2364 O O   . GLN A 1 306 ? 20.995  1.446   9.522  1.00 54.16 ? 306 GLN B O   1 
ATOM   2365 C CB  . GLN A 1 306 ? 22.556  3.127   11.376 1.00 64.71 ? 306 GLN B CB  1 
ATOM   2366 C CG  . GLN A 1 306 ? 23.924  2.484   11.168 1.00 63.94 ? 306 GLN B CG  1 
ATOM   2367 C CD  . GLN A 1 306 ? 25.014  3.512   10.931 1.00 68.12 ? 306 GLN B CD  1 
ATOM   2368 O OE1 . GLN A 1 306 ? 24.748  4.613   10.443 1.00 69.80 ? 306 GLN B OE1 1 
ATOM   2369 N NE2 . GLN A 1 306 ? 26.251  3.157   11.271 1.00 66.69 ? 306 GLN B NE2 1 
ATOM   2370 N N   . SER B 1 1   ? -4.885  -2.931  28.935 1.00 19.81 ? 1   SER A N   1 
ATOM   2371 C CA  . SER B 1 1   ? -4.344  -3.589  30.119 1.00 22.42 ? 1   SER A CA  1 
ATOM   2372 C C   . SER B 1 1   ? -2.835  -3.396  30.207 1.00 24.12 ? 1   SER A C   1 
ATOM   2373 O O   . SER B 1 1   ? -2.138  -3.424  29.196 1.00 22.44 ? 1   SER A O   1 
ATOM   2374 C CB  . SER B 1 1   ? -4.675  -5.087  30.120 1.00 25.57 ? 1   SER A CB  1 
ATOM   2375 O OG  . SER B 1 1   ? -4.428  -5.686  28.854 1.00 26.61 ? 1   SER A OG  1 
ATOM   2376 N N   . GLY B 1 2   ? -2.338  -3.230  31.430 1.00 23.69 ? 2   GLY A N   1 
ATOM   2377 C CA  . GLY B 1 2   ? -0.941  -2.910  31.681 1.00 23.65 ? 2   GLY A CA  1 
ATOM   2378 C C   . GLY B 1 2   ? -0.686  -1.420  31.643 1.00 21.32 ? 2   GLY A C   1 
ATOM   2379 O O   . GLY B 1 2   ? -1.407  -0.669  30.982 1.00 22.96 ? 2   GLY A O   1 
ATOM   2380 N N   . PHE B 1 3   ? 0.348   -0.967  32.342 1.00 21.59 ? 3   PHE A N   1 
ATOM   2381 C CA  . PHE B 1 3   ? 0.722   0.440   32.310 1.00 23.02 ? 3   PHE A CA  1 
ATOM   2382 C C   . PHE B 1 3   ? 2.238   0.521   32.320 1.00 20.96 ? 3   PHE A C   1 
ATOM   2383 O O   . PHE B 1 3   ? 2.878   0.025   33.251 1.00 23.98 ? 3   PHE A O   1 
ATOM   2384 C CB  . PHE B 1 3   ? 0.140   1.213   33.493 1.00 21.18 ? 3   PHE A CB  1 
ATOM   2385 C CG  . PHE B 1 3   ? 0.216   2.698   33.324 1.00 19.61 ? 3   PHE A CG  1 
ATOM   2386 C CD1 . PHE B 1 3   ? -0.659  3.361   32.467 1.00 20.64 ? 3   PHE A CD1 1 
ATOM   2387 C CD2 . PHE B 1 3   ? 1.148   3.438   34.034 1.00 25.47 ? 3   PHE A CD2 1 
ATOM   2388 C CE1 . PHE B 1 3   ? -0.586  4.736   32.307 1.00 29.91 ? 3   PHE A CE1 1 
ATOM   2389 C CE2 . PHE B 1 3   ? 1.238   4.810   33.870 1.00 21.13 ? 3   PHE A CE2 1 
ATOM   2390 C CZ  . PHE B 1 3   ? 0.356   5.466   33.016 1.00 23.99 ? 3   PHE A CZ  1 
ATOM   2391 N N   . ARG B 1 4   ? 2.818   1.144   31.292 1.00 20.37 ? 4   ARG A N   1 
ATOM   2392 C CA  . ARG B 1 4   ? 4.264   1.172   31.144 1.00 20.46 ? 4   ARG A CA  1 
ATOM   2393 C C   . ARG B 1 4   ? 4.739   2.581   30.845 1.00 19.09 ? 4   ARG A C   1 
ATOM   2394 O O   . ARG B 1 4   ? 4.060   3.339   30.144 1.00 19.05 ? 4   ARG A O   1 
ATOM   2395 C CB  . ARG B 1 4   ? 4.723   0.227   30.025 1.00 20.57 ? 4   ARG A CB  1 
ATOM   2396 C CG  . ARG B 1 4   ? 4.335   -1.205  30.292 1.00 20.22 ? 4   ARG A CG  1 
ATOM   2397 C CD  . ARG B 1 4   ? 5.207   -1.768  31.401 1.00 21.35 ? 4   ARG A CD  1 
ATOM   2398 N NE  . ARG B 1 4   ? 6.585   -1.320  31.243 1.00 21.89 ? 4   ARG A NE  1 
ATOM   2399 C CZ  . ARG B 1 4   ? 7.476   -1.976  30.514 1.00 23.86 ? 4   ARG A CZ  1 
ATOM   2400 N NH1 . ARG B 1 4   ? 7.164   -3.102  29.904 1.00 19.74 ? 4   ARG A NH1 1 
ATOM   2401 N NH2 . ARG B 1 4   ? 8.692   -1.464  30.345 1.00 20.77 ? 4   ARG A NH2 1 
ATOM   2402 N N   . LYS B 1 5   ? 5.907   2.920   31.370 1.00 20.23 ? 5   LYS A N   1 
ATOM   2403 C CA  . LYS B 1 5   ? 6.595   4.105   30.872 1.00 17.03 ? 5   LYS A CA  1 
ATOM   2404 C C   . LYS B 1 5   ? 6.924   3.879   29.404 1.00 19.54 ? 5   LYS A C   1 
ATOM   2405 O O   . LYS B 1 5   ? 7.635   2.927   29.053 1.00 20.90 ? 5   LYS A O   1 
ATOM   2406 C CB  . LYS B 1 5   ? 7.857   4.386   31.675 1.00 23.00 ? 5   LYS A CB  1 
ATOM   2407 C CG  . LYS B 1 5   ? 8.421   5.786   31.438 1.00 23.93 ? 5   LYS A CG  1 
ATOM   2408 C CD  . LYS B 1 5   ? 9.303   6.197   32.597 1.00 25.88 ? 5   LYS A CD  1 
ATOM   2409 C CE  . LYS B 1 5   ? 8.514   6.938   33.658 1.00 29.50 ? 5   LYS A CE  1 
ATOM   2410 N NZ  . LYS B 1 5   ? 9.313   6.965   34.915 1.00 31.92 ? 5   LYS A NZ  1 
ATOM   2411 N N   . MET B 1 6   ? 6.415   4.768   28.564 1.00 19.24 ? 6   MET A N   1 
ATOM   2412 C CA  . MET B 1 6   ? 6.238   4.595   27.132 1.00 22.62 ? 6   MET A CA  1 
ATOM   2413 C C   . MET B 1 6   ? 6.780   5.825   26.414 1.00 23.30 ? 6   MET A C   1 
ATOM   2414 O O   . MET B 1 6   ? 6.361   6.944   26.724 1.00 22.13 ? 6   MET A O   1 
ATOM   2415 C CB  . MET B 1 6   ? 4.737   4.448   26.838 1.00 25.63 ? 6   MET A CB  1 
ATOM   2416 C CG  . MET B 1 6   ? 4.375   4.277   25.396 1.00 30.09 ? 6   MET A CG  1 
ATOM   2417 S SD  . MET B 1 6   ? 2.894   3.279   25.194 1.00 33.41 ? 6   MET A SD  1 
ATOM   2418 C CE  . MET B 1 6   ? 2.924   2.277   26.661 1.00 24.48 ? 6   MET A CE  1 
ATOM   2419 N N   . ALA B 1 7   ? 7.695   5.632   25.460 1.00 20.63 ? 7   ALA A N   1 
ATOM   2420 C CA  . ALA B 1 7   ? 8.188   6.743   24.654 1.00 20.39 ? 7   ALA A CA  1 
ATOM   2421 C C   . ALA B 1 7   ? 7.402   6.855   23.352 1.00 22.33 ? 7   ALA A C   1 
ATOM   2422 O O   . ALA B 1 7   ? 6.717   5.920   22.935 1.00 21.36 ? 7   ALA A O   1 
ATOM   2423 C CB  . ALA B 1 7   ? 9.675   6.558   24.335 1.00 20.82 ? 7   ALA A CB  1 
ATOM   2424 N N   . PHE B 1 8   ? 7.515   8.011   22.692 1.00 19.37 ? 8   PHE A N   1 
ATOM   2425 C CA  . PHE B 1 8   ? 6.914   8.117   21.368 1.00 19.68 ? 8   PHE A CA  1 
ATOM   2426 C C   . PHE B 1 8   ? 7.725   7.313   20.355 1.00 18.71 ? 8   PHE A C   1 
ATOM   2427 O O   . PHE B 1 8   ? 8.922   7.117   20.536 1.00 23.18 ? 8   PHE A O   1 
ATOM   2428 C CB  . PHE B 1 8   ? 6.836   9.562   20.898 1.00 23.21 ? 8   PHE A CB  1 
ATOM   2429 C CG  . PHE B 1 8   ? 5.831   10.367  21.625 1.00 23.77 ? 8   PHE A CG  1 
ATOM   2430 C CD1 . PHE B 1 8   ? 4.495   10.330  21.250 1.00 33.79 ? 8   PHE A CD1 1 
ATOM   2431 C CD2 . PHE B 1 8   ? 6.209   11.195  22.670 1.00 25.54 ? 8   PHE A CD2 1 
ATOM   2432 C CE1 . PHE B 1 8   ? 3.549   11.078  21.927 1.00 32.73 ? 8   PHE A CE1 1 
ATOM   2433 C CE2 . PHE B 1 8   ? 5.263   11.948  23.350 1.00 27.53 ? 8   PHE A CE2 1 
ATOM   2434 C CZ  . PHE B 1 8   ? 3.931   11.888  22.976 1.00 31.78 ? 8   PHE A CZ  1 
ATOM   2435 N N   . PRO B 1 9   ? 7.087   6.839   19.280 1.00 20.23 ? 9   PRO A N   1 
ATOM   2436 C CA  . PRO B 1 9   ? 7.853   6.253   18.172 1.00 21.89 ? 9   PRO A CA  1 
ATOM   2437 C C   . PRO B 1 9   ? 8.833   7.289   17.645 1.00 21.84 ? 9   PRO A C   1 
ATOM   2438 O O   . PRO B 1 9   ? 8.482   8.455   17.466 1.00 24.66 ? 9   PRO A O   1 
ATOM   2439 C CB  . PRO B 1 9   ? 6.775   5.911   17.137 1.00 25.31 ? 9   PRO A CB  1 
ATOM   2440 C CG  . PRO B 1 9   ? 5.516   5.787   17.949 1.00 25.37 ? 9   PRO A CG  1 
ATOM   2441 C CD  . PRO B 1 9   ? 5.645   6.856   18.997 1.00 22.70 ? 9   PRO A CD  1 
ATOM   2442 N N   . SER B 1 10  ? 10.067  6.857   17.425 1.00 19.26 ? 10  SER A N   1 
ATOM   2443 C CA  . SER B 1 10  ? 11.188  7.761   17.178 1.00 24.21 ? 10  SER A CA  1 
ATOM   2444 C C   . SER B 1 10  ? 11.549  7.899   15.699 1.00 25.51 ? 10  SER A C   1 
ATOM   2445 O O   . SER B 1 10  ? 12.477  8.653   15.372 1.00 24.50 ? 10  SER A O   1 
ATOM   2446 C CB  . SER B 1 10  ? 12.422  7.291   17.964 1.00 22.08 ? 10  SER A CB  1 
ATOM   2447 O OG  . SER B 1 10  ? 12.874  6.012   17.520 1.00 25.18 ? 10  SER A OG  1 
ATOM   2448 N N   . GLY B 1 11  ? 10.832  7.210   14.805 1.00 24.10 ? 11  GLY A N   1 
ATOM   2449 C CA  . GLY B 1 11  ? 11.190  7.229   13.393 1.00 23.39 ? 11  GLY A CA  1 
ATOM   2450 C C   . GLY B 1 11  ? 11.268  8.627   12.801 1.00 24.63 ? 11  GLY A C   1 
ATOM   2451 O O   . GLY B 1 11  ? 12.221  8.950   12.083 1.00 26.61 ? 11  GLY A O   1 
ATOM   2452 N N   . LYS B 1 12  ? 10.275  9.472   13.091 1.00 23.24 ? 12  LYS A N   1 
ATOM   2453 C CA  . LYS B 1 12  ? 10.265  10.815  12.513 1.00 24.52 ? 12  LYS A CA  1 
ATOM   2454 C C   . LYS B 1 12  ? 11.480  11.626  12.957 1.00 21.94 ? 12  LYS A C   1 
ATOM   2455 O O   . LYS B 1 12  ? 11.941  12.510  12.220 1.00 25.95 ? 12  LYS A O   1 
ATOM   2456 C CB  . LYS B 1 12  ? 8.963   11.533  12.882 1.00 27.44 ? 12  LYS A CB  1 
ATOM   2457 C CG  . LYS B 1 12  ? 7.710   10.864  12.312 1.00 31.15 ? 12  LYS A CG  1 
ATOM   2458 C CD  . LYS B 1 12  ? 6.499   11.785  12.325 1.00 37.08 ? 12  LYS A CD  1 
ATOM   2459 C CE  . LYS B 1 12  ? 5.349   11.206  11.505 1.00 43.05 ? 12  LYS A CE  1 
ATOM   2460 N NZ  . LYS B 1 12  ? 4.914   9.880   12.039 1.00 49.83 ? 12  LYS A NZ  1 
ATOM   2461 N N   . VAL B 1 13  ? 12.025  11.338  14.138 1.00 22.67 ? 13  VAL A N   1 
ATOM   2462 C CA  . VAL B 1 13  ? 13.211  12.050  14.608 1.00 24.85 ? 13  VAL A CA  1 
ATOM   2463 C C   . VAL B 1 13  ? 14.518  11.381  14.162 1.00 25.30 ? 13  VAL A C   1 
ATOM   2464 O O   . VAL B 1 13  ? 15.518  12.076  13.929 1.00 25.31 ? 13  VAL A O   1 
ATOM   2465 C CB  . VAL B 1 13  ? 13.146  12.197  16.140 1.00 23.34 ? 13  VAL A CB  1 
ATOM   2466 C CG1 . VAL B 1 13  ? 14.388  12.897  16.652 1.00 25.56 ? 13  VAL A CG1 1 
ATOM   2467 C CG2 . VAL B 1 13  ? 11.887  12.972  16.553 1.00 23.25 ? 13  VAL A CG2 1 
ATOM   2468 N N   . GLU B 1 14  ? 14.531  10.048  14.025 1.00 23.33 ? 14  GLU A N   1 
ATOM   2469 C CA  . GLU B 1 14  ? 15.700  9.340   13.494 1.00 24.07 ? 14  GLU A CA  1 
ATOM   2470 C C   . GLU B 1 14  ? 16.130  9.911   12.149 1.00 22.45 ? 14  GLU A C   1 
ATOM   2471 O O   . GLU B 1 14  ? 17.327  10.088  11.891 1.00 23.19 ? 14  GLU A O   1 
ATOM   2472 C CB  . GLU B 1 14  ? 15.386  7.847   13.333 1.00 23.05 ? 14  GLU A CB  1 
ATOM   2473 C CG  . GLU B 1 14  ? 15.266  7.091   14.635 1.00 24.44 ? 14  GLU A CG  1 
ATOM   2474 C CD  . GLU B 1 14  ? 14.724  5.693   14.421 1.00 26.58 ? 14  GLU A CD  1 
ATOM   2475 O OE1 . GLU B 1 14  ? 15.282  4.958   13.575 1.00 28.14 ? 14  GLU A OE1 1 
ATOM   2476 O OE2 . GLU B 1 14  ? 13.714  5.365   15.074 1.00 26.55 ? 14  GLU A OE2 1 
ATOM   2477 N N   . GLY B 1 15  ? 15.161  10.192  11.279 1.00 24.02 ? 15  GLY A N   1 
ATOM   2478 C CA  . GLY B 1 15  ? 15.402  10.755  9.962  1.00 26.31 ? 15  GLY A CA  1 
ATOM   2479 C C   . GLY B 1 15  ? 16.013  12.148  9.967  1.00 28.11 ? 15  GLY A C   1 
ATOM   2480 O O   . GLY B 1 15  ? 16.433  12.619  8.906  1.00 26.50 ? 15  GLY A O   1 
ATOM   2481 N N   . CYS B 1 16  ? 16.079  12.807  11.124 1.00 23.95 ? 16  CYS A N   1 
ATOM   2482 C CA  . CYS B 1 16  ? 16.646  14.146  11.229 1.00 25.40 ? 16  CYS A CA  1 
ATOM   2483 C C   . CYS B 1 16  ? 18.025  14.180  11.866 1.00 26.65 ? 16  CYS A C   1 
ATOM   2484 O O   . CYS B 1 16  ? 18.645  15.248  11.905 1.00 23.80 ? 16  CYS A O   1 
ATOM   2485 C CB  . CYS B 1 16  ? 15.715  15.038  12.041 1.00 25.06 ? 16  CYS A CB  1 
ATOM   2486 S SG  . CYS B 1 16  ? 14.103  15.194  11.373 1.00 26.55 ? 16  CYS A SG  1 
ATOM   2487 N N   . MET B 1 17  ? 18.519  13.054  12.367 1.00 23.64 ? 17  MET A N   1 
ATOM   2488 C CA  . MET B 1 17  ? 19.789  13.021  13.083 1.00 21.20 ? 17  MET A CA  1 
ATOM   2489 C C   . MET B 1 17  ? 20.965  13.032  12.105 1.00 22.91 ? 17  MET A C   1 
ATOM   2490 O O   . MET B 1 17  ? 21.014  12.230  11.164 1.00 23.71 ? 17  MET A O   1 
ATOM   2491 C CB  . MET B 1 17  ? 19.821  11.773  13.963 1.00 23.88 ? 17  MET A CB  1 
ATOM   2492 C CG  . MET B 1 17  ? 19.028  11.869  15.291 1.00 24.49 ? 17  MET A CG  1 
ATOM   2493 S SD  . MET B 1 17  ? 18.512  13.504  15.903 1.00 23.35 ? 17  MET A SD  1 
ATOM   2494 C CE  . MET B 1 17  ? 20.070  13.957  16.656 1.00 22.67 ? 17  MET A CE  1 
ATOM   2495 N N   . VAL B 1 18  ? 21.909  13.952  12.322 1.00 20.64 ? 18  VAL A N   1 
ATOM   2496 C CA  . VAL B 1 18  ? 23.170  14.002  11.580 1.00 24.68 ? 18  VAL A CA  1 
ATOM   2497 C C   . VAL B 1 18  ? 24.328  14.087  12.566 1.00 21.45 ? 18  VAL A C   1 
ATOM   2498 O O   . VAL B 1 18  ? 24.141  14.248  13.769 1.00 22.68 ? 18  VAL A O   1 
ATOM   2499 C CB  . VAL B 1 18  ? 23.235  15.184  10.588 1.00 24.97 ? 18  VAL A CB  1 
ATOM   2500 C CG1 . VAL B 1 18  ? 22.195  15.032  9.495  1.00 24.83 ? 18  VAL A CG1 1 
ATOM   2501 C CG2 . VAL B 1 18  ? 23.048  16.502  11.316 1.00 23.35 ? 18  VAL A CG2 1 
ATOM   2502 N N   . GLN B 1 19  ? 25.542  13.987  12.030 1.00 23.69 ? 19  GLN A N   1 
ATOM   2503 C CA  . GLN B 1 19  ? 26.770  14.109  12.799 1.00 24.81 ? 19  GLN A CA  1 
ATOM   2504 C C   . GLN B 1 19  ? 27.437  15.439  12.451 1.00 25.68 ? 19  GLN A C   1 
ATOM   2505 O O   . GLN B 1 19  ? 27.538  15.786  11.271 1.00 27.11 ? 19  GLN A O   1 
ATOM   2506 C CB  . GLN B 1 19  ? 27.682  12.913  12.491 1.00 27.43 ? 19  GLN A CB  1 
ATOM   2507 C CG  . GLN B 1 19  ? 28.932  12.801  13.314 1.00 31.43 ? 19  GLN A CG  1 
ATOM   2508 C CD  . GLN B 1 19  ? 29.772  11.596  12.911 1.00 34.34 ? 19  GLN A CD  1 
ATOM   2509 O OE1 . GLN B 1 19  ? 30.653  11.175  13.650 1.00 39.82 ? 19  GLN A OE1 1 
ATOM   2510 N NE2 . GLN B 1 19  ? 29.478  11.023  11.752 1.00 37.60 ? 19  GLN A NE2 1 
ATOM   2511 N N   . VAL B 1 20  ? 27.838  16.207  13.469 1.00 23.42 ? 20  VAL A N   1 
ATOM   2512 C CA  . VAL B 1 20  ? 28.521  17.496  13.274 1.00 22.67 ? 20  VAL A CA  1 
ATOM   2513 C C   . VAL B 1 20  ? 29.906  17.419  13.901 1.00 26.64 ? 20  VAL A C   1 
ATOM   2514 O O   . VAL B 1 20  ? 30.041  17.140  15.100 1.00 25.68 ? 20  VAL A O   1 
ATOM   2515 C CB  . VAL B 1 20  ? 27.732  18.677  13.874 1.00 23.25 ? 20  VAL A CB  1 
ATOM   2516 C CG1 . VAL B 1 20  ? 28.414  19.994  13.538 1.00 21.46 ? 20  VAL A CG1 1 
ATOM   2517 C CG2 . VAL B 1 20  ? 26.287  18.701  13.381 1.00 23.05 ? 20  VAL A CG2 1 
ATOM   2518 N N   . THR B 1 21  ? 30.937  17.687  13.105 1.00 27.14 ? 21  THR A N   1 
ATOM   2519 C CA  . THR B 1 21  ? 32.304  17.698  13.596 1.00 28.98 ? 21  THR A CA  1 
ATOM   2520 C C   . THR B 1 21  ? 32.911  19.066  13.335 1.00 28.61 ? 21  THR A C   1 
ATOM   2521 O O   . THR B 1 21  ? 32.758  19.623  12.243 1.00 27.89 ? 21  THR A O   1 
ATOM   2522 C CB  . THR B 1 21  ? 33.159  16.610  12.936 1.00 28.70 ? 21  THR A CB  1 
ATOM   2523 O OG1 . THR B 1 21  ? 32.560  15.322  13.157 1.00 30.16 ? 21  THR A OG1 1 
ATOM   2524 C CG2 . THR B 1 21  ? 34.542  16.613  13.554 1.00 30.08 ? 21  THR A CG2 1 
ATOM   2525 N N   . CYS B 1 22  ? 33.565  19.612  14.352 1.00 27.94 ? 22  CYS A N   1 
ATOM   2526 C CA  . CYS B 1 22  ? 34.338  20.837  14.227 1.00 31.53 ? 22  CYS A CA  1 
ATOM   2527 C C   . CYS B 1 22  ? 35.663  20.572  14.919 1.00 35.45 ? 22  CYS A C   1 
ATOM   2528 O O   . CYS B 1 22  ? 35.695  20.310  16.126 1.00 36.66 ? 22  CYS A O   1 
ATOM   2529 C CB  . CYS B 1 22  ? 33.605  22.036  14.837 1.00 29.05 ? 22  CYS A CB  1 
ATOM   2530 S SG  . CYS B 1 22  ? 34.308  23.641  14.363 1.00 37.27 ? 22  CYS A SG  1 
ATOM   2531 N N   . GLY B 1 23  ? 36.740  20.575  14.146 1.00 34.10 ? 23  GLY A N   1 
ATOM   2532 C CA  . GLY B 1 23  ? 38.042  20.249  14.689 1.00 39.58 ? 23  GLY A CA  1 
ATOM   2533 C C   . GLY B 1 23  ? 38.104  18.866  15.303 1.00 44.41 ? 23  GLY A C   1 
ATOM   2534 O O   . GLY B 1 23  ? 37.979  17.853  14.605 1.00 45.91 ? 23  GLY A O   1 
ATOM   2535 N N   . THR B 1 24  ? 38.273  18.812  16.621 1.00 48.07 ? 24  THR A N   1 
ATOM   2536 C CA  . THR B 1 24  ? 38.451  17.555  17.334 1.00 49.78 ? 24  THR A CA  1 
ATOM   2537 C C   . THR B 1 24  ? 37.161  17.029  17.960 1.00 47.42 ? 24  THR A C   1 
ATOM   2538 O O   . THR B 1 24  ? 37.179  15.963  18.582 1.00 47.30 ? 24  THR A O   1 
ATOM   2539 C CB  . THR B 1 24  ? 39.522  17.728  18.417 1.00 50.17 ? 24  THR A CB  1 
ATOM   2540 O OG1 . THR B 1 24  ? 39.808  16.462  19.018 1.00 58.15 ? 24  THR A OG1 1 
ATOM   2541 C CG2 . THR B 1 24  ? 39.048  18.707  19.493 1.00 50.26 ? 24  THR A CG2 1 
ATOM   2542 N N   . THR B 1 25  ? 36.047  17.733  17.802 1.00 41.22 ? 25  THR A N   1 
ATOM   2543 C CA  . THR B 1 25  ? 34.820  17.425  18.524 1.00 37.34 ? 25  THR A CA  1 
ATOM   2544 C C   . THR B 1 25  ? 33.752  16.926  17.563 1.00 32.18 ? 25  THR A C   1 
ATOM   2545 O O   . THR B 1 25  ? 33.455  17.586  16.559 1.00 29.75 ? 25  THR A O   1 
ATOM   2546 C CB  . THR B 1 25  ? 34.302  18.658  19.268 1.00 38.01 ? 25  THR A CB  1 
ATOM   2547 O OG1 . THR B 1 25  ? 35.360  19.237  20.042 1.00 42.25 ? 25  THR A OG1 1 
ATOM   2548 C CG2 . THR B 1 25  ? 33.149  18.259  20.177 1.00 37.44 ? 25  THR A CG2 1 
ATOM   2549 N N   . THR B 1 26  ? 33.159  15.778  17.884 1.00 32.65 ? 26  THR A N   1 
ATOM   2550 C CA  . THR B 1 26  ? 32.059  15.219  17.110 1.00 30.20 ? 26  THR A CA  1 
ATOM   2551 C C   . THR B 1 26  ? 30.847  15.092  18.029 1.00 27.69 ? 26  THR A C   1 
ATOM   2552 O O   . THR B 1 26  ? 30.961  14.548  19.131 1.00 30.29 ? 26  THR A O   1 
ATOM   2553 C CB  . THR B 1 26  ? 32.440  13.858  16.521 1.00 32.54 ? 26  THR A CB  1 
ATOM   2554 O OG1 . THR B 1 26  ? 33.215  14.040  15.325 1.00 31.33 ? 26  THR A OG1 1 
ATOM   2555 C CG2 . THR B 1 26  ? 31.200  13.075  16.156 1.00 33.60 ? 26  THR A CG2 1 
ATOM   2556 N N   . LEU B 1 27  ? 29.702  15.631  17.608 1.00 22.73 ? 27  LEU A N   1 
ATOM   2557 C CA  . LEU B 1 27  ? 28.454  15.401  18.341 1.00 19.36 ? 27  LEU A CA  1 
ATOM   2558 C C   . LEU B 1 27  ? 27.308  15.322  17.334 1.00 20.61 ? 27  LEU A C   1 
ATOM   2559 O O   . LEU B 1 27  ? 27.521  15.232  16.122 1.00 23.00 ? 27  LEU A O   1 
ATOM   2560 C CB  . LEU B 1 27  ? 28.241  16.479  19.412 1.00 20.99 ? 27  LEU A CB  1 
ATOM   2561 C CG  . LEU B 1 27  ? 28.552  17.938  19.084 1.00 18.88 ? 27  LEU A CG  1 
ATOM   2562 C CD1 . LEU B 1 27  ? 27.580  18.507  18.052 1.00 21.20 ? 27  LEU A CD1 1 
ATOM   2563 C CD2 . LEU B 1 27  ? 28.538  18.779  20.357 1.00 22.17 ? 27  LEU A CD2 1 
ATOM   2564 N N   . ASN B 1 28  ? 26.071  15.336  17.829 1.00 20.56 ? 28  ASN A N   1 
ATOM   2565 C CA  . ASN B 1 28  ? 24.900  15.162  16.984 1.00 19.07 ? 28  ASN A CA  1 
ATOM   2566 C C   . ASN B 1 28  ? 24.287  16.503  16.627 1.00 18.34 ? 28  ASN A C   1 
ATOM   2567 O O   . ASN B 1 28  ? 24.354  17.456  17.405 1.00 18.73 ? 28  ASN A O   1 
ATOM   2568 C CB  . ASN B 1 28  ? 23.829  14.325  17.682 1.00 18.13 ? 28  ASN A CB  1 
ATOM   2569 C CG  . ASN B 1 28  ? 24.385  13.034  18.220 1.00 21.12 ? 28  ASN A CG  1 
ATOM   2570 O OD1 . ASN B 1 28  ? 24.708  12.118  17.460 1.00 23.63 ? 28  ASN A OD1 1 
ATOM   2571 N ND2 . ASN B 1 28  ? 24.518  12.955  19.536 1.00 20.87 ? 28  ASN A ND2 1 
ATOM   2572 N N   . GLY B 1 29  ? 23.651  16.544  15.454 1.00 17.26 ? 29  GLY A N   1 
ATOM   2573 C CA  . GLY B 1 29  ? 22.903  17.706  15.033 1.00 19.46 ? 29  GLY A CA  1 
ATOM   2574 C C   . GLY B 1 29  ? 21.538  17.296  14.517 1.00 20.59 ? 29  GLY A C   1 
ATOM   2575 O O   . GLY B 1 29  ? 21.298  16.137  14.190 1.00 18.19 ? 29  GLY A O   1 
ATOM   2576 N N   . LEU B 1 30  ? 20.628  18.266  14.485 1.00 17.17 ? 30  LEU A N   1 
ATOM   2577 C CA  . LEU B 1 30  ? 19.244  18.037  14.078 1.00 22.21 ? 30  LEU A CA  1 
ATOM   2578 C C   . LEU B 1 30  ? 19.015  18.727  12.740 1.00 22.79 ? 30  LEU A C   1 
ATOM   2579 O O   . LEU B 1 30  ? 19.151  19.951  12.639 1.00 23.42 ? 30  LEU A O   1 
ATOM   2580 C CB  . LEU B 1 30  ? 18.266  18.561  15.128 1.00 17.20 ? 30  LEU A CB  1 
ATOM   2581 C CG  . LEU B 1 30  ? 16.779  18.261  14.917 1.00 18.68 ? 30  LEU A CG  1 
ATOM   2582 C CD1 . LEU B 1 30  ? 16.518  16.761  15.035 1.00 20.34 ? 30  LEU A CD1 1 
ATOM   2583 C CD2 . LEU B 1 30  ? 15.913  19.011  15.927 1.00 21.24 ? 30  LEU A CD2 1 
ATOM   2584 N N   . TRP B 1 31  ? 18.669  17.947  11.720 1.00 22.57 ? 31  TRP A N   1 
ATOM   2585 C CA  . TRP B 1 31  ? 18.610  18.431  10.342 1.00 23.84 ? 31  TRP A CA  1 
ATOM   2586 C C   . TRP B 1 31  ? 17.150  18.610  9.946  1.00 25.47 ? 31  TRP A C   1 
ATOM   2587 O O   . TRP B 1 31  ? 16.446  17.626  9.698  1.00 25.53 ? 31  TRP A O   1 
ATOM   2588 C CB  . TRP B 1 31  ? 19.333  17.464  9.411  1.00 26.65 ? 31  TRP A CB  1 
ATOM   2589 C CG  . TRP B 1 31  ? 19.410  17.883  7.969  1.00 27.68 ? 31  TRP A CG  1 
ATOM   2590 C CD1 . TRP B 1 31  ? 19.290  19.146  7.457  1.00 26.74 ? 31  TRP A CD1 1 
ATOM   2591 C CD2 . TRP B 1 31  ? 19.622  17.014  6.853  1.00 30.33 ? 31  TRP A CD2 1 
ATOM   2592 N NE1 . TRP B 1 31  ? 19.419  19.111  6.084  1.00 29.54 ? 31  TRP A NE1 1 
ATOM   2593 C CE2 . TRP B 1 31  ? 19.625  17.816  5.689  1.00 29.52 ? 31  TRP A CE2 1 
ATOM   2594 C CE3 . TRP B 1 31  ? 19.804  15.633  6.725  1.00 27.56 ? 31  TRP A CE3 1 
ATOM   2595 C CZ2 . TRP B 1 31  ? 19.808  17.280  4.412  1.00 28.89 ? 31  TRP A CZ2 1 
ATOM   2596 C CZ3 . TRP B 1 31  ? 19.988  15.102  5.458  1.00 30.94 ? 31  TRP A CZ3 1 
ATOM   2597 C CH2 . TRP B 1 31  ? 19.989  15.929  4.316  1.00 31.37 ? 31  TRP A CH2 1 
ATOM   2598 N N   . LEU B 1 32  ? 16.703  19.866  9.892  1.00 21.02 ? 32  LEU A N   1 
ATOM   2599 C CA  . LEU B 1 32  ? 15.333  20.212  9.543  1.00 24.61 ? 32  LEU A CA  1 
ATOM   2600 C C   . LEU B 1 32  ? 15.365  21.181  8.371  1.00 28.17 ? 32  LEU A C   1 
ATOM   2601 O O   . LEU B 1 32  ? 16.044  22.213  8.444  1.00 23.90 ? 32  LEU A O   1 
ATOM   2602 C CB  . LEU B 1 32  ? 14.625  20.845  10.740 1.00 29.43 ? 32  LEU A CB  1 
ATOM   2603 C CG  . LEU B 1 32  ? 14.488  19.956  11.983 1.00 24.98 ? 32  LEU A CG  1 
ATOM   2604 C CD1 . LEU B 1 32  ? 13.985  20.798  13.175 1.00 23.48 ? 32  LEU A CD1 1 
ATOM   2605 C CD2 . LEU B 1 32  ? 13.560  18.765  11.734 1.00 22.28 ? 32  LEU A CD2 1 
ATOM   2606 N N   . ASP B 1 33  ? 14.638  20.863  7.296  1.00 26.72 ? 33  ASP A N   1 
ATOM   2607 C CA  . ASP B 1 33  ? 14.688  21.693  6.076  1.00 27.26 ? 33  ASP A CA  1 
ATOM   2608 C C   . ASP B 1 33  ? 16.166  21.838  5.712  1.00 27.78 ? 33  ASP A C   1 
ATOM   2609 O O   . ASP B 1 33  ? 16.866  20.817  5.663  1.00 27.37 ? 33  ASP A O   1 
ATOM   2610 C CB  . ASP B 1 33  ? 13.924  22.998  6.285  1.00 27.93 ? 33  ASP A CB  1 
ATOM   2611 C CG  . ASP B 1 33  ? 12.437  22.774  6.519  1.00 31.24 ? 33  ASP A CG  1 
ATOM   2612 O OD1 . ASP B 1 33  ? 11.881  21.866  5.864  1.00 31.38 ? 33  ASP A OD1 1 
ATOM   2613 O OD2 . ASP B 1 33  ? 11.824  23.498  7.338  1.00 36.84 ? 33  ASP A OD2 1 
ATOM   2614 N N   . ASP B 1 34  ? 16.682  23.052  5.483  1.00 27.37 ? 34  ASP A N   1 
ATOM   2615 C CA  . ASP B 1 34  ? 18.083  23.234  5.116  1.00 27.22 ? 34  ASP A CA  1 
ATOM   2616 C C   . ASP B 1 34  ? 18.929  23.776  6.267  1.00 27.98 ? 34  ASP A C   1 
ATOM   2617 O O   . ASP B 1 34  ? 19.902  24.502  6.032  1.00 25.65 ? 34  ASP A O   1 
ATOM   2618 C CB  . ASP B 1 34  ? 18.219  24.149  3.893  1.00 29.14 ? 34  ASP A CB  1 
ATOM   2619 C CG  . ASP B 1 34  ? 17.565  25.518  4.090  1.00 35.38 ? 34  ASP A CG  1 
ATOM   2620 O OD1 . ASP B 1 34  ? 16.798  25.704  5.056  1.00 29.26 ? 34  ASP A OD1 1 
ATOM   2621 O OD2 . ASP B 1 34  ? 17.816  26.418  3.259  1.00 36.60 ? 34  ASP A OD2 1 
ATOM   2622 N N   . VAL B 1 35  ? 18.592  23.435  7.511  1.00 24.67 ? 35  VAL A N   1 
ATOM   2623 C CA  . VAL B 1 35  ? 19.324  23.921  8.675  1.00 24.26 ? 35  VAL A CA  1 
ATOM   2624 C C   . VAL B 1 35  ? 19.659  22.745  9.582  1.00 24.97 ? 35  VAL A C   1 
ATOM   2625 O O   . VAL B 1 35  ? 18.797  21.897  9.850  1.00 25.16 ? 35  VAL A O   1 
ATOM   2626 C CB  . VAL B 1 35  ? 18.524  24.988  9.449  1.00 26.28 ? 35  VAL A CB  1 
ATOM   2627 C CG1 . VAL B 1 35  ? 19.331  25.486  10.615 1.00 24.28 ? 35  VAL A CG1 1 
ATOM   2628 C CG2 . VAL B 1 35  ? 18.173  26.159  8.529  1.00 28.25 ? 35  VAL A CG2 1 
ATOM   2629 N N   . VAL B 1 36  ? 20.905  22.699  10.051 1.00 23.78 ? 36  VAL A N   1 
ATOM   2630 C CA  . VAL B 1 36  ? 21.341  21.767  11.085 1.00 21.46 ? 36  VAL A CA  1 
ATOM   2631 C C   . VAL B 1 36  ? 21.525  22.550  12.380 1.00 24.97 ? 36  VAL A C   1 
ATOM   2632 O O   . VAL B 1 36  ? 22.235  23.562  12.406 1.00 22.58 ? 36  VAL A O   1 
ATOM   2633 C CB  . VAL B 1 36  ? 22.636  21.040  10.680 1.00 21.73 ? 36  VAL A CB  1 
ATOM   2634 C CG1 . VAL B 1 36  ? 23.183  20.181  11.846 1.00 23.12 ? 36  VAL A CG1 1 
ATOM   2635 C CG2 . VAL B 1 36  ? 22.391  20.195  9.448  1.00 24.39 ? 36  VAL A CG2 1 
ATOM   2636 N N   . TYR B 1 37  ? 20.857  22.098  13.439 1.00 20.85 ? 37  TYR A N   1 
ATOM   2637 C CA  . TYR B 1 37  ? 20.959  22.671  14.778 1.00 19.45 ? 37  TYR A CA  1 
ATOM   2638 C C   . TYR B 1 37  ? 21.833  21.770  15.646 1.00 21.68 ? 37  TYR A C   1 
ATOM   2639 O O   . TYR B 1 37  ? 21.636  20.554  15.670 1.00 20.72 ? 37  TYR A O   1 
ATOM   2640 C CB  . TYR B 1 37  ? 19.571  22.811  15.423 1.00 17.82 ? 37  TYR A CB  1 
ATOM   2641 C CG  . TYR B 1 37  ? 18.561  23.553  14.582 1.00 22.79 ? 37  TYR A CG  1 
ATOM   2642 C CD1 . TYR B 1 37  ? 17.930  22.935  13.499 1.00 22.34 ? 37  TYR A CD1 1 
ATOM   2643 C CD2 . TYR B 1 37  ? 18.230  24.870  14.869 1.00 21.50 ? 37  TYR A CD2 1 
ATOM   2644 C CE1 . TYR B 1 37  ? 17.004  23.627  12.721 1.00 23.25 ? 37  TYR A CE1 1 
ATOM   2645 C CE2 . TYR B 1 37  ? 17.308  25.558  14.105 1.00 23.95 ? 37  TYR A CE2 1 
ATOM   2646 C CZ  . TYR B 1 37  ? 16.700  24.931  13.033 1.00 26.00 ? 37  TYR A CZ  1 
ATOM   2647 O OH  . TYR B 1 37  ? 15.792  25.635  12.270 1.00 26.84 ? 37  TYR A OH  1 
ATOM   2648 N N   . CYS B 1 38  ? 22.776  22.360  16.376 1.00 21.28 ? 38  CYS A N   1 
ATOM   2649 C CA  . CYS B 1 38  ? 23.612  21.570  17.272 1.00 19.19 ? 38  CYS A CA  1 
ATOM   2650 C C   . CYS B 1 38  ? 24.111  22.458  18.409 1.00 21.01 ? 38  CYS A C   1 
ATOM   2651 O O   . CYS B 1 38  ? 23.996  23.687  18.338 1.00 19.12 ? 38  CYS A O   1 
ATOM   2652 C CB  . CYS B 1 38  ? 24.781  20.927  16.514 1.00 18.92 ? 38  CYS A CB  1 
ATOM   2653 S SG  . CYS B 1 38  ? 26.071  22.102  16.041 1.00 22.46 ? 38  CYS A SG  1 
ATOM   2654 N N   . PRO B 1 39  ? 24.635  21.850  19.486 1.00 18.69 ? 39  PRO A N   1 
ATOM   2655 C CA  . PRO B 1 39  ? 25.184  22.660  20.588 1.00 17.99 ? 39  PRO A CA  1 
ATOM   2656 C C   . PRO B 1 39  ? 26.394  23.467  20.148 1.00 18.71 ? 39  PRO A C   1 
ATOM   2657 O O   . PRO B 1 39  ? 27.273  22.974  19.449 1.00 17.48 ? 39  PRO A O   1 
ATOM   2658 C CB  . PRO B 1 39  ? 25.562  21.611  21.646 1.00 18.65 ? 39  PRO A CB  1 
ATOM   2659 C CG  . PRO B 1 39  ? 24.715  20.395  21.297 1.00 20.04 ? 39  PRO A CG  1 
ATOM   2660 C CD  . PRO B 1 39  ? 24.670  20.413  19.802 1.00 18.67 ? 39  PRO A CD  1 
ATOM   2661 N N   . ARG B 1 40  ? 26.440  24.722  20.590 1.00 18.26 ? 40  ARG A N   1 
ATOM   2662 C CA  . ARG B 1 40  ? 27.520  25.590  20.136 1.00 20.44 ? 40  ARG A CA  1 
ATOM   2663 C C   . ARG B 1 40  ? 28.886  25.139  20.635 1.00 23.14 ? 40  ARG A C   1 
ATOM   2664 O O   . ARG B 1 40  ? 29.904  25.548  20.061 1.00 20.49 ? 40  ARG A O   1 
ATOM   2665 C CB  . ARG B 1 40  ? 27.263  27.027  20.569 1.00 18.78 ? 40  ARG A CB  1 
ATOM   2666 C CG  . ARG B 1 40  ? 27.269  27.269  22.064 1.00 20.49 ? 40  ARG A CG  1 
ATOM   2667 C CD  . ARG B 1 40  ? 27.050  28.750  22.339 1.00 19.50 ? 40  ARG A CD  1 
ATOM   2668 N NE  . ARG B 1 40  ? 26.962  29.063  23.763 1.00 20.73 ? 40  ARG A NE  1 
ATOM   2669 C CZ  . ARG B 1 40  ? 26.962  30.290  24.261 1.00 22.25 ? 40  ARG A CZ  1 
ATOM   2670 N NH1 . ARG B 1 40  ? 27.009  31.358  23.472 1.00 22.83 ? 40  ARG A NH1 1 
ATOM   2671 N NH2 . ARG B 1 40  ? 26.948  30.452  25.582 1.00 20.31 ? 40  ARG A NH2 1 
ATOM   2672 N N   . HIS B 1 41  ? 28.944  24.314  21.694 1.00 19.29 ? 41  HIS A N   1 
ATOM   2673 C CA  . HIS B 1 41  ? 30.263  23.920  22.187 1.00 21.63 ? 41  HIS A CA  1 
ATOM   2674 C C   . HIS B 1 41  ? 30.948  22.893  21.298 1.00 20.89 ? 41  HIS A C   1 
ATOM   2675 O O   . HIS B 1 41  ? 32.055  22.452  21.611 1.00 23.87 ? 41  HIS A O   1 
ATOM   2676 C CB  . HIS B 1 41  ? 30.175  23.446  23.641 1.00 22.75 ? 41  HIS A CB  1 
ATOM   2677 C CG  . HIS B 1 41  ? 29.475  22.134  23.835 1.00 20.45 ? 41  HIS A CG  1 
ATOM   2678 N ND1 . HIS B 1 41  ? 28.196  22.043  24.341 1.00 22.96 ? 41  HIS A ND1 1 
ATOM   2679 C CD2 . HIS B 1 41  ? 29.893  20.859  23.640 1.00 25.41 ? 41  HIS A CD2 1 
ATOM   2680 C CE1 . HIS B 1 41  ? 27.848  20.769  24.432 1.00 19.78 ? 41  HIS A CE1 1 
ATOM   2681 N NE2 . HIS B 1 41  ? 28.863  20.030  24.020 1.00 24.42 ? 41  HIS A NE2 1 
ATOM   2682 N N   . VAL B 1 42  ? 30.354  22.539  20.156 1.00 20.60 ? 42  VAL A N   1 
ATOM   2683 C CA  . VAL B 1 42  ? 31.078  21.797  19.125 1.00 21.63 ? 42  VAL A CA  1 
ATOM   2684 C C   . VAL B 1 42  ? 32.317  22.551  18.641 1.00 26.35 ? 42  VAL A C   1 
ATOM   2685 O O   . VAL B 1 42  ? 33.264  21.929  18.139 1.00 25.81 ? 42  VAL A O   1 
ATOM   2686 C CB  . VAL B 1 42  ? 30.134  21.489  17.945 1.00 19.43 ? 42  VAL A CB  1 
ATOM   2687 C CG1 . VAL B 1 42  ? 29.800  22.774  17.167 1.00 25.17 ? 42  VAL A CG1 1 
ATOM   2688 C CG2 . VAL B 1 42  ? 30.714  20.402  17.041 1.00 23.05 ? 42  VAL A CG2 1 
ATOM   2689 N N   . ILE B 1 43  ? 32.347  23.882  18.794 1.00 23.91 ? 43  ILE A N   1 
ATOM   2690 C CA  . ILE B 1 43  ? 33.518  24.654  18.354 1.00 23.00 ? 43  ILE A CA  1 
ATOM   2691 C C   . ILE B 1 43  ? 34.612  24.742  19.410 1.00 30.81 ? 43  ILE A C   1 
ATOM   2692 O O   . ILE B 1 43  ? 35.687  25.308  19.135 1.00 29.25 ? 43  ILE A O   1 
ATOM   2693 C CB  . ILE B 1 43  ? 33.146  26.089  17.920 1.00 22.97 ? 43  ILE A CB  1 
ATOM   2694 C CG1 . ILE B 1 43  ? 32.850  26.994  19.132 1.00 23.23 ? 43  ILE A CG1 1 
ATOM   2695 C CG2 . ILE B 1 43  ? 31.975  26.055  16.958 1.00 26.04 ? 43  ILE A CG2 1 
ATOM   2696 C CD1 . ILE B 1 43  ? 32.324  28.402  18.774 1.00 24.30 ? 43  ILE A CD1 1 
ATOM   2697 N N   . CYS B 1 44  ? 34.395  24.190  20.594 1.00 29.18 ? 44  CYS A N   1 
ATOM   2698 C CA  . CYS B 1 44  ? 35.347  24.322  21.687 1.00 29.45 ? 44  CYS A CA  1 
ATOM   2699 C C   . CYS B 1 44  ? 36.389  23.214  21.618 1.00 33.26 ? 44  CYS A C   1 
ATOM   2700 O O   . CYS B 1 44  ? 36.081  22.084  21.237 1.00 32.43 ? 44  CYS A O   1 
ATOM   2701 C CB  . CYS B 1 44  ? 34.617  24.243  23.026 1.00 29.25 ? 44  CYS A CB  1 
ATOM   2702 S SG  . CYS B 1 44  ? 33.704  25.731  23.438 1.00 29.12 ? 44  CYS A SG  1 
ATOM   2703 N N   . THR B 1 45  ? 37.622  23.546  21.982 1.00 33.69 ? 45  THR A N   1 
ATOM   2704 C CA  . THR B 1 45  ? 38.578  22.519  22.364 1.00 37.19 ? 45  THR A CA  1 
ATOM   2705 C C   . THR B 1 45  ? 38.419  22.220  23.854 1.00 39.22 ? 45  THR A C   1 
ATOM   2706 O O   . THR B 1 45  ? 37.698  22.910  24.578 1.00 39.23 ? 45  THR A O   1 
ATOM   2707 C CB  . THR B 1 45  ? 40.014  22.957  22.070 1.00 36.67 ? 45  THR A CB  1 
ATOM   2708 O OG1 . THR B 1 45  ? 40.390  23.982  22.994 1.00 39.72 ? 45  THR A OG1 1 
ATOM   2709 C CG2 . THR B 1 45  ? 40.144  23.494  20.645 1.00 32.42 ? 45  THR A CG2 1 
ATOM   2710 N N   . SER B 1 46  ? 39.118  21.183  24.321 1.00 41.20 ? 46  SER A N   1 
ATOM   2711 C CA  . SER B 1 46  ? 39.049  20.849  25.740 1.00 41.67 ? 46  SER A CA  1 
ATOM   2712 C C   . SER B 1 46  ? 39.532  22.005  26.613 1.00 40.80 ? 46  SER A C   1 
ATOM   2713 O O   . SER B 1 46  ? 39.019  22.201  27.721 1.00 42.35 ? 46  SER A O   1 
ATOM   2714 C CB  . SER B 1 46  ? 39.855  19.582  26.022 1.00 45.00 ? 46  SER A CB  1 
ATOM   2715 O OG  . SER B 1 46  ? 41.182  19.898  26.404 1.00 50.05 ? 46  SER A OG  1 
ATOM   2716 N N   . GLU B 1 47  ? 40.497  22.790  26.129 1.00 42.37 ? 47  GLU A N   1 
ATOM   2717 C CA  . GLU B 1 47  ? 40.944  23.963  26.874 1.00 41.52 ? 47  GLU A CA  1 
ATOM   2718 C C   . GLU B 1 47  ? 39.871  25.047  26.876 1.00 36.32 ? 47  GLU A C   1 
ATOM   2719 O O   . GLU B 1 47  ? 39.582  25.649  27.917 1.00 36.38 ? 47  GLU A O   1 
ATOM   2720 C CB  . GLU B 1 47  ? 42.248  24.502  26.283 1.00 43.93 ? 47  GLU A CB  1 
ATOM   2721 C CG  . GLU B 1 47  ? 43.226  23.421  25.799 1.00 50.14 ? 47  GLU A CG  1 
ATOM   2722 C CD  . GLU B 1 47  ? 42.908  22.908  24.393 1.00 51.11 ? 47  GLU A CD  1 
ATOM   2723 O OE1 . GLU B 1 47  ? 43.112  23.671  23.416 1.00 52.18 ? 47  GLU A OE1 1 
ATOM   2724 O OE2 . GLU B 1 47  ? 42.443  21.751  24.269 1.00 46.32 ? 47  GLU A OE2 1 
ATOM   2725 N N   . ASP B 1 48  ? 39.263  25.301  25.713 1.00 35.78 ? 48  ASP A N   1 
ATOM   2726 C CA  . ASP B 1 48  ? 38.200  26.299  25.618 1.00 36.23 ? 48  ASP A CA  1 
ATOM   2727 C C   . ASP B 1 48  ? 37.065  26.026  26.597 1.00 30.60 ? 48  ASP A C   1 
ATOM   2728 O O   . ASP B 1 48  ? 36.460  26.971  27.116 1.00 29.38 ? 48  ASP A O   1 
ATOM   2729 C CB  . ASP B 1 48  ? 37.628  26.338  24.200 1.00 32.56 ? 48  ASP A CB  1 
ATOM   2730 C CG  . ASP B 1 48  ? 38.611  26.858  23.190 1.00 35.91 ? 48  ASP A CG  1 
ATOM   2731 O OD1 . ASP B 1 48  ? 39.448  27.710  23.563 1.00 36.49 ? 48  ASP A OD1 1 
ATOM   2732 O OD2 . ASP B 1 48  ? 38.520  26.429  22.023 1.00 34.59 ? 48  ASP A OD2 1 
ATOM   2733 N N   . MET B 1 49  ? 36.773  24.744  26.860 1.00 32.56 ? 49  MET A N   1 
ATOM   2734 C CA  . MET B 1 49  ? 35.583  24.352  27.620 1.00 29.72 ? 49  MET A CA  1 
ATOM   2735 C C   . MET B 1 49  ? 35.533  24.962  29.011 1.00 30.29 ? 49  MET A C   1 
ATOM   2736 O O   . MET B 1 49  ? 34.435  25.195  29.541 1.00 25.69 ? 49  MET A O   1 
ATOM   2737 C CB  . MET B 1 49  ? 35.513  22.829  27.743 1.00 31.07 ? 49  MET A CB  1 
ATOM   2738 C CG  . MET B 1 49  ? 34.115  22.257  27.650 1.00 36.57 ? 49  MET A CG  1 
ATOM   2739 S SD  . MET B 1 49  ? 33.258  22.681  26.133 1.00 44.70 ? 49  MET A SD  1 
ATOM   2740 C CE  . MET B 1 49  ? 33.399  21.098  25.296 1.00 35.13 ? 49  MET A CE  1 
ATOM   2741 N N   . LEU B 1 50  ? 36.690  25.230  29.625 1.00 28.31 ? 50  LEU A N   1 
ATOM   2742 C CA  . LEU B 1 50  ? 36.681  25.681  31.014 1.00 30.79 ? 50  LEU A CA  1 
ATOM   2743 C C   . LEU B 1 50  ? 36.151  27.104  31.160 1.00 31.65 ? 50  LEU A C   1 
ATOM   2744 O O   . LEU B 1 50  ? 35.562  27.435  32.193 1.00 32.37 ? 50  LEU A O   1 
ATOM   2745 C CB  . LEU B 1 50  ? 38.081  25.573  31.614 1.00 30.98 ? 50  LEU A CB  1 
ATOM   2746 C CG  . LEU B 1 50  ? 38.637  24.148  31.588 1.00 35.92 ? 50  LEU A CG  1 
ATOM   2747 C CD1 . LEU B 1 50  ? 40.162  24.155  31.564 1.00 36.56 ? 50  LEU A CD1 1 
ATOM   2748 C CD2 . LEU B 1 50  ? 38.084  23.313  32.751 1.00 30.06 ? 50  LEU A CD2 1 
ATOM   2749 N N   . ASN B 1 51  ? 36.359  27.961  30.158 1.00 31.99 ? 51  ASN A N   1 
ATOM   2750 C CA  . ASN B 1 51  ? 35.813  29.308  30.206 1.00 31.37 ? 51  ASN A CA  1 
ATOM   2751 C C   . ASN B 1 51  ? 35.758  29.862  28.788 1.00 32.10 ? 51  ASN A C   1 
ATOM   2752 O O   . ASN B 1 51  ? 36.590  30.695  28.410 1.00 34.06 ? 51  ASN A O   1 
ATOM   2753 C CB  . ASN B 1 51  ? 36.658  30.220  31.096 1.00 34.55 ? 51  ASN A CB  1 
ATOM   2754 C CG  . ASN B 1 51  ? 35.951  31.525  31.420 1.00 42.61 ? 51  ASN A CG  1 
ATOM   2755 O OD1 . ASN B 1 51  ? 34.892  31.824  30.866 1.00 40.64 ? 51  ASN A OD1 1 
ATOM   2756 N ND2 . ASN B 1 51  ? 36.534  32.309  32.320 1.00 44.89 ? 51  ASN A ND2 1 
ATOM   2757 N N   . PRO B 1 52  ? 34.800  29.420  27.983 1.00 26.95 ? 52  PRO A N   1 
ATOM   2758 C CA  . PRO B 1 52  ? 34.800  29.761  26.557 1.00 23.69 ? 52  PRO A CA  1 
ATOM   2759 C C   . PRO B 1 52  ? 34.166  31.113  26.271 1.00 27.32 ? 52  PRO A C   1 
ATOM   2760 O O   . PRO B 1 52  ? 33.145  31.485  26.853 1.00 28.15 ? 52  PRO A O   1 
ATOM   2761 C CB  . PRO B 1 52  ? 33.978  28.622  25.935 1.00 28.26 ? 52  PRO A CB  1 
ATOM   2762 C CG  . PRO B 1 52  ? 32.998  28.263  27.018 1.00 28.60 ? 52  PRO A CG  1 
ATOM   2763 C CD  . PRO B 1 52  ? 33.677  28.538  28.349 1.00 27.01 ? 52  PRO A CD  1 
ATOM   2764 N N   . ASN B 1 53  ? 34.795  31.861  25.360 1.00 27.20 ? 53  ASN A N   1 
ATOM   2765 C CA  . ASN B 1 53  ? 34.180  33.064  24.792 1.00 27.68 ? 53  ASN A CA  1 
ATOM   2766 C C   . ASN B 1 53  ? 33.609  32.640  23.441 1.00 26.61 ? 53  ASN A C   1 
ATOM   2767 O O   . ASN B 1 53  ? 34.304  32.632  22.424 1.00 27.42 ? 53  ASN A O   1 
ATOM   2768 C CB  . ASN B 1 53  ? 35.186  34.200  24.649 1.00 32.83 ? 53  ASN A CB  1 
ATOM   2769 C CG  . ASN B 1 53  ? 34.523  35.508  24.243 1.00 34.10 ? 53  ASN A CG  1 
ATOM   2770 O OD1 . ASN B 1 53  ? 33.639  35.530  23.381 1.00 31.83 ? 53  ASN A OD1 1 
ATOM   2771 N ND2 . ASN B 1 53  ? 34.949  36.606  24.860 1.00 40.48 ? 53  ASN A ND2 1 
ATOM   2772 N N   . TYR B 1 54  ? 32.327  32.258  23.434 1.00 26.47 ? 54  TYR A N   1 
ATOM   2773 C CA  . TYR B 1 54  ? 31.774  31.613  22.247 1.00 25.43 ? 54  TYR A CA  1 
ATOM   2774 C C   . TYR B 1 54  ? 31.744  32.551  21.050 1.00 27.19 ? 54  TYR A C   1 
ATOM   2775 O O   . TYR B 1 54  ? 32.037  32.132  19.922 1.00 26.59 ? 54  TYR A O   1 
ATOM   2776 C CB  . TYR B 1 54  ? 30.373  31.084  22.540 1.00 24.49 ? 54  TYR A CB  1 
ATOM   2777 C CG  . TYR B 1 54  ? 30.388  29.802  23.330 1.00 25.30 ? 54  TYR A CG  1 
ATOM   2778 C CD1 . TYR B 1 54  ? 30.748  28.607  22.722 1.00 23.30 ? 54  TYR A CD1 1 
ATOM   2779 C CD2 . TYR B 1 54  ? 30.030  29.777  24.676 1.00 23.30 ? 54  TYR A CD2 1 
ATOM   2780 C CE1 . TYR B 1 54  ? 30.748  27.433  23.423 1.00 24.78 ? 54  TYR A CE1 1 
ATOM   2781 C CE2 . TYR B 1 54  ? 30.030  28.597  25.389 1.00 21.26 ? 54  TYR A CE2 1 
ATOM   2782 C CZ  . TYR B 1 54  ? 30.394  27.426  24.751 1.00 23.39 ? 54  TYR A CZ  1 
ATOM   2783 O OH  . TYR B 1 54  ? 30.411  26.219  25.429 1.00 23.59 ? 54  TYR A OH  1 
ATOM   2784 N N   . GLU B 1 55  ? 31.353  33.810  21.265 1.00 30.38 ? 55  GLU A N   1 
ATOM   2785 C CA  . GLU B 1 55  ? 31.315  34.752  20.153 1.00 27.92 ? 55  GLU A CA  1 
ATOM   2786 C C   . GLU B 1 55  ? 32.696  34.910  19.540 1.00 28.36 ? 55  GLU A C   1 
ATOM   2787 O O   . GLU B 1 55  ? 32.847  34.852  18.315 1.00 26.81 ? 55  GLU A O   1 
ATOM   2788 C CB  . GLU B 1 55  ? 30.731  36.093  20.608 1.00 28.84 ? 55  GLU A CB  1 
ATOM   2789 C CG  . GLU B 1 55  ? 29.330  35.997  21.231 1.00 32.19 ? 55  GLU A CG  1 
ATOM   2790 C CD  . GLU B 1 55  ? 29.323  35.738  22.735 1.00 36.94 ? 55  GLU A CD  1 
ATOM   2791 O OE1 . GLU B 1 55  ? 30.329  35.215  23.276 1.00 39.28 ? 55  GLU A OE1 1 
ATOM   2792 O OE2 . GLU B 1 55  ? 28.288  36.047  23.373 1.00 42.81 ? 55  GLU A OE2 1 
ATOM   2793 N N   . ASP B 1 56  ? 33.727  35.022  20.379 1.00 26.62 ? 56  ASP A N   1 
ATOM   2794 C CA  . ASP B 1 56  ? 35.083  35.150  19.859 1.00 28.47 ? 56  ASP A CA  1 
ATOM   2795 C C   . ASP B 1 56  ? 35.541  33.870  19.169 1.00 29.96 ? 56  ASP A C   1 
ATOM   2796 O O   . ASP B 1 56  ? 36.172  33.916  18.103 1.00 27.23 ? 56  ASP A O   1 
ATOM   2797 C CB  . ASP B 1 56  ? 36.029  35.515  20.995 1.00 32.11 ? 56  ASP A CB  1 
ATOM   2798 C CG  . ASP B 1 56  ? 37.424  35.812  20.503 1.00 32.80 ? 56  ASP A CG  1 
ATOM   2799 O OD1 . ASP B 1 56  ? 37.639  36.946  20.026 1.00 37.16 ? 56  ASP A OD1 1 
ATOM   2800 O OD2 . ASP B 1 56  ? 38.286  34.914  20.577 1.00 31.73 ? 56  ASP A OD2 1 
ATOM   2801 N N   . LEU B 1 57  ? 35.237  32.710  19.759 1.00 24.00 ? 57  LEU A N   1 
ATOM   2802 C CA  . LEU B 1 57  ? 35.661  31.455  19.158 1.00 24.96 ? 57  LEU A CA  1 
ATOM   2803 C C   . LEU B 1 57  ? 34.994  31.246  17.807 1.00 23.70 ? 57  LEU A C   1 
ATOM   2804 O O   . LEU B 1 57  ? 35.605  30.698  16.885 1.00 25.91 ? 57  LEU A O   1 
ATOM   2805 C CB  . LEU B 1 57  ? 35.342  30.291  20.105 1.00 25.68 ? 57  LEU A CB  1 
ATOM   2806 C CG  . LEU B 1 57  ? 36.203  30.199  21.362 1.00 27.86 ? 57  LEU A CG  1 
ATOM   2807 C CD1 . LEU B 1 57  ? 35.700  29.089  22.292 1.00 30.39 ? 57  LEU A CD1 1 
ATOM   2808 C CD2 . LEU B 1 57  ? 37.661  29.984  20.992 1.00 32.49 ? 57  LEU A CD2 1 
ATOM   2809 N N   . LEU B 1 58  ? 33.734  31.674  17.674 1.00 24.44 ? 58  LEU A N   1 
ATOM   2810 C CA  . LEU B 1 58  ? 32.997  31.409  16.440 1.00 23.80 ? 58  LEU A CA  1 
ATOM   2811 C C   . LEU B 1 58  ? 33.495  32.269  15.287 1.00 24.94 ? 58  LEU A C   1 
ATOM   2812 O O   . LEU B 1 58  ? 33.436  31.847  14.130 1.00 26.07 ? 58  LEU A O   1 
ATOM   2813 C CB  . LEU B 1 58  ? 31.501  31.638  16.658 1.00 27.40 ? 58  LEU A CB  1 
ATOM   2814 C CG  . LEU B 1 58  ? 30.583  31.216  15.507 1.00 29.22 ? 58  LEU A CG  1 
ATOM   2815 C CD1 . LEU B 1 58  ? 30.716  29.719  15.249 1.00 26.16 ? 58  LEU A CD1 1 
ATOM   2816 C CD2 . LEU B 1 58  ? 29.139  31.580  15.826 1.00 29.28 ? 58  LEU A CD2 1 
ATOM   2817 N N   . ILE B 1 59  ? 33.959  33.485  15.574 1.00 27.24 ? 59  ILE A N   1 
ATOM   2818 C CA  . ILE B 1 59  ? 34.527  34.323  14.521 1.00 29.48 ? 59  ILE A CA  1 
ATOM   2819 C C   . ILE B 1 59  ? 35.686  33.615  13.837 1.00 27.75 ? 59  ILE A C   1 
ATOM   2820 O O   . ILE B 1 59  ? 35.882  33.745  12.621 1.00 29.57 ? 59  ILE A O   1 
ATOM   2821 C CB  . ILE B 1 59  ? 34.941  35.686  15.102 1.00 27.31 ? 59  ILE A CB  1 
ATOM   2822 C CG1 . ILE B 1 59  ? 33.697  36.528  15.377 1.00 27.52 ? 59  ILE A CG1 1 
ATOM   2823 C CG2 . ILE B 1 59  ? 35.962  36.377  14.197 1.00 31.44 ? 59  ILE A CG2 1 
ATOM   2824 C CD1 . ILE B 1 59  ? 33.943  37.722  16.276 1.00 32.66 ? 59  ILE A CD1 1 
ATOM   2825 N N   . ARG B 1 60  ? 36.446  32.822  14.595 1.00 27.50 ? 60  ARG A N   1 
ATOM   2826 C CA  . ARG B 1 60  ? 37.594  32.101  14.067 1.00 29.58 ? 60  ARG A CA  1 
ATOM   2827 C C   . ARG B 1 60  ? 37.208  30.912  13.196 1.00 33.07 ? 60  ARG A C   1 
ATOM   2828 O O   . ARG B 1 60  ? 38.090  30.295  12.583 1.00 30.99 ? 60  ARG A O   1 
ATOM   2829 C CB  . ARG B 1 60  ? 38.459  31.632  15.230 1.00 34.52 ? 60  ARG A CB  1 
ATOM   2830 C CG  . ARG B 1 60  ? 38.880  32.764  16.160 1.00 33.49 ? 60  ARG A CG  1 
ATOM   2831 C CD  . ARG B 1 60  ? 40.322  33.159  15.908 1.00 43.30 ? 60  ARG A CD  1 
ATOM   2832 N NE  . ARG B 1 60  ? 41.233  32.046  16.165 1.00 51.76 ? 60  ARG A NE  1 
ATOM   2833 C CZ  . ARG B 1 60  ? 41.915  31.394  15.230 1.00 51.54 ? 60  ARG A CZ  1 
ATOM   2834 N NH1 . ARG B 1 60  ? 41.818  31.716  13.949 1.00 47.94 ? 60  ARG A NH1 1 
ATOM   2835 N NH2 . ARG B 1 60  ? 42.712  30.391  15.591 1.00 53.89 ? 60  ARG A NH2 1 
ATOM   2836 N N   . LYS B 1 61  ? 35.928  30.570  13.130 1.00 29.82 ? 61  LYS A N   1 
ATOM   2837 C CA  . LYS B 1 61  ? 35.478  29.437  12.344 1.00 29.55 ? 61  LYS A CA  1 
ATOM   2838 C C   . LYS B 1 61  ? 34.953  29.914  10.993 1.00 28.01 ? 61  LYS A C   1 
ATOM   2839 O O   . LYS B 1 61  ? 34.489  31.047  10.852 1.00 31.82 ? 61  LYS A O   1 
ATOM   2840 C CB  . LYS B 1 61  ? 34.388  28.663  13.105 1.00 24.75 ? 61  LYS A CB  1 
ATOM   2841 C CG  . LYS B 1 61  ? 34.871  28.059  14.415 1.00 27.75 ? 61  LYS A CG  1 
ATOM   2842 C CD  . LYS B 1 61  ? 36.062  27.132  14.194 1.00 32.39 ? 61  LYS A CD  1 
ATOM   2843 C CE  . LYS B 1 61  ? 36.500  26.456  15.485 1.00 35.91 ? 61  LYS A CE  1 
ATOM   2844 N NZ  . LYS B 1 61  ? 37.473  25.360  15.208 1.00 40.15 ? 61  LYS A NZ  1 
ATOM   2845 N N   . SER B 1 62  ? 35.031  29.032  9.998  1.00 28.19 ? 62  SER A N   1 
ATOM   2846 C CA  . SER B 1 62  ? 34.456  29.253  8.678  1.00 30.62 ? 62  SER A CA  1 
ATOM   2847 C C   . SER B 1 62  ? 33.472  28.135  8.372  1.00 30.90 ? 62  SER A C   1 
ATOM   2848 O O   . SER B 1 62  ? 33.433  27.116  9.063  1.00 30.63 ? 62  SER A O   1 
ATOM   2849 C CB  . SER B 1 62  ? 35.537  29.295  7.593  1.00 32.28 ? 62  SER A CB  1 
ATOM   2850 O OG  . SER B 1 62  ? 35.881  27.973  7.191  1.00 36.84 ? 62  SER A OG  1 
ATOM   2851 N N   . ASN B 1 63  ? 32.679  28.330  7.310  1.00 28.81 ? 63  ASN A N   1 
ATOM   2852 C CA  . ASN B 1 63  ? 31.705  27.312  6.908  1.00 30.15 ? 63  ASN A CA  1 
ATOM   2853 C C   . ASN B 1 63  ? 32.346  25.939  6.739  1.00 30.56 ? 63  ASN A C   1 
ATOM   2854 O O   . ASN B 1 63  ? 31.746  24.917  7.097  1.00 30.50 ? 63  ASN A O   1 
ATOM   2855 C CB  . ASN B 1 63  ? 31.017  27.716  5.609  1.00 30.07 ? 63  ASN A CB  1 
ATOM   2856 C CG  . ASN B 1 63  ? 30.023  28.844  5.793  1.00 32.38 ? 63  ASN A CG  1 
ATOM   2857 O OD1 . ASN B 1 63  ? 29.421  29.003  6.858  1.00 29.25 ? 63  ASN A OD1 1 
ATOM   2858 N ND2 . ASN B 1 63  ? 29.840  29.635  4.744  1.00 34.56 ? 63  ASN A ND2 1 
ATOM   2859 N N   . HIS B 1 64  ? 33.559  25.884  6.187  1.00 30.13 ? 64  HIS A N   1 
ATOM   2860 C CA  . HIS B 1 64  ? 34.150  24.590  5.872  1.00 30.84 ? 64  HIS A CA  1 
ATOM   2861 C C   . HIS B 1 64  ? 34.772  23.914  7.085  1.00 32.11 ? 64  HIS A C   1 
ATOM   2862 O O   . HIS B 1 64  ? 35.122  22.730  6.999  1.00 34.51 ? 64  HIS A O   1 
ATOM   2863 C CB  . HIS B 1 64  ? 35.207  24.723  4.772  1.00 33.67 ? 64  HIS A CB  1 
ATOM   2864 C CG  . HIS B 1 64  ? 36.616  24.807  5.286  1.00 37.04 ? 64  HIS A CG  1 
ATOM   2865 N ND1 . HIS B 1 64  ? 37.161  25.964  5.798  1.00 37.52 ? 64  HIS A ND1 1 
ATOM   2866 C CD2 . HIS B 1 64  ? 37.603  23.877  5.325  1.00 39.46 ? 64  HIS A CD2 1 
ATOM   2867 C CE1 . HIS B 1 64  ? 38.418  25.742  6.145  1.00 42.91 ? 64  HIS A CE1 1 
ATOM   2868 N NE2 . HIS B 1 64  ? 38.710  24.482  5.872  1.00 41.98 ? 64  HIS A NE2 1 
ATOM   2869 N N   . ASN B 1 65  ? 34.920  24.627  8.206  1.00 29.04 ? 65  ASN A N   1 
ATOM   2870 C CA  . ASN B 1 65  ? 35.351  23.993  9.443  1.00 29.21 ? 65  ASN A CA  1 
ATOM   2871 C C   . ASN B 1 65  ? 34.283  23.057  10.005 1.00 31.84 ? 65  ASN A C   1 
ATOM   2872 O O   . ASN B 1 65  ? 34.583  22.255  10.897 1.00 30.06 ? 65  ASN A O   1 
ATOM   2873 C CB  . ASN B 1 65  ? 35.710  25.058  10.481 1.00 29.03 ? 65  ASN A CB  1 
ATOM   2874 C CG  . ASN B 1 65  ? 36.942  25.872  10.102 1.00 33.02 ? 65  ASN A CG  1 
ATOM   2875 O OD1 . ASN B 1 65  ? 37.090  27.020  10.528 1.00 35.10 ? 65  ASN A OD1 1 
ATOM   2876 N ND2 . ASN B 1 65  ? 37.849  25.269  9.340  1.00 33.76 ? 65  ASN A ND2 1 
ATOM   2877 N N   . PHE B 1 66  ? 33.053  23.138  9.505  1.00 26.51 ? 66  PHE A N   1 
ATOM   2878 C CA  . PHE B 1 66  ? 31.952  22.305  9.986  1.00 30.43 ? 66  PHE A CA  1 
ATOM   2879 C C   . PHE B 1 66  ? 31.754  21.137  9.019  1.00 28.40 ? 66  PHE A C   1 
ATOM   2880 O O   . PHE B 1 66  ? 31.325  21.322  7.875  1.00 32.48 ? 66  PHE A O   1 
ATOM   2881 C CB  . PHE B 1 66  ? 30.677  23.132  10.149 1.00 26.13 ? 66  PHE A CB  1 
ATOM   2882 C CG  . PHE B 1 66  ? 30.800  24.241  11.164 1.00 29.38 ? 66  PHE A CG  1 
ATOM   2883 C CD1 . PHE B 1 66  ? 30.774  23.963  12.525 1.00 30.28 ? 66  PHE A CD1 1 
ATOM   2884 C CD2 . PHE B 1 66  ? 30.947  25.558  10.764 1.00 25.14 ? 66  PHE A CD2 1 
ATOM   2885 C CE1 . PHE B 1 66  ? 30.897  24.977  13.462 1.00 29.75 ? 66  PHE A CE1 1 
ATOM   2886 C CE2 . PHE B 1 66  ? 31.075  26.584  11.701 1.00 29.98 ? 66  PHE A CE2 1 
ATOM   2887 C CZ  . PHE B 1 66  ? 31.052  26.291  13.048 1.00 30.60 ? 66  PHE A CZ  1 
ATOM   2888 N N   . LEU B 1 67  ? 32.072  19.939  9.474  1.00 27.73 ? 67  LEU A N   1 
ATOM   2889 C CA  . LEU B 1 67  ? 31.847  18.730  8.697  1.00 29.59 ? 67  LEU A CA  1 
ATOM   2890 C C   . LEU B 1 67  ? 30.545  18.110  9.191  1.00 29.70 ? 67  LEU A C   1 
ATOM   2891 O O   . LEU B 1 67  ? 30.437  17.756  10.368 1.00 28.27 ? 67  LEU A O   1 
ATOM   2892 C CB  . LEU B 1 67  ? 33.021  17.767  8.847  1.00 30.01 ? 67  LEU A CB  1 
ATOM   2893 C CG  . LEU B 1 67  ? 32.877  16.293  8.466  1.00 34.00 ? 67  LEU A CG  1 
ATOM   2894 C CD1 . LEU B 1 67  ? 32.296  16.132  7.058  1.00 34.64 ? 67  LEU A CD1 1 
ATOM   2895 C CD2 . LEU B 1 67  ? 34.244  15.624  8.542  1.00 35.69 ? 67  LEU A CD2 1 
ATOM   2896 N N   . VAL B 1 68  ? 29.558  18.014  8.304  1.00 27.48 ? 68  VAL A N   1 
ATOM   2897 C CA  . VAL B 1 68  ? 28.221  17.528  8.640  1.00 30.13 ? 68  VAL A CA  1 
ATOM   2898 C C   . VAL B 1 68  ? 27.928  16.305  7.784  1.00 29.33 ? 68  VAL A C   1 
ATOM   2899 O O   . VAL B 1 68  ? 27.988  16.373  6.553  1.00 31.57 ? 68  VAL A O   1 
ATOM   2900 C CB  . VAL B 1 68  ? 27.149  18.601  8.418  1.00 27.12 ? 68  VAL A CB  1 
ATOM   2901 C CG1 . VAL B 1 68  ? 25.758  18.053  8.758  1.00 24.37 ? 68  VAL A CG1 1 
ATOM   2902 C CG2 . VAL B 1 68  ? 27.459  19.842  9.226  1.00 30.58 ? 68  VAL A CG2 1 
ATOM   2903 N N   . GLN B 1 69  ? 27.584  15.198  8.427  1.00 29.92 ? 69  GLN A N   1 
ATOM   2904 C CA  . GLN B 1 69  ? 27.371  13.941  7.720  1.00 28.12 ? 69  GLN A CA  1 
ATOM   2905 C C   . GLN B 1 69  ? 26.001  13.387  8.070  1.00 24.21 ? 69  GLN A C   1 
ATOM   2906 O O   . GLN B 1 69  ? 25.639  13.313  9.247  1.00 27.38 ? 69  GLN A O   1 
ATOM   2907 C CB  . GLN B 1 69  ? 28.475  12.934  8.046  1.00 30.33 ? 69  GLN A CB  1 
ATOM   2908 C CG  . GLN B 1 69  ? 29.753  13.609  8.523  1.00 35.71 ? 69  GLN A CG  1 
ATOM   2909 C CD  . GLN B 1 69  ? 30.966  12.693  8.522  1.00 43.11 ? 69  GLN A CD  1 
ATOM   2910 O OE1 . GLN B 1 69  ? 31.193  11.936  7.572  1.00 41.90 ? 69  GLN A OE1 1 
ATOM   2911 N NE2 . GLN B 1 69  ? 31.772  12.783  9.580  1.00 39.92 ? 69  GLN A NE2 1 
ATOM   2912 N N   . ALA B 1 70  ? 25.244  13.021  7.041  1.00 25.74 ? 70  ALA A N   1 
ATOM   2913 C CA  . ALA B 1 70  ? 23.932  12.394  7.172  1.00 28.44 ? 70  ALA A CA  1 
ATOM   2914 C C   . ALA B 1 70  ? 24.093  10.985  6.619  1.00 34.57 ? 70  ALA A C   1 
ATOM   2915 O O   . ALA B 1 70  ? 24.088  10.786  5.401  1.00 34.25 ? 70  ALA A O   1 
ATOM   2916 C CB  . ALA B 1 70  ? 22.866  13.184  6.422  1.00 29.65 ? 70  ALA A CB  1 
ATOM   2917 N N   . GLY B 1 71  ? 24.262  10.016  7.513  1.00 34.03 ? 71  GLY A N   1 
ATOM   2918 C CA  . GLY B 1 71  ? 24.634  8.683   7.066  1.00 35.18 ? 71  GLY A CA  1 
ATOM   2919 C C   . GLY B 1 71  ? 25.968  8.740   6.343  1.00 37.64 ? 71  GLY A C   1 
ATOM   2920 O O   . GLY B 1 71  ? 26.979  9.207   6.886  1.00 40.53 ? 71  GLY A O   1 
ATOM   2921 N N   . ASN B 1 72  ? 25.963  8.297   5.086  1.00 41.80 ? 72  ASN A N   1 
ATOM   2922 C CA  . ASN B 1 72  ? 27.148  8.249   4.238  1.00 46.14 ? 72  ASN A CA  1 
ATOM   2923 C C   . ASN B 1 72  ? 27.233  9.425   3.268  1.00 47.19 ? 72  ASN A C   1 
ATOM   2924 O O   . ASN B 1 72  ? 27.894  9.313   2.230  1.00 50.39 ? 72  ASN A O   1 
ATOM   2925 C CB  . ASN B 1 72  ? 27.176  6.932   3.458  1.00 48.70 ? 72  ASN A CB  1 
ATOM   2926 C CG  . ASN B 1 72  ? 25.835  6.614   2.808  1.00 52.16 ? 72  ASN A CG  1 
ATOM   2927 O OD1 . ASN B 1 72  ? 24.809  7.203   3.158  1.00 52.50 ? 72  ASN A OD1 1 
ATOM   2928 N ND2 . ASN B 1 72  ? 25.837  5.678   1.858  1.00 57.22 ? 72  ASN A ND2 1 
ATOM   2929 N N   . VAL B 1 73  ? 26.579  10.544  3.573  1.00 43.20 ? 73  VAL A N   1 
ATOM   2930 C CA  . VAL B 1 73  ? 26.576  11.717  2.705  1.00 40.57 ? 73  VAL A CA  1 
ATOM   2931 C C   . VAL B 1 73  ? 27.095  12.906  3.503  1.00 41.09 ? 73  VAL A C   1 
ATOM   2932 O O   . VAL B 1 73  ? 26.679  13.123  4.645  1.00 35.28 ? 73  VAL A O   1 
ATOM   2933 C CB  . VAL B 1 73  ? 25.171  12.012  2.143  1.00 42.50 ? 73  VAL A CB  1 
ATOM   2934 C CG1 . VAL B 1 73  ? 25.225  13.147  1.131  1.00 42.40 ? 73  VAL A CG1 1 
ATOM   2935 C CG2 . VAL B 1 73  ? 24.565  10.768  1.514  1.00 43.96 ? 73  VAL A CG2 1 
ATOM   2936 N N   . GLN B 1 74  ? 28.007  13.667  2.907  1.00 41.10 ? 74  GLN A N   1 
ATOM   2937 C CA  . GLN B 1 74  ? 28.453  14.925  3.488  1.00 37.37 ? 74  GLN A CA  1 
ATOM   2938 C C   . GLN B 1 74  ? 27.551  16.048  2.991  1.00 36.40 ? 74  GLN A C   1 
ATOM   2939 O O   . GLN B 1 74  ? 27.289  16.155  1.787  1.00 38.59 ? 74  GLN A O   1 
ATOM   2940 C CB  . GLN B 1 74  ? 29.912  15.196  3.119  1.00 41.30 ? 74  GLN A CB  1 
ATOM   2941 C CG  . GLN B 1 74  ? 30.373  16.628  3.357  1.00 42.71 ? 74  GLN A CG  1 
ATOM   2942 C CD  . GLN B 1 74  ? 31.886  16.764  3.327  1.00 49.67 ? 74  GLN A CD  1 
ATOM   2943 O OE1 . GLN B 1 74  ? 32.596  15.839  2.922  1.00 51.32 ? 74  GLN A OE1 1 
ATOM   2944 N NE2 . GLN B 1 74  ? 32.386  17.923  3.749  1.00 49.34 ? 74  GLN A NE2 1 
ATOM   2945 N N   . LEU B 1 75  ? 27.054  16.865  3.914  1.00 30.68 ? 75  LEU A N   1 
ATOM   2946 C CA  . LEU B 1 75  ? 26.260  18.032  3.565  1.00 30.56 ? 75  LEU A CA  1 
ATOM   2947 C C   . LEU B 1 75  ? 27.147  19.268  3.563  1.00 33.75 ? 75  LEU A C   1 
ATOM   2948 O O   . LEU B 1 75  ? 27.948  19.471  4.478  1.00 38.37 ? 75  LEU A O   1 
ATOM   2949 C CB  . LEU B 1 75  ? 25.093  18.236  4.536  1.00 31.31 ? 75  LEU A CB  1 
ATOM   2950 C CG  . LEU B 1 75  ? 24.285  16.984  4.869  1.00 33.36 ? 75  LEU A CG  1 
ATOM   2951 C CD1 . LEU B 1 75  ? 23.182  17.330  5.872  1.00 29.11 ? 75  LEU A CD1 1 
ATOM   2952 C CD2 . LEU B 1 75  ? 23.725  16.364  3.595  1.00 32.26 ? 75  LEU A CD2 1 
ATOM   2953 N N   . ARG B 1 76  ? 27.002  20.090  2.532  1.00 30.79 ? 76  ARG A N   1 
ATOM   2954 C CA  . ARG B 1 76  ? 27.822  21.286  2.404  1.00 34.53 ? 76  ARG A CA  1 
ATOM   2955 C C   . ARG B 1 76  ? 27.257  22.394  3.281  1.00 30.54 ? 76  ARG A C   1 
ATOM   2956 O O   . ARG B 1 76  ? 26.083  22.750  3.154  1.00 30.55 ? 76  ARG A O   1 
ATOM   2957 C CB  . ARG B 1 76  ? 27.875  21.735  0.948  1.00 34.82 ? 76  ARG A CB  1 
ATOM   2958 C CG  . ARG B 1 76  ? 28.688  23.001  0.732  1.00 36.71 ? 76  ARG A CG  1 
ATOM   2959 C CD  . ARG B 1 76  ? 28.601  23.467  -0.715 1.00 37.30 ? 76  ARG A CD  1 
ATOM   2960 N NE  . ARG B 1 76  ? 29.629  22.861  -1.547 1.00 42.74 ? 76  ARG A NE  1 
ATOM   2961 C CZ  . ARG B 1 76  ? 30.924  23.136  -1.460 1.00 41.18 ? 76  ARG A CZ  1 
ATOM   2962 N NH1 . ARG B 1 76  ? 31.390  24.023  -0.593 1.00 41.92 ? 76  ARG A NH1 1 
ATOM   2963 N NH2 . ARG B 1 76  ? 31.773  22.523  -2.278 1.00 41.94 ? 76  ARG A NH2 1 
ATOM   2964 N N   . VAL B 1 77  ? 28.088  22.940  4.166  1.00 31.46 ? 77  VAL A N   1 
ATOM   2965 C CA  . VAL B 1 77  ? 27.690  24.077  4.989  1.00 27.24 ? 77  VAL A CA  1 
ATOM   2966 C C   . VAL B 1 77  ? 27.953  25.354  4.202  1.00 29.64 ? 77  VAL A C   1 
ATOM   2967 O O   . VAL B 1 77  ? 29.077  25.584  3.742  1.00 29.92 ? 77  VAL A O   1 
ATOM   2968 C CB  . VAL B 1 77  ? 28.441  24.094  6.328  1.00 28.13 ? 77  VAL A CB  1 
ATOM   2969 C CG1 . VAL B 1 77  ? 27.972  25.264  7.172  1.00 24.78 ? 77  VAL A CG1 1 
ATOM   2970 C CG2 . VAL B 1 77  ? 28.234  22.770  7.075  1.00 29.05 ? 77  VAL A CG2 1 
ATOM   2971 N N   . ILE B 1 78  ? 26.914  26.177  4.044  1.00 28.01 ? 78  ILE A N   1 
ATOM   2972 C CA  . ILE B 1 78  ? 26.951  27.407  3.258  1.00 31.35 ? 78  ILE A CA  1 
ATOM   2973 C C   . ILE B 1 78  ? 26.658  28.638  4.102  1.00 30.35 ? 78  ILE A C   1 
ATOM   2974 O O   . ILE B 1 78  ? 26.563  29.748  3.572  1.00 32.05 ? 78  ILE A O   1 
ATOM   2975 C CB  . ILE B 1 78  ? 25.998  27.323  2.048  1.00 29.95 ? 78  ILE A CB  1 
ATOM   2976 C CG1 . ILE B 1 78  ? 24.554  27.077  2.504  1.00 33.25 ? 78  ILE A CG1 1 
ATOM   2977 C CG2 . ILE B 1 78  ? 26.468  26.258  1.072  1.00 32.16 ? 78  ILE A CG2 1 
ATOM   2978 C CD1 . ILE B 1 78  ? 23.524  27.225  1.392  1.00 33.02 ? 78  ILE A CD1 1 
ATOM   2979 N N   . GLY B 1 79  ? 26.539  28.472  5.412  1.00 28.37 ? 79  GLY A N   1 
ATOM   2980 C CA  . GLY B 1 79  ? 26.250  29.583  6.290  1.00 27.33 ? 79  GLY A CA  1 
ATOM   2981 C C   . GLY B 1 79  ? 26.164  29.092  7.712  1.00 29.79 ? 79  GLY A C   1 
ATOM   2982 O O   . GLY B 1 79  ? 25.826  27.926  7.942  1.00 26.58 ? 79  GLY A O   1 
ATOM   2983 N N   . HIS B 1 80  ? 26.478  29.951  8.677  1.00 29.60 ? 80  HIS A N   1 
ATOM   2984 C CA  . HIS B 1 80  ? 26.386  29.550  10.071 1.00 27.98 ? 80  HIS A CA  1 
ATOM   2985 C C   . HIS B 1 80  ? 26.096  30.764  10.936 1.00 32.20 ? 80  HIS A C   1 
ATOM   2986 O O   . HIS B 1 80  ? 26.467  31.895  10.604 1.00 25.71 ? 80  HIS A O   1 
ATOM   2987 C CB  . HIS B 1 80  ? 27.663  28.868  10.549 1.00 27.23 ? 80  HIS A CB  1 
ATOM   2988 C CG  . HIS B 1 80  ? 28.846  29.780  10.602 1.00 31.22 ? 80  HIS A CG  1 
ATOM   2989 N ND1 . HIS B 1 80  ? 29.661  30.004  9.515  1.00 33.66 ? 80  HIS A ND1 1 
ATOM   2990 C CD2 . HIS B 1 80  ? 29.346  30.531  11.611 1.00 32.52 ? 80  HIS A CD2 1 
ATOM   2991 C CE1 . HIS B 1 80  ? 30.623  30.845  9.855  1.00 31.82 ? 80  HIS A CE1 1 
ATOM   2992 N NE2 . HIS B 1 80  ? 30.452  31.182  11.120 1.00 31.50 ? 80  HIS A NE2 1 
ATOM   2993 N N   . SER B 1 81  ? 25.450  30.504  12.066 1.00 26.09 ? 81  SER A N   1 
ATOM   2994 C CA  . SER B 1 81  ? 25.024  31.550  12.977 1.00 23.75 ? 81  SER A CA  1 
ATOM   2995 C C   . SER B 1 81  ? 24.796  30.941  14.354 1.00 28.77 ? 81  SER A C   1 
ATOM   2996 O O   . SER B 1 81  ? 24.507  29.752  14.482 1.00 26.90 ? 81  SER A O   1 
ATOM   2997 C CB  . SER B 1 81  ? 23.785  32.256  12.415 1.00 26.52 ? 81  SER A CB  1 
ATOM   2998 O OG  . SER B 1 81  ? 22.593  31.726  12.937 1.00 27.41 ? 81  SER A OG  1 
ATOM   2999 N N   . MET B 1 82  ? 25.008  31.752  15.377 1.00 23.56 ? 82  MET A N   1 
ATOM   3000 C CA  . MET B 1 82  ? 24.749  31.379  16.764 1.00 26.07 ? 82  MET A CA  1 
ATOM   3001 C C   . MET B 1 82  ? 23.401  31.914  17.188 1.00 26.81 ? 82  MET A C   1 
ATOM   3002 O O   . MET B 1 82  ? 23.114  33.090  16.970 1.00 25.85 ? 82  MET A O   1 
ATOM   3003 C CB  . MET B 1 82  ? 25.767  31.988  17.724 1.00 29.16 ? 82  MET A CB  1 
ATOM   3004 C CG  . MET B 1 82  ? 25.772  31.311  19.069 1.00 27.48 ? 82  MET A CG  1 
ATOM   3005 S SD  . MET B 1 82  ? 27.355  31.285  19.880 1.00 28.08 ? 82  MET A SD  1 
ATOM   3006 C CE  . MET B 1 82  ? 27.785  33.019  19.766 1.00 30.53 ? 82  MET A CE  1 
ATOM   3007 N N   . GLN B 1 83  ? 22.606  31.084  17.850 1.00 24.23 ? 83  GLN A N   1 
ATOM   3008 C CA  . GLN B 1 83  ? 21.422  31.566  18.552 1.00 23.61 ? 83  GLN A CA  1 
ATOM   3009 C C   . GLN B 1 83  ? 21.491  31.064  19.986 1.00 21.29 ? 83  GLN A C   1 
ATOM   3010 O O   . GLN B 1 83  ? 21.275  29.875  20.231 1.00 20.94 ? 83  GLN A O   1 
ATOM   3011 C CB  . GLN B 1 83  ? 20.133  31.100  17.883 1.00 25.90 ? 83  GLN A CB  1 
ATOM   3012 C CG  . GLN B 1 83  ? 18.914  31.552  18.666 1.00 24.36 ? 83  GLN A CG  1 
ATOM   3013 C CD  . GLN B 1 83  ? 17.601  31.162  18.028 1.00 28.21 ? 83  GLN A CD  1 
ATOM   3014 O OE1 . GLN B 1 83  ? 17.554  30.312  17.145 1.00 29.88 ? 83  GLN A OE1 1 
ATOM   3015 N NE2 . GLN B 1 83  ? 16.518  31.772  18.494 1.00 30.67 ? 83  GLN A NE2 1 
ATOM   3016 N N   . ASN B 1 84  ? 21.762  31.967  20.927 1.00 22.68 ? 84  ASN A N   1 
ATOM   3017 C CA  . ASN B 1 84  ? 21.960  31.585  22.322 1.00 20.21 ? 84  ASN A CA  1 
ATOM   3018 C C   . ASN B 1 84  ? 22.990  30.453  22.401 1.00 22.95 ? 84  ASN A C   1 
ATOM   3019 O O   . ASN B 1 84  ? 24.138  30.653  21.972 1.00 20.03 ? 84  ASN A O   1 
ATOM   3020 C CB  . ASN B 1 84  ? 20.604  31.233  22.963 1.00 17.85 ? 84  ASN A CB  1 
ATOM   3021 C CG  . ASN B 1 84  ? 19.628  32.419  22.939 1.00 24.94 ? 84  ASN A CG  1 
ATOM   3022 O OD1 . ASN B 1 84  ? 19.937  33.497  23.445 1.00 24.85 ? 84  ASN A OD1 1 
ATOM   3023 N ND2 . ASN B 1 84  ? 18.452  32.216  22.358 1.00 21.37 ? 84  ASN A ND2 1 
ATOM   3024 N N   . CYS B 1 85  ? 22.627  29.261  22.901 1.00 19.41 ? 85  CYS A N   1 
ATOM   3025 C CA  . CYS B 1 85  ? 23.609  28.183  23.048 1.00 19.72 ? 85  CYS A CA  1 
ATOM   3026 C C   . CYS B 1 85  ? 23.566  27.138  21.933 1.00 19.64 ? 85  CYS A C   1 
ATOM   3027 O O   . CYS B 1 85  ? 24.205  26.087  22.061 1.00 19.44 ? 85  CYS A O   1 
ATOM   3028 C CB  . CYS B 1 85  ? 23.470  27.488  24.410 1.00 20.76 ? 85  CYS A CB  1 
ATOM   3029 S SG  . CYS B 1 85  ? 23.692  28.576  25.856 1.00 21.44 ? 85  CYS A SG  1 
ATOM   3030 N N   . VAL B 1 86  ? 22.876  27.399  20.829 1.00 20.99 ? 86  VAL A N   1 
ATOM   3031 C CA  . VAL B 1 86  ? 22.932  26.485  19.697 1.00 21.53 ? 86  VAL A CA  1 
ATOM   3032 C C   . VAL B 1 86  ? 23.519  27.203  18.489 1.00 23.60 ? 86  VAL A C   1 
ATOM   3033 O O   . VAL B 1 86  ? 23.433  28.429  18.355 1.00 21.49 ? 86  VAL A O   1 
ATOM   3034 C CB  . VAL B 1 86  ? 21.562  25.874  19.334 1.00 22.80 ? 86  VAL A CB  1 
ATOM   3035 C CG1 . VAL B 1 86  ? 21.078  24.950  20.456 1.00 24.34 ? 86  VAL A CG1 1 
ATOM   3036 C CG2 . VAL B 1 86  ? 20.549  26.959  19.059 1.00 25.20 ? 86  VAL A CG2 1 
ATOM   3037 N N   . LEU B 1 87  ? 24.135  26.422  17.620 1.00 20.27 ? 87  LEU A N   1 
ATOM   3038 C CA  . LEU B 1 87  ? 24.498  26.856  16.278 1.00 20.10 ? 87  LEU A CA  1 
ATOM   3039 C C   . LEU B 1 87  ? 23.468  26.397  15.272 1.00 25.09 ? 87  LEU A C   1 
ATOM   3040 O O   . LEU B 1 87  ? 22.841  25.339  15.417 1.00 24.28 ? 87  LEU A O   1 
ATOM   3041 C CB  . LEU B 1 87  ? 25.871  26.347  15.829 1.00 21.73 ? 87  LEU A CB  1 
ATOM   3042 C CG  . LEU B 1 87  ? 27.058  26.398  16.757 1.00 27.03 ? 87  LEU A CG  1 
ATOM   3043 C CD1 . LEU B 1 87  ? 28.243  25.740  16.062 1.00 24.96 ? 87  LEU A CD1 1 
ATOM   3044 C CD2 . LEU B 1 87  ? 27.340  27.848  17.041 1.00 30.02 ? 87  LEU A CD2 1 
ATOM   3045 N N   . LYS B 1 88  ? 23.290  27.227  14.255 1.00 20.08 ? 88  LYS A N   1 
ATOM   3046 C CA  . LYS B 1 88  ? 22.445  26.927  13.110 1.00 21.40 ? 88  LYS A CA  1 
ATOM   3047 C C   . LYS B 1 88  ? 23.371  26.902  11.899 1.00 27.76 ? 88  LYS A C   1 
ATOM   3048 O O   . LYS B 1 88  ? 23.983  27.920  11.555 1.00 25.28 ? 88  LYS A O   1 
ATOM   3049 C CB  . LYS B 1 88  ? 21.326  27.958  12.975 1.00 25.80 ? 88  LYS A CB  1 
ATOM   3050 C CG  . LYS B 1 88  ? 20.378  27.960  14.173 1.00 26.84 ? 88  LYS A CG  1 
ATOM   3051 C CD  . LYS B 1 88  ? 19.153  28.803  13.936 1.00 27.01 ? 88  LYS A CD  1 
ATOM   3052 C CE  . LYS B 1 88  ? 19.498  30.263  13.906 1.00 31.67 ? 88  LYS A CE  1 
ATOM   3053 N NZ  . LYS B 1 88  ? 18.325  31.074  14.289 1.00 33.14 ? 88  LYS A NZ  1 
ATOM   3054 N N   . LEU B 1 89  ? 23.527  25.732  11.303 1.00 23.26 ? 89  LEU A N   1 
ATOM   3055 C CA  . LEU B 1 89  ? 24.342  25.558  10.106 1.00 23.50 ? 89  LEU A CA  1 
ATOM   3056 C C   . LEU B 1 89  ? 23.407  25.473  8.908  1.00 25.38 ? 89  LEU A C   1 
ATOM   3057 O O   . LEU B 1 89  ? 22.637  24.515  8.775  1.00 23.96 ? 89  LEU A O   1 
ATOM   3058 C CB  . LEU B 1 89  ? 25.215  24.312  10.217 1.00 24.52 ? 89  LEU A CB  1 
ATOM   3059 C CG  . LEU B 1 89  ? 25.984  24.209  11.530 1.00 22.15 ? 89  LEU A CG  1 
ATOM   3060 C CD1 . LEU B 1 89  ? 26.702  22.889  11.610 1.00 21.76 ? 89  LEU A CD1 1 
ATOM   3061 C CD2 . LEU B 1 89  ? 26.979  25.389  11.683 1.00 24.72 ? 89  LEU A CD2 1 
ATOM   3062 N N   . LYS B 1 90  ? 23.444  26.492  8.055  1.00 24.98 ? 90  LYS A N   1 
ATOM   3063 C CA  . LYS B 1 90  ? 22.734  26.411  6.788  1.00 26.99 ? 90  LYS A CA  1 
ATOM   3064 C C   . LYS B 1 90  ? 23.481  25.470  5.854  1.00 25.93 ? 90  LYS A C   1 
ATOM   3065 O O   . LYS B 1 90  ? 24.705  25.565  5.699  1.00 27.61 ? 90  LYS A O   1 
ATOM   3066 C CB  . LYS B 1 90  ? 22.592  27.795  6.148  1.00 27.02 ? 90  LYS A CB  1 
ATOM   3067 C CG  . LYS B 1 90  ? 21.657  27.799  4.939  1.00 30.85 ? 90  LYS A CG  1 
ATOM   3068 C CD  . LYS B 1 90  ? 20.803  29.048  4.830  1.00 39.69 ? 90  LYS A CD  1 
ATOM   3069 C CE  . LYS B 1 90  ? 19.594  28.985  5.755  1.00 41.78 ? 90  LYS A CE  1 
ATOM   3070 N NZ  . LYS B 1 90  ? 19.304  30.329  6.332  1.00 42.00 ? 90  LYS A NZ  1 
ATOM   3071 N N   . VAL B 1 91  ? 22.745  24.542  5.245  1.00 28.02 ? 91  VAL A N   1 
ATOM   3072 C CA  . VAL B 1 91  ? 23.337  23.564  4.349  1.00 26.61 ? 91  VAL A CA  1 
ATOM   3073 C C   . VAL B 1 91  ? 22.664  23.713  2.990  1.00 25.81 ? 91  VAL A C   1 
ATOM   3074 O O   . VAL B 1 91  ? 21.581  24.292  2.870  1.00 26.58 ? 91  VAL A O   1 
ATOM   3075 C CB  . VAL B 1 91  ? 23.218  22.113  4.880  1.00 29.06 ? 91  VAL A CB  1 
ATOM   3076 C CG1 . VAL B 1 91  ? 24.158  21.896  6.074  1.00 25.23 ? 91  VAL A CG1 1 
ATOM   3077 C CG2 . VAL B 1 91  ? 21.778  21.782  5.256  1.00 27.02 ? 91  VAL A CG2 1 
ATOM   3078 N N   . ASP B 1 92  ? 23.334  23.207  1.947  1.00 28.00 ? 92  ASP A N   1 
ATOM   3079 C CA  . ASP B 1 92  ? 22.829  23.404  0.589  1.00 31.62 ? 92  ASP A CA  1 
ATOM   3080 C C   . ASP B 1 92  ? 21.719  22.427  0.216  1.00 33.86 ? 92  ASP A C   1 
ATOM   3081 O O   . ASP B 1 92  ? 21.142  22.548  -0.871 1.00 32.42 ? 92  ASP A O   1 
ATOM   3082 C CB  . ASP B 1 92  ? 23.972  23.320  -0.438 1.00 34.85 ? 92  ASP A CB  1 
ATOM   3083 C CG  . ASP B 1 92  ? 24.597  21.927  -0.538 1.00 38.55 ? 92  ASP A CG  1 
ATOM   3084 O OD1 . ASP B 1 92  ? 24.059  20.950  0.028  1.00 39.50 ? 92  ASP A OD1 1 
ATOM   3085 O OD2 . ASP B 1 92  ? 25.630  21.810  -1.229 1.00 42.86 ? 92  ASP A OD2 1 
ATOM   3086 N N   . THR B 1 93  ? 21.404  21.479  1.090  1.00 29.53 ? 93  THR A N   1 
ATOM   3087 C CA  . THR B 1 93  ? 20.408  20.456  0.832  1.00 30.59 ? 93  THR A CA  1 
ATOM   3088 C C   . THR B 1 93  ? 19.352  20.486  1.924  1.00 28.21 ? 93  THR A C   1 
ATOM   3089 O O   . THR B 1 93  ? 19.676  20.619  3.105  1.00 28.81 ? 93  THR A O   1 
ATOM   3090 C CB  . THR B 1 93  ? 21.061  19.080  0.779  1.00 32.78 ? 93  THR A CB  1 
ATOM   3091 O OG1 . THR B 1 93  ? 22.261  19.163  -0.007 1.00 40.59 ? 93  THR A OG1 1 
ATOM   3092 C CG2 . THR B 1 93  ? 20.111  18.066  0.175  1.00 35.48 ? 93  THR A CG2 1 
ATOM   3093 N N   . ALA B 1 94  ? 18.091  20.363  1.530  1.00 28.60 ? 94  ALA A N   1 
ATOM   3094 C CA  . ALA B 1 94  ? 17.007  20.263  2.490  1.00 28.55 ? 94  ALA A CA  1 
ATOM   3095 C C   . ALA B 1 94  ? 16.777  18.798  2.825  1.00 27.12 ? 94  ALA A C   1 
ATOM   3096 O O   . ALA B 1 94  ? 16.941  17.921  1.969  1.00 30.66 ? 94  ALA A O   1 
ATOM   3097 C CB  . ALA B 1 94  ? 15.726  20.884  1.937  1.00 26.92 ? 94  ALA A CB  1 
ATOM   3098 N N   . ASN B 1 95  ? 16.438  18.533  4.074  1.00 25.69 ? 95  ASN A N   1 
ATOM   3099 C CA  . ASN B 1 95  ? 16.244  17.153  4.507  1.00 27.73 ? 95  ASN A CA  1 
ATOM   3100 C C   . ASN B 1 95  ? 14.955  16.594  3.908  1.00 26.55 ? 95  ASN A C   1 
ATOM   3101 O O   . ASN B 1 95  ? 13.866  17.085  4.239  1.00 26.10 ? 95  ASN A O   1 
ATOM   3102 C CB  . ASN B 1 95  ? 16.224  17.087  6.040  1.00 24.68 ? 95  ASN A CB  1 
ATOM   3103 C CG  . ASN B 1 95  ? 16.165  15.658  6.568  1.00 28.32 ? 95  ASN A CG  1 
ATOM   3104 O OD1 . ASN B 1 95  ? 16.121  14.697  5.802  1.00 25.20 ? 95  ASN A OD1 1 
ATOM   3105 N ND2 . ASN B 1 95  ? 16.212  15.517  7.889  1.00 26.27 ? 95  ASN A ND2 1 
ATOM   3106 N N   . PRO B 1 96  ? 15.022  15.602  3.019  1.00 28.58 ? 96  PRO A N   1 
ATOM   3107 C CA  . PRO B 1 96  ? 13.778  15.047  2.454  1.00 29.42 ? 96  PRO A CA  1 
ATOM   3108 C C   . PRO B 1 96  ? 12.907  14.358  3.492  1.00 30.88 ? 96  PRO A C   1 
ATOM   3109 O O   . PRO B 1 96  ? 11.694  14.210  3.277  1.00 31.29 ? 96  PRO A O   1 
ATOM   3110 C CB  . PRO B 1 96  ? 14.277  14.061  1.388  1.00 33.11 ? 96  PRO A CB  1 
ATOM   3111 C CG  . PRO B 1 96  ? 15.692  13.758  1.734  1.00 31.35 ? 96  PRO A CG  1 
ATOM   3112 C CD  . PRO B 1 96  ? 16.221  14.832  2.645  1.00 29.28 ? 96  PRO A CD  1 
ATOM   3113 N N   . LYS B 1 97  ? 13.479  13.953  4.620  1.00 29.09 ? 97  LYS A N   1 
ATOM   3114 C CA  . LYS B 1 97  ? 12.730  13.301  5.684  1.00 28.34 ? 97  LYS A CA  1 
ATOM   3115 C C   . LYS B 1 97  ? 12.261  14.276  6.757  1.00 29.10 ? 97  LYS A C   1 
ATOM   3116 O O   . LYS B 1 97  ? 11.861  13.836  7.840  1.00 27.55 ? 97  LYS A O   1 
ATOM   3117 C CB  . LYS B 1 97  ? 13.580  12.197  6.315  1.00 29.97 ? 97  LYS A CB  1 
ATOM   3118 C CG  . LYS B 1 97  ? 14.188  11.226  5.304  1.00 35.07 ? 97  LYS A CG  1 
ATOM   3119 C CD  . LYS B 1 97  ? 14.629  9.943   5.991  1.00 33.88 ? 97  LYS A CD  1 
ATOM   3120 C CE  . LYS B 1 97  ? 14.239  8.704   5.197  1.00 43.38 ? 97  LYS A CE  1 
ATOM   3121 N NZ  . LYS B 1 97  ? 15.235  8.363   4.147  1.00 42.88 ? 97  LYS A NZ  1 
ATOM   3122 N N   . THR B 1 98  ? 12.307  15.587  6.492  1.00 27.22 ? 98  THR A N   1 
ATOM   3123 C CA  . THR B 1 98  ? 11.853  16.553  7.483  1.00 26.32 ? 98  THR A CA  1 
ATOM   3124 C C   . THR B 1 98  ? 10.384  16.312  7.793  1.00 30.93 ? 98  THR A C   1 
ATOM   3125 O O   . THR B 1 98  ? 9.544   16.404  6.886  1.00 29.50 ? 98  THR A O   1 
ATOM   3126 C CB  . THR B 1 98  ? 12.013  17.993  7.016  1.00 25.46 ? 98  THR A CB  1 
ATOM   3127 O OG1 . THR B 1 98  ? 13.363  18.216  6.593  1.00 27.08 ? 98  THR A OG1 1 
ATOM   3128 C CG2 . THR B 1 98  ? 11.682  18.944  8.167  1.00 27.75 ? 98  THR A CG2 1 
ATOM   3129 N N   . PRO B 1 99  ? 10.029  16.029  9.035  1.00 27.33 ? 99  PRO A N   1 
ATOM   3130 C CA  . PRO B 1 99  ? 8.620   15.892  9.394  1.00 30.07 ? 99  PRO A CA  1 
ATOM   3131 C C   . PRO B 1 99  ? 7.998   17.257  9.662  1.00 30.89 ? 99  PRO A C   1 
ATOM   3132 O O   . PRO B 1 99  ? 8.678   18.280  9.770  1.00 31.34 ? 99  PRO A O   1 
ATOM   3133 C CB  . PRO B 1 99  ? 8.685   15.043  10.665 1.00 30.79 ? 99  PRO A CB  1 
ATOM   3134 C CG  . PRO B 1 99  ? 9.957   15.523  11.331 1.00 28.44 ? 99  PRO A CG  1 
ATOM   3135 C CD  . PRO B 1 99  ? 10.917  15.863  10.201 1.00 28.16 ? 99  PRO A CD  1 
ATOM   3136 N N   . LYS B 1 100 ? 6.674   17.269  9.741  1.00 30.88 ? 100 LYS A N   1 
ATOM   3137 C CA  . LYS B 1 100 ? 6.017   18.456  10.259 1.00 31.73 ? 100 LYS A CA  1 
ATOM   3138 C C   . LYS B 1 100 ? 6.495   18.662  11.689 1.00 31.80 ? 100 LYS A C   1 
ATOM   3139 O O   . LYS B 1 100 ? 6.547   17.707  12.473 1.00 29.26 ? 100 LYS A O   1 
ATOM   3140 C CB  . LYS B 1 100 ? 4.500   18.299  10.212 1.00 34.12 ? 100 LYS A CB  1 
ATOM   3141 C CG  . LYS B 1 100 ? 3.749   19.386  10.953 1.00 41.06 ? 100 LYS A CG  1 
ATOM   3142 C CD  . LYS B 1 100 ? 2.248   19.225  10.764 1.00 45.23 ? 100 LYS A CD  1 
ATOM   3143 C CE  . LYS B 1 100 ? 1.840   19.598  9.347  1.00 42.92 ? 100 LYS A CE  1 
ATOM   3144 N NZ  . LYS B 1 100 ? 1.554   18.367  8.542  1.00 47.05 ? 100 LYS A NZ  1 
ATOM   3145 N N   . TYR B 1 101 ? 6.888   19.890  12.024 1.00 31.91 ? 101 TYR A N   1 
ATOM   3146 C CA  . TYR B 1 101 ? 7.523   20.096  13.318 1.00 31.69 ? 101 TYR A CA  1 
ATOM   3147 C C   . TYR B 1 101 ? 7.288   21.507  13.825 1.00 28.73 ? 101 TYR A C   1 
ATOM   3148 O O   . TYR B 1 101 ? 6.888   22.406  13.082 1.00 29.12 ? 101 TYR A O   1 
ATOM   3149 C CB  . TYR B 1 101 ? 9.030   19.827  13.253 1.00 27.33 ? 101 TYR A CB  1 
ATOM   3150 C CG  . TYR B 1 101 ? 9.813   20.886  12.496 1.00 26.96 ? 101 TYR A CG  1 
ATOM   3151 C CD1 . TYR B 1 101 ? 9.940   20.831  11.108 1.00 31.32 ? 101 TYR A CD1 1 
ATOM   3152 C CD2 . TYR B 1 101 ? 10.421  21.944  13.169 1.00 29.82 ? 101 TYR A CD2 1 
ATOM   3153 C CE1 . TYR B 1 101 ? 10.659  21.801  10.409 1.00 32.20 ? 101 TYR A CE1 1 
ATOM   3154 C CE2 . TYR B 1 101 ? 11.140  22.915  12.482 1.00 26.73 ? 101 TYR A CE2 1 
ATOM   3155 C CZ  . TYR B 1 101 ? 11.255  22.839  11.104 1.00 31.04 ? 101 TYR A CZ  1 
ATOM   3156 O OH  . TYR B 1 101 ? 11.969  23.800  10.418 1.00 32.55 ? 101 TYR A OH  1 
ATOM   3157 N N   . LYS B 1 102 ? 7.572   21.685  15.116 1.00 28.56 ? 102 LYS A N   1 
ATOM   3158 C CA  . LYS B 1 102 ? 7.659   22.995  15.745 1.00 27.59 ? 102 LYS A CA  1 
ATOM   3159 C C   . LYS B 1 102 ? 8.671   22.899  16.878 1.00 27.05 ? 102 LYS A C   1 
ATOM   3160 O O   . LYS B 1 102 ? 9.053   21.802  17.296 1.00 24.59 ? 102 LYS A O   1 
ATOM   3161 C CB  . LYS B 1 102 ? 6.303   23.461  16.284 1.00 29.61 ? 102 LYS A CB  1 
ATOM   3162 C CG  . LYS B 1 102 ? 5.777   22.595  17.403 1.00 34.36 ? 102 LYS A CG  1 
ATOM   3163 C CD  . LYS B 1 102 ? 4.497   23.150  18.004 1.00 36.98 ? 102 LYS A CD  1 
ATOM   3164 C CE  . LYS B 1 102 ? 3.325   22.943  17.073 1.00 42.08 ? 102 LYS A CE  1 
ATOM   3165 N NZ  . LYS B 1 102 ? 2.622   21.659  17.403 1.00 45.88 ? 102 LYS A NZ  1 
ATOM   3166 N N   . PHE B 1 103 ? 9.104   24.062  17.365 1.00 25.35 ? 103 PHE A N   1 
ATOM   3167 C CA  . PHE B 1 103 ? 9.958   24.175  18.542 1.00 22.41 ? 103 PHE A CA  1 
ATOM   3168 C C   . PHE B 1 103 ? 9.122   24.700  19.706 1.00 25.50 ? 103 PHE A C   1 
ATOM   3169 O O   . PHE B 1 103 ? 8.455   25.734  19.572 1.00 23.91 ? 103 PHE A O   1 
ATOM   3170 C CB  . PHE B 1 103 ? 11.133  25.131  18.291 1.00 22.88 ? 103 PHE A CB  1 
ATOM   3171 C CG  . PHE B 1 103 ? 12.123  24.660  17.255 1.00 23.59 ? 103 PHE A CG  1 
ATOM   3172 C CD1 . PHE B 1 103 ? 12.104  23.354  16.753 1.00 21.76 ? 103 PHE A CD1 1 
ATOM   3173 C CD2 . PHE B 1 103 ? 13.115  25.527  16.803 1.00 23.89 ? 103 PHE A CD2 1 
ATOM   3174 C CE1 . PHE B 1 103 ? 13.036  22.944  15.810 1.00 22.91 ? 103 PHE A CE1 1 
ATOM   3175 C CE2 . PHE B 1 103 ? 14.056  25.120  15.865 1.00 24.52 ? 103 PHE A CE2 1 
ATOM   3176 C CZ  . PHE B 1 103 ? 14.015  23.830  15.363 1.00 25.03 ? 103 PHE A CZ  1 
ATOM   3177 N N   . VAL B 1 104 ? 9.163   24.008  20.851 1.00 21.16 ? 104 VAL A N   1 
ATOM   3178 C CA  . VAL B 1 104 ? 8.419   24.450  22.025 1.00 23.83 ? 104 VAL A CA  1 
ATOM   3179 C C   . VAL B 1 104 ? 9.332   24.440  23.241 1.00 23.85 ? 104 VAL A C   1 
ATOM   3180 O O   . VAL B 1 104 ? 10.257  23.628  23.347 1.00 24.46 ? 104 VAL A O   1 
ATOM   3181 C CB  . VAL B 1 104 ? 7.161   23.591  22.321 1.00 25.13 ? 104 VAL A CB  1 
ATOM   3182 C CG1 . VAL B 1 104 ? 6.007   23.999  21.416 1.00 32.34 ? 104 VAL A CG1 1 
ATOM   3183 C CG2 . VAL B 1 104 ? 7.461   22.115  22.250 1.00 25.63 ? 104 VAL A CG2 1 
ATOM   3184 N N   . ARG B 1 105 ? 9.057   25.348  24.169 1.00 20.45 ? 105 ARG A N   1 
ATOM   3185 C CA  . ARG B 1 105 ? 9.702   25.351  25.471 1.00 19.69 ? 105 ARG A CA  1 
ATOM   3186 C C   . ARG B 1 105 ? 8.716   24.767  26.470 1.00 25.37 ? 105 ARG A C   1 
ATOM   3187 O O   . ARG B 1 105 ? 7.606   25.291  26.646 1.00 26.25 ? 105 ARG A O   1 
ATOM   3188 C CB  . ARG B 1 105 ? 10.159  26.759  25.864 1.00 24.89 ? 105 ARG A CB  1 
ATOM   3189 C CG  . ARG B 1 105 ? 10.962  26.800  27.150 1.00 21.68 ? 105 ARG A CG  1 
ATOM   3190 C CD  . ARG B 1 105 ? 11.517  28.184  27.441 1.00 25.09 ? 105 ARG A CD  1 
ATOM   3191 N NE  . ARG B 1 105 ? 12.281  28.176  28.681 1.00 24.02 ? 105 ARG A NE  1 
ATOM   3192 C CZ  . ARG B 1 105 ? 13.550  27.804  28.792 1.00 22.97 ? 105 ARG A CZ  1 
ATOM   3193 N NH1 . ARG B 1 105 ? 14.240  27.361  27.750 1.00 19.98 ? 105 ARG A NH1 1 
ATOM   3194 N NH2 . ARG B 1 105 ? 14.140  27.870  29.981 1.00 20.20 ? 105 ARG A NH2 1 
ATOM   3195 N N   . ILE B 1 106 ? 9.087   23.655  27.075 1.00 23.25 ? 106 ILE A N   1 
ATOM   3196 C CA  . ILE B 1 106 ? 8.171   22.977  27.972 1.00 23.92 ? 106 ILE A CA  1 
ATOM   3197 C C   . ILE B 1 106 ? 8.346   23.502  29.386 1.00 24.31 ? 106 ILE A C   1 
ATOM   3198 O O   . ILE B 1 106 ? 9.325   24.176  29.719 1.00 22.73 ? 106 ILE A O   1 
ATOM   3199 C CB  . ILE B 1 106 ? 8.359   21.459  27.915 1.00 23.86 ? 106 ILE A CB  1 
ATOM   3200 C CG1 . ILE B 1 106 ? 9.806   21.093  28.260 1.00 21.13 ? 106 ILE A CG1 1 
ATOM   3201 C CG2 . ILE B 1 106 ? 7.947   20.942  26.535 1.00 25.45 ? 106 ILE A CG2 1 
ATOM   3202 C CD1 . ILE B 1 106 ? 9.926   19.652  28.710 1.00 26.82 ? 106 ILE A CD1 1 
ATOM   3203 N N   . GLN B 1 107 ? 7.365   23.217  30.209 1.00 24.54 ? 107 GLN A N   1 
ATOM   3204 C CA  . GLN B 1 107 ? 7.210   23.611  31.591 1.00 26.65 ? 107 GLN A CA  1 
ATOM   3205 C C   . GLN B 1 107 ? 7.617   22.459  32.502 1.00 23.44 ? 107 GLN A C   1 
ATOM   3206 O O   . GLN B 1 107 ? 7.448   21.293  32.137 1.00 21.97 ? 107 GLN A O   1 
ATOM   3207 C CB  . GLN B 1 107 ? 5.742   23.971  31.862 1.00 26.26 ? 107 GLN A CB  1 
ATOM   3208 C CG  . GLN B 1 107 ? 5.288   25.271  31.188 1.00 33.22 ? 107 GLN A CG  1 
ATOM   3209 C CD  . GLN B 1 107 ? 6.112   26.471  31.574 1.00 38.46 ? 107 GLN A CD  1 
ATOM   3210 O OE1 . GLN B 1 107 ? 6.219   26.813  32.755 1.00 42.25 ? 107 GLN A OE1 1 
ATOM   3211 N NE2 . GLN B 1 107 ? 6.732   27.107  30.580 1.00 40.08 ? 107 GLN A NE2 1 
ATOM   3212 N N   . PRO B 1 108 ? 8.139   22.744  33.694 1.00 26.40 ? 108 PRO A N   1 
ATOM   3213 C CA  . PRO B 1 108 ? 8.434   21.667  34.646 1.00 25.60 ? 108 PRO A CA  1 
ATOM   3214 C C   . PRO B 1 108 ? 7.216   20.797  34.914 1.00 24.62 ? 108 PRO A C   1 
ATOM   3215 O O   . PRO B 1 108 ? 6.087   21.285  35.028 1.00 24.36 ? 108 PRO A O   1 
ATOM   3216 C CB  . PRO B 1 108 ? 8.878   22.408  35.912 1.00 26.06 ? 108 PRO A CB  1 
ATOM   3217 C CG  . PRO B 1 108 ? 9.007   23.857  35.534 1.00 28.08 ? 108 PRO A CG  1 
ATOM   3218 C CD  . PRO B 1 108 ? 8.781   24.014  34.068 1.00 29.20 ? 108 PRO A CD  1 
ATOM   3219 N N   . GLY B 1 109 ? 7.464   19.491  35.025 1.00 20.61 ? 109 GLY A N   1 
ATOM   3220 C CA  . GLY B 1 109 ? 6.428   18.489  35.150 1.00 20.06 ? 109 GLY A CA  1 
ATOM   3221 C C   . GLY B 1 109 ? 6.024   17.858  33.839 1.00 22.17 ? 109 GLY A C   1 
ATOM   3222 O O   . GLY B 1 109 ? 5.519   16.727  33.833 1.00 22.38 ? 109 GLY A O   1 
ATOM   3223 N N   . GLN B 1 110 ? 6.288   18.526  32.722 1.00 18.09 ? 110 GLN A N   1 
ATOM   3224 C CA  . GLN B 1 110 ? 5.943   17.979  31.424 1.00 18.80 ? 110 GLN A CA  1 
ATOM   3225 C C   . GLN B 1 110 ? 6.969   16.930  31.033 1.00 20.51 ? 110 GLN A C   1 
ATOM   3226 O O   . GLN B 1 110 ? 8.150   17.027  31.370 1.00 18.91 ? 110 GLN A O   1 
ATOM   3227 C CB  . GLN B 1 110 ? 5.895   19.079  30.371 1.00 25.14 ? 110 GLN A CB  1 
ATOM   3228 C CG  . GLN B 1 110 ? 4.709   20.036  30.477 1.00 26.02 ? 110 GLN A CG  1 
ATOM   3229 C CD  . GLN B 1 110 ? 4.632   20.951  29.273 1.00 30.13 ? 110 GLN A CD  1 
ATOM   3230 O OE1 . GLN B 1 110 ? 5.072   22.105  29.324 1.00 30.39 ? 110 GLN A OE1 1 
ATOM   3231 N NE2 . GLN B 1 110 ? 4.065   20.446  28.177 1.00 34.70 ? 110 GLN A NE2 1 
ATOM   3232 N N   . THR B 1 111 ? 6.509   15.910  30.324 1.00 16.90 ? 111 THR A N   1 
ATOM   3233 C CA  . THR B 1 111 ? 7.371   14.820  29.904 1.00 19.33 ? 111 THR A CA  1 
ATOM   3234 C C   . THR B 1 111 ? 7.652   14.904  28.410 1.00 19.17 ? 111 THR A C   1 
ATOM   3235 O O   . THR B 1 111 ? 6.949   15.589  27.665 1.00 21.90 ? 111 THR A O   1 
ATOM   3236 C CB  . THR B 1 111 ? 6.727   13.477  30.226 1.00 20.58 ? 111 THR A CB  1 
ATOM   3237 O OG1 . THR B 1 111 ? 5.454   13.428  29.583 1.00 22.88 ? 111 THR A OG1 1 
ATOM   3238 C CG2 . THR B 1 111 ? 6.551   13.311  31.737 1.00 19.56 ? 111 THR A CG2 1 
ATOM   3239 N N   . PHE B 1 112 ? 8.687   14.179  27.983 1.00 20.67 ? 112 PHE A N   1 
ATOM   3240 C CA  . PHE B 1 112 ? 9.067   14.103  26.578 1.00 17.91 ? 112 PHE A CA  1 
ATOM   3241 C C   . PHE B 1 112 ? 9.929   12.865  26.378 1.00 19.47 ? 112 PHE A C   1 
ATOM   3242 O O   . PHE B 1 112 ? 10.434  12.283  27.339 1.00 19.02 ? 112 PHE A O   1 
ATOM   3243 C CB  . PHE B 1 112 ? 9.811   15.371  26.116 1.00 19.21 ? 112 PHE A CB  1 
ATOM   3244 C CG  . PHE B 1 112 ? 11.053  15.693  26.916 1.00 17.13 ? 112 PHE A CG  1 
ATOM   3245 C CD1 . PHE B 1 112 ? 10.968  16.474  28.065 1.00 22.82 ? 112 PHE A CD1 1 
ATOM   3246 C CD2 . PHE B 1 112 ? 12.306  15.248  26.506 1.00 14.63 ? 112 PHE A CD2 1 
ATOM   3247 C CE1 . PHE B 1 112 ? 12.105  16.797  28.801 1.00 19.54 ? 112 PHE A CE1 1 
ATOM   3248 C CE2 . PHE B 1 112 ? 13.444  15.568  27.221 1.00 16.51 ? 112 PHE A CE2 1 
ATOM   3249 C CZ  . PHE B 1 112 ? 13.355  16.347  28.368 1.00 18.05 ? 112 PHE A CZ  1 
ATOM   3250 N N   . SER B 1 113 ? 10.059  12.445  25.121 1.00 16.51 ? 113 SER A N   1 
ATOM   3251 C CA  . SER B 1 113 ? 10.913  11.325  24.753 1.00 19.54 ? 113 SER A CA  1 
ATOM   3252 C C   . SER B 1 113 ? 12.266  11.834  24.285 1.00 17.02 ? 113 SER A C   1 
ATOM   3253 O O   . SER B 1 113 ? 12.344  12.823  23.554 1.00 18.65 ? 113 SER A O   1 
ATOM   3254 C CB  . SER B 1 113 ? 10.284  10.483  23.643 1.00 17.99 ? 113 SER A CB  1 
ATOM   3255 O OG  . SER B 1 113 ? 8.963   10.076  23.989 1.00 20.23 ? 113 SER A OG  1 
ATOM   3256 N N   . VAL B 1 114 ? 13.323  11.148  24.702 1.00 16.49 ? 114 VAL A N   1 
ATOM   3257 C CA  . VAL B 1 114 ? 14.687  11.433  24.264 1.00 15.33 ? 114 VAL A CA  1 
ATOM   3258 C C   . VAL B 1 114 ? 15.124  10.330  23.314 1.00 19.43 ? 114 VAL A C   1 
ATOM   3259 O O   . VAL B 1 114 ? 14.991  9.137   23.625 1.00 18.88 ? 114 VAL A O   1 
ATOM   3260 C CB  . VAL B 1 114 ? 15.656  11.539  25.455 1.00 18.91 ? 114 VAL A CB  1 
ATOM   3261 C CG1 . VAL B 1 114 ? 17.095  11.660  24.956 1.00 16.80 ? 114 VAL A CG1 1 
ATOM   3262 C CG2 . VAL B 1 114 ? 15.296  12.739  26.335 1.00 19.39 ? 114 VAL A CG2 1 
ATOM   3263 N N   . LEU B 1 115 ? 15.639  10.721  22.153 1.00 19.48 ? 115 LEU A N   1 
ATOM   3264 C CA  . LEU B 1 115 ? 16.309  9.786   21.251 1.00 18.46 ? 115 LEU A CA  1 
ATOM   3265 C C   . LEU B 1 115 ? 17.807  9.949   21.476 1.00 21.73 ? 115 LEU A C   1 
ATOM   3266 O O   . LEU B 1 115 ? 18.425  10.870  20.943 1.00 19.30 ? 115 LEU A O   1 
ATOM   3267 C CB  . LEU B 1 115 ? 15.931  10.049  19.798 1.00 17.81 ? 115 LEU A CB  1 
ATOM   3268 C CG  . LEU B 1 115 ? 16.614  9.125   18.790 1.00 19.44 ? 115 LEU A CG  1 
ATOM   3269 C CD1 . LEU B 1 115 ? 16.112  7.686   18.983 1.00 22.14 ? 115 LEU A CD1 1 
ATOM   3270 C CD2 . LEU B 1 115 ? 16.309  9.581   17.380 1.00 20.66 ? 115 LEU A CD2 1 
ATOM   3271 N N   . ALA B 1 116 ? 18.382  9.063   22.287 1.00 20.37 ? 116 ALA A N   1 
ATOM   3272 C CA  . ALA B 1 116 ? 19.817  9.095   22.541 1.00 19.43 ? 116 ALA A CA  1 
ATOM   3273 C C   . ALA B 1 116 ? 20.578  8.691   21.284 1.00 20.83 ? 116 ALA A C   1 
ATOM   3274 O O   . ALA B 1 116 ? 20.326  7.630   20.708 1.00 22.14 ? 116 ALA A O   1 
ATOM   3275 C CB  . ALA B 1 116 ? 20.170  8.166   23.700 1.00 20.13 ? 116 ALA A CB  1 
ATOM   3276 N N   . CYS B 1 117 ? 21.514  9.539   20.864 1.00 18.53 ? 117 CYS A N   1 
ATOM   3277 C CA  . CYS B 1 117 ? 22.247  9.359   19.617 1.00 21.86 ? 117 CYS A CA  1 
ATOM   3278 C C   . CYS B 1 117 ? 23.738  9.517   19.853 1.00 21.58 ? 117 CYS A C   1 
ATOM   3279 O O   . CYS B 1 117 ? 24.159  10.317  20.692 1.00 20.11 ? 117 CYS A O   1 
ATOM   3280 C CB  . CYS B 1 117 ? 21.824  10.394  18.587 1.00 23.71 ? 117 CYS A CB  1 
ATOM   3281 S SG  . CYS B 1 117 ? 20.191  10.098  17.971 1.00 27.66 ? 117 CYS A SG  1 
ATOM   3282 N N   . TYR B 1 118 ? 24.529  8.765   19.076 1.00 19.72 ? 118 TYR A N   1 
ATOM   3283 C CA  . TYR B 1 118 ? 25.982  8.843   19.089 1.00 23.42 ? 118 TYR A CA  1 
ATOM   3284 C C   . TYR B 1 118 ? 26.484  8.850   17.652 1.00 25.15 ? 118 TYR A C   1 
ATOM   3285 O O   . TYR B 1 118 ? 26.102  7.987   16.853 1.00 21.47 ? 118 TYR A O   1 
ATOM   3286 C CB  . TYR B 1 118 ? 26.585  7.672   19.888 1.00 24.91 ? 118 TYR A CB  1 
ATOM   3287 C CG  . TYR B 1 118 ? 26.161  7.753   21.335 1.00 23.32 ? 118 TYR A CG  1 
ATOM   3288 C CD1 . TYR B 1 118 ? 26.870  8.526   22.246 1.00 25.06 ? 118 TYR A CD1 1 
ATOM   3289 C CD2 . TYR B 1 118 ? 24.998  7.131   21.772 1.00 27.60 ? 118 TYR A CD2 1 
ATOM   3290 C CE1 . TYR B 1 118 ? 26.456  8.642   23.571 1.00 25.64 ? 118 TYR A CE1 1 
ATOM   3291 C CE2 . TYR B 1 118 ? 24.565  7.256   23.093 1.00 22.38 ? 118 TYR A CE2 1 
ATOM   3292 C CZ  . TYR B 1 118 ? 25.301  8.004   23.984 1.00 22.22 ? 118 TYR A CZ  1 
ATOM   3293 O OH  . TYR B 1 118 ? 24.878  8.134   25.291 1.00 21.50 ? 118 TYR A OH  1 
ATOM   3294 N N   . ASN B 1 119 ? 27.322  9.838   17.327 1.00 25.64 ? 119 ASN A N   1 
ATOM   3295 C CA  . ASN B 1 119 ? 27.890  9.986   15.984 1.00 27.35 ? 119 ASN A CA  1 
ATOM   3296 C C   . ASN B 1 119 ? 26.803  10.019  14.914 1.00 25.49 ? 119 ASN A C   1 
ATOM   3297 O O   . ASN B 1 119 ? 26.919  9.400   13.854 1.00 24.98 ? 119 ASN A O   1 
ATOM   3298 C CB  . ASN B 1 119 ? 28.911  8.884   15.704 1.00 29.61 ? 119 ASN A CB  1 
ATOM   3299 C CG  . ASN B 1 119 ? 30.050  8.898   16.703 1.00 30.84 ? 119 ASN A CG  1 
ATOM   3300 O OD1 . ASN B 1 119 ? 30.869  9.818   16.709 1.00 40.49 ? 119 ASN A OD1 1 
ATOM   3301 N ND2 . ASN B 1 119 ? 30.098  7.894   17.563 1.00 36.29 ? 119 ASN A ND2 1 
ATOM   3302 N N   . GLY B 1 120 ? 25.730  10.754  15.202 1.00 21.97 ? 120 GLY A N   1 
ATOM   3303 C CA  . GLY B 1 120 ? 24.637  10.902  14.265 1.00 23.88 ? 120 GLY A CA  1 
ATOM   3304 C C   . GLY B 1 120 ? 23.759  9.685   14.093 1.00 23.47 ? 120 GLY A C   1 
ATOM   3305 O O   . GLY B 1 120 ? 22.921  9.675   13.185 1.00 27.58 ? 120 GLY A O   1 
ATOM   3306 N N   . SER B 1 121 ? 23.911  8.665   14.937 1.00 24.14 ? 121 SER A N   1 
ATOM   3307 C CA  . SER B 1 121 ? 23.200  7.397   14.772 1.00 25.93 ? 121 SER A CA  1 
ATOM   3308 C C   . SER B 1 121 ? 22.336  7.123   15.995 1.00 26.86 ? 121 SER A C   1 
ATOM   3309 O O   . SER B 1 121 ? 22.863  7.099   17.119 1.00 25.36 ? 121 SER A O   1 
ATOM   3310 C CB  . SER B 1 121 ? 24.190  6.249   14.554 1.00 32.75 ? 121 SER A CB  1 
ATOM   3311 O OG  . SER B 1 121 ? 24.727  6.302   13.246 1.00 32.23 ? 121 SER A OG  1 
ATOM   3312 N N   . PRO B 1 122 ? 21.025  6.926   15.834 1.00 29.79 ? 122 PRO A N   1 
ATOM   3313 C CA  . PRO B 1 122 ? 20.157  6.689   17.001 1.00 29.75 ? 122 PRO A CA  1 
ATOM   3314 C C   . PRO B 1 122 ? 20.478  5.390   17.719 1.00 31.82 ? 122 PRO A C   1 
ATOM   3315 O O   . PRO B 1 122 ? 20.687  4.344   17.097 1.00 33.39 ? 122 PRO A O   1 
ATOM   3316 C CB  . PRO B 1 122 ? 18.748  6.668   16.394 1.00 27.84 ? 122 PRO A CB  1 
ATOM   3317 C CG  . PRO B 1 122 ? 18.868  7.571   15.180 1.00 31.08 ? 122 PRO A CG  1 
ATOM   3318 C CD  . PRO B 1 122 ? 20.238  7.205   14.619 1.00 26.55 ? 122 PRO A CD  1 
ATOM   3319 N N   . SER B 1 123 ? 20.495  5.468   19.050 1.00 30.11 ? 123 SER A N   1 
ATOM   3320 C CA  . SER B 1 123 ? 20.905  4.380   19.932 1.00 28.91 ? 123 SER A CA  1 
ATOM   3321 C C   . SER B 1 123 ? 19.783  3.838   20.809 1.00 27.31 ? 123 SER A C   1 
ATOM   3322 O O   . SER B 1 123 ? 19.672  2.621   20.991 1.00 24.42 ? 123 SER A O   1 
ATOM   3323 C CB  . SER B 1 123 ? 22.063  4.853   20.821 1.00 31.45 ? 123 SER A CB  1 
ATOM   3324 O OG  . SER B 1 123 ? 22.189  4.059   21.985 1.00 40.92 ? 123 SER A OG  1 
ATOM   3325 N N   . GLY B 1 124 ? 18.943  4.697   21.370 1.00 22.02 ? 124 GLY A N   1 
ATOM   3326 C CA  . GLY B 1 124 ? 17.827  4.214   22.166 1.00 20.19 ? 124 GLY A CA  1 
ATOM   3327 C C   . GLY B 1 124 ? 16.871  5.350   22.427 1.00 21.97 ? 124 GLY A C   1 
ATOM   3328 O O   . GLY B 1 124 ? 17.183  6.518   22.183 1.00 20.31 ? 124 GLY A O   1 
ATOM   3329 N N   . VAL B 1 125 ? 15.694  4.999   22.945 1.00 16.71 ? 125 VAL A N   1 
ATOM   3330 C CA  . VAL B 1 125 ? 14.646  5.970   23.224 1.00 20.05 ? 125 VAL A CA  1 
ATOM   3331 C C   . VAL B 1 125 ? 14.084  5.722   24.619 1.00 21.88 ? 125 VAL A C   1 
ATOM   3332 O O   . VAL B 1 125 ? 13.911  4.572   25.044 1.00 22.24 ? 125 VAL A O   1 
ATOM   3333 C CB  . VAL B 1 125 ? 13.543  5.922   22.141 1.00 21.29 ? 125 VAL A CB  1 
ATOM   3334 C CG1 . VAL B 1 125 ? 12.775  4.639   22.226 1.00 26.97 ? 125 VAL A CG1 1 
ATOM   3335 C CG2 . VAL B 1 125 ? 12.598  7.126   22.232 1.00 21.72 ? 125 VAL A CG2 1 
ATOM   3336 N N   . TYR B 1 126 ? 13.832  6.807   25.347 1.00 22.01 ? 126 TYR A N   1 
ATOM   3337 C CA  . TYR B 1 126 ? 13.287  6.710   26.692 1.00 20.35 ? 126 TYR A CA  1 
ATOM   3338 C C   . TYR B 1 126 ? 12.566  8.003   27.043 1.00 19.64 ? 126 TYR A C   1 
ATOM   3339 O O   . TYR B 1 126 ? 12.790  9.047   26.436 1.00 18.34 ? 126 TYR A O   1 
ATOM   3340 C CB  . TYR B 1 126 ? 14.376  6.398   27.730 1.00 18.53 ? 126 TYR A CB  1 
ATOM   3341 C CG  . TYR B 1 126 ? 15.568  7.344   27.717 1.00 20.27 ? 126 TYR A CG  1 
ATOM   3342 C CD1 . TYR B 1 126 ? 15.574  8.500   28.485 1.00 24.28 ? 126 TYR A CD1 1 
ATOM   3343 C CD2 . TYR B 1 126 ? 16.714  7.039   26.983 1.00 22.50 ? 126 TYR A CD2 1 
ATOM   3344 C CE1 . TYR B 1 126 ? 16.654  9.353   28.484 1.00 23.70 ? 126 TYR A CE1 1 
ATOM   3345 C CE2 . TYR B 1 126 ? 17.824  7.896   26.980 1.00 23.82 ? 126 TYR A CE2 1 
ATOM   3346 C CZ  . TYR B 1 126 ? 17.777  9.046   27.731 1.00 21.89 ? 126 TYR A CZ  1 
ATOM   3347 O OH  . TYR B 1 126 ? 18.850  9.894   27.759 1.00 23.77 ? 126 TYR A OH  1 
ATOM   3348 N N   . GLN B 1 127 ? 11.698  7.915   28.046 1.00 18.99 ? 127 GLN A N   1 
ATOM   3349 C CA  . GLN B 1 127 ? 10.864  9.026   28.469 1.00 18.50 ? 127 GLN A CA  1 
ATOM   3350 C C   . GLN B 1 127 ? 11.493  9.771   29.643 1.00 20.04 ? 127 GLN A C   1 
ATOM   3351 O O   . GLN B 1 127 ? 12.034  9.153   30.568 1.00 18.18 ? 127 GLN A O   1 
ATOM   3352 C CB  . GLN B 1 127 ? 9.485   8.474   28.852 1.00 23.20 ? 127 GLN A CB  1 
ATOM   3353 C CG  . GLN B 1 127 ? 8.401   9.468   28.966 1.00 27.86 ? 127 GLN A CG  1 
ATOM   3354 C CD  . GLN B 1 127 ? 7.862   9.883   27.618 1.00 26.38 ? 127 GLN A CD  1 
ATOM   3355 O OE1 . GLN B 1 127 ? 8.437   9.566   26.559 1.00 26.81 ? 127 GLN A OE1 1 
ATOM   3356 N NE2 . GLN B 1 127 ? 6.729   10.552  27.642 1.00 26.92 ? 127 GLN A NE2 1 
ATOM   3357 N N   . CYS B 1 128 ? 11.407  11.107  29.605 1.00 19.87 ? 128 CYS A N   1 
ATOM   3358 C CA  . CYS B 1 128 ? 11.952  11.979  30.639 1.00 18.92 ? 128 CYS A CA  1 
ATOM   3359 C C   . CYS B 1 128 ? 10.898  13.006  31.030 1.00 21.09 ? 128 CYS A C   1 
ATOM   3360 O O   . CYS B 1 128 ? 10.020  13.339  30.237 1.00 24.03 ? 128 CYS A O   1 
ATOM   3361 C CB  . CYS B 1 128 ? 13.188  12.740  30.136 1.00 21.28 ? 128 CYS A CB  1 
ATOM   3362 S SG  . CYS B 1 128 ? 14.652  11.769  30.252 1.00 25.38 ? 128 CYS A SG  1 
ATOM   3363 N N   . ALA B 1 129 ? 11.006  13.530  32.251 1.00 18.70 ? 129 ALA A N   1 
ATOM   3364 C CA  . ALA B 1 129 ? 10.252  14.699  32.679 1.00 19.74 ? 129 ALA A CA  1 
ATOM   3365 C C   . ALA B 1 129 ? 11.225  15.839  32.959 1.00 19.65 ? 129 ALA A C   1 
ATOM   3366 O O   . ALA B 1 129 ? 12.314  15.606  33.493 1.00 19.82 ? 129 ALA A O   1 
ATOM   3367 C CB  . ALA B 1 129 ? 9.447   14.407  33.941 1.00 21.27 ? 129 ALA A CB  1 
ATOM   3368 N N   . MET B 1 130 ? 10.837  17.063  32.578 1.00 20.72 ? 130 MET A N   1 
ATOM   3369 C CA  . MET B 1 130 ? 11.490  18.278  33.064 1.00 18.70 ? 130 MET A CA  1 
ATOM   3370 C C   . MET B 1 130 ? 11.147  18.476  34.523 1.00 19.68 ? 130 MET A C   1 
ATOM   3371 O O   . MET B 1 130 ? 9.988   18.720  34.865 1.00 21.18 ? 130 MET A O   1 
ATOM   3372 C CB  . MET B 1 130 ? 11.045  19.481  32.244 1.00 21.59 ? 130 MET A CB  1 
ATOM   3373 C CG  . MET B 1 130 ? 11.832  20.790  32.443 1.00 20.63 ? 130 MET A CG  1 
ATOM   3374 S SD  . MET B 1 130 ? 13.610  20.674  32.487 1.00 19.55 ? 130 MET A SD  1 
ATOM   3375 C CE  . MET B 1 130 ? 13.907  20.450  30.753 1.00 22.07 ? 130 MET A CE  1 
ATOM   3376 N N   . ARG B 1 131 ? 12.142  18.355  35.380 1.00 17.50 ? 131 ARG A N   1 
ATOM   3377 C CA  . ARG B 1 131 ? 11.889  18.454  36.802 1.00 17.29 ? 131 ARG A CA  1 
ATOM   3378 C C   . ARG B 1 131 ? 11.849  19.920  37.217 1.00 21.72 ? 131 ARG A C   1 
ATOM   3379 O O   . ARG B 1 131 ? 12.219  20.816  36.454 1.00 18.16 ? 131 ARG A O   1 
ATOM   3380 C CB  . ARG B 1 131 ? 12.942  17.664  37.560 1.00 18.83 ? 131 ARG A CB  1 
ATOM   3381 C CG  . ARG B 1 131 ? 13.165  16.289  36.905 1.00 23.43 ? 131 ARG A CG  1 
ATOM   3382 C CD  . ARG B 1 131 ? 13.254  15.116  37.858 1.00 22.71 ? 131 ARG A CD  1 
ATOM   3383 N NE  . ARG B 1 131 ? 12.507  15.260  39.101 1.00 21.32 ? 131 ARG A NE  1 
ATOM   3384 C CZ  . ARG B 1 131 ? 11.458  14.511  39.422 1.00 20.07 ? 131 ARG A CZ  1 
ATOM   3385 N NH1 . ARG B 1 131 ? 10.934  13.647  38.559 1.00 18.02 ? 131 ARG A NH1 1 
ATOM   3386 N NH2 . ARG B 1 131 ? 10.928  14.624  40.639 1.00 19.65 ? 131 ARG A NH2 1 
ATOM   3387 N N   . HIS B 1 132 ? 11.347  20.168  38.429 1.00 18.40 ? 132 HIS A N   1 
ATOM   3388 C CA  . HIS B 1 132 ? 11.176  21.558  38.822 1.00 17.42 ? 132 HIS A CA  1 
ATOM   3389 C C   . HIS B 1 132 ? 12.495  22.261  39.117 1.00 18.34 ? 132 HIS A C   1 
ATOM   3390 O O   . HIS B 1 132 ? 12.507  23.493  39.169 1.00 18.56 ? 132 HIS A O   1 
ATOM   3391 C CB  . HIS B 1 132 ? 10.231  21.655  40.018 1.00 21.31 ? 132 HIS A CB  1 
ATOM   3392 C CG  . HIS B 1 132 ? 8.787   21.564  39.640 1.00 23.42 ? 132 HIS A CG  1 
ATOM   3393 N ND1 . HIS B 1 132 ? 8.025   22.679  39.359 1.00 24.11 ? 132 HIS A ND1 1 
ATOM   3394 C CD2 . HIS B 1 132 ? 7.963   20.499  39.490 1.00 22.14 ? 132 HIS A CD2 1 
ATOM   3395 C CE1 . HIS B 1 132 ? 6.791   22.307  39.065 1.00 23.46 ? 132 HIS A CE1 1 
ATOM   3396 N NE2 . HIS B 1 132 ? 6.724   20.992  39.145 1.00 23.89 ? 132 HIS A NE2 1 
ATOM   3397 N N   . ASN B 1 133 ? 13.594  21.526  39.285 1.00 17.61 ? 133 ASN A N   1 
ATOM   3398 C CA  . ASN B 1 133 ? 14.918  22.142  39.333 1.00 18.72 ? 133 ASN A CA  1 
ATOM   3399 C C   . ASN B 1 133 ? 15.568  22.208  37.956 1.00 19.69 ? 133 ASN A C   1 
ATOM   3400 O O   . ASN B 1 133 ? 16.781  22.454  37.854 1.00 18.14 ? 133 ASN A O   1 
ATOM   3401 C CB  . ASN B 1 133 ? 15.814  21.403  40.330 1.00 18.84 ? 133 ASN A CB  1 
ATOM   3402 C CG  . ASN B 1 133 ? 16.107  19.973  39.923 1.00 17.28 ? 133 ASN A CG  1 
ATOM   3403 O OD1 . ASN B 1 133 ? 15.704  19.511  38.848 1.00 17.90 ? 133 ASN A OD1 1 
ATOM   3404 N ND2 . ASN B 1 133 ? 16.812  19.261  40.788 1.00 19.06 ? 133 ASN A ND2 1 
ATOM   3405 N N   . PHE B 1 134 ? 14.782  21.954  36.911 1.00 19.70 ? 134 PHE A N   1 
ATOM   3406 C CA  . PHE B 1 134 ? 15.156  22.102  35.512 1.00 19.37 ? 134 PHE A CA  1 
ATOM   3407 C C   . PHE B 1 134 ? 16.241  21.125  35.085 1.00 20.77 ? 134 PHE A C   1 
ATOM   3408 O O   . PHE B 1 134 ? 16.978  21.404  34.134 1.00 18.91 ? 134 PHE A O   1 
ATOM   3409 C CB  . PHE B 1 134 ? 15.582  23.538  35.205 1.00 19.08 ? 134 PHE A CB  1 
ATOM   3410 C CG  . PHE B 1 134 ? 14.520  24.538  35.518 1.00 22.81 ? 134 PHE A CG  1 
ATOM   3411 C CD1 . PHE B 1 134 ? 13.411  24.664  34.695 1.00 25.77 ? 134 PHE A CD1 1 
ATOM   3412 C CD2 . PHE B 1 134 ? 14.603  25.324  36.662 1.00 24.69 ? 134 PHE A CD2 1 
ATOM   3413 C CE1 . PHE B 1 134 ? 12.408  25.576  34.995 1.00 26.33 ? 134 PHE A CE1 1 
ATOM   3414 C CE2 . PHE B 1 134 ? 13.598  26.234  36.968 1.00 22.80 ? 134 PHE A CE2 1 
ATOM   3415 C CZ  . PHE B 1 134 ? 12.511  26.360  36.132 1.00 27.99 ? 134 PHE A CZ  1 
ATOM   3416 N N   . THR B 1 135 ? 16.350  19.981  35.758 1.00 17.00 ? 135 THR A N   1 
ATOM   3417 C CA  . THR B 1 135 ? 17.180  18.880  35.287 1.00 18.36 ? 135 THR A CA  1 
ATOM   3418 C C   . THR B 1 135 ? 16.289  17.768  34.744 1.00 18.44 ? 135 THR A C   1 
ATOM   3419 O O   . THR B 1 135 ? 15.072  17.752  34.954 1.00 17.06 ? 135 THR A O   1 
ATOM   3420 C CB  . THR B 1 135 ? 18.071  18.315  36.404 1.00 21.37 ? 135 THR A CB  1 
ATOM   3421 O OG1 . THR B 1 135 ? 17.267  17.695  37.420 1.00 19.57 ? 135 THR A OG1 1 
ATOM   3422 C CG2 . THR B 1 135 ? 18.915  19.424  37.020 1.00 20.15 ? 135 THR A CG2 1 
ATOM   3423 N N   . ILE B 1 136 ? 16.909  16.825  34.052 1.00 16.18 ? 136 ILE A N   1 
ATOM   3424 C CA  . ILE B 1 136 ? 16.235  15.596  33.648 1.00 13.69 ? 136 ILE A CA  1 
ATOM   3425 C C   . ILE B 1 136 ? 17.080  14.413  34.088 1.00 21.53 ? 136 ILE A C   1 
ATOM   3426 O O   . ILE B 1 136 ? 18.300  14.515  34.263 1.00 19.25 ? 136 ILE A O   1 
ATOM   3427 C CB  . ILE B 1 136 ? 15.958  15.565  32.127 1.00 17.09 ? 136 ILE A CB  1 
ATOM   3428 C CG1 . ILE B 1 136 ? 17.269  15.529  31.313 1.00 15.95 ? 136 ILE A CG1 1 
ATOM   3429 C CG2 . ILE B 1 136 ? 15.114  16.786  31.716 1.00 18.94 ? 136 ILE A CG2 1 
ATOM   3430 C CD1 . ILE B 1 136 ? 17.080  15.163  29.836 1.00 15.05 ? 136 ILE A CD1 1 
ATOM   3431 N N   . LYS B 1 137 ? 16.415  13.284  34.285 1.00 20.62 ? 137 LYS A N   1 
ATOM   3432 C CA  . LYS B 1 137 ? 17.069  12.054  34.720 1.00 23.44 ? 137 LYS A CA  1 
ATOM   3433 C C   . LYS B 1 137 ? 17.240  11.191  33.481 1.00 22.32 ? 137 LYS A C   1 
ATOM   3434 O O   . LYS B 1 137 ? 16.386  10.366  33.144 1.00 21.05 ? 137 LYS A O   1 
ATOM   3435 C CB  . LYS B 1 137 ? 16.248  11.382  35.815 1.00 22.83 ? 137 LYS A CB  1 
ATOM   3436 C CG  . LYS B 1 137 ? 16.037  12.307  37.013 1.00 26.45 ? 137 LYS A CG  1 
ATOM   3437 C CD  . LYS B 1 137 ? 15.473  11.584  38.246 1.00 28.54 ? 137 LYS A CD  1 
ATOM   3438 C CE  . LYS B 1 137 ? 13.991  11.263  38.102 1.00 31.98 ? 137 LYS A CE  1 
ATOM   3439 N NZ  . LYS B 1 137 ? 13.318  11.126  39.438 1.00 31.13 ? 137 LYS A NZ  1 
ATOM   3440 N N   . GLY B 1 138 ? 18.365  11.389  32.799 1.00 19.01 ? 138 GLY A N   1 
ATOM   3441 C CA  . GLY B 1 138 ? 18.604  10.794  31.508 1.00 18.38 ? 138 GLY A CA  1 
ATOM   3442 C C   . GLY B 1 138 ? 19.619  9.670   31.546 1.00 18.23 ? 138 GLY A C   1 
ATOM   3443 O O   . GLY B 1 138 ? 19.994  9.149   32.596 1.00 18.11 ? 138 GLY A O   1 
ATOM   3444 N N   . SER B 1 139 ? 20.047  9.287   30.354 1.00 15.62 ? 139 SER A N   1 
ATOM   3445 C CA  . SER B 1 139 ? 21.094  8.285   30.175 1.00 16.30 ? 139 SER A CA  1 
ATOM   3446 C C   . SER B 1 139 ? 21.917  8.790   28.996 1.00 16.06 ? 139 SER A C   1 
ATOM   3447 O O   . SER B 1 139 ? 21.514  8.641   27.841 1.00 16.74 ? 139 SER A O   1 
ATOM   3448 C CB  . SER B 1 139 ? 20.503  6.897   29.931 1.00 19.14 ? 139 SER A CB  1 
ATOM   3449 O OG  . SER B 1 139 ? 21.532  5.964   29.701 1.00 20.59 ? 139 SER A OG  1 
ATOM   3450 N N   . PHE B 1 140 ? 23.038  9.437   29.304 1.00 19.60 ? 140 PHE A N   1 
ATOM   3451 C CA  . PHE B 1 140 ? 23.796  10.221  28.339 1.00 18.88 ? 140 PHE A CA  1 
ATOM   3452 C C   . PHE B 1 140 ? 25.276  9.949   28.568 1.00 20.71 ? 140 PHE A C   1 
ATOM   3453 O O   . PHE B 1 140 ? 25.769  10.103  29.693 1.00 20.73 ? 140 PHE A O   1 
ATOM   3454 C CB  . PHE B 1 140 ? 23.514  11.729  28.509 1.00 17.66 ? 140 PHE A CB  1 
ATOM   3455 C CG  . PHE B 1 140 ? 22.141  12.177  28.051 1.00 18.11 ? 140 PHE A CG  1 
ATOM   3456 C CD1 . PHE B 1 140 ? 21.763  12.083  26.718 1.00 20.76 ? 140 PHE A CD1 1 
ATOM   3457 C CD2 . PHE B 1 140 ? 21.246  12.706  28.951 1.00 17.23 ? 140 PHE A CD2 1 
ATOM   3458 C CE1 . PHE B 1 140 ? 20.503  12.526  26.307 1.00 21.67 ? 140 PHE A CE1 1 
ATOM   3459 C CE2 . PHE B 1 140 ? 19.995  13.145  28.544 1.00 18.05 ? 140 PHE A CE2 1 
ATOM   3460 C CZ  . PHE B 1 140 ? 19.631  13.051  27.214 1.00 18.43 ? 140 PHE A CZ  1 
ATOM   3461 N N   . LEU B 1 141 ? 25.979  9.562   27.510 1.00 20.10 ? 141 LEU A N   1 
ATOM   3462 C CA  . LEU B 1 141 ? 27.418  9.332   27.562 1.00 22.14 ? 141 LEU A CA  1 
ATOM   3463 C C   . LEU B 1 141 ? 28.143  10.333  26.676 1.00 23.58 ? 141 LEU A C   1 
ATOM   3464 O O   . LEU B 1 141 ? 27.530  11.111  25.959 1.00 23.26 ? 141 LEU A O   1 
ATOM   3465 C CB  . LEU B 1 141 ? 27.770  7.921   27.101 1.00 24.15 ? 141 LEU A CB  1 
ATOM   3466 C CG  . LEU B 1 141 ? 27.152  6.791   27.911 1.00 24.72 ? 141 LEU A CG  1 
ATOM   3467 C CD1 . LEU B 1 141 ? 27.383  5.478   27.180 1.00 27.01 ? 141 LEU A CD1 1 
ATOM   3468 C CD2 . LEU B 1 141 ? 27.763  6.804   29.300 1.00 24.80 ? 141 LEU A CD2 1 
ATOM   3469 N N   . ASN B 1 142 ? 29.472  10.263  26.705 1.00 24.52 ? 142 ASN A N   1 
ATOM   3470 C CA  . ASN B 1 142 ? 30.290  11.026  25.768 1.00 26.88 ? 142 ASN A CA  1 
ATOM   3471 C C   . ASN B 1 142 ? 29.799  10.799  24.340 1.00 23.10 ? 142 ASN A C   1 
ATOM   3472 O O   . ASN B 1 142 ? 29.646  9.657   23.896 1.00 26.71 ? 142 ASN A O   1 
ATOM   3473 C CB  . ASN B 1 142 ? 31.753  10.588  25.897 1.00 32.58 ? 142 ASN A CB  1 
ATOM   3474 C CG  . ASN B 1 142 ? 32.434  11.169  27.122 1.00 31.25 ? 142 ASN A CG  1 
ATOM   3475 O OD1 . ASN B 1 142 ? 31.931  12.094  27.748 1.00 33.58 ? 142 ASN A OD1 1 
ATOM   3476 N ND2 . ASN B 1 142 ? 33.600  10.625  27.465 1.00 38.77 ? 142 ASN A ND2 1 
ATOM   3477 N N   . GLY B 1 143 ? 29.525  11.891  23.629 1.00 27.10 ? 143 GLY A N   1 
ATOM   3478 C CA  . GLY B 1 143 ? 29.015  11.820  22.271 1.00 26.36 ? 143 GLY A CA  1 
ATOM   3479 C C   . GLY B 1 143 ? 27.524  12.063  22.130 1.00 23.33 ? 143 GLY A C   1 
ATOM   3480 O O   . GLY B 1 143 ? 27.041  12.225  20.999 1.00 23.50 ? 143 GLY A O   1 
ATOM   3481 N N   . SER B 1 144 ? 26.775  12.079  23.232 1.00 19.57 ? 144 SER A N   1 
ATOM   3482 C CA  . SER B 1 144 ? 25.329  12.221  23.157 1.00 17.81 ? 144 SER A CA  1 
ATOM   3483 C C   . SER B 1 144 ? 24.855  13.660  22.982 1.00 19.63 ? 144 SER A C   1 
ATOM   3484 O O   . SER B 1 144 ? 23.659  13.874  22.749 1.00 18.64 ? 144 SER A O   1 
ATOM   3485 C CB  . SER B 1 144 ? 24.692  11.643  24.417 1.00 17.60 ? 144 SER A CB  1 
ATOM   3486 O OG  . SER B 1 144 ? 25.223  12.275  25.562 1.00 17.79 ? 144 SER A OG  1 
ATOM   3487 N N   . CYS B 1 145 ? 25.725  14.649  23.160 1.00 17.94 ? 145 CYS A N   1 
ATOM   3488 C CA  . CYS B 1 145 ? 25.310  16.032  22.976 1.00 19.26 ? 145 CYS A CA  1 
ATOM   3489 C C   . CYS B 1 145 ? 24.695  16.234  21.600 1.00 17.43 ? 145 CYS A C   1 
ATOM   3490 O O   . CYS B 1 145 ? 25.125  15.638  20.613 1.00 17.53 ? 145 CYS A O   1 
ATOM   3491 C CB  . CYS B 1 145 ? 26.501  16.969  23.180 1.00 18.20 ? 145 CYS A CB  1 
ATOM   3492 S SG  . CYS B 1 145 ? 26.881  17.135  24.925 1.00 22.15 ? 145 CYS A SG  1 
ATOM   3493 N N   . GLY B 1 146 ? 23.629  17.031  21.550 1.00 18.70 ? 146 GLY A N   1 
ATOM   3494 C CA  . GLY B 1 146 ? 22.869  17.193  20.332 1.00 19.95 ? 146 GLY A CA  1 
ATOM   3495 C C   . GLY B 1 146 ? 21.678  16.266  20.182 1.00 18.04 ? 146 GLY A C   1 
ATOM   3496 O O   . GLY B 1 146 ? 20.799  16.552  19.360 1.00 18.88 ? 146 GLY A O   1 
ATOM   3497 N N   . SER B 1 147 ? 21.633  15.149  20.922 1.00 16.36 ? 147 SER A N   1 
ATOM   3498 C CA  . SER B 1 147 ? 20.403  14.368  21.003 1.00 15.05 ? 147 SER A CA  1 
ATOM   3499 C C   . SER B 1 147 ? 19.263  15.258  21.473 1.00 16.89 ? 147 SER A C   1 
ATOM   3500 O O   . SER B 1 147 ? 19.457  16.162  22.289 1.00 17.60 ? 147 SER A O   1 
ATOM   3501 C CB  . SER B 1 147 ? 20.537  13.177  21.970 1.00 16.78 ? 147 SER A CB  1 
ATOM   3502 O OG  . SER B 1 147 ? 21.659  12.350  21.687 1.00 18.13 ? 147 SER A OG  1 
ATOM   3503 N N   . VAL B 1 148 ? 18.051  14.982  20.984 1.00 14.83 ? 148 VAL A N   1 
ATOM   3504 C CA  . VAL B 1 148 ? 16.938  15.885  21.252 1.00 15.30 ? 148 VAL A CA  1 
ATOM   3505 C C   . VAL B 1 148 ? 15.814  15.161  21.988 1.00 18.55 ? 148 VAL A C   1 
ATOM   3506 O O   . VAL B 1 148 ? 15.656  13.938  21.910 1.00 17.56 ? 148 VAL A O   1 
ATOM   3507 C CB  . VAL B 1 148 ? 16.394  16.543  19.966 1.00 17.90 ? 148 VAL A CB  1 
ATOM   3508 C CG1 . VAL B 1 148 ? 17.497  17.372  19.296 1.00 20.14 ? 148 VAL A CG1 1 
ATOM   3509 C CG2 . VAL B 1 148 ? 15.780  15.526  19.023 1.00 21.16 ? 148 VAL A CG2 1 
ATOM   3510 N N   . GLY B 1 149 ? 15.011  15.960  22.695 1.00 15.73 ? 149 GLY A N   1 
ATOM   3511 C CA  . GLY B 1 149 ? 13.775  15.499  23.309 1.00 16.35 ? 149 GLY A CA  1 
ATOM   3512 C C   . GLY B 1 149 ? 12.568  16.075  22.587 1.00 17.39 ? 149 GLY A C   1 
ATOM   3513 O O   . GLY B 1 149 ? 12.628  17.176  22.033 1.00 18.86 ? 149 GLY A O   1 
ATOM   3514 N N   . PHE B 1 150 ? 11.456  15.332  22.597 1.00 17.53 ? 150 PHE A N   1 
ATOM   3515 C CA  . PHE B 1 150 ? 10.340  15.687  21.730 1.00 19.09 ? 150 PHE A CA  1 
ATOM   3516 C C   . PHE B 1 150 ? 9.054   15.005  22.178 1.00 21.82 ? 150 PHE A C   1 
ATOM   3517 O O   . PHE B 1 150 ? 9.062   13.972  22.855 1.00 19.77 ? 150 PHE A O   1 
ATOM   3518 C CB  . PHE B 1 150 ? 10.628  15.298  20.278 1.00 18.57 ? 150 PHE A CB  1 
ATOM   3519 C CG  . PHE B 1 150 ? 10.814  13.824  20.080 1.00 21.13 ? 150 PHE A CG  1 
ATOM   3520 C CD1 . PHE B 1 150 ? 12.035  13.228  20.342 1.00 23.81 ? 150 PHE A CD1 1 
ATOM   3521 C CD2 . PHE B 1 150 ? 9.761   13.031  19.636 1.00 25.88 ? 150 PHE A CD2 1 
ATOM   3522 C CE1 . PHE B 1 150 ? 12.208  11.859  20.174 1.00 23.00 ? 150 PHE A CE1 1 
ATOM   3523 C CE2 . PHE B 1 150 ? 9.936   11.665  19.463 1.00 24.57 ? 150 PHE A CE2 1 
ATOM   3524 C CZ  . PHE B 1 150 ? 11.156  11.087  19.731 1.00 23.55 ? 150 PHE A CZ  1 
ATOM   3525 N N   . ASN B 1 151 ? 7.946   15.596  21.753 1.00 21.94 ? 151 ASN A N   1 
ATOM   3526 C CA  . ASN B 1 151 ? 6.639   14.964  21.795 1.00 23.57 ? 151 ASN A CA  1 
ATOM   3527 C C   . ASN B 1 151 ? 6.111   14.882  20.367 1.00 28.49 ? 151 ASN A C   1 
ATOM   3528 O O   . ASN B 1 151 ? 6.552   15.615  19.475 1.00 23.22 ? 151 ASN A O   1 
ATOM   3529 C CB  . ASN B 1 151 ? 5.668   15.754  22.682 1.00 24.65 ? 151 ASN A CB  1 
ATOM   3530 C CG  . ASN B 1 151 ? 5.946   15.578  24.165 1.00 26.23 ? 151 ASN A CG  1 
ATOM   3531 O OD1 . ASN B 1 151 ? 5.404   14.679  24.811 1.00 27.66 ? 151 ASN A OD1 1 
ATOM   3532 N ND2 . ASN B 1 151 ? 6.766   16.456  24.721 1.00 24.02 ? 151 ASN A ND2 1 
ATOM   3533 N N   . ILE B 1 152 ? 5.177   13.967  20.139 1.00 28.35 ? 152 ILE A N   1 
ATOM   3534 C CA  . ILE B 1 152 ? 4.506   13.850  18.852 1.00 30.78 ? 152 ILE A CA  1 
ATOM   3535 C C   . ILE B 1 152 ? 3.018   14.050  19.077 1.00 42.41 ? 152 ILE A C   1 
ATOM   3536 O O   . ILE B 1 152 ? 2.423   13.398  19.942 1.00 44.39 ? 152 ILE A O   1 
ATOM   3537 C CB  . ILE B 1 152 ? 4.786   12.496  18.175 1.00 34.82 ? 152 ILE A CB  1 
ATOM   3538 C CG1 . ILE B 1 152 ? 6.282   12.342  17.921 1.00 32.32 ? 152 ILE A CG1 1 
ATOM   3539 C CG2 . ILE B 1 152 ? 4.008   12.388  16.868 1.00 42.89 ? 152 ILE A CG2 1 
ATOM   3540 C CD1 . ILE B 1 152 ? 6.680   10.972  17.528 1.00 33.45 ? 152 ILE A CD1 1 
ATOM   3541 N N   . ASP B 1 153 ? 2.426   14.964  18.321 1.00 44.42 ? 153 ASP A N   1 
ATOM   3542 C CA  . ASP B 1 153 ? 0.977   15.143  18.296 1.00 53.58 ? 153 ASP A CA  1 
ATOM   3543 C C   . ASP B 1 153 ? 0.521   14.858  16.868 1.00 55.76 ? 153 ASP A C   1 
ATOM   3544 O O   . ASP B 1 153 ? 0.721   15.684  15.969 1.00 53.27 ? 153 ASP A O   1 
ATOM   3545 C CB  . ASP B 1 153 ? 0.581   16.542  18.752 1.00 53.01 ? 153 ASP A CB  1 
ATOM   3546 C CG  . ASP B 1 153 ? -0.823  16.918  18.316 1.00 63.85 ? 153 ASP A CG  1 
ATOM   3547 O OD1 . ASP B 1 153 ? -1.763  16.143  18.605 1.00 66.18 ? 153 ASP A OD1 1 
ATOM   3548 O OD2 . ASP B 1 153 ? -0.988  17.985  17.686 1.00 64.76 ? 153 ASP A OD2 1 
ATOM   3549 N N   . TYR B 1 154 ? -0.063  13.674  16.668 1.00 58.18 ? 154 TYR A N   1 
ATOM   3550 C CA  . TYR B 1 154 ? -0.580  13.229  15.377 1.00 61.79 ? 154 TYR A CA  1 
ATOM   3551 C C   . TYR B 1 154 ? 0.578   12.996  14.412 1.00 60.28 ? 154 TYR A C   1 
ATOM   3552 O O   . TYR B 1 154 ? 1.232   11.949  14.465 1.00 63.55 ? 154 TYR A O   1 
ATOM   3553 C CB  . TYR B 1 154 ? -1.580  14.244  14.811 1.00 62.74 ? 154 TYR A CB  1 
ATOM   3554 C CG  . TYR B 1 154 ? -2.927  14.234  15.510 1.00 68.61 ? 154 TYR A CG  1 
ATOM   3555 C CD1 . TYR B 1 154 ? -3.054  13.760  16.816 1.00 68.22 ? 154 TYR A CD1 1 
ATOM   3556 C CD2 . TYR B 1 154 ? -4.066  14.725  14.879 1.00 71.92 ? 154 TYR A CD2 1 
ATOM   3557 C CE1 . TYR B 1 154 ? -4.273  13.758  17.465 1.00 69.47 ? 154 TYR A CE1 1 
ATOM   3558 C CE2 . TYR B 1 154 ? -5.296  14.730  15.524 1.00 68.53 ? 154 TYR A CE2 1 
ATOM   3559 C CZ  . TYR B 1 154 ? -5.391  14.244  16.817 1.00 70.80 ? 154 TYR A CZ  1 
ATOM   3560 O OH  . TYR B 1 154 ? -6.608  14.243  17.466 1.00 69.25 ? 154 TYR A OH  1 
ATOM   3561 N N   . ASP B 1 155 ? 0.850   13.958  13.530 1.00 54.56 ? 155 ASP A N   1 
ATOM   3562 C CA  . ASP B 1 155 ? 2.014   13.875  12.660 1.00 54.16 ? 155 ASP A CA  1 
ATOM   3563 C C   . ASP B 1 155 ? 3.051   14.944  12.966 1.00 47.08 ? 155 ASP A C   1 
ATOM   3564 O O   . ASP B 1 155 ? 4.097   14.973  12.306 1.00 45.60 ? 155 ASP A O   1 
ATOM   3565 C CB  . ASP B 1 155 ? 1.607   13.978  11.181 1.00 54.97 ? 155 ASP A CB  1 
ATOM   3566 C CG  . ASP B 1 155 ? 0.757   15.207  10.882 1.00 55.06 ? 155 ASP A CG  1 
ATOM   3567 O OD1 . ASP B 1 155 ? 0.380   15.935  11.831 1.00 54.99 ? 155 ASP A OD1 1 
ATOM   3568 O OD2 . ASP B 1 155 ? 0.485   15.455  9.684  1.00 53.12 ? 155 ASP A OD2 1 
ATOM   3569 N N   . CYS B 1 156 ? 2.796   15.815  13.942 1.00 44.54 ? 156 CYS A N   1 
ATOM   3570 C CA  . CYS B 1 156 ? 3.631   16.983  14.202 1.00 40.80 ? 156 CYS A CA  1 
ATOM   3571 C C   . CYS B 1 156 ? 4.574   16.701  15.366 1.00 35.08 ? 156 CYS A C   1 
ATOM   3572 O O   . CYS B 1 156 ? 4.123   16.415  16.481 1.00 33.89 ? 156 CYS A O   1 
ATOM   3573 C CB  . CYS B 1 156 ? 2.767   18.207  14.501 1.00 40.09 ? 156 CYS A CB  1 
ATOM   3574 S SG  . CYS B 1 156 ? 3.675   19.684  15.032 1.00 38.69 ? 156 CYS A SG  1 
ATOM   3575 N N   . VAL B 1 157 ? 5.873   16.801  15.106 1.00 30.08 ? 157 VAL A N   1 
ATOM   3576 C CA  . VAL B 1 157 ? 6.899   16.626  16.127 1.00 28.11 ? 157 VAL A CA  1 
ATOM   3577 C C   . VAL B 1 157 ? 7.166   17.970  16.788 1.00 26.28 ? 157 VAL A C   1 
ATOM   3578 O O   . VAL B 1 157 ? 7.590   18.917  16.121 1.00 27.85 ? 157 VAL A O   1 
ATOM   3579 C CB  . VAL B 1 157 ? 8.195   16.065  15.522 1.00 22.52 ? 157 VAL A CB  1 
ATOM   3580 C CG1 . VAL B 1 157 ? 9.244   15.868  16.622 1.00 21.35 ? 157 VAL A CG1 1 
ATOM   3581 C CG2 . VAL B 1 157 ? 7.911   14.764  14.779 1.00 30.14 ? 157 VAL A CG2 1 
ATOM   3582 N N   . SER B 1 158 ? 6.937   18.058  18.099 1.00 24.80 ? 158 SER A N   1 
ATOM   3583 C CA  . SER B 1 158 ? 7.324   19.237  18.875 1.00 25.55 ? 158 SER A CA  1 
ATOM   3584 C C   . SER B 1 158 ? 8.665   18.961  19.542 1.00 21.84 ? 158 SER A C   1 
ATOM   3585 O O   . SER B 1 158 ? 8.728   18.199  20.507 1.00 20.87 ? 158 SER A O   1 
ATOM   3586 C CB  . SER B 1 158 ? 6.282   19.591  19.936 1.00 26.26 ? 158 SER A CB  1 
ATOM   3587 O OG  . SER B 1 158 ? 5.058   20.003  19.360 1.00 32.12 ? 158 SER A OG  1 
ATOM   3588 N N   . PHE B 1 159 ? 9.729   19.600  19.054 1.00 20.67 ? 159 PHE A N   1 
ATOM   3589 C CA  . PHE B 1 159 ? 11.034  19.475  19.692 1.00 17.97 ? 159 PHE A CA  1 
ATOM   3590 C C   . PHE B 1 159 ? 11.108  20.405  20.895 1.00 20.62 ? 159 PHE A C   1 
ATOM   3591 O O   . PHE B 1 159 ? 10.792  21.591  20.786 1.00 19.52 ? 159 PHE A O   1 
ATOM   3592 C CB  . PHE B 1 159 ? 12.158  19.813  18.711 1.00 22.38 ? 159 PHE A CB  1 
ATOM   3593 C CG  . PHE B 1 159 ? 12.250  18.876  17.549 1.00 18.24 ? 159 PHE A CG  1 
ATOM   3594 C CD1 . PHE B 1 159 ? 12.880  17.645  17.681 1.00 20.40 ? 159 PHE A CD1 1 
ATOM   3595 C CD2 . PHE B 1 159 ? 11.703  19.222  16.325 1.00 18.83 ? 159 PHE A CD2 1 
ATOM   3596 C CE1 . PHE B 1 159 ? 12.978  16.776  16.617 1.00 21.40 ? 159 PHE A CE1 1 
ATOM   3597 C CE2 . PHE B 1 159 ? 11.791  18.365  15.250 1.00 21.39 ? 159 PHE A CE2 1 
ATOM   3598 C CZ  . PHE B 1 159 ? 12.435  17.125  15.394 1.00 22.14 ? 159 PHE A CZ  1 
ATOM   3599 N N   . CYS B 1 160 ? 11.517  19.872  22.052 1.00 19.39 ? 160 CYS A N   1 
ATOM   3600 C CA  . CYS B 1 160 ? 11.585  20.686  23.261 1.00 18.33 ? 160 CYS A CA  1 
ATOM   3601 C C   . CYS B 1 160 ? 12.937  20.671  23.969 1.00 19.40 ? 160 CYS A C   1 
ATOM   3602 O O   . CYS B 1 160 ? 13.143  21.502  24.862 1.00 21.91 ? 160 CYS A O   1 
ATOM   3603 C CB  . CYS B 1 160 ? 10.516  20.255  24.276 1.00 18.53 ? 160 CYS A CB  1 
ATOM   3604 S SG  . CYS B 1 160 ? 10.604  18.515  24.746 1.00 20.73 ? 160 CYS A SG  1 
ATOM   3605 N N   . TYR B 1 161 ? 13.860  19.785  23.610 1.00 16.16 ? 161 TYR A N   1 
ATOM   3606 C CA  . TYR B 1 161 ? 15.090  19.664  24.376 1.00 19.78 ? 161 TYR A CA  1 
ATOM   3607 C C   . TYR B 1 161 ? 16.227  19.288  23.444 1.00 18.14 ? 161 TYR A C   1 
ATOM   3608 O O   . TYR B 1 161 ? 16.033  18.530  22.484 1.00 17.27 ? 161 TYR A O   1 
ATOM   3609 C CB  . TYR B 1 161 ? 14.934  18.616  25.497 1.00 16.16 ? 161 TYR A CB  1 
ATOM   3610 C CG  . TYR B 1 161 ? 16.172  18.323  26.317 1.00 15.34 ? 161 TYR A CG  1 
ATOM   3611 C CD1 . TYR B 1 161 ? 16.456  19.066  27.451 1.00 16.65 ? 161 TYR A CD1 1 
ATOM   3612 C CD2 . TYR B 1 161 ? 17.050  17.301  25.967 1.00 16.18 ? 161 TYR A CD2 1 
ATOM   3613 C CE1 . TYR B 1 161 ? 17.561  18.807  28.223 1.00 18.37 ? 161 TYR A CE1 1 
ATOM   3614 C CE2 . TYR B 1 161 ? 18.176  17.025  26.748 1.00 15.59 ? 161 TYR A CE2 1 
ATOM   3615 C CZ  . TYR B 1 161 ? 18.420  17.792  27.869 1.00 16.85 ? 161 TYR A CZ  1 
ATOM   3616 O OH  . TYR B 1 161 ? 19.522  17.569  28.659 1.00 17.51 ? 161 TYR A OH  1 
ATOM   3617 N N   . MET B 1 162 ? 17.399  19.873  23.700 1.00 16.34 ? 162 MET A N   1 
ATOM   3618 C CA  . MET B 1 162 ? 18.653  19.440  23.092 1.00 15.87 ? 162 MET A CA  1 
ATOM   3619 C C   . MET B 1 162 ? 19.690  19.261  24.196 1.00 15.21 ? 162 MET A C   1 
ATOM   3620 O O   . MET B 1 162 ? 19.841  20.135  25.060 1.00 17.00 ? 162 MET A O   1 
ATOM   3621 C CB  . MET B 1 162 ? 19.153  20.433  22.034 1.00 17.07 ? 162 MET A CB  1 
ATOM   3622 C CG  . MET B 1 162 ? 20.583  20.097  21.586 1.00 18.33 ? 162 MET A CG  1 
ATOM   3623 S SD  . MET B 1 162 ? 21.023  20.880  20.021 1.00 23.29 ? 162 MET A SD  1 
ATOM   3624 C CE  . MET B 1 162 ? 20.002  20.021  18.838 1.00 17.91 ? 162 MET A CE  1 
ATOM   3625 N N   . HIS B 1 163 ? 20.396  18.126  24.182 1.00 16.17 ? 163 HIS A N   1 
ATOM   3626 C CA  . HIS B 1 163 ? 21.209  17.747  25.334 1.00 13.99 ? 163 HIS A CA  1 
ATOM   3627 C C   . HIS B 1 163 ? 22.564  18.458  25.293 1.00 16.54 ? 163 HIS A C   1 
ATOM   3628 O O   . HIS B 1 163 ? 23.215  18.485  24.249 1.00 16.53 ? 163 HIS A O   1 
ATOM   3629 C CB  . HIS B 1 163 ? 21.428  16.235  25.376 1.00 15.46 ? 163 HIS A CB  1 
ATOM   3630 C CG  . HIS B 1 163 ? 22.285  15.827  26.520 1.00 15.54 ? 163 HIS A CG  1 
ATOM   3631 N ND1 . HIS B 1 163 ? 21.957  16.152  27.817 1.00 17.74 ? 163 HIS A ND1 1 
ATOM   3632 C CD2 . HIS B 1 163 ? 23.504  15.240  26.570 1.00 15.14 ? 163 HIS A CD2 1 
ATOM   3633 C CE1 . HIS B 1 163 ? 22.910  15.731  28.626 1.00 15.37 ? 163 HIS A CE1 1 
ATOM   3634 N NE2 . HIS B 1 163 ? 23.856  15.165  27.897 1.00 15.36 ? 163 HIS A NE2 1 
ATOM   3635 N N   . HIS B 1 164 ? 22.994  19.028  26.432 1.00 16.94 ? 164 HIS A N   1 
ATOM   3636 C CA  . HIS B 1 164 ? 24.304  19.680  26.496 1.00 17.93 ? 164 HIS A CA  1 
ATOM   3637 C C   . HIS B 1 164 ? 25.239  19.154  27.574 1.00 19.24 ? 164 HIS A C   1 
ATOM   3638 O O   . HIS B 1 164 ? 26.452  19.141  27.349 1.00 20.32 ? 164 HIS A O   1 
ATOM   3639 C CB  . HIS B 1 164 ? 24.171  21.197  26.716 1.00 14.67 ? 164 HIS A CB  1 
ATOM   3640 C CG  . HIS B 1 164 ? 23.593  21.936  25.554 1.00 17.62 ? 164 HIS A CG  1 
ATOM   3641 N ND1 . HIS B 1 164 ? 24.292  22.907  24.864 1.00 18.05 ? 164 HIS A ND1 1 
ATOM   3642 C CD2 . HIS B 1 164 ? 22.349  21.914  25.016 1.00 19.57 ? 164 HIS A CD2 1 
ATOM   3643 C CE1 . HIS B 1 164 ? 23.521  23.413  23.917 1.00 20.47 ? 164 HIS A CE1 1 
ATOM   3644 N NE2 . HIS B 1 164 ? 22.336  22.830  23.988 1.00 18.42 ? 164 HIS A NE2 1 
ATOM   3645 N N   . MET B 1 165 ? 24.752  18.790  28.760 1.00 15.48 ? 165 MET A N   1 
ATOM   3646 C CA  . MET B 1 165 ? 25.710  18.574  29.834 1.00 18.92 ? 165 MET A CA  1 
ATOM   3647 C C   . MET B 1 165 ? 25.167  17.685  30.939 1.00 21.06 ? 165 MET A C   1 
ATOM   3648 O O   . MET B 1 165 ? 23.963  17.418  31.044 1.00 18.84 ? 165 MET A O   1 
ATOM   3649 C CB  . MET B 1 165 ? 26.179  19.889  30.448 1.00 21.68 ? 165 MET A CB  1 
ATOM   3650 C CG  . MET B 1 165 ? 25.119  20.676  31.081 1.00 26.85 ? 165 MET A CG  1 
ATOM   3651 S SD  . MET B 1 165 ? 25.867  22.259  31.559 1.00 44.59 ? 165 MET A SD  1 
ATOM   3652 C CE  . MET B 1 165 ? 25.193  22.415  33.203 1.00 28.05 ? 165 MET A CE  1 
ATOM   3653 N N   . GLU B 1 166 ? 26.109  17.221  31.753 1.00 21.66 ? 166 GLU A N   1 
ATOM   3654 C CA  . GLU B 1 166 ? 25.853  16.408  32.929 1.00 18.87 ? 166 GLU A CA  1 
ATOM   3655 C C   . GLU B 1 166 ? 26.136  17.211  34.193 1.00 20.62 ? 166 GLU A C   1 
ATOM   3656 O O   . GLU B 1 166 ? 27.150  17.916  34.291 1.00 20.37 ? 166 GLU A O   1 
ATOM   3657 C CB  . GLU B 1 166 ? 26.701  15.132  32.894 1.00 24.51 ? 166 GLU A CB  1 
ATOM   3658 C CG  . GLU B 1 166 ? 26.656  14.319  34.171 1.00 27.01 ? 166 GLU A CG  1 
ATOM   3659 C CD  . GLU B 1 166 ? 26.589  12.810  33.985 1.00 24.93 ? 166 GLU A CD  1 
ATOM   3660 O OE1 . GLU B 1 166 ? 26.829  12.134  35.007 1.00 30.09 ? 166 GLU A OE1 1 
ATOM   3661 O OE2 . GLU B 1 166 ? 26.225  12.293  32.889 1.00 23.42 ? 166 GLU A OE2 1 
ATOM   3662 N N   . LEU B 1 167 ? 25.228  17.100  35.148 1.00 20.35 ? 167 LEU A N   1 
ATOM   3663 C CA  . LEU B 1 167 ? 25.269  17.738  36.452 1.00 23.30 ? 167 LEU A CA  1 
ATOM   3664 C C   . LEU B 1 167 ? 25.534  16.690  37.533 1.00 26.25 ? 167 LEU A C   1 
ATOM   3665 O O   . LEU B 1 167 ? 25.525  15.488  37.257 1.00 21.70 ? 167 LEU A O   1 
ATOM   3666 C CB  . LEU B 1 167 ? 23.935  18.459  36.710 1.00 20.78 ? 167 LEU A CB  1 
ATOM   3667 C CG  . LEU B 1 167 ? 23.766  19.757  35.922 1.00 20.44 ? 167 LEU A CG  1 
ATOM   3668 C CD1 . LEU B 1 167 ? 22.293  20.169  35.910 1.00 20.41 ? 167 LEU A CD1 1 
ATOM   3669 C CD2 . LEU B 1 167 ? 24.641  20.877  36.497 1.00 22.24 ? 167 LEU A CD2 1 
ATOM   3670 N N   . PRO B 1 168 ? 25.807  17.111  38.772 1.00 27.79 ? 168 PRO A N   1 
ATOM   3671 C CA  . PRO B 1 168 ? 26.176  16.129  39.803 1.00 35.97 ? 168 PRO A CA  1 
ATOM   3672 C C   . PRO B 1 168 ? 25.098  15.086  40.069 1.00 29.43 ? 168 PRO A C   1 
ATOM   3673 O O   . PRO B 1 168 ? 23.906  15.312  39.854 1.00 24.91 ? 168 PRO A O   1 
ATOM   3674 C CB  . PRO B 1 168 ? 26.448  16.994  41.040 1.00 42.36 ? 168 PRO A CB  1 
ATOM   3675 C CG  . PRO B 1 168 ? 25.993  18.371  40.680 1.00 38.52 ? 168 PRO A CG  1 
ATOM   3676 C CD  . PRO B 1 168 ? 26.114  18.481  39.213 1.00 44.05 ? 168 PRO A CD  1 
ATOM   3677 N N   . SER B 1 169 ? 25.553  13.913  40.519 1.00 26.23 ? 169 SER A N   1 
ATOM   3678 C CA  . SER B 1 169 ? 24.680  12.786  40.869 1.00 28.26 ? 169 SER A CA  1 
ATOM   3679 C C   . SER B 1 169 ? 23.850  12.299  39.689 1.00 27.93 ? 169 SER A C   1 
ATOM   3680 O O   . SER B 1 169 ? 22.704  11.865  39.860 1.00 24.24 ? 169 SER A O   1 
ATOM   3681 C CB  . SER B 1 169 ? 23.774  13.122  42.054 1.00 30.05 ? 169 SER A CB  1 
ATOM   3682 O OG  . SER B 1 169 ? 24.512  13.786  43.062 1.00 35.34 ? 169 SER A OG  1 
ATOM   3683 N N   . GLY B 1 170 ? 24.420  12.374  38.491 1.00 24.36 ? 170 GLY A N   1 
ATOM   3684 C CA  . GLY B 1 170 ? 23.876  11.682  37.339 1.00 24.86 ? 170 GLY A CA  1 
ATOM   3685 C C   . GLY B 1 170 ? 22.594  12.234  36.757 1.00 23.30 ? 170 GLY A C   1 
ATOM   3686 O O   . GLY B 1 170 ? 21.763  11.452  36.280 1.00 28.39 ? 170 GLY A O   1 
ATOM   3687 N N   . VAL B 1 171 ? 22.397  13.552  36.787 1.00 20.68 ? 171 VAL A N   1 
ATOM   3688 C CA  . VAL B 1 171 ? 21.268  14.184  36.119 1.00 21.58 ? 171 VAL A CA  1 
ATOM   3689 C C   . VAL B 1 171 ? 21.819  15.102  35.029 1.00 19.95 ? 171 VAL A C   1 
ATOM   3690 O O   . VAL B 1 171 ? 23.030  15.301  34.907 1.00 21.60 ? 171 VAL A O   1 
ATOM   3691 C CB  . VAL B 1 171 ? 20.342  14.950  37.088 1.00 19.35 ? 171 VAL A CB  1 
ATOM   3692 C CG1 . VAL B 1 171 ? 19.664  13.954  38.058 1.00 23.38 ? 171 VAL A CG1 1 
ATOM   3693 C CG2 . VAL B 1 171 ? 21.090  16.039  37.831 1.00 18.68 ? 171 VAL A CG2 1 
ATOM   3694 N N   . HIS B 1 172 ? 20.919  15.617  34.196 1.00 16.59 ? 172 HIS A N   1 
ATOM   3695 C CA  . HIS B 1 172 ? 21.354  16.189  32.923 1.00 18.31 ? 172 HIS A CA  1 
ATOM   3696 C C   . HIS B 1 172 ? 20.662  17.513  32.656 1.00 17.12 ? 172 HIS A C   1 
ATOM   3697 O O   . HIS B 1 172 ? 19.580  17.780  33.173 1.00 18.30 ? 172 HIS A O   1 
ATOM   3698 C CB  . HIS B 1 172 ? 21.101  15.192  31.797 1.00 20.68 ? 172 HIS A CB  1 
ATOM   3699 C CG  . HIS B 1 172 ? 21.796  13.888  32.017 1.00 19.28 ? 172 HIS A CG  1 
ATOM   3700 N ND1 . HIS B 1 172 ? 21.175  12.786  32.573 1.00 19.47 ? 172 HIS A ND1 1 
ATOM   3701 C CD2 . HIS B 1 172 ? 23.087  13.532  31.810 1.00 18.99 ? 172 HIS A CD2 1 
ATOM   3702 C CE1 . HIS B 1 172 ? 22.048  11.793  32.657 1.00 20.03 ? 172 HIS A CE1 1 
ATOM   3703 N NE2 . HIS B 1 172 ? 23.213  12.220  32.198 1.00 21.35 ? 172 HIS A NE2 1 
ATOM   3704 N N   . ALA B 1 173 ? 21.327  18.367  31.865 1.00 16.30 ? 173 ALA A N   1 
ATOM   3705 C CA  . ALA B 1 173 ? 20.786  19.672  31.535 1.00 16.21 ? 173 ALA A CA  1 
ATOM   3706 C C   . ALA B 1 173 ? 20.951  19.954  30.049 1.00 15.64 ? 173 ALA A C   1 
ATOM   3707 O O   . ALA B 1 173 ? 21.874  19.458  29.400 1.00 16.63 ? 173 ALA A O   1 
ATOM   3708 C CB  . ALA B 1 173 ? 21.471  20.781  32.358 1.00 19.59 ? 173 ALA A CB  1 
ATOM   3709 N N   . GLY B 1 174 ? 20.067  20.792  29.521 1.00 17.12 ? 174 GLY A N   1 
ATOM   3710 C CA  . GLY B 1 174 ? 20.135  21.132  28.119 1.00 15.22 ? 174 GLY A CA  1 
ATOM   3711 C C   . GLY B 1 174 ? 19.303  22.361  27.833 1.00 15.79 ? 174 GLY A C   1 
ATOM   3712 O O   . GLY B 1 174 ? 18.865  23.056  28.748 1.00 17.74 ? 174 GLY A O   1 
ATOM   3713 N N   . THR B 1 175 ? 19.081  22.614  26.543 1.00 15.79 ? 175 THR A N   1 
ATOM   3714 C CA  . THR B 1 175 ? 18.381  23.805  26.080 1.00 17.77 ? 175 THR A CA  1 
ATOM   3715 C C   . THR B 1 175 ? 17.092  23.429  25.360 1.00 17.21 ? 175 THR A C   1 
ATOM   3716 O O   . THR B 1 175 ? 16.831  22.261  25.047 1.00 17.57 ? 175 THR A O   1 
ATOM   3717 C CB  . THR B 1 175 ? 19.268  24.628  25.132 1.00 16.21 ? 175 THR A CB  1 
ATOM   3718 O OG1 . THR B 1 175 ? 19.514  23.880  23.927 1.00 17.73 ? 175 THR A OG1 1 
ATOM   3719 C CG2 . THR B 1 175 ? 20.594  24.924  25.791 1.00 18.56 ? 175 THR A CG2 1 
ATOM   3720 N N   . ASP B 1 176 ? 16.275  24.441  25.104 1.00 19.79 ? 176 ASP A N   1 
ATOM   3721 C CA  . ASP B 1 176 ? 15.259  24.311  24.073 1.00 19.52 ? 176 ASP A CA  1 
ATOM   3722 C C   . ASP B 1 176 ? 15.927  24.477  22.702 1.00 16.34 ? 176 ASP A C   1 
ATOM   3723 O O   . ASP B 1 176 ? 17.149  24.629  22.592 1.00 18.69 ? 176 ASP A O   1 
ATOM   3724 C CB  . ASP B 1 176 ? 14.113  25.286  24.363 1.00 20.61 ? 176 ASP A CB  1 
ATOM   3725 C CG  . ASP B 1 176 ? 14.506  26.751  24.223 1.00 22.44 ? 176 ASP A CG  1 
ATOM   3726 O OD1 . ASP B 1 176 ? 15.557  27.090  23.642 1.00 21.17 ? 176 ASP A OD1 1 
ATOM   3727 O OD2 . ASP B 1 176 ? 13.752  27.589  24.756 1.00 23.14 ? 176 ASP A OD2 1 
ATOM   3728 N N   . LEU B 1 177 ? 15.141  24.392  21.630 1.00 18.18 ? 177 LEU A N   1 
ATOM   3729 C CA  . LEU B 1 177 ? 15.741  24.406  20.303 1.00 19.25 ? 177 LEU A CA  1 
ATOM   3730 C C   . LEU B 1 177 ? 16.035  25.823  19.817 1.00 19.51 ? 177 LEU A C   1 
ATOM   3731 O O   . LEU B 1 177 ? 16.582  25.992  18.726 1.00 22.01 ? 177 LEU A O   1 
ATOM   3732 C CB  . LEU B 1 177 ? 14.858  23.647  19.304 1.00 20.47 ? 177 LEU A CB  1 
ATOM   3733 C CG  . LEU B 1 177 ? 15.266  22.176  19.119 1.00 22.27 ? 177 LEU A CG  1 
ATOM   3734 C CD1 . LEU B 1 177 ? 16.658  22.055  18.506 1.00 20.73 ? 177 LEU A CD1 1 
ATOM   3735 C CD2 . LEU B 1 177 ? 15.205  21.422  20.463 1.00 21.17 ? 177 LEU A CD2 1 
ATOM   3736 N N   . GLU B 1 178 ? 15.705  26.826  20.620 1.00 21.36 ? 178 GLU A N   1 
ATOM   3737 C CA  . GLU B 1 178 ? 16.208  28.184  20.470 1.00 22.75 ? 178 GLU A CA  1 
ATOM   3738 C C   . GLU B 1 178 ? 17.485  28.404  21.269 1.00 21.68 ? 178 GLU A C   1 
ATOM   3739 O O   . GLU B 1 178 ? 17.971  29.538  21.342 1.00 21.79 ? 178 GLU A O   1 
ATOM   3740 C CB  . GLU B 1 178 ? 15.129  29.185  20.900 1.00 22.65 ? 178 GLU A CB  1 
ATOM   3741 C CG  . GLU B 1 178 ? 13.971  29.266  19.918 1.00 29.05 ? 178 GLU A CG  1 
ATOM   3742 C CD  . GLU B 1 178 ? 12.929  30.325  20.273 1.00 36.92 ? 178 GLU A CD  1 
ATOM   3743 O OE1 . GLU B 1 178 ? 12.821  30.728  21.455 1.00 37.96 ? 178 GLU A OE1 1 
ATOM   3744 O OE2 . GLU B 1 178 ? 12.199  30.752  19.357 1.00 36.35 ? 178 GLU A OE2 1 
ATOM   3745 N N   . GLY B 1 179 ? 18.030  27.353  21.887 1.00 22.27 ? 179 GLY A N   1 
ATOM   3746 C CA  . GLY B 1 179 ? 19.299  27.446  22.574 1.00 20.17 ? 179 GLY A CA  1 
ATOM   3747 C C   . GLY B 1 179 ? 19.260  28.041  23.961 1.00 18.90 ? 179 GLY A C   1 
ATOM   3748 O O   . GLY B 1 179 ? 20.317  28.319  24.530 1.00 18.76 ? 179 GLY A O   1 
ATOM   3749 N N   . ASN B 1 180 ? 18.083  28.258  24.531 1.00 20.21 ? 180 ASN A N   1 
ATOM   3750 C CA  . ASN B 1 180 ? 17.980  28.762  25.893 1.00 18.42 ? 180 ASN A CA  1 
ATOM   3751 C C   . ASN B 1 180 ? 17.971  27.588  26.866 1.00 18.98 ? 180 ASN A C   1 
ATOM   3752 O O   . ASN B 1 180 ? 17.103  26.710  26.783 1.00 20.77 ? 180 ASN A O   1 
ATOM   3753 C CB  . ASN B 1 180 ? 16.728  29.624  26.043 1.00 19.66 ? 180 ASN A CB  1 
ATOM   3754 C CG  . ASN B 1 180 ? 16.853  30.946  25.297 1.00 26.09 ? 180 ASN A CG  1 
ATOM   3755 O OD1 . ASN B 1 180 ? 17.839  31.653  25.459 1.00 26.39 ? 180 ASN A OD1 1 
ATOM   3756 N ND2 . ASN B 1 180 ? 15.882  31.257  24.448 1.00 27.55 ? 180 ASN A ND2 1 
ATOM   3757 N N   . PHE B 1 181 ? 18.911  27.595  27.808 1.00 16.93 ? 181 PHE A N   1 
ATOM   3758 C CA  . PHE B 1 181 ? 18.934  26.563  28.839 1.00 18.51 ? 181 PHE A CA  1 
ATOM   3759 C C   . PHE B 1 181 ? 17.640  26.510  29.650 1.00 17.44 ? 181 PHE A C   1 
ATOM   3760 O O   . PHE B 1 181 ? 17.030  27.535  29.999 1.00 18.32 ? 181 PHE A O   1 
ATOM   3761 C CB  . PHE B 1 181 ? 20.106  26.781  29.792 1.00 18.96 ? 181 PHE A CB  1 
ATOM   3762 C CG  . PHE B 1 181 ? 21.297  25.949  29.467 1.00 20.39 ? 181 PHE A CG  1 
ATOM   3763 C CD1 . PHE B 1 181 ? 21.395  24.642  29.921 1.00 18.92 ? 181 PHE A CD1 1 
ATOM   3764 C CD2 . PHE B 1 181 ? 22.319  26.467  28.677 1.00 19.51 ? 181 PHE A CD2 1 
ATOM   3765 C CE1 . PHE B 1 181 ? 22.485  23.859  29.597 1.00 18.47 ? 181 PHE A CE1 1 
ATOM   3766 C CE2 . PHE B 1 181 ? 23.422  25.693  28.367 1.00 19.79 ? 181 PHE A CE2 1 
ATOM   3767 C CZ  . PHE B 1 181 ? 23.507  24.395  28.819 1.00 19.64 ? 181 PHE A CZ  1 
ATOM   3768 N N   . TYR B 1 182 ? 17.237  25.292  29.975 1.00 17.65 ? 182 TYR A N   1 
ATOM   3769 C CA  . TYR B 1 182 ? 16.307  25.055  31.062 1.00 17.23 ? 182 TYR A CA  1 
ATOM   3770 C C   . TYR B 1 182 ? 17.093  25.169  32.366 1.00 21.47 ? 182 TYR A C   1 
ATOM   3771 O O   . TYR B 1 182 ? 18.061  24.428  32.575 1.00 21.40 ? 182 TYR A O   1 
ATOM   3772 C CB  . TYR B 1 182 ? 15.687  23.664  30.913 1.00 19.20 ? 182 TYR A CB  1 
ATOM   3773 C CG  . TYR B 1 182 ? 14.710  23.521  29.762 1.00 17.46 ? 182 TYR A CG  1 
ATOM   3774 C CD1 . TYR B 1 182 ? 13.407  24.009  29.865 1.00 20.37 ? 182 TYR A CD1 1 
ATOM   3775 C CD2 . TYR B 1 182 ? 15.093  22.907  28.574 1.00 18.10 ? 182 TYR A CD2 1 
ATOM   3776 C CE1 . TYR B 1 182 ? 12.510  23.876  28.816 1.00 22.83 ? 182 TYR A CE1 1 
ATOM   3777 C CE2 . TYR B 1 182 ? 14.225  22.786  27.520 1.00 19.21 ? 182 TYR A CE2 1 
ATOM   3778 C CZ  . TYR B 1 182 ? 12.920  23.272  27.652 1.00 19.13 ? 182 TYR A CZ  1 
ATOM   3779 O OH  . TYR B 1 182 ? 12.040  23.140  26.604 1.00 19.63 ? 182 TYR A OH  1 
ATOM   3780 N N   . GLY B 1 183 ? 16.716  26.111  33.224 1.00 22.12 ? 183 GLY A N   1 
ATOM   3781 C CA  . GLY B 1 183 ? 17.368  26.258  34.503 1.00 21.58 ? 183 GLY A CA  1 
ATOM   3782 C C   . GLY B 1 183 ? 18.524  27.235  34.480 1.00 22.99 ? 183 GLY A C   1 
ATOM   3783 O O   . GLY B 1 183 ? 18.858  27.817  33.444 1.00 24.10 ? 183 GLY A O   1 
ATOM   3784 N N   . PRO B 1 184 ? 19.160  27.430  35.633 1.00 23.12 ? 184 PRO A N   1 
ATOM   3785 C CA  . PRO B 1 184 ? 20.187  28.478  35.767 1.00 20.86 ? 184 PRO A CA  1 
ATOM   3786 C C   . PRO B 1 184 ? 21.554  28.117  35.198 1.00 28.19 ? 184 PRO A C   1 
ATOM   3787 O O   . PRO B 1 184 ? 22.526  28.835  35.458 1.00 33.23 ? 184 PRO A O   1 
ATOM   3788 C CB  . PRO B 1 184 ? 20.261  28.671  37.291 1.00 22.57 ? 184 PRO A CB  1 
ATOM   3789 C CG  . PRO B 1 184 ? 19.921  27.316  37.836 1.00 28.25 ? 184 PRO A CG  1 
ATOM   3790 C CD  . PRO B 1 184 ? 18.835  26.805  36.928 1.00 22.98 ? 184 PRO A CD  1 
ATOM   3791 N N   . PHE B 1 185 ? 21.650  27.081  34.384 1.00 20.80 ? 185 PHE A N   1 
ATOM   3792 C CA  . PHE B 1 185 ? 22.918  26.488  33.978 1.00 21.25 ? 185 PHE A CA  1 
ATOM   3793 C C   . PHE B 1 185 ? 23.518  27.189  32.762 1.00 20.81 ? 185 PHE A C   1 
ATOM   3794 O O   . PHE B 1 185 ? 22.833  27.892  32.004 1.00 21.74 ? 185 PHE A O   1 
ATOM   3795 C CB  . PHE B 1 185 ? 22.710  25.007  33.699 1.00 22.59 ? 185 PHE A CB  1 
ATOM   3796 C CG  . PHE B 1 185 ? 21.923  24.320  34.771 1.00 22.51 ? 185 PHE A CG  1 
ATOM   3797 C CD1 . PHE B 1 185 ? 22.449  24.201  36.042 1.00 20.91 ? 185 PHE A CD1 1 
ATOM   3798 C CD2 . PHE B 1 185 ? 20.646  23.834  34.524 1.00 21.19 ? 185 PHE A CD2 1 
ATOM   3799 C CE1 . PHE B 1 185 ? 21.707  23.582  37.061 1.00 21.57 ? 185 PHE A CE1 1 
ATOM   3800 C CE2 . PHE B 1 185 ? 19.917  23.216  35.528 1.00 21.07 ? 185 PHE A CE2 1 
ATOM   3801 C CZ  . PHE B 1 185 ? 20.461  23.095  36.797 1.00 21.01 ? 185 PHE A CZ  1 
ATOM   3802 N N   . VAL B 1 186 ? 24.825  26.997  32.595 1.00 21.74 ? 186 VAL A N   1 
ATOM   3803 C CA  . VAL B 1 186 ? 25.582  27.565  31.485 1.00 22.00 ? 186 VAL A CA  1 
ATOM   3804 C C   . VAL B 1 186 ? 26.449  26.480  30.854 1.00 21.49 ? 186 VAL A C   1 
ATOM   3805 O O   . VAL B 1 186 ? 26.888  25.543  31.530 1.00 21.65 ? 186 VAL A O   1 
ATOM   3806 C CB  . VAL B 1 186 ? 26.456  28.753  31.952 1.00 21.49 ? 186 VAL A CB  1 
ATOM   3807 C CG1 . VAL B 1 186 ? 25.578  29.937  32.327 1.00 25.18 ? 186 VAL A CG1 1 
ATOM   3808 C CG2 . VAL B 1 186 ? 27.365  28.349  33.109 1.00 20.44 ? 186 VAL A CG2 1 
ATOM   3809 N N   . ASP B 1 187 ? 26.705  26.607  29.541 1.00 19.17 ? 187 ASP A N   1 
ATOM   3810 C CA  . ASP B 1 187 ? 27.494  25.598  28.829 1.00 17.93 ? 187 ASP A CA  1 
ATOM   3811 C C   . ASP B 1 187 ? 28.978  25.910  29.019 1.00 22.88 ? 187 ASP A C   1 
ATOM   3812 O O   . ASP B 1 187 ? 29.673  26.414  28.135 1.00 21.21 ? 187 ASP A O   1 
ATOM   3813 C CB  . ASP B 1 187 ? 27.098  25.485  27.349 1.00 18.31 ? 187 ASP A CB  1 
ATOM   3814 C CG  . ASP B 1 187 ? 27.037  26.826  26.609 1.00 21.22 ? 187 ASP A CG  1 
ATOM   3815 O OD1 . ASP B 1 187 ? 27.111  27.908  27.234 1.00 21.58 ? 187 ASP A OD1 1 
ATOM   3816 O OD2 . ASP B 1 187 ? 26.882  26.774  25.368 1.00 18.47 ? 187 ASP A OD2 1 
ATOM   3817 N N   . ARG B 1 188 ? 29.467  25.581  30.212 1.00 21.88 ? 188 ARG A N   1 
ATOM   3818 C CA  . ARG B 1 188 ? 30.848  25.831  30.588 1.00 24.02 ? 188 ARG A CA  1 
ATOM   3819 C C   . ARG B 1 188 ? 31.274  24.704  31.519 1.00 24.11 ? 188 ARG A C   1 
ATOM   3820 O O   . ARG B 1 188 ? 30.473  24.239  32.331 1.00 22.30 ? 188 ARG A O   1 
ATOM   3821 C CB  . ARG B 1 188 ? 30.959  27.205  31.268 1.00 26.69 ? 188 ARG A CB  1 
ATOM   3822 C CG  . ARG B 1 188 ? 32.299  27.545  31.877 1.00 33.85 ? 188 ARG A CG  1 
ATOM   3823 C CD  . ARG B 1 188 ? 32.424  29.076  32.094 1.00 39.92 ? 188 ARG A CD  1 
ATOM   3824 N NE  . ARG B 1 188 ? 33.365  29.407  33.161 1.00 43.04 ? 188 ARG A NE  1 
ATOM   3825 C CZ  . ARG B 1 188 ? 33.186  30.358  34.071 1.00 43.30 ? 188 ARG A CZ  1 
ATOM   3826 N NH1 . ARG B 1 188 ? 32.104  31.126  34.071 1.00 44.69 ? 188 ARG A NH1 1 
ATOM   3827 N NH2 . ARG B 1 188 ? 34.112  30.537  35.009 1.00 47.32 ? 188 ARG A NH2 1 
ATOM   3828 N N   . GLN B 1 189 ? 32.521  24.249  31.381 1.00 22.72 ? 189 GLN A N   1 
ATOM   3829 C CA  . GLN B 1 189 ? 33.058  23.198  32.249 1.00 24.44 ? 189 GLN A CA  1 
ATOM   3830 C C   . GLN B 1 189 ? 33.494  23.820  33.573 1.00 23.80 ? 189 GLN A C   1 
ATOM   3831 O O   . GLN B 1 189 ? 34.675  24.033  33.852 1.00 26.61 ? 189 GLN A O   1 
ATOM   3832 C CB  . GLN B 1 189 ? 34.202  22.460  31.565 1.00 22.27 ? 189 GLN A CB  1 
ATOM   3833 C CG  . GLN B 1 189 ? 34.770  21.278  32.357 1.00 23.94 ? 189 GLN A CG  1 
ATOM   3834 C CD  . GLN B 1 189 ? 35.714  20.414  31.528 1.00 23.63 ? 189 GLN A CD  1 
ATOM   3835 O OE1 . GLN B 1 189 ? 35.771  20.533  30.307 1.00 23.72 ? 189 GLN A OE1 1 
ATOM   3836 N NE2 . GLN B 1 189 ? 36.439  19.508  32.198 1.00 24.97 ? 189 GLN A NE2 1 
ATOM   3837 N N   . THR B 1 190 ? 32.502  24.109  34.408 1.00 24.40 ? 190 THR A N   1 
ATOM   3838 C CA  . THR B 1 190 ? 32.701  24.613  35.759 1.00 28.43 ? 190 THR A CA  1 
ATOM   3839 C C   . THR B 1 190 ? 31.715  23.922  36.679 1.00 30.32 ? 190 THR A C   1 
ATOM   3840 O O   . THR B 1 190 ? 30.705  23.374  36.230 1.00 27.47 ? 190 THR A O   1 
ATOM   3841 C CB  . THR B 1 190 ? 32.508  26.141  35.881 1.00 30.47 ? 190 THR A CB  1 
ATOM   3842 O OG1 . THR B 1 190 ? 31.136  26.491  35.637 1.00 31.83 ? 190 THR A OG1 1 
ATOM   3843 C CG2 . THR B 1 190 ? 33.421  26.892  34.968 1.00 36.77 ? 190 THR A CG2 1 
ATOM   3844 N N   . ALA B 1 191 ? 32.016  23.970  37.977 1.00 31.09 ? 191 ALA A N   1 
ATOM   3845 C CA  . ALA B 1 191 ? 31.134  23.370  38.968 1.00 30.27 ? 191 ALA A CA  1 
ATOM   3846 C C   . ALA B 1 191 ? 29.813  24.121  38.998 1.00 28.88 ? 191 ALA A C   1 
ATOM   3847 O O   . ALA B 1 191 ? 29.782  25.352  39.108 1.00 31.67 ? 191 ALA A O   1 
ATOM   3848 C CB  . ALA B 1 191 ? 31.786  23.389  40.351 1.00 33.08 ? 191 ALA A CB  1 
ATOM   3849 N N   . GLN B 1 192 ? 28.721  23.373  38.881 1.00 25.04 ? 192 GLN A N   1 
ATOM   3850 C CA  . GLN B 1 192 ? 27.384  23.932  38.877 1.00 25.18 ? 192 GLN A CA  1 
ATOM   3851 C C   . GLN B 1 192 ? 26.484  22.987  39.643 1.00 23.78 ? 192 GLN A C   1 
ATOM   3852 O O   . GLN B 1 192 ? 26.618  21.765  39.530 1.00 24.04 ? 192 GLN A O   1 
ATOM   3853 C CB  . GLN B 1 192 ? 26.852  24.132  37.459 1.00 24.10 ? 192 GLN A CB  1 
ATOM   3854 C CG  . GLN B 1 192 ? 27.638  25.152  36.647 1.00 24.07 ? 192 GLN A CG  1 
ATOM   3855 C CD  . GLN B 1 192 ? 27.111  25.273  35.238 1.00 22.97 ? 192 GLN A CD  1 
ATOM   3856 O OE1 . GLN B 1 192 ? 25.971  25.663  35.032 1.00 21.30 ? 192 GLN A OE1 1 
ATOM   3857 N NE2 . GLN B 1 192 ? 27.941  24.929  34.256 1.00 23.77 ? 192 GLN A NE2 1 
ATOM   3858 N N   . ALA B 1 193 ? 25.583  23.559  40.427 1.00 24.28 ? 193 ALA A N   1 
ATOM   3859 C CA  . ALA B 1 193 ? 24.682  22.789  41.265 1.00 24.26 ? 193 ALA A CA  1 
ATOM   3860 C C   . ALA B 1 193 ? 23.248  23.038  40.822 1.00 19.57 ? 193 ALA A C   1 
ATOM   3861 O O   . ALA B 1 193 ? 22.892  24.150  40.421 1.00 24.45 ? 193 ALA A O   1 
ATOM   3862 C CB  . ALA B 1 193 ? 24.856  23.157  42.746 1.00 26.19 ? 193 ALA A CB  1 
ATOM   3863 N N   . ALA B 1 194 ? 22.445  21.982  40.860 1.00 20.92 ? 194 ALA A N   1 
ATOM   3864 C CA  . ALA B 1 194 ? 21.014  22.131  40.663 1.00 24.11 ? 194 ALA A CA  1 
ATOM   3865 C C   . ALA B 1 194 ? 20.334  22.379  41.999 1.00 22.09 ? 194 ALA A C   1 
ATOM   3866 O O   . ALA B 1 194 ? 20.799  21.932  43.052 1.00 22.90 ? 194 ALA A O   1 
ATOM   3867 C CB  . ALA B 1 194 ? 20.415  20.886  40.010 1.00 20.14 ? 194 ALA A CB  1 
ATOM   3868 N N   . GLY B 1 195 ? 19.211  23.078  41.943 1.00 23.45 ? 195 GLY A N   1 
ATOM   3869 C CA  . GLY B 1 195 ? 18.404  23.243  43.134 1.00 24.13 ? 195 GLY A CA  1 
ATOM   3870 C C   . GLY B 1 195 ? 17.863  21.921  43.644 1.00 24.26 ? 195 GLY A C   1 
ATOM   3871 O O   . GLY B 1 195 ? 17.804  20.907  42.937 1.00 19.29 ? 195 GLY A O   1 
ATOM   3872 N N   . THR B 1 196 ? 17.447  21.955  44.909 1.00 21.75 ? 196 THR A N   1 
ATOM   3873 C CA  . THR B 1 196 ? 16.844  20.789  45.547 1.00 22.49 ? 196 THR A CA  1 
ATOM   3874 C C   . THR B 1 196 ? 15.648  20.313  44.743 1.00 22.45 ? 196 THR A C   1 
ATOM   3875 O O   . THR B 1 196 ? 14.808  21.116  44.333 1.00 24.00 ? 196 THR A O   1 
ATOM   3876 C CB  . THR B 1 196 ? 16.405  21.145  46.970 1.00 25.03 ? 196 THR A CB  1 
ATOM   3877 O OG1 . THR B 1 196 ? 17.539  21.615  47.704 1.00 26.13 ? 196 THR A OG1 1 
ATOM   3878 C CG2 . THR B 1 196 ? 15.786  19.918  47.681 1.00 22.77 ? 196 THR A CG2 1 
ATOM   3879 N N   . ASP B 1 197 ? 15.555  19.010  44.526 1.00 21.33 ? 197 ASP A N   1 
ATOM   3880 C CA  . ASP B 1 197 ? 14.418  18.611  43.723 1.00 23.55 ? 197 ASP A CA  1 
ATOM   3881 C C   . ASP B 1 197 ? 13.217  18.299  44.611 1.00 24.52 ? 197 ASP A C   1 
ATOM   3882 O O   . ASP B 1 197 ? 13.333  18.091  45.822 1.00 24.12 ? 197 ASP A O   1 
ATOM   3883 C CB  . ASP B 1 197 ? 14.724  17.424  42.834 1.00 29.31 ? 197 ASP A CB  1 
ATOM   3884 C CG  . ASP B 1 197 ? 13.775  17.369  41.660 1.00 22.40 ? 197 ASP A CG  1 
ATOM   3885 O OD1 . ASP B 1 197 ? 13.197  18.458  41.307 1.00 28.15 ? 197 ASP A OD1 1 
ATOM   3886 O OD2 . ASP B 1 197 ? 13.627  16.297  41.093 1.00 25.27 ? 197 ASP A OD2 1 
ATOM   3887 N N   . THR B 1 198 ? 12.053  18.301  43.980 1.00 21.83 ? 198 THR A N   1 
ATOM   3888 C CA  . THR B 1 198 ? 10.764  18.096  44.630 1.00 20.84 ? 198 THR A CA  1 
ATOM   3889 C C   . THR B 1 198 ? 9.973   17.079  43.823 1.00 20.55 ? 198 THR A C   1 
ATOM   3890 O O   . THR B 1 198 ? 10.274  16.817  42.656 1.00 18.81 ? 198 THR A O   1 
ATOM   3891 C CB  . THR B 1 198 ? 9.974   19.407  44.710 1.00 20.80 ? 198 THR A CB  1 
ATOM   3892 O OG1 . THR B 1 198 ? 9.946   20.000  43.409 1.00 24.03 ? 198 THR A OG1 1 
ATOM   3893 C CG2 . THR B 1 198 ? 10.608  20.396  45.700 1.00 21.94 ? 198 THR A CG2 1 
ATOM   3894 N N   . THR B 1 199 ? 8.944   16.500  44.450 1.00 17.36 ? 199 THR A N   1 
ATOM   3895 C CA  . THR B 1 199 ? 8.097   15.532  43.764 1.00 16.70 ? 199 THR A CA  1 
ATOM   3896 C C   . THR B 1 199 ? 6.960   16.241  43.040 1.00 18.15 ? 199 THR A C   1 
ATOM   3897 O O   . THR B 1 199 ? 6.335   17.152  43.594 1.00 18.01 ? 199 THR A O   1 
ATOM   3898 C CB  . THR B 1 199 ? 7.545   14.523  44.767 1.00 15.27 ? 199 THR A CB  1 
ATOM   3899 O OG1 . THR B 1 199 ? 8.650   13.904  45.437 1.00 20.58 ? 199 THR A OG1 1 
ATOM   3900 C CG2 . THR B 1 199 ? 6.746   13.443  44.044 1.00 16.25 ? 199 THR A CG2 1 
ATOM   3901 N N   . ILE B 1 200 ? 6.696   15.813  41.802 1.00 16.63 ? 200 ILE A N   1 
ATOM   3902 C CA  . ILE B 1 200 ? 5.723   16.466  40.935 1.00 16.55 ? 200 ILE A CA  1 
ATOM   3903 C C   . ILE B 1 200 ? 4.321   15.980  41.270 1.00 14.97 ? 200 ILE A C   1 
ATOM   3904 O O   . ILE B 1 200 ? 3.853   14.965  40.734 1.00 16.25 ? 200 ILE A O   1 
ATOM   3905 C CB  . ILE B 1 200 ? 6.053   16.247  39.452 1.00 17.76 ? 200 ILE A CB  1 
ATOM   3906 C CG1 . ILE B 1 200 ? 7.540   16.551  39.180 1.00 18.85 ? 200 ILE A CG1 1 
ATOM   3907 C CG2 . ILE B 1 200 ? 5.147   17.107  38.562 1.00 18.98 ? 200 ILE A CG2 1 
ATOM   3908 C CD1 . ILE B 1 200 ? 7.978   16.145  37.795 1.00 19.42 ? 200 ILE A CD1 1 
ATOM   3909 N N   . THR B 1 201 ? 3.657   16.725  42.151 1.00 15.70 ? 201 THR A N   1 
ATOM   3910 C CA  . THR B 1 201 ? 2.414   16.276  42.784 1.00 17.23 ? 201 THR A CA  1 
ATOM   3911 C C   . THR B 1 201 ? 1.334   15.937  41.770 1.00 13.36 ? 201 THR A C   1 
ATOM   3912 O O   . THR B 1 201 ? 0.692   14.882  41.863 1.00 15.88 ? 201 THR A O   1 
ATOM   3913 C CB  . THR B 1 201 ? 1.936   17.364  43.744 1.00 16.71 ? 201 THR A CB  1 
ATOM   3914 O OG1 . THR B 1 201 ? 3.009   17.696  44.631 1.00 16.94 ? 201 THR A OG1 1 
ATOM   3915 C CG2 . THR B 1 201 ? 0.733   16.912  44.559 1.00 17.07 ? 201 THR A CG2 1 
ATOM   3916 N N   . VAL B 1 202 ? 1.084   16.831  40.814 1.00 14.30 ? 202 VAL A N   1 
ATOM   3917 C CA  . VAL B 1 202 ? 0.006   16.580  39.868 1.00 14.66 ? 202 VAL A CA  1 
ATOM   3918 C C   . VAL B 1 202 ? 0.259   15.295  39.099 1.00 17.04 ? 202 VAL A C   1 
ATOM   3919 O O   . VAL B 1 202 ? -0.687  14.568  38.767 1.00 13.96 ? 202 VAL A O   1 
ATOM   3920 C CB  . VAL B 1 202 ? -0.205  17.800  38.938 1.00 16.41 ? 202 VAL A CB  1 
ATOM   3921 C CG1 . VAL B 1 202 ? 1.033   18.068  38.038 1.00 17.56 ? 202 VAL A CG1 1 
ATOM   3922 C CG2 . VAL B 1 202 ? -1.485  17.636  38.104 1.00 15.32 ? 202 VAL A CG2 1 
ATOM   3923 N N   . ASN B 1 203 ? 1.530   14.977  38.839 1.00 14.56 ? 203 ASN A N   1 
ATOM   3924 C CA  . ASN B 1 203 ? 1.868   13.740  38.137 1.00 13.92 ? 203 ASN A CA  1 
ATOM   3925 C C   . ASN B 1 203 ? 1.644   12.514  39.014 1.00 13.47 ? 203 ASN A C   1 
ATOM   3926 O O   . ASN B 1 203 ? 1.136   11.490  38.533 1.00 16.68 ? 203 ASN A O   1 
ATOM   3927 C CB  . ASN B 1 203 ? 3.320   13.797  37.658 1.00 13.18 ? 203 ASN A CB  1 
ATOM   3928 C CG  . ASN B 1 203 ? 3.494   14.675  36.439 1.00 14.37 ? 203 ASN A CG  1 
ATOM   3929 O OD1 . ASN B 1 203 ? 2.549   15.306  35.970 1.00 15.62 ? 203 ASN A OD1 1 
ATOM   3930 N ND2 . ASN B 1 203 ? 4.724   14.727  35.922 1.00 15.99 ? 203 ASN A ND2 1 
ATOM   3931 N N   . VAL B 1 204 ? 2.011   12.584  40.300 1.00 13.45 ? 204 VAL A N   1 
ATOM   3932 C CA  . VAL B 1 204 ? 1.701   11.467  41.203 1.00 15.85 ? 204 VAL A CA  1 
ATOM   3933 C C   . VAL B 1 204 ? 0.197   11.203  41.230 1.00 12.72 ? 204 VAL A C   1 
ATOM   3934 O O   . VAL B 1 204 ? -0.250  10.051  41.205 1.00 14.64 ? 204 VAL A O   1 
ATOM   3935 C CB  . VAL B 1 204 ? 2.243   11.731  42.619 1.00 10.76 ? 204 VAL A CB  1 
ATOM   3936 C CG1 . VAL B 1 204 ? 1.841   10.633  43.574 1.00 15.59 ? 204 VAL A CG1 1 
ATOM   3937 C CG2 . VAL B 1 204 ? 3.792   11.876  42.590 1.00 14.15 ? 204 VAL A CG2 1 
ATOM   3938 N N   . LEU B 1 205 ? -0.605  12.265  41.281 1.00 13.26 ? 205 LEU A N   1 
ATOM   3939 C CA  . LEU B 1 205 ? -2.052  12.085  41.278 1.00 14.73 ? 205 LEU A CA  1 
ATOM   3940 C C   . LEU B 1 205 ? -2.521  11.434  39.975 1.00 15.57 ? 205 LEU A C   1 
ATOM   3941 O O   . LEU B 1 205 ? -3.352  10.517  39.996 1.00 16.49 ? 205 LEU A O   1 
ATOM   3942 C CB  . LEU B 1 205 ? -2.715  13.446  41.527 1.00 14.10 ? 205 LEU A CB  1 
ATOM   3943 C CG  . LEU B 1 205 ? -2.614  13.907  42.992 1.00 11.54 ? 205 LEU A CG  1 
ATOM   3944 C CD1 . LEU B 1 205 ? -3.087  15.350  43.104 1.00 14.50 ? 205 LEU A CD1 1 
ATOM   3945 C CD2 . LEU B 1 205 ? -3.419  13.024  43.958 1.00 14.26 ? 205 LEU A CD2 1 
ATOM   3946 N N   . ALA B 1 206 ? -1.951  11.850  38.838 1.00 15.73 ? 206 ALA A N   1 
ATOM   3947 C CA  . ALA B 1 206 ? -2.297  11.228  37.560 1.00 15.95 ? 206 ALA A CA  1 
ATOM   3948 C C   . ALA B 1 206 ? -1.995  9.735   37.580 1.00 16.01 ? 206 ALA A C   1 
ATOM   3949 O O   . ALA B 1 206 ? -2.771  8.923   37.060 1.00 15.75 ? 206 ALA A O   1 
ATOM   3950 C CB  . ALA B 1 206 ? -1.522  11.893  36.416 1.00 16.19 ? 206 ALA A CB  1 
ATOM   3951 N N   . TRP B 1 207 ? -0.863  9.372   38.172 1.00 14.97 ? 207 TRP A N   1 
ATOM   3952 C CA  . TRP B 1 207 ? -0.424  7.987   38.205 1.00 15.84 ? 207 TRP A CA  1 
ATOM   3953 C C   . TRP B 1 207 ? -1.265  7.183   39.184 1.00 16.39 ? 207 TRP A C   1 
ATOM   3954 O O   . TRP B 1 207 ? -1.522  5.997   38.956 1.00 17.60 ? 207 TRP A O   1 
ATOM   3955 C CB  . TRP B 1 207 ? 1.064   7.968   38.565 1.00 16.32 ? 207 TRP A CB  1 
ATOM   3956 C CG  . TRP B 1 207 ? 1.674   6.644   38.836 1.00 17.84 ? 207 TRP A CG  1 
ATOM   3957 C CD1 . TRP B 1 207 ? 2.122   5.736   37.918 1.00 20.90 ? 207 TRP A CD1 1 
ATOM   3958 C CD2 . TRP B 1 207 ? 1.969   6.100   40.117 1.00 17.53 ? 207 TRP A CD2 1 
ATOM   3959 N NE1 . TRP B 1 207 ? 2.676   4.652   38.554 1.00 20.01 ? 207 TRP A NE1 1 
ATOM   3960 C CE2 . TRP B 1 207 ? 2.590   4.850   39.909 1.00 21.36 ? 207 TRP A CE2 1 
ATOM   3961 C CE3 . TRP B 1 207 ? 1.768   6.550   41.426 1.00 19.52 ? 207 TRP A CE3 1 
ATOM   3962 C CZ2 . TRP B 1 207 ? 3.001   4.037   40.963 1.00 22.77 ? 207 TRP A CZ2 1 
ATOM   3963 C CZ3 . TRP B 1 207 ? 2.176   5.735   42.474 1.00 21.48 ? 207 TRP A CZ3 1 
ATOM   3964 C CH2 . TRP B 1 207 ? 2.784   4.501   42.236 1.00 19.30 ? 207 TRP A CH2 1 
ATOM   3965 N N   . LEU B 1 208 ? -1.739  7.816   40.261 1.00 16.18 ? 208 LEU A N   1 
ATOM   3966 C CA  . LEU B 1 208 ? -2.705  7.122   41.103 1.00 18.42 ? 208 LEU A CA  1 
ATOM   3967 C C   . LEU B 1 208 ? -4.003  6.877   40.345 1.00 16.36 ? 208 LEU A C   1 
ATOM   3968 O O   . LEU B 1 208 ? -4.638  5.835   40.530 1.00 15.32 ? 208 LEU A O   1 
ATOM   3969 C CB  . LEU B 1 208 ? -2.956  7.901   42.391 1.00 16.95 ? 208 LEU A CB  1 
ATOM   3970 C CG  . LEU B 1 208 ? -1.798  7.974   43.387 1.00 18.57 ? 208 LEU A CG  1 
ATOM   3971 C CD1 . LEU B 1 208 ? -2.199  8.827   44.594 1.00 17.05 ? 208 LEU A CD1 1 
ATOM   3972 C CD2 . LEU B 1 208 ? -1.322  6.595   43.840 1.00 14.53 ? 208 LEU A CD2 1 
ATOM   3973 N N   . TYR B 1 209 ? -4.412  7.811   39.471 1.00 14.73 ? 209 TYR A N   1 
ATOM   3974 C CA  . TYR B 1 209 ? -5.573  7.523   38.627 1.00 16.59 ? 209 TYR A CA  1 
ATOM   3975 C C   . TYR B 1 209 ? -5.274  6.388   37.657 1.00 19.20 ? 209 TYR A C   1 
ATOM   3976 O O   . TYR B 1 209 ? -6.127  5.524   37.435 1.00 17.57 ? 209 TYR A O   1 
ATOM   3977 C CB  . TYR B 1 209 ? -6.035  8.763   37.863 1.00 16.58 ? 209 TYR A CB  1 
ATOM   3978 C CG  . TYR B 1 209 ? -6.897  9.699   38.695 1.00 15.20 ? 209 TYR A CG  1 
ATOM   3979 C CD1 . TYR B 1 209 ? -8.204  9.345   39.017 1.00 16.86 ? 209 TYR A CD1 1 
ATOM   3980 C CD2 . TYR B 1 209 ? -6.424  10.933  39.123 1.00 14.78 ? 209 TYR A CD2 1 
ATOM   3981 C CE1 . TYR B 1 209 ? -9.021  10.189  39.769 1.00 19.58 ? 209 TYR A CE1 1 
ATOM   3982 C CE2 . TYR B 1 209 ? -7.224  11.785  39.880 1.00 16.88 ? 209 TYR A CE2 1 
ATOM   3983 C CZ  . TYR B 1 209 ? -8.530  11.400  40.193 1.00 16.97 ? 209 TYR A CZ  1 
ATOM   3984 O OH  . TYR B 1 209 ? -9.326  12.243  40.934 1.00 17.99 ? 209 TYR A OH  1 
ATOM   3985 N N   . ALA B 1 210 ? -4.067  6.372   37.069 1.00 16.31 ? 210 ALA A N   1 
ATOM   3986 C CA  . ALA B 1 210 ? -3.659  5.239   36.238 1.00 15.67 ? 210 ALA A CA  1 
ATOM   3987 C C   . ALA B 1 210 ? -3.773  3.931   37.004 1.00 14.97 ? 210 ALA A C   1 
ATOM   3988 O O   . ALA B 1 210 ? -4.192  2.908   36.449 1.00 16.29 ? 210 ALA A O   1 
ATOM   3989 C CB  . ALA B 1 210 ? -2.222  5.439   35.732 1.00 15.07 ? 210 ALA A CB  1 
ATOM   3990 N N   . ALA B 1 211 ? -3.416  3.947   38.287 1.00 14.14 ? 211 ALA A N   1 
ATOM   3991 C CA  . ALA B 1 211 ? -3.458  2.721   39.073 1.00 17.01 ? 211 ALA A CA  1 
ATOM   3992 C C   . ALA B 1 211 ? -4.889  2.233   39.216 1.00 17.16 ? 211 ALA A C   1 
ATOM   3993 O O   . ALA B 1 211 ? -5.178  1.047   39.009 1.00 17.68 ? 211 ALA A O   1 
ATOM   3994 C CB  . ALA B 1 211 ? -2.833  2.951   40.445 1.00 16.30 ? 211 ALA A CB  1 
ATOM   3995 N N   . VAL B 1 212 ? -5.808  3.149   39.539 1.00 16.97 ? 212 VAL A N   1 
ATOM   3996 C CA  . VAL B 1 212 ? -7.205  2.753   39.690 1.00 16.48 ? 212 VAL A CA  1 
ATOM   3997 C C   . VAL B 1 212 ? -7.733  2.190   38.375 1.00 17.86 ? 212 VAL A C   1 
ATOM   3998 O O   . VAL B 1 212 ? -8.388  1.134   38.352 1.00 18.06 ? 212 VAL A O   1 
ATOM   3999 C CB  . VAL B 1 212 ? -8.046  3.939   40.195 1.00 16.33 ? 212 VAL A CB  1 
ATOM   4000 C CG1 . VAL B 1 212 ? -9.543  3.591   40.160 1.00 18.97 ? 212 VAL A CG1 1 
ATOM   4001 C CG2 . VAL B 1 212 ? -7.626  4.291   41.620 1.00 17.28 ? 212 VAL A CG2 1 
ATOM   4002 N N   . ILE B 1 213 ? -7.432  2.868   37.260 1.00 18.00 ? 213 ILE A N   1 
ATOM   4003 C CA  . ILE B 1 213 ? -7.863  2.407   35.942 1.00 18.13 ? 213 ILE A CA  1 
ATOM   4004 C C   . ILE B 1 213 ? -7.357  0.992   35.670 1.00 19.01 ? 213 ILE A C   1 
ATOM   4005 O O   . ILE B 1 213 ? -8.061  0.179   35.053 1.00 20.90 ? 213 ILE A O   1 
ATOM   4006 C CB  . ILE B 1 213 ? -7.409  3.411   34.862 1.00 17.66 ? 213 ILE A CB  1 
ATOM   4007 C CG1 . ILE B 1 213 ? -8.212  4.713   34.977 1.00 20.19 ? 213 ILE A CG1 1 
ATOM   4008 C CG2 . ILE B 1 213 ? -7.546  2.820   33.467 1.00 23.84 ? 213 ILE A CG2 1 
ATOM   4009 C CD1 . ILE B 1 213 ? -7.538  5.902   34.310 1.00 24.72 ? 213 ILE A CD1 1 
ATOM   4010 N N   . ASN B 1 214 ? -6.168  0.652   36.165 1.00 19.07 ? 214 ASN A N   1 
ATOM   4011 C CA  . ASN B 1 214 ? -5.591  -0.669  35.955 1.00 19.51 ? 214 ASN A CA  1 
ATOM   4012 C C   . ASN B 1 214 ? -5.815  -1.616  37.128 1.00 21.78 ? 214 ASN A C   1 
ATOM   4013 O O   . ASN B 1 214 ? -5.133  -2.639  37.228 1.00 24.86 ? 214 ASN A O   1 
ATOM   4014 C CB  . ASN B 1 214 ? -4.109  -0.540  35.622 1.00 22.06 ? 214 ASN A CB  1 
ATOM   4015 C CG  . ASN B 1 214 ? -3.901  -0.050  34.213 1.00 25.22 ? 214 ASN A CG  1 
ATOM   4016 O OD1 . ASN B 1 214 ? -3.977  -0.834  33.266 1.00 26.20 ? 214 ASN A OD1 1 
ATOM   4017 N ND2 . ASN B 1 214 ? -3.718  1.263   34.053 1.00 21.58 ? 214 ASN A ND2 1 
ATOM   4018 N N   . GLY B 1 215 ? -6.784  -1.319  37.991 1.00 18.80 ? 215 GLY A N   1 
ATOM   4019 C CA  . GLY B 1 215 ? -7.244  -2.280  38.969 1.00 19.88 ? 215 GLY A CA  1 
ATOM   4020 C C   . GLY B 1 215 ? -6.518  -2.286  40.291 1.00 24.83 ? 215 GLY A C   1 
ATOM   4021 O O   . GLY B 1 215 ? -6.730  -3.213  41.077 1.00 20.92 ? 215 GLY A O   1 
ATOM   4022 N N   . ASP B 1 216 ? -5.654  -1.302  40.562 1.00 19.04 ? 216 ASP A N   1 
ATOM   4023 C CA  . ASP B 1 216 ? -5.007  -1.167  41.866 1.00 19.19 ? 216 ASP A CA  1 
ATOM   4024 C C   . ASP B 1 216 ? -5.801  -0.129  42.646 1.00 22.62 ? 216 ASP A C   1 
ATOM   4025 O O   . ASP B 1 216 ? -5.756  1.057   42.309 1.00 26.03 ? 216 ASP A O   1 
ATOM   4026 C CB  . ASP B 1 216 ? -3.554  -0.707  41.750 1.00 24.26 ? 216 ASP A CB  1 
ATOM   4027 C CG  . ASP B 1 216 ? -2.590  -1.841  41.460 1.00 28.68 ? 216 ASP A CG  1 
ATOM   4028 O OD1 . ASP B 1 216 ? -2.962  -3.012  41.696 1.00 31.37 ? 216 ASP A OD1 1 
ATOM   4029 O OD2 . ASP B 1 216 ? -1.500  -1.566  40.899 1.00 25.44 ? 216 ASP A OD2 1 
ATOM   4030 N N   . ARG B 1 217 ? -6.515  -0.563  43.696 1.00 19.86 ? 217 ARG A N   1 
ATOM   4031 C CA  . ARG B 1 217 ? -7.437  0.315   44.421 1.00 20.21 ? 217 ARG A CA  1 
ATOM   4032 C C   . ARG B 1 217 ? -7.185  0.380   45.916 1.00 20.59 ? 217 ARG A C   1 
ATOM   4033 O O   . ARG B 1 217 ? -7.917  1.090   46.610 1.00 19.60 ? 217 ARG A O   1 
ATOM   4034 C CB  . ARG B 1 217 ? -8.896  -0.139  44.228 1.00 25.42 ? 217 ARG A CB  1 
ATOM   4035 C CG  . ARG B 1 217 ? -9.449  0.172   42.872 1.00 28.98 ? 217 ARG A CG  1 
ATOM   4036 C CD  . ARG B 1 217 ? -10.729 -0.619  42.584 1.00 29.31 ? 217 ARG A CD  1 
ATOM   4037 N NE  . ARG B 1 217 ? -11.287 -0.178  41.310 1.00 29.09 ? 217 ARG A NE  1 
ATOM   4038 C CZ  . ARG B 1 217 ? -12.125 0.838   41.166 1.00 28.87 ? 217 ARG A CZ  1 
ATOM   4039 N NH1 . ARG B 1 217 ? -12.551 1.535   42.209 1.00 30.69 ? 217 ARG A NH1 1 
ATOM   4040 N NH2 . ARG B 1 217 ? -12.514 1.187   39.939 1.00 31.54 ? 217 ARG A NH2 1 
ATOM   4041 N N   . TRP B 1 218 ? -6.187  -0.340  46.433 1.00 20.54 ? 218 TRP A N   1 
ATOM   4042 C CA  . TRP B 1 218 ? -6.065  -0.555  47.874 1.00 20.94 ? 218 TRP A CA  1 
ATOM   4043 C C   . TRP B 1 218 ? -5.784  0.715   48.662 1.00 23.63 ? 218 TRP A C   1 
ATOM   4044 O O   . TRP B 1 218 ? -6.074  0.760   49.867 1.00 19.69 ? 218 TRP A O   1 
ATOM   4045 C CB  . TRP B 1 218 ? -4.953  -1.579  48.155 1.00 21.20 ? 218 TRP A CB  1 
ATOM   4046 C CG  . TRP B 1 218 ? -3.546  -1.111  47.774 1.00 22.93 ? 218 TRP A CG  1 
ATOM   4047 C CD1 . TRP B 1 218 ? -2.870  -1.400  46.624 1.00 21.38 ? 218 TRP A CD1 1 
ATOM   4048 C CD2 . TRP B 1 218 ? -2.665  -0.304  48.566 1.00 22.68 ? 218 TRP A CD2 1 
ATOM   4049 N NE1 . TRP B 1 218 ? -1.617  -0.809  46.642 1.00 22.57 ? 218 TRP A NE1 1 
ATOM   4050 C CE2 . TRP B 1 218 ? -1.465  -0.141  47.828 1.00 21.37 ? 218 TRP A CE2 1 
ATOM   4051 C CE3 . TRP B 1 218 ? -2.770  0.299   49.826 1.00 22.45 ? 218 TRP A CE3 1 
ATOM   4052 C CZ2 . TRP B 1 218 ? -0.394  0.605   48.305 1.00 22.32 ? 218 TRP A CZ2 1 
ATOM   4053 C CZ3 . TRP B 1 218 ? -1.700  1.029   50.301 1.00 26.16 ? 218 TRP A CZ3 1 
ATOM   4054 C CH2 . TRP B 1 218 ? -0.525  1.177   49.539 1.00 22.16 ? 218 TRP A CH2 1 
ATOM   4055 N N   . PHE B 1 219 ? -5.200  1.735   48.024 1.00 18.20 ? 219 PHE A N   1 
ATOM   4056 C CA  . PHE B 1 219 ? -4.867  2.986   48.694 1.00 18.05 ? 219 PHE A CA  1 
ATOM   4057 C C   . PHE B 1 219 ? -6.044  3.958   48.773 1.00 19.13 ? 219 PHE A C   1 
ATOM   4058 O O   . PHE B 1 219 ? -5.921  4.989   49.436 1.00 21.55 ? 219 PHE A O   1 
ATOM   4059 C CB  . PHE B 1 219 ? -3.708  3.668   47.955 1.00 18.91 ? 219 PHE A CB  1 
ATOM   4060 C CG  . PHE B 1 219 ? -3.951  3.792   46.483 1.00 19.43 ? 219 PHE A CG  1 
ATOM   4061 C CD1 . PHE B 1 219 ? -4.619  4.889   45.970 1.00 17.42 ? 219 PHE A CD1 1 
ATOM   4062 C CD2 . PHE B 1 219 ? -3.517  2.805   45.608 1.00 16.02 ? 219 PHE A CD2 1 
ATOM   4063 C CE1 . PHE B 1 219 ? -4.867  4.999   44.609 1.00 19.91 ? 219 PHE A CE1 1 
ATOM   4064 C CE2 . PHE B 1 219 ? -3.754  2.906   44.258 1.00 18.67 ? 219 PHE A CE2 1 
ATOM   4065 C CZ  . PHE B 1 219 ? -4.418  3.993   43.747 1.00 16.81 ? 219 PHE A CZ  1 
ATOM   4066 N N   . LEU B 1 220 ? -7.169  3.678   48.119 1.00 19.14 ? 220 LEU A N   1 
ATOM   4067 C CA  . LEU B 1 220 ? -8.314  4.580   48.208 1.00 19.78 ? 220 LEU A CA  1 
ATOM   4068 C C   . LEU B 1 220 ? -8.917  4.528   49.607 1.00 25.53 ? 220 LEU A C   1 
ATOM   4069 O O   . LEU B 1 220 ? -9.249  3.450   50.111 1.00 25.39 ? 220 LEU A O   1 
ATOM   4070 C CB  . LEU B 1 220 ? -9.380  4.209   47.179 1.00 22.56 ? 220 LEU A CB  1 
ATOM   4071 C CG  . LEU B 1 220 ? -9.013  4.326   45.695 1.00 22.51 ? 220 LEU A CG  1 
ATOM   4072 C CD1 . LEU B 1 220 ? -10.102 3.755   44.810 1.00 24.51 ? 220 LEU A CD1 1 
ATOM   4073 C CD2 . LEU B 1 220 ? -8.740  5.791   45.317 1.00 23.54 ? 220 LEU A CD2 1 
ATOM   4074 N N   . ASN B 1 221 ? -9.058  5.685   50.239 1.00 22.08 ? 221 ASN A N   1 
ATOM   4075 C CA  . ASN B 1 221 ? -9.688  5.758   51.546 1.00 23.82 ? 221 ASN A CA  1 
ATOM   4076 C C   . ASN B 1 221 ? -11.031 6.480   51.437 1.00 25.43 ? 221 ASN A C   1 
ATOM   4077 O O   . ASN B 1 221 ? -11.458 6.912   50.360 1.00 24.32 ? 221 ASN A O   1 
ATOM   4078 C CB  . ASN B 1 221 ? -8.724  6.381   52.568 1.00 23.12 ? 221 ASN A CB  1 
ATOM   4079 C CG  . ASN B 1 221 ? -8.452  7.870   52.341 1.00 25.24 ? 221 ASN A CG  1 
ATOM   4080 O OD1 . ASN B 1 221 ? -9.246  8.598   51.747 1.00 22.47 ? 221 ASN A OD1 1 
ATOM   4081 N ND2 . ASN B 1 221 ? -7.297  8.319   52.819 1.00 24.41 ? 221 ASN A ND2 1 
ATOM   4082 N N   . ARG B 1 222 ? -11.713 6.586   52.566 1.00 23.37 ? 222 ARG A N   1 
ATOM   4083 C CA  . ARG B 1 222 ? -13.068 7.129   52.601 1.00 25.64 ? 222 ARG A CA  1 
ATOM   4084 C C   . ARG B 1 222 ? -13.125 8.632   52.869 1.00 28.28 ? 222 ARG A C   1 
ATOM   4085 O O   . ARG B 1 222 ? -14.210 9.149   53.165 1.00 23.67 ? 222 ARG A O   1 
ATOM   4086 C CB  . ARG B 1 222 ? -13.898 6.389   53.654 1.00 34.71 ? 222 ARG A CB  1 
ATOM   4087 C CG  . ARG B 1 222 ? -13.353 6.581   55.066 1.00 40.38 ? 222 ARG A CG  1 
ATOM   4088 C CD  . ARG B 1 222 ? -13.323 5.265   55.825 1.00 42.25 ? 222 ARG A CD  1 
ATOM   4089 N NE  . ARG B 1 222 ? -12.775 4.184   55.010 1.00 49.45 ? 222 ARG A NE  1 
ATOM   4090 C CZ  . ARG B 1 222 ? -11.505 4.062   54.642 1.00 44.89 ? 222 ARG A CZ  1 
ATOM   4091 N NH1 . ARG B 1 222 ? -10.596 4.968   54.972 1.00 36.72 ? 222 ARG A NH1 1 
ATOM   4092 N NH2 . ARG B 1 222 ? -11.140 3.004   53.918 1.00 42.55 ? 222 ARG A NH2 1 
ATOM   4093 N N   . PHE B 1 223 ? -12.009 9.349   52.752 1.00 23.72 ? 223 PHE A N   1 
ATOM   4094 C CA  . PHE B 1 223 ? -11.941 10.755  53.132 1.00 24.38 ? 223 PHE A CA  1 
ATOM   4095 C C   . PHE B 1 223 ? -11.845 11.669  51.917 1.00 20.40 ? 223 PHE A C   1 
ATOM   4096 O O   . PHE B 1 223 ? -11.542 11.242  50.797 1.00 19.95 ? 223 PHE A O   1 
ATOM   4097 C CB  . PHE B 1 223 ? -10.743 11.020  54.059 1.00 23.54 ? 223 PHE A CB  1 
ATOM   4098 C CG  . PHE B 1 223 ? -10.768 10.216  55.327 1.00 30.15 ? 223 PHE A CG  1 
ATOM   4099 C CD1 . PHE B 1 223 ? -11.459 10.677  56.439 1.00 34.46 ? 223 PHE A CD1 1 
ATOM   4100 C CD2 . PHE B 1 223 ? -10.115 8.997   55.408 1.00 28.97 ? 223 PHE A CD2 1 
ATOM   4101 C CE1 . PHE B 1 223 ? -11.494 9.937   57.609 1.00 37.60 ? 223 PHE A CE1 1 
ATOM   4102 C CE2 . PHE B 1 223 ? -10.148 8.251   56.578 1.00 36.31 ? 223 PHE A CE2 1 
ATOM   4103 C CZ  . PHE B 1 223 ? -10.845 8.724   57.680 1.00 40.06 ? 223 PHE A CZ  1 
ATOM   4104 N N   . THR B 1 224 ? -12.101 12.944  52.158 1.00 19.43 ? 224 THR A N   1 
ATOM   4105 C CA  . THR B 1 224 ? -11.748 14.000  51.218 1.00 20.06 ? 224 THR A CA  1 
ATOM   4106 C C   . THR B 1 224 ? -10.867 15.008  51.941 1.00 19.45 ? 224 THR A C   1 
ATOM   4107 O O   . THR B 1 224 ? -10.586 14.875  53.133 1.00 22.87 ? 224 THR A O   1 
ATOM   4108 C CB  . THR B 1 224 ? -12.995 14.650  50.600 1.00 23.72 ? 224 THR A CB  1 
ATOM   4109 O OG1 . THR B 1 224 ? -12.615 15.388  49.424 1.00 22.96 ? 224 THR A OG1 1 
ATOM   4110 C CG2 . THR B 1 224 ? -13.688 15.608  51.571 1.00 21.45 ? 224 THR A CG2 1 
ATOM   4111 N N   . THR B 1 225 ? -10.379 15.994  51.201 1.00 19.80 ? 225 THR A N   1 
ATOM   4112 C CA  . THR B 1 225 ? -9.535  17.017  51.805 1.00 20.03 ? 225 THR A CA  1 
ATOM   4113 C C   . THR B 1 225 ? -9.819  18.342  51.124 1.00 20.46 ? 225 THR A C   1 
ATOM   4114 O O   . THR B 1 225 ? -10.320 18.395  49.994 1.00 22.06 ? 225 THR A O   1 
ATOM   4115 C CB  . THR B 1 225 ? -8.032  16.657  51.715 1.00 19.72 ? 225 THR A CB  1 
ATOM   4116 O OG1 . THR B 1 225 ? -7.243  17.634  52.411 1.00 19.60 ? 225 THR A OG1 1 
ATOM   4117 C CG2 . THR B 1 225 ? -7.548  16.609  50.276 1.00 22.86 ? 225 THR A CG2 1 
ATOM   4118 N N   . THR B 1 226 ? -9.524  19.421  51.835 1.00 24.69 ? 226 THR A N   1 
ATOM   4119 C CA  . THR B 1 226 ? -9.461  20.696  51.144 1.00 25.85 ? 226 THR A CA  1 
ATOM   4120 C C   . THR B 1 226 ? -8.096  20.835  50.495 1.00 23.00 ? 226 THR A C   1 
ATOM   4121 O O   . THR B 1 226 ? -7.131  20.170  50.883 1.00 22.47 ? 226 THR A O   1 
ATOM   4122 C CB  . THR B 1 226 ? -9.668  21.855  52.107 1.00 23.03 ? 226 THR A CB  1 
ATOM   4123 O OG1 . THR B 1 226 ? -8.627  21.828  53.086 1.00 23.72 ? 226 THR A OG1 1 
ATOM   4124 C CG2 . THR B 1 226 ? -11.010 21.693  52.834 1.00 26.70 ? 226 THR A CG2 1 
ATOM   4125 N N   . LEU B 1 227 ? -8.021  21.712  49.494 1.00 23.43 ? 227 LEU A N   1 
ATOM   4126 C CA  . LEU B 1 227 ? -6.751  21.976  48.832 1.00 21.85 ? 227 LEU A CA  1 
ATOM   4127 C C   . LEU B 1 227 ? -5.701  22.460  49.824 1.00 24.68 ? 227 LEU A C   1 
ATOM   4128 O O   . LEU B 1 227 ? -4.564  21.973  49.821 1.00 21.37 ? 227 LEU A O   1 
ATOM   4129 C CB  . LEU B 1 227 ? -6.943  22.988  47.707 1.00 24.00 ? 227 LEU A CB  1 
ATOM   4130 C CG  . LEU B 1 227 ? -5.839  23.100  46.657 1.00 25.15 ? 227 LEU A CG  1 
ATOM   4131 C CD1 . LEU B 1 227 ? -5.289  21.726  46.210 1.00 22.10 ? 227 LEU A CD1 1 
ATOM   4132 C CD2 . LEU B 1 227 ? -6.309  23.926  45.475 1.00 25.17 ? 227 LEU A CD2 1 
ATOM   4133 N N   . ASN B 1 228 ? -6.073  23.411  50.697 1.00 19.62 ? 228 ASN A N   1 
ATOM   4134 C CA  . ASN B 1 228 ? -5.148  23.899  51.717 1.00 22.95 ? 228 ASN A CA  1 
ATOM   4135 C C   . ASN B 1 228 ? -4.640  22.770  52.603 1.00 21.56 ? 228 ASN A C   1 
ATOM   4136 O O   . ASN B 1 228 ? -3.431  22.644  52.824 1.00 20.06 ? 228 ASN A O   1 
ATOM   4137 C CB  . ASN B 1 228 ? -5.816  24.970  52.584 1.00 21.48 ? 228 ASN A CB  1 
ATOM   4138 C CG  . ASN B 1 228 ? -4.907  25.459  53.697 1.00 26.68 ? 228 ASN A CG  1 
ATOM   4139 O OD1 . ASN B 1 228 ? -3.847  26.032  53.447 1.00 29.49 ? 228 ASN A OD1 1 
ATOM   4140 N ND2 . ASN B 1 228 ? -5.301  25.198  54.937 1.00 30.28 ? 228 ASN A ND2 1 
ATOM   4141 N N   . ASP B 1 229 ? -5.551  21.956  53.155 1.00 22.85 ? 229 ASP A N   1 
ATOM   4142 C CA  . ASP B 1 229 ? -5.108  20.920  54.082 1.00 21.54 ? 229 ASP A CA  1 
ATOM   4143 C C   . ASP B 1 229 ? -4.209  19.907  53.383 1.00 19.55 ? 229 ASP A C   1 
ATOM   4144 O O   . ASP B 1 229 ? -3.271  19.385  53.987 1.00 20.83 ? 229 ASP A O   1 
ATOM   4145 C CB  . ASP B 1 229 ? -6.289  20.206  54.740 1.00 29.57 ? 229 ASP A CB  1 
ATOM   4146 C CG  . ASP B 1 229 ? -7.016  21.085  55.747 1.00 31.96 ? 229 ASP A CG  1 
ATOM   4147 O OD1 . ASP B 1 229 ? -6.402  22.063  56.227 1.00 31.14 ? 229 ASP A OD1 1 
ATOM   4148 O OD2 . ASP B 1 229 ? -8.209  20.816  56.023 1.00 30.31 ? 229 ASP A OD2 1 
ATOM   4149 N N   . PHE B 1 230 ? -4.484  19.608  52.116 1.00 18.15 ? 230 PHE A N   1 
ATOM   4150 C CA  . PHE B 1 230 ? -3.588  18.721  51.378 1.00 15.69 ? 230 PHE A CA  1 
ATOM   4151 C C   . PHE B 1 230 ? -2.194  19.325  51.272 1.00 21.27 ? 230 PHE A C   1 
ATOM   4152 O O   . PHE B 1 230 ? -1.188  18.655  51.531 1.00 20.09 ? 230 PHE A O   1 
ATOM   4153 C CB  . PHE B 1 230 ? -4.128  18.441  49.981 1.00 15.88 ? 230 PHE A CB  1 
ATOM   4154 C CG  . PHE B 1 230 ? -3.136  17.708  49.117 1.00 17.85 ? 230 PHE A CG  1 
ATOM   4155 C CD1 . PHE B 1 230 ? -2.993  16.343  49.233 1.00 18.04 ? 230 PHE A CD1 1 
ATOM   4156 C CD2 . PHE B 1 230 ? -2.307  18.404  48.235 1.00 17.94 ? 230 PHE A CD2 1 
ATOM   4157 C CE1 . PHE B 1 230 ? -2.039  15.659  48.453 1.00 18.30 ? 230 PHE A CE1 1 
ATOM   4158 C CE2 . PHE B 1 230 ? -1.360  17.733  47.465 1.00 19.55 ? 230 PHE A CE2 1 
ATOM   4159 C CZ  . PHE B 1 230 ? -1.228  16.365  47.582 1.00 17.42 ? 230 PHE A CZ  1 
ATOM   4160 N N   . ASN B 1 231 ? -2.116  20.589  50.865 1.00 19.57 ? 231 ASN A N   1 
ATOM   4161 C CA  . ASN B 1 231 ? -0.811  21.192  50.635 1.00 19.97 ? 231 ASN A CA  1 
ATOM   4162 C C   . ASN B 1 231 ? -0.003  21.339  51.917 1.00 20.99 ? 231 ASN A C   1 
ATOM   4163 O O   . ASN B 1 231 ? 1.230   21.314  51.862 1.00 22.07 ? 231 ASN A O   1 
ATOM   4164 C CB  . ASN B 1 231 ? -0.970  22.538  49.958 1.00 18.28 ? 231 ASN A CB  1 
ATOM   4165 C CG  . ASN B 1 231 ? -1.245  22.401  48.491 1.00 19.38 ? 231 ASN A CG  1 
ATOM   4166 O OD1 . ASN B 1 231 ? -0.717  21.498  47.841 1.00 22.08 ? 231 ASN A OD1 1 
ATOM   4167 N ND2 . ASN B 1 231 ? -2.043  23.313  47.945 1.00 20.87 ? 231 ASN A ND2 1 
ATOM   4168 N N   . LEU B 1 232 ? -0.666  21.509  53.063 1.00 18.35 ? 232 LEU A N   1 
ATOM   4169 C CA  . LEU B 1 232 ? 0.052   21.507  54.332 1.00 23.12 ? 232 LEU A CA  1 
ATOM   4170 C C   . LEU B 1 232 ? 0.845   20.216  54.498 1.00 26.00 ? 232 LEU A C   1 
ATOM   4171 O O   . LEU B 1 232 ? 2.004   20.236  54.937 1.00 26.77 ? 232 LEU A O   1 
ATOM   4172 C CB  . LEU B 1 232 ? -0.941  21.682  55.477 1.00 22.83 ? 232 LEU A CB  1 
ATOM   4173 C CG  . LEU B 1 232 ? -1.593  23.051  55.663 1.00 28.18 ? 232 LEU A CG  1 
ATOM   4174 C CD1 . LEU B 1 232 ? -2.368  23.083  56.961 1.00 28.40 ? 232 LEU A CD1 1 
ATOM   4175 C CD2 . LEU B 1 232 ? -0.529  24.126  55.673 1.00 26.90 ? 232 LEU A CD2 1 
ATOM   4176 N N   . VAL B 1 233 ? 0.241   19.082  54.135 1.00 20.07 ? 233 VAL A N   1 
ATOM   4177 C CA  . VAL B 1 233 ? 0.937   17.802  54.262 1.00 21.97 ? 233 VAL A CA  1 
ATOM   4178 C C   . VAL B 1 233 ? 1.947   17.630  53.137 1.00 20.28 ? 233 VAL A C   1 
ATOM   4179 O O   . VAL B 1 233 ? 3.067   17.166  53.363 1.00 21.95 ? 233 VAL A O   1 
ATOM   4180 C CB  . VAL B 1 233 ? -0.075  16.646  54.289 1.00 19.43 ? 233 VAL A CB  1 
ATOM   4181 C CG1 . VAL B 1 233 ? 0.645   15.294  54.341 1.00 21.83 ? 233 VAL A CG1 1 
ATOM   4182 C CG2 . VAL B 1 233 ? -1.021  16.782  55.465 1.00 23.44 ? 233 VAL A CG2 1 
ATOM   4183 N N   . ALA B 1 234 ? 1.569   17.998  51.909 1.00 19.39 ? 234 ALA A N   1 
ATOM   4184 C CA  . ALA B 1 234 ? 2.454   17.810  50.765 1.00 25.27 ? 234 ALA A CA  1 
ATOM   4185 C C   . ALA B 1 234 ? 3.781   18.533  50.961 1.00 21.64 ? 234 ALA A C   1 
ATOM   4186 O O   . ALA B 1 234 ? 4.848   17.972  50.689 1.00 21.63 ? 234 ALA A O   1 
ATOM   4187 C CB  . ALA B 1 234 ? 1.764   18.304  49.495 1.00 25.50 ? 234 ALA A CB  1 
ATOM   4188 N N   . MET B 1 235 ? 3.735   19.778  51.445 1.00 21.46 ? 235 MET A N   1 
ATOM   4189 C CA  . MET B 1 235 ? 4.964   20.545  51.614 1.00 22.92 ? 235 MET A CA  1 
ATOM   4190 C C   . MET B 1 235 ? 5.873   19.909  52.664 1.00 23.94 ? 235 MET A C   1 
ATOM   4191 O O   . MET B 1 235 ? 7.100   19.944  52.526 1.00 20.33 ? 235 MET A O   1 
ATOM   4192 C CB  . MET B 1 235 ? 4.623   21.998  51.954 1.00 27.12 ? 235 MET A CB  1 
ATOM   4193 C CG  . MET B 1 235 ? 4.171   22.238  53.372 1.00 31.82 ? 235 MET A CG  1 
ATOM   4194 S SD  . MET B 1 235 ? 3.732   23.975  53.694 1.00 48.73 ? 235 MET A SD  1 
ATOM   4195 C CE  . MET B 1 235 ? 2.487   24.289  52.435 1.00 32.72 ? 235 MET A CE  1 
ATOM   4196 N N   . LYS B 1 236 ? 5.293   19.260  53.670 1.00 22.89 ? 236 LYS A N   1 
ATOM   4197 C CA  . LYS B 1 236 ? 6.088   18.590  54.688 1.00 24.52 ? 236 LYS A CA  1 
ATOM   4198 C C   . LYS B 1 236 ? 6.891   17.418  54.108 1.00 25.53 ? 236 LYS A C   1 
ATOM   4199 O O   . LYS B 1 236 ? 7.907   17.013  54.684 1.00 24.86 ? 236 LYS A O   1 
ATOM   4200 C CB  . LYS B 1 236 ? 5.139   18.173  55.819 1.00 24.84 ? 236 LYS A CB  1 
ATOM   4201 C CG  . LYS B 1 236 ? 5.713   17.256  56.881 1.00 31.55 ? 236 LYS A CG  1 
ATOM   4202 C CD  . LYS B 1 236 ? 4.761   17.195  58.082 1.00 32.24 ? 236 LYS A CD  1 
ATOM   4203 C CE  . LYS B 1 236 ? 4.912   15.875  58.831 1.00 39.24 ? 236 LYS A CE  1 
ATOM   4204 N NZ  . LYS B 1 236 ? 5.251   16.016  60.277 1.00 43.95 ? 236 LYS A NZ  1 
ATOM   4205 N N   . TYR B 1 237 ? 6.503   16.898  52.944 1.00 21.90 ? 237 TYR A N   1 
ATOM   4206 C CA  . TYR B 1 237 ? 7.188   15.765  52.337 1.00 22.05 ? 237 TYR A CA  1 
ATOM   4207 C C   . TYR B 1 237 ? 7.885   16.144  51.036 1.00 22.08 ? 237 TYR A C   1 
ATOM   4208 O O   . TYR B 1 237 ? 8.184   15.276  50.213 1.00 20.46 ? 237 TYR A O   1 
ATOM   4209 C CB  . TYR B 1 237 ? 6.193   14.615  52.149 1.00 23.77 ? 237 TYR A CB  1 
ATOM   4210 C CG  . TYR B 1 237 ? 5.737   14.069  53.484 1.00 26.78 ? 237 TYR A CG  1 
ATOM   4211 C CD1 . TYR B 1 237 ? 6.587   13.286  54.259 1.00 28.14 ? 237 TYR A CD1 1 
ATOM   4212 C CD2 . TYR B 1 237 ? 4.488   14.378  53.998 1.00 24.32 ? 237 TYR A CD2 1 
ATOM   4213 C CE1 . TYR B 1 237 ? 6.181   12.790  55.490 1.00 32.52 ? 237 TYR A CE1 1 
ATOM   4214 C CE2 . TYR B 1 237 ? 4.075   13.899  55.223 1.00 26.17 ? 237 TYR A CE2 1 
ATOM   4215 C CZ  . TYR B 1 237 ? 4.922   13.104  55.970 1.00 31.25 ? 237 TYR A CZ  1 
ATOM   4216 O OH  . TYR B 1 237 ? 4.510   12.621  57.192 1.00 34.06 ? 237 TYR A OH  1 
ATOM   4217 N N   . ASN B 1 238 ? 8.162   17.439  50.845 1.00 20.06 ? 238 ASN A N   1 
ATOM   4218 C CA  . ASN B 1 238 ? 8.894   17.927  49.685 1.00 21.06 ? 238 ASN A CA  1 
ATOM   4219 C C   . ASN B 1 238 ? 8.132   17.730  48.380 1.00 21.51 ? 238 ASN A C   1 
ATOM   4220 O O   . ASN B 1 238 ? 8.734   17.502  47.332 1.00 22.13 ? 238 ASN A O   1 
ATOM   4221 C CB  . ASN B 1 238 ? 10.271  17.276  49.597 1.00 26.16 ? 238 ASN A CB  1 
ATOM   4222 C CG  . ASN B 1 238 ? 11.336  18.265  49.358 1.00 26.38 ? 238 ASN A CG  1 
ATOM   4223 O OD1 . ASN B 1 238 ? 11.397  19.290  50.033 1.00 26.50 ? 238 ASN A OD1 1 
ATOM   4224 N ND2 . ASN B 1 238 ? 12.202  17.981  48.386 1.00 29.61 ? 238 ASN A ND2 1 
ATOM   4225 N N   . TYR B 1 239 ? 6.810   17.823  48.433 1.00 17.10 ? 239 TYR A N   1 
ATOM   4226 C CA  . TYR B 1 239 ? 5.975   17.758  47.251 1.00 17.38 ? 239 TYR A CA  1 
ATOM   4227 C C   . TYR B 1 239 ? 5.698   19.169  46.755 1.00 18.22 ? 239 TYR A C   1 
ATOM   4228 O O   . TYR B 1 239 ? 5.587   20.110  47.546 1.00 18.69 ? 239 TYR A O   1 
ATOM   4229 C CB  . TYR B 1 239 ? 4.652   17.042  47.561 1.00 17.21 ? 239 TYR A CB  1 
ATOM   4230 C CG  . TYR B 1 239 ? 4.675   15.556  47.330 1.00 18.27 ? 239 TYR A CG  1 
ATOM   4231 C CD1 . TYR B 1 239 ? 5.613   14.738  47.960 1.00 19.23 ? 239 TYR A CD1 1 
ATOM   4232 C CD2 . TYR B 1 239 ? 3.780   14.966  46.446 1.00 18.03 ? 239 TYR A CD2 1 
ATOM   4233 C CE1 . TYR B 1 239 ? 5.631   13.365  47.733 1.00 22.11 ? 239 TYR A CE1 1 
ATOM   4234 C CE2 . TYR B 1 239 ? 3.797   13.608  46.225 1.00 20.18 ? 239 TYR A CE2 1 
ATOM   4235 C CZ  . TYR B 1 239 ? 4.726   12.816  46.860 1.00 19.75 ? 239 TYR A CZ  1 
ATOM   4236 O OH  . TYR B 1 239 ? 4.738   11.457  46.625 1.00 19.47 ? 239 TYR A OH  1 
ATOM   4237 N N   . GLU B 1 240 ? 5.592   19.307  45.438 1.00 17.99 ? 240 GLU A N   1 
ATOM   4238 C CA  . GLU B 1 240 ? 5.210   20.586  44.850 1.00 20.59 ? 240 GLU A CA  1 
ATOM   4239 C C   . GLU B 1 240 ? 3.809   20.986  45.313 1.00 21.80 ? 240 GLU A C   1 
ATOM   4240 O O   . GLU B 1 240 ? 2.946   20.123  45.498 1.00 17.09 ? 240 GLU A O   1 
ATOM   4241 C CB  . GLU B 1 240 ? 5.237   20.509  43.318 1.00 20.48 ? 240 GLU A CB  1 
ATOM   4242 C CG  . GLU B 1 240 ? 6.611   20.671  42.709 1.00 22.23 ? 240 GLU A CG  1 
ATOM   4243 C CD  . GLU B 1 240 ? 7.221   22.033  42.972 1.00 22.36 ? 240 GLU A CD  1 
ATOM   4244 O OE1 . GLU B 1 240 ? 6.541   23.059  42.745 1.00 25.79 ? 240 GLU A OE1 1 
ATOM   4245 O OE2 . GLU B 1 240 ? 8.379   22.065  43.421 1.00 25.36 ? 240 GLU A OE2 1 
ATOM   4246 N N   . PRO B 1 241 ? 3.562   22.272  45.548 1.00 20.68 ? 241 PRO A N   1 
ATOM   4247 C CA  . PRO B 1 241 ? 2.193   22.723  45.827 1.00 21.74 ? 241 PRO A CA  1 
ATOM   4248 C C   . PRO B 1 241 ? 1.246   22.306  44.711 1.00 19.23 ? 241 PRO A C   1 
ATOM   4249 O O   . PRO B 1 241 ? 1.610   22.316  43.530 1.00 20.16 ? 241 PRO A O   1 
ATOM   4250 C CB  . PRO B 1 241 ? 2.338   24.247  45.900 1.00 25.10 ? 241 PRO A CB  1 
ATOM   4251 C CG  . PRO B 1 241 ? 3.712   24.451  46.340 1.00 22.30 ? 241 PRO A CG  1 
ATOM   4252 C CD  . PRO B 1 241 ? 4.530   23.370  45.660 1.00 24.99 ? 241 PRO A CD  1 
ATOM   4253 N N   . LEU B 1 242 ? 0.046   21.869  45.094 1.00 20.10 ? 242 LEU A N   1 
ATOM   4254 C CA  . LEU B 1 242 ? -1.005  21.569  44.122 1.00 17.93 ? 242 LEU A CA  1 
ATOM   4255 C C   . LEU B 1 242 ? -1.875  22.810  43.938 1.00 20.01 ? 242 LEU A C   1 
ATOM   4256 O O   . LEU B 1 242 ? -2.367  23.379  44.917 1.00 21.38 ? 242 LEU A O   1 
ATOM   4257 C CB  . LEU B 1 242 ? -1.856  20.380  44.574 1.00 19.64 ? 242 LEU A CB  1 
ATOM   4258 C CG  . LEU B 1 242 ? -2.777  19.747  43.530 1.00 17.05 ? 242 LEU A CG  1 
ATOM   4259 C CD1 . LEU B 1 242 ? -1.963  18.965  42.520 1.00 16.35 ? 242 LEU A CD1 1 
ATOM   4260 C CD2 . LEU B 1 242 ? -3.804  18.841  44.217 1.00 19.41 ? 242 LEU A CD2 1 
ATOM   4261 N N   . THR B 1 243 ? -2.029  23.249  42.695 1.00 18.48 ? 243 THR A N   1 
ATOM   4262 C CA  . THR B 1 243 ? -2.810  24.443  42.393 1.00 20.47 ? 243 THR A CA  1 
ATOM   4263 C C   . THR B 1 243 ? -4.203  24.075  41.909 1.00 19.10 ? 243 THR A C   1 
ATOM   4264 O O   . THR B 1 243 ? -4.505  22.915  41.608 1.00 18.55 ? 243 THR A O   1 
ATOM   4265 C CB  . THR B 1 243 ? -2.109  25.312  41.342 1.00 19.63 ? 243 THR A CB  1 
ATOM   4266 O OG1 . THR B 1 243 ? -2.112  24.642  40.075 1.00 18.33 ? 243 THR A OG1 1 
ATOM   4267 C CG2 . THR B 1 243 ? -0.684  25.664  41.765 1.00 23.68 ? 243 THR A CG2 1 
ATOM   4268 N N   . GLN B 1 244 ? -5.082  25.084  41.856 1.00 18.90 ? 244 GLN A N   1 
ATOM   4269 C CA  . GLN B 1 244 ? -6.406  24.820  41.318 1.00 21.54 ? 244 GLN A CA  1 
ATOM   4270 C C   . GLN B 1 244 ? -6.325  24.463  39.847 1.00 23.12 ? 244 GLN A C   1 
ATOM   4271 O O   . GLN B 1 244 ? -7.124  23.648  39.371 1.00 20.45 ? 244 GLN A O   1 
ATOM   4272 C CB  . GLN B 1 244 ? -7.342  26.013  41.535 1.00 19.77 ? 244 GLN A CB  1 
ATOM   4273 C CG  . GLN B 1 244 ? -8.777  25.731  41.095 1.00 20.62 ? 244 GLN A CG  1 
ATOM   4274 C CD  . GLN B 1 244 ? -9.446  24.683  41.962 1.00 22.16 ? 244 GLN A CD  1 
ATOM   4275 O OE1 . GLN B 1 244 ? -9.346  24.717  43.194 1.00 23.81 ? 244 GLN A OE1 1 
ATOM   4276 N NE2 . GLN B 1 244 ? -10.142 23.743  41.327 1.00 21.95 ? 244 GLN A NE2 1 
ATOM   4277 N N   . ASP B 1 245 ? -5.359  25.038  39.120 1.00 18.72 ? 245 ASP A N   1 
ATOM   4278 C CA  . ASP B 1 245 ? -5.125  24.602  37.745 1.00 22.04 ? 245 ASP A CA  1 
ATOM   4279 C C   . ASP B 1 245 ? -4.837  23.105  37.680 1.00 21.11 ? 245 ASP A C   1 
ATOM   4280 O O   . ASP B 1 245 ? -5.349  22.414  36.795 1.00 20.16 ? 245 ASP A O   1 
ATOM   4281 C CB  . ASP B 1 245 ? -3.975  25.372  37.096 1.00 21.25 ? 245 ASP A CB  1 
ATOM   4282 C CG  . ASP B 1 245 ? -4.373  26.767  36.649 1.00 26.33 ? 245 ASP A CG  1 
ATOM   4283 O OD1 . ASP B 1 245 ? -5.578  27.109  36.698 1.00 30.12 ? 245 ASP A OD1 1 
ATOM   4284 O OD2 . ASP B 1 245 ? -3.476  27.485  36.170 1.00 31.27 ? 245 ASP A OD2 1 
ATOM   4285 N N   . HIS B 1 246 ? -4.025  22.588  38.612 1.00 19.07 ? 246 HIS A N   1 
ATOM   4286 C CA  . HIS B 1 246 ? -3.744  21.153  38.642 1.00 21.43 ? 246 HIS A CA  1 
ATOM   4287 C C   . HIS B 1 246 ? -5.016  20.358  38.891 1.00 19.98 ? 246 HIS A C   1 
ATOM   4288 O O   . HIS B 1 246 ? -5.264  19.338  38.239 1.00 18.75 ? 246 HIS A O   1 
ATOM   4289 C CB  . HIS B 1 246 ? -2.715  20.835  39.728 1.00 16.84 ? 246 HIS A CB  1 
ATOM   4290 C CG  . HIS B 1 246 ? -1.356  21.387  39.456 1.00 20.14 ? 246 HIS A CG  1 
ATOM   4291 N ND1 . HIS B 1 246 ? -0.546  21.897  40.449 1.00 20.54 ? 246 HIS A ND1 1 
ATOM   4292 C CD2 . HIS B 1 246 ? -0.663  21.511  38.299 1.00 18.04 ? 246 HIS A CD2 1 
ATOM   4293 C CE1 . HIS B 1 246 ? 0.593   22.306  39.912 1.00 17.49 ? 246 HIS A CE1 1 
ATOM   4294 N NE2 . HIS B 1 246 ? 0.545   22.085  38.609 1.00 16.39 ? 246 HIS A NE2 1 
ATOM   4295 N N   . VAL B 1 247 ? -5.825  20.799  39.859 1.00 16.85 ? 247 VAL A N   1 
ATOM   4296 C CA  . VAL B 1 247 ? -7.084  20.110  40.148 1.00 18.03 ? 247 VAL A CA  1 
ATOM   4297 C C   . VAL B 1 247 ? -7.935  20.065  38.887 1.00 18.42 ? 247 VAL A C   1 
ATOM   4298 O O   . VAL B 1 247 ? -8.474  19.013  38.508 1.00 17.92 ? 247 VAL A O   1 
ATOM   4299 C CB  . VAL B 1 247 ? -7.808  20.810  41.318 1.00 18.04 ? 247 VAL A CB  1 
ATOM   4300 C CG1 . VAL B 1 247 ? -9.248  20.250  41.541 1.00 18.96 ? 247 VAL A CG1 1 
ATOM   4301 C CG2 . VAL B 1 247 ? -7.002  20.658  42.606 1.00 17.16 ? 247 VAL A CG2 1 
ATOM   4302 N N   . ASP B 1 248 ? -8.011  21.207  38.185 1.00 17.88 ? 248 ASP A N   1 
ATOM   4303 C CA  . ASP B 1 248 ? -8.824  21.300  36.980 1.00 20.16 ? 248 ASP A CA  1 
ATOM   4304 C C   . ASP B 1 248 ? -8.292  20.371  35.900 1.00 20.09 ? 248 ASP A C   1 
ATOM   4305 O O   . ASP B 1 248 ? -9.069  19.705  35.200 1.00 20.81 ? 248 ASP A O   1 
ATOM   4306 C CB  . ASP B 1 248 ? -8.859  22.749  36.495 1.00 21.75 ? 248 ASP A CB  1 
ATOM   4307 C CG  . ASP B 1 248 ? -9.685  23.652  37.400 1.00 21.64 ? 248 ASP A CG  1 
ATOM   4308 O OD1 . ASP B 1 248 ? -10.425 23.146  38.281 1.00 26.47 ? 248 ASP A OD1 1 
ATOM   4309 O OD2 . ASP B 1 248 ? -9.574  24.884  37.248 1.00 23.62 ? 248 ASP A OD2 1 
ATOM   4310 N N   . ILE B 1 249 ? -6.963  20.277  35.788 1.00 17.81 ? 249 ILE A N   1 
ATOM   4311 C CA  . ILE B 1 249 ? -6.333  19.427  34.791 1.00 16.48 ? 249 ILE A CA  1 
ATOM   4312 C C   . ILE B 1 249 ? -6.633  17.953  35.051 1.00 19.51 ? 249 ILE A C   1 
ATOM   4313 O O   . ILE B 1 249 ? -6.786  17.173  34.108 1.00 19.17 ? 249 ILE A O   1 
ATOM   4314 C CB  . ILE B 1 249 ? -4.814  19.723  34.763 1.00 19.47 ? 249 ILE A CB  1 
ATOM   4315 C CG1 . ILE B 1 249 ? -4.556  21.064  34.068 1.00 23.45 ? 249 ILE A CG1 1 
ATOM   4316 C CG2 . ILE B 1 249 ? -4.052  18.644  34.049 1.00 18.55 ? 249 ILE A CG2 1 
ATOM   4317 C CD1 . ILE B 1 249 ? -3.148  21.598  34.261 1.00 24.68 ? 249 ILE A CD1 1 
ATOM   4318 N N   . LEU B 1 250 ? -6.755  17.553  36.315 1.00 16.47 ? 250 LEU A N   1 
ATOM   4319 C CA  . LEU B 1 250 ? -7.069  16.176  36.680 1.00 16.95 ? 250 LEU A CA  1 
ATOM   4320 C C   . LEU B 1 250 ? -8.547  15.829  36.505 1.00 16.37 ? 250 LEU A C   1 
ATOM   4321 O O   . LEU B 1 250 ? -8.932  14.669  36.739 1.00 19.29 ? 250 LEU A O   1 
ATOM   4322 C CB  . LEU B 1 250 ? -6.632  15.929  38.132 1.00 15.92 ? 250 LEU A CB  1 
ATOM   4323 C CG  . LEU B 1 250 ? -5.107  15.862  38.352 1.00 17.77 ? 250 LEU A CG  1 
ATOM   4324 C CD1 . LEU B 1 250 ? -4.805  15.954  39.842 1.00 15.76 ? 250 LEU A CD1 1 
ATOM   4325 C CD2 . LEU B 1 250 ? -4.497  14.557  37.766 1.00 18.29 ? 250 LEU A CD2 1 
ATOM   4326 N N   . GLY B 1 251 ? -9.376  16.792  36.092 1.00 18.71 ? 251 GLY A N   1 
ATOM   4327 C CA  . GLY B 1 251 ? -10.809 16.584  35.964 1.00 21.06 ? 251 GLY A CA  1 
ATOM   4328 C C   . GLY B 1 251 ? -11.199 15.393  35.098 1.00 22.36 ? 251 GLY A C   1 
ATOM   4329 O O   . GLY B 1 251 ? -11.926 14.498  35.547 1.00 22.91 ? 251 GLY A O   1 
ATOM   4330 N N   . PRO B 1 252 ? -10.733 15.356  33.842 1.00 23.22 ? 252 PRO A N   1 
ATOM   4331 C CA  . PRO B 1 252 ? -11.071 14.216  32.965 1.00 20.92 ? 252 PRO A CA  1 
ATOM   4332 C C   . PRO B 1 252 ? -10.767 12.855  33.564 1.00 22.97 ? 252 PRO A C   1 
ATOM   4333 O O   . PRO B 1 252 ? -11.591 11.943  33.432 1.00 22.62 ? 252 PRO A O   1 
ATOM   4334 C CB  . PRO B 1 252 ? -10.219 14.480  31.714 1.00 24.96 ? 252 PRO A CB  1 
ATOM   4335 C CG  . PRO B 1 252 ? -10.058 15.943  31.688 1.00 28.16 ? 252 PRO A CG  1 
ATOM   4336 C CD  . PRO B 1 252 ? -10.000 16.405  33.111 1.00 23.85 ? 252 PRO A CD  1 
ATOM   4337 N N   . LEU B 1 253 ? -9.615  12.686  34.223 1.00 20.00 ? 253 LEU A N   1 
ATOM   4338 C CA  . LEU B 1 253 ? -9.306  11.409  34.870 1.00 21.91 ? 253 LEU A CA  1 
ATOM   4339 C C   . LEU B 1 253 ? -10.261 11.115  36.020 1.00 23.12 ? 253 LEU A C   1 
ATOM   4340 O O   . LEU B 1 253 ? -10.662 9.958   36.229 1.00 21.47 ? 253 LEU A O   1 
ATOM   4341 C CB  . LEU B 1 253 ? -7.848  11.407  35.356 1.00 17.97 ? 253 LEU A CB  1 
ATOM   4342 C CG  . LEU B 1 253 ? -6.783  11.097  34.302 1.00 20.88 ? 253 LEU A CG  1 
ATOM   4343 C CD1 . LEU B 1 253 ? -5.359  11.370  34.800 1.00 19.53 ? 253 LEU A CD1 1 
ATOM   4344 C CD2 . LEU B 1 253 ? -6.888  9.641   33.804 1.00 18.96 ? 253 LEU A CD2 1 
ATOM   4345 N N   . SER B 1 254 ? -10.654 12.141  36.776 1.00 20.17 ? 254 SER A N   1 
ATOM   4346 C CA  . SER B 1 254 ? -11.553 11.865  37.887 1.00 20.25 ? 254 SER A CA  1 
ATOM   4347 C C   . SER B 1 254 ? -12.952 11.510  37.383 1.00 23.57 ? 254 SER A C   1 
ATOM   4348 O O   . SER B 1 254 ? -13.649 10.718  38.022 1.00 24.45 ? 254 SER A O   1 
ATOM   4349 C CB  . SER B 1 254 ? -11.579 13.046  38.853 1.00 23.23 ? 254 SER A CB  1 
ATOM   4350 O OG  . SER B 1 254 ? -12.528 14.005  38.490 1.00 27.57 ? 254 SER A OG  1 
ATOM   4351 N N   . ALA B 1 255 ? -13.369 12.055  36.232 1.00 22.62 ? 255 ALA A N   1 
ATOM   4352 C CA  . ALA B 1 255 ? -14.637 11.628  35.638 1.00 26.58 ? 255 ALA A CA  1 
ATOM   4353 C C   . ALA B 1 255 ? -14.559 10.185  35.148 1.00 30.22 ? 255 ALA A C   1 
ATOM   4354 O O   . ALA B 1 255 ? -15.521 9.416   35.282 1.00 29.30 ? 255 ALA A O   1 
ATOM   4355 C CB  . ALA B 1 255 ? -15.023 12.558  34.487 1.00 22.42 ? 255 ALA A CB  1 
ATOM   4356 N N   . GLN B 1 256 ? -13.415 9.806   34.577 1.00 27.96 ? 256 GLN A N   1 
ATOM   4357 C CA  . GLN B 1 256 ? -13.244 8.466   34.047 1.00 27.05 ? 256 GLN A CA  1 
ATOM   4358 C C   . GLN B 1 256 ? -13.329 7.423   35.153 1.00 29.88 ? 256 GLN A C   1 
ATOM   4359 O O   . GLN B 1 256 ? -13.847 6.324   34.927 1.00 32.76 ? 256 GLN A O   1 
ATOM   4360 C CB  . GLN B 1 256 ? -11.910 8.397   33.295 1.00 28.69 ? 256 GLN A CB  1 
ATOM   4361 C CG  . GLN B 1 256 ? -11.327 7.023   33.093 1.00 35.22 ? 256 GLN A CG  1 
ATOM   4362 C CD  . GLN B 1 256 ? -10.447 6.974   31.850 1.00 38.51 ? 256 GLN A CD  1 
ATOM   4363 O OE1 . GLN B 1 256 ? -10.199 8.004   31.212 1.00 37.59 ? 256 GLN A OE1 1 
ATOM   4364 N NE2 . GLN B 1 256 ? -9.979  5.778   31.497 1.00 41.35 ? 256 GLN A NE2 1 
ATOM   4365 N N   . THR B 1 257 ? -12.884 7.761   36.367 1.00 23.90 ? 257 THR A N   1 
ATOM   4366 C CA  . THR B 1 257 ? -12.833 6.815   37.477 1.00 25.60 ? 257 THR A CA  1 
ATOM   4367 C C   . THR B 1 257 ? -13.942 7.006   38.506 1.00 27.52 ? 257 THR A C   1 
ATOM   4368 O O   . THR B 1 257 ? -14.116 6.132   39.370 1.00 24.21 ? 257 THR A O   1 
ATOM   4369 C CB  . THR B 1 257 ? -11.492 6.924   38.207 1.00 23.10 ? 257 THR A CB  1 
ATOM   4370 O OG1 . THR B 1 257 ? -11.317 8.276   38.661 1.00 21.16 ? 257 THR A OG1 1 
ATOM   4371 C CG2 . THR B 1 257 ? -10.350 6.541   37.291 1.00 22.12 ? 257 THR A CG2 1 
ATOM   4372 N N   . GLY B 1 258 ? -14.666 8.122   38.457 1.00 25.27 ? 258 GLY A N   1 
ATOM   4373 C CA  . GLY B 1 258 ? -15.651 8.425   39.481 1.00 24.21 ? 258 GLY A CA  1 
ATOM   4374 C C   . GLY B 1 258 ? -15.068 8.755   40.836 1.00 24.13 ? 258 GLY A C   1 
ATOM   4375 O O   . GLY B 1 258 ? -15.753 8.615   41.852 1.00 24.84 ? 258 GLY A O   1 
ATOM   4376 N N   . ILE B 1 259 ? -13.815 9.196   40.885 1.00 20.61 ? 259 ILE A N   1 
ATOM   4377 C CA  . ILE B 1 259 ? -13.132 9.521   42.128 1.00 21.43 ? 259 ILE A CA  1 
ATOM   4378 C C   . ILE B 1 259 ? -12.768 10.994  42.043 1.00 22.57 ? 259 ILE A C   1 
ATOM   4379 O O   . ILE B 1 259 ? -11.917 11.366  41.226 1.00 19.74 ? 259 ILE A O   1 
ATOM   4380 C CB  . ILE B 1 259 ? -11.876 8.660   42.327 1.00 20.80 ? 259 ILE A CB  1 
ATOM   4381 C CG1 . ILE B 1 259 ? -12.238 7.183   42.426 1.00 25.88 ? 259 ILE A CG1 1 
ATOM   4382 C CG2 . ILE B 1 259 ? -11.089 9.109   43.547 1.00 20.80 ? 259 ILE A CG2 1 
ATOM   4383 C CD1 . ILE B 1 259 ? -11.055 6.292   42.258 1.00 24.05 ? 259 ILE A CD1 1 
ATOM   4384 N N   . ALA B 1 260 ? -13.417 11.832  42.858 1.00 19.70 ? 260 ALA A N   1 
ATOM   4385 C CA  . ALA B 1 260 ? -13.147 13.268  42.838 1.00 20.65 ? 260 ALA A CA  1 
ATOM   4386 C C   . ALA B 1 260 ? -11.671 13.532  43.096 1.00 18.42 ? 260 ALA A C   1 
ATOM   4387 O O   . ALA B 1 260 ? -11.014 12.807  43.840 1.00 16.84 ? 260 ALA A O   1 
ATOM   4388 C CB  . ALA B 1 260 ? -13.990 13.995  43.893 1.00 20.29 ? 260 ALA A CB  1 
ATOM   4389 N N   . VAL B 1 261 ? -11.152 14.593  42.480 1.00 17.06 ? 261 VAL A N   1 
ATOM   4390 C CA  . VAL B 1 261 ? -9.737  14.914  42.642 1.00 16.49 ? 261 VAL A CA  1 
ATOM   4391 C C   . VAL B 1 261 ? -9.378  15.067  44.117 1.00 15.08 ? 261 VAL A C   1 
ATOM   4392 O O   . VAL B 1 261 ? -8.373  14.518  44.583 1.00 15.45 ? 261 VAL A O   1 
ATOM   4393 C CB  . VAL B 1 261 ? -9.383  16.175  41.835 1.00 18.41 ? 261 VAL A CB  1 
ATOM   4394 C CG1 . VAL B 1 261 ? -7.931  16.589  42.104 1.00 17.54 ? 261 VAL A CG1 1 
ATOM   4395 C CG2 . VAL B 1 261 ? -9.588  15.918  40.346 1.00 20.58 ? 261 VAL A CG2 1 
ATOM   4396 N N   . LEU B 1 262 ? -10.198 15.795  44.886 1.00 16.36 ? 262 LEU A N   1 
ATOM   4397 C CA  . LEU B 1 262 ? -9.832  16.018  46.281 1.00 16.65 ? 262 LEU A CA  1 
ATOM   4398 C C   . LEU B 1 262 ? -9.961  14.752  47.115 1.00 15.52 ? 262 LEU A C   1 
ATOM   4399 O O   . LEU B 1 262 ? -9.305  14.652  48.157 1.00 16.07 ? 262 LEU A O   1 
ATOM   4400 C CB  . LEU B 1 262 ? -10.648 17.187  46.868 1.00 17.45 ? 262 LEU A CB  1 
ATOM   4401 C CG  . LEU B 1 262 ? -10.281 18.563  46.271 1.00 20.55 ? 262 LEU A CG  1 
ATOM   4402 C CD1 . LEU B 1 262 ? -11.224 19.665  46.730 1.00 20.58 ? 262 LEU A CD1 1 
ATOM   4403 C CD2 . LEU B 1 262 ? -8.844  18.941  46.620 1.00 22.16 ? 262 LEU A CD2 1 
ATOM   4404 N N   . ASP B 1 263 ? -10.792 13.788  46.681 1.00 17.52 ? 263 ASP A N   1 
ATOM   4405 C CA  . ASP B 1 263 ? -10.773 12.459  47.285 1.00 17.73 ? 263 ASP A CA  1 
ATOM   4406 C C   . ASP B 1 263 ? -9.443  11.752  47.006 1.00 14.57 ? 263 ASP A C   1 
ATOM   4407 O O   . ASP B 1 263 ? -8.861  11.134  47.904 1.00 16.13 ? 263 ASP A O   1 
ATOM   4408 C CB  . ASP B 1 263 ? -11.949 11.615  46.769 1.00 17.21 ? 263 ASP A CB  1 
ATOM   4409 C CG  . ASP B 1 263 ? -13.311 12.119  47.258 1.00 24.67 ? 263 ASP A CG  1 
ATOM   4410 O OD1 . ASP B 1 263 ? -13.376 13.202  47.872 1.00 22.50 ? 263 ASP A OD1 1 
ATOM   4411 O OD2 . ASP B 1 263 ? -14.320 11.418  47.014 1.00 25.21 ? 263 ASP A OD2 1 
ATOM   4412 N N   . MET B 1 264 ? -8.936  11.838  45.772 1.00 14.19 ? 264 MET A N   1 
ATOM   4413 C CA  . MET B 1 264 ? -7.648  11.206  45.502 1.00 16.32 ? 264 MET A CA  1 
ATOM   4414 C C   . MET B 1 264 ? -6.543  11.891  46.303 1.00 15.99 ? 264 MET A C   1 
ATOM   4415 O O   . MET B 1 264 ? -5.627  11.222  46.798 1.00 16.52 ? 264 MET A O   1 
ATOM   4416 C CB  . MET B 1 264 ? -7.299  11.218  44.007 1.00 13.97 ? 264 MET A CB  1 
ATOM   4417 C CG  . MET B 1 264 ? -6.011  10.435  43.771 1.00 14.11 ? 264 MET A CG  1 
ATOM   4418 S SD  . MET B 1 264 ? -6.398  8.636   43.940 1.00 18.77 ? 264 MET A SD  1 
ATOM   4419 C CE  . MET B 1 264 ? -7.273  8.328   42.426 1.00 16.39 ? 264 MET A CE  1 
ATOM   4420 N N   . CYS B 1 265 ? -6.623  13.220  46.464 1.00 16.23 ? 265 CYS A N   1 
ATOM   4421 C CA  . CYS B 1 265 ? -5.648  13.914  47.309 1.00 16.66 ? 265 CYS A CA  1 
ATOM   4422 C C   . CYS B 1 265 ? -5.702  13.433  48.746 1.00 16.49 ? 265 CYS A C   1 
ATOM   4423 O O   . CYS B 1 265 ? -4.656  13.306  49.395 1.00 14.62 ? 265 CYS A O   1 
ATOM   4424 C CB  . CYS B 1 265 ? -5.806  15.441  47.260 1.00 18.33 ? 265 CYS A CB  1 
ATOM   4425 S SG  . CYS B 1 265 ? -5.704  16.251  45.640 1.00 18.05 ? 265 CYS A SG  1 
ATOM   4426 N N   . ALA B 1 266 ? -6.904  13.130  49.265 1.00 14.10 ? 266 ALA A N   1 
ATOM   4427 C CA  . ALA B 1 266 ? -6.959  12.584  50.616 1.00 14.92 ? 266 ALA A CA  1 
ATOM   4428 C C   . ALA B 1 266 ? -6.304  11.199  50.695 1.00 15.66 ? 266 ALA A C   1 
ATOM   4429 O O   . ALA B 1 266 ? -5.669  10.869  51.704 1.00 17.57 ? 266 ALA A O   1 
ATOM   4430 C CB  . ALA B 1 266 ? -8.412  12.529  51.108 1.00 17.09 ? 266 ALA A CB  1 
ATOM   4431 N N   . SER B 1 267 ? -6.415  10.387  49.639 1.00 15.34 ? 267 SER A N   1 
ATOM   4432 C CA  . SER B 1 267 ? -5.701  9.117   49.640 1.00 16.79 ? 267 SER A CA  1 
ATOM   4433 C C   . SER B 1 267 ? -4.199  9.331   49.524 1.00 16.76 ? 267 SER A C   1 
ATOM   4434 O O   . SER B 1 267 ? -3.425  8.644   50.195 1.00 16.32 ? 267 SER A O   1 
ATOM   4435 C CB  . SER B 1 267 ? -6.196  8.208   48.513 1.00 20.77 ? 267 SER A CB  1 
ATOM   4436 O OG  . SER B 1 267 ? -7.579  7.912   48.690 1.00 20.64 ? 267 SER A OG  1 
ATOM   4437 N N   . LEU B 1 268 ? -3.767  10.280  48.688 1.00 14.78 ? 268 LEU A N   1 
ATOM   4438 C CA  . LEU B 1 268 ? -2.334  10.581  48.630 1.00 16.19 ? 268 LEU A CA  1 
ATOM   4439 C C   . LEU B 1 268 ? -1.836  11.108  49.970 1.00 15.68 ? 268 LEU A C   1 
ATOM   4440 O O   . LEU B 1 268 ? -0.747  10.749  50.423 1.00 14.45 ? 268 LEU A O   1 
ATOM   4441 C CB  . LEU B 1 268 ? -2.038  11.588  47.517 1.00 13.93 ? 268 LEU A CB  1 
ATOM   4442 C CG  . LEU B 1 268 ? -0.593  12.074  47.352 1.00 12.15 ? 268 LEU A CG  1 
ATOM   4443 C CD1 . LEU B 1 268 ? 0.371   10.868  47.187 1.00 13.32 ? 268 LEU A CD1 1 
ATOM   4444 C CD2 . LEU B 1 268 ? -0.492  12.977  46.148 1.00 14.45 ? 268 LEU A CD2 1 
ATOM   4445 N N   . LYS B 1 269 ? -2.631  11.947  50.637 1.00 15.83 ? 269 LYS A N   1 
ATOM   4446 C CA  . LYS B 1 269 ? -2.187  12.470  51.922 1.00 15.99 ? 269 LYS A CA  1 
ATOM   4447 C C   . LYS B 1 269 ? -1.924  11.331  52.905 1.00 16.39 ? 269 LYS A C   1 
ATOM   4448 O O   . LYS B 1 269 ? -0.949  11.372  53.661 1.00 18.70 ? 269 LYS A O   1 
ATOM   4449 C CB  . LYS B 1 269 ? -3.221  13.457  52.481 1.00 19.59 ? 269 LYS A CB  1 
ATOM   4450 C CG  . LYS B 1 269 ? -2.921  13.921  53.920 1.00 23.03 ? 269 LYS A CG  1 
ATOM   4451 C CD  . LYS B 1 269 ? -4.149  14.477  54.651 1.00 24.71 ? 269 LYS A CD  1 
ATOM   4452 C CE  . LYS B 1 269 ? -4.851  15.506  53.808 1.00 24.83 ? 269 LYS A CE  1 
ATOM   4453 N NZ  . LYS B 1 269 ? -5.945  16.223  54.545 1.00 29.77 ? 269 LYS A NZ  1 
ATOM   4454 N N   . GLU B 1 270 ? -2.786  10.311  52.910 1.00 17.20 ? 270 GLU A N   1 
ATOM   4455 C CA  . GLU B 1 270 ? -2.573  9.169   53.801 1.00 18.56 ? 270 GLU A CA  1 
ATOM   4456 C C   . GLU B 1 270 ? -1.320  8.396   53.426 1.00 18.90 ? 270 GLU A C   1 
ATOM   4457 O O   . GLU B 1 270 ? -0.578  7.956   54.310 1.00 20.56 ? 270 GLU A O   1 
ATOM   4458 C CB  . GLU B 1 270 ? -3.784  8.241   53.802 1.00 20.38 ? 270 GLU A CB  1 
ATOM   4459 C CG  . GLU B 1 270 ? -3.604  7.010   54.728 1.00 25.57 ? 270 GLU A CG  1 
ATOM   4460 C CD  . GLU B 1 270 ? -4.859  6.138   54.839 1.00 27.42 ? 270 GLU A CD  1 
ATOM   4461 O OE1 . GLU B 1 270 ? -5.976  6.689   54.816 1.00 27.13 ? 270 GLU A OE1 1 
ATOM   4462 O OE2 . GLU B 1 270 ? -4.726  4.904   54.987 1.00 31.18 ? 270 GLU A OE2 1 
ATOM   4463 N N   . LEU B 1 271 ? -1.064  8.238   52.124 1.00 18.49 ? 271 LEU A N   1 
ATOM   4464 C CA  . LEU B 1 271 ? 0.157   7.562   51.674 1.00 17.16 ? 271 LEU A CA  1 
ATOM   4465 C C   . LEU B 1 271 ? 1.403   8.309   52.123 1.00 20.42 ? 271 LEU A C   1 
ATOM   4466 O O   . LEU B 1 271 ? 2.404   7.690   52.500 1.00 21.09 ? 271 LEU A O   1 
ATOM   4467 C CB  . LEU B 1 271 ? 0.144   7.423   50.153 1.00 15.84 ? 271 LEU A CB  1 
ATOM   4468 C CG  . LEU B 1 271 ? -0.724  6.317   49.559 1.00 17.39 ? 271 LEU A CG  1 
ATOM   4469 C CD1 . LEU B 1 271 ? -0.730  6.420   48.046 1.00 20.89 ? 271 LEU A CD1 1 
ATOM   4470 C CD2 . LEU B 1 271 ? -0.266  4.915   49.978 1.00 20.41 ? 271 LEU A CD2 1 
ATOM   4471 N N   . LEU B 1 272 ? 1.373   9.645   52.073 1.00 17.99 ? 272 LEU A N   1 
ATOM   4472 C CA  . LEU B 1 272 ? 2.538   10.416  52.489 1.00 21.09 ? 272 LEU A CA  1 
ATOM   4473 C C   . LEU B 1 272 ? 2.760   10.300  53.990 1.00 24.18 ? 272 LEU A C   1 
ATOM   4474 O O   . LEU B 1 272 ? 3.903   10.217  54.453 1.00 25.35 ? 272 LEU A O   1 
ATOM   4475 C CB  . LEU B 1 272 ? 2.362   11.878  52.092 1.00 20.30 ? 272 LEU A CB  1 
ATOM   4476 C CG  . LEU B 1 272 ? 2.370   12.081  50.577 1.00 18.88 ? 272 LEU A CG  1 
ATOM   4477 C CD1 . LEU B 1 272 ? 2.266   13.565  50.211 1.00 21.27 ? 272 LEU A CD1 1 
ATOM   4478 C CD2 . LEU B 1 272 ? 3.584   11.415  49.933 1.00 21.84 ? 272 LEU A CD2 1 
ATOM   4479 N N   . GLN B 1 273 ? 1.681   10.291  54.764 1.00 21.63 ? 273 GLN A N   1 
ATOM   4480 C CA  . GLN B 1 273 ? 1.823   10.262  56.214 1.00 25.64 ? 273 GLN A CA  1 
ATOM   4481 C C   . GLN B 1 273 ? 2.188   8.874   56.727 1.00 24.13 ? 273 GLN A C   1 
ATOM   4482 O O   . GLN B 1 273 ? 2.960   8.751   57.682 1.00 24.81 ? 273 GLN A O   1 
ATOM   4483 C CB  . GLN B 1 273 ? 0.531   10.742  56.877 1.00 23.29 ? 273 GLN A CB  1 
ATOM   4484 C CG  . GLN B 1 273 ? 0.238   12.221  56.613 1.00 25.63 ? 273 GLN A CG  1 
ATOM   4485 C CD  . GLN B 1 273 ? -1.121  12.645  57.127 1.00 23.25 ? 273 GLN A CD  1 
ATOM   4486 O OE1 . GLN B 1 273 ? -2.068  11.852  57.159 1.00 27.09 ? 273 GLN A OE1 1 
ATOM   4487 N NE2 . GLN B 1 273 ? -1.227  13.902  57.535 1.00 30.42 ? 273 GLN A NE2 1 
ATOM   4488 N N   . ASN B 1 274 ? 1.645   7.825   56.119 1.00 24.09 ? 274 ASN A N   1 
ATOM   4489 C CA  . ASN B 1 274 ? 1.835   6.478   56.633 1.00 25.44 ? 274 ASN A CA  1 
ATOM   4490 C C   . ASN B 1 274 ? 2.786   5.634   55.800 1.00 27.67 ? 274 ASN A C   1 
ATOM   4491 O O   . ASN B 1 274 ? 3.191   4.558   56.255 1.00 30.43 ? 274 ASN A O   1 
ATOM   4492 C CB  . ASN B 1 274 ? 0.489   5.745   56.734 1.00 26.70 ? 274 ASN A CB  1 
ATOM   4493 C CG  . ASN B 1 274 ? -0.509  6.474   57.614 1.00 31.51 ? 274 ASN A CG  1 
ATOM   4494 O OD1 . ASN B 1 274 ? -0.139  7.347   58.400 1.00 34.58 ? 274 ASN A OD1 1 
ATOM   4495 N ND2 . ASN B 1 274 ? -1.781  6.105   57.499 1.00 30.31 ? 274 ASN A ND2 1 
ATOM   4496 N N   . GLY B 1 275 ? 3.142   6.069   54.606 1.00 26.47 ? 275 GLY A N   1 
ATOM   4497 C CA  . GLY B 1 275 ? 3.915   5.220   53.726 1.00 26.74 ? 275 GLY A CA  1 
ATOM   4498 C C   . GLY B 1 275 ? 3.065   4.149   53.073 1.00 29.64 ? 275 GLY A C   1 
ATOM   4499 O O   . GLY B 1 275 ? 1.844   4.085   53.211 1.00 25.35 ? 275 GLY A O   1 
ATOM   4500 N N   . MET B 1 276 ? 3.752   3.268   52.356 1.00 26.49 ? 276 MET A N   1 
ATOM   4501 C CA  . MET B 1 276 ? 3.109   2.283   51.504 1.00 31.19 ? 276 MET A CA  1 
ATOM   4502 C C   . MET B 1 276 ? 3.010   0.920   52.179 1.00 29.41 ? 276 MET A C   1 
ATOM   4503 O O   . MET B 1 276 ? 2.354   0.016   51.644 1.00 29.74 ? 276 MET A O   1 
ATOM   4504 C CB  . MET B 1 276 ? 3.908   2.215   50.208 1.00 30.34 ? 276 MET A CB  1 
ATOM   4505 C CG  . MET B 1 276 ? 3.434   3.283   49.230 1.00 28.59 ? 276 MET A CG  1 
ATOM   4506 S SD  . MET B 1 276 ? 4.407   3.329   47.733 1.00 28.52 ? 276 MET A SD  1 
ATOM   4507 C CE  . MET B 1 276 ? 3.584   2.134   46.706 1.00 21.48 ? 276 MET A CE  1 
ATOM   4508 N N   . ASN B 1 277 ? 3.657   0.763   53.339 1.00 32.18 ? 277 ASN A N   1 
ATOM   4509 C CA  . ASN B 1 277 ? 3.522   -0.411  54.205 1.00 32.87 ? 277 ASN A CA  1 
ATOM   4510 C C   . ASN B 1 277 ? 4.034   -1.660  53.476 1.00 33.89 ? 277 ASN A C   1 
ATOM   4511 O O   . ASN B 1 277 ? 3.644   -2.791  53.753 1.00 34.89 ? 277 ASN A O   1 
ATOM   4512 C CB  . ASN B 1 277 ? 2.065   -0.480  54.736 1.00 35.11 ? 277 ASN A CB  1 
ATOM   4513 C CG  . ASN B 1 277 ? 1.638   -1.842  55.320 1.00 44.08 ? 277 ASN A CG  1 
ATOM   4514 O OD1 . ASN B 1 277 ? 1.381   -2.806  54.592 1.00 45.79 ? 277 ASN A OD1 1 
ATOM   4515 N ND2 . ASN B 1 277 ? 1.593   -1.922  56.650 1.00 43.23 ? 277 ASN A ND2 1 
ATOM   4516 N N   . GLY B 1 278 ? 4.991   -1.458  52.571 1.00 32.93 ? 278 GLY A N   1 
ATOM   4517 C CA  . GLY B 1 278 ? 5.592   -2.546  51.829 1.00 30.68 ? 278 GLY A CA  1 
ATOM   4518 C C   . GLY B 1 278 ? 4.807   -3.016  50.622 1.00 25.90 ? 278 GLY A C   1 
ATOM   4519 O O   . GLY B 1 278 ? 5.214   -3.993  49.979 1.00 28.12 ? 278 GLY A O   1 
ATOM   4520 N N   . ARG B 1 279 ? 3.701   -2.361  50.293 1.00 26.79 ? 279 ARG A N   1 
ATOM   4521 C CA  . ARG B 1 279 ? 2.883   -2.747  49.154 1.00 23.98 ? 279 ARG A CA  1 
ATOM   4522 C C   . ARG B 1 279 ? 3.276   -1.934  47.924 1.00 24.93 ? 279 ARG A C   1 
ATOM   4523 O O   . ARG B 1 279 ? 3.890   -0.869  48.030 1.00 27.42 ? 279 ARG A O   1 
ATOM   4524 C CB  . ARG B 1 279 ? 1.398   -2.572  49.484 1.00 27.02 ? 279 ARG A CB  1 
ATOM   4525 C CG  . ARG B 1 279 ? 0.477   -3.253  48.492 1.00 30.12 ? 279 ARG A CG  1 
ATOM   4526 C CD  . ARG B 1 279 ? -0.836  -3.665  49.152 1.00 30.17 ? 279 ARG A CD  1 
ATOM   4527 N NE  . ARG B 1 279 ? -1.719  -4.354  48.217 1.00 30.54 ? 279 ARG A NE  1 
ATOM   4528 C CZ  . ARG B 1 279 ? -3.023  -4.490  48.403 1.00 32.88 ? 279 ARG A CZ  1 
ATOM   4529 N NH1 . ARG B 1 279 ? -3.603  -4.080  49.518 1.00 29.74 ? 279 ARG A NH1 1 
ATOM   4530 N NH2 . ARG B 1 279 ? -3.760  -5.063  47.452 1.00 35.32 ? 279 ARG A NH2 1 
ATOM   4531 N N   . THR B 1 280 ? 2.951   -2.466  46.747 1.00 24.78 ? 280 THR A N   1 
ATOM   4532 C CA  . THR B 1 280 ? 3.246   -1.786  45.494 1.00 20.62 ? 280 THR A CA  1 
ATOM   4533 C C   . THR B 1 280 ? 1.989   -1.175  44.877 1.00 22.88 ? 280 THR A C   1 
ATOM   4534 O O   . THR B 1 280 ? 0.849   -1.564  45.165 1.00 20.48 ? 280 THR A O   1 
ATOM   4535 C CB  . THR B 1 280 ? 3.899   -2.721  44.467 1.00 19.26 ? 280 THR A CB  1 
ATOM   4536 O OG1 . THR B 1 280 ? 3.045   -3.845  44.203 1.00 23.46 ? 280 THR A OG1 1 
ATOM   4537 C CG2 . THR B 1 280 ? 5.252   -3.199  44.965 1.00 21.21 ? 280 THR A CG2 1 
ATOM   4538 N N   . ILE B 1 281 ? 2.222   -0.191  44.018 1.00 17.08 ? 281 ILE A N   1 
ATOM   4539 C CA  . ILE B 1 281 ? 1.196   0.384   43.155 1.00 18.34 ? 281 ILE A CA  1 
ATOM   4540 C C   . ILE B 1 281 ? 1.742   0.347   41.732 1.00 21.10 ? 281 ILE A C   1 
ATOM   4541 O O   . ILE B 1 281 ? 2.848   0.835   41.486 1.00 17.93 ? 281 ILE A O   1 
ATOM   4542 C CB  . ILE B 1 281 ? 0.842   1.832   43.565 1.00 18.71 ? 281 ILE A CB  1 
ATOM   4543 C CG1 . ILE B 1 281 ? 0.227   1.883   44.963 1.00 22.75 ? 281 ILE A CG1 1 
ATOM   4544 C CG2 . ILE B 1 281 ? -0.113  2.455   42.589 1.00 19.19 ? 281 ILE A CG2 1 
ATOM   4545 C CD1 . ILE B 1 281 ? 0.207   3.285   45.543 1.00 22.42 ? 281 ILE A CD1 1 
ATOM   4546 N N   . LEU B 1 282 ? 0.998   -0.267  40.803 1.00 19.65 ? 282 LEU A N   1 
ATOM   4547 C CA  . LEU B 1 282 ? 1.447   -0.383  39.409 1.00 18.41 ? 282 LEU A CA  1 
ATOM   4548 C C   . LEU B 1 282 ? 2.880   -0.894  39.330 1.00 22.04 ? 282 LEU A C   1 
ATOM   4549 O O   . LEU B 1 282 ? 3.709   -0.377  38.570 1.00 23.57 ? 282 LEU A O   1 
ATOM   4550 C CB  . LEU B 1 282 ? 1.323   0.945   38.669 1.00 19.12 ? 282 LEU A CB  1 
ATOM   4551 C CG  . LEU B 1 282 ? -0.105  1.362   38.355 1.00 18.65 ? 282 LEU A CG  1 
ATOM   4552 C CD1 . LEU B 1 282 ? -0.072  2.797   37.836 1.00 18.84 ? 282 LEU A CD1 1 
ATOM   4553 C CD2 . LEU B 1 282 ? -0.751  0.426   37.345 1.00 19.04 ? 282 LEU A CD2 1 
ATOM   4554 N N   . GLY B 1 283 ? 3.186   -1.884  40.164 1.00 24.52 ? 283 GLY A N   1 
ATOM   4555 C CA  . GLY B 1 283 ? 4.489   -2.507  40.144 1.00 22.97 ? 283 GLY A CA  1 
ATOM   4556 C C   . GLY B 1 283 ? 5.627   -1.661  40.655 1.00 24.92 ? 283 GLY A C   1 
ATOM   4557 O O   . GLY B 1 283 ? 6.788   -2.003  40.412 1.00 23.50 ? 283 GLY A O   1 
ATOM   4558 N N   . SER B 1 284 ? 5.343   -0.558  41.347 1.00 18.70 ? 284 SER A N   1 
ATOM   4559 C CA  . SER B 1 284 ? 6.375   0.276   41.946 1.00 19.06 ? 284 SER A CA  1 
ATOM   4560 C C   . SER B 1 284 ? 6.201   0.313   43.457 1.00 21.65 ? 284 SER A C   1 
ATOM   4561 O O   . SER B 1 284 ? 5.072   0.352   43.963 1.00 19.38 ? 284 SER A O   1 
ATOM   4562 C CB  . SER B 1 284 ? 6.336   1.709   41.389 1.00 21.51 ? 284 SER A CB  1 
ATOM   4563 O OG  . SER B 1 284 ? 7.419   2.454   41.924 1.00 25.41 ? 284 SER A OG  1 
ATOM   4564 N N   . ALA B 1 285 ? 7.323   0.319   44.172 1.00 18.47 ? 285 ALA A N   1 
ATOM   4565 C CA  . ALA B 1 285 ? 7.334   0.436   45.622 1.00 17.40 ? 285 ALA A CA  1 
ATOM   4566 C C   . ALA B 1 285 ? 7.543   1.876   46.084 1.00 20.07 ? 285 ALA A C   1 
ATOM   4567 O O   . ALA B 1 285 ? 7.785   2.115   47.271 1.00 22.72 ? 285 ALA A O   1 
ATOM   4568 C CB  . ALA B 1 285 ? 8.409   -0.472  46.214 1.00 24.88 ? 285 ALA A CB  1 
ATOM   4569 N N   . LEU B 1 286 ? 7.459   2.838   45.178 1.00 19.24 ? 286 LEU A N   1 
ATOM   4570 C CA  . LEU B 1 286 ? 7.420   4.245   45.560 1.00 21.33 ? 286 LEU A CA  1 
ATOM   4571 C C   . LEU B 1 286 ? 6.390   4.944   44.683 1.00 21.51 ? 286 LEU A C   1 
ATOM   4572 O O   . LEU B 1 286 ? 5.853   4.365   43.735 1.00 19.42 ? 286 LEU A O   1 
ATOM   4573 C CB  . LEU B 1 286 ? 8.794   4.905   45.454 1.00 24.02 ? 286 LEU A CB  1 
ATOM   4574 C CG  . LEU B 1 286 ? 9.663   4.581   44.244 1.00 24.95 ? 286 LEU A CG  1 
ATOM   4575 C CD1 . LEU B 1 286 ? 9.150   5.334   43.019 1.00 27.86 ? 286 LEU A CD1 1 
ATOM   4576 C CD2 . LEU B 1 286 ? 11.112  4.948   44.534 1.00 29.15 ? 286 LEU A CD2 1 
ATOM   4577 N N   . LEU B 1 287 ? 6.108   6.203   44.997 1.00 20.82 ? 287 LEU A N   1 
ATOM   4578 C CA  . LEU B 1 287 ? 5.130   6.965   44.236 1.00 21.28 ? 287 LEU A CA  1 
ATOM   4579 C C   . LEU B 1 287 ? 5.815   7.604   43.033 1.00 18.15 ? 287 LEU A C   1 
ATOM   4580 O O   . LEU B 1 287 ? 6.750   8.395   43.194 1.00 19.11 ? 287 LEU A O   1 
ATOM   4581 C CB  . LEU B 1 287 ? 4.490   8.020   45.130 1.00 17.49 ? 287 LEU A CB  1 
ATOM   4582 C CG  . LEU B 1 287 ? 3.865   7.428   46.393 1.00 19.42 ? 287 LEU A CG  1 
ATOM   4583 C CD1 . LEU B 1 287 ? 3.281   8.541   47.256 1.00 21.97 ? 287 LEU A CD1 1 
ATOM   4584 C CD2 . LEU B 1 287 ? 2.807   6.392   46.034 1.00 21.99 ? 287 LEU A CD2 1 
ATOM   4585 N N   . GLU B 1 288 ? 5.347   7.267   41.838 1.00 17.75 ? 288 GLU A N   1 
ATOM   4586 C CA  . GLU B 1 288 ? 5.957   7.717   40.593 1.00 18.57 ? 288 GLU A CA  1 
ATOM   4587 C C   . GLU B 1 288 ? 5.416   9.062   40.131 1.00 16.08 ? 288 GLU A C   1 
ATOM   4588 O O   . GLU B 1 288 ? 4.206   9.310   40.168 1.00 15.81 ? 288 GLU A O   1 
ATOM   4589 C CB  . GLU B 1 288 ? 5.762   6.675   39.494 1.00 22.75 ? 288 GLU A CB  1 
ATOM   4590 C CG  . GLU B 1 288 ? 6.242   5.300   39.887 1.00 21.95 ? 288 GLU A CG  1 
ATOM   4591 C CD  . GLU B 1 288 ? 7.722   5.171   39.609 1.00 28.86 ? 288 GLU A CD  1 
ATOM   4592 O OE1 . GLU B 1 288 ? 8.264   6.084   38.944 1.00 28.75 ? 288 GLU A OE1 1 
ATOM   4593 O OE2 . GLU B 1 288 ? 8.341   4.175   40.041 1.00 31.94 ? 288 GLU A OE2 1 
ATOM   4594 N N   . ASP B 1 289 ? 6.332   9.936   39.679 1.00 16.92 ? 289 ASP A N   1 
ATOM   4595 C CA  . ASP B 1 289 ? 5.943   11.302  39.352 1.00 14.24 ? 289 ASP A CA  1 
ATOM   4596 C C   . ASP B 1 289 ? 6.341   11.754  37.948 1.00 16.68 ? 289 ASP A C   1 
ATOM   4597 O O   . ASP B 1 289 ? 6.286   12.949  37.668 1.00 15.73 ? 289 ASP A O   1 
ATOM   4598 C CB  . ASP B 1 289 ? 6.469   12.286  40.419 1.00 15.93 ? 289 ASP A CB  1 
ATOM   4599 C CG  . ASP B 1 289 ? 7.960   12.605  40.293 1.00 18.57 ? 289 ASP A CG  1 
ATOM   4600 O OD1 . ASP B 1 289 ? 8.724   11.836  39.661 1.00 16.98 ? 289 ASP A OD1 1 
ATOM   4601 O OD2 . ASP B 1 289 ? 8.371   13.630  40.889 1.00 18.03 ? 289 ASP A OD2 1 
ATOM   4602 N N   . GLU B 1 290 ? 6.693   10.844  37.032 1.00 16.43 ? 290 GLU A N   1 
ATOM   4603 C CA  . GLU B 1 290 ? 7.037   11.249  35.669 1.00 18.39 ? 290 GLU A CA  1 
ATOM   4604 C C   . GLU B 1 290 ? 6.025   10.792  34.617 1.00 20.16 ? 290 GLU A C   1 
ATOM   4605 O O   . GLU B 1 290 ? 6.388   10.580  33.453 1.00 18.39 ? 290 GLU A O   1 
ATOM   4606 C CB  . GLU B 1 290 ? 8.447   10.774  35.322 1.00 19.85 ? 290 GLU A CB  1 
ATOM   4607 C CG  . GLU B 1 290 ? 9.501   11.400  36.238 1.00 19.90 ? 290 GLU A CG  1 
ATOM   4608 C CD  . GLU B 1 290 ? 10.827  11.648  35.541 1.00 23.45 ? 290 GLU A CD  1 
ATOM   4609 O OE1 . GLU B 1 290 ? 11.048  11.076  34.447 1.00 27.26 ? 290 GLU A OE1 1 
ATOM   4610 O OE2 . GLU B 1 290 ? 11.651  12.399  36.096 1.00 24.10 ? 290 GLU A OE2 1 
ATOM   4611 N N   . PHE B 1 291 ? 4.747   10.676  35.002 1.00 18.49 ? 291 PHE A N   1 
ATOM   4612 C CA  . PHE B 1 291 ? 3.620   10.527  34.082 1.00 17.84 ? 291 PHE A CA  1 
ATOM   4613 C C   . PHE B 1 291 ? 2.716   11.751  34.242 1.00 16.38 ? 291 PHE A C   1 
ATOM   4614 O O   . PHE B 1 291 ? 2.176   11.981  35.329 1.00 17.23 ? 291 PHE A O   1 
ATOM   4615 C CB  . PHE B 1 291 ? 2.813   9.258   34.399 1.00 18.32 ? 291 PHE A CB  1 
ATOM   4616 C CG  . PHE B 1 291 ? 3.552   7.971   34.192 1.00 20.06 ? 291 PHE A CG  1 
ATOM   4617 C CD1 . PHE B 1 291 ? 3.610   7.370   32.941 1.00 21.33 ? 291 PHE A CD1 1 
ATOM   4618 C CD2 . PHE B 1 291 ? 4.182   7.347   35.259 1.00 22.28 ? 291 PHE A CD2 1 
ATOM   4619 C CE1 . PHE B 1 291 ? 4.292   6.153   32.761 1.00 22.52 ? 291 PHE A CE1 1 
ATOM   4620 C CE2 . PHE B 1 291 ? 4.869   6.142   35.080 1.00 24.33 ? 291 PHE A CE2 1 
ATOM   4621 C CZ  . PHE B 1 291 ? 4.914   5.551   33.824 1.00 22.75 ? 291 PHE A CZ  1 
ATOM   4622 N N   . THR B 1 292 ? 2.528   12.529  33.173 1.00 17.32 ? 292 THR A N   1 
ATOM   4623 C CA  . THR B 1 292 ? 1.582   13.639  33.248 1.00 17.55 ? 292 THR A CA  1 
ATOM   4624 C C   . THR B 1 292 ? 0.147   13.124  33.172 1.00 21.34 ? 292 THR A C   1 
ATOM   4625 O O   . THR B 1 292 ? -0.087  11.980  32.791 1.00 16.68 ? 292 THR A O   1 
ATOM   4626 C CB  . THR B 1 292 ? 1.797   14.624  32.108 1.00 17.88 ? 292 THR A CB  1 
ATOM   4627 O OG1 . THR B 1 292 ? 1.520   13.962  30.870 1.00 19.89 ? 292 THR A OG1 1 
ATOM   4628 C CG2 . THR B 1 292 ? 3.234   15.180  32.118 1.00 19.97 ? 292 THR A CG2 1 
ATOM   4629 N N   . PRO B 1 293 ? -0.835  13.959  33.518 1.00 19.79 ? 293 PRO A N   1 
ATOM   4630 C CA  . PRO B 1 293 ? -2.234  13.595  33.222 1.00 17.70 ? 293 PRO A CA  1 
ATOM   4631 C C   . PRO B 1 293 ? -2.449  13.168  31.775 1.00 21.05 ? 293 PRO A C   1 
ATOM   4632 O O   . PRO B 1 293 ? -3.121  12.152  31.517 1.00 21.18 ? 293 PRO A O   1 
ATOM   4633 C CB  . PRO B 1 293 ? -2.994  14.888  33.568 1.00 19.45 ? 293 PRO A CB  1 
ATOM   4634 C CG  . PRO B 1 293 ? -2.178  15.474  34.700 1.00 20.05 ? 293 PRO A CG  1 
ATOM   4635 C CD  . PRO B 1 293 ? -0.742  15.231  34.265 1.00 19.15 ? 293 PRO A CD  1 
ATOM   4636 N N   . PHE B 1 294 ? -1.851  13.887  30.820 1.00 20.60 ? 294 PHE A N   1 
ATOM   4637 C CA  . PHE B 1 294 ? -2.042  13.529  29.417 1.00 25.60 ? 294 PHE A CA  1 
ATOM   4638 C C   . PHE B 1 294 ? -1.398  12.185  29.087 1.00 24.51 ? 294 PHE A C   1 
ATOM   4639 O O   . PHE B 1 294 ? -1.957  11.403  28.306 1.00 24.09 ? 294 PHE A O   1 
ATOM   4640 C CB  . PHE B 1 294 ? -1.487  14.612  28.491 1.00 26.19 ? 294 PHE A CB  1 
ATOM   4641 C CG  . PHE B 1 294 ? -1.401  14.169  27.050 1.00 35.14 ? 294 PHE A CG  1 
ATOM   4642 C CD1 . PHE B 1 294 ? -2.532  14.188  26.243 1.00 39.42 ? 294 PHE A CD1 1 
ATOM   4643 C CD2 . PHE B 1 294 ? -0.212  13.677  26.522 1.00 38.04 ? 294 PHE A CD2 1 
ATOM   4644 C CE1 . PHE B 1 294 ? -2.471  13.762  24.924 1.00 42.09 ? 294 PHE A CE1 1 
ATOM   4645 C CE2 . PHE B 1 294 ? -0.144  13.243  25.207 1.00 41.15 ? 294 PHE A CE2 1 
ATOM   4646 C CZ  . PHE B 1 294 ? -1.279  13.285  24.407 1.00 39.78 ? 294 PHE A CZ  1 
ATOM   4647 N N   . ASP B 1 295 ? -0.201  11.917  29.629 1.00 22.74 ? 295 ASP A N   1 
ATOM   4648 C CA  . ASP B 1 295 ? 0.429   10.610  29.435 1.00 23.17 ? 295 ASP A CA  1 
ATOM   4649 C C   . ASP B 1 295 ? -0.510  9.484   29.832 1.00 22.72 ? 295 ASP A C   1 
ATOM   4650 O O   . ASP B 1 295 ? -0.568  8.452   29.156 1.00 22.27 ? 295 ASP A O   1 
ATOM   4651 C CB  . ASP B 1 295 ? 1.705   10.484  30.261 1.00 18.68 ? 295 ASP A CB  1 
ATOM   4652 C CG  . ASP B 1 295 ? 2.805   11.387  29.784 1.00 23.02 ? 295 ASP A CG  1 
ATOM   4653 O OD1 . ASP B 1 295 ? 2.732   11.857  28.627 1.00 24.86 ? 295 ASP A OD1 1 
ATOM   4654 O OD2 . ASP B 1 295 ? 3.741   11.597  30.578 1.00 21.96 ? 295 ASP A OD2 1 
ATOM   4655 N N   . VAL B 1 296 ? -1.227  9.659   30.949 1.00 21.46 ? 296 VAL A N   1 
ATOM   4656 C CA  . VAL B 1 296 ? -2.115  8.613   31.455 1.00 22.65 ? 296 VAL A CA  1 
ATOM   4657 C C   . VAL B 1 296 ? -3.285  8.405   30.507 1.00 23.86 ? 296 VAL A C   1 
ATOM   4658 O O   . VAL B 1 296 ? -3.615  7.271   30.147 1.00 21.25 ? 296 VAL A O   1 
ATOM   4659 C CB  . VAL B 1 296 ? -2.610  8.960   32.871 1.00 18.33 ? 296 VAL A CB  1 
ATOM   4660 C CG1 . VAL B 1 296 ? -3.674  7.930   33.337 1.00 17.93 ? 296 VAL A CG1 1 
ATOM   4661 C CG2 . VAL B 1 296 ? -1.459  8.973   33.843 1.00 20.21 ? 296 VAL A CG2 1 
ATOM   4662 N N   . VAL B 1 297 ? -3.955  9.498   30.132 1.00 21.30 ? 297 VAL A N   1 
ATOM   4663 C CA  . VAL B 1 297 ? -5.074  9.422   29.195 1.00 24.76 ? 297 VAL A CA  1 
ATOM   4664 C C   . VAL B 1 297 ? -4.613  8.822   27.873 1.00 29.71 ? 297 VAL A C   1 
ATOM   4665 O O   . VAL B 1 297 ? -5.265  7.926   27.315 1.00 27.17 ? 297 VAL A O   1 
ATOM   4666 C CB  . VAL B 1 297 ? -5.695  10.819  28.994 1.00 30.47 ? 297 VAL A CB  1 
ATOM   4667 C CG1 . VAL B 1 297 ? -6.700  10.816  27.832 1.00 31.12 ? 297 VAL A CG1 1 
ATOM   4668 C CG2 . VAL B 1 297 ? -6.353  11.313  30.282 1.00 24.12 ? 297 VAL A CG2 1 
ATOM   4669 N N   . ARG B 1 298 ? -3.472  9.302   27.356 1.00 24.02 ? 298 ARG A N   1 
ATOM   4670 C CA  . ARG B 1 298 ? -2.987  8.824   26.063 1.00 27.54 ? 298 ARG A CA  1 
ATOM   4671 C C   . ARG B 1 298 ? -2.787  7.315   26.083 1.00 29.79 ? 298 ARG A C   1 
ATOM   4672 O O   . ARG B 1 298 ? -3.188  6.617   25.145 1.00 32.46 ? 298 ARG A O   1 
ATOM   4673 C CB  . ARG B 1 298 ? -1.689  9.549   25.682 1.00 30.13 ? 298 ARG A CB  1 
ATOM   4674 C CG  . ARG B 1 298 ? -0.632  8.666   25.035 1.00 34.06 ? 298 ARG A CG  1 
ATOM   4675 C CD  . ARG B 1 298 ? 0.650   9.422   24.682 1.00 39.07 ? 298 ARG A CD  1 
ATOM   4676 N NE  . ARG B 1 298 ? 1.541   8.576   23.893 1.00 40.64 ? 298 ARG A NE  1 
ATOM   4677 C CZ  . ARG B 1 298 ? 2.773   8.225   24.248 1.00 39.79 ? 298 ARG A CZ  1 
ATOM   4678 N NH1 . ARG B 1 298 ? 3.340   8.692   25.353 1.00 37.46 ? 298 ARG A NH1 1 
ATOM   4679 N NH2 . ARG B 1 298 ? 3.454   7.377   23.477 1.00 30.68 ? 298 ARG A NH2 1 
ATOM   4680 N N   . GLN B 1 299 ? -2.220  6.788   27.167 1.00 27.28 ? 299 GLN A N   1 
ATOM   4681 C CA  . GLN B 1 299 ? -1.900  5.368   27.215 1.00 25.58 ? 299 GLN A CA  1 
ATOM   4682 C C   . GLN B 1 299 ? -3.128  4.528   27.501 1.00 29.92 ? 299 GLN A C   1 
ATOM   4683 O O   . GLN B 1 299 ? -3.260  3.420   26.969 1.00 28.53 ? 299 GLN A O   1 
ATOM   4684 C CB  . GLN B 1 299 ? -0.857  5.072   28.287 1.00 27.23 ? 299 GLN A CB  1 
ATOM   4685 C CG  . GLN B 1 299 ? -0.170  3.732   28.073 1.00 25.73 ? 299 GLN A CG  1 
ATOM   4686 C CD  . GLN B 1 299 ? 0.852   3.405   29.143 1.00 24.56 ? 299 GLN A CD  1 
ATOM   4687 O OE1 . GLN B 1 299 ? 1.010   2.243   29.517 1.00 21.58 ? 299 GLN A OE1 1 
ATOM   4688 N NE2 . GLN B 1 299 ? 1.543   4.425   29.651 1.00 22.57 ? 299 GLN A NE2 1 
ATOM   4689 N N   . CYS B 1 300 ? -4.009  5.019   28.368 1.00 25.81 ? 300 CYS A N   1 
ATOM   4690 C CA  . CYS B 1 300 ? -5.187  4.263   28.759 1.00 29.39 ? 300 CYS A CA  1 
ATOM   4691 C C   . CYS B 1 300 ? -6.311  4.347   27.730 1.00 34.54 ? 300 CYS A C   1 
ATOM   4692 O O   . CYS B 1 300 ? -7.277  3.584   27.838 1.00 39.55 ? 300 CYS A O   1 
ATOM   4693 C CB  . CYS B 1 300 ? -5.675  4.744   30.132 1.00 27.05 ? 300 CYS A CB  1 
ATOM   4694 S SG  . CYS B 1 300 ? -4.495  4.425   31.500 1.00 34.65 ? 300 CYS A SG  1 
ATOM   4695 N N   . SER B 1 301 ? -6.196  5.222   26.725 1.00 33.68 ? 301 SER A N   1 
ATOM   4696 C CA  . SER B 1 301 ? -7.208  5.361   25.685 1.00 34.55 ? 301 SER A CA  1 
ATOM   4697 C C   . SER B 1 301 ? -6.683  5.106   24.274 1.00 39.32 ? 301 SER A C   1 
ATOM   4698 O O   . SER B 1 301 ? -7.480  5.096   23.327 1.00 42.15 ? 301 SER A O   1 
ATOM   4699 C CB  . SER B 1 301 ? -7.847  6.755   25.761 1.00 40.89 ? 301 SER A CB  1 
ATOM   4700 O OG  . SER B 1 301 ? -7.142  7.689   24.964 1.00 46.59 ? 301 SER A OG  1 
ATOM   4701 N N   . GLY B 1 302 ? -5.378  4.903   24.100 1.00 39.02 ? 302 GLY A N   1 
ATOM   4702 C CA  . GLY B 1 302 ? -4.855  4.397   22.840 1.00 42.25 ? 302 GLY A CA  1 
ATOM   4703 C C   . GLY B 1 302 ? -4.617  5.421   21.752 1.00 47.02 ? 302 GLY A C   1 
ATOM   4704 O O   . GLY B 1 302 ? -4.703  5.079   20.565 1.00 43.96 ? 302 GLY A O   1 
ATOM   4705 N N   . VAL B 1 303 ? -4.313  6.669   22.122 1.00 48.21 ? 303 VAL A N   1 
ATOM   4706 C CA  . VAL B 1 303 ? -4.045  7.711   21.132 1.00 55.54 ? 303 VAL A CA  1 
ATOM   4707 C C   . VAL B 1 303 ? -2.833  7.323   20.294 1.00 58.47 ? 303 VAL A C   1 
ATOM   4708 O O   . VAL B 1 303 ? -1.797  6.905   20.827 1.00 51.59 ? 303 VAL A O   1 
ATOM   4709 C CB  . VAL B 1 303 ? -3.842  9.067   21.829 1.00 51.90 ? 303 VAL A CB  1 
ATOM   4710 C CG1 . VAL B 1 303 ? -3.649  10.183  20.803 1.00 59.65 ? 303 VAL A CG1 1 
ATOM   4711 C CG2 . VAL B 1 303 ? -5.021  9.378   22.752 1.00 44.48 ? 303 VAL A CG2 1 
ATOM   4712 N N   . THR B 1 304 ? -2.958  7.466   18.974 1.00 62.31 ? 304 THR A N   1 
ATOM   4713 C CA  . THR B 1 304 ? -1.946  7.027   18.021 1.00 64.86 ? 304 THR A CA  1 
ATOM   4714 C C   . THR B 1 304 ? -1.443  8.210   17.192 1.00 70.13 ? 304 THR A C   1 
ATOM   4715 O O   . THR B 1 304 ? -1.997  9.313   17.235 1.00 71.31 ? 304 THR A O   1 
ATOM   4716 C CB  . THR B 1 304 ? -2.500  5.920   17.111 1.00 59.75 ? 304 THR A CB  1 
ATOM   4717 O OG1 . THR B 1 304 ? -1.454  5.425   16.269 1.00 55.34 ? 304 THR A OG1 1 
ATOM   4718 C CG2 . THR B 1 304 ? -3.645  6.447   16.242 1.00 60.94 ? 304 THR A CG2 1 
ATOM   4719 N N   . PHE B 1 305 ? -0.373  7.966   16.427 1.00 72.35 ? 305 PHE A N   1 
ATOM   4720 C CA  . PHE B 1 305 ? 0.324   9.013   15.685 1.00 76.00 ? 305 PHE A CA  1 
ATOM   4721 C C   . PHE B 1 305 ? 0.756   8.499   14.318 1.00 79.73 ? 305 PHE A C   1 
ATOM   4722 O O   . PHE B 1 305 ? 1.132   7.332   14.171 1.00 94.02 ? 305 PHE A O   1 
ATOM   4723 C CB  . PHE B 1 305 ? 1.562   9.513   16.456 1.00 70.02 ? 305 PHE A CB  1 
ATOM   4724 C CG  . PHE B 1 305 ? 1.341   9.629   17.934 1.00 63.80 ? 305 PHE A CG  1 
ATOM   4725 C CD1 . PHE B 1 305 ? 0.732   10.752  18.471 1.00 62.20 ? 305 PHE A CD1 1 
ATOM   4726 C CD2 . PHE B 1 305 ? 1.705   8.594   18.783 1.00 55.41 ? 305 PHE A CD2 1 
ATOM   4727 C CE1 . PHE B 1 305 ? 0.509   10.852  19.831 1.00 59.04 ? 305 PHE A CE1 1 
ATOM   4728 C CE2 . PHE B 1 305 ? 1.484   8.684   20.143 1.00 53.46 ? 305 PHE A CE2 1 
ATOM   4729 C CZ  . PHE B 1 305 ? 0.881   9.814   20.668 1.00 58.00 ? 305 PHE A CZ  1 
ATOM   4730 N N   . GLN B 1 306 ? 0.705   9.381   13.323 1.00 77.02 ? 306 GLN A N   1 
ATOM   4731 C CA  . GLN B 1 306 ? 1.231   9.079   11.996 1.00 79.36 ? 306 GLN A CA  1 
ATOM   4732 C C   . GLN B 1 306 ? 1.530   10.358  11.225 1.00 74.75 ? 306 GLN A C   1 
ATOM   4733 O O   . GLN B 1 306 ? 2.039   10.309  10.106 1.00 76.39 ? 306 GLN A O   1 
ATOM   4734 C CB  . GLN B 1 306 ? 0.258   8.204   11.196 1.00 82.21 ? 306 GLN A CB  1 
ATOM   4735 C CG  . GLN B 1 306 ? 0.837   6.845   10.800 1.00 74.11 ? 306 GLN A CG  1 
ATOM   4736 C CD  . GLN B 1 306 ? -0.132  5.998   9.986  1.00 69.58 ? 306 GLN A CD  1 
ATOM   4737 O OE1 . GLN B 1 306 ? -1.251  6.425   9.686  1.00 74.36 ? 306 GLN A OE1 1 
ATOM   4738 N NE2 . GLN B 1 306 ? 0.307   4.799   9.602  1.00 59.80 ? 306 GLN A NE2 1 
HETATM 4739 O O26 . O6K C 2 .   ? -10.455 -11.811 28.393 1.00 32.73 ? 401 O6K B O26 1 
HETATM 4740 C C24 . O6K C 2 .   ? -9.225  -11.741 28.406 1.00 30.98 ? 401 O6K B C24 1 
HETATM 4741 O O25 . O6K C 2 .   ? -8.518  -11.253 29.445 1.00 27.06 ? 401 O6K B O25 1 
HETATM 4742 C C27 . O6K C 2 .   ? -9.096  -10.775 30.689 1.00 31.68 ? 401 O6K B C27 1 
HETATM 4743 C C31 . O6K C 2 .   ? -10.085 -9.622  30.405 1.00 32.54 ? 401 O6K B C31 1 
HETATM 4744 C C32 . O6K C 2 .   ? -9.827  -11.956 31.435 1.00 34.88 ? 401 O6K B C32 1 
HETATM 4745 C C33 . O6K C 2 .   ? -7.955  -10.281 31.584 1.00 30.57 ? 401 O6K B C33 1 
HETATM 4746 N N23 . O6K C 2 .   ? -8.560  -12.194 27.289 1.00 25.70 ? 401 O6K B N23 1 
HETATM 4747 C C19 . O6K C 2 .   ? -8.965  -12.464 26.044 1.00 26.26 ? 401 O6K B C19 1 
HETATM 4748 C C21 . O6K C 2 .   ? -8.134  -12.120 24.927 1.00 27.42 ? 401 O6K B C21 1 
HETATM 4749 O O22 . O6K C 2 .   ? -7.059  -11.579 24.897 1.00 24.87 ? 401 O6K B O22 1 
HETATM 4750 C C18 . O6K C 2 .   ? -10.232 -13.118 25.685 1.00 29.71 ? 401 O6K B C18 1 
HETATM 4751 C C17 . O6K C 2 .   ? -10.613 -13.386 24.424 1.00 29.08 ? 401 O6K B C17 1 
HETATM 4752 C C16 . O6K C 2 .   ? -9.773  -13.037 23.316 1.00 30.37 ? 401 O6K B C16 1 
HETATM 4753 N N15 . O6K C 2 .   ? -8.602  -12.458 23.447 1.00 26.37 ? 401 O6K B N15 1 
HETATM 4754 C C20 . O6K C 2 .   ? -7.600  -12.048 22.406 1.00 25.69 ? 401 O6K B C20 1 
HETATM 4755 C C22 . O6K C 2 .   ? -7.864  -12.832 21.078 1.00 26.01 ? 401 O6K B C22 1 
HETATM 4756 C C29 . O6K C 2 .   ? -7.634  -14.329 21.111 1.00 27.13 ? 401 O6K B C29 1 
HETATM 4757 C C34 . O6K C 2 .   ? -6.206  -14.834 21.017 1.00 28.20 ? 401 O6K B C34 1 
HETATM 4758 C C30 . O6K C 2 .   ? -7.157  -15.072 19.882 1.00 28.33 ? 401 O6K B C30 1 
HETATM 4759 C C36 . O6K C 2 .   ? -7.722  -10.532 22.176 1.00 26.43 ? 401 O6K B C36 1 
HETATM 4760 O O37 . O6K C 2 .   ? -8.827  -10.012 22.406 1.00 23.36 ? 401 O6K B O37 1 
HETATM 4761 N N38 . O6K C 2 .   ? -6.645  -9.820  21.736 1.00 21.94 ? 401 O6K B N38 1 
HETATM 4762 C C40 . O6K C 2 .   ? -6.631  -8.418  21.390 1.00 24.45 ? 401 O6K B C40 1 
HETATM 4763 C C42 . O6K C 2 .   ? -5.635  -7.654  22.276 1.00 23.71 ? 401 O6K B C42 1 
HETATM 4764 C C45 . O6K C 2 .   ? -6.074  -7.477  23.743 1.00 26.16 ? 401 O6K B C45 1 
HETATM 4765 C C47 . O6K C 2 .   ? -5.128  -6.775  24.740 1.00 25.47 ? 401 O6K B C47 1 
HETATM 4766 O O48 . O6K C 2 .   ? -3.946  -7.078  24.867 1.00 25.42 ? 401 O6K B O48 1 
HETATM 4767 N N49 . O6K C 2 .   ? -5.758  -5.782  25.462 1.00 26.13 ? 401 O6K B N49 1 
HETATM 4768 C C51 . O6K C 2 .   ? -7.171  -5.659  25.074 1.00 25.21 ? 401 O6K B C51 1 
HETATM 4769 C C54 . O6K C 2 .   ? -7.268  -6.516  23.775 1.00 28.80 ? 401 O6K B C54 1 
HETATM 4770 C C57 . O6K C 2 .   ? -6.285  -8.382  19.819 1.00 24.45 ? 401 O6K B C57 1 
HETATM 4771 O O40 . O6K C 2 .   ? -6.989  -9.447  19.286 1.00 27.77 ? 401 O6K B O40 1 
HETATM 4772 C C35 . O6K C 2 .   ? -6.863  -7.147  19.136 1.00 27.89 ? 401 O6K B C35 1 
HETATM 4773 O O41 . O6K C 2 .   ? -6.412  -6.097  19.552 1.00 23.77 ? 401 O6K B O41 1 
HETATM 4774 N N36 . O6K C 2 .   ? -7.819  -7.221  18.123 1.00 29.19 ? 401 O6K B N36 1 
HETATM 4775 C C13 . O6K C 2 .   ? -8.482  -6.097  17.403 1.00 31.16 ? 401 O6K B C13 1 
HETATM 4776 C C14 . O6K C 2 .   ? -9.642  -5.476  18.245 1.00 32.10 ? 401 O6K B C14 1 
HETATM 4777 C C28 . O6K C 2 .   ? -10.098 -6.091  19.420 1.00 34.08 ? 401 O6K B C28 1 
HETATM 4778 C C26 . O6K C 2 .   ? -11.129 -5.576  20.217 1.00 30.36 ? 401 O6K B C26 1 
HETATM 4779 C C25 . O6K C 2 .   ? -11.755 -4.395  19.847 1.00 32.73 ? 401 O6K B C25 1 
HETATM 4780 C C23 . O6K C 2 .   ? -11.336 -3.745  18.681 1.00 31.74 ? 401 O6K B C23 1 
HETATM 4781 C C15 . O6K C 2 .   ? -10.299 -4.276  17.895 1.00 35.70 ? 401 O6K B C15 1 
HETATM 4782 O O26 . O6K D 2 .   ? 31.862  17.007  34.724 1.00 27.56 ? 401 O6K A O26 1 
HETATM 4783 C C24 . O6K D 2 .   ? 30.648  17.203  34.650 1.00 25.77 ? 401 O6K A C24 1 
HETATM 4784 O O25 . O6K D 2 .   ? 29.805  17.090  35.694 1.00 26.28 ? 401 O6K A O25 1 
HETATM 4785 C C27 . O6K D 2 .   ? 30.226  16.770  37.013 1.00 29.21 ? 401 O6K A C27 1 
HETATM 4786 C C31 . O6K D 2 .   ? 28.955  16.749  37.849 1.00 28.94 ? 401 O6K A C31 1 
HETATM 4787 C C32 . O6K D 2 .   ? 30.842  15.348  36.998 1.00 28.70 ? 401 O6K A C32 1 
HETATM 4788 C C33 . O6K D 2 .   ? 31.240  17.789  37.594 1.00 29.23 ? 401 O6K A C33 1 
HETATM 4789 N N23 . O6K D 2 .   ? 30.161  17.590  33.434 1.00 24.22 ? 401 O6K A N23 1 
HETATM 4790 C C19 . O6K D 2 .   ? 30.767  18.085  32.347 1.00 21.99 ? 401 O6K A C19 1 
HETATM 4791 C C21 . O6K D 2 .   ? 29.993  18.326  31.188 1.00 25.19 ? 401 O6K A C21 1 
HETATM 4792 O O22 . O6K D 2 .   ? 28.809  18.153  31.007 1.00 23.36 ? 401 O6K A O22 1 
HETATM 4793 C C18 . O6K D 2 .   ? 32.206  18.384  32.208 1.00 24.48 ? 401 O6K A C18 1 
HETATM 4794 C C17 . O6K D 2 .   ? 32.764  18.865  31.085 1.00 26.27 ? 401 O6K A C17 1 
HETATM 4795 C C16 . O6K D 2 .   ? 31.957  19.109  29.928 1.00 24.61 ? 401 O6K A C16 1 
HETATM 4796 N N15 . O6K D 2 .   ? 30.662  18.880  29.897 1.00 23.27 ? 401 O6K A N15 1 
HETATM 4797 C C20 . O6K D 2 .   ? 29.699  19.065  28.806 1.00 23.70 ? 401 O6K A C20 1 
HETATM 4798 C C22 . O6K D 2 .   ? 30.162  20.248  27.913 1.00 23.75 ? 401 O6K A C22 1 
HETATM 4799 C C29 . O6K D 2 .   ? 30.060  21.634  28.508 1.00 24.40 ? 401 O6K A C29 1 
HETATM 4800 C C34 . O6K D 2 .   ? 29.618  22.772  27.610 1.00 24.31 ? 401 O6K A C34 1 
HETATM 4801 C C30 . O6K D 2 .   ? 28.704  22.263  28.680 1.00 24.59 ? 401 O6K A C30 1 
HETATM 4802 C C36 . O6K D 2 .   ? 29.732  17.717  28.063 1.00 23.71 ? 401 O6K A C36 1 
HETATM 4803 O O37 . O6K D 2 .   ? 30.762  17.036  28.190 1.00 25.07 ? 401 O6K A O37 1 
HETATM 4804 N N38 . O6K D 2 .   ? 28.710  17.274  27.319 1.00 21.45 ? 401 O6K A N38 1 
HETATM 4805 C C40 . O6K D 2 .   ? 28.732  16.045  26.563 1.00 20.96 ? 401 O6K A C40 1 
HETATM 4806 C C42 . O6K D 2 .   ? 27.675  15.071  27.131 1.00 20.82 ? 401 O6K A C42 1 
HETATM 4807 C C45 . O6K D 2 .   ? 28.016  14.602  28.549 1.00 20.70 ? 401 O6K A C45 1 
HETATM 4808 C C47 . O6K D 2 .   ? 26.979  13.826  29.353 1.00 23.90 ? 401 O6K A C47 1 
HETATM 4809 O O48 . O6K D 2 .   ? 25.821  14.179  29.418 1.00 23.29 ? 401 O6K A O48 1 
HETATM 4810 N N49 . O6K D 2 .   ? 27.508  12.728  29.990 1.00 26.13 ? 401 O6K A N49 1 
HETATM 4811 C C51 . O6K D 2 .   ? 28.952  12.601  29.690 1.00 30.58 ? 401 O6K A C51 1 
HETATM 4812 C C54 . O6K D 2 .   ? 29.127  13.555  28.483 1.00 25.72 ? 401 O6K A C54 1 
HETATM 4813 C C57 . O6K D 2 .   ? 28.517  16.494  25.053 1.00 25.62 ? 401 O6K A C57 1 
HETATM 4814 O O40 . O6K D 2 .   ? 29.357  17.613  24.893 1.00 28.25 ? 401 O6K A O40 1 
HETATM 4815 C C35 . O6K D 2 .   ? 29.052  15.482  24.073 1.00 28.31 ? 401 O6K A C35 1 
HETATM 4816 O O41 . O6K D 2 .   ? 28.415  14.441  23.997 1.00 27.60 ? 401 O6K A O41 1 
HETATM 4817 N N36 . O6K D 2 .   ? 30.189  15.764  23.320 1.00 29.59 ? 401 O6K A N36 1 
HETATM 4818 C C13 . O6K D 2 .   ? 30.903  14.906  22.323 1.00 31.06 ? 401 O6K A C13 1 
HETATM 4819 C C14 . O6K D 2 .   ? 32.086  14.153  22.989 1.00 31.67 ? 401 O6K A C14 1 
HETATM 4820 C C28 . O6K D 2 .   ? 32.482  14.472  24.299 1.00 34.34 ? 401 O6K A C28 1 
HETATM 4821 C C26 . O6K D 2 .   ? 33.541  13.831  24.955 1.00 37.71 ? 401 O6K A C26 1 
HETATM 4822 C C25 . O6K D 2 .   ? 34.248  12.827  24.298 1.00 34.57 ? 401 O6K A C25 1 
HETATM 4823 C C23 . O6K D 2 .   ? 33.886  12.473  22.990 1.00 35.37 ? 401 O6K A C23 1 
HETATM 4824 C C15 . O6K D 2 .   ? 32.825  13.127  22.349 1.00 33.88 ? 401 O6K A C15 1 
HETATM 4825 O O   . HOH E 3 .   ? -17.175 -20.547 13.830 1.00 45.05 ? 501 HOH B O   1 
HETATM 4826 O O   . HOH E 3 .   ? -6.572  -4.466  0.534  1.00 38.45 ? 502 HOH B O   1 
HETATM 4827 O O   . HOH E 3 .   ? 18.656  -21.276 36.465 1.00 28.69 ? 503 HOH B O   1 
HETATM 4828 O O   . HOH E 3 .   ? 15.107  -11.712 56.792 1.00 38.54 ? 504 HOH B O   1 
HETATM 4829 O O   . HOH E 3 .   ? 15.806  7.714   45.501 1.00 33.01 ? 505 HOH B O   1 
HETATM 4830 O O   . HOH E 3 .   ? 14.553  -23.286 36.790 1.00 45.87 ? 506 HOH B O   1 
HETATM 4831 O O   . HOH E 3 .   ? 6.489   1.768   3.349  1.00 45.88 ? 507 HOH B O   1 
HETATM 4832 O O   . HOH E 3 .   ? 13.501  -4.271  29.952 1.00 41.15 ? 508 HOH B O   1 
HETATM 4833 O O   . HOH E 3 .   ? 24.632  -23.939 43.213 1.00 33.41 ? 509 HOH B O   1 
HETATM 4834 O O   . HOH E 3 .   ? 22.062  -21.135 32.818 1.00 29.95 ? 510 HOH B O   1 
HETATM 4835 O O   . HOH E 3 .   ? 11.019  -4.175  30.932 1.00 23.83 ? 511 HOH B O   1 
HETATM 4836 O O   . HOH E 3 .   ? -7.907  -24.379 14.040 1.00 34.92 ? 512 HOH B O   1 
HETATM 4837 O O   . HOH E 3 .   ? 29.050  -6.489  47.641 1.00 18.29 ? 513 HOH B O   1 
HETATM 4838 O O   . HOH E 3 .   ? 20.860  5.379   46.307 1.00 28.13 ? 514 HOH B O   1 
HETATM 4839 O O   . HOH E 3 .   ? 4.729   -25.353 15.542 1.00 42.70 ? 515 HOH B O   1 
HETATM 4840 O O   . HOH E 3 .   ? -9.392  -19.054 1.231  1.00 38.15 ? 516 HOH B O   1 
HETATM 4841 O O   . HOH E 3 .   ? 10.800  -13.361 43.677 1.00 31.74 ? 517 HOH B O   1 
HETATM 4842 O O   . HOH E 3 .   ? -0.601  0.542   23.999 1.00 24.94 ? 518 HOH B O   1 
HETATM 4843 O O   . HOH E 3 .   ? 8.355   -11.094 3.760  1.00 30.67 ? 519 HOH B O   1 
HETATM 4844 O O   . HOH E 3 .   ? 31.827  3.583   36.657 1.00 28.38 ? 520 HOH B O   1 
HETATM 4845 O O   . HOH E 3 .   ? 21.129  -10.467 26.239 1.00 38.76 ? 521 HOH B O   1 
HETATM 4846 O O   . HOH E 3 .   ? -7.463  -6.731  -0.717 1.00 39.17 ? 522 HOH B O   1 
HETATM 4847 O O   . HOH E 3 .   ? 22.729  -11.587 54.142 1.00 35.31 ? 523 HOH B O   1 
HETATM 4848 O O   . HOH E 3 .   ? 11.286  -3.591  47.821 1.00 35.11 ? 524 HOH B O   1 
HETATM 4849 O O   . HOH E 3 .   ? -1.089  -22.374 20.659 1.00 26.32 ? 525 HOH B O   1 
HETATM 4850 O O   . HOH E 3 .   ? 10.592  -14.780 34.867 1.00 24.48 ? 526 HOH B O   1 
HETATM 4851 O O   . HOH E 3 .   ? 12.841  -9.548  50.272 1.00 36.17 ? 527 HOH B O   1 
HETATM 4852 O O   . HOH E 3 .   ? -7.650  -23.365 4.975  1.00 39.07 ? 528 HOH B O   1 
HETATM 4853 O O   . HOH E 3 .   ? 9.910   -0.519  40.348 1.00 30.68 ? 529 HOH B O   1 
HETATM 4854 O O   . HOH E 3 .   ? 35.223  -11.081 34.744 1.00 27.32 ? 530 HOH B O   1 
HETATM 4855 O O   . HOH E 3 .   ? 17.851  -15.751 28.680 1.00 30.68 ? 531 HOH B O   1 
HETATM 4856 O O   . HOH E 3 .   ? 18.899  -12.822 31.084 1.00 22.36 ? 532 HOH B O   1 
HETATM 4857 O O   . HOH E 3 .   ? -14.611 -12.641 9.342  1.00 42.60 ? 533 HOH B O   1 
HETATM 4858 O O   . HOH E 3 .   ? 13.045  -4.170  35.626 1.00 28.64 ? 534 HOH B O   1 
HETATM 4859 O O   . HOH E 3 .   ? 4.515   -3.074  16.014 1.00 22.69 ? 535 HOH B O   1 
HETATM 4860 O O   . HOH E 3 .   ? 29.194  8.999   31.716 1.00 28.85 ? 536 HOH B O   1 
HETATM 4861 O O   . HOH E 3 .   ? 16.665  -5.659  24.232 1.00 23.94 ? 537 HOH B O   1 
HETATM 4862 O O   . HOH E 3 .   ? 27.565  -11.289 28.669 1.00 35.82 ? 538 HOH B O   1 
HETATM 4863 O O   . HOH E 3 .   ? -15.519 -25.564 17.155 1.00 38.82 ? 539 HOH B O   1 
HETATM 4864 O O   . HOH E 3 .   ? 1.191   -22.995 23.109 1.00 28.87 ? 540 HOH B O   1 
HETATM 4865 O O   . HOH E 3 .   ? -9.019  -23.444 17.518 1.00 37.20 ? 541 HOH B O   1 
HETATM 4866 O O   . HOH E 3 .   ? 33.182  -16.882 35.365 1.00 33.29 ? 542 HOH B O   1 
HETATM 4867 O O   . HOH E 3 .   ? 3.553   2.972   10.411 1.00 40.06 ? 543 HOH B O   1 
HETATM 4868 O O   . HOH E 3 .   ? -2.113  -23.115 11.518 1.00 30.46 ? 544 HOH B O   1 
HETATM 4869 O O   . HOH E 3 .   ? 15.988  -3.697  28.736 1.00 28.12 ? 545 HOH B O   1 
HETATM 4870 O O   . HOH E 3 .   ? 1.146   -12.685 35.791 1.00 31.78 ? 546 HOH B O   1 
HETATM 4871 O O   . HOH E 3 .   ? 16.620  3.238   35.892 1.00 28.64 ? 547 HOH B O   1 
HETATM 4872 O O   . HOH E 3 .   ? 1.573   -5.523  31.940 1.00 28.18 ? 548 HOH B O   1 
HETATM 4873 O O   . HOH E 3 .   ? 15.886  -7.794  58.613 1.00 36.10 ? 549 HOH B O   1 
HETATM 4874 O O   . HOH E 3 .   ? -13.104 -2.857  11.956 1.00 41.78 ? 550 HOH B O   1 
HETATM 4875 O O   . HOH E 3 .   ? 35.234  -8.916  44.340 1.00 22.20 ? 551 HOH B O   1 
HETATM 4876 O O   . HOH E 3 .   ? 3.244   -15.721 25.209 1.00 21.78 ? 552 HOH B O   1 
HETATM 4877 O O   . HOH E 3 .   ? -7.634  -1.975  6.914  1.00 34.08 ? 553 HOH B O   1 
HETATM 4878 O O   . HOH E 3 .   ? 10.234  -14.987 15.230 1.00 23.58 ? 554 HOH B O   1 
HETATM 4879 O O   . HOH E 3 .   ? 18.088  -2.145  7.715  1.00 38.30 ? 555 HOH B O   1 
HETATM 4880 O O   . HOH E 3 .   ? 10.672  0.839   28.124 1.00 22.41 ? 556 HOH B O   1 
HETATM 4881 O O   . HOH E 3 .   ? 18.750  5.510   43.573 1.00 21.73 ? 557 HOH B O   1 
HETATM 4882 O O   . HOH E 3 .   ? 28.861  -18.802 51.521 1.00 27.86 ? 558 HOH B O   1 
HETATM 4883 O O   . HOH E 3 .   ? -5.998  -1.739  15.140 1.00 27.72 ? 559 HOH B O   1 
HETATM 4884 O O   . HOH E 3 .   ? -4.239  -15.557 16.203 1.00 24.17 ? 560 HOH B O   1 
HETATM 4885 O O   . HOH E 3 .   ? 30.500  -23.730 39.242 1.00 37.09 ? 561 HOH B O   1 
HETATM 4886 O O   . HOH E 3 .   ? 9.264   -17.353 47.764 1.00 32.50 ? 562 HOH B O   1 
HETATM 4887 O O   . HOH E 3 .   ? 17.518  -6.266  35.742 1.00 16.02 ? 563 HOH B O   1 
HETATM 4888 O O   . HOH E 3 .   ? 11.097  0.701   7.650  1.00 31.75 ? 564 HOH B O   1 
HETATM 4889 O O   . HOH E 3 .   ? -3.389  -21.752 19.294 1.00 25.46 ? 565 HOH B O   1 
HETATM 4890 O O   . HOH E 3 .   ? 7.934   -8.251  30.671 1.00 21.85 ? 566 HOH B O   1 
HETATM 4891 O O   . HOH E 3 .   ? 26.308  -4.989  54.720 1.00 34.07 ? 567 HOH B O   1 
HETATM 4892 O O   . HOH E 3 .   ? 26.132  -25.147 50.341 1.00 34.82 ? 568 HOH B O   1 
HETATM 4893 O O   . HOH E 3 .   ? 24.919  6.260   30.869 1.00 28.87 ? 569 HOH B O   1 
HETATM 4894 O O   . HOH E 3 .   ? -14.898 -17.624 7.231  1.00 37.14 ? 570 HOH B O   1 
HETATM 4895 O O   . HOH E 3 .   ? 28.863  6.262   35.404 1.00 35.88 ? 571 HOH B O   1 
HETATM 4896 O O   . HOH E 3 .   ? 14.331  -2.840  54.560 1.00 34.11 ? 572 HOH B O   1 
HETATM 4897 O O   . HOH E 3 .   ? 35.458  -10.741 53.254 1.00 25.01 ? 573 HOH B O   1 
HETATM 4898 O O   . HOH E 3 .   ? -14.124 -8.390  4.855  1.00 40.03 ? 574 HOH B O   1 
HETATM 4899 O O   . HOH E 3 .   ? 28.605  -14.709 53.363 1.00 28.97 ? 575 HOH B O   1 
HETATM 4900 O O   . HOH E 3 .   ? 34.572  -5.641  30.813 1.00 31.74 ? 576 HOH B O   1 
HETATM 4901 O O   . HOH E 3 .   ? 2.672   -19.656 31.890 1.00 26.96 ? 577 HOH B O   1 
HETATM 4902 O O   . HOH E 3 .   ? -5.120  -26.043 20.616 1.00 42.94 ? 578 HOH B O   1 
HETATM 4903 O O   . HOH E 3 .   ? 10.316  -8.826  38.680 1.00 34.42 ? 579 HOH B O   1 
HETATM 4904 O O   . HOH E 3 .   ? -3.573  -22.543 27.382 1.00 37.19 ? 580 HOH B O   1 
HETATM 4905 O O   . HOH E 3 .   ? 3.389   -12.976 34.484 1.00 23.59 ? 581 HOH B O   1 
HETATM 4906 O O   . HOH E 3 .   ? 35.456  -8.436  57.710 1.00 26.21 ? 582 HOH B O   1 
HETATM 4907 O O   . HOH E 3 .   ? 22.830  -20.028 52.363 1.00 31.35 ? 583 HOH B O   1 
HETATM 4908 O O   . HOH E 3 .   ? 32.881  -17.585 47.341 1.00 27.60 ? 584 HOH B O   1 
HETATM 4909 O O   . HOH E 3 .   ? -4.880  -24.704 12.934 1.00 35.55 ? 585 HOH B O   1 
HETATM 4910 O O   . HOH E 3 .   ? 12.922  -9.312  44.767 1.00 23.33 ? 586 HOH B O   1 
HETATM 4911 O O   . HOH E 3 .   ? 28.984  -23.816 49.872 1.00 30.37 ? 587 HOH B O   1 
HETATM 4912 O O   . HOH E 3 .   ? -7.531  -15.803 24.393 1.00 42.72 ? 588 HOH B O   1 
HETATM 4913 O O   . HOH E 3 .   ? 19.484  -8.202  25.663 1.00 31.93 ? 589 HOH B O   1 
HETATM 4914 O O   . HOH E 3 .   ? 6.774   -16.830 9.219  1.00 31.53 ? 590 HOH B O   1 
HETATM 4915 O O   . HOH E 3 .   ? 32.300  -13.793 36.100 1.00 27.74 ? 591 HOH B O   1 
HETATM 4916 O O   . HOH E 3 .   ? 15.020  2.038   13.822 1.00 29.01 ? 592 HOH B O   1 
HETATM 4917 O O   . HOH E 3 .   ? 19.449  -11.071 57.719 1.00 40.27 ? 593 HOH B O   1 
HETATM 4918 O O   . HOH E 3 .   ? 8.005   -21.137 38.590 1.00 39.95 ? 594 HOH B O   1 
HETATM 4919 O O   . HOH E 3 .   ? -8.057  1.233   21.697 1.00 38.85 ? 595 HOH B O   1 
HETATM 4920 O O   . HOH E 3 .   ? 0.711   -24.122 9.862  1.00 31.21 ? 596 HOH B O   1 
HETATM 4921 O O   . HOH E 3 .   ? 15.660  -7.038  3.890  1.00 39.93 ? 597 HOH B O   1 
HETATM 4922 O O   . HOH E 3 .   ? 12.245  4.249   30.960 1.00 26.83 ? 598 HOH B O   1 
HETATM 4923 O O   . HOH E 3 .   ? 13.605  9.869   34.042 1.00 27.14 ? 599 HOH B O   1 
HETATM 4924 O O   . HOH E 3 .   ? 29.263  5.008   20.559 1.00 46.59 ? 600 HOH B O   1 
HETATM 4925 O O   . HOH E 3 .   ? 23.938  -18.019 53.452 1.00 32.91 ? 601 HOH B O   1 
HETATM 4926 O O   . HOH E 3 .   ? 23.569  -5.224  50.592 1.00 29.86 ? 602 HOH B O   1 
HETATM 4927 O O   . HOH E 3 .   ? 25.078  -11.615 52.495 1.00 31.79 ? 603 HOH B O   1 
HETATM 4928 O O   . HOH E 3 .   ? 15.159  -18.652 16.849 1.00 34.94 ? 604 HOH B O   1 
HETATM 4929 O O   . HOH E 3 .   ? 33.269  -14.527 31.299 1.00 37.84 ? 605 HOH B O   1 
HETATM 4930 O O   . HOH E 3 .   ? 15.180  -15.683 54.510 1.00 30.06 ? 606 HOH B O   1 
HETATM 4931 O O   . HOH E 3 .   ? -3.075  -14.796 34.380 1.00 28.81 ? 607 HOH B O   1 
HETATM 4932 O O   . HOH E 3 .   ? -5.517  -16.748 -3.882 1.00 43.12 ? 608 HOH B O   1 
HETATM 4933 O O   . HOH E 3 .   ? 31.077  -21.238 44.933 1.00 20.90 ? 609 HOH B O   1 
HETATM 4934 O O   . HOH E 3 .   ? 1.263   -21.864 18.953 1.00 24.32 ? 610 HOH B O   1 
HETATM 4935 O O   . HOH E 3 .   ? 12.205  -21.574 44.105 1.00 32.85 ? 611 HOH B O   1 
HETATM 4936 O O   . HOH E 3 .   ? 14.392  -15.123 9.328  1.00 33.61 ? 612 HOH B O   1 
HETATM 4937 O O   . HOH E 3 .   ? 17.197  -16.767 34.497 1.00 31.64 ? 613 HOH B O   1 
HETATM 4938 O O   . HOH E 3 .   ? 7.948   8.587   14.617 1.00 28.92 ? 614 HOH B O   1 
HETATM 4939 O O   . HOH E 3 .   ? 26.751  4.914   32.610 1.00 38.30 ? 615 HOH B O   1 
HETATM 4940 O O   . HOH E 3 .   ? -7.090  -21.795 18.909 1.00 29.98 ? 616 HOH B O   1 
HETATM 4941 O O   . HOH E 3 .   ? 11.426  -5.966  37.123 1.00 36.94 ? 617 HOH B O   1 
HETATM 4942 O O   . HOH E 3 .   ? 26.153  -23.535 33.847 1.00 28.07 ? 618 HOH B O   1 
HETATM 4943 O O   . HOH E 3 .   ? 22.140  -19.457 30.647 1.00 35.52 ? 619 HOH B O   1 
HETATM 4944 O O   . HOH E 3 .   ? -2.995  -21.929 4.591  1.00 35.19 ? 620 HOH B O   1 
HETATM 4945 O O   . HOH E 3 .   ? 16.873  -1.009  28.556 1.00 25.42 ? 621 HOH B O   1 
HETATM 4946 O O   . HOH E 3 .   ? 5.191   -21.182 34.678 1.00 39.57 ? 622 HOH B O   1 
HETATM 4947 O O   . HOH E 3 .   ? 28.412  -8.992  31.807 1.00 24.83 ? 623 HOH B O   1 
HETATM 4948 O O   . HOH E 3 .   ? 31.762  -5.315  46.949 1.00 26.81 ? 624 HOH B O   1 
HETATM 4949 O O   . HOH E 3 .   ? 17.725  -9.587  24.601 1.00 27.30 ? 625 HOH B O   1 
HETATM 4950 O O   . HOH E 3 .   ? 14.896  -10.292 18.978 1.00 24.81 ? 626 HOH B O   1 
HETATM 4951 O O   . HOH E 3 .   ? 7.308   -21.711 24.752 1.00 29.94 ? 627 HOH B O   1 
HETATM 4952 O O   . HOH E 3 .   ? -8.936  -2.009  25.617 1.00 34.34 ? 628 HOH B O   1 
HETATM 4953 O O   . HOH E 3 .   ? 11.213  -20.730 31.326 1.00 38.78 ? 629 HOH B O   1 
HETATM 4954 O O   . HOH E 3 .   ? 38.650  -5.981  37.226 1.00 29.09 ? 630 HOH B O   1 
HETATM 4955 O O   . HOH E 3 .   ? 19.781  -0.731  27.735 1.00 29.13 ? 631 HOH B O   1 
HETATM 4956 O O   . HOH E 3 .   ? 1.795   -23.568 17.107 1.00 34.54 ? 632 HOH B O   1 
HETATM 4957 O O   . HOH E 3 .   ? 14.274  -7.031  48.831 1.00 34.23 ? 633 HOH B O   1 
HETATM 4958 O O   . HOH E 3 .   ? 33.130  -13.371 39.015 1.00 19.96 ? 634 HOH B O   1 
HETATM 4959 O O   . HOH E 3 .   ? -13.064 -13.159 28.173 1.00 39.29 ? 635 HOH B O   1 
HETATM 4960 O O   . HOH E 3 .   ? 18.847  -16.111 36.377 1.00 24.75 ? 636 HOH B O   1 
HETATM 4961 O O   . HOH E 3 .   ? 25.978  7.930   44.894 1.00 39.69 ? 637 HOH B O   1 
HETATM 4962 O O   . HOH E 3 .   ? 32.838  -17.105 50.304 1.00 26.76 ? 638 HOH B O   1 
HETATM 4963 O O   . HOH E 3 .   ? -15.133 -22.430 13.160 1.00 34.85 ? 639 HOH B O   1 
HETATM 4964 O O   . HOH E 3 .   ? 16.200  1.092   38.025 1.00 23.39 ? 640 HOH B O   1 
HETATM 4965 O O   . HOH E 3 .   ? 9.773   -10.868 40.033 1.00 43.95 ? 641 HOH B O   1 
HETATM 4966 O O   . HOH E 3 .   ? 25.878  1.518   53.197 1.00 40.43 ? 642 HOH B O   1 
HETATM 4967 O O   . HOH E 3 .   ? -15.160 -11.077 5.304  1.00 47.12 ? 643 HOH B O   1 
HETATM 4968 O O   . HOH E 3 .   ? -8.522  -15.938 30.473 1.00 36.00 ? 644 HOH B O   1 
HETATM 4969 O O   . HOH E 3 .   ? 26.049  -24.356 37.662 1.00 32.88 ? 645 HOH B O   1 
HETATM 4970 O O   . HOH E 3 .   ? 22.650  -10.678 28.151 1.00 30.42 ? 646 HOH B O   1 
HETATM 4971 O O   . HOH E 3 .   ? 22.363  -24.619 46.237 1.00 28.99 ? 647 HOH B O   1 
HETATM 4972 O O   . HOH E 3 .   ? 24.868  5.001   46.799 1.00 29.98 ? 648 HOH B O   1 
HETATM 4973 O O   . HOH E 3 .   ? 6.995   -23.794 13.008 1.00 38.47 ? 649 HOH B O   1 
HETATM 4974 O O   . HOH E 3 .   ? 29.043  -4.121  57.935 1.00 39.42 ? 650 HOH B O   1 
HETATM 4975 O O   . HOH E 3 .   ? 12.368  -6.554  45.367 1.00 23.13 ? 651 HOH B O   1 
HETATM 4976 O O   . HOH E 3 .   ? 37.229  -7.215  44.415 1.00 36.09 ? 652 HOH B O   1 
HETATM 4977 O O   . HOH E 3 .   ? 39.168  -6.641  42.326 1.00 37.19 ? 653 HOH B O   1 
HETATM 4978 O O   . HOH E 3 .   ? 17.348  -16.617 20.548 1.00 37.68 ? 654 HOH B O   1 
HETATM 4979 O O   . HOH E 3 .   ? 31.026  -4.159  54.400 1.00 26.43 ? 655 HOH B O   1 
HETATM 4980 O O   . HOH E 3 .   ? 10.107  1.047   42.796 1.00 14.69 ? 656 HOH B O   1 
HETATM 4981 O O   . HOH E 3 .   ? 11.612  -19.718 24.053 1.00 36.41 ? 657 HOH B O   1 
HETATM 4982 O O   . HOH E 3 .   ? 30.711  -19.487 40.662 1.00 28.86 ? 658 HOH B O   1 
HETATM 4983 O O   . HOH E 3 .   ? -8.815  -1.908  15.953 1.00 39.65 ? 659 HOH B O   1 
HETATM 4984 O O   . HOH E 3 .   ? -10.615 -9.795  19.931 1.00 40.05 ? 660 HOH B O   1 
HETATM 4985 O O   . HOH E 3 .   ? -4.352  -17.683 -1.853 1.00 42.50 ? 661 HOH B O   1 
HETATM 4986 O O   . HOH E 3 .   ? 25.546  -2.212  52.582 1.00 42.42 ? 662 HOH B O   1 
HETATM 4987 O O   . HOH E 3 .   ? -8.302  -17.878 33.739 1.00 38.66 ? 663 HOH B O   1 
HETATM 4988 O O   . HOH E 3 .   ? 29.404  -23.429 45.700 1.00 22.84 ? 664 HOH B O   1 
HETATM 4989 O O   . HOH E 3 .   ? 32.597  -14.939 41.231 1.00 20.77 ? 665 HOH B O   1 
HETATM 4990 O O   . HOH E 3 .   ? 37.350  -9.341  41.789 1.00 36.46 ? 666 HOH B O   1 
HETATM 4991 O O   . HOH E 3 .   ? 17.263  -15.132 23.055 1.00 35.41 ? 667 HOH B O   1 
HETATM 4992 O O   . HOH E 3 .   ? 9.784   -21.400 24.115 1.00 43.42 ? 668 HOH B O   1 
HETATM 4993 O O   . HOH E 3 .   ? 11.562  -21.376 36.283 1.00 43.03 ? 669 HOH B O   1 
HETATM 4994 O O   . HOH E 3 .   ? 36.724  -7.651  51.915 1.00 36.72 ? 670 HOH B O   1 
HETATM 4995 O O   . HOH E 3 .   ? 10.850  -23.655 9.953  1.00 41.58 ? 671 HOH B O   1 
HETATM 4996 O O   . HOH E 3 .   ? 16.028  -23.103 56.214 1.00 46.38 ? 672 HOH B O   1 
HETATM 4997 O O   . HOH E 3 .   ? 26.472  -13.752 52.391 1.00 26.62 ? 673 HOH B O   1 
HETATM 4998 O O   . HOH E 3 .   ? -10.109 -9.338  17.670 1.00 35.90 ? 674 HOH B O   1 
HETATM 4999 O O   . HOH E 3 .   ? 21.081  6.505   40.894 1.00 31.11 ? 675 HOH B O   1 
HETATM 5000 O O   . HOH E 3 .   ? -11.145 -11.227 16.333 1.00 38.21 ? 676 HOH B O   1 
HETATM 5001 O O   . HOH E 3 .   ? -7.124  -15.029 28.571 1.00 34.59 ? 677 HOH B O   1 
HETATM 5002 O O   . HOH E 3 .   ? 30.187  -24.841 47.609 1.00 31.81 ? 678 HOH B O   1 
HETATM 5003 O O   . HOH E 3 .   ? 33.650  -18.163 38.064 1.00 29.82 ? 679 HOH B O   1 
HETATM 5004 O O   . HOH E 3 .   ? -15.628 -27.101 12.928 1.00 40.54 ? 680 HOH B O   1 
HETATM 5005 O O   . HOH E 3 .   ? 9.375   -7.037  36.400 1.00 34.02 ? 681 HOH B O   1 
HETATM 5006 O O   . HOH E 3 .   ? 12.219  3.340   7.898  1.00 39.82 ? 682 HOH B O   1 
HETATM 5007 O O   . HOH E 3 .   ? -4.851  -24.016 19.026 1.00 32.74 ? 683 HOH B O   1 
HETATM 5008 O O   . HOH E 3 .   ? -15.760 -24.872 14.438 1.00 38.06 ? 684 HOH B O   1 
HETATM 5009 O O   . HOH E 3 .   ? 30.238  -27.473 47.764 1.00 36.95 ? 685 HOH B O   1 
HETATM 5010 O O   . HOH E 3 .   ? -1.593  -4.807  34.790 1.00 42.46 ? 686 HOH B O   1 
HETATM 5011 O O   . HOH E 3 .   ? 35.897  -4.993  44.737 1.00 36.18 ? 687 HOH B O   1 
HETATM 5012 O O   . HOH E 3 .   ? -15.878 -23.100 10.764 1.00 42.58 ? 688 HOH B O   1 
HETATM 5013 O O   . HOH E 3 .   ? 6.783   -23.921 23.375 1.00 40.43 ? 689 HOH B O   1 
HETATM 5014 O O   . HOH E 3 .   ? 8.185   -13.923 43.691 1.00 35.72 ? 690 HOH B O   1 
HETATM 5015 O O   . HOH E 3 .   ? 34.344  -13.476 45.266 1.00 25.93 ? 691 HOH B O   1 
HETATM 5016 O O   . HOH E 3 .   ? 23.271  -23.506 32.204 1.00 34.97 ? 692 HOH B O   1 
HETATM 5017 O O   . HOH E 3 .   ? 22.438  -3.666  52.240 1.00 33.37 ? 693 HOH B O   1 
HETATM 5018 O O   . HOH E 3 .   ? 37.106  -5.681  58.182 1.00 44.14 ? 694 HOH B O   1 
HETATM 5019 O O   . HOH E 3 .   ? 25.367  -3.011  57.009 1.00 44.66 ? 695 HOH B O   1 
HETATM 5020 O O   . HOH E 3 .   ? 1.508   -10.367 37.401 1.00 42.72 ? 696 HOH B O   1 
HETATM 5021 O O   . HOH E 3 .   ? 25.461  -10.837 27.068 1.00 41.03 ? 697 HOH B O   1 
HETATM 5022 O O   . HOH E 3 .   ? 19.456  -21.676 33.569 1.00 37.82 ? 698 HOH B O   1 
HETATM 5023 O O   . HOH E 3 .   ? -15.166 -29.369 14.043 1.00 32.18 ? 699 HOH B O   1 
HETATM 5024 O O   . HOH E 3 .   ? -12.583 -7.518  17.356 1.00 42.29 ? 700 HOH B O   1 
HETATM 5025 O O   . HOH E 3 .   ? 18.530  -15.455 31.651 1.00 32.60 ? 701 HOH B O   1 
HETATM 5026 O O   . HOH E 3 .   ? 3.843   -21.784 31.961 1.00 40.41 ? 702 HOH B O   1 
HETATM 5027 O O   . HOH E 3 .   ? 17.522  -11.170 18.987 1.00 37.13 ? 703 HOH B O   1 
HETATM 5028 O O   . HOH E 3 .   ? 16.619  -13.954 56.493 1.00 35.73 ? 704 HOH B O   1 
HETATM 5029 O O   . HOH E 3 .   ? -0.927  -23.690 15.795 1.00 43.50 ? 705 HOH B O   1 
HETATM 5030 O O   . HOH E 3 .   ? 31.364  -18.370 52.449 1.00 37.01 ? 706 HOH B O   1 
HETATM 5031 O O   . HOH E 3 .   ? 36.023  -11.306 45.414 1.00 25.48 ? 707 HOH B O   1 
HETATM 5032 O O   . HOH E 3 .   ? 0.442   -10.008 39.505 1.00 45.56 ? 708 HOH B O   1 
HETATM 5033 O O   . HOH E 3 .   ? 36.055  -12.883 39.407 1.00 29.85 ? 709 HOH B O   1 
HETATM 5034 O O   . HOH E 3 .   ? 31.505  -21.311 42.443 1.00 27.60 ? 710 HOH B O   1 
HETATM 5035 O O   . HOH E 3 .   ? 30.828  -23.986 41.752 1.00 31.87 ? 711 HOH B O   1 
HETATM 5036 O O   . HOH E 3 .   ? -5.326  -23.052 5.828  1.00 40.24 ? 712 HOH B O   1 
HETATM 5037 O O   . HOH E 3 .   ? 33.281  -20.087 46.434 1.00 30.26 ? 713 HOH B O   1 
HETATM 5038 O O   . HOH E 3 .   ? 37.559  -7.672  54.379 1.00 32.28 ? 714 HOH B O   1 
HETATM 5039 O O   . HOH E 3 .   ? -9.416  -14.674 36.972 1.00 38.47 ? 715 HOH B O   1 
HETATM 5040 O O   . HOH E 3 .   ? 34.717  -13.815 35.173 1.00 30.10 ? 716 HOH B O   1 
HETATM 5041 O O   . HOH E 3 .   ? 37.885  -5.207  55.486 1.00 31.00 ? 717 HOH B O   1 
HETATM 5042 O O   . HOH E 3 .   ? 32.735  -17.589 40.628 1.00 24.52 ? 718 HOH B O   1 
HETATM 5043 O O   . HOH E 3 .   ? 11.833  -24.022 43.619 1.00 44.85 ? 719 HOH B O   1 
HETATM 5044 O O   . HOH E 3 .   ? 11.656  -10.551 47.698 1.00 38.76 ? 720 HOH B O   1 
HETATM 5045 O O   . HOH E 3 .   ? 27.921  -7.157  24.800 1.00 39.59 ? 721 HOH B O   1 
HETATM 5046 O O   . HOH E 3 .   ? -15.903 -6.664  23.045 1.00 47.24 ? 722 HOH B O   1 
HETATM 5047 O O   . HOH F 3 .   ? 29.951  19.412  5.723  1.00 31.59 ? 501 HOH A O   1 
HETATM 5048 O O   . HOH F 3 .   ? 26.855  13.098  37.162 1.00 27.63 ? 502 HOH A O   1 
HETATM 5049 O O   . HOH F 3 .   ? 13.275  29.854  24.062 1.00 27.03 ? 503 HOH A O   1 
HETATM 5050 O O   . HOH F 3 .   ? 36.937  21.884  11.413 1.00 36.78 ? 504 HOH A O   1 
HETATM 5051 O O   . HOH F 3 .   ? 26.838  34.238  24.162 1.00 32.58 ? 505 HOH A O   1 
HETATM 5052 O O   . HOH F 3 .   ? 10.434  9.227   32.905 1.00 23.25 ? 506 HOH A O   1 
HETATM 5053 O O   . HOH F 3 .   ? 6.658   10.191  47.577 1.00 27.87 ? 507 HOH A O   1 
HETATM 5054 O O   . HOH F 3 .   ? -13.850 3.729   40.105 1.00 39.01 ? 508 HOH A O   1 
HETATM 5055 O O   . HOH F 3 .   ? 33.536  20.478  22.219 1.00 41.80 ? 509 HOH A O   1 
HETATM 5056 O O   . HOH F 3 .   ? -2.391  4.016   56.177 1.00 33.64 ? 510 HOH A O   1 
HETATM 5057 O O   . HOH F 3 .   ? 32.158  32.959  12.219 1.00 31.46 ? 511 HOH A O   1 
HETATM 5058 O O   . HOH F 3 .   ? -16.152 7.524   44.127 1.00 33.18 ? 512 HOH A O   1 
HETATM 5059 O O   . HOH F 3 .   ? -4.274  6.044   51.086 1.00 22.14 ? 513 HOH A O   1 
HETATM 5060 O O   . HOH F 3 .   ? -15.176 10.542  44.765 1.00 26.18 ? 514 HOH A O   1 
HETATM 5061 O O   . HOH F 3 .   ? 31.499  24.838  3.309  1.00 31.70 ? 515 HOH A O   1 
HETATM 5062 O O   . HOH F 3 .   ? 22.680  6.949   25.909 1.00 25.47 ? 516 HOH A O   1 
HETATM 5063 O O   . HOH F 3 .   ? 10.386  2.899   40.941 1.00 36.60 ? 517 HOH A O   1 
HETATM 5064 O O   . HOH F 3 .   ? -9.442  18.808  54.949 1.00 29.98 ? 518 HOH A O   1 
HETATM 5065 O O   . HOH F 3 .   ? -4.113  -3.397  33.612 1.00 30.82 ? 519 HOH A O   1 
HETATM 5066 O O   . HOH F 3 .   ? -10.019 8.735   49.077 1.00 28.02 ? 520 HOH A O   1 
HETATM 5067 O O   . HOH F 3 .   ? -7.908  26.928  37.851 1.00 23.89 ? 521 HOH A O   1 
HETATM 5068 O O   . HOH F 3 .   ? 15.314  27.630  5.996  1.00 40.42 ? 522 HOH A O   1 
HETATM 5069 O O   . HOH F 3 .   ? -0.499  25.420  38.171 1.00 23.13 ? 523 HOH A O   1 
HETATM 5070 O O   . HOH F 3 .   ? 4.153   -5.221  54.596 1.00 35.45 ? 524 HOH A O   1 
HETATM 5071 O O   . HOH F 3 .   ? 7.287   22.008  48.167 1.00 27.84 ? 525 HOH A O   1 
HETATM 5072 O O   . HOH F 3 .   ? 37.889  26.634  18.611 1.00 34.50 ? 526 HOH A O   1 
HETATM 5073 O O   . HOH F 3 .   ? 2.370   14.933  28.584 1.00 26.09 ? 527 HOH A O   1 
HETATM 5074 O O   . HOH F 3 .   ? 18.119  12.770  19.156 1.00 18.92 ? 528 HOH A O   1 
HETATM 5075 O O   . HOH F 3 .   ? 17.337  30.134  29.771 1.00 30.66 ? 529 HOH A O   1 
HETATM 5076 O O   . HOH F 3 .   ? 3.497   18.057  18.436 1.00 40.06 ? 530 HOH A O   1 
HETATM 5077 O O   . HOH F 3 .   ? -1.015  -3.023  38.759 1.00 28.12 ? 531 HOH A O   1 
HETATM 5078 O O   . HOH F 3 .   ? 39.224  20.731  29.905 1.00 40.84 ? 532 HOH A O   1 
HETATM 5079 O O   . HOH F 3 .   ? 5.586   9.706   30.515 1.00 23.79 ? 533 HOH A O   1 
HETATM 5080 O O   . HOH F 3 .   ? -8.165  5.411   55.914 1.00 35.00 ? 534 HOH A O   1 
HETATM 5081 O O   . HOH F 3 .   ? 19.887  26.155  1.632  1.00 35.86 ? 535 HOH A O   1 
HETATM 5082 O O   . HOH F 3 .   ? -8.925  26.884  44.660 1.00 28.06 ? 536 HOH A O   1 
HETATM 5083 O O   . HOH F 3 .   ? 18.762  35.735  22.646 1.00 37.89 ? 537 HOH A O   1 
HETATM 5084 O O   . HOH F 3 .   ? 5.520   12.775  26.845 1.00 26.85 ? 538 HOH A O   1 
HETATM 5085 O O   . HOH F 3 .   ? 7.987   8.079   37.214 1.00 26.59 ? 539 HOH A O   1 
HETATM 5086 O O   . HOH F 3 .   ? 14.877  16.608  47.400 1.00 35.01 ? 540 HOH A O   1 
HETATM 5087 O O   . HOH F 3 .   ? -7.695  1.581   29.542 1.00 39.02 ? 541 HOH A O   1 
HETATM 5088 O O   . HOH F 3 .   ? 17.663  16.550  39.792 1.00 22.38 ? 542 HOH A O   1 
HETATM 5089 O O   . HOH F 3 .   ? 16.672  27.819  16.789 1.00 28.56 ? 543 HOH A O   1 
HETATM 5090 O O   . HOH F 3 .   ? 10.269  12.519  43.827 1.00 39.25 ? 544 HOH A O   1 
HETATM 5091 O O   . HOH F 3 .   ? 10.456  18.226  40.031 1.00 22.57 ? 545 HOH A O   1 
HETATM 5092 O O   . HOH F 3 .   ? 35.772  38.751  19.397 1.00 33.92 ? 546 HOH A O   1 
HETATM 5093 O O   . HOH F 3 .   ? 12.196  11.832  9.584  1.00 31.29 ? 547 HOH A O   1 
HETATM 5094 O O   . HOH F 3 .   ? 8.671   9.110   44.917 1.00 33.40 ? 548 HOH A O   1 
HETATM 5095 O O   . HOH F 3 .   ? 7.771   3.903   49.269 1.00 30.69 ? 549 HOH A O   1 
HETATM 5096 O O   . HOH F 3 .   ? 17.423  12.367  5.465  1.00 34.82 ? 550 HOH A O   1 
HETATM 5097 O O   . HOH F 3 .   ? 28.537  11.837  18.656 1.00 27.31 ? 551 HOH A O   1 
HETATM 5098 O O   . HOH F 3 .   ? 2.833   24.357  42.274 1.00 32.61 ? 552 HOH A O   1 
HETATM 5099 O O   . HOH F 3 .   ? -9.072  23.963  54.664 1.00 30.79 ? 553 HOH A O   1 
HETATM 5100 O O   . HOH F 3 .   ? -7.206  14.559  33.621 1.00 20.04 ? 554 HOH A O   1 
HETATM 5101 O O   . HOH F 3 .   ? -10.132 0.477   48.023 1.00 31.73 ? 555 HOH A O   1 
HETATM 5102 O O   . HOH F 3 .   ? 20.046  20.856  47.056 1.00 46.18 ? 556 HOH A O   1 
HETATM 5103 O O   . HOH F 3 .   ? -9.061  26.229  34.964 1.00 34.09 ? 557 HOH A O   1 
HETATM 5104 O O   . HOH F 3 .   ? 18.258  24.055  39.613 1.00 22.43 ? 558 HOH A O   1 
HETATM 5105 O O   . HOH F 3 .   ? 14.730  24.472  10.071 1.00 26.91 ? 559 HOH A O   1 
HETATM 5106 O O   . HOH F 3 .   ? 25.370  27.653  36.765 1.00 34.59 ? 560 HOH A O   1 
HETATM 5107 O O   . HOH F 3 .   ? 4.889   0.722   34.927 1.00 30.39 ? 561 HOH A O   1 
HETATM 5108 O O   . HOH F 3 .   ? 10.134  13.336  1.239  1.00 44.09 ? 562 HOH A O   1 
HETATM 5109 O O   . HOH F 3 .   ? 6.247   -0.009  49.077 1.00 28.45 ? 563 HOH A O   1 
HETATM 5110 O O   . HOH F 3 .   ? -6.357  -4.748  48.197 1.00 41.31 ? 564 HOH A O   1 
HETATM 5111 O O   . HOH F 3 .   ? -6.650  11.595  54.135 1.00 26.26 ? 565 HOH A O   1 
HETATM 5112 O O   . HOH F 3 .   ? 24.019  5.788   28.599 1.00 27.15 ? 566 HOH A O   1 
HETATM 5113 O O   . HOH F 3 .   ? 9.077   9.530   42.341 1.00 39.96 ? 567 HOH A O   1 
HETATM 5114 O O   . HOH F 3 .   ? 4.055   20.455  38.994 1.00 22.93 ? 568 HOH A O   1 
HETATM 5115 O O   . HOH F 3 .   ? -2.347  0.844   26.950 1.00 27.89 ? 569 HOH A O   1 
HETATM 5116 O O   . HOH F 3 .   ? 9.187   16.095  56.920 1.00 29.03 ? 570 HOH A O   1 
HETATM 5117 O O   . HOH F 3 .   ? 18.428  21.839  31.763 1.00 20.63 ? 571 HOH A O   1 
HETATM 5118 O O   . HOH F 3 .   ? -0.706  3.114   53.450 1.00 31.59 ? 572 HOH A O   1 
HETATM 5119 O O   . HOH F 3 .   ? -3.368  -0.538  29.070 1.00 29.35 ? 573 HOH A O   1 
HETATM 5120 O O   . HOH F 3 .   ? 36.075  18.623  28.362 1.00 39.94 ? 574 HOH A O   1 
HETATM 5121 O O   . HOH F 3 .   ? 7.123   -5.755  50.871 1.00 30.37 ? 575 HOH A O   1 
HETATM 5122 O O   . HOH F 3 .   ? 13.573  13.291  34.268 1.00 21.95 ? 576 HOH A O   1 
HETATM 5123 O O   . HOH F 3 .   ? 5.262   14.798  9.820  1.00 34.98 ? 577 HOH A O   1 
HETATM 5124 O O   . HOH F 3 .   ? -5.119  17.037  57.043 1.00 34.66 ? 578 HOH A O   1 
HETATM 5125 O O   . HOH F 3 .   ? 12.246  24.401  21.600 1.00 24.04 ? 579 HOH A O   1 
HETATM 5126 O O   . HOH F 3 .   ? 3.448   22.056  56.423 1.00 35.05 ? 580 HOH A O   1 
HETATM 5127 O O   . HOH F 3 .   ? 10.152  26.082  31.537 1.00 37.93 ? 581 HOH A O   1 
HETATM 5128 O O   . HOH F 3 .   ? 2.635   -5.613  46.286 1.00 30.95 ? 582 HOH A O   1 
HETATM 5129 O O   . HOH F 3 .   ? 28.655  20.605  38.066 1.00 29.55 ? 583 HOH A O   1 
HETATM 5130 O O   . HOH F 3 .   ? 5.227   9.048   14.661 1.00 40.09 ? 584 HOH A O   1 
HETATM 5131 O O   . HOH F 3 .   ? 9.344   1.256   30.453 1.00 20.73 ? 585 HOH A O   1 
HETATM 5132 O O   . HOH F 3 .   ? 2.473   17.865  34.906 1.00 19.67 ? 586 HOH A O   1 
HETATM 5133 O O   . HOH F 3 .   ? 4.760   2.332   55.348 1.00 36.60 ? 587 HOH A O   1 
HETATM 5134 O O   . HOH F 3 .   ? 26.657  24.345  24.036 1.00 20.48 ? 588 HOH A O   1 
HETATM 5135 O O   . HOH F 3 .   ? -12.973 8.843   49.054 1.00 36.07 ? 589 HOH A O   1 
HETATM 5136 O O   . HOH F 3 .   ? 6.189   9.836   52.915 1.00 35.43 ? 590 HOH A O   1 
HETATM 5137 O O   . HOH F 3 .   ? 30.572  35.541  16.867 1.00 30.51 ? 591 HOH A O   1 
HETATM 5138 O O   . HOH F 3 .   ? -12.158 20.977  38.068 1.00 29.72 ? 592 HOH A O   1 
HETATM 5139 O O   . HOH F 3 .   ? 10.667  11.026  41.496 1.00 34.29 ? 593 HOH A O   1 
HETATM 5140 O O   . HOH F 3 .   ? 30.690  14.867  11.094 1.00 31.47 ? 594 HOH A O   1 
HETATM 5141 O O   . HOH F 3 .   ? 2.615   14.854  24.749 1.00 43.77 ? 595 HOH A O   1 
HETATM 5142 O O   . HOH F 3 .   ? 4.414   16.675  28.129 1.00 26.72 ? 596 HOH A O   1 
HETATM 5143 O O   . HOH F 3 .   ? 24.844  33.358  21.859 1.00 29.86 ? 597 HOH A O   1 
HETATM 5144 O O   . HOH F 3 .   ? 22.597  17.733  40.378 1.00 30.24 ? 598 HOH A O   1 
HETATM 5145 O O   . HOH F 3 .   ? 32.552  14.769  0.325  1.00 45.49 ? 599 HOH A O   1 
HETATM 5146 O O   . HOH F 3 .   ? -12.729 1.092   44.978 1.00 29.88 ? 600 HOH A O   1 
HETATM 5147 O O   . HOH F 3 .   ? -9.795  22.541  44.927 1.00 20.93 ? 601 HOH A O   1 
HETATM 5148 O O   . HOH F 3 .   ? -15.691 14.739  47.390 1.00 30.42 ? 602 HOH A O   1 
HETATM 5149 O O   . HOH F 3 .   ? 23.763  10.712  10.201 1.00 34.59 ? 603 HOH A O   1 
HETATM 5150 O O   . HOH F 3 .   ? 27.967  30.475  1.232  1.00 41.55 ? 604 HOH A O   1 
HETATM 5151 O O   . HOH F 3 .   ? 14.656  28.046  33.261 1.00 27.31 ? 605 HOH A O   1 
HETATM 5152 O O   . HOH F 3 .   ? -6.973  -1.491  51.330 1.00 36.58 ? 606 HOH A O   1 
HETATM 5153 O O   . HOH F 3 .   ? 15.057  23.791  43.437 1.00 28.50 ? 607 HOH A O   1 
HETATM 5154 O O   . HOH F 3 .   ? 20.564  12.455  41.620 1.00 33.46 ? 608 HOH A O   1 
HETATM 5155 O O   . HOH F 3 .   ? 6.847   0.600   51.972 1.00 34.62 ? 609 HOH A O   1 
HETATM 5156 O O   . HOH F 3 .   ? 19.593  18.757  43.421 1.00 24.17 ? 610 HOH A O   1 
HETATM 5157 O O   . HOH F 3 .   ? 22.886  29.785  29.885 1.00 23.62 ? 611 HOH A O   1 
HETATM 5158 O O   . HOH F 3 .   ? 20.600  29.645  32.140 1.00 29.32 ? 612 HOH A O   1 
HETATM 5159 O O   . HOH F 3 .   ? 25.292  29.523  28.707 1.00 23.85 ? 613 HOH A O   1 
HETATM 5160 O O   . HOH F 3 .   ? 3.426   10.130  37.535 1.00 15.25 ? 614 HOH A O   1 
HETATM 5161 O O   . HOH F 3 .   ? -2.768  25.972  46.019 1.00 33.49 ? 615 HOH A O   1 
HETATM 5162 O O   . HOH F 3 .   ? -13.020 15.958  40.501 1.00 26.64 ? 616 HOH A O   1 
HETATM 5163 O O   . HOH F 3 .   ? 17.740  17.293  45.176 1.00 30.29 ? 617 HOH A O   1 
HETATM 5164 O O   . HOH F 3 .   ? 17.663  24.507  46.169 1.00 28.93 ? 618 HOH A O   1 
HETATM 5165 O O   . HOH F 3 .   ? -7.735  -2.589  34.427 1.00 25.45 ? 619 HOH A O   1 
HETATM 5166 O O   . HOH F 3 .   ? 23.463  19.604  42.073 1.00 24.23 ? 620 HOH A O   1 
HETATM 5167 O O   . HOH F 3 .   ? 8.636   26.416  15.812 1.00 29.83 ? 621 HOH A O   1 
HETATM 5168 O O   . HOH F 3 .   ? 6.661   21.905  10.008 1.00 43.70 ? 622 HOH A O   1 
HETATM 5169 O O   . HOH F 3 .   ? 17.725  34.496  25.762 1.00 39.29 ? 623 HOH A O   1 
HETATM 5170 O O   . HOH F 3 .   ? 12.400  21.351  42.767 1.00 27.18 ? 624 HOH A O   1 
HETATM 5171 O O   . HOH F 3 .   ? 21.690  34.809  20.466 1.00 36.89 ? 625 HOH A O   1 
HETATM 5172 O O   . HOH F 3 .   ? -1.660  2.874   24.636 1.00 33.15 ? 626 HOH A O   1 
HETATM 5173 O O   . HOH F 3 .   ? 38.650  17.914  31.259 1.00 27.90 ? 627 HOH A O   1 
HETATM 5174 O O   . HOH F 3 .   ? 5.823   -1.274  36.825 1.00 31.92 ? 628 HOH A O   1 
HETATM 5175 O O   . HOH F 3 .   ? 4.978   23.750  36.036 1.00 28.94 ? 629 HOH A O   1 
HETATM 5176 O O   . HOH F 3 .   ? -3.371  19.109  56.858 1.00 25.85 ? 630 HOH A O   1 
HETATM 5177 O O   . HOH F 3 .   ? 19.439  9.662   35.383 1.00 32.37 ? 631 HOH A O   1 
HETATM 5178 O O   . HOH F 3 .   ? 1.295   -3.234  41.884 1.00 25.69 ? 632 HOH A O   1 
HETATM 5179 O O   . HOH F 3 .   ? 30.472  33.273  25.417 1.00 31.83 ? 633 HOH A O   1 
HETATM 5180 O O   . HOH F 3 .   ? 38.683  29.224  9.520  1.00 36.43 ? 634 HOH A O   1 
HETATM 5181 O O   . HOH F 3 .   ? -3.780  15.112  58.206 1.00 42.34 ? 635 HOH A O   1 
HETATM 5182 O O   . HOH F 3 .   ? 20.756  29.824  28.059 1.00 21.61 ? 636 HOH A O   1 
HETATM 5183 O O   . HOH F 3 .   ? -4.598  27.587  43.259 1.00 26.89 ? 637 HOH A O   1 
HETATM 5184 O O   . HOH F 3 .   ? 7.023   27.318  23.492 1.00 25.79 ? 638 HOH A O   1 
HETATM 5185 O O   . HOH F 3 .   ? 7.556   18.852  23.249 1.00 23.44 ? 639 HOH A O   1 
HETATM 5186 O O   . HOH F 3 .   ? 32.782  17.939  26.273 1.00 34.53 ? 640 HOH A O   1 
HETATM 5187 O O   . HOH F 3 .   ? 7.850   24.934  11.959 1.00 40.42 ? 641 HOH A O   1 
HETATM 5188 O O   . HOH F 3 .   ? 27.227  32.575  7.610  1.00 30.85 ? 642 HOH A O   1 
HETATM 5189 O O   . HOH F 3 .   ? 23.728  26.480  38.842 1.00 34.12 ? 643 HOH A O   1 
HETATM 5190 O O   . HOH F 3 .   ? -12.462 17.316  43.784 1.00 22.23 ? 644 HOH A O   1 
HETATM 5191 O O   . HOH F 3 .   ? 37.563  31.359  24.493 1.00 32.73 ? 645 HOH A O   1 
HETATM 5192 O O   . HOH F 3 .   ? 11.936  28.204  31.904 1.00 30.85 ? 646 HOH A O   1 
HETATM 5193 O O   . HOH F 3 .   ? 4.435   2.415   37.799 1.00 23.09 ? 647 HOH A O   1 
HETATM 5194 O O   . HOH F 3 .   ? 32.210  17.869  23.711 1.00 35.26 ? 648 HOH A O   1 
HETATM 5195 O O   . HOH F 3 .   ? 26.335  34.342  14.928 1.00 31.68 ? 649 HOH A O   1 
HETATM 5196 O O   . HOH F 3 .   ? 13.999  25.122  41.117 1.00 26.31 ? 650 HOH A O   1 
HETATM 5197 O O   . HOH F 3 .   ? 38.159  23.953  12.712 1.00 41.28 ? 651 HOH A O   1 
HETATM 5198 O O   . HOH F 3 .   ? 28.118  32.799  26.927 1.00 36.66 ? 652 HOH A O   1 
HETATM 5199 O O   . HOH F 3 .   ? 31.195  11.212  19.293 1.00 36.08 ? 653 HOH A O   1 
HETATM 5200 O O   . HOH F 3 .   ? 17.789  20.077  -1.395 1.00 36.87 ? 654 HOH A O   1 
HETATM 5201 O O   . HOH F 3 .   ? -10.547 0.603   33.503 1.00 37.50 ? 655 HOH A O   1 
HETATM 5202 O O   . HOH F 3 .   ? 2.010   7.164   28.471 1.00 26.10 ? 656 HOH A O   1 
HETATM 5203 O O   . HOH F 3 .   ? 2.263   19.548  41.171 1.00 20.36 ? 657 HOH A O   1 
HETATM 5204 O O   . HOH F 3 .   ? 13.070  6.756   10.245 1.00 41.07 ? 658 HOH A O   1 
HETATM 5205 O O   . HOH F 3 .   ? 17.919  33.661  15.725 1.00 45.05 ? 659 HOH A O   1 
HETATM 5206 O O   . HOH F 3 .   ? -11.968 22.047  42.996 1.00 24.49 ? 660 HOH A O   1 
HETATM 5207 O O   . HOH F 3 .   ? 37.560  23.456  17.684 1.00 41.20 ? 661 HOH A O   1 
HETATM 5208 O O   . HOH F 3 .   ? 7.408   7.541   47.357 1.00 26.76 ? 662 HOH A O   1 
HETATM 5209 O O   . HOH F 3 .   ? -10.393 23.039  48.197 1.00 27.97 ? 663 HOH A O   1 
HETATM 5210 O O   . HOH F 3 .   ? -2.570  -6.212  44.931 1.00 34.94 ? 664 HOH A O   1 
HETATM 5211 O O   . HOH F 3 .   ? 4.743   7.177   29.292 1.00 21.17 ? 665 HOH A O   1 
HETATM 5212 O O   . HOH F 3 .   ? 37.927  33.225  27.422 1.00 39.13 ? 666 HOH A O   1 
HETATM 5213 O O   . HOH F 3 .   ? 2.124   -3.248  33.270 1.00 35.09 ? 667 HOH A O   1 
HETATM 5214 O O   . HOH F 3 .   ? 20.687  11.122  8.355  1.00 38.27 ? 668 HOH A O   1 
HETATM 5215 O O   . HOH F 3 .   ? 16.646  28.443  11.472 1.00 38.95 ? 669 HOH A O   1 
HETATM 5216 O O   . HOH F 3 .   ? -7.884  13.879  54.444 1.00 27.93 ? 670 HOH A O   1 
HETATM 5217 O O   . HOH F 3 .   ? 3.954   -5.801  42.048 1.00 35.68 ? 671 HOH A O   1 
HETATM 5218 O O   . HOH F 3 .   ? -8.596  25.081  50.290 1.00 29.09 ? 672 HOH A O   1 
HETATM 5219 O O   . HOH F 3 .   ? 14.157  31.259  16.608 1.00 37.90 ? 673 HOH A O   1 
HETATM 5220 O O   . HOH F 3 .   ? 28.606  32.441  4.885  1.00 33.18 ? 674 HOH A O   1 
HETATM 5221 O O   . HOH F 3 .   ? -4.150  27.776  39.814 1.00 26.38 ? 675 HOH A O   1 
HETATM 5222 O O   . HOH F 3 .   ? 3.526   20.112  36.294 1.00 26.74 ? 676 HOH A O   1 
HETATM 5223 O O   . HOH F 3 .   ? 18.385  10.623  7.574  1.00 42.11 ? 677 HOH A O   1 
HETATM 5224 O O   . HOH F 3 .   ? -1.402  27.919  38.428 1.00 32.76 ? 678 HOH A O   1 
HETATM 5225 O O   . HOH F 3 .   ? 31.437  29.270  2.104  1.00 40.24 ? 679 HOH A O   1 
HETATM 5226 O O   . HOH F 3 .   ? 14.730  8.559   40.510 1.00 31.24 ? 680 HOH A O   1 
HETATM 5227 O O   . HOH F 3 .   ? -7.335  28.002  34.274 1.00 38.86 ? 681 HOH A O   1 
HETATM 5228 O O   . HOH F 3 .   ? 5.015   7.436   50.799 1.00 40.54 ? 682 HOH A O   1 
HETATM 5229 O O   . HOH F 3 .   ? 34.077  28.116  4.059  1.00 37.94 ? 683 HOH A O   1 
HETATM 5230 O O   . HOH F 3 .   ? -0.949  16.879  31.129 1.00 24.76 ? 684 HOH A O   1 
HETATM 5231 O O   . HOH F 3 .   ? -8.755  16.403  55.942 1.00 40.95 ? 685 HOH A O   1 
HETATM 5232 O O   . HOH F 3 .   ? -12.221 20.170  35.478 1.00 28.39 ? 686 HOH A O   1 
HETATM 5233 O O   . HOH F 3 .   ? 6.811   18.121  62.138 1.00 28.13 ? 687 HOH A O   1 
HETATM 5234 O O   . HOH F 3 .   ? 11.898  9.280   8.900  1.00 34.79 ? 688 HOH A O   1 
HETATM 5235 O O   . HOH F 3 .   ? 32.191  31.388  6.362  1.00 38.71 ? 689 HOH A O   1 
HETATM 5236 O O   . HOH F 3 .   ? 35.792  14.686  21.280 1.00 42.03 ? 690 HOH A O   1 
HETATM 5237 O O   . HOH F 3 .   ? -15.751 6.276   32.233 1.00 35.58 ? 691 HOH A O   1 
HETATM 5238 O O   . HOH F 3 .   ? 28.954  29.939  29.100 1.00 32.99 ? 692 HOH A O   1 
HETATM 5239 O O   . HOH F 3 .   ? 16.265  14.441  40.196 1.00 29.31 ? 693 HOH A O   1 
HETATM 5240 O O   . HOH F 3 .   ? 15.073  30.404  31.975 1.00 36.01 ? 694 HOH A O   1 
HETATM 5241 O O   . HOH F 3 .   ? 11.666  27.205  22.125 1.00 33.42 ? 695 HOH A O   1 
HETATM 5242 O O   . HOH F 3 .   ? 9.930   13.097  52.223 1.00 36.40 ? 696 HOH A O   1 
HETATM 5243 O O   . HOH F 3 .   ? 0.795   21.539  35.220 1.00 32.01 ? 697 HOH A O   1 
HETATM 5244 O O   . HOH F 3 .   ? -2.990  3.824   52.188 1.00 28.68 ? 698 HOH A O   1 
HETATM 5245 O O   . HOH F 3 .   ? 1.237   18.502  57.908 1.00 33.19 ? 699 HOH A O   1 
HETATM 5246 O O   . HOH F 3 .   ? 16.029  29.066  36.133 1.00 33.00 ? 700 HOH A O   1 
HETATM 5247 O O   . HOH F 3 .   ? -10.802 23.202  56.681 1.00 39.94 ? 701 HOH A O   1 
HETATM 5248 O O   . HOH F 3 .   ? 24.840  33.383  7.751  1.00 38.28 ? 702 HOH A O   1 
HETATM 5249 O O   . HOH F 3 .   ? 2.184   25.274  39.016 1.00 28.63 ? 703 HOH A O   1 
HETATM 5250 O O   . HOH F 3 .   ? 28.969  20.972  42.229 1.00 39.32 ? 704 HOH A O   1 
HETATM 5251 O O   . HOH F 3 .   ? 1.264   -5.011  39.832 1.00 36.19 ? 705 HOH A O   1 
HETATM 5252 O O   . HOH F 3 .   ? 8.915   17.082  60.498 1.00 27.25 ? 706 HOH A O   1 
HETATM 5253 O O   . HOH F 3 .   ? -0.502  24.361  35.709 1.00 31.69 ? 707 HOH A O   1 
HETATM 5254 O O   . HOH F 3 .   ? 17.586  1.891   13.689 1.00 35.81 ? 708 HOH A O   1 
HETATM 5255 O O   . HOH F 3 .   ? -7.800  -3.836  46.382 1.00 35.12 ? 709 HOH A O   1 
HETATM 5256 O O   . HOH F 3 .   ? 34.776  16.658  22.843 1.00 38.12 ? 710 HOH A O   1 
HETATM 5257 O O   . HOH F 3 .   ? 5.106   19.823  23.650 1.00 32.88 ? 711 HOH A O   1 
HETATM 5258 O O   . HOH F 3 .   ? 40.360  19.574  30.305 1.00 42.26 ? 712 HOH A O   1 
HETATM 5259 O O   . HOH F 3 .   ? 5.774   25.896  39.458 1.00 36.36 ? 713 HOH A O   1 
HETATM 5260 O O   . HOH F 3 .   ? 19.970  16.997  41.362 1.00 27.98 ? 714 HOH A O   1 
HETATM 5261 O O   . HOH F 3 .   ? 12.555  13.958  44.855 1.00 46.81 ? 715 HOH A O   1 
HETATM 5262 O O   . HOH F 3 .   ? 26.547  31.727  29.298 1.00 31.34 ? 716 HOH A O   1 
HETATM 5263 O O   . HOH F 3 .   ? -0.953  0.361   53.796 1.00 31.88 ? 717 HOH A O   1 
HETATM 5264 O O   . HOH F 3 .   ? 29.028  23.507  42.929 1.00 34.26 ? 718 HOH A O   1 
HETATM 5265 O O   . HOH F 3 .   ? 41.985  17.561  29.708 1.00 38.05 ? 719 HOH A O   1 
HETATM 5266 O O   . HOH F 3 .   ? -6.532  14.700  30.814 1.00 38.17 ? 720 HOH A O   1 
HETATM 5267 O O   . HOH F 3 .   ? 16.084  25.891  44.751 1.00 33.40 ? 721 HOH A O   1 
HETATM 5268 O O   . HOH F 3 .   ? -9.117  -2.424  48.637 1.00 43.41 ? 722 HOH A O   1 
HETATM 5269 O O   . HOH F 3 .   ? 20.324  14.463  42.810 1.00 36.66 ? 723 HOH A O   1 
HETATM 5270 O O   . HOH F 3 .   ? 5.809   20.232  60.121 1.00 35.04 ? 724 HOH A O   1 
HETATM 5271 O O   . HOH F 3 .   ? 33.806  31.119  4.192  1.00 38.92 ? 725 HOH A O   1 
HETATM 5272 O O   . HOH F 3 .   ? 4.818   -4.076  58.491 1.00 39.21 ? 726 HOH A O   1 
HETATM 5273 O O   . HOH F 3 .   ? 40.144  28.108  32.199 1.00 46.93 ? 727 HOH A O   1 
HETATM 5274 O O   . HOH F 3 .   ? 26.583  17.314  44.413 1.00 35.01 ? 728 HOH A O   1 
HETATM 5275 O O   . HOH F 3 .   ? 6.163   25.837  36.974 1.00 36.26 ? 729 HOH A O   1 
HETATM 5276 O O   . HOH F 3 .   ? 25.946  30.473  -0.674 1.00 43.83 ? 730 HOH A O   1 
HETATM 5277 O O   . HOH F 3 .   ? 30.233  19.523  40.492 1.00 31.52 ? 731 HOH A O   1 
HETATM 5278 O O   . HOH F 3 .   ? 16.450  26.247  40.036 1.00 27.57 ? 732 HOH A O   1 
HETATM 5279 O O   . HOH F 3 .   ? 18.984  17.458  47.602 1.00 35.28 ? 733 HOH A O   1 
HETATM 5280 O O   . HOH F 3 .   ? 15.309  29.901  4.260  1.00 42.79 ? 734 HOH A O   1 
HETATM 5281 O O   . HOH F 3 .   ? 18.614  10.225  39.113 1.00 43.61 ? 735 HOH A O   1 
HETATM 5282 O O   . HOH F 3 .   ? 22.639  32.225  31.190 1.00 36.46 ? 736 HOH A O   1 
HETATM 5283 O O   . HOH F 3 .   ? 8.989   -3.610  52.235 1.00 38.19 ? 737 HOH A O   1 
HETATM 5284 O O   . HOH F 3 .   ? -9.992  29.078  43.513 1.00 43.98 ? 738 HOH A O   1 
HETATM 5285 O O   . HOH F 3 .   ? -9.166  28.960  38.967 1.00 42.57 ? 739 HOH A O   1 
HETATM 5286 O O   . HOH F 3 .   ? 17.397  27.089  42.626 1.00 33.35 ? 740 HOH A O   1 
HETATM 5287 O O   . HOH F 3 .   ? -1.219  19.244  58.379 1.00 35.87 ? 741 HOH A O   1 
HETATM 5288 O O   . HOH F 3 .   ? 35.155  16.091  28.244 1.00 33.19 ? 742 HOH A O   1 
HETATM 5289 O O   . HOH F 3 .   ? 15.968  28.340  38.666 1.00 33.45 ? 743 HOH A O   1 
HETATM 5290 O O   . HOH F 3 .   ? 15.773  13.549  44.102 1.00 40.71 ? 744 HOH A O   1 
HETATM 5291 O O   . HOH F 3 .   ? -14.696 17.215  45.658 1.00 30.18 ? 745 HOH A O   1 
HETATM 5292 O O   . HOH F 3 .   ? 29.853  16.399  41.218 1.00 32.35 ? 746 HOH A O   1 
HETATM 5293 O O   . HOH F 3 .   ? 9.052   26.819  37.180 1.00 37.48 ? 747 HOH A O   1 
HETATM 5294 O O   . HOH F 3 .   ? 18.095  14.948  44.279 1.00 38.07 ? 748 HOH A O   1 
HETATM 5295 O O   . HOH F 3 .   ? 17.908  12.206  40.749 1.00 31.68 ? 749 HOH A O   1 
HETATM 5296 O O   . HOH F 3 .   ? 8.844   11.241  53.125 1.00 40.62 ? 750 HOH A O   1 
HETATM 5297 O O   . HOH F 3 .   ? -0.397  19.046  32.568 1.00 33.60 ? 751 HOH A O   1 
HETATM 5298 O O   . HOH F 3 .   ? 9.200   10.278  55.474 1.00 37.79 ? 752 HOH A O   1 
HETATM 5299 O O   . HOH F 3 .   ? 29.177  17.084  43.638 1.00 32.85 ? 753 HOH A O   1 
# 
