data_8X9C
# 
_entry.id   8X9C 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8X9C         pdb_00008x9c 10.2210/pdb8x9c/pdb 
WWPDB D_1300042927 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8X9C 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jianhexu@ecust.edu.cn 
_pdbx_contact_author.name_first         Jian-He 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4301-7630 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, Z.Y.' 1 ? 
'Li, W.L.'    2 ? 
'Xu, J.H.'    3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Molecule insights of a dihydrated sesquiterpene synthase PeTS3' 
_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 'Huang, Z.Y.' 1 ? 
primary 'Li, W.L.'    2 ? 
primary 'Xu, J.H.'    3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer man 'Terpenoid synthase' 37705.867 2   ? ? ? ? 
2 water   nat water                18.015    418 ? ? ? ? 
# 
_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       
;MQVAPTSSPAGPVSAIPSVFETLQGYKVPVFFSRYPAGISIAAQEVEDALRKIDEEASEEGTRERRRALIRHTNPYGDPF
TICHCSAFPDRLALLSCLVEVMWIHDDVTEEMDHISACREHDELAKVLQLDIDPSKFESGNVRQKSLAVVLRKAIDIDPK
QAPAMIEMLRHYLATFDNIGGDFTRMEEYMPYRIANCGYWMSSYFIRWGMDMTLSEEEYASIEQFDIAMGNVLGLTNDYF
SWNIEKDQETDRMRNGVVVLMKEHHTTADAAKMMLLGVIVEQESLAAKLKEERLKKPASKEILQYFEAIELYVGGSCYWH
STAPRYQVFE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQVAPTSSPAGPVSAIPSVFETLQGYKVPVFFSRYPAGISIAAQEVEDALRKIDEEASEEGTRERRRALIRHTNPYGDPF
TICHCSAFPDRLALLSCLVEVMWIHDDVTEEMDHISACREHDELAKVLQLDIDPSKFESGNVRQKSLAVVLRKAIDIDPK
QAPAMIEMLRHYLATFDNIGGDFTRMEEYMPYRIANCGYWMSSYFIRWGMDMTLSEEEYASIEQFDIAMGNVLGLTNDYF
SWNIEKDQETDRMRNGVVVLMKEHHTTADAAKMMLLGVIVEQESLAAKLKEERLKKPASKEILQYFEAIELYVGGSCYWH
STAPRYQVFE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLN n 
1 3   VAL n 
1 4   ALA n 
1 5   PRO n 
1 6   THR n 
1 7   SER n 
1 8   SER n 
1 9   PRO n 
1 10  ALA n 
1 11  GLY n 
1 12  PRO n 
1 13  VAL n 
1 14  SER n 
1 15  ALA n 
1 16  ILE n 
1 17  PRO n 
1 18  SER n 
1 19  VAL n 
1 20  PHE n 
1 21  GLU n 
1 22  THR n 
1 23  LEU n 
1 24  GLN n 
1 25  GLY n 
1 26  TYR n 
1 27  LYS n 
1 28  VAL n 
1 29  PRO n 
1 30  VAL n 
1 31  PHE n 
1 32  PHE n 
1 33  SER n 
1 34  ARG n 
1 35  TYR n 
1 36  PRO n 
1 37  ALA n 
1 38  GLY n 
1 39  ILE n 
1 40  SER n 
1 41  ILE n 
1 42  ALA n 
1 43  ALA n 
1 44  GLN n 
1 45  GLU n 
1 46  VAL n 
1 47  GLU n 
1 48  ASP n 
1 49  ALA n 
1 50  LEU n 
1 51  ARG n 
1 52  LYS n 
1 53  ILE n 
1 54  ASP n 
1 55  GLU n 
1 56  GLU n 
1 57  ALA n 
1 58  SER n 
1 59  GLU n 
1 60  GLU n 
1 61  GLY n 
1 62  THR n 
1 63  ARG n 
1 64  GLU n 
1 65  ARG n 
1 66  ARG n 
1 67  ARG n 
1 68  ALA n 
1 69  LEU n 
1 70  ILE n 
1 71  ARG n 
1 72  HIS n 
1 73  THR n 
1 74  ASN n 
1 75  PRO n 
1 76  TYR n 
1 77  GLY n 
1 78  ASP n 
1 79  PRO n 
1 80  PHE n 
1 81  THR n 
1 82  ILE n 
1 83  CYS n 
1 84  HIS n 
1 85  CYS n 
1 86  SER n 
1 87  ALA n 
1 88  PHE n 
1 89  PRO n 
1 90  ASP n 
1 91  ARG n 
1 92  LEU n 
1 93  ALA n 
1 94  LEU n 
1 95  LEU n 
1 96  SER n 
1 97  CYS n 
1 98  LEU n 
1 99  VAL n 
1 100 GLU n 
1 101 VAL n 
1 102 MET n 
1 103 TRP n 
1 104 ILE n 
1 105 HIS n 
1 106 ASP n 
1 107 ASP n 
1 108 VAL n 
1 109 THR n 
1 110 GLU n 
1 111 GLU n 
1 112 MET n 
1 113 ASP n 
1 114 HIS n 
1 115 ILE n 
1 116 SER n 
1 117 ALA n 
1 118 CYS n 
1 119 ARG n 
1 120 GLU n 
1 121 HIS n 
1 122 ASP n 
1 123 GLU n 
1 124 LEU n 
1 125 ALA n 
1 126 LYS n 
1 127 VAL n 
1 128 LEU n 
1 129 GLN n 
1 130 LEU n 
1 131 ASP n 
1 132 ILE n 
1 133 ASP n 
1 134 PRO n 
1 135 SER n 
1 136 LYS n 
1 137 PHE n 
1 138 GLU n 
1 139 SER n 
1 140 GLY n 
1 141 ASN n 
1 142 VAL n 
1 143 ARG n 
1 144 GLN n 
1 145 LYS n 
1 146 SER n 
1 147 LEU n 
1 148 ALA n 
1 149 VAL n 
1 150 VAL n 
1 151 LEU n 
1 152 ARG n 
1 153 LYS n 
1 154 ALA n 
1 155 ILE n 
1 156 ASP n 
1 157 ILE n 
1 158 ASP n 
1 159 PRO n 
1 160 LYS n 
1 161 GLN n 
1 162 ALA n 
1 163 PRO n 
1 164 ALA n 
1 165 MET n 
1 166 ILE n 
1 167 GLU n 
1 168 MET n 
1 169 LEU n 
1 170 ARG n 
1 171 HIS n 
1 172 TYR n 
1 173 LEU n 
1 174 ALA n 
1 175 THR n 
1 176 PHE n 
1 177 ASP n 
1 178 ASN n 
1 179 ILE n 
1 180 GLY n 
1 181 GLY n 
1 182 ASP n 
1 183 PHE n 
1 184 THR n 
1 185 ARG n 
1 186 MET n 
1 187 GLU n 
1 188 GLU n 
1 189 TYR n 
1 190 MET n 
1 191 PRO n 
1 192 TYR n 
1 193 ARG n 
1 194 ILE n 
1 195 ALA n 
1 196 ASN n 
1 197 CYS n 
1 198 GLY n 
1 199 TYR n 
1 200 TRP n 
1 201 MET n 
1 202 SER n 
1 203 SER n 
1 204 TYR n 
1 205 PHE n 
1 206 ILE n 
1 207 ARG n 
1 208 TRP n 
1 209 GLY n 
1 210 MET n 
1 211 ASP n 
1 212 MET n 
1 213 THR n 
1 214 LEU n 
1 215 SER n 
1 216 GLU n 
1 217 GLU n 
1 218 GLU n 
1 219 TYR n 
1 220 ALA n 
1 221 SER n 
1 222 ILE n 
1 223 GLU n 
1 224 GLN n 
1 225 PHE n 
1 226 ASP n 
1 227 ILE n 
1 228 ALA n 
1 229 MET n 
1 230 GLY n 
1 231 ASN n 
1 232 VAL n 
1 233 LEU n 
1 234 GLY n 
1 235 LEU n 
1 236 THR n 
1 237 ASN n 
1 238 ASP n 
1 239 TYR n 
1 240 PHE n 
1 241 SER n 
1 242 TRP n 
1 243 ASN n 
1 244 ILE n 
1 245 GLU n 
1 246 LYS n 
1 247 ASP n 
1 248 GLN n 
1 249 GLU n 
1 250 THR n 
1 251 ASP n 
1 252 ARG n 
1 253 MET n 
1 254 ARG n 
1 255 ASN n 
1 256 GLY n 
1 257 VAL n 
1 258 VAL n 
1 259 VAL n 
1 260 LEU n 
1 261 MET n 
1 262 LYS n 
1 263 GLU n 
1 264 HIS n 
1 265 HIS n 
1 266 THR n 
1 267 THR n 
1 268 ALA n 
1 269 ASP n 
1 270 ALA n 
1 271 ALA n 
1 272 LYS n 
1 273 MET n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLY n 
1 278 VAL n 
1 279 ILE n 
1 280 VAL n 
1 281 GLU n 
1 282 GLN n 
1 283 GLU n 
1 284 SER n 
1 285 LEU n 
1 286 ALA n 
1 287 ALA n 
1 288 LYS n 
1 289 LEU n 
1 290 LYS n 
1 291 GLU n 
1 292 GLU n 
1 293 ARG n 
1 294 LEU n 
1 295 LYS n 
1 296 LYS n 
1 297 PRO n 
1 298 ALA n 
1 299 SER n 
1 300 LYS n 
1 301 GLU n 
1 302 ILE n 
1 303 LEU n 
1 304 GLN n 
1 305 TYR n 
1 306 PHE n 
1 307 GLU n 
1 308 ALA n 
1 309 ILE n 
1 310 GLU n 
1 311 LEU n 
1 312 TYR n 
1 313 VAL n 
1 314 GLY n 
1 315 GLY n 
1 316 SER n 
1 317 CYS n 
1 318 TYR n 
1 319 TRP n 
1 320 HIS n 
1 321 SER n 
1 322 THR n 
1 323 ALA n 
1 324 PRO n 
1 325 ARG n 
1 326 TYR n 
1 327 GLN n 
1 328 VAL n 
1 329 PHE n 
1 330 GLU 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                   330 
_entity_src_gen.gene_src_common_name               'Blue mold rot fungus' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PEX2_005160 
_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      'Penicillium expansum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     27334 
_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 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   ?   ?   ?   A . n 
A 1 4   ALA 4   4   ?   ?   ?   A . n 
A 1 5   PRO 5   5   ?   ?   ?   A . n 
A 1 6   THR 6   6   ?   ?   ?   A . n 
A 1 7   SER 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   PRO 9   9   ?   ?   ?   A . n 
A 1 10  ALA 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  PRO 12  12  ?   ?   ?   A . n 
A 1 13  VAL 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  ILE 16  16  16  ILE ILE A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  TYR 26  26  26  TYR TYR A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  ILE 39  39  39  ILE ILE A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  ARG 71  71  71  ARG ARG A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  PHE 80  80  80  PHE PHE A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  CYS 83  83  83  CYS CYS A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  PHE 88  88  88  PHE PHE A . n 
A 1 89  PRO 89  89  89  PRO PRO A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  SER 96  96  96  SER SER A . n 
A 1 97  CYS 97  97  97  CYS CYS A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 MET 102 102 102 MET MET A . n 
A 1 103 TRP 103 103 103 TRP TRP A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 MET 112 112 112 MET MET A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 HIS 114 114 114 HIS HIS A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 CYS 118 118 118 CYS CYS A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ASN 141 141 141 ASN ASN A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 SER 146 146 146 SER SER A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 MET 168 168 168 MET MET A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 ARG 170 170 170 ARG ARG A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 TYR 172 172 172 TYR TYR A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 ASP 177 177 177 ASP ASP A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 GLU 188 188 188 GLU GLU A . n 
A 1 189 TYR 189 189 189 TYR TYR A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 ILE 194 194 194 ILE ILE A . n 
A 1 195 ALA 195 195 195 ALA ALA A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 CYS 197 197 197 CYS CYS A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 MET 201 201 201 MET MET A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 TYR 204 204 204 TYR TYR A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 MET 212 212 212 MET MET A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 GLU 217 217 217 GLU GLU A . n 
A 1 218 GLU 218 218 218 GLU GLU A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 GLU 223 223 223 GLU GLU A . n 
A 1 224 GLN 224 224 224 GLN GLN A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 LEU 233 233 233 LEU LEU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 LEU 235 235 235 LEU LEU A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 ASN 237 237 237 ASN ASN A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 PHE 240 240 240 PHE PHE A . n 
A 1 241 SER 241 241 241 SER SER A . n 
A 1 242 TRP 242 242 242 TRP TRP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 ILE 244 244 ?   ?   ?   A . n 
A 1 245 GLU 245 245 ?   ?   ?   A . n 
A 1 246 LYS 246 246 ?   ?   ?   A . n 
A 1 247 ASP 247 247 ?   ?   ?   A . n 
A 1 248 GLN 248 248 ?   ?   ?   A . n 
A 1 249 GLU 249 249 ?   ?   ?   A . n 
A 1 250 THR 250 250 ?   ?   ?   A . n 
A 1 251 ASP 251 251 ?   ?   ?   A . n 
A 1 252 ARG 252 252 ?   ?   ?   A . n 
A 1 253 MET 253 253 ?   ?   ?   A . n 
A 1 254 ARG 254 254 254 ARG ARG A . n 
A 1 255 ASN 255 255 255 ASN ASN A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 VAL 258 258 258 VAL VAL A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 MET 261 261 261 MET MET A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 HIS 264 264 264 HIS HIS A . n 
A 1 265 HIS 265 265 265 HIS HIS A . n 
A 1 266 THR 266 266 266 THR THR A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 ALA 270 270 270 ALA ALA A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 MET 273 273 273 MET MET A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 GLN 282 282 282 GLN GLN A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 LYS 290 290 290 LYS LYS A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 GLU 292 292 292 GLU GLU A . n 
A 1 293 ARG 293 293 293 ARG ARG A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 LYS 295 295 295 LYS LYS A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 PRO 297 297 297 PRO PRO A . n 
A 1 298 ALA 298 298 298 ALA ALA A . n 
A 1 299 SER 299 299 299 SER SER A . n 
A 1 300 LYS 300 300 300 LYS LYS A . n 
A 1 301 GLU 301 301 301 GLU GLU A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 LEU 303 303 303 LEU LEU A . n 
A 1 304 GLN 304 304 304 GLN GLN A . n 
A 1 305 TYR 305 305 305 TYR TYR A . n 
A 1 306 PHE 306 306 306 PHE PHE A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 ALA 308 308 308 ALA ALA A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 GLU 310 310 310 GLU GLU A . n 
A 1 311 LEU 311 311 311 LEU LEU A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 VAL 313 313 313 VAL VAL A . n 
A 1 314 GLY 314 314 314 GLY GLY A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 SER 316 316 316 SER SER A . n 
A 1 317 CYS 317 317 317 CYS CYS A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 TRP 319 319 319 TRP TRP A . n 
A 1 320 HIS 320 320 320 HIS HIS A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 THR 322 322 322 THR THR A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 PRO 324 324 324 PRO PRO A . n 
A 1 325 ARG 325 325 ?   ?   ?   A . n 
A 1 326 TYR 326 326 ?   ?   ?   A . n 
A 1 327 GLN 327 327 ?   ?   ?   A . n 
A 1 328 VAL 328 328 ?   ?   ?   A . n 
A 1 329 PHE 329 329 ?   ?   ?   A . n 
A 1 330 GLU 330 330 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLN 2   2   ?   ?   ?   B . n 
B 1 3   VAL 3   3   ?   ?   ?   B . n 
B 1 4   ALA 4   4   ?   ?   ?   B . n 
B 1 5   PRO 5   5   ?   ?   ?   B . n 
B 1 6   THR 6   6   ?   ?   ?   B . n 
B 1 7   SER 7   7   ?   ?   ?   B . n 
B 1 8   SER 8   8   ?   ?   ?   B . n 
B 1 9   PRO 9   9   ?   ?   ?   B . n 
B 1 10  ALA 10  10  ?   ?   ?   B . n 
B 1 11  GLY 11  11  ?   ?   ?   B . n 
B 1 12  PRO 12  12  ?   ?   ?   B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  ILE 16  16  16  ILE ILE B . n 
B 1 17  PRO 17  17  17  PRO PRO B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  TYR 26  26  26  TYR TYR B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  PRO 36  36  36  PRO PRO B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  ILE 39  39  39  ILE ILE B . n 
B 1 40  SER 40  40  40  SER SER B . n 
B 1 41  ILE 41  41  41  ILE ILE B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  ASP 54  54  54  ASP ASP B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ARG 63  63  63  ARG ARG B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  ARG 65  65  65  ARG ARG B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  ARG 67  67  67  ARG ARG B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  ARG 71  71  71  ARG ARG B . n 
B 1 72  HIS 72  72  72  HIS HIS B . n 
B 1 73  THR 73  73  73  THR THR B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  PRO 75  75  75  PRO PRO B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  PRO 79  79  79  PRO PRO B . n 
B 1 80  PHE 80  80  80  PHE PHE B . n 
B 1 81  THR 81  81  81  THR THR B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  CYS 83  83  83  CYS CYS B . n 
B 1 84  HIS 84  84  84  HIS HIS B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  PHE 88  88  88  PHE PHE B . n 
B 1 89  PRO 89  89  89  PRO PRO B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  SER 96  96  96  SER SER B . n 
B 1 97  CYS 97  97  97  CYS CYS B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 MET 102 102 102 MET MET B . n 
B 1 103 TRP 103 103 103 TRP TRP B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 ASP 106 106 106 ASP ASP B . n 
B 1 107 ASP 107 107 107 ASP ASP B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 MET 112 112 112 MET MET B . n 
B 1 113 ASP 113 113 113 ASP ASP B . n 
B 1 114 HIS 114 114 114 HIS HIS B . n 
B 1 115 ILE 115 115 115 ILE ILE B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 CYS 118 118 118 CYS CYS B . n 
B 1 119 ARG 119 119 119 ARG ARG B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 LEU 124 124 124 LEU LEU B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 ASP 131 131 131 ASP ASP B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 SER 135 135 135 SER SER B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ASN 141 141 141 ASN ASN B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 GLN 144 144 144 GLN GLN B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 SER 146 146 146 SER SER B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 ASP 158 158 158 ASP ASP B . n 
B 1 159 PRO 159 159 159 PRO PRO B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 ALA 162 162 162 ALA ALA B . n 
B 1 163 PRO 163 163 163 PRO PRO B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 MET 168 168 168 MET MET B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
B 1 170 ARG 170 170 170 ARG ARG B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 TYR 172 172 172 TYR TYR B . n 
B 1 173 LEU 173 173 173 LEU LEU B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 PHE 176 176 176 PHE PHE B . n 
B 1 177 ASP 177 177 177 ASP ASP B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 ASP 182 182 182 ASP ASP B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 ARG 185 185 185 ARG ARG B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 GLU 188 188 188 GLU GLU B . n 
B 1 189 TYR 189 189 189 TYR TYR B . n 
B 1 190 MET 190 190 190 MET MET B . n 
B 1 191 PRO 191 191 191 PRO PRO B . n 
B 1 192 TYR 192 192 192 TYR TYR B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 ILE 194 194 194 ILE ILE B . n 
B 1 195 ALA 195 195 195 ALA ALA B . n 
B 1 196 ASN 196 196 196 ASN ASN B . n 
B 1 197 CYS 197 197 197 CYS CYS B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 TYR 199 199 199 TYR TYR B . n 
B 1 200 TRP 200 200 200 TRP TRP B . n 
B 1 201 MET 201 201 201 MET MET B . n 
B 1 202 SER 202 202 202 SER SER B . n 
B 1 203 SER 203 203 203 SER SER B . n 
B 1 204 TYR 204 204 204 TYR TYR B . n 
B 1 205 PHE 205 205 205 PHE PHE B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 MET 210 210 210 MET MET B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 MET 212 212 212 MET MET B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 LEU 214 214 214 LEU LEU B . n 
B 1 215 SER 215 215 215 SER SER B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 GLU 217 217 217 GLU GLU B . n 
B 1 218 GLU 218 218 218 GLU GLU B . n 
B 1 219 TYR 219 219 219 TYR TYR B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 GLU 223 223 223 GLU GLU B . n 
B 1 224 GLN 224 224 224 GLN GLN B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 ILE 227 227 227 ILE ILE B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 VAL 232 232 232 VAL VAL B . n 
B 1 233 LEU 233 233 233 LEU LEU B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 LEU 235 235 235 LEU LEU B . n 
B 1 236 THR 236 236 236 THR THR B . n 
B 1 237 ASN 237 237 237 ASN ASN B . n 
B 1 238 ASP 238 238 238 ASP ASP B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 PHE 240 240 240 PHE PHE B . n 
B 1 241 SER 241 241 241 SER SER B . n 
B 1 242 TRP 242 242 242 TRP TRP B . n 
B 1 243 ASN 243 243 243 ASN ASN B . n 
B 1 244 ILE 244 244 ?   ?   ?   B . n 
B 1 245 GLU 245 245 ?   ?   ?   B . n 
B 1 246 LYS 246 246 ?   ?   ?   B . n 
B 1 247 ASP 247 247 ?   ?   ?   B . n 
B 1 248 GLN 248 248 ?   ?   ?   B . n 
B 1 249 GLU 249 249 ?   ?   ?   B . n 
B 1 250 THR 250 250 ?   ?   ?   B . n 
B 1 251 ASP 251 251 ?   ?   ?   B . n 
B 1 252 ARG 252 252 ?   ?   ?   B . n 
B 1 253 MET 253 253 ?   ?   ?   B . n 
B 1 254 ARG 254 254 ?   ?   ?   B . n 
B 1 255 ASN 255 255 255 ASN ASN B . n 
B 1 256 GLY 256 256 256 GLY GLY B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 VAL 258 258 258 VAL VAL B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 LEU 260 260 260 LEU LEU B . n 
B 1 261 MET 261 261 261 MET MET B . n 
B 1 262 LYS 262 262 262 LYS LYS B . n 
B 1 263 GLU 263 263 263 GLU GLU B . n 
B 1 264 HIS 264 264 264 HIS HIS B . n 
B 1 265 HIS 265 265 265 HIS HIS B . n 
B 1 266 THR 266 266 266 THR THR B . n 
B 1 267 THR 267 267 267 THR THR B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 ASP 269 269 269 ASP ASP B . n 
B 1 270 ALA 270 270 270 ALA ALA B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 MET 273 273 273 MET MET B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 VAL 278 278 278 VAL VAL B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 GLU 281 281 281 GLU GLU B . n 
B 1 282 GLN 282 282 282 GLN GLN B . n 
B 1 283 GLU 283 283 283 GLU GLU B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 ALA 286 286 286 ALA ALA B . n 
B 1 287 ALA 287 287 287 ALA ALA B . n 
B 1 288 LYS 288 288 288 LYS LYS B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 LYS 290 290 290 LYS LYS B . n 
B 1 291 GLU 291 291 291 GLU GLU B . n 
B 1 292 GLU 292 292 292 GLU GLU B . n 
B 1 293 ARG 293 293 293 ARG ARG B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 LYS 295 295 295 LYS LYS B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 PRO 297 297 297 PRO PRO B . n 
B 1 298 ALA 298 298 298 ALA ALA B . n 
B 1 299 SER 299 299 299 SER SER B . n 
B 1 300 LYS 300 300 300 LYS LYS B . n 
B 1 301 GLU 301 301 301 GLU GLU B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 LEU 303 303 303 LEU LEU B . n 
B 1 304 GLN 304 304 304 GLN GLN B . n 
B 1 305 TYR 305 305 305 TYR TYR B . n 
B 1 306 PHE 306 306 306 PHE PHE B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 ALA 308 308 308 ALA ALA B . n 
B 1 309 ILE 309 309 309 ILE ILE B . n 
B 1 310 GLU 310 310 310 GLU GLU B . n 
B 1 311 LEU 311 311 311 LEU LEU B . n 
B 1 312 TYR 312 312 312 TYR TYR B . n 
B 1 313 VAL 313 313 313 VAL VAL B . n 
B 1 314 GLY 314 314 314 GLY GLY B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 SER 316 316 316 SER SER B . n 
B 1 317 CYS 317 317 317 CYS CYS B . n 
B 1 318 TYR 318 318 318 TYR TYR B . n 
B 1 319 TRP 319 319 319 TRP TRP B . n 
B 1 320 HIS 320 320 320 HIS HIS B . n 
B 1 321 SER 321 321 321 SER SER B . n 
B 1 322 THR 322 322 322 THR THR B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 PRO 324 324 ?   ?   ?   B . n 
B 1 325 ARG 325 325 ?   ?   ?   B . n 
B 1 326 TYR 326 326 ?   ?   ?   B . n 
B 1 327 GLN 327 327 ?   ?   ?   B . n 
B 1 328 VAL 328 328 ?   ?   ?   B . n 
B 1 329 PHE 329 329 ?   ?   ?   B . n 
B 1 330 GLU 330 330 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1   401 100 HOH HOH A . 
C 2 HOH 2   402 416 HOH HOH A . 
C 2 HOH 3   403 130 HOH HOH A . 
C 2 HOH 4   404 7   HOH HOH A . 
C 2 HOH 5   405 364 HOH HOH A . 
C 2 HOH 6   406 407 HOH HOH A . 
C 2 HOH 7   407 181 HOH HOH A . 
C 2 HOH 8   408 180 HOH HOH A . 
C 2 HOH 9   409 305 HOH HOH A . 
C 2 HOH 10  410 74  HOH HOH A . 
C 2 HOH 11  411 408 HOH HOH A . 
C 2 HOH 12  412 132 HOH HOH A . 
C 2 HOH 13  413 15  HOH HOH A . 
C 2 HOH 14  414 241 HOH HOH A . 
C 2 HOH 15  415 311 HOH HOH A . 
C 2 HOH 16  416 189 HOH HOH A . 
C 2 HOH 17  417 199 HOH HOH A . 
C 2 HOH 18  418 373 HOH HOH A . 
C 2 HOH 19  419 99  HOH HOH A . 
C 2 HOH 20  420 229 HOH HOH A . 
C 2 HOH 21  421 194 HOH HOH A . 
C 2 HOH 22  422 276 HOH HOH A . 
C 2 HOH 23  423 171 HOH HOH A . 
C 2 HOH 24  424 29  HOH HOH A . 
C 2 HOH 25  425 184 HOH HOH A . 
C 2 HOH 26  426 25  HOH HOH A . 
C 2 HOH 27  427 87  HOH HOH A . 
C 2 HOH 28  428 139 HOH HOH A . 
C 2 HOH 29  429 32  HOH HOH A . 
C 2 HOH 30  430 267 HOH HOH A . 
C 2 HOH 31  431 35  HOH HOH A . 
C 2 HOH 32  432 48  HOH HOH A . 
C 2 HOH 33  433 17  HOH HOH A . 
C 2 HOH 34  434 46  HOH HOH A . 
C 2 HOH 35  435 24  HOH HOH A . 
C 2 HOH 36  436 164 HOH HOH A . 
C 2 HOH 37  437 270 HOH HOH A . 
C 2 HOH 38  438 62  HOH HOH A . 
C 2 HOH 39  439 34  HOH HOH A . 
C 2 HOH 40  440 81  HOH HOH A . 
C 2 HOH 41  441 41  HOH HOH A . 
C 2 HOH 42  442 84  HOH HOH A . 
C 2 HOH 43  443 157 HOH HOH A . 
C 2 HOH 44  444 23  HOH HOH A . 
C 2 HOH 45  445 4   HOH HOH A . 
C 2 HOH 46  446 327 HOH HOH A . 
C 2 HOH 47  447 98  HOH HOH A . 
C 2 HOH 48  448 1   HOH HOH A . 
C 2 HOH 49  449 374 HOH HOH A . 
C 2 HOH 50  450 73  HOH HOH A . 
C 2 HOH 51  451 326 HOH HOH A . 
C 2 HOH 52  452 82  HOH HOH A . 
C 2 HOH 53  453 283 HOH HOH A . 
C 2 HOH 54  454 249 HOH HOH A . 
C 2 HOH 55  455 97  HOH HOH A . 
C 2 HOH 56  456 138 HOH HOH A . 
C 2 HOH 57  457 59  HOH HOH A . 
C 2 HOH 58  458 168 HOH HOH A . 
C 2 HOH 59  459 308 HOH HOH A . 
C 2 HOH 60  460 90  HOH HOH A . 
C 2 HOH 61  461 68  HOH HOH A . 
C 2 HOH 62  462 185 HOH HOH A . 
C 2 HOH 63  463 151 HOH HOH A . 
C 2 HOH 64  464 146 HOH HOH A . 
C 2 HOH 65  465 167 HOH HOH A . 
C 2 HOH 66  466 58  HOH HOH A . 
C 2 HOH 67  467 116 HOH HOH A . 
C 2 HOH 68  468 76  HOH HOH A . 
C 2 HOH 69  469 302 HOH HOH A . 
C 2 HOH 70  470 135 HOH HOH A . 
C 2 HOH 71  471 268 HOH HOH A . 
C 2 HOH 72  472 264 HOH HOH A . 
C 2 HOH 73  473 422 HOH HOH A . 
C 2 HOH 74  474 242 HOH HOH A . 
C 2 HOH 75  475 224 HOH HOH A . 
C 2 HOH 76  476 20  HOH HOH A . 
C 2 HOH 77  477 44  HOH HOH A . 
C 2 HOH 78  478 288 HOH HOH A . 
C 2 HOH 79  479 114 HOH HOH A . 
C 2 HOH 80  480 207 HOH HOH A . 
C 2 HOH 81  481 148 HOH HOH A . 
C 2 HOH 82  482 320 HOH HOH A . 
C 2 HOH 83  483 387 HOH HOH A . 
C 2 HOH 84  484 222 HOH HOH A . 
C 2 HOH 85  485 234 HOH HOH A . 
C 2 HOH 86  486 11  HOH HOH A . 
C 2 HOH 87  487 292 HOH HOH A . 
C 2 HOH 88  488 159 HOH HOH A . 
C 2 HOH 89  489 375 HOH HOH A . 
C 2 HOH 90  490 198 HOH HOH A . 
C 2 HOH 91  491 252 HOH HOH A . 
C 2 HOH 92  492 271 HOH HOH A . 
C 2 HOH 93  493 178 HOH HOH A . 
C 2 HOH 94  494 45  HOH HOH A . 
C 2 HOH 95  495 290 HOH HOH A . 
C 2 HOH 96  496 27  HOH HOH A . 
C 2 HOH 97  497 397 HOH HOH A . 
C 2 HOH 98  498 303 HOH HOH A . 
C 2 HOH 99  499 399 HOH HOH A . 
C 2 HOH 100 500 40  HOH HOH A . 
C 2 HOH 101 501 237 HOH HOH A . 
C 2 HOH 102 502 143 HOH HOH A . 
C 2 HOH 103 503 142 HOH HOH A . 
C 2 HOH 104 504 54  HOH HOH A . 
C 2 HOH 105 505 206 HOH HOH A . 
C 2 HOH 106 506 371 HOH HOH A . 
C 2 HOH 107 507 316 HOH HOH A . 
C 2 HOH 108 508 192 HOH HOH A . 
C 2 HOH 109 509 71  HOH HOH A . 
C 2 HOH 110 510 108 HOH HOH A . 
C 2 HOH 111 511 228 HOH HOH A . 
C 2 HOH 112 512 235 HOH HOH A . 
C 2 HOH 113 513 219 HOH HOH A . 
C 2 HOH 114 514 417 HOH HOH A . 
C 2 HOH 115 515 266 HOH HOH A . 
C 2 HOH 116 516 246 HOH HOH A . 
C 2 HOH 117 517 88  HOH HOH A . 
C 2 HOH 118 518 319 HOH HOH A . 
C 2 HOH 119 519 254 HOH HOH A . 
C 2 HOH 120 520 406 HOH HOH A . 
C 2 HOH 121 521 13  HOH HOH A . 
C 2 HOH 122 522 33  HOH HOH A . 
C 2 HOH 123 523 210 HOH HOH A . 
C 2 HOH 124 524 154 HOH HOH A . 
C 2 HOH 125 525 69  HOH HOH A . 
C 2 HOH 126 526 309 HOH HOH A . 
C 2 HOH 127 527 395 HOH HOH A . 
C 2 HOH 128 528 117 HOH HOH A . 
C 2 HOH 129 529 231 HOH HOH A . 
C 2 HOH 130 530 156 HOH HOH A . 
C 2 HOH 131 531 215 HOH HOH A . 
C 2 HOH 132 532 212 HOH HOH A . 
C 2 HOH 133 533 260 HOH HOH A . 
C 2 HOH 134 534 137 HOH HOH A . 
C 2 HOH 135 535 201 HOH HOH A . 
C 2 HOH 136 536 328 HOH HOH A . 
C 2 HOH 137 537 106 HOH HOH A . 
C 2 HOH 138 538 89  HOH HOH A . 
C 2 HOH 139 539 429 HOH HOH A . 
C 2 HOH 140 540 110 HOH HOH A . 
C 2 HOH 141 541 370 HOH HOH A . 
C 2 HOH 142 542 340 HOH HOH A . 
C 2 HOH 143 543 280 HOH HOH A . 
C 2 HOH 144 544 332 HOH HOH A . 
C 2 HOH 145 545 277 HOH HOH A . 
C 2 HOH 146 546 301 HOH HOH A . 
C 2 HOH 147 547 259 HOH HOH A . 
C 2 HOH 148 548 321 HOH HOH A . 
C 2 HOH 149 549 427 HOH HOH A . 
C 2 HOH 150 550 363 HOH HOH A . 
C 2 HOH 151 551 369 HOH HOH A . 
C 2 HOH 152 552 354 HOH HOH A . 
C 2 HOH 153 553 379 HOH HOH A . 
C 2 HOH 154 554 421 HOH HOH A . 
C 2 HOH 155 555 337 HOH HOH A . 
C 2 HOH 156 556 350 HOH HOH A . 
C 2 HOH 157 557 155 HOH HOH A . 
C 2 HOH 158 558 324 HOH HOH A . 
C 2 HOH 159 559 186 HOH HOH A . 
C 2 HOH 160 560 323 HOH HOH A . 
C 2 HOH 161 561 124 HOH HOH A . 
C 2 HOH 162 562 162 HOH HOH A . 
C 2 HOH 163 563 343 HOH HOH A . 
C 2 HOH 164 564 341 HOH HOH A . 
C 2 HOH 165 565 333 HOH HOH A . 
C 2 HOH 166 566 423 HOH HOH A . 
C 2 HOH 167 567 275 HOH HOH A . 
C 2 HOH 168 568 298 HOH HOH A . 
C 2 HOH 169 569 312 HOH HOH A . 
C 2 HOH 170 570 291 HOH HOH A . 
C 2 HOH 171 571 187 HOH HOH A . 
C 2 HOH 172 572 310 HOH HOH A . 
C 2 HOH 173 573 431 HOH HOH A . 
C 2 HOH 174 574 318 HOH HOH A . 
C 2 HOH 175 575 225 HOH HOH A . 
C 2 HOH 176 576 424 HOH HOH A . 
C 2 HOH 177 577 353 HOH HOH A . 
C 2 HOH 178 578 418 HOH HOH A . 
C 2 HOH 179 579 265 HOH HOH A . 
C 2 HOH 180 580 75  HOH HOH A . 
C 2 HOH 181 581 403 HOH HOH A . 
C 2 HOH 182 582 385 HOH HOH A . 
C 2 HOH 183 583 345 HOH HOH A . 
C 2 HOH 184 584 211 HOH HOH A . 
C 2 HOH 185 585 411 HOH HOH A . 
C 2 HOH 186 586 386 HOH HOH A . 
C 2 HOH 187 587 393 HOH HOH A . 
C 2 HOH 188 588 398 HOH HOH A . 
C 2 HOH 189 589 170 HOH HOH A . 
C 2 HOH 190 590 282 HOH HOH A . 
C 2 HOH 191 591 47  HOH HOH A . 
C 2 HOH 192 592 60  HOH HOH A . 
C 2 HOH 193 593 426 HOH HOH A . 
C 2 HOH 194 594 216 HOH HOH A . 
C 2 HOH 195 595 396 HOH HOH A . 
C 2 HOH 196 596 217 HOH HOH A . 
C 2 HOH 197 597 334 HOH HOH A . 
C 2 HOH 198 598 284 HOH HOH A . 
C 2 HOH 199 599 295 HOH HOH A . 
C 2 HOH 200 600 287 HOH HOH A . 
C 2 HOH 201 601 313 HOH HOH A . 
C 2 HOH 202 602 414 HOH HOH A . 
C 2 HOH 203 603 261 HOH HOH A . 
C 2 HOH 204 604 314 HOH HOH A . 
C 2 HOH 205 605 347 HOH HOH A . 
D 2 HOH 1   401 258 HOH HOH B . 
D 2 HOH 2   402 338 HOH HOH B . 
D 2 HOH 3   403 344 HOH HOH B . 
D 2 HOH 4   404 197 HOH HOH B . 
D 2 HOH 5   405 65  HOH HOH B . 
D 2 HOH 6   406 109 HOH HOH B . 
D 2 HOH 7   407 208 HOH HOH B . 
D 2 HOH 8   408 86  HOH HOH B . 
D 2 HOH 9   409 14  HOH HOH B . 
D 2 HOH 10  410 160 HOH HOH B . 
D 2 HOH 11  411 299 HOH HOH B . 
D 2 HOH 12  412 238 HOH HOH B . 
D 2 HOH 13  413 200 HOH HOH B . 
D 2 HOH 14  414 221 HOH HOH B . 
D 2 HOH 15  415 8   HOH HOH B . 
D 2 HOH 16  416 66  HOH HOH B . 
D 2 HOH 17  417 21  HOH HOH B . 
D 2 HOH 18  418 96  HOH HOH B . 
D 2 HOH 19  419 9   HOH HOH B . 
D 2 HOH 20  420 42  HOH HOH B . 
D 2 HOH 21  421 3   HOH HOH B . 
D 2 HOH 22  422 182 HOH HOH B . 
D 2 HOH 23  423 92  HOH HOH B . 
D 2 HOH 24  424 95  HOH HOH B . 
D 2 HOH 25  425 257 HOH HOH B . 
D 2 HOH 26  426 236 HOH HOH B . 
D 2 HOH 27  427 204 HOH HOH B . 
D 2 HOH 28  428 113 HOH HOH B . 
D 2 HOH 29  429 183 HOH HOH B . 
D 2 HOH 30  430 118 HOH HOH B . 
D 2 HOH 31  431 101 HOH HOH B . 
D 2 HOH 32  432 402 HOH HOH B . 
D 2 HOH 33  433 22  HOH HOH B . 
D 2 HOH 34  434 28  HOH HOH B . 
D 2 HOH 35  435 72  HOH HOH B . 
D 2 HOH 36  436 83  HOH HOH B . 
D 2 HOH 37  437 274 HOH HOH B . 
D 2 HOH 38  438 127 HOH HOH B . 
D 2 HOH 39  439 50  HOH HOH B . 
D 2 HOH 40  440 381 HOH HOH B . 
D 2 HOH 41  441 105 HOH HOH B . 
D 2 HOH 42  442 172 HOH HOH B . 
D 2 HOH 43  443 10  HOH HOH B . 
D 2 HOH 44  444 56  HOH HOH B . 
D 2 HOH 45  445 61  HOH HOH B . 
D 2 HOH 46  446 18  HOH HOH B . 
D 2 HOH 47  447 26  HOH HOH B . 
D 2 HOH 48  448 91  HOH HOH B . 
D 2 HOH 49  449 107 HOH HOH B . 
D 2 HOH 50  450 122 HOH HOH B . 
D 2 HOH 51  451 128 HOH HOH B . 
D 2 HOH 52  452 79  HOH HOH B . 
D 2 HOH 53  453 360 HOH HOH B . 
D 2 HOH 54  454 6   HOH HOH B . 
D 2 HOH 55  455 49  HOH HOH B . 
D 2 HOH 56  456 64  HOH HOH B . 
D 2 HOH 57  457 165 HOH HOH B . 
D 2 HOH 58  458 391 HOH HOH B . 
D 2 HOH 59  459 349 HOH HOH B . 
D 2 HOH 60  460 111 HOH HOH B . 
D 2 HOH 61  461 366 HOH HOH B . 
D 2 HOH 62  462 169 HOH HOH B . 
D 2 HOH 63  463 150 HOH HOH B . 
D 2 HOH 64  464 306 HOH HOH B . 
D 2 HOH 65  465 57  HOH HOH B . 
D 2 HOH 66  466 359 HOH HOH B . 
D 2 HOH 67  467 144 HOH HOH B . 
D 2 HOH 68  468 16  HOH HOH B . 
D 2 HOH 69  469 120 HOH HOH B . 
D 2 HOH 70  470 388 HOH HOH B . 
D 2 HOH 71  471 256 HOH HOH B . 
D 2 HOH 72  472 112 HOH HOH B . 
D 2 HOH 73  473 36  HOH HOH B . 
D 2 HOH 74  474 43  HOH HOH B . 
D 2 HOH 75  475 297 HOH HOH B . 
D 2 HOH 76  476 263 HOH HOH B . 
D 2 HOH 77  477 413 HOH HOH B . 
D 2 HOH 78  478 390 HOH HOH B . 
D 2 HOH 79  479 161 HOH HOH B . 
D 2 HOH 80  480 272 HOH HOH B . 
D 2 HOH 81  481 5   HOH HOH B . 
D 2 HOH 82  482 80  HOH HOH B . 
D 2 HOH 83  483 173 HOH HOH B . 
D 2 HOH 84  484 176 HOH HOH B . 
D 2 HOH 85  485 39  HOH HOH B . 
D 2 HOH 86  486 325 HOH HOH B . 
D 2 HOH 87  487 31  HOH HOH B . 
D 2 HOH 88  488 425 HOH HOH B . 
D 2 HOH 89  489 404 HOH HOH B . 
D 2 HOH 90  490 126 HOH HOH B . 
D 2 HOH 91  491 85  HOH HOH B . 
D 2 HOH 92  492 78  HOH HOH B . 
D 2 HOH 93  493 289 HOH HOH B . 
D 2 HOH 94  494 239 HOH HOH B . 
D 2 HOH 95  495 121 HOH HOH B . 
D 2 HOH 96  496 383 HOH HOH B . 
D 2 HOH 97  497 55  HOH HOH B . 
D 2 HOH 98  498 279 HOH HOH B . 
D 2 HOH 99  499 175 HOH HOH B . 
D 2 HOH 100 500 322 HOH HOH B . 
D 2 HOH 101 501 251 HOH HOH B . 
D 2 HOH 102 502 420 HOH HOH B . 
D 2 HOH 103 503 223 HOH HOH B . 
D 2 HOH 104 504 190 HOH HOH B . 
D 2 HOH 105 505 304 HOH HOH B . 
D 2 HOH 106 506 129 HOH HOH B . 
D 2 HOH 107 507 307 HOH HOH B . 
D 2 HOH 108 508 140 HOH HOH B . 
D 2 HOH 109 509 123 HOH HOH B . 
D 2 HOH 110 510 119 HOH HOH B . 
D 2 HOH 111 511 188 HOH HOH B . 
D 2 HOH 112 512 19  HOH HOH B . 
D 2 HOH 113 513 285 HOH HOH B . 
D 2 HOH 114 514 12  HOH HOH B . 
D 2 HOH 115 515 250 HOH HOH B . 
D 2 HOH 116 516 196 HOH HOH B . 
D 2 HOH 117 517 218 HOH HOH B . 
D 2 HOH 118 518 136 HOH HOH B . 
D 2 HOH 119 519 193 HOH HOH B . 
D 2 HOH 120 520 278 HOH HOH B . 
D 2 HOH 121 521 2   HOH HOH B . 
D 2 HOH 122 522 227 HOH HOH B . 
D 2 HOH 123 523 405 HOH HOH B . 
D 2 HOH 124 524 153 HOH HOH B . 
D 2 HOH 125 525 209 HOH HOH B . 
D 2 HOH 126 526 102 HOH HOH B . 
D 2 HOH 127 527 152 HOH HOH B . 
D 2 HOH 128 528 77  HOH HOH B . 
D 2 HOH 129 529 52  HOH HOH B . 
D 2 HOH 130 530 382 HOH HOH B . 
D 2 HOH 131 531 331 HOH HOH B . 
D 2 HOH 132 532 245 HOH HOH B . 
D 2 HOH 133 533 94  HOH HOH B . 
D 2 HOH 134 534 191 HOH HOH B . 
D 2 HOH 135 535 296 HOH HOH B . 
D 2 HOH 136 536 53  HOH HOH B . 
D 2 HOH 137 537 133 HOH HOH B . 
D 2 HOH 138 538 213 HOH HOH B . 
D 2 HOH 139 539 233 HOH HOH B . 
D 2 HOH 140 540 214 HOH HOH B . 
D 2 HOH 141 541 51  HOH HOH B . 
D 2 HOH 142 542 330 HOH HOH B . 
D 2 HOH 143 543 243 HOH HOH B . 
D 2 HOH 144 544 177 HOH HOH B . 
D 2 HOH 145 545 147 HOH HOH B . 
D 2 HOH 146 546 358 HOH HOH B . 
D 2 HOH 147 547 125 HOH HOH B . 
D 2 HOH 148 548 232 HOH HOH B . 
D 2 HOH 149 549 335 HOH HOH B . 
D 2 HOH 150 550 70  HOH HOH B . 
D 2 HOH 151 551 432 HOH HOH B . 
D 2 HOH 152 552 361 HOH HOH B . 
D 2 HOH 153 553 410 HOH HOH B . 
D 2 HOH 154 554 247 HOH HOH B . 
D 2 HOH 155 555 145 HOH HOH B . 
D 2 HOH 156 556 67  HOH HOH B . 
D 2 HOH 157 557 377 HOH HOH B . 
D 2 HOH 158 558 357 HOH HOH B . 
D 2 HOH 159 559 115 HOH HOH B . 
D 2 HOH 160 560 380 HOH HOH B . 
D 2 HOH 161 561 205 HOH HOH B . 
D 2 HOH 162 562 286 HOH HOH B . 
D 2 HOH 163 563 372 HOH HOH B . 
D 2 HOH 164 564 158 HOH HOH B . 
D 2 HOH 165 565 356 HOH HOH B . 
D 2 HOH 166 566 392 HOH HOH B . 
D 2 HOH 167 567 346 HOH HOH B . 
D 2 HOH 168 568 415 HOH HOH B . 
D 2 HOH 169 569 409 HOH HOH B . 
D 2 HOH 170 570 195 HOH HOH B . 
D 2 HOH 171 571 293 HOH HOH B . 
D 2 HOH 172 572 166 HOH HOH B . 
D 2 HOH 173 573 378 HOH HOH B . 
D 2 HOH 174 574 63  HOH HOH B . 
D 2 HOH 175 575 93  HOH HOH B . 
D 2 HOH 176 576 30  HOH HOH B . 
D 2 HOH 177 577 367 HOH HOH B . 
D 2 HOH 178 578 329 HOH HOH B . 
D 2 HOH 179 579 352 HOH HOH B . 
D 2 HOH 180 580 253 HOH HOH B . 
D 2 HOH 181 581 244 HOH HOH B . 
D 2 HOH 182 582 365 HOH HOH B . 
D 2 HOH 183 583 317 HOH HOH B . 
D 2 HOH 184 584 134 HOH HOH B . 
D 2 HOH 185 585 174 HOH HOH B . 
D 2 HOH 186 586 351 HOH HOH B . 
D 2 HOH 187 587 419 HOH HOH B . 
D 2 HOH 188 588 255 HOH HOH B . 
D 2 HOH 189 589 355 HOH HOH B . 
D 2 HOH 190 590 37  HOH HOH B . 
D 2 HOH 191 591 294 HOH HOH B . 
D 2 HOH 192 592 368 HOH HOH B . 
D 2 HOH 193 593 389 HOH HOH B . 
D 2 HOH 194 594 262 HOH HOH B . 
D 2 HOH 195 595 400 HOH HOH B . 
D 2 HOH 196 596 131 HOH HOH B . 
D 2 HOH 197 597 38  HOH HOH B . 
D 2 HOH 198 598 394 HOH HOH B . 
D 2 HOH 199 599 104 HOH HOH B . 
D 2 HOH 200 600 300 HOH HOH B . 
D 2 HOH 201 601 273 HOH HOH B . 
D 2 HOH 202 602 281 HOH HOH B . 
D 2 HOH 203 603 384 HOH HOH B . 
D 2 HOH 204 604 220 HOH HOH B . 
D 2 HOH 205 605 315 HOH HOH B . 
D 2 HOH 206 606 430 HOH HOH B . 
D 2 HOH 207 607 141 HOH HOH B . 
D 2 HOH 208 608 248 HOH HOH B . 
D 2 HOH 209 609 336 HOH HOH B . 
D 2 HOH 210 610 163 HOH HOH B . 
D 2 HOH 211 611 269 HOH HOH B . 
D 2 HOH 212 612 401 HOH HOH B . 
D 2 HOH 213 613 230 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? .                    2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                    3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .                    4 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? xia2        ? ? ? .                    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   111.53 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8X9C 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.650 
_cell.length_a_esd                 ? 
_cell.length_b                     118.960 
_cell.length_b_esd                 ? 
_cell.length_c                     65.600 
_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                         8X9C 
_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                   8X9C 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.75 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.23 
_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    
;20% v/v ethylene glycol, 10% w/v PEG8000, 0.2% w/v cytidine, 0.2% w/v inosine, 0.2% w/v ribavirin, 0.2% w/v thymidine, 0.2% w/v uridine, 0.1 M imidazole-MES monohydrate Buffer pH 6.5
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979183 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8X9C 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.68 
_reflns.d_resolution_low                               61.02 
_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                                     91596 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.045 
_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                                    1.68 
_reflns_shell.d_res_low                                     1.72 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6795 
_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                               5.6 
_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                                  0.731 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.8 
_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                                 8X9C 
_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                            1.68 
_refine.ls_d_res_low                             33.25 
_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                     91521 
_refine.ls_number_reflns_R_free                  4472 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.74 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1921 
_refine.ls_R_factor_R_free                       0.2090 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1912 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.04 
_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                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        33.25 
_refine_hist.number_atoms_solvent             418 
_refine_hist.number_atoms_total               5229 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 4934 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.904 ? 6672 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.545 ? 658  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052 ? 725  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 859  ? 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' 1.68 1.70  . . 141 2867 100.00 . . . . 0.3233 . . . . . . . . . . . 0.3369 
'X-RAY DIFFRACTION' 1.70 1.72  . . 140 2949 100.00 . . . . 0.3123 . . . . . . . . . . . 0.3608 
'X-RAY DIFFRACTION' 1.72 1.74  . . 147 2849 100.00 . . . . 0.2992 . . . . . . . . . . . 0.3429 
'X-RAY DIFFRACTION' 1.74 1.76  . . 144 2911 100.00 . . . . 0.2778 . . . . . . . . . . . 0.3221 
'X-RAY DIFFRACTION' 1.76 1.79  . . 159 2894 100.00 . . . . 0.2687 . . . . . . . . . . . 0.3002 
'X-RAY DIFFRACTION' 1.79 1.81  . . 152 2902 100.00 . . . . 0.2457 . . . . . . . . . . . 0.2794 
'X-RAY DIFFRACTION' 1.81 1.84  . . 169 2894 100.00 . . . . 0.2361 . . . . . . . . . . . 0.2902 
'X-RAY DIFFRACTION' 1.84 1.86  . . 165 2853 100.00 . . . . 0.2330 . . . . . . . . . . . 0.2490 
'X-RAY DIFFRACTION' 1.86 1.89  . . 153 2888 100.00 . . . . 0.2319 . . . . . . . . . . . 0.2717 
'X-RAY DIFFRACTION' 1.89 1.92  . . 138 2914 100.00 . . . . 0.2309 . . . . . . . . . . . 0.2580 
'X-RAY DIFFRACTION' 1.92 1.96  . . 131 2921 100.00 . . . . 0.2387 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.96 1.99  . . 152 2880 100.00 . . . . 0.2180 . . . . . . . . . . . 0.2498 
'X-RAY DIFFRACTION' 1.99 2.03  . . 142 2951 100.00 . . . . 0.2139 . . . . . . . . . . . 0.2969 
'X-RAY DIFFRACTION' 2.03 2.07  . . 150 2847 100.00 . . . . 0.2045 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 2.07 2.12  . . 157 2946 100.00 . . . . 0.2068 . . . . . . . . . . . 0.2087 
'X-RAY DIFFRACTION' 2.12 2.17  . . 148 2878 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2080 
'X-RAY DIFFRACTION' 2.17 2.22  . . 171 2853 100.00 . . . . 0.1950 . . . . . . . . . . . 0.2240 
'X-RAY DIFFRACTION' 2.22 2.28  . . 136 2933 100.00 . . . . 0.2048 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.28 2.35  . . 155 2917 100.00 . . . . 0.2043 . . . . . . . . . . . 0.2225 
'X-RAY DIFFRACTION' 2.35 2.42  . . 123 2903 100.00 . . . . 0.1951 . . . . . . . . . . . 0.2253 
'X-RAY DIFFRACTION' 2.42 2.51  . . 146 2911 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2226 
'X-RAY DIFFRACTION' 2.51 2.61  . . 144 2904 100.00 . . . . 0.2033 . . . . . . . . . . . 0.2233 
'X-RAY DIFFRACTION' 2.61 2.73  . . 144 2928 100.00 . . . . 0.2039 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 2.73 2.87  . . 157 2901 100.00 . . . . 0.1961 . . . . . . . . . . . 0.2142 
'X-RAY DIFFRACTION' 2.87 3.05  . . 185 2854 100.00 . . . . 0.2009 . . . . . . . . . . . 0.2125 
'X-RAY DIFFRACTION' 3.05 3.29  . . 142 2930 99.00  . . . . 0.1949 . . . . . . . . . . . 0.1758 
'X-RAY DIFFRACTION' 3.29 3.62  . . 133 2921 100.00 . . . . 0.1894 . . . . . . . . . . . 0.2069 
'X-RAY DIFFRACTION' 3.62 4.14  . . 159 2898 100.00 . . . . 0.1648 . . . . . . . . . . . 0.1737 
'X-RAY DIFFRACTION' 4.14 5.21  . . 132 2954 100.00 . . . . 0.1524 . . . . . . . . . . . 0.1878 
'X-RAY DIFFRACTION' 5.21 33.25 . . 157 2898 98.00  . . . . 0.1674 . . . . . . . . . . . 0.1720 
# 
_struct.entry_id                     8X9C 
_struct.title                        'Class I terpene synthase: eudesmanediol synthase (apo-PeTS3)' 
_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        8X9C 
_struct_keywords.text            'sesquiterpene, terpene synthase, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0A2JK86_PENEN 
_struct_ref.pdbx_db_accession          A0A0A2JK86 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MQVAPTSSPAGPVSAIPSVFETLQGYKVPVFFSRYPAGISIAAQEVEDALRKIDEEASEEGTRERRRALIRHTNPYGDPF
TICHCSAFPDRLALLSCLVEVMWIHDDVTEEMDHISACREHDELAKVLQLDIDPSKFESGNVRQKSLAVVLRKAIDIDPK
QAPAMIEMLRHYLATFDNIGGDFTRMEEYMPYRIANCGYWMSSYFIRWGMDMTLSEEEYASIEQFDIAMGNVLGLTNDYF
SWNIEKDQETDRMRNGVVVLMKEHHTTADAAKMMLLGVIVEQESLAAKLKEERLKKPASKEILQYFEAIELYVGGSCYWH
STAPRYQVFE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8X9C A 1 ? 330 ? A0A0A2JK86 1 ? 330 ? 1 330 
2 1 8X9C B 1 ? 330 ? A0A0A2JK86 1 ? 330 ? 1 330 
# 
_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)' 1760  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  25930 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 24  ? VAL A 28  ? GLN A 24  VAL A 28  5 ? 5  
HELX_P HELX_P2  AA2 ALA A 42  ? SER A 58  ? ALA A 42  SER A 58  1 ? 17 
HELX_P HELX_P3  AA3 THR A 62  ? HIS A 72  ? THR A 62  HIS A 72  1 ? 11 
HELX_P HELX_P4  AA4 ASP A 78  ? HIS A 84  ? ASP A 78  HIS A 84  1 ? 7  
HELX_P HELX_P5  AA5 PHE A 88  ? GLU A 111 ? PHE A 88  GLU A 111 1 ? 24 
HELX_P HELX_P6  AA6 ASP A 113 ? LYS A 126 ? ASP A 113 LYS A 126 1 ? 14 
HELX_P HELX_P7  AA7 ASP A 133 ? GLU A 138 ? ASP A 133 GLU A 138 5 ? 6  
HELX_P HELX_P8  AA8 ASN A 141 ? ASP A 158 ? ASN A 141 ASP A 158 1 ? 18 
HELX_P HELX_P9  AA9 GLN A 161 ? PHE A 176 ? GLN A 161 PHE A 176 1 ? 16 
HELX_P HELX_P10 AB1 ARG A 185 ? CYS A 197 ? ARG A 185 CYS A 197 1 ? 13 
HELX_P HELX_P11 AB2 GLY A 198 ? MET A 210 ? GLY A 198 MET A 210 1 ? 13 
HELX_P HELX_P12 AB3 SER A 215 ? SER A 221 ? SER A 215 SER A 221 1 ? 7  
HELX_P HELX_P13 AB4 ILE A 222 ? TRP A 242 ? ILE A 222 TRP A 242 1 ? 21 
HELX_P HELX_P14 AB5 ASN A 255 ? HIS A 265 ? ASN A 255 HIS A 265 1 ? 11 
HELX_P HELX_P15 AB6 THR A 267 ? LEU A 294 ? THR A 267 LEU A 294 1 ? 28 
HELX_P HELX_P16 AB7 SER A 299 ? ALA A 323 ? SER A 299 ALA A 323 1 ? 25 
HELX_P HELX_P17 AB8 GLN B 24  ? VAL B 28  ? GLN B 24  VAL B 28  5 ? 5  
HELX_P HELX_P18 AB9 ALA B 42  ? SER B 58  ? ALA B 42  SER B 58  1 ? 17 
HELX_P HELX_P19 AC1 THR B 62  ? HIS B 72  ? THR B 62  HIS B 72  1 ? 11 
HELX_P HELX_P20 AC2 ASP B 78  ? HIS B 84  ? ASP B 78  HIS B 84  1 ? 7  
HELX_P HELX_P21 AC3 PHE B 88  ? GLU B 111 ? PHE B 88  GLU B 111 1 ? 24 
HELX_P HELX_P22 AC4 ASP B 113 ? LYS B 126 ? ASP B 113 LYS B 126 1 ? 14 
HELX_P HELX_P23 AC5 ASP B 133 ? GLU B 138 ? ASP B 133 GLU B 138 5 ? 6  
HELX_P HELX_P24 AC6 ASN B 141 ? ASP B 158 ? ASN B 141 ASP B 158 1 ? 18 
HELX_P HELX_P25 AC7 GLN B 161 ? PHE B 176 ? GLN B 161 PHE B 176 1 ? 16 
HELX_P HELX_P26 AC8 ARG B 185 ? CYS B 197 ? ARG B 185 CYS B 197 1 ? 13 
HELX_P HELX_P27 AC9 GLY B 198 ? MET B 210 ? GLY B 198 MET B 210 1 ? 13 
HELX_P HELX_P28 AD1 SER B 215 ? SER B 221 ? SER B 215 SER B 221 1 ? 7  
HELX_P HELX_P29 AD2 ILE B 222 ? TRP B 242 ? ILE B 222 TRP B 242 1 ? 21 
HELX_P HELX_P30 AD3 GLY B 256 ? HIS B 265 ? GLY B 256 HIS B 265 1 ? 10 
HELX_P HELX_P31 AD4 THR B 267 ? LEU B 294 ? THR B 267 LEU B 294 1 ? 28 
HELX_P HELX_P32 AD5 SER B 299 ? ALA B 323 ? SER B 299 ALA B 323 1 ? 25 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
# 
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 
AA2 1 2 ? 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 PHE A 20 ? THR A 22 ? PHE A 20 THR A 22 
AA1 2 GLY A 38 ? SER A 40 ? GLY A 38 SER A 40 
AA2 1 PHE B 20 ? LEU B 23 ? PHE B 20 LEU B 23 
AA2 2 ALA B 37 ? SER B 40 ? ALA B 37 SER B 40 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLU A 21 ? N GLU A 21 O ILE A 39 ? O ILE A 39 
AA2 1 2 N LEU B 23 ? N LEU B 23 O ALA B 37 ? O ALA B 37 
# 
_pdbx_entry_details.entry_id                   8X9C 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 131 ? ? -97.71  30.63 
2 1 ASP A 158 ? ? -152.99 74.15 
3 1 ASP B 158 ? ? -150.03 78.24 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLN 2   ? A GLN 2   
3  1 Y 1 A VAL 3   ? A VAL 3   
4  1 Y 1 A ALA 4   ? A ALA 4   
5  1 Y 1 A PRO 5   ? A PRO 5   
6  1 Y 1 A THR 6   ? A THR 6   
7  1 Y 1 A SER 7   ? A SER 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A PRO 9   ? A PRO 9   
10 1 Y 1 A ALA 10  ? A ALA 10  
11 1 Y 1 A GLY 11  ? A GLY 11  
12 1 Y 1 A PRO 12  ? A PRO 12  
13 1 Y 1 A VAL 13  ? A VAL 13  
14 1 Y 1 A ILE 244 ? A ILE 244 
15 1 Y 1 A GLU 245 ? A GLU 245 
16 1 Y 1 A LYS 246 ? A LYS 246 
17 1 Y 1 A ASP 247 ? A ASP 247 
18 1 Y 1 A GLN 248 ? A GLN 248 
19 1 Y 1 A GLU 249 ? A GLU 249 
20 1 Y 1 A THR 250 ? A THR 250 
21 1 Y 1 A ASP 251 ? A ASP 251 
22 1 Y 1 A ARG 252 ? A ARG 252 
23 1 Y 1 A MET 253 ? A MET 253 
24 1 Y 1 A ARG 325 ? A ARG 325 
25 1 Y 1 A TYR 326 ? A TYR 326 
26 1 Y 1 A GLN 327 ? A GLN 327 
27 1 Y 1 A VAL 328 ? A VAL 328 
28 1 Y 1 A PHE 329 ? A PHE 329 
29 1 Y 1 A GLU 330 ? A GLU 330 
30 1 Y 1 B MET 1   ? B MET 1   
31 1 Y 1 B GLN 2   ? B GLN 2   
32 1 Y 1 B VAL 3   ? B VAL 3   
33 1 Y 1 B ALA 4   ? B ALA 4   
34 1 Y 1 B PRO 5   ? B PRO 5   
35 1 Y 1 B THR 6   ? B THR 6   
36 1 Y 1 B SER 7   ? B SER 7   
37 1 Y 1 B SER 8   ? B SER 8   
38 1 Y 1 B PRO 9   ? B PRO 9   
39 1 Y 1 B ALA 10  ? B ALA 10  
40 1 Y 1 B GLY 11  ? B GLY 11  
41 1 Y 1 B PRO 12  ? B PRO 12  
42 1 Y 1 B ILE 244 ? B ILE 244 
43 1 Y 1 B GLU 245 ? B GLU 245 
44 1 Y 1 B LYS 246 ? B LYS 246 
45 1 Y 1 B ASP 247 ? B ASP 247 
46 1 Y 1 B GLN 248 ? B GLN 248 
47 1 Y 1 B GLU 249 ? B GLU 249 
48 1 Y 1 B THR 250 ? B THR 250 
49 1 Y 1 B ASP 251 ? B ASP 251 
50 1 Y 1 B ARG 252 ? B ARG 252 
51 1 Y 1 B MET 253 ? B MET 253 
52 1 Y 1 B ARG 254 ? B ARG 254 
53 1 Y 1 B PRO 324 ? B PRO 324 
54 1 Y 1 B ARG 325 ? B ARG 325 
55 1 Y 1 B TYR 326 ? B TYR 326 
56 1 Y 1 B GLN 327 ? B GLN 327 
57 1 Y 1 B VAL 328 ? B VAL 328 
58 1 Y 1 B PHE 329 ? B PHE 329 
59 1 Y 1 B GLU 330 ? B GLU 330 
# 
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 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2019YFA0905000 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8X9C 
_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]   0.017652 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006964 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008406 
_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]   0.016387 
_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 14  ? -4.432  15.096  -0.797  1.00 55.08  ? 14  SER A N   1 
ATOM   2    C CA  . SER A 1 14  ? -3.451  14.813  0.248   1.00 54.97  ? 14  SER A CA  1 
ATOM   3    C C   . SER A 1 14  ? -3.315  15.992  1.211   1.00 56.55  ? 14  SER A C   1 
ATOM   4    O O   . SER A 1 14  ? -3.408  17.154  0.810   1.00 54.61  ? 14  SER A O   1 
ATOM   5    C CB  . SER A 1 14  ? -2.086  14.473  -0.367  1.00 54.79  ? 14  SER A CB  1 
ATOM   6    O OG  . SER A 1 14  ? -1.060  14.418  0.620   1.00 53.92  ? 14  SER A OG  1 
ATOM   7    N N   . ALA A 1 15  ? -3.103  15.680  2.488   1.00 51.00  ? 15  ALA A N   1 
ATOM   8    C CA  . ALA A 1 15  ? -2.874  16.681  3.518   1.00 53.23  ? 15  ALA A CA  1 
ATOM   9    C C   . ALA A 1 15  ? -1.399  16.841  3.857   1.00 51.27  ? 15  ALA A C   1 
ATOM   10   O O   . ALA A 1 15  ? -1.058  17.658  4.718   1.00 50.25  ? 15  ALA A O   1 
ATOM   11   C CB  . ALA A 1 15  ? -3.662  16.326  4.784   1.00 50.26  ? 15  ALA A CB  1 
ATOM   12   N N   . ILE A 1 16  ? -0.526  16.090  3.190   1.00 49.56  ? 16  ILE A N   1 
ATOM   13   C CA  . ILE A 1 16  ? 0.911   16.066  3.449   1.00 52.82  ? 16  ILE A CA  1 
ATOM   14   C C   . ILE A 1 16  ? 1.585   16.883  2.352   1.00 49.95  ? 16  ILE A C   1 
ATOM   15   O O   . ILE A 1 16  ? 1.135   16.840  1.198   1.00 51.67  ? 16  ILE A O   1 
ATOM   16   C CB  . ILE A 1 16  ? 1.431   14.613  3.477   1.00 48.18  ? 16  ILE A CB  1 
ATOM   17   C CG1 . ILE A 1 16  ? 0.832   13.841  4.641   1.00 42.68  ? 16  ILE A CG1 1 
ATOM   18   C CG2 . ILE A 1 16  ? 2.954   14.526  3.570   1.00 47.09  ? 16  ILE A CG2 1 
ATOM   19   C CD1 . ILE A 1 16  ? 1.128   12.360  4.535   1.00 41.16  ? 16  ILE A CD1 1 
ATOM   20   N N   . PRO A 1 17  ? 2.649   17.635  2.645   1.00 52.73  ? 17  PRO A N   1 
ATOM   21   C CA  . PRO A 1 17  ? 3.417   18.264  1.565   1.00 51.66  ? 17  PRO A CA  1 
ATOM   22   C C   . PRO A 1 17  ? 3.925   17.229  0.567   1.00 51.09  ? 17  PRO A C   1 
ATOM   23   O O   . PRO A 1 17  ? 4.062   16.038  0.868   1.00 50.78  ? 17  PRO A O   1 
ATOM   24   C CB  . PRO A 1 17  ? 4.569   18.948  2.310   1.00 51.42  ? 17  PRO A CB  1 
ATOM   25   C CG  . PRO A 1 17  ? 4.730   18.100  3.560   1.00 50.27  ? 17  PRO A CG  1 
ATOM   26   C CD  . PRO A 1 17  ? 3.302   17.836  3.953   1.00 54.10  ? 17  PRO A CD  1 
ATOM   27   N N   . SER A 1 18  ? 4.153   17.709  -0.656  1.00 53.19  ? 18  SER A N   1 
ATOM   28   C CA  . SER A 1 18  ? 4.602   16.832  -1.767  1.00 50.20  ? 18  SER A CA  1 
ATOM   29   C C   . SER A 1 18  ? 6.082   16.499  -1.603  1.00 49.96  ? 18  SER A C   1 
ATOM   30   O O   . SER A 1 18  ? 6.908   17.096  -2.305  1.00 48.76  ? 18  SER A O   1 
ATOM   31   C CB  . SER A 1 18  ? 4.329   17.515  -3.082  1.00 50.14  ? 18  SER A CB  1 
ATOM   32   O OG  . SER A 1 18  ? 4.875   16.767  -4.154  1.00 58.70  ? 18  SER A OG  1 
ATOM   33   N N   . VAL A 1 19  ? 6.390   15.572  -0.708  1.00 41.34  ? 19  VAL A N   1 
ATOM   34   C CA  . VAL A 1 19  ? 7.775   15.213  -0.440  1.00 39.84  ? 19  VAL A CA  1 
ATOM   35   C C   . VAL A 1 19  ? 8.040   13.732  -0.686  1.00 39.68  ? 19  VAL A C   1 
ATOM   36   O O   . VAL A 1 19  ? 9.087   13.218  -0.277  1.00 38.31  ? 19  VAL A O   1 
ATOM   37   C CB  . VAL A 1 19  ? 8.192   15.616  0.990   1.00 39.26  ? 19  VAL A CB  1 
ATOM   38   C CG1 . VAL A 1 19  ? 8.127   17.137  1.161   1.00 42.33  ? 19  VAL A CG1 1 
ATOM   39   C CG2 . VAL A 1 19  ? 7.299   14.942  2.011   1.00 38.87  ? 19  VAL A CG2 1 
ATOM   40   N N   . PHE A 1 20  ? 7.119   13.028  -1.347  1.00 37.13  ? 20  PHE A N   1 
ATOM   41   C CA  . PHE A 1 20  ? 7.372   11.623  -1.630  1.00 37.50  ? 20  PHE A CA  1 
ATOM   42   C C   . PHE A 1 20  ? 6.748   11.229  -2.963  1.00 39.34  ? 20  PHE A C   1 
ATOM   43   O O   . PHE A 1 20  ? 5.819   11.873  -3.460  1.00 42.64  ? 20  PHE A O   1 
ATOM   44   C CB  . PHE A 1 20  ? 6.831   10.686  -0.531  1.00 35.38  ? 20  PHE A CB  1 
ATOM   45   C CG  . PHE A 1 20  ? 5.349   10.809  -0.281  1.00 34.98  ? 20  PHE A CG  1 
ATOM   46   C CD1 . PHE A 1 20  ? 4.838   11.802  0.547   1.00 37.72  ? 20  PHE A CD1 1 
ATOM   47   C CD2 . PHE A 1 20  ? 4.459   9.937   -0.911  1.00 37.52  ? 20  PHE A CD2 1 
ATOM   48   C CE1 . PHE A 1 20  ? 3.476   11.909  0.767   1.00 39.55  ? 20  PHE A CE1 1 
ATOM   49   C CE2 . PHE A 1 20  ? 3.093   10.038  -0.694  1.00 37.47  ? 20  PHE A CE2 1 
ATOM   50   C CZ  . PHE A 1 20  ? 2.603   11.019  0.147   1.00 36.13  ? 20  PHE A CZ  1 
ATOM   51   N N   . GLU A 1 21  ? 7.271   10.148  -3.527  1.00 37.51  ? 21  GLU A N   1 
ATOM   52   C CA  . GLU A 1 21  ? 6.700   9.502   -4.701  1.00 40.97  ? 21  GLU A CA  1 
ATOM   53   C C   . GLU A 1 21  ? 6.036   8.199   -4.273  1.00 41.22  ? 21  GLU A C   1 
ATOM   54   O O   . GLU A 1 21  ? 6.550   7.492   -3.405  1.00 39.89  ? 21  GLU A O   1 
ATOM   55   C CB  . GLU A 1 21  ? 7.789   9.226   -5.741  1.00 42.53  ? 21  GLU A CB  1 
ATOM   56   C CG  . GLU A 1 21  ? 8.571   10.493  -6.130  1.00 52.50  ? 21  GLU A CG  1 
ATOM   57   C CD  . GLU A 1 21  ? 8.893   10.584  -7.612  1.00 66.64  ? 21  GLU A CD  1 
ATOM   58   O OE1 . GLU A 1 21  ? 9.896   9.959   -8.032  1.00 67.91  ? 21  GLU A OE1 1 
ATOM   59   O OE2 . GLU A 1 21  ? 8.156   11.280  -8.352  1.00 66.25  ? 21  GLU A OE2 1 
ATOM   60   N N   . THR A 1 22  ? 4.900   7.878   -4.889  1.00 39.60  ? 22  THR A N   1 
ATOM   61   C CA  . THR A 1 22  ? 4.181   6.653   -4.556  1.00 39.32  ? 22  THR A CA  1 
ATOM   62   C C   . THR A 1 22  ? 4.879   5.438   -5.150  1.00 43.63  ? 22  THR A C   1 
ATOM   63   O O   . THR A 1 22  ? 5.365   5.475   -6.283  1.00 48.76  ? 22  THR A O   1 
ATOM   64   C CB  . THR A 1 22  ? 2.739   6.728   -5.068  1.00 45.37  ? 22  THR A CB  1 
ATOM   65   O OG1 . THR A 1 22  ? 2.090   7.872   -4.496  1.00 48.82  ? 22  THR A OG1 1 
ATOM   66   C CG2 . THR A 1 22  ? 1.961   5.456   -4.721  1.00 45.64  ? 22  THR A CG2 1 
ATOM   67   N N   . LEU A 1 23  ? 4.936   4.357   -4.374  1.00 37.35  ? 23  LEU A N   1 
ATOM   68   C CA  . LEU A 1 23  ? 5.478   3.094   -4.847  1.00 41.38  ? 23  LEU A CA  1 
ATOM   69   C C   . LEU A 1 23  ? 4.346   2.154   -5.250  1.00 43.35  ? 23  LEU A C   1 
ATOM   70   O O   . LEU A 1 23  ? 3.251   2.185   -4.679  1.00 43.34  ? 23  LEU A O   1 
ATOM   71   C CB  . LEU A 1 23  ? 6.342   2.422   -3.778  1.00 41.58  ? 23  LEU A CB  1 
ATOM   72   C CG  . LEU A 1 23  ? 7.648   3.122   -3.411  1.00 37.57  ? 23  LEU A CG  1 
ATOM   73   C CD1 . LEU A 1 23  ? 8.029   2.821   -1.950  1.00 39.39  ? 23  LEU A CD1 1 
ATOM   74   C CD2 . LEU A 1 23  ? 8.764   2.735   -4.364  1.00 43.68  ? 23  LEU A CD2 1 
ATOM   75   N N   . GLN A 1 24  ? 4.622   1.307   -6.241  1.00 45.55  ? 24  GLN A N   1 
ATOM   76   C CA  . GLN A 1 24  ? 3.617   0.377   -6.751  1.00 49.91  ? 24  GLN A CA  1 
ATOM   77   C C   . GLN A 1 24  ? 3.785   -0.941  -6.007  1.00 47.01  ? 24  GLN A C   1 
ATOM   78   O O   . GLN A 1 24  ? 4.508   -1.838  -6.440  1.00 46.26  ? 24  GLN A O   1 
ATOM   79   C CB  . GLN A 1 24  ? 3.754   0.202   -8.258  1.00 56.10  ? 24  GLN A CB  1 
ATOM   80   C CG  . GLN A 1 24  ? 4.085   1.485   -9.010  1.00 57.47  ? 24  GLN A CG  1 
ATOM   81   C CD  . GLN A 1 24  ? 3.540   1.488   -10.430 1.00 69.20  ? 24  GLN A CD  1 
ATOM   82   O OE1 . GLN A 1 24  ? 2.327   1.445   -10.644 1.00 71.18  ? 24  GLN A OE1 1 
ATOM   83   N NE2 . GLN A 1 24  ? 4.439   1.532   -11.409 1.00 70.12  ? 24  GLN A NE2 1 
ATOM   84   N N   . GLY A 1 25  ? 3.102   -1.057  -4.867  1.00 43.12  ? 25  GLY A N   1 
ATOM   85   C CA  . GLY A 1 25  ? 3.244   -2.246  -4.048  1.00 42.18  ? 25  GLY A CA  1 
ATOM   86   C C   . GLY A 1 25  ? 2.657   -3.479  -4.698  1.00 43.53  ? 25  GLY A C   1 
ATOM   87   O O   . GLY A 1 25  ? 3.097   -4.598  -4.417  1.00 43.71  ? 25  GLY A O   1 
ATOM   88   N N   . TYR A 1 26  ? 1.670   -3.295  -5.583  1.00 45.61  ? 26  TYR A N   1 
ATOM   89   C CA  . TYR A 1 26  ? 1.048   -4.441  -6.238  1.00 50.37  ? 26  TYR A CA  1 
ATOM   90   C C   . TYR A 1 26  ? 2.053   -5.225  -7.065  1.00 49.14  ? 26  TYR A C   1 
ATOM   91   O O   . TYR A 1 26  ? 1.827   -6.410  -7.334  1.00 53.08  ? 26  TYR A O   1 
ATOM   92   C CB  . TYR A 1 26  ? -0.123  -4.002  -7.131  1.00 51.89  ? 26  TYR A CB  1 
ATOM   93   C CG  . TYR A 1 26  ? 0.256   -3.212  -8.374  1.00 55.30  ? 26  TYR A CG  1 
ATOM   94   C CD1 . TYR A 1 26  ? 0.348   -1.824  -8.346  1.00 58.95  ? 26  TYR A CD1 1 
ATOM   95   C CD2 . TYR A 1 26  ? 0.490   -3.858  -9.584  1.00 59.23  ? 26  TYR A CD2 1 
ATOM   96   C CE1 . TYR A 1 26  ? 0.686   -1.103  -9.489  1.00 61.20  ? 26  TYR A CE1 1 
ATOM   97   C CE2 . TYR A 1 26  ? 0.826   -3.148  -10.728 1.00 62.29  ? 26  TYR A CE2 1 
ATOM   98   C CZ  . TYR A 1 26  ? 0.923   -1.772  -10.673 1.00 64.44  ? 26  TYR A CZ  1 
ATOM   99   O OH  . TYR A 1 26  ? 1.257   -1.067  -11.809 1.00 69.36  ? 26  TYR A OH  1 
ATOM   100  N N   . LYS A 1 27  ? 3.156   -4.593  -7.473  1.00 43.91  ? 27  LYS A N   1 
ATOM   101  C CA  . LYS A 1 27  ? 4.180   -5.273  -8.255  1.00 46.89  ? 27  LYS A CA  1 
ATOM   102  C C   . LYS A 1 27  ? 5.014   -6.243  -7.430  1.00 45.58  ? 27  LYS A C   1 
ATOM   103  O O   . LYS A 1 27  ? 5.776   -7.024  -8.010  1.00 47.01  ? 27  LYS A O   1 
ATOM   104  C CB  . LYS A 1 27  ? 5.091   -4.240  -8.924  1.00 47.69  ? 27  LYS A CB  1 
ATOM   105  C CG  . LYS A 1 27  ? 4.373   -3.370  -9.951  1.00 51.86  ? 27  LYS A CG  1 
ATOM   106  C CD  . LYS A 1 27  ? 5.215   -3.173  -11.202 1.00 58.85  ? 27  LYS A CD  1 
ATOM   107  C CE  . LYS A 1 27  ? 6.401   -2.268  -10.935 1.00 61.57  ? 27  LYS A CE  1 
ATOM   108  N NZ  . LYS A 1 27  ? 5.965   -0.874  -10.641 1.00 64.38  ? 27  LYS A NZ  1 
ATOM   109  N N   . VAL A 1 28  ? 4.897   -6.219  -6.103  1.00 40.07  ? 28  VAL A N   1 
ATOM   110  C CA  . VAL A 1 28  ? 5.681   -7.079  -5.229  1.00 36.48  ? 28  VAL A CA  1 
ATOM   111  C C   . VAL A 1 28  ? 4.763   -8.203  -4.728  1.00 34.85  ? 28  VAL A C   1 
ATOM   112  O O   . VAL A 1 28  ? 3.871   -7.931  -3.910  1.00 32.28  ? 28  VAL A O   1 
ATOM   113  C CB  . VAL A 1 28  ? 6.295   -6.286  -4.066  1.00 33.72  ? 28  VAL A CB  1 
ATOM   114  C CG1 . VAL A 1 28  ? 7.261   -7.156  -3.270  1.00 35.41  ? 28  VAL A CG1 1 
ATOM   115  C CG2 . VAL A 1 28  ? 7.001   -5.068  -4.626  1.00 38.01  ? 28  VAL A CG2 1 
ATOM   116  N N   . PRO A 1 29  ? 4.899   -9.458  -5.200  1.00 32.69  ? 29  PRO A N   1 
ATOM   117  C CA  . PRO A 1 29  ? 3.986   -10.512 -4.779  1.00 34.48  ? 29  PRO A CA  1 
ATOM   118  C C   . PRO A 1 29  ? 3.892   -10.692 -3.261  1.00 35.16  ? 29  PRO A C   1 
ATOM   119  O O   . PRO A 1 29  ? 2.826   -10.950 -2.781  1.00 33.70  ? 29  PRO A O   1 
ATOM   120  C CB  . PRO A 1 29  ? 4.607   -11.763 -5.408  1.00 34.22  ? 29  PRO A CB  1 
ATOM   121  C CG  . PRO A 1 29  ? 5.250   -11.244 -6.665  1.00 35.01  ? 29  PRO A CG  1 
ATOM   122  C CD  . PRO A 1 29  ? 5.846   -9.927  -6.225  1.00 38.14  ? 29  PRO A CD  1 
ATOM   123  N N   . VAL A 1 30  ? 5.015   -10.556 -2.566  1.00 32.25  ? 30  VAL A N   1 
ATOM   124  C CA  . VAL A 1 30  ? 5.031   -10.792 -1.130  1.00 38.39  ? 30  VAL A CA  1 
ATOM   125  C C   . VAL A 1 30  ? 4.370   -9.655  -0.345  1.00 36.33  ? 30  VAL A C   1 
ATOM   126  O O   . VAL A 1 30  ? 3.909   -9.873  0.783   1.00 34.04  ? 30  VAL A O   1 
ATOM   127  C CB  . VAL A 1 30  ? 6.501   -11.056 -0.742  1.00 40.43  ? 30  VAL A CB  1 
ATOM   128  C CG1 . VAL A 1 30  ? 6.772   -10.783 0.697   1.00 42.41  ? 30  VAL A CG1 1 
ATOM   129  C CG2 . VAL A 1 30  ? 6.858   -12.504 -1.077  1.00 41.82  ? 30  VAL A CG2 1 
ATOM   130  N N   . PHE A 1 31  ? 4.280   -8.461  -0.927  1.00 31.88  ? 31  PHE A N   1 
ATOM   131  C CA  . PHE A 1 31  ? 3.658   -7.315  -0.265  1.00 30.51  ? 31  PHE A CA  1 
ATOM   132  C C   . PHE A 1 31  ? 2.152   -7.522  -0.149  1.00 34.27  ? 31  PHE A C   1 
ATOM   133  O O   . PHE A 1 31  ? 1.451   -7.567  -1.167  1.00 35.59  ? 31  PHE A O   1 
ATOM   134  C CB  . PHE A 1 31  ? 3.963   -6.056  -1.074  1.00 29.42  ? 31  PHE A CB  1 
ATOM   135  C CG  . PHE A 1 31  ? 3.308   -4.797  -0.552  1.00 34.37  ? 31  PHE A CG  1 
ATOM   136  C CD1 . PHE A 1 31  ? 3.687   -4.224  0.648   1.00 29.46  ? 31  PHE A CD1 1 
ATOM   137  C CD2 . PHE A 1 31  ? 2.264   -4.223  -1.263  1.00 35.94  ? 31  PHE A CD2 1 
ATOM   138  C CE1 . PHE A 1 31  ? 3.064   -3.066  1.112   1.00 29.21  ? 31  PHE A CE1 1 
ATOM   139  C CE2 . PHE A 1 31  ? 1.632   -3.086  -0.808  1.00 35.62  ? 31  PHE A CE2 1 
ATOM   140  C CZ  . PHE A 1 31  ? 2.043   -2.496  0.387   1.00 32.68  ? 31  PHE A CZ  1 
ATOM   141  N N   . PHE A 1 32  ? 1.639   -7.626  1.081   1.00 29.96  ? 32  PHE A N   1 
ATOM   142  C CA  . PHE A 1 32  ? 0.231   -7.948  1.284   1.00 30.52  ? 32  PHE A CA  1 
ATOM   143  C C   . PHE A 1 32  ? -0.567  -6.819  1.921   1.00 32.33  ? 32  PHE A C   1 
ATOM   144  O O   . PHE A 1 32  ? -1.785  -6.960  2.068   1.00 31.28  ? 32  PHE A O   1 
ATOM   145  C CB  . PHE A 1 32  ? 0.069   -9.201  2.168   1.00 29.55  ? 32  PHE A CB  1 
ATOM   146  C CG  . PHE A 1 32  ? 0.654   -9.040  3.557   1.00 29.40  ? 32  PHE A CG  1 
ATOM   147  C CD1 . PHE A 1 32  ? -0.118  -8.521  4.589   1.00 33.02  ? 32  PHE A CD1 1 
ATOM   148  C CD2 . PHE A 1 32  ? 1.953   -9.403  3.822   1.00 32.19  ? 32  PHE A CD2 1 
ATOM   149  C CE1 . PHE A 1 32  ? 0.423   -8.348  5.866   1.00 31.61  ? 32  PHE A CE1 1 
ATOM   150  C CE2 . PHE A 1 32  ? 2.496   -9.252  5.099   1.00 32.58  ? 32  PHE A CE2 1 
ATOM   151  C CZ  . PHE A 1 32  ? 1.720   -8.726  6.119   1.00 30.50  ? 32  PHE A CZ  1 
ATOM   152  N N   . SER A 1 33  ? 0.080   -5.733  2.340   1.00 30.65  ? 33  SER A N   1 
ATOM   153  C CA  . SER A 1 33  ? -0.618  -4.700  3.090   1.00 29.67  ? 33  SER A CA  1 
ATOM   154  C C   . SER A 1 33  ? -1.632  -3.980  2.207   1.00 31.10  ? 33  SER A C   1 
ATOM   155  O O   . SER A 1 33  ? -1.418  -3.793  1.011   1.00 32.99  ? 33  SER A O   1 
ATOM   156  C CB  . SER A 1 33  ? 0.382   -3.688  3.659   1.00 26.61  ? 33  SER A CB  1 
ATOM   157  O OG  . SER A 1 33  ? -0.298  -2.710  4.419   1.00 28.56  ? 33  SER A OG  1 
ATOM   158  N N   . ARG A 1 34  ? -2.751  -3.583  2.816   1.00 28.42  ? 34  ARG A N   1 
ATOM   159  C CA  . ARG A 1 34  ? -3.730  -2.696  2.193   1.00 31.49  ? 34  ARG A CA  1 
ATOM   160  C C   . ARG A 1 34  ? -3.292  -1.237  2.199   1.00 33.25  ? 34  ARG A C   1 
ATOM   161  O O   . ARG A 1 34  ? -3.944  -0.398  1.556   1.00 33.78  ? 34  ARG A O   1 
ATOM   162  C CB  . ARG A 1 34  ? -5.070  -2.850  2.917   1.00 32.69  ? 34  ARG A CB  1 
ATOM   163  C CG  . ARG A 1 34  ? -5.100  -2.125  4.259   1.00 32.33  ? 34  ARG A CG  1 
ATOM   164  C CD  . ARG A 1 34  ? -6.384  -2.407  5.017   1.00 34.68  ? 34  ARG A CD  1 
ATOM   165  N NE  . ARG A 1 34  ? -7.551  -1.936  4.286   1.00 40.76  ? 34  ARG A NE  1 
ATOM   166  C CZ  . ARG A 1 34  ? -8.698  -2.594  4.211   1.00 39.10  ? 34  ARG A CZ  1 
ATOM   167  N NH1 . ARG A 1 34  ? -8.845  -3.792  4.757   1.00 38.44  ? 34  ARG A NH1 1 
ATOM   168  N NH2 . ARG A 1 34  ? -9.720  -2.037  3.568   1.00 37.19  ? 34  ARG A NH2 1 
ATOM   169  N N   . TYR A 1 35  ? -2.194  -0.905  2.925   1.00 30.37  ? 35  TYR A N   1 
ATOM   170  C CA  . TYR A 1 35  ? -1.804  0.479   3.071   1.00 27.66  ? 35  TYR A CA  1 
ATOM   171  C C   . TYR A 1 35  ? -0.741  0.848   2.044   1.00 27.86  ? 35  TYR A C   1 
ATOM   172  O O   . TYR A 1 35  ? -0.025  -0.019  1.532   1.00 32.09  ? 35  TYR A O   1 
ATOM   173  C CB  . TYR A 1 35  ? -1.300  0.714   4.509   1.00 27.25  ? 35  TYR A CB  1 
ATOM   174  C CG  . TYR A 1 35  ? -2.475  0.582   5.442   1.00 28.70  ? 35  TYR A CG  1 
ATOM   175  C CD1 . TYR A 1 35  ? -3.547  1.460   5.335   1.00 29.69  ? 35  TYR A CD1 1 
ATOM   176  C CD2 . TYR A 1 35  ? -2.557  -0.443  6.374   1.00 29.60  ? 35  TYR A CD2 1 
ATOM   177  C CE1 . TYR A 1 35  ? -4.660  1.343   6.139   1.00 29.14  ? 35  TYR A CE1 1 
ATOM   178  C CE2 . TYR A 1 35  ? -3.687  -0.569  7.195   1.00 31.22  ? 35  TYR A CE2 1 
ATOM   179  C CZ  . TYR A 1 35  ? -4.735  0.331   7.058   1.00 30.83  ? 35  TYR A CZ  1 
ATOM   180  O OH  . TYR A 1 35  ? -5.866  0.251   7.850   1.00 30.45  ? 35  TYR A OH  1 
ATOM   181  N N   . PRO A 1 36  ? -0.658  2.120   1.689   1.00 30.03  ? 36  PRO A N   1 
ATOM   182  C CA  . PRO A 1 36  ? 0.254   2.549   0.625   1.00 33.18  ? 36  PRO A CA  1 
ATOM   183  C C   . PRO A 1 36  ? 1.696   2.660   1.095   1.00 30.47  ? 36  PRO A C   1 
ATOM   184  O O   . PRO A 1 36  ? 2.001   2.675   2.290   1.00 30.22  ? 36  PRO A O   1 
ATOM   185  C CB  . PRO A 1 36  ? -0.293  3.925   0.248   1.00 34.46  ? 36  PRO A CB  1 
ATOM   186  C CG  . PRO A 1 36  ? -0.821  4.460   1.539   1.00 34.13  ? 36  PRO A CG  1 
ATOM   187  C CD  . PRO A 1 36  ? -1.380  3.257   2.287   1.00 30.17  ? 36  PRO A CD  1 
ATOM   188  N N   . ALA A 1 37  ? 2.588   2.750   0.110   1.00 32.25  ? 37  ALA A N   1 
ATOM   189  C CA  . ALA A 1 37  ? 4.006   2.978   0.351   1.00 28.80  ? 37  ALA A CA  1 
ATOM   190  C C   . ALA A 1 37  ? 4.492   4.095   -0.560  1.00 34.36  ? 37  ALA A C   1 
ATOM   191  O O   . ALA A 1 37  ? 4.038   4.228   -1.701  1.00 36.21  ? 37  ALA A O   1 
ATOM   192  C CB  . ALA A 1 37  ? 4.846   1.720   0.121   1.00 32.79  ? 37  ALA A CB  1 
ATOM   193  N N   . GLY A 1 38  ? 5.397   4.912   -0.040  1.00 30.49  ? 38  GLY A N   1 
ATOM   194  C CA  . GLY A 1 38  ? 6.010   5.962   -0.822  1.00 31.13  ? 38  GLY A CA  1 
ATOM   195  C C   . GLY A 1 38  ? 7.485   6.055   -0.495  1.00 34.59  ? 38  GLY A C   1 
ATOM   196  O O   . GLY A 1 38  ? 7.980   5.363   0.393   1.00 32.24  ? 38  GLY A O   1 
ATOM   197  N N   . ILE A 1 39  ? 8.150   7.014   -1.194  1.00 32.21  ? 39  ILE A N   1 
ATOM   198  C CA  . ILE A 1 39  ? 9.573   7.118   -0.886  1.00 34.76  ? 39  ILE A CA  1 
ATOM   199  C C   . ILE A 1 39  ? 9.987   8.581   -0.918  1.00 33.63  ? 39  ILE A C   1 
ATOM   200  O O   . ILE A 1 39  ? 9.557   9.347   -1.784  1.00 35.84  ? 39  ILE A O   1 
ATOM   201  C CB  . ILE A 1 39  ? 10.430  6.242   -1.831  1.00 35.37  ? 39  ILE A CB  1 
ATOM   202  C CG1 . ILE A 1 39  ? 11.905  6.261   -1.380  1.00 38.10  ? 39  ILE A CG1 1 
ATOM   203  C CG2 . ILE A 1 39  ? 10.200  6.603   -3.309  1.00 36.85  ? 39  ILE A CG2 1 
ATOM   204  C CD1 . ILE A 1 39  ? 12.770  5.197   -2.042  1.00 39.76  ? 39  ILE A CD1 1 
ATOM   205  N N   . SER A 1 40  ? 10.822  9.008   -0.152  1.00 31.88  ? 40  SER A N   1 
ATOM   206  C CA  . SER A 1 40  ? 11.075  10.430  0.010   1.00 32.92  ? 40  SER A CA  1 
ATOM   207  C C   . SER A 1 40  ? 11.846  10.964  -1.189  1.00 34.61  ? 40  SER A C   1 
ATOM   208  O O   . SER A 1 40  ? 12.743  10.298  -1.718  1.00 33.39  ? 40  SER A O   1 
ATOM   209  C CB  . SER A 1 40  ? 11.867  10.673  1.297   1.00 31.64  ? 40  SER A CB  1 
ATOM   210  O OG  . SER A 1 40  ? 12.479  11.967  1.295   1.00 32.67  ? 40  SER A OG  1 
ATOM   211  N N   . ILE A 1 41  ? 11.481  12.173  -1.628  1.00 37.98  ? 41  ILE A N   1 
ATOM   212  C CA  . ILE A 1 41  ? 12.258  12.869  -2.650  1.00 39.24  ? 41  ILE A CA  1 
ATOM   213  C C   . ILE A 1 41  ? 13.703  13.105  -2.223  1.00 36.90  ? 41  ILE A C   1 
ATOM   214  O O   . ILE A 1 41  ? 14.569  13.317  -3.075  1.00 38.93  ? 41  ILE A O   1 
ATOM   215  C CB  . ILE A 1 41  ? 11.578  14.205  -3.018  1.00 36.77  ? 41  ILE A CB  1 
ATOM   216  C CG1 . ILE A 1 41  ? 11.639  15.175  -1.836  1.00 37.94  ? 41  ILE A CG1 1 
ATOM   217  C CG2 . ILE A 1 41  ? 10.146  13.968  -3.494  1.00 38.84  ? 41  ILE A CG2 1 
ATOM   218  C CD1 . ILE A 1 41  ? 11.180  16.598  -2.162  1.00 40.94  ? 41  ILE A CD1 1 
ATOM   219  N N   . ALA A 1 42  ? 13.992  13.074  -0.920  1.00 35.02  ? 42  ALA A N   1 
ATOM   220  C CA  . ALA A 1 42  ? 15.343  13.283  -0.412  1.00 39.72  ? 42  ALA A CA  1 
ATOM   221  C C   . ALA A 1 42  ? 16.042  11.973  -0.059  1.00 36.81  ? 42  ALA A C   1 
ATOM   222  O O   . ALA A 1 42  ? 16.943  11.958  0.784   1.00 37.74  ? 42  ALA A O   1 
ATOM   223  C CB  . ALA A 1 42  ? 15.310  14.215  0.799   1.00 37.13  ? 42  ALA A CB  1 
ATOM   224  N N   . ALA A 1 43  ? 15.650  10.872  -0.687  1.00 35.72  ? 43  ALA A N   1 
ATOM   225  C CA  . ALA A 1 43  ? 16.198  9.547   -0.322  1.00 36.11  ? 43  ALA A CA  1 
ATOM   226  C C   . ALA A 1 43  ? 17.723  9.536   -0.365  1.00 37.51  ? 43  ALA A C   1 
ATOM   227  O O   . ALA A 1 43  ? 18.334  9.055   0.588   1.00 37.76  ? 43  ALA A O   1 
ATOM   228  C CB  . ALA A 1 43  ? 15.644  8.501   -1.241  1.00 37.55  ? 43  ALA A CB  1 
ATOM   229  N N   . GLN A 1 44  ? 18.298  10.035  -1.454  1.00 39.39  ? 44  GLN A N   1 
ATOM   230  C CA  . GLN A 1 44  ? 19.752  9.945   -1.586  1.00 42.24  ? 44  GLN A CA  1 
ATOM   231  C C   . GLN A 1 44  ? 20.463  10.644  -0.430  1.00 38.27  ? 44  GLN A C   1 
ATOM   232  O O   . GLN A 1 44  ? 21.398  10.096  0.160   1.00 40.81  ? 44  GLN A O   1 
ATOM   233  C CB  . GLN A 1 44  ? 20.199  10.538  -2.923  1.00 45.33  ? 44  GLN A CB  1 
ATOM   234  C CG  . GLN A 1 44  ? 21.672  10.322  -3.231  1.00 44.37  ? 44  GLN A CG  1 
ATOM   235  C CD  . GLN A 1 44  ? 22.085  8.868   -3.170  1.00 49.55  ? 44  GLN A CD  1 
ATOM   236  O OE1 . GLN A 1 44  ? 21.605  8.044   -3.945  1.00 55.16  ? 44  GLN A OE1 1 
ATOM   237  N NE2 . GLN A 1 44  ? 22.978  8.541   -2.239  1.00 51.86  ? 44  GLN A NE2 1 
ATOM   238  N N   . GLU A 1 45  ? 20.027  11.860  -0.096  1.00 39.30  ? 45  GLU A N   1 
ATOM   239  C CA  . GLU A 1 45  ? 20.688  12.631  0.955   1.00 40.37  ? 45  GLU A CA  1 
ATOM   240  C C   . GLU A 1 45  ? 20.532  11.960  2.314   1.00 37.69  ? 45  GLU A C   1 
ATOM   241  O O   . GLU A 1 45  ? 21.455  11.986  3.142   1.00 37.30  ? 45  GLU A O   1 
ATOM   242  C CB  . GLU A 1 45  ? 20.100  14.037  0.984   1.00 41.45  ? 45  GLU A CB  1 
ATOM   243  C CG  . GLU A 1 45  ? 20.487  14.871  -0.219  1.00 47.04  ? 45  GLU A CG  1 
ATOM   244  C CD  . GLU A 1 45  ? 19.319  15.033  -1.185  1.00 52.81  ? 45  GLU A CD  1 
ATOM   245  O OE1 . GLU A 1 45  ? 18.695  14.000  -1.523  1.00 51.59  ? 45  GLU A OE1 1 
ATOM   246  O OE2 . GLU A 1 45  ? 19.024  16.175  -1.610  1.00 56.66  ? 45  GLU A OE2 1 
ATOM   247  N N   . VAL A 1 46  ? 19.358  11.378  2.569   1.00 33.27  ? 46  VAL A N   1 
ATOM   248  C CA  . VAL A 1 46  ? 19.115  10.682  3.828   1.00 30.92  ? 46  VAL A CA  1 
ATOM   249  C C   . VAL A 1 46  ? 19.952  9.411   3.925   1.00 33.66  ? 46  VAL A C   1 
ATOM   250  O O   . VAL A 1 46  ? 20.554  9.132   4.970   1.00 34.27  ? 46  VAL A O   1 
ATOM   251  C CB  . VAL A 1 46  ? 17.611  10.401  3.981   1.00 36.72  ? 46  VAL A CB  1 
ATOM   252  C CG1 . VAL A 1 46  ? 17.360  9.501   5.170   1.00 33.05  ? 46  VAL A CG1 1 
ATOM   253  C CG2 . VAL A 1 46  ? 16.856  11.714  4.157   1.00 33.42  ? 46  VAL A CG2 1 
ATOM   254  N N   . GLU A 1 47  ? 20.025  8.647   2.848   1.00 36.63  ? 47  GLU A N   1 
ATOM   255  C CA  . GLU A 1 47  ? 20.888  7.444   2.861   1.00 37.05  ? 47  GLU A CA  1 
ATOM   256  C C   . GLU A 1 47  ? 22.335  7.858   3.149   1.00 37.52  ? 47  GLU A C   1 
ATOM   257  O O   . GLU A 1 47  ? 23.007  7.156   3.902   1.00 37.52  ? 47  GLU A O   1 
ATOM   258  C CB  . GLU A 1 47  ? 20.789  6.724   1.520   1.00 41.94  ? 47  GLU A CB  1 
ATOM   259  C CG  . GLU A 1 47  ? 19.469  6.019   1.292   1.00 43.60  ? 47  GLU A CG  1 
ATOM   260  C CD  . GLU A 1 47  ? 19.516  5.035   0.138   1.00 49.66  ? 47  GLU A CD  1 
ATOM   261  O OE1 . GLU A 1 47  ? 20.630  4.684   -0.292  1.00 51.71  ? 47  GLU A OE1 1 
ATOM   262  O OE2 . GLU A 1 47  ? 18.447  4.628   -0.330  1.00 50.91  ? 47  GLU A OE2 1 
ATOM   263  N N   . ASP A 1 48  ? 22.785  8.954   2.539   1.00 39.39  ? 48  ASP A N   1 
ATOM   264  C CA  . ASP A 1 48  ? 24.144  9.422   2.803   1.00 41.89  ? 48  ASP A CA  1 
ATOM   265  C C   . ASP A 1 48  ? 24.332  9.787   4.276   1.00 39.53  ? 48  ASP A C   1 
ATOM   266  O O   . ASP A 1 48  ? 25.355  9.444   4.879   1.00 40.53  ? 48  ASP A O   1 
ATOM   267  C CB  . ASP A 1 48  ? 24.485  10.616  1.906   1.00 42.48  ? 48  ASP A CB  1 
ATOM   268  C CG  . ASP A 1 48  ? 24.600  10.243  0.426   1.00 43.89  ? 48  ASP A CG  1 
ATOM   269  O OD1 . ASP A 1 48  ? 24.683  9.041   0.100   1.00 47.59  ? 48  ASP A OD1 1 
ATOM   270  O OD2 . ASP A 1 48  ? 24.607  11.168  -0.419  1.00 47.81  ? 48  ASP A OD2 1 
ATOM   271  N N   . ALA A 1 49  ? 23.356  10.480  4.876   1.00 38.44  ? 49  ALA A N   1 
ATOM   272  C CA  . ALA A 1 49  ? 23.458  10.791  6.301   1.00 35.35  ? 49  ALA A CA  1 
ATOM   273  C C   . ALA A 1 49  ? 23.468  9.519   7.139   1.00 35.97  ? 49  ALA A C   1 
ATOM   274  O O   . ALA A 1 49  ? 24.206  9.424   8.129   1.00 37.81  ? 49  ALA A O   1 
ATOM   275  C CB  . ALA A 1 49  ? 22.311  11.699  6.739   1.00 33.82  ? 49  ALA A CB  1 
ATOM   276  N N   . LEU A 1 50  ? 22.656  8.527   6.756   1.00 36.22  ? 50  LEU A N   1 
ATOM   277  C CA  . LEU A 1 50  ? 22.602  7.294   7.533   1.00 31.66  ? 50  LEU A CA  1 
ATOM   278  C C   . LEU A 1 50  ? 23.912  6.532   7.438   1.00 38.35  ? 50  LEU A C   1 
ATOM   279  O O   . LEU A 1 50  ? 24.373  5.955   8.429   1.00 33.85  ? 50  LEU A O   1 
ATOM   280  C CB  . LEU A 1 50  ? 21.446  6.409   7.068   1.00 32.56  ? 50  LEU A CB  1 
ATOM   281  C CG  . LEU A 1 50  ? 20.050  6.871   7.499   1.00 31.65  ? 50  LEU A CG  1 
ATOM   282  C CD1 . LEU A 1 50  ? 18.968  6.387   6.539   1.00 30.03  ? 50  LEU A CD1 1 
ATOM   283  C CD2 . LEU A 1 50  ? 19.773  6.396   8.900   1.00 30.37  ? 50  LEU A CD2 1 
ATOM   284  N N   . ARG A 1 51  ? 24.546  6.546   6.272   1.00 37.63  ? 51  ARG A N   1 
ATOM   285  C CA  . ARG A 1 51  ? 25.859  5.859   6.133   1.00 39.11  ? 51  ARG A CA  1 
ATOM   286  C C   . ARG A 1 51  ? 26.878  6.506   7.072   1.00 39.03  ? 51  ARG A C   1 
ATOM   287  O O   . ARG A 1 51  ? 27.635  5.782   7.706   1.00 39.58  ? 51  ARG A O   1 
ATOM   288  C CB  . ARG A 1 51  ? 26.357  5.902   4.688   1.00 43.50  ? 51  ARG A CB  1 
ATOM   289  C CG  . ARG A 1 51  ? 27.637  5.121   4.441   1.00 51.73  ? 51  ARG A CG  1 
ATOM   290  C CD  . ARG A 1 51  ? 27.984  5.150   2.965   1.00 57.58  ? 51  ARG A CD  1 
ATOM   291  N NE  . ARG A 1 51  ? 28.032  6.504   2.429   1.00 58.60  ? 51  ARG A NE  1 
ATOM   292  C CZ  . ARG A 1 51  ? 27.130  7.032   1.608   1.00 57.08  ? 51  ARG A CZ  1 
ATOM   293  N NH1 . ARG A 1 51  ? 26.084  6.321   1.221   1.00 53.34  ? 51  ARG A NH1 1 
ATOM   294  N NH2 . ARG A 1 51  ? 27.276  8.273   1.183   1.00 56.18  ? 51  ARG A NH2 1 
ATOM   295  N N   . LYS A 1 52  ? 26.874  7.831   7.132   1.00 40.14  ? 52  LYS A N   1 
ATOM   296  C CA  . LYS A 1 52  ? 27.821  8.566   8.001   1.00 37.31  ? 52  LYS A CA  1 
ATOM   297  C C   . LYS A 1 52  ? 27.576  8.175   9.454   1.00 39.08  ? 52  LYS A C   1 
ATOM   298  O O   . LYS A 1 52  ? 28.534  7.821   10.134  1.00 38.66  ? 52  LYS A O   1 
ATOM   299  C CB  . LYS A 1 52  ? 27.626  10.064  7.778   1.00 39.80  ? 52  LYS A CB  1 
ATOM   300  C CG  . LYS A 1 52  ? 28.600  10.971  8.511   1.00 45.21  ? 52  LYS A CG  1 
ATOM   301  C CD  . LYS A 1 52  ? 28.824  12.282  7.791   1.00 46.83  ? 52  LYS A CD  1 
ATOM   302  C CE  . LYS A 1 52  ? 28.842  13.477  8.719   1.00 49.32  ? 52  LYS A CE  1 
ATOM   303  N NZ  . LYS A 1 52  ? 29.431  13.140  10.035  1.00 49.22  ? 52  LYS A NZ  1 
ATOM   304  N N   . ILE A 1 53  ? 26.320  8.235   9.896   1.00 36.16  ? 53  ILE A N   1 
ATOM   305  C CA  . ILE A 1 53  ? 26.051  7.960   11.337  1.00 37.19  ? 53  ILE A CA  1 
ATOM   306  C C   . ILE A 1 53  ? 26.386  6.492   11.629  1.00 38.19  ? 53  ILE A C   1 
ATOM   307  O O   . ILE A 1 53  ? 26.849  6.210   12.729  1.00 36.50  ? 53  ILE A O   1 
ATOM   308  C CB  . ILE A 1 53  ? 24.614  8.340   11.753  1.00 35.61  ? 53  ILE A CB  1 
ATOM   309  C CG1 . ILE A 1 53  ? 24.551  8.641   13.252  1.00 40.10  ? 53  ILE A CG1 1 
ATOM   310  C CG2 . ILE A 1 53  ? 23.614  7.272   11.353  1.00 35.78  ? 53  ILE A CG2 1 
ATOM   311  C CD1 . ILE A 1 53  ? 23.931  9.969   13.589  1.00 46.50  ? 53  ILE A CD1 1 
ATOM   312  N N   . ASP A 1 54  ? 26.178  5.611   10.656  1.00 35.26  ? 54  ASP A N   1 
ATOM   313  C CA  . ASP A 1 54  ? 26.512  4.212   10.913  1.00 35.17  ? 54  ASP A CA  1 
ATOM   314  C C   . ASP A 1 54  ? 28.006  4.022   11.149  1.00 36.71  ? 54  ASP A C   1 
ATOM   315  O O   . ASP A 1 54  ? 28.406  3.202   11.981  1.00 38.38  ? 54  ASP A O   1 
ATOM   316  C CB  . ASP A 1 54  ? 26.040  3.341   9.751   1.00 36.43  ? 54  ASP A CB  1 
ATOM   317  C CG  . ASP A 1 54  ? 24.571  3.026   9.835   1.00 38.07  ? 54  ASP A CG  1 
ATOM   318  O OD1 . ASP A 1 54  ? 24.022  3.141   10.951  1.00 34.46  ? 54  ASP A OD1 1 
ATOM   319  O OD2 . ASP A 1 54  ? 23.970  2.679   8.799   1.00 37.15  ? 54  ASP A OD2 1 
ATOM   320  N N   . GLU A 1 55  ? 28.847  4.757   10.415  1.00 41.18  ? 55  GLU A N   1 
ATOM   321  C CA  . GLU A 1 55  ? 30.290  4.618   10.603  1.00 43.22  ? 55  GLU A CA  1 
ATOM   322  C C   . GLU A 1 55  ? 30.761  5.247   11.905  1.00 43.72  ? 55  GLU A C   1 
ATOM   323  O O   . GLU A 1 55  ? 31.847  4.911   12.391  1.00 46.60  ? 55  GLU A O   1 
ATOM   324  C CB  . GLU A 1 55  ? 31.045  5.236   9.424   1.00 48.07  ? 55  GLU A CB  1 
ATOM   325  C CG  . GLU A 1 55  ? 31.016  4.403   8.150   1.00 54.95  ? 55  GLU A CG  1 
ATOM   326  C CD  . GLU A 1 55  ? 31.641  5.130   6.969   1.00 62.62  ? 55  GLU A CD  1 
ATOM   327  O OE1 . GLU A 1 55  ? 32.210  6.222   7.179   1.00 65.85  ? 55  GLU A OE1 1 
ATOM   328  O OE2 . GLU A 1 55  ? 31.545  4.622   5.829   1.00 66.95  ? 55  GLU A OE2 1 
ATOM   329  N N   . GLU A 1 56  ? 29.970  6.144   12.486  1.00 41.19  ? 56  GLU A N   1 
ATOM   330  C CA  . GLU A 1 56  ? 30.332  6.768   13.750  1.00 39.14  ? 56  GLU A CA  1 
ATOM   331  C C   . GLU A 1 56  ? 29.688  6.098   14.957  1.00 38.93  ? 56  GLU A C   1 
ATOM   332  O O   . GLU A 1 56  ? 30.289  6.093   16.039  1.00 41.24  ? 56  GLU A O   1 
ATOM   333  C CB  . GLU A 1 56  ? 29.967  8.260   13.721  1.00 40.88  ? 56  GLU A CB  1 
ATOM   334  C CG  . GLU A 1 56  ? 30.514  8.983   12.488  1.00 43.07  ? 56  GLU A CG  1 
ATOM   335  C CD  . GLU A 1 56  ? 29.817  10.296  12.198  1.00 49.91  ? 56  GLU A CD  1 
ATOM   336  O OE1 . GLU A 1 56  ? 28.669  10.482  12.662  1.00 50.23  ? 56  GLU A OE1 1 
ATOM   337  O OE2 . GLU A 1 56  ? 30.408  11.143  11.486  1.00 50.46  ? 56  GLU A OE2 1 
ATOM   338  N N   . ALA A 1 57  ? 28.499  5.501   14.800  1.00 37.90  ? 57  ALA A N   1 
ATOM   339  C CA  . ALA A 1 57  ? 27.757  4.932   15.921  1.00 34.64  ? 57  ALA A CA  1 
ATOM   340  C C   . ALA A 1 57  ? 27.960  3.427   16.081  1.00 37.10  ? 57  ALA A C   1 
ATOM   341  O O   . ALA A 1 57  ? 27.399  2.834   17.008  1.00 34.32  ? 57  ALA A O   1 
ATOM   342  C CB  . ALA A 1 57  ? 26.258  5.236   15.771  1.00 34.67  ? 57  ALA A CB  1 
ATOM   343  N N   . SER A 1 58  ? 28.728  2.797   15.198  1.00 38.17  ? 58  SER A N   1 
ATOM   344  C CA  . SER A 1 58  ? 29.078  1.387   15.322  1.00 39.61  ? 58  SER A CA  1 
ATOM   345  C C   . SER A 1 58  ? 30.538  1.213   14.937  1.00 43.88  ? 58  SER A C   1 
ATOM   346  O O   . SER A 1 58  ? 31.019  1.855   14.006  1.00 44.63  ? 58  SER A O   1 
ATOM   347  C CB  . SER A 1 58  ? 28.173  0.512   14.436  1.00 38.13  ? 58  SER A CB  1 
ATOM   348  O OG  . SER A 1 58  ? 28.419  0.749   13.061  1.00 41.51  ? 58  SER A OG  1 
ATOM   349  N N   . GLU A 1 59  ? 31.242  0.349   15.645  1.00 47.12  ? 59  GLU A N   1 
ATOM   350  C CA  . GLU A 1 59  ? 32.655  0.166   15.372  1.00 50.72  ? 59  GLU A CA  1 
ATOM   351  C C   . GLU A 1 59  ? 32.865  -0.815  14.243  1.00 51.53  ? 59  GLU A C   1 
ATOM   352  O O   . GLU A 1 59  ? 32.118  -1.784  14.103  1.00 50.84  ? 59  GLU A O   1 
ATOM   353  C CB  . GLU A 1 59  ? 33.392  -0.328  16.602  1.00 53.24  ? 59  GLU A CB  1 
ATOM   354  C CG  . GLU A 1 59  ? 33.638  0.736   17.598  1.00 57.26  ? 59  GLU A CG  1 
ATOM   355  C CD  . GLU A 1 59  ? 33.001  0.354   18.927  1.00 58.76  ? 59  GLU A CD  1 
ATOM   356  O OE1 . GLU A 1 59  ? 32.080  -0.458  18.955  1.00 60.20  ? 59  GLU A OE1 1 
ATOM   357  O OE2 . GLU A 1 59  ? 33.478  0.906   19.944  1.00 62.18  ? 59  GLU A OE2 1 
ATOM   358  N N   . GLU A 1 60  ? 33.925  -0.576  13.480  1.00 53.96  ? 60  GLU A N   1 
ATOM   359  C CA  . GLU A 1 60  ? 34.268  -1.417  12.350  1.00 54.53  ? 60  GLU A CA  1 
ATOM   360  C C   . GLU A 1 60  ? 34.473  -2.857  12.808  1.00 55.28  ? 60  GLU A C   1 
ATOM   361  O O   . GLU A 1 60  ? 35.005  -3.114  13.892  1.00 53.28  ? 60  GLU A O   1 
ATOM   362  C CB  . GLU A 1 60  ? 35.530  -0.855  11.689  1.00 59.80  ? 60  GLU A CB  1 
ATOM   363  C CG  . GLU A 1 60  ? 36.212  -1.769  10.697  1.00 63.46  ? 60  GLU A CG  1 
ATOM   364  C CD  . GLU A 1 60  ? 37.279  -2.644  11.325  1.00 66.71  ? 60  GLU A CD  1 
ATOM   365  O OE1 . GLU A 1 60  ? 37.608  -2.464  12.520  1.00 66.80  ? 60  GLU A OE1 1 
ATOM   366  O OE2 . GLU A 1 60  ? 37.781  -3.533  10.610  1.00 68.17  ? 60  GLU A OE2 1 
ATOM   367  N N   . GLY A 1 61  ? 34.019  -3.801  11.985  1.00 55.69  ? 61  GLY A N   1 
ATOM   368  C CA  . GLY A 1 61  ? 34.179  -5.209  12.270  1.00 54.67  ? 61  GLY A CA  1 
ATOM   369  C C   . GLY A 1 61  ? 33.244  -5.774  13.315  1.00 56.48  ? 61  GLY A C   1 
ATOM   370  O O   . GLY A 1 61  ? 33.288  -6.986  13.567  1.00 54.28  ? 61  GLY A O   1 
ATOM   371  N N   . THR A 1 62  ? 32.408  -4.948  13.939  1.00 51.38  ? 62  THR A N   1 
ATOM   372  C CA  . THR A 1 62  ? 31.463  -5.463  14.916  1.00 48.20  ? 62  THR A CA  1 
ATOM   373  C C   . THR A 1 62  ? 30.223  -6.015  14.222  1.00 47.68  ? 62  THR A C   1 
ATOM   374  O O   . THR A 1 62  ? 29.947  -5.734  13.052  1.00 48.69  ? 62  THR A O   1 
ATOM   375  C CB  . THR A 1 62  ? 31.042  -4.381  15.916  1.00 47.84  ? 62  THR A CB  1 
ATOM   376  O OG1 . THR A 1 62  ? 30.427  -3.283  15.222  1.00 45.10  ? 62  THR A OG1 1 
ATOM   377  C CG2 . THR A 1 62  ? 32.247  -3.875  16.709  1.00 50.86  ? 62  THR A CG2 1 
ATOM   378  N N   . ARG A 1 63  ? 29.470  -6.813  14.976  1.00 47.78  ? 63  ARG A N   1 
ATOM   379  C CA  . ARG A 1 63  ? 28.219  -7.358  14.470  1.00 46.16  ? 63  ARG A CA  1 
ATOM   380  C C   . ARG A 1 63  ? 27.222  -6.249  14.170  1.00 47.66  ? 63  ARG A C   1 
ATOM   381  O O   . ARG A 1 63  ? 26.499  -6.302  13.167  1.00 45.69  ? 63  ARG A O   1 
ATOM   382  C CB  . ARG A 1 63  ? 27.634  -8.317  15.497  1.00 51.30  ? 63  ARG A CB  1 
ATOM   383  C CG  . ARG A 1 63  ? 26.417  -9.060  15.029  1.00 53.52  ? 63  ARG A CG  1 
ATOM   384  C CD  . ARG A 1 63  ? 25.793  -9.899  16.134  1.00 57.91  ? 63  ARG A CD  1 
ATOM   385  N NE  . ARG A 1 63  ? 26.579  -11.065 16.539  1.00 65.12  ? 63  ARG A NE  1 
ATOM   386  C CZ  . ARG A 1 63  ? 27.605  -11.056 17.384  1.00 64.35  ? 63  ARG A CZ  1 
ATOM   387  N NH1 . ARG A 1 63  ? 27.957  -9.961  18.041  1.00 64.33  ? 63  ARG A NH1 1 
ATOM   388  N NH2 . ARG A 1 63  ? 28.274  -12.185 17.604  1.00 64.74  ? 63  ARG A NH2 1 
ATOM   389  N N   . GLU A 1 64  ? 27.160  -5.245  15.047  1.00 45.98  ? 64  GLU A N   1 
ATOM   390  C CA  . GLU A 1 64  ? 26.195  -4.168  14.869  1.00 42.72  ? 64  GLU A CA  1 
ATOM   391  C C   . GLU A 1 64  ? 26.501  -3.355  13.621  1.00 43.20  ? 64  GLU A C   1 
ATOM   392  O O   . GLU A 1 64  ? 25.575  -2.894  12.944  1.00 40.81  ? 64  GLU A O   1 
ATOM   393  C CB  . GLU A 1 64  ? 26.179  -3.278  16.112  1.00 39.07  ? 64  GLU A CB  1 
ATOM   394  C CG  . GLU A 1 64  ? 27.535  -2.757  16.548  1.00 41.64  ? 64  GLU A CG  1 
ATOM   395  C CD  . GLU A 1 64  ? 28.193  -3.627  17.603  1.00 44.37  ? 64  GLU A CD  1 
ATOM   396  O OE1 . GLU A 1 64  ? 27.927  -4.853  17.621  1.00 45.62  ? 64  GLU A OE1 1 
ATOM   397  O OE2 . GLU A 1 64  ? 28.967  -3.080  18.420  1.00 40.19  ? 64  GLU A OE2 1 
ATOM   398  N N   . ARG A 1 65  ? 27.785  -3.173  13.299  1.00 39.50  ? 65  ARG A N   1 
ATOM   399  C CA  . ARG A 1 65  ? 28.150  -2.522  12.045  1.00 45.80  ? 65  ARG A CA  1 
ATOM   400  C C   . ARG A 1 65  ? 27.638  -3.312  10.847  1.00 44.42  ? 65  ARG A C   1 
ATOM   401  O O   . ARG A 1 65  ? 27.079  -2.733  9.906   1.00 43.68  ? 65  ARG A O   1 
ATOM   402  C CB  . ARG A 1 65  ? 29.669  -2.328  11.981  1.00 42.45  ? 65  ARG A CB  1 
ATOM   403  C CG  . ARG A 1 65  ? 30.201  -1.760  10.672  1.00 45.54  ? 65  ARG A CG  1 
ATOM   404  C CD  . ARG A 1 65  ? 29.729  -0.323  10.479  1.00 44.31  ? 65  ARG A CD  1 
ATOM   405  N NE  . ARG A 1 65  ? 30.591  0.697   11.066  1.00 46.44  ? 65  ARG A NE  1 
ATOM   406  C CZ  . ARG A 1 65  ? 31.841  0.956   10.704  1.00 47.72  ? 65  ARG A CZ  1 
ATOM   407  N NH1 . ARG A 1 65  ? 32.434  0.288   9.729   1.00 52.81  ? 65  ARG A NH1 1 
ATOM   408  N NH2 . ARG A 1 65  ? 32.503  1.931   11.320  1.00 47.93  ? 65  ARG A NH2 1 
ATOM   409  N N   . ARG A 1 66  ? 27.792  -4.638  10.871  1.00 46.92  ? 66  ARG A N   1 
ATOM   410  C CA  . ARG A 1 66  ? 27.292  -5.455  9.768   1.00 44.79  ? 66  ARG A CA  1 
ATOM   411  C C   . ARG A 1 66  ? 25.773  -5.394  9.672   1.00 45.22  ? 66  ARG A C   1 
ATOM   412  O O   . ARG A 1 66  ? 25.220  -5.302  8.571   1.00 44.74  ? 66  ARG A O   1 
ATOM   413  C CB  . ARG A 1 66  ? 27.759  -6.903  9.926   1.00 47.54  ? 66  ARG A CB  1 
ATOM   414  C CG  . ARG A 1 66  ? 29.265  -7.073  10.048  1.00 51.04  ? 66  ARG A CG  1 
ATOM   415  C CD  . ARG A 1 66  ? 29.683  -8.508  9.700   1.00 58.40  ? 66  ARG A CD  1 
ATOM   416  N NE  . ARG A 1 66  ? 29.444  -9.400  10.830  1.00 52.53  ? 66  ARG A NE  1 
ATOM   417  C CZ  . ARG A 1 66  ? 30.247  -9.495  11.882  1.00 53.56  ? 66  ARG A CZ  1 
ATOM   418  N NH1 . ARG A 1 66  ? 31.375  -8.804  11.954  1.00 55.71  ? 66  ARG A NH1 1 
ATOM   419  N NH2 . ARG A 1 66  ? 29.905  -10.290 12.891  1.00 56.66  ? 66  ARG A NH2 1 
ATOM   420  N N   . ARG A 1 67  ? 25.079  -5.453  10.813  1.00 42.52  ? 67  ARG A N   1 
ATOM   421  C CA  . ARG A 1 67  ? 23.619  -5.399  10.787  1.00 41.38  ? 67  ARG A CA  1 
ATOM   422  C C   . ARG A 1 67  ? 23.129  -4.040  10.295  1.00 41.84  ? 67  ARG A C   1 
ATOM   423  O O   . ARG A 1 67  ? 22.115  -3.952  9.587   1.00 40.45  ? 67  ARG A O   1 
ATOM   424  C CB  . ARG A 1 67  ? 23.064  -5.708  12.175  1.00 42.14  ? 67  ARG A CB  1 
ATOM   425  C CG  . ARG A 1 67  ? 22.822  -7.195  12.398  1.00 47.67  ? 67  ARG A CG  1 
ATOM   426  C CD  . ARG A 1 67  ? 22.718  -7.574  13.869  1.00 50.33  ? 67  ARG A CD  1 
ATOM   427  N NE  . ARG A 1 67  ? 21.333  -7.749  14.296  1.00 53.71  ? 67  ARG A NE  1 
ATOM   428  C CZ  . ARG A 1 67  ? 20.961  -8.082  15.526  1.00 48.86  ? 67  ARG A CZ  1 
ATOM   429  N NH1 . ARG A 1 67  ? 21.849  -8.321  16.479  1.00 54.33  ? 67  ARG A NH1 1 
ATOM   430  N NH2 . ARG A 1 67  ? 19.664  -8.184  15.806  1.00 55.76  ? 67  ARG A NH2 1 
ATOM   431  N N   . ALA A 1 68  ? 23.866  -2.983  10.593  1.00 39.69  ? 68  ALA A N   1 
ATOM   432  C CA  . ALA A 1 68  ? 23.473  -1.643  10.108  1.00 41.22  ? 68  ALA A CA  1 
ATOM   433  C C   . ALA A 1 68  ? 23.602  -1.570  8.589   1.00 44.16  ? 68  ALA A C   1 
ATOM   434  O O   . ALA A 1 68  ? 22.751  -0.951  7.953   1.00 43.16  ? 68  ALA A O   1 
ATOM   435  C CB  . ALA A 1 68  ? 24.311  -0.590  10.778  1.00 39.35  ? 68  ALA A CB  1 
ATOM   436  N N   . LEU A 1 69  ? 24.640  -2.194  8.037   1.00 47.12  ? 69  LEU A N   1 
ATOM   437  C CA  . LEU A 1 69  ? 24.876  -2.099  6.574   1.00 49.17  ? 69  LEU A CA  1 
ATOM   438  C C   . LEU A 1 69  ? 23.808  -2.901  5.834   1.00 45.31  ? 69  LEU A C   1 
ATOM   439  O O   . LEU A 1 69  ? 23.297  -2.403  4.832   1.00 49.79  ? 69  LEU A O   1 
ATOM   440  C CB  . LEU A 1 69  ? 26.291  -2.597  6.274   1.00 51.74  ? 69  LEU A CB  1 
ATOM   441  C CG  . LEU A 1 69  ? 27.401  -1.684  6.791   1.00 50.08  ? 69  LEU A CG  1 
ATOM   442  C CD1 . LEU A 1 69  ? 28.727  -2.421  6.883   1.00 52.62  ? 69  LEU A CD1 1 
ATOM   443  C CD2 . LEU A 1 69  ? 27.534  -0.451  5.914   1.00 54.43  ? 69  LEU A CD2 1 
ATOM   444  N N   . ILE A 1 70  ? 23.470  -4.083  6.332   1.00 47.15  ? 70  ILE A N   1 
ATOM   445  C CA  . ILE A 1 70  ? 22.373  -4.873  5.707   1.00 47.05  ? 70  ILE A CA  1 
ATOM   446  C C   . ILE A 1 70  ? 21.088  -4.043  5.726   1.00 47.25  ? 70  ILE A C   1 
ATOM   447  O O   . ILE A 1 70  ? 20.359  -4.069  4.730   1.00 41.23  ? 70  ILE A O   1 
ATOM   448  C CB  . ILE A 1 70  ? 22.172  -6.200  6.454   1.00 50.42  ? 70  ILE A CB  1 
ATOM   449  C CG1 . ILE A 1 70  ? 23.446  -7.047  6.462   1.00 51.56  ? 70  ILE A CG1 1 
ATOM   450  C CG2 . ILE A 1 70  ? 20.991  -6.965  5.880   1.00 52.15  ? 70  ILE A CG2 1 
ATOM   451  C CD1 . ILE A 1 70  ? 23.538  -7.991  7.636   1.00 57.83  ? 70  ILE A CD1 1 
ATOM   452  N N   . ARG A 1 71  ? 20.838  -3.338  6.832   1.00 42.59  ? 71  ARG A N   1 
ATOM   453  C CA  . ARG A 1 71  ? 19.593  -2.538  6.984   1.00 43.33  ? 71  ARG A CA  1 
ATOM   454  C C   . ARG A 1 71  ? 19.523  -1.471  5.892   1.00 37.00  ? 71  ARG A C   1 
ATOM   455  O O   . ARG A 1 71  ? 18.418  -1.052  5.564   1.00 36.09  ? 71  ARG A O   1 
ATOM   456  C CB  . ARG A 1 71  ? 19.541  -1.937  8.396   1.00 40.73  ? 71  ARG A CB  1 
ATOM   457  C CG  . ARG A 1 71  ? 18.326  -1.078  8.702   1.00 38.43  ? 71  ARG A CG  1 
ATOM   458  C CD  . ARG A 1 71  ? 18.139  -1.007  10.202  1.00 37.29  ? 71  ARG A CD  1 
ATOM   459  N NE  . ARG A 1 71  ? 19.266  -0.414  10.904  1.00 34.55  ? 71  ARG A NE  1 
ATOM   460  C CZ  . ARG A 1 71  ? 20.031  -1.050  11.782  1.00 34.18  ? 71  ARG A CZ  1 
ATOM   461  N NH1 . ARG A 1 71  ? 19.799  -2.318  12.068  1.00 35.10  ? 71  ARG A NH1 1 
ATOM   462  N NH2 . ARG A 1 71  ? 21.027  -0.415  12.370  1.00 33.49  ? 71  ARG A NH2 1 
ATOM   463  N N   . HIS A 1 72  ? 20.668  -1.081  5.332   1.00 38.70  ? 72  HIS A N   1 
ATOM   464  C CA  . HIS A 1 72  ? 20.615  0.007   4.362   1.00 39.31  ? 72  HIS A CA  1 
ATOM   465  C C   . HIS A 1 72  ? 21.077  -0.419  2.972   1.00 45.17  ? 72  HIS A C   1 
ATOM   466  O O   . HIS A 1 72  ? 21.605  0.398   2.216   1.00 47.62  ? 72  HIS A O   1 
ATOM   467  C CB  . HIS A 1 72  ? 21.436  1.192   4.866   1.00 42.71  ? 72  HIS A CB  1 
ATOM   468  C CG  . HIS A 1 72  ? 20.954  1.716   6.180   1.00 40.08  ? 72  HIS A CG  1 
ATOM   469  N ND1 . HIS A 1 72  ? 19.737  2.348   6.329   1.00 37.38  ? 72  HIS A ND1 1 
ATOM   470  C CD2 . HIS A 1 72  ? 21.492  1.634   7.419   1.00 41.14  ? 72  HIS A CD2 1 
ATOM   471  C CE1 . HIS A 1 72  ? 19.561  2.655   7.603   1.00 36.81  ? 72  HIS A CE1 1 
ATOM   472  N NE2 . HIS A 1 72  ? 20.611  2.235   8.284   1.00 38.10  ? 72  HIS A NE2 1 
ATOM   473  N N   . THR A 1 73  ? 20.858  -1.684  2.600   1.00 42.28  ? 73  THR A N   1 
ATOM   474  C CA  . THR A 1 73  ? 21.263  -2.142  1.276   1.00 44.61  ? 73  THR A CA  1 
ATOM   475  C C   . THR A 1 73  ? 20.113  -2.790  0.512   1.00 44.57  ? 73  THR A C   1 
ATOM   476  O O   . THR A 1 73  ? 20.348  -3.574  -0.411  1.00 50.04  ? 73  THR A O   1 
ATOM   477  C CB  . THR A 1 73  ? 22.435  -3.119  1.356   1.00 44.81  ? 73  THR A CB  1 
ATOM   478  O OG1 . THR A 1 73  ? 22.137  -4.139  2.314   1.00 46.97  ? 73  THR A OG1 1 
ATOM   479  C CG2 . THR A 1 73  ? 23.708  -2.391  1.757   1.00 47.48  ? 73  THR A CG2 1 
ATOM   480  N N   . ASN A 1 74  ? 18.876  -2.493  0.873   1.00 42.12  ? 74  ASN A N   1 
ATOM   481  C CA  . ASN A 1 74  ? 17.752  -2.975  0.065   1.00 42.70  ? 74  ASN A CA  1 
ATOM   482  C C   . ASN A 1 74  ? 17.755  -2.226  -1.262  1.00 44.59  ? 74  ASN A C   1 
ATOM   483  O O   . ASN A 1 74  ? 17.676  -0.993  -1.266  1.00 43.55  ? 74  ASN A O   1 
ATOM   484  C CB  . ASN A 1 74  ? 16.424  -2.776  0.810   1.00 39.15  ? 74  ASN A CB  1 
ATOM   485  C CG  . ASN A 1 74  ? 15.236  -3.407  0.091   1.00 44.83  ? 74  ASN A CG  1 
ATOM   486  O OD1 . ASN A 1 74  ? 15.341  -3.817  -1.067  1.00 41.71  ? 74  ASN A OD1 1 
ATOM   487  N ND2 . ASN A 1 74  ? 14.102  -3.488  0.778   1.00 42.21  ? 74  ASN A ND2 1 
ATOM   488  N N   . PRO A 1 75  ? 17.853  -2.914  -2.401  1.00 46.24  ? 75  PRO A N   1 
ATOM   489  C CA  . PRO A 1 75  ? 17.827  -2.203  -3.691  1.00 43.23  ? 75  PRO A CA  1 
ATOM   490  C C   . PRO A 1 75  ? 16.544  -1.424  -3.926  1.00 43.56  ? 75  PRO A C   1 
ATOM   491  O O   . PRO A 1 75  ? 16.531  -0.496  -4.745  1.00 46.31  ? 75  PRO A O   1 
ATOM   492  C CB  . PRO A 1 75  ? 17.983  -3.325  -4.737  1.00 46.36  ? 75  PRO A CB  1 
ATOM   493  C CG  . PRO A 1 75  ? 18.024  -4.608  -4.003  1.00 48.23  ? 75  PRO A CG  1 
ATOM   494  C CD  . PRO A 1 75  ? 18.083  -4.362  -2.533  1.00 46.42  ? 75  PRO A CD  1 
ATOM   495  N N   . TYR A 1 76  ? 15.461  -1.775  -3.237  1.00 42.17  ? 76  TYR A N   1 
ATOM   496  C CA  . TYR A 1 76  ? 14.170  -1.128  -3.429  1.00 41.97  ? 76  TYR A CA  1 
ATOM   497  C C   . TYR A 1 76  ? 13.955  0.092   -2.556  1.00 40.81  ? 76  TYR A C   1 
ATOM   498  O O   . TYR A 1 76  ? 12.948  0.785   -2.733  1.00 40.16  ? 76  TYR A O   1 
ATOM   499  C CB  . TYR A 1 76  ? 13.043  -2.128  -3.194  1.00 42.51  ? 76  TYR A CB  1 
ATOM   500  C CG  . TYR A 1 76  ? 13.005  -3.221  -4.231  1.00 45.69  ? 76  TYR A CG  1 
ATOM   501  C CD1 . TYR A 1 76  ? 13.779  -4.366  -4.105  1.00 44.66  ? 76  TYR A CD1 1 
ATOM   502  C CD2 . TYR A 1 76  ? 12.181  -3.099  -5.344  1.00 45.85  ? 76  TYR A CD2 1 
ATOM   503  C CE1 . TYR A 1 76  ? 13.733  -5.367  -5.067  1.00 48.64  ? 76  TYR A CE1 1 
ATOM   504  C CE2 . TYR A 1 76  ? 12.130  -4.085  -6.305  1.00 49.51  ? 76  TYR A CE2 1 
ATOM   505  C CZ  . TYR A 1 76  ? 12.902  -5.219  -6.160  1.00 52.17  ? 76  TYR A CZ  1 
ATOM   506  O OH  . TYR A 1 76  ? 12.844  -6.203  -7.122  1.00 52.69  ? 76  TYR A OH  1 
ATOM   507  N N   . GLY A 1 77  ? 14.863  0.384   -1.643  1.00 41.04  ? 77  GLY A N   1 
ATOM   508  C CA  . GLY A 1 77  ? 14.776  1.593   -0.851  1.00 38.47  ? 77  GLY A CA  1 
ATOM   509  C C   . GLY A 1 77  ? 15.128  1.316   0.595   1.00 39.27  ? 77  GLY A C   1 
ATOM   510  O O   . GLY A 1 77  ? 15.159  0.175   1.059   1.00 35.83  ? 77  GLY A O   1 
ATOM   511  N N   . ASP A 1 78  ? 15.382  2.333   1.285   1.00 38.72  ? 78  ASP A N   1 
ATOM   512  C CA  . ASP A 1 78  ? 15.788  2.372   2.676   1.00 35.01  ? 78  ASP A CA  1 
ATOM   513  C C   . ASP A 1 78  ? 14.572  2.344   3.597   1.00 31.76  ? 78  ASP A C   1 
ATOM   514  O O   . ASP A 1 78  ? 13.523  2.903   3.260   1.00 32.53  ? 78  ASP A O   1 
ATOM   515  C CB  . ASP A 1 78  ? 16.594  3.637   2.936   1.00 34.34  ? 78  ASP A CB  1 
ATOM   516  C CG  . ASP A 1 78  ? 17.348  3.579   4.226   1.00 36.57  ? 78  ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 78  ? 16.760  4.002   5.243   1.00 34.93  ? 78  ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 78  ? 18.503  3.108   4.228   1.00 37.40  ? 78  ASP A OD2 1 
ATOM   519  N N   . PRO A 1 79  ? 14.681  1.714   4.772   1.00 30.87  ? 79  PRO A N   1 
ATOM   520  C CA  . PRO A 1 79  ? 13.542  1.722   5.700   1.00 31.38  ? 79  PRO A CA  1 
ATOM   521  C C   . PRO A 1 79  ? 13.119  3.119   6.103   1.00 30.31  ? 79  PRO A C   1 
ATOM   522  O O   . PRO A 1 79  ? 11.915  3.365   6.248   1.00 29.71  ? 79  PRO A O   1 
ATOM   523  C CB  . PRO A 1 79  ? 14.050  0.912   6.898   1.00 32.91  ? 79  PRO A CB  1 
ATOM   524  C CG  . PRO A 1 79  ? 15.545  0.975   6.791   1.00 34.26  ? 79  PRO A CG  1 
ATOM   525  C CD  . PRO A 1 79  ? 15.810  0.939   5.309   1.00 32.58  ? 79  PRO A CD  1 
ATOM   526  N N   . PHE A 1 80  ? 14.060  4.054   6.246   1.00 29.09  ? 80  PHE A N   1 
ATOM   527  C CA  . PHE A 1 80  ? 13.679  5.394   6.679   1.00 29.07  ? 80  PHE A CA  1 
ATOM   528  C C   . PHE A 1 80  ? 13.076  6.212   5.551   1.00 30.17  ? 80  PHE A C   1 
ATOM   529  O O   . PHE A 1 80  ? 12.092  6.924   5.771   1.00 29.42  ? 80  PHE A O   1 
ATOM   530  C CB  . PHE A 1 80  ? 14.875  6.122   7.294   1.00 28.08  ? 80  PHE A CB  1 
ATOM   531  C CG  . PHE A 1 80  ? 15.247  5.585   8.629   1.00 30.66  ? 80  PHE A CG  1 
ATOM   532  C CD1 . PHE A 1 80  ? 14.451  5.859   9.733   1.00 30.53  ? 80  PHE A CD1 1 
ATOM   533  C CD2 . PHE A 1 80  ? 16.338  4.740   8.783   1.00 29.23  ? 80  PHE A CD2 1 
ATOM   534  C CE1 . PHE A 1 80  ? 14.752  5.332   10.976  1.00 30.25  ? 80  PHE A CE1 1 
ATOM   535  C CE2 . PHE A 1 80  ? 16.651  4.213   10.038  1.00 31.20  ? 80  PHE A CE2 1 
ATOM   536  C CZ  . PHE A 1 80  ? 15.847  4.510   11.132  1.00 28.72  ? 80  PHE A CZ  1 
ATOM   537  N N   . THR A 1 81  ? 13.650  6.135   4.351   1.00 29.70  ? 81  THR A N   1 
ATOM   538  C CA  . THR A 1 81  ? 13.149  6.967   3.265   1.00 29.86  ? 81  THR A CA  1 
ATOM   539  C C   . THR A 1 81  ? 11.796  6.478   2.777   1.00 31.68  ? 81  THR A C   1 
ATOM   540  O O   . THR A 1 81  ? 11.040  7.254   2.182   1.00 29.97  ? 81  THR A O   1 
ATOM   541  C CB  . THR A 1 81  ? 14.141  6.988   2.103   1.00 32.21  ? 81  THR A CB  1 
ATOM   542  O OG1 . THR A 1 81  ? 14.369  5.652   1.646   1.00 34.32  ? 81  THR A OG1 1 
ATOM   543  C CG2 . THR A 1 81  ? 15.472  7.591   2.550   1.00 32.65  ? 81  THR A CG2 1 
ATOM   544  N N   . ILE A 1 82  ? 11.476  5.208   3.022   1.00 29.09  ? 82  ILE A N   1 
ATOM   545  C CA  . ILE A 1 82  ? 10.168  4.675   2.677   1.00 29.20  ? 82  ILE A CA  1 
ATOM   546  C C   . ILE A 1 82  ? 9.190   4.911   3.817   1.00 29.69  ? 82  ILE A C   1 
ATOM   547  O O   . ILE A 1 82  ? 8.177   5.585   3.634   1.00 29.72  ? 82  ILE A O   1 
ATOM   548  C CB  . ILE A 1 82  ? 10.246  3.182   2.314   1.00 30.17  ? 82  ILE A CB  1 
ATOM   549  C CG1 . ILE A 1 82  ? 11.063  2.992   1.033   1.00 31.85  ? 82  ILE A CG1 1 
ATOM   550  C CG2 . ILE A 1 82  ? 8.856   2.588   2.169   1.00 29.68  ? 82  ILE A CG2 1 
ATOM   551  C CD1 . ILE A 1 82  ? 11.460  1.527   0.770   1.00 32.18  ? 82  ILE A CD1 1 
ATOM   552  N N   . CYS A 1 83  ? 9.479   4.373   4.996   1.00 28.32  ? 83  CYS A N   1 
ATOM   553  C CA  . CYS A 1 83  ? 8.477   4.445   6.093   1.00 26.55  ? 83  CYS A CA  1 
ATOM   554  C C   . CYS A 1 83  ? 8.204   5.889   6.515   1.00 28.10  ? 83  CYS A C   1 
ATOM   555  O O   . CYS A 1 83  ? 7.063   6.187   6.839   1.00 28.58  ? 83  CYS A O   1 
ATOM   556  C CB  . CYS A 1 83  ? 8.942   3.617   7.279   1.00 28.10  ? 83  CYS A CB  1 
ATOM   557  S SG  . CYS A 1 83  ? 9.146   1.867   6.872   1.00 30.19  ? 83  CYS A SG  1 
ATOM   558  N N   . HIS A 1 84  ? 9.234   6.725   6.537   1.00 29.39  ? 84  HIS A N   1 
ATOM   559  C CA  . HIS A 1 84  ? 9.070   8.114   6.943   1.00 26.45  ? 84  HIS A CA  1 
ATOM   560  C C   . HIS A 1 84  ? 9.042   9.060   5.749   1.00 27.86  ? 84  HIS A C   1 
ATOM   561  O O   . HIS A 1 84  ? 9.439   10.229  5.864   1.00 29.66  ? 84  HIS A O   1 
ATOM   562  C CB  . HIS A 1 84  ? 10.174  8.494   7.927   1.00 26.15  ? 84  HIS A CB  1 
ATOM   563  C CG  . HIS A 1 84  ? 10.084  7.759   9.225   1.00 27.38  ? 84  HIS A CG  1 
ATOM   564  N ND1 . HIS A 1 84  ? 9.379   8.250   10.302  1.00 27.40  ? 84  HIS A ND1 1 
ATOM   565  C CD2 . HIS A 1 84  ? 10.572  6.555   9.610   1.00 32.17  ? 84  HIS A CD2 1 
ATOM   566  C CE1 . HIS A 1 84  ? 9.454   7.390   11.304  1.00 29.24  ? 84  HIS A CE1 1 
ATOM   567  N NE2 . HIS A 1 84  ? 10.171  6.352   10.909  1.00 28.53  ? 84  HIS A NE2 1 
ATOM   568  N N   . CYS A 1 85  ? 8.550   8.571   4.600   1.00 28.59  ? 85  CYS A N   1 
ATOM   569  C CA  . CYS A 1 85  ? 8.510   9.375   3.380   1.00 29.56  ? 85  CYS A CA  1 
ATOM   570  C C   . CYS A 1 85  ? 7.652   10.627  3.513   1.00 30.59  ? 85  CYS A C   1 
ATOM   571  O O   . CYS A 1 85  ? 7.814   11.553  2.714   1.00 32.22  ? 85  CYS A O   1 
ATOM   572  C CB  . CYS A 1 85  ? 8.024   8.495   2.213   1.00 31.43  ? 85  CYS A CB  1 
ATOM   573  S SG  . CYS A 1 85  ? 6.284   8.029   2.308   1.00 32.07  ? 85  CYS A SG  1 
ATOM   574  N N   . SER A 1 86  ? 6.752   10.684  4.496   1.00 27.31  ? 86  SER A N   1 
ATOM   575  C CA  . SER A 1 86  ? 5.899   11.844  4.720   1.00 29.03  ? 86  SER A CA  1 
ATOM   576  C C   . SER A 1 86  ? 6.624   13.034  5.350   1.00 29.73  ? 86  SER A C   1 
ATOM   577  O O   . SER A 1 86  ? 6.049   14.131  5.392   1.00 30.46  ? 86  SER A O   1 
ATOM   578  C CB  . SER A 1 86  ? 4.734   11.431  5.611   1.00 29.20  ? 86  SER A CB  1 
ATOM   579  O OG  . SER A 1 86  ? 5.212   10.904  6.840   1.00 30.61  ? 86  SER A OG  1 
ATOM   580  N N   . ALA A 1 87  ? 7.843   12.849  5.854   1.00 26.63  ? 87  ALA A N   1 
ATOM   581  C CA  . ALA A 1 87  ? 8.516   13.894  6.619   1.00 26.66  ? 87  ALA A CA  1 
ATOM   582  C C   . ALA A 1 87  ? 9.162   14.944  5.716   1.00 32.83  ? 87  ALA A C   1 
ATOM   583  O O   . ALA A 1 87  ? 9.632   14.651  4.614   1.00 32.62  ? 87  ALA A O   1 
ATOM   584  C CB  . ALA A 1 87  ? 9.592   13.291  7.528   1.00 27.45  ? 87  ALA A CB  1 
ATOM   585  N N   . PHE A 1 88  ? 9.208   16.180  6.209   1.00 31.63  ? 88  PHE A N   1 
ATOM   586  C CA  . PHE A 1 88  ? 10.026  17.184  5.543   1.00 35.18  ? 88  PHE A CA  1 
ATOM   587  C C   . PHE A 1 88  ? 11.473  16.698  5.481   1.00 30.84  ? 88  PHE A C   1 
ATOM   588  O O   . PHE A 1 88  ? 11.978  16.132  6.464   1.00 31.43  ? 88  PHE A O   1 
ATOM   589  C CB  . PHE A 1 88  ? 9.964   18.520  6.286   1.00 35.85  ? 88  PHE A CB  1 
ATOM   590  C CG  . PHE A 1 88  ? 8.632   19.218  6.186   1.00 34.48  ? 88  PHE A CG  1 
ATOM   591  C CD1 . PHE A 1 88  ? 8.165   19.699  4.972   1.00 40.74  ? 88  PHE A CD1 1 
ATOM   592  C CD2 . PHE A 1 88  ? 7.857   19.409  7.320   1.00 35.01  ? 88  PHE A CD2 1 
ATOM   593  C CE1 . PHE A 1 88  ? 6.954   20.349  4.901   1.00 41.53  ? 88  PHE A CE1 1 
ATOM   594  C CE2 . PHE A 1 88  ? 6.646   20.038  7.255   1.00 37.15  ? 88  PHE A CE2 1 
ATOM   595  C CZ  . PHE A 1 88  ? 6.186   20.511  6.040   1.00 38.31  ? 88  PHE A CZ  1 
ATOM   596  N N   . PRO A 1 89  ? 12.163  16.886  4.345   1.00 33.28  ? 89  PRO A N   1 
ATOM   597  C CA  . PRO A 1 89  ? 13.529  16.345  4.201   1.00 32.54  ? 89  PRO A CA  1 
ATOM   598  C C   . PRO A 1 89  ? 14.512  16.714  5.300   1.00 31.34  ? 89  PRO A C   1 
ATOM   599  O O   . PRO A 1 89  ? 15.289  15.847  5.720   1.00 31.61  ? 89  PRO A O   1 
ATOM   600  C CB  . PRO A 1 89  ? 13.959  16.896  2.840   1.00 34.18  ? 89  PRO A CB  1 
ATOM   601  C CG  . PRO A 1 89  ? 12.652  16.831  2.047   1.00 35.44  ? 89  PRO A CG  1 
ATOM   602  C CD  . PRO A 1 89  ? 11.590  17.278  3.041   1.00 34.07  ? 89  PRO A CD  1 
ATOM   603  N N   . ASP A 1 90  ? 14.520  17.958  5.783   1.00 34.43  ? 90  ASP A N   1 
ATOM   604  C CA  . ASP A 1 90  ? 15.517  18.282  6.799   1.00 33.72  ? 90  ASP A CA  1 
ATOM   605  C C   . ASP A 1 90  ? 15.223  17.548  8.104   1.00 33.36  ? 90  ASP A C   1 
ATOM   606  O O   . ASP A 1 90  ? 16.139  17.011  8.745   1.00 35.14  ? 90  ASP A O   1 
ATOM   607  C CB  . ASP A 1 90  ? 15.621  19.808  6.979   1.00 36.30  ? 90  ASP A CB  1 
ATOM   608  C CG  . ASP A 1 90  ? 14.296  20.493  7.298   1.00 39.14  ? 90  ASP A CG  1 
ATOM   609  O OD1 . ASP A 1 90  ? 13.219  19.869  7.274   1.00 38.58  ? 90  ASP A OD1 1 
ATOM   610  O OD2 . ASP A 1 90  ? 14.339  21.724  7.530   1.00 39.54  ? 90  ASP A OD2 1 
ATOM   611  N N   . ARG A 1 91  ? 13.947  17.461  8.481   1.00 34.18  ? 91  ARG A N   1 
ATOM   612  C CA  . ARG A 1 91  ? 13.580  16.671  9.647   1.00 32.14  ? 91  ARG A CA  1 
ATOM   613  C C   . ARG A 1 91  ? 13.809  15.189  9.397   1.00 28.71  ? 91  ARG A C   1 
ATOM   614  O O   . ARG A 1 91  ? 14.192  14.457  10.317  1.00 29.73  ? 91  ARG A O   1 
ATOM   615  C CB  . ARG A 1 91  ? 12.127  16.929  10.006  1.00 30.28  ? 91  ARG A CB  1 
ATOM   616  C CG  . ARG A 1 91  ? 11.885  18.374  10.362  1.00 34.21  ? 91  ARG A CG  1 
ATOM   617  C CD  . ARG A 1 91  ? 10.600  18.562  11.104  1.00 33.89  ? 91  ARG A CD  1 
ATOM   618  N NE  . ARG A 1 91  ? 10.488  19.955  11.518  1.00 35.16  ? 91  ARG A NE  1 
ATOM   619  C CZ  . ARG A 1 91  ? 10.001  20.331  12.689  1.00 34.64  ? 91  ARG A CZ  1 
ATOM   620  N NH1 . ARG A 1 91  ? 9.572   19.443  13.574  1.00 31.01  ? 91  ARG A NH1 1 
ATOM   621  N NH2 . ARG A 1 91  ? 10.006  21.621  13.007  1.00 33.77  ? 91  ARG A NH2 1 
ATOM   622  N N   . LEU A 1 92  ? 13.577  14.731  8.163   1.00 31.60  ? 92  LEU A N   1 
ATOM   623  C CA  . LEU A 1 92  ? 13.770  13.308  7.860   1.00 28.57  ? 92  LEU A CA  1 
ATOM   624  C C   . LEU A 1 92  ? 15.211  12.878  8.108   1.00 30.47  ? 92  LEU A C   1 
ATOM   625  O O   . LEU A 1 92  ? 15.459  11.813  8.689   1.00 31.71  ? 92  LEU A O   1 
ATOM   626  C CB  . LEU A 1 92  ? 13.370  13.016  6.409   1.00 27.60  ? 92  LEU A CB  1 
ATOM   627  C CG  . LEU A 1 92  ? 13.549  11.561  5.959   1.00 28.45  ? 92  LEU A CG  1 
ATOM   628  C CD1 . LEU A 1 92  ? 12.844  10.611  6.913   1.00 29.85  ? 92  LEU A CD1 1 
ATOM   629  C CD2 . LEU A 1 92  ? 12.997  11.395  4.556   1.00 29.56  ? 92  LEU A CD2 1 
ATOM   630  N N   . ALA A 1 93  ? 16.178  13.688  7.669   1.00 28.91  ? 93  ALA A N   1 
ATOM   631  C CA  . ALA A 1 93  ? 17.579  13.353  7.883   1.00 32.28  ? 93  ALA A CA  1 
ATOM   632  C C   . ALA A 1 93  ? 17.891  13.215  9.369   1.00 32.78  ? 93  ALA A C   1 
ATOM   633  O O   . ALA A 1 93  ? 18.612  12.298  9.781   1.00 31.74  ? 93  ALA A O   1 
ATOM   634  C CB  . ALA A 1 93  ? 18.478  14.416  7.249   1.00 37.25  ? 93  ALA A CB  1 
ATOM   635  N N   . LEU A 1 94  ? 17.329  14.101  10.187  1.00 30.58  ? 94  LEU A N   1 
ATOM   636  C CA  . LEU A 1 94  ? 17.629  14.116  11.616  1.00 29.77  ? 94  LEU A CA  1 
ATOM   637  C C   . LEU A 1 94  ? 16.981  12.933  12.322  1.00 30.50  ? 94  LEU A C   1 
ATOM   638  O O   . LEU A 1 94  ? 17.648  12.184  13.051  1.00 29.33  ? 94  LEU A O   1 
ATOM   639  C CB  . LEU A 1 94  ? 17.127  15.437  12.210  1.00 30.10  ? 94  LEU A CB  1 
ATOM   640  C CG  . LEU A 1 94  ? 17.928  16.690  11.856  1.00 34.85  ? 94  LEU A CG  1 
ATOM   641  C CD1 . LEU A 1 94  ? 17.458  17.834  12.722  1.00 34.60  ? 94  LEU A CD1 1 
ATOM   642  C CD2 . LEU A 1 94  ? 19.420  16.462  12.038  1.00 38.24  ? 94  LEU A CD2 1 
ATOM   643  N N   . LEU A 1 95  ? 15.669  12.751  12.123  1.00 28.99  ? 95  LEU A N   1 
ATOM   644  C CA  . LEU A 1 95  ? 14.981  11.685  12.830  1.00 28.98  ? 95  LEU A CA  1 
ATOM   645  C C   . LEU A 1 95  ? 15.462  10.325  12.353  1.00 28.20  ? 95  LEU A C   1 
ATOM   646  O O   . LEU A 1 95  ? 15.524  9.388   13.150  1.00 28.09  ? 95  LEU A O   1 
ATOM   647  C CB  . LEU A 1 95  ? 13.463  11.826  12.673  1.00 29.02  ? 95  LEU A CB  1 
ATOM   648  C CG  . LEU A 1 95  ? 12.793  11.509  11.324  1.00 30.53  ? 95  LEU A CG  1 
ATOM   649  C CD1 . LEU A 1 95  ? 12.380  10.027  11.184  1.00 27.13  ? 95  LEU A CD1 1 
ATOM   650  C CD2 . LEU A 1 95  ? 11.606  12.419  11.128  1.00 26.85  ? 95  LEU A CD2 1 
ATOM   651  N N   . SER A 1 96  ? 15.816  10.202  11.069  1.00 29.10  ? 96  SER A N   1 
ATOM   652  C CA  . SER A 1 96  ? 16.316  8.921   10.577  1.00 30.30  ? 96  SER A CA  1 
ATOM   653  C C   . SER A 1 96  ? 17.620  8.559   11.260  1.00 28.43  ? 96  SER A C   1 
ATOM   654  O O   . SER A 1 96  ? 17.802  7.423   11.703  1.00 29.45  ? 96  SER A O   1 
ATOM   655  C CB  . SER A 1 96  ? 16.523  8.961   9.065   1.00 28.17  ? 96  SER A CB  1 
ATOM   656  O OG  . SER A 1 96  ? 15.295  9.153   8.380   1.00 28.79  ? 96  SER A OG  1 
ATOM   657  N N   . CYS A 1 97  ? 18.536  9.524   11.374  1.00 29.59  ? 97  CYS A N   1 
ATOM   658  C CA  . CYS A 1 97  ? 19.817  9.238   12.010  1.00 28.28  ? 97  CYS A CA  1 
ATOM   659  C C   . CYS A 1 97  ? 19.669  9.022   13.511  1.00 30.35  ? 97  CYS A C   1 
ATOM   660  O O   . CYS A 1 97  ? 20.374  8.187   14.088  1.00 28.86  ? 97  CYS A O   1 
ATOM   661  C CB  . CYS A 1 97  ? 20.808  10.365  11.719  1.00 29.20  ? 97  CYS A CB  1 
ATOM   662  S SG  . CYS A 1 97  ? 21.348  10.360  10.005  1.00 33.58  ? 97  CYS A SG  1 
ATOM   663  N N   . LEU A 1 98  ? 18.747  9.744   14.152  1.00 28.40  ? 98  LEU A N   1 
ATOM   664  C CA  . LEU A 1 98  ? 18.490  9.539   15.572  1.00 26.00  ? 98  LEU A CA  1 
ATOM   665  C C   . LEU A 1 98  ? 17.937  8.146   15.825  1.00 28.70  ? 98  LEU A C   1 
ATOM   666  O O   . LEU A 1 98  ? 18.431  7.409   16.687  1.00 29.39  ? 98  LEU A O   1 
ATOM   667  C CB  . LEU A 1 98  ? 17.517  10.605  16.087  1.00 29.39  ? 98  LEU A CB  1 
ATOM   668  C CG  . LEU A 1 98  ? 17.487  10.804  17.605  1.00 28.33  ? 98  LEU A CG  1 
ATOM   669  C CD1 . LEU A 1 98  ? 17.051  12.214  17.970  1.00 30.82  ? 98  LEU A CD1 1 
ATOM   670  C CD2 . LEU A 1 98  ? 16.539  9.807   18.259  1.00 30.51  ? 98  LEU A CD2 1 
ATOM   671  N N   . VAL A 1 99  ? 16.886  7.778   15.096  1.00 27.96  ? 99  VAL A N   1 
ATOM   672  C CA  . VAL A 1 99  ? 16.308  6.455   15.277  1.00 26.45  ? 99  VAL A CA  1 
ATOM   673  C C   . VAL A 1 99  ? 17.327  5.383   14.911  1.00 28.87  ? 99  VAL A C   1 
ATOM   674  O O   . VAL A 1 99  ? 17.379  4.317   15.532  1.00 30.65  ? 99  VAL A O   1 
ATOM   675  C CB  . VAL A 1 99  ? 15.020  6.331   14.436  1.00 26.66  ? 99  VAL A CB  1 
ATOM   676  C CG1 . VAL A 1 99  ? 14.513  4.890   14.472  1.00 29.71  ? 99  VAL A CG1 1 
ATOM   677  C CG2 . VAL A 1 99  ? 13.970  7.258   14.993  1.00 26.64  ? 99  VAL A CG2 1 
ATOM   678  N N   . GLU A 1 100 ? 18.161  5.656   13.902  1.00 28.81  ? 100 GLU A N   1 
ATOM   679  C CA  . GLU A 1 100 ? 19.183  4.690   13.516  1.00 28.10  ? 100 GLU A CA  1 
ATOM   680  C C   . GLU A 1 100 ? 20.138  4.386   14.673  1.00 28.52  ? 100 GLU A C   1 
ATOM   681  O O   . GLU A 1 100 ? 20.514  3.225   14.883  1.00 28.35  ? 100 GLU A O   1 
ATOM   682  C CB  . GLU A 1 100 ? 19.935  5.192   12.280  1.00 27.61  ? 100 GLU A CB  1 
ATOM   683  C CG  . GLU A 1 100 ? 21.098  4.297   11.874  1.00 29.75  ? 100 GLU A CG  1 
ATOM   684  C CD  . GLU A 1 100 ? 20.701  2.952   11.288  1.00 34.33  ? 100 GLU A CD  1 
ATOM   685  O OE1 . GLU A 1 100 ? 19.490  2.635   11.144  1.00 32.78  ? 100 GLU A OE1 1 
ATOM   686  O OE2 . GLU A 1 100 ? 21.635  2.167   11.022  1.00 35.13  ? 100 GLU A OE2 1 
ATOM   687  N N   . VAL A 1 101 ? 20.517  5.397   15.460  1.00 26.99  ? 101 VAL A N   1 
ATOM   688  C CA  . VAL A 1 101 ? 21.364  5.102   16.623  1.00 27.60  ? 101 VAL A CA  1 
ATOM   689  C C   . VAL A 1 101 ? 20.617  4.211   17.608  1.00 29.27  ? 101 VAL A C   1 
ATOM   690  O O   . VAL A 1 101 ? 21.195  3.290   18.205  1.00 29.35  ? 101 VAL A O   1 
ATOM   691  C CB  . VAL A 1 101 ? 21.853  6.392   17.306  1.00 27.05  ? 101 VAL A CB  1 
ATOM   692  C CG1 . VAL A 1 101 ? 22.700  6.028   18.546  1.00 27.84  ? 101 VAL A CG1 1 
ATOM   693  C CG2 . VAL A 1 101 ? 22.650  7.243   16.335  1.00 28.45  ? 101 VAL A CG2 1 
ATOM   694  N N   . MET A 1 102 ? 19.326  4.462   17.766  1.00 28.57  ? 102 MET A N   1 
ATOM   695  C CA  . MET A 1 102 ? 18.525  3.606   18.664  1.00 28.79  ? 102 MET A CA  1 
ATOM   696  C C   . MET A 1 102 ? 18.456  2.182   18.086  1.00 29.43  ? 102 MET A C   1 
ATOM   697  O O   . MET A 1 102 ? 18.472  1.235   18.864  1.00 30.13  ? 102 MET A O   1 
ATOM   698  C CB  . MET A 1 102 ? 17.130  4.195   18.862  1.00 28.08  ? 102 MET A CB  1 
ATOM   699  C CG  . MET A 1 102 ? 17.145  5.650   19.272  1.00 26.36  ? 102 MET A CG  1 
ATOM   700  S SD  . MET A 1 102 ? 17.894  5.900   20.899  1.00 38.15  ? 102 MET A SD  1 
ATOM   701  C CE  . MET A 1 102 ? 17.258  4.477   21.775  1.00 29.61  ? 102 MET A CE  1 
ATOM   702  N N   . TRP A 1 103 ? 18.417  2.060   16.761  1.00 29.64  ? 103 TRP A N   1 
ATOM   703  C CA  . TRP A 1 103 ? 18.360  0.739   16.141  1.00 32.51  ? 103 TRP A CA  1 
ATOM   704  C C   . TRP A 1 103 ? 19.680  -0.006  16.315  1.00 30.95  ? 103 TRP A C   1 
ATOM   705  O O   . TRP A 1 103 ? 19.695  -1.205  16.623  1.00 32.16  ? 103 TRP A O   1 
ATOM   706  C CB  . TRP A 1 103 ? 18.005  0.904   14.668  1.00 32.66  ? 103 TRP A CB  1 
ATOM   707  C CG  . TRP A 1 103 ? 17.303  -0.224  14.030  1.00 34.90  ? 103 TRP A CG  1 
ATOM   708  C CD1 . TRP A 1 103 ? 17.380  -1.553  14.338  1.00 37.50  ? 103 TRP A CD1 1 
ATOM   709  C CD2 . TRP A 1 103 ? 16.344  -0.107  12.980  1.00 35.19  ? 103 TRP A CD2 1 
ATOM   710  N NE1 . TRP A 1 103 ? 16.542  -2.276  13.509  1.00 36.30  ? 103 TRP A NE1 1 
ATOM   711  C CE2 . TRP A 1 103 ? 15.894  -1.405  12.672  1.00 37.84  ? 103 TRP A CE2 1 
ATOM   712  C CE3 . TRP A 1 103 ? 15.832  0.978   12.263  1.00 35.56  ? 103 TRP A CE3 1 
ATOM   713  C CZ2 . TRP A 1 103 ? 14.951  -1.648  11.672  1.00 38.36  ? 103 TRP A CZ2 1 
ATOM   714  C CZ3 . TRP A 1 103 ? 14.904  0.740   11.272  1.00 36.74  ? 103 TRP A CZ3 1 
ATOM   715  C CH2 . TRP A 1 103 ? 14.475  -0.568  10.981  1.00 36.35  ? 103 TRP A CH2 1 
ATOM   716  N N   . ILE A 1 104 ? 20.800  0.689   16.104  1.00 29.43  ? 104 ILE A N   1 
ATOM   717  C CA  . ILE A 1 104 ? 22.107  0.110   16.416  1.00 33.17  ? 104 ILE A CA  1 
ATOM   718  C C   . ILE A 1 104 ? 22.136  -0.355  17.864  1.00 32.48  ? 104 ILE A C   1 
ATOM   719  O O   . ILE A 1 104 ? 22.581  -1.466  18.171  1.00 32.88  ? 104 ILE A O   1 
ATOM   720  C CB  . ILE A 1 104 ? 23.228  1.126   16.137  1.00 31.94  ? 104 ILE A CB  1 
ATOM   721  C CG1 . ILE A 1 104 ? 23.337  1.409   14.645  1.00 29.48  ? 104 ILE A CG1 1 
ATOM   722  C CG2 . ILE A 1 104 ? 24.565  0.594   16.669  1.00 29.17  ? 104 ILE A CG2 1 
ATOM   723  C CD1 . ILE A 1 104 ? 24.300  2.564   14.322  1.00 31.01  ? 104 ILE A CD1 1 
ATOM   724  N N   . HIS A 1 105 ? 21.660  0.502   18.775  1.00 31.70  ? 105 HIS A N   1 
ATOM   725  C CA  . HIS A 1 105 ? 21.607  0.159   20.192  1.00 31.14  ? 105 HIS A CA  1 
ATOM   726  C C   . HIS A 1 105 ? 20.764  -1.084  20.442  1.00 32.31  ? 105 HIS A C   1 
ATOM   727  O O   . HIS A 1 105 ? 21.123  -1.942  21.261  1.00 33.03  ? 105 HIS A O   1 
ATOM   728  C CB  . HIS A 1 105 ? 21.044  1.343   20.968  1.00 31.31  ? 105 HIS A CB  1 
ATOM   729  C CG  . HIS A 1 105 ? 20.950  1.106   22.434  1.00 29.24  ? 105 HIS A CG  1 
ATOM   730  N ND1 . HIS A 1 105 ? 22.032  1.241   23.277  1.00 28.29  ? 105 HIS A ND1 1 
ATOM   731  C CD2 . HIS A 1 105 ? 19.898  0.765   23.214  1.00 29.50  ? 105 HIS A CD2 1 
ATOM   732  C CE1 . HIS A 1 105 ? 21.650  0.989   24.515  1.00 30.14  ? 105 HIS A CE1 1 
ATOM   733  N NE2 . HIS A 1 105 ? 20.364  0.698   24.506  1.00 28.77  ? 105 HIS A NE2 1 
ATOM   734  N N   . ASP A 1 106 ? 19.635  -1.197  19.742  1.00 30.02  ? 106 ASP A N   1 
ATOM   735  C CA  . ASP A 1 106 ? 18.788  -2.374  19.865  1.00 32.51  ? 106 ASP A CA  1 
ATOM   736  C C   . ASP A 1 106 ? 19.552  -3.623  19.440  1.00 34.94  ? 106 ASP A C   1 
ATOM   737  O O   . ASP A 1 106 ? 19.498  -4.655  20.120  1.00 37.60  ? 106 ASP A O   1 
ATOM   738  C CB  . ASP A 1 106 ? 17.531  -2.159  19.013  1.00 32.31  ? 106 ASP A CB  1 
ATOM   739  C CG  . ASP A 1 106 ? 16.458  -3.214  19.231  1.00 45.58  ? 106 ASP A CG  1 
ATOM   740  O OD1 . ASP A 1 106 ? 16.686  -4.221  19.941  1.00 44.68  ? 106 ASP A OD1 1 
ATOM   741  O OD2 . ASP A 1 106 ? 15.347  -2.996  18.697  1.00 46.66  ? 106 ASP A OD2 1 
ATOM   742  N N   . ASP A 1 107 ? 20.316  -3.532  18.346  1.00 31.90  ? 107 ASP A N   1 
ATOM   743  C CA  . ASP A 1 107 ? 21.077  -4.690  17.892  1.00 33.99  ? 107 ASP A CA  1 
ATOM   744  C C   . ASP A 1 107 ? 22.171  -5.038  18.888  1.00 36.51  ? 107 ASP A C   1 
ATOM   745  O O   . ASP A 1 107 ? 22.436  -6.218  19.141  1.00 36.89  ? 107 ASP A O   1 
ATOM   746  C CB  . ASP A 1 107 ? 21.703  -4.454  16.512  1.00 36.86  ? 107 ASP A CB  1 
ATOM   747  C CG  . ASP A 1 107 ? 20.673  -4.324  15.390  1.00 37.57  ? 107 ASP A CG  1 
ATOM   748  O OD1 . ASP A 1 107 ? 19.558  -4.872  15.510  1.00 40.41  ? 107 ASP A OD1 1 
ATOM   749  O OD2 . ASP A 1 107 ? 21.029  -3.756  14.335  1.00 39.80  ? 107 ASP A OD2 1 
ATOM   750  N N   . VAL A 1 108 ? 22.825  -4.024  19.455  1.00 31.14  ? 108 VAL A N   1 
ATOM   751  C CA  . VAL A 1 108 ? 23.888  -4.281  20.426  1.00 31.33  ? 108 VAL A CA  1 
ATOM   752  C C   . VAL A 1 108 ? 23.328  -4.968  21.661  1.00 35.88  ? 108 VAL A C   1 
ATOM   753  O O   . VAL A 1 108 ? 23.890  -5.961  22.151  1.00 37.39  ? 108 VAL A O   1 
ATOM   754  C CB  . VAL A 1 108 ? 24.600  -2.964  20.784  1.00 31.08  ? 108 VAL A CB  1 
ATOM   755  C CG1 . VAL A 1 108 ? 25.500  -3.142  22.019  1.00 31.49  ? 108 VAL A CG1 1 
ATOM   756  C CG2 . VAL A 1 108 ? 25.403  -2.457  19.587  1.00 33.56  ? 108 VAL A CG2 1 
ATOM   757  N N   . THR A 1 109 ? 22.207  -4.470  22.175  1.00 33.85  ? 109 THR A N   1 
ATOM   758  C CA  . THR A 1 109 ? 21.684  -4.977  23.436  1.00 34.34  ? 109 THR A CA  1 
ATOM   759  C C   . THR A 1 109 ? 20.877  -6.258  23.286  1.00 38.48  ? 109 THR A C   1 
ATOM   760  O O   . THR A 1 109 ? 20.677  -6.956  24.286  1.00 34.34  ? 109 THR A O   1 
ATOM   761  C CB  . THR A 1 109 ? 20.850  -3.898  24.130  1.00 32.60  ? 109 THR A CB  1 
ATOM   762  O OG1 . THR A 1 109 ? 19.732  -3.522  23.305  1.00 34.64  ? 109 THR A OG1 1 
ATOM   763  C CG2 . THR A 1 109 ? 21.721  -2.703  24.437  1.00 31.31  ? 109 THR A CG2 1 
ATOM   764  N N   . GLU A 1 110 ? 20.405  -6.579  22.075  1.00 36.83  ? 110 GLU A N   1 
ATOM   765  C CA  . GLU A 1 110 ? 19.725  -7.850  21.856  1.00 37.80  ? 110 GLU A CA  1 
ATOM   766  C C   . GLU A 1 110 ? 20.627  -9.023  22.194  1.00 39.18  ? 110 GLU A C   1 
ATOM   767  O O   . GLU A 1 110 ? 20.159  -10.052 22.693  1.00 43.32  ? 110 GLU A O   1 
ATOM   768  C CB  . GLU A 1 110 ? 19.271  -7.974  20.406  1.00 39.22  ? 110 GLU A CB  1 
ATOM   769  C CG  . GLU A 1 110 ? 17.861  -8.460  20.255  1.00 52.69  ? 110 GLU A CG  1 
ATOM   770  C CD  . GLU A 1 110 ? 17.216  -7.904  19.012  1.00 55.52  ? 110 GLU A CD  1 
ATOM   771  O OE1 . GLU A 1 110 ? 17.705  -8.258  17.914  1.00 55.72  ? 110 GLU A OE1 1 
ATOM   772  O OE2 . GLU A 1 110 ? 16.251  -7.111  19.128  1.00 57.07  ? 110 GLU A OE2 1 
ATOM   773  N N   . GLU A 1 111 ? 21.922  -8.881  21.936  1.00 43.73  ? 111 GLU A N   1 
ATOM   774  C CA  . GLU A 1 111 ? 22.892  -9.988  22.138  1.00 46.15  ? 111 GLU A CA  1 
ATOM   775  C C   . GLU A 1 111 ? 23.389  -10.043 23.579  1.00 45.66  ? 111 GLU A C   1 
ATOM   776  O O   . GLU A 1 111 ? 24.286  -10.846 23.849  1.00 48.07  ? 111 GLU A O   1 
ATOM   777  C CB  . GLU A 1 111 ? 24.085  -9.756  21.214  1.00 49.26  ? 111 GLU A CB  1 
ATOM   778  C CG  . GLU A 1 111 ? 23.683  -9.451  19.785  1.00 59.84  ? 111 GLU A CG  1 
ATOM   779  C CD  . GLU A 1 111 ? 23.766  -10.634 18.837  1.00 62.52  ? 111 GLU A CD  1 
ATOM   780  O OE1 . GLU A 1 111 ? 24.322  -11.672 19.238  1.00 62.52  ? 111 GLU A OE1 1 
ATOM   781  O OE2 . GLU A 1 111 ? 23.272  -10.512 17.703  1.00 67.03  ? 111 GLU A OE2 1 
ATOM   782  N N   . MET A 1 112 ? 22.818  -9.242  24.462  1.00 39.05  ? 112 MET A N   1 
ATOM   783  C CA  . MET A 1 112 ? 23.262  -9.150  25.843  1.00 39.38  ? 112 MET A CA  1 
ATOM   784  C C   . MET A 1 112 ? 22.312  -9.897  26.765  1.00 38.46  ? 112 MET A C   1 
ATOM   785  O O   . MET A 1 112 ? 21.137  -10.100 26.447  1.00 38.75  ? 112 MET A O   1 
ATOM   786  C CB  . MET A 1 112 ? 23.331  -7.679  26.249  1.00 35.89  ? 112 MET A CB  1 
ATOM   787  C CG  . MET A 1 112 ? 24.431  -6.926  25.551  1.00 37.20  ? 112 MET A CG  1 
ATOM   788  S SD  . MET A 1 112 ? 24.659  -5.295  26.242  1.00 36.58  ? 112 MET A SD  1 
ATOM   789  C CE  . MET A 1 112 ? 26.049  -4.743  25.261  1.00 38.97  ? 112 MET A CE  1 
ATOM   790  N N   . ASP A 1 113 ? 22.831  -10.318 27.914  1.00 37.24  ? 113 ASP A N   1 
ATOM   791  C CA  . ASP A 1 113 ? 21.950  -10.783 28.970  1.00 37.86  ? 113 ASP A CA  1 
ATOM   792  C C   . ASP A 1 113 ? 21.074  -9.625  29.429  1.00 36.35  ? 113 ASP A C   1 
ATOM   793  O O   . ASP A 1 113 ? 21.377  -8.456  29.184  1.00 36.79  ? 113 ASP A O   1 
ATOM   794  C CB  . ASP A 1 113 ? 22.760  -11.323 30.149  1.00 42.85  ? 113 ASP A CB  1 
ATOM   795  C CG  . ASP A 1 113 ? 23.779  -10.322 30.647  1.00 41.63  ? 113 ASP A CG  1 
ATOM   796  O OD1 . ASP A 1 113 ? 24.875  -10.225 30.049  1.00 47.27  ? 113 ASP A OD1 1 
ATOM   797  O OD2 . ASP A 1 113 ? 23.461  -9.598  31.610  1.00 41.76  ? 113 ASP A OD2 1 
ATOM   798  N N   . HIS A 1 114 ? 19.974  -9.953  30.110  1.00 35.45  ? 114 HIS A N   1 
ATOM   799  C CA  . HIS A 1 114 ? 19.013  -8.906  30.435  1.00 35.78  ? 114 HIS A CA  1 
ATOM   800  C C   . HIS A 1 114 ? 19.600  -7.874  31.402  1.00 36.61  ? 114 HIS A C   1 
ATOM   801  O O   . HIS A 1 114 ? 19.318  -6.676  31.278  1.00 33.50  ? 114 HIS A O   1 
ATOM   802  C CB  . HIS A 1 114 ? 17.728  -9.539  30.973  1.00 35.31  ? 114 HIS A CB  1 
ATOM   803  C CG  . HIS A 1 114 ? 16.596  -8.570  31.129  1.00 39.51  ? 114 HIS A CG  1 
ATOM   804  N ND1 . HIS A 1 114 ? 15.622  -8.702  32.094  1.00 42.34  ? 114 HIS A ND1 1 
ATOM   805  C CD2 . HIS A 1 114 ? 16.299  -7.437  30.448  1.00 43.95  ? 114 HIS A CD2 1 
ATOM   806  C CE1 . HIS A 1 114 ? 14.769  -7.697  31.997  1.00 42.71  ? 114 HIS A CE1 1 
ATOM   807  N NE2 . HIS A 1 114 ? 15.156  -6.915  31.006  1.00 46.07  ? 114 HIS A NE2 1 
ATOM   808  N N   . ILE A 1 115 ? 20.451  -8.298  32.339  1.00 32.99  ? 115 ILE A N   1 
ATOM   809  C CA  . ILE A 1 115 ? 21.053  -7.332  33.253  1.00 31.13  ? 115 ILE A CA  1 
ATOM   810  C C   . ILE A 1 115 ? 21.919  -6.339  32.491  1.00 32.78  ? 115 ILE A C   1 
ATOM   811  O O   . ILE A 1 115 ? 21.816  -5.120  32.682  1.00 36.12  ? 115 ILE A O   1 
ATOM   812  C CB  . ILE A 1 115 ? 21.869  -8.057  34.338  1.00 36.18  ? 115 ILE A CB  1 
ATOM   813  C CG1 . ILE A 1 115 ? 20.931  -8.712  35.345  1.00 34.55  ? 115 ILE A CG1 1 
ATOM   814  C CG2 . ILE A 1 115 ? 22.785  -7.067  35.048  1.00 38.90  ? 115 ILE A CG2 1 
ATOM   815  C CD1 . ILE A 1 115 ? 21.628  -9.809  36.186  1.00 36.32  ? 115 ILE A CD1 1 
ATOM   816  N N   . SER A 1 116 ? 22.795  -6.845  31.621  1.00 34.72  ? 116 SER A N   1 
ATOM   817  C CA  . SER A 1 116 ? 23.694  -5.951  30.901  1.00 33.53  ? 116 SER A CA  1 
ATOM   818  C C   . SER A 1 116 ? 22.932  -5.065  29.922  1.00 35.48  ? 116 SER A C   1 
ATOM   819  O O   . SER A 1 116 ? 23.271  -3.887  29.752  1.00 32.98  ? 116 SER A O   1 
ATOM   820  C CB  . SER A 1 116 ? 24.767  -6.751  30.171  1.00 37.29  ? 116 SER A CB  1 
ATOM   821  O OG  . SER A 1 116 ? 25.500  -7.554  31.091  1.00 39.85  ? 116 SER A OG  1 
ATOM   822  N N   . ALA A 1 117 ? 21.906  -5.610  29.269  1.00 33.50  ? 117 ALA A N   1 
ATOM   823  C CA  . ALA A 1 117 ? 21.112  -4.779  28.361  1.00 29.23  ? 117 ALA A CA  1 
ATOM   824  C C   . ALA A 1 117 ? 20.476  -3.611  29.110  1.00 31.93  ? 117 ALA A C   1 
ATOM   825  O O   . ALA A 1 117 ? 20.565  -2.455  28.680  1.00 32.52  ? 117 ALA A O   1 
ATOM   826  C CB  . ALA A 1 117 ? 20.051  -5.635  27.659  1.00 32.21  ? 117 ALA A CB  1 
ATOM   827  N N   . CYS A 1 118 ? 19.870  -3.893  30.263  1.00 34.64  ? 118 CYS A N   1 
ATOM   828  C CA  . CYS A 1 118 ? 19.213  -2.850  31.044  1.00 33.65  ? 118 CYS A CA  1 
ATOM   829  C C   . CYS A 1 118 ? 20.203  -1.768  31.468  1.00 37.45  ? 118 CYS A C   1 
ATOM   830  O O   . CYS A 1 118 ? 19.883  -0.571  31.445  1.00 34.46  ? 118 CYS A O   1 
ATOM   831  C CB  . CYS A 1 118 ? 18.561  -3.484  32.271  1.00 39.45  ? 118 CYS A CB  1 
ATOM   832  S SG  . CYS A 1 118 ? 16.971  -4.240  31.935  1.00 49.78  ? 118 CYS A SG  1 
ATOM   833  N N   . ARG A 1 119 ? 21.420  -2.176  31.813  1.00 35.33  ? 119 ARG A N   1 
ATOM   834  C CA  . ARG A 1 119 ? 22.458  -1.191  32.196  1.00 37.33  ? 119 ARG A CA  1 
ATOM   835  C C   . ARG A 1 119 ? 22.817  -0.334  30.983  1.00 36.48  ? 119 ARG A C   1 
ATOM   836  O O   . ARG A 1 119 ? 23.031  0.867   31.143  1.00 33.61  ? 119 ARG A O   1 
ATOM   837  C CB  . ARG A 1 119 ? 23.693  -1.910  32.737  1.00 43.15  ? 119 ARG A CB  1 
ATOM   838  C CG  . ARG A 1 119 ? 24.975  -1.093  32.682  1.00 45.53  ? 119 ARG A CG  1 
ATOM   839  C CD  . ARG A 1 119 ? 25.963  -1.499  33.759  1.00 50.21  ? 119 ARG A CD  1 
ATOM   840  N NE  . ARG A 1 119 ? 26.109  -2.944  33.869  1.00 52.04  ? 119 ARG A NE  1 
ATOM   841  C CZ  . ARG A 1 119 ? 25.552  -3.688  34.818  1.00 51.74  ? 119 ARG A CZ  1 
ATOM   842  N NH1 . ARG A 1 119 ? 24.801  -3.128  35.750  1.00 50.77  ? 119 ARG A NH1 1 
ATOM   843  N NH2 . ARG A 1 119 ? 25.744  -4.991  34.830  1.00 51.11  ? 119 ARG A NH2 1 
ATOM   844  N N   . GLU A 1 120 ? 22.881  -0.962  29.815  1.00 37.03  ? 120 GLU A N   1 
ATOM   845  C CA  . GLU A 1 120 ? 23.225  -0.200  28.615  1.00 36.22  ? 120 GLU A CA  1 
ATOM   846  C C   . GLU A 1 120 ? 22.129  0.793   28.251  1.00 33.04  ? 120 GLU A C   1 
ATOM   847  O O   . GLU A 1 120 ? 22.428  1.893   27.766  1.00 33.43  ? 120 GLU A O   1 
ATOM   848  C CB  . GLU A 1 120 ? 23.500  -1.132  27.434  1.00 35.97  ? 120 GLU A CB  1 
ATOM   849  C CG  . GLU A 1 120 ? 24.799  -1.936  27.548  1.00 42.85  ? 120 GLU A CG  1 
ATOM   850  C CD  . GLU A 1 120 ? 26.061  -1.080  27.619  1.00 47.54  ? 120 GLU A CD  1 
ATOM   851  O OE1 . GLU A 1 120 ? 27.046  -1.550  28.229  1.00 51.14  ? 120 GLU A OE1 1 
ATOM   852  O OE2 . GLU A 1 120 ? 26.080  0.050   27.075  1.00 49.81  ? 120 GLU A OE2 1 
ATOM   853  N N   . HIS A 1 121 ? 20.858  0.436   28.482  1.00 33.11  ? 121 HIS A N   1 
ATOM   854  C CA  . HIS A 1 121 ? 19.780  1.394   28.224  1.00 31.01  ? 121 HIS A CA  1 
ATOM   855  C C   . HIS A 1 121 ? 19.898  2.587   29.152  1.00 33.58  ? 121 HIS A C   1 
ATOM   856  O O   . HIS A 1 121 ? 19.709  3.732   28.731  1.00 32.08  ? 121 HIS A O   1 
ATOM   857  C CB  . HIS A 1 121 ? 18.394  0.764   28.403  1.00 31.61  ? 121 HIS A CB  1 
ATOM   858  C CG  . HIS A 1 121 ? 18.170  -0.462  27.578  1.00 29.79  ? 121 HIS A CG  1 
ATOM   859  N ND1 . HIS A 1 121 ? 18.739  -0.635  26.337  1.00 33.57  ? 121 HIS A ND1 1 
ATOM   860  C CD2 . HIS A 1 121 ? 17.419  -1.566  27.805  1.00 31.70  ? 121 HIS A CD2 1 
ATOM   861  C CE1 . HIS A 1 121 ? 18.376  -1.808  25.848  1.00 33.27  ? 121 HIS A CE1 1 
ATOM   862  N NE2 . HIS A 1 121 ? 17.568  -2.389  26.718  1.00 31.77  ? 121 HIS A NE2 1 
ATOM   863  N N   . ASP A 1 122 ? 20.206  2.336   30.424  1.00 33.93  ? 122 ASP A N   1 
ATOM   864  C CA  . ASP A 1 122 ? 20.358  3.435   31.372  1.00 35.06  ? 122 ASP A CA  1 
ATOM   865  C C   . ASP A 1 122 ? 21.557  4.302   31.030  1.00 32.47  ? 122 ASP A C   1 
ATOM   866  O O   . ASP A 1 122 ? 21.502  5.522   31.205  1.00 32.58  ? 122 ASP A O   1 
ATOM   867  C CB  . ASP A 1 122 ? 20.471  2.866   32.785  1.00 38.64  ? 122 ASP A CB  1 
ATOM   868  C CG  . ASP A 1 122 ? 19.140  2.366   33.303  1.00 44.18  ? 122 ASP A CG  1 
ATOM   869  O OD1 . ASP A 1 122 ? 18.145  2.489   32.561  1.00 47.33  ? 122 ASP A OD1 1 
ATOM   870  O OD2 . ASP A 1 122 ? 19.070  1.910   34.461  1.00 47.07  ? 122 ASP A OD2 1 
ATOM   871  N N   . GLU A 1 123 ? 22.625  3.703   30.518  1.00 31.84  ? 123 GLU A N   1 
ATOM   872  C CA  . GLU A 1 123 ? 23.818  4.486   30.134  1.00 33.61  ? 123 GLU A CA  1 
ATOM   873  C C   . GLU A 1 123 ? 23.480  5.378   28.937  1.00 31.07  ? 123 GLU A C   1 
ATOM   874  O O   . GLU A 1 123 ? 23.850  6.551   28.955  1.00 32.61  ? 123 GLU A O   1 
ATOM   875  C CB  . GLU A 1 123 ? 24.996  3.584   29.784  1.00 36.97  ? 123 GLU A CB  1 
ATOM   876  C CG  . GLU A 1 123 ? 25.834  3.192   30.981  1.00 41.09  ? 123 GLU A CG  1 
ATOM   877  C CD  . GLU A 1 123 ? 26.396  4.379   31.739  1.00 43.54  ? 123 GLU A CD  1 
ATOM   878  O OE1 . GLU A 1 123 ? 27.228  5.100   31.170  1.00 47.32  ? 123 GLU A OE1 1 
ATOM   879  O OE2 . GLU A 1 123 ? 25.989  4.581   32.888  1.00 49.95  ? 123 GLU A OE2 1 
ATOM   880  N N   . LEU A 1 124 ? 22.820  4.814   27.929  1.00 30.12  ? 124 LEU A N   1 
ATOM   881  C CA  . LEU A 1 124 ? 22.460  5.647   26.783  1.00 28.02  ? 124 LEU A CA  1 
ATOM   882  C C   . LEU A 1 124 ? 21.510  6.771   27.182  1.00 29.03  ? 124 LEU A C   1 
ATOM   883  O O   . LEU A 1 124 ? 21.589  7.882   26.644  1.00 30.46  ? 124 LEU A O   1 
ATOM   884  C CB  . LEU A 1 124 ? 21.839  4.789   25.681  1.00 28.40  ? 124 LEU A CB  1 
ATOM   885  C CG  . LEU A 1 124 ? 21.564  5.521   24.370  1.00 32.16  ? 124 LEU A CG  1 
ATOM   886  C CD1 . LEU A 1 124 ? 22.854  6.037   23.758  1.00 29.58  ? 124 LEU A CD1 1 
ATOM   887  C CD2 . LEU A 1 124 ? 20.852  4.548   23.416  1.00 29.34  ? 124 LEU A CD2 1 
ATOM   888  N N   . ALA A 1 125 ? 20.584  6.502   28.099  1.00 28.24  ? 125 ALA A N   1 
ATOM   889  C CA  . ALA A 1 125 ? 19.616  7.517   28.482  1.00 28.86  ? 125 ALA A CA  1 
ATOM   890  C C   . ALA A 1 125 ? 20.246  8.725   29.171  1.00 32.77  ? 125 ALA A C   1 
ATOM   891  O O   . ALA A 1 125 ? 19.580  9.762   29.283  1.00 32.45  ? 125 ALA A O   1 
ATOM   892  C CB  . ALA A 1 125 ? 18.546  6.909   29.387  1.00 32.65  ? 125 ALA A CB  1 
ATOM   893  N N   . LYS A 1 126 ? 21.488  8.632   29.618  1.00 30.48  ? 126 LYS A N   1 
ATOM   894  C CA  . LYS A 1 126 ? 22.146  9.814   30.232  1.00 34.07  ? 126 LYS A CA  1 
ATOM   895  C C   . LYS A 1 126 ? 22.251  10.956  29.211  1.00 35.98  ? 126 LYS A C   1 
ATOM   896  O O   . LYS A 1 126 ? 22.303  12.112  29.636  1.00 35.21  ? 126 LYS A O   1 
ATOM   897  C CB  . LYS A 1 126 ? 23.510  9.396   30.781  1.00 37.68  ? 126 LYS A CB  1 
ATOM   898  C CG  . LYS A 1 126 ? 23.472  8.332   31.865  1.00 37.96  ? 126 LYS A CG  1 
ATOM   899  C CD  . LYS A 1 126 ? 24.840  7.780   32.178  1.00 44.07  ? 126 LYS A CD  1 
ATOM   900  C CE  . LYS A 1 126 ? 25.063  7.543   33.655  1.00 51.18  ? 126 LYS A CE  1 
ATOM   901  N NZ  . LYS A 1 126 ? 26.494  7.300   33.952  1.00 52.91  ? 126 LYS A NZ  1 
ATOM   902  N N   . VAL A 1 127 ? 22.248  10.636  27.924  1.00 34.29  ? 127 VAL A N   1 
ATOM   903  C CA  . VAL A 1 127 ? 22.394  11.619  26.855  1.00 31.33  ? 127 VAL A CA  1 
ATOM   904  C C   . VAL A 1 127 ? 21.094  12.379  26.607  1.00 31.67  ? 127 VAL A C   1 
ATOM   905  O O   . VAL A 1 127 ? 21.110  13.463  26.008  1.00 31.87  ? 127 VAL A O   1 
ATOM   906  C CB  . VAL A 1 127 ? 22.912  10.840  25.629  1.00 39.16  ? 127 VAL A CB  1 
ATOM   907  C CG1 . VAL A 1 127 ? 22.506  11.447  24.302  1.00 39.55  ? 127 VAL A CG1 1 
ATOM   908  C CG2 . VAL A 1 127 ? 24.431  10.674  25.712  1.00 38.65  ? 127 VAL A CG2 1 
ATOM   909  N N   . LEU A 1 128 ? 19.971  11.858  27.093  1.00 30.49  ? 128 LEU A N   1 
ATOM   910  C CA  . LEU A 1 128 ? 18.650  12.389  26.778  1.00 33.36  ? 128 LEU A CA  1 
ATOM   911  C C   . LEU A 1 128 ? 18.345  13.549  27.714  1.00 33.53  ? 128 LEU A C   1 
ATOM   912  O O   . LEU A 1 128 ? 17.564  13.439  28.660  1.00 33.65  ? 128 LEU A O   1 
ATOM   913  C CB  . LEU A 1 128 ? 17.598  11.289  26.872  1.00 30.75  ? 128 LEU A CB  1 
ATOM   914  C CG  . LEU A 1 128 ? 17.795  10.095  25.945  1.00 31.26  ? 128 LEU A CG  1 
ATOM   915  C CD1 . LEU A 1 128 ? 16.704  9.057   26.205  1.00 29.59  ? 128 LEU A CD1 1 
ATOM   916  C CD2 . LEU A 1 128 ? 17.727  10.575  24.491  1.00 30.11  ? 128 LEU A CD2 1 
ATOM   917  N N   . GLN A 1 129 ? 18.973  14.688  27.421  1.00 31.69  ? 129 GLN A N   1 
ATOM   918  C CA  . GLN A 1 129 ? 18.802  15.902  28.209  1.00 33.97  ? 129 GLN A CA  1 
ATOM   919  C C   . GLN A 1 129 ? 18.495  17.080  27.303  1.00 31.20  ? 129 GLN A C   1 
ATOM   920  O O   . GLN A 1 129 ? 19.131  17.250  26.259  1.00 33.36  ? 129 GLN A O   1 
ATOM   921  C CB  . GLN A 1 129 ? 20.039  16.226  29.049  1.00 36.07  ? 129 GLN A CB  1 
ATOM   922  C CG  . GLN A 1 129 ? 20.657  15.007  29.696  1.00 33.70  ? 129 GLN A CG  1 
ATOM   923  C CD  . GLN A 1 129 ? 19.859  14.587  30.910  1.00 41.23  ? 129 GLN A CD  1 
ATOM   924  O OE1 . GLN A 1 129 ? 19.075  15.369  31.447  1.00 39.11  ? 129 GLN A OE1 1 
ATOM   925  N NE2 . GLN A 1 129 ? 20.022  13.333  31.325  1.00 42.94  ? 129 GLN A NE2 1 
ATOM   926  N N   . LEU A 1 130 ? 17.542  17.907  27.738  1.00 32.66  ? 130 LEU A N   1 
ATOM   927  C CA  . LEU A 1 130 ? 17.188  19.113  26.986  1.00 34.00  ? 130 LEU A CA  1 
ATOM   928  C C   . LEU A 1 130 ? 18.382  20.041  26.779  1.00 39.11  ? 130 LEU A C   1 
ATOM   929  O O   . LEU A 1 130 ? 18.470  20.715  25.743  1.00 38.09  ? 130 LEU A O   1 
ATOM   930  C CB  . LEU A 1 130 ? 16.063  19.862  27.702  1.00 38.80  ? 130 LEU A CB  1 
ATOM   931  C CG  . LEU A 1 130 ? 15.267  20.893  26.900  1.00 38.60  ? 130 LEU A CG  1 
ATOM   932  C CD1 . LEU A 1 130 ? 14.670  20.292  25.626  1.00 38.07  ? 130 LEU A CD1 1 
ATOM   933  C CD2 . LEU A 1 130 ? 14.169  21.499  27.772  1.00 42.84  ? 130 LEU A CD2 1 
ATOM   934  N N   . ASP A 1 131 ? 19.297  20.101  27.749  1.00 35.52  ? 131 ASP A N   1 
ATOM   935  C CA  . ASP A 1 131 ? 20.498  20.924  27.654  1.00 41.81  ? 131 ASP A CA  1 
ATOM   936  C C   . ASP A 1 131 ? 21.722  20.129  27.206  1.00 38.95  ? 131 ASP A C   1 
ATOM   937  O O   . ASP A 1 131 ? 22.844  20.458  27.609  1.00 36.81  ? 131 ASP A O   1 
ATOM   938  C CB  . ASP A 1 131 ? 20.810  21.586  28.996  1.00 42.84  ? 131 ASP A CB  1 
ATOM   939  C CG  . ASP A 1 131 ? 20.635  20.638  30.172  1.00 48.83  ? 131 ASP A CG  1 
ATOM   940  O OD1 . ASP A 1 131 ? 21.027  19.457  30.047  1.00 42.91  ? 131 ASP A OD1 1 
ATOM   941  O OD2 . ASP A 1 131 ? 20.236  21.102  31.268  1.00 51.80  ? 131 ASP A OD2 1 
ATOM   942  N N   . ILE A 1 132 ? 21.517  19.094  26.401  1.00 36.32  ? 132 ILE A N   1 
ATOM   943  C CA  . ILE A 1 132 ? 22.649  18.199  26.028  1.00 34.15  ? 132 ILE A CA  1 
ATOM   944  C C   . ILE A 1 132 ? 23.814  18.974  25.425  1.00 33.65  ? 132 ILE A C   1 
ATOM   945  O O   . ILE A 1 132 ? 23.588  19.770  24.511  1.00 35.25  ? 132 ILE A O   1 
ATOM   946  C CB  . ILE A 1 132 ? 22.197  17.073  25.073  1.00 33.54  ? 132 ILE A CB  1 
ATOM   947  C CG1 . ILE A 1 132 ? 23.356  16.150  24.689  1.00 32.73  ? 132 ILE A CG1 1 
ATOM   948  C CG2 . ILE A 1 132 ? 21.507  17.641  23.843  1.00 34.20  ? 132 ILE A CG2 1 
ATOM   949  C CD1 . ILE A 1 132 ? 23.898  15.339  25.837  1.00 34.04  ? 132 ILE A CD1 1 
ATOM   950  N N   . ASP A 1 133 ? 25.011  18.736  25.943  1.00 34.25  ? 133 ASP A N   1 
ATOM   951  C CA  . ASP A 1 133 ? 26.235  19.298  25.339  1.00 38.77  ? 133 ASP A CA  1 
ATOM   952  C C   . ASP A 1 133 ? 26.998  18.079  24.837  1.00 41.10  ? 133 ASP A C   1 
ATOM   953  O O   . ASP A 1 133 ? 27.577  17.363  25.656  1.00 42.03  ? 133 ASP A O   1 
ATOM   954  C CB  . ASP A 1 133 ? 27.052  20.129  26.326  1.00 40.87  ? 133 ASP A CB  1 
ATOM   955  C CG  . ASP A 1 133 ? 28.331  20.698  25.737  1.00 48.71  ? 133 ASP A CG  1 
ATOM   956  O OD1 . ASP A 1 133 ? 28.687  20.312  24.611  1.00 45.95  ? 133 ASP A OD1 1 
ATOM   957  O OD2 . ASP A 1 133 ? 28.961  21.529  26.413  1.00 49.41  ? 133 ASP A OD2 1 
ATOM   958  N N   . PRO A 1 134 ? 26.965  17.789  23.529  1.00 40.85  ? 134 PRO A N   1 
ATOM   959  C CA  . PRO A 1 134 ? 27.593  16.576  23.015  1.00 41.89  ? 134 PRO A CA  1 
ATOM   960  C C   . PRO A 1 134 ? 29.075  16.464  23.409  1.00 47.61  ? 134 PRO A C   1 
ATOM   961  O O   . PRO A 1 134 ? 29.549  15.371  23.593  1.00 43.49  ? 134 PRO A O   1 
ATOM   962  C CB  . PRO A 1 134 ? 27.388  16.756  21.507  1.00 38.07  ? 134 PRO A CB  1 
ATOM   963  C CG  . PRO A 1 134 ? 26.140  17.583  21.392  1.00 40.47  ? 134 PRO A CG  1 
ATOM   964  C CD  . PRO A 1 134 ? 26.289  18.585  22.510  1.00 39.07  ? 134 PRO A CD  1 
ATOM   965  N N   . SER A 1 135 ? 29.749  17.605  23.545  1.00 47.14  ? 135 SER A N   1 
ATOM   966  C CA  . SER A 1 135 ? 31.164  17.586  23.898  1.00 51.66  ? 135 SER A CA  1 
ATOM   967  C C   . SER A 1 135 ? 31.409  16.928  25.251  1.00 51.73  ? 135 SER A C   1 
ATOM   968  O O   . SER A 1 135 ? 32.497  16.395  25.491  1.00 57.02  ? 135 SER A O   1 
ATOM   969  C CB  . SER A 1 135 ? 31.711  19.013  23.877  1.00 48.19  ? 135 SER A CB  1 
ATOM   970  O OG  . SER A 1 135 ? 31.359  19.705  25.061  1.00 48.33  ? 135 SER A OG  1 
ATOM   971  N N   . LYS A 1 136 ? 30.417  16.935  26.137  1.00 50.13  ? 136 LYS A N   1 
ATOM   972  C CA  . LYS A 1 136 ? 30.560  16.279  27.435  1.00 52.49  ? 136 LYS A CA  1 
ATOM   973  C C   . LYS A 1 136 ? 30.457  14.768  27.352  1.00 51.97  ? 136 LYS A C   1 
ATOM   974  O O   . LYS A 1 136 ? 30.444  14.114  28.407  1.00 54.08  ? 136 LYS A O   1 
ATOM   975  C CB  . LYS A 1 136 ? 29.515  16.814  28.417  1.00 51.11  ? 136 LYS A CB  1 
ATOM   976  C CG  . LYS A 1 136 ? 29.994  17.977  29.273  1.00 56.47  ? 136 LYS A CG  1 
ATOM   977  C CD  . LYS A 1 136 ? 29.302  19.275  28.891  1.00 51.53  ? 136 LYS A CD  1 
ATOM   978  C CE  . LYS A 1 136 ? 29.244  20.267  30.051  1.00 55.07  ? 136 LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 136 ? 28.495  21.518  29.679  1.00 53.62  ? 136 LYS A NZ  1 
ATOM   980  N N   . PHE A 1 137 ? 30.375  14.151  26.172  1.00 49.94  ? 137 PHE A N   1 
ATOM   981  C CA  . PHE A 1 137 ? 30.280  12.698  26.091  1.00 53.92  ? 137 PHE A CA  1 
ATOM   982  C C   . PHE A 1 137 ? 31.375  12.098  25.220  1.00 61.15  ? 137 PHE A C   1 
ATOM   983  O O   . PHE A 1 137 ? 31.238  10.959  24.772  1.00 64.41  ? 137 PHE A O   1 
ATOM   984  C CB  . PHE A 1 137 ? 28.899  12.268  25.587  1.00 49.22  ? 137 PHE A CB  1 
ATOM   985  C CG  . PHE A 1 137 ? 27.846  12.267  26.660  1.00 45.65  ? 137 PHE A CG  1 
ATOM   986  C CD1 . PHE A 1 137 ? 27.122  13.416  26.937  1.00 45.62  ? 137 PHE A CD1 1 
ATOM   987  C CD2 . PHE A 1 137 ? 27.601  11.125  27.406  1.00 42.94  ? 137 PHE A CD2 1 
ATOM   988  C CE1 . PHE A 1 137 ? 26.167  13.421  27.931  1.00 46.70  ? 137 PHE A CE1 1 
ATOM   989  C CE2 . PHE A 1 137 ? 26.649  11.123  28.399  1.00 39.85  ? 137 PHE A CE2 1 
ATOM   990  C CZ  . PHE A 1 137 ? 25.931  12.268  28.666  1.00 44.81  ? 137 PHE A CZ  1 
ATOM   991  N N   . GLU A 1 138 ? 32.471  12.830  24.991  1.00 63.97  ? 138 GLU A N   1 
ATOM   992  C CA  . GLU A 1 138 ? 33.572  12.302  24.189  1.00 68.74  ? 138 GLU A CA  1 
ATOM   993  C C   . GLU A 1 138 ? 34.261  11.113  24.846  1.00 69.25  ? 138 GLU A C   1 
ATOM   994  O O   . GLU A 1 138 ? 34.934  10.345  24.154  1.00 71.81  ? 138 GLU A O   1 
ATOM   995  C CB  . GLU A 1 138 ? 34.593  13.404  23.910  1.00 63.78  ? 138 GLU A CB  1 
ATOM   996  C CG  . GLU A 1 138 ? 34.389  14.106  22.584  1.00 67.54  ? 138 GLU A CG  1 
ATOM   997  C CD  . GLU A 1 138 ? 34.750  15.574  22.658  1.00 69.10  ? 138 GLU A CD  1 
ATOM   998  O OE1 . GLU A 1 138 ? 34.392  16.325  21.726  1.00 67.98  ? 138 GLU A OE1 1 
ATOM   999  O OE2 . GLU A 1 138 ? 35.377  15.979  23.661  1.00 68.46  ? 138 GLU A OE2 1 
ATOM   1000 N N   . SER A 1 139 ? 34.116  10.947  26.157  1.00 71.19  ? 139 SER A N   1 
ATOM   1001 C CA  . SER A 1 139 ? 34.637  9.781   26.856  1.00 76.29  ? 139 SER A CA  1 
ATOM   1002 C C   . SER A 1 139 ? 33.668  8.606   26.848  1.00 80.60  ? 139 SER A C   1 
ATOM   1003 O O   . SER A 1 139 ? 33.963  7.573   27.457  1.00 76.44  ? 139 SER A O   1 
ATOM   1004 C CB  . SER A 1 139 ? 34.975  10.145  28.303  1.00 74.01  ? 139 SER A CB  1 
ATOM   1005 O OG  . SER A 1 139 ? 33.843  10.694  28.956  1.00 74.28  ? 139 SER A OG  1 
ATOM   1006 N N   . GLY A 1 140 ? 32.519  8.737   26.184  1.00 103.61 ? 140 GLY A N   1 
ATOM   1007 C CA  . GLY A 1 140 ? 31.489  7.726   26.222  1.00 72.69  ? 140 GLY A CA  1 
ATOM   1008 C C   . GLY A 1 140 ? 31.574  6.751   25.058  1.00 77.58  ? 140 GLY A C   1 
ATOM   1009 O O   . GLY A 1 140 ? 32.412  6.861   24.166  1.00 169.63 ? 140 GLY A O   1 
ATOM   1010 N N   . ASN A 1 141 ? 30.672  5.773   25.090  1.00 51.38  ? 141 ASN A N   1 
ATOM   1011 C CA  . ASN A 1 141 ? 30.604  4.811   24.001  1.00 46.19  ? 141 ASN A CA  1 
ATOM   1012 C C   . ASN A 1 141 ? 30.074  5.500   22.747  1.00 41.13  ? 141 ASN A C   1 
ATOM   1013 O O   . ASN A 1 141 ? 29.516  6.596   22.807  1.00 36.92  ? 141 ASN A O   1 
ATOM   1014 C CB  . ASN A 1 141 ? 29.782  3.580   24.426  1.00 41.74  ? 141 ASN A CB  1 
ATOM   1015 C CG  . ASN A 1 141 ? 28.268  3.820   24.486  1.00 40.24  ? 141 ASN A CG  1 
ATOM   1016 O OD1 . ASN A 1 141 ? 27.660  4.406   23.589  1.00 37.08  ? 141 ASN A OD1 1 
ATOM   1017 N ND2 . ASN A 1 141 ? 27.658  3.363   25.576  1.00 39.72  ? 141 ASN A ND2 1 
ATOM   1018 N N   . VAL A 1 142 ? 30.299  4.863   21.593  1.00 38.27  ? 142 VAL A N   1 
ATOM   1019 C CA  . VAL A 1 142 ? 30.039  5.541   20.327  1.00 41.70  ? 142 VAL A CA  1 
ATOM   1020 C C   . VAL A 1 142 ? 28.556  5.819   20.113  1.00 38.91  ? 142 VAL A C   1 
ATOM   1021 O O   . VAL A 1 142 ? 28.211  6.728   19.354  1.00 34.63  ? 142 VAL A O   1 
ATOM   1022 C CB  . VAL A 1 142 ? 30.604  4.738   19.136  1.00 39.96  ? 142 VAL A CB  1 
ATOM   1023 C CG1 . VAL A 1 142 ? 32.115  4.560   19.276  1.00 45.91  ? 142 VAL A CG1 1 
ATOM   1024 C CG2 . VAL A 1 142 ? 29.906  3.383   19.015  1.00 40.19  ? 142 VAL A CG2 1 
ATOM   1025 N N   . ARG A 1 143 ? 27.663  5.060   20.754  1.00 36.24  ? 143 ARG A N   1 
ATOM   1026 C CA  . ARG A 1 143 ? 26.241  5.356   20.604  1.00 35.91  ? 143 ARG A CA  1 
ATOM   1027 C C   . ARG A 1 143 ? 25.850  6.571   21.427  1.00 33.65  ? 143 ARG A C   1 
ATOM   1028 O O   . ARG A 1 143 ? 25.042  7.394   20.984  1.00 31.09  ? 143 ARG A O   1 
ATOM   1029 C CB  . ARG A 1 143 ? 25.414  4.129   20.981  1.00 32.57  ? 143 ARG A CB  1 
ATOM   1030 C CG  . ARG A 1 143 ? 25.605  3.022   19.979  1.00 32.56  ? 143 ARG A CG  1 
ATOM   1031 C CD  . ARG A 1 143 ? 24.903  1.735   20.357  1.00 33.83  ? 143 ARG A CD  1 
ATOM   1032 N NE  . ARG A 1 143 ? 24.924  1.479   21.791  1.00 39.71  ? 143 ARG A NE  1 
ATOM   1033 C CZ  . ARG A 1 143 ? 25.928  0.882   22.416  1.00 38.28  ? 143 ARG A CZ  1 
ATOM   1034 N NH1 . ARG A 1 143 ? 27.035  0.534   21.775  1.00 39.78  ? 143 ARG A NH1 1 
ATOM   1035 N NH2 . ARG A 1 143 ? 25.823  0.631   23.717  1.00 41.17  ? 143 ARG A NH2 1 
ATOM   1036 N N   . GLN A 1 144 ? 26.441  6.718   22.614  1.00 30.32  ? 144 GLN A N   1 
ATOM   1037 C CA  . GLN A 1 144 ? 26.224  7.924   23.400  1.00 31.40  ? 144 GLN A CA  1 
ATOM   1038 C C   . GLN A 1 144 ? 26.701  9.157   22.642  1.00 33.03  ? 144 GLN A C   1 
ATOM   1039 O O   . GLN A 1 144 ? 26.000  10.175  22.582  1.00 33.54  ? 144 GLN A O   1 
ATOM   1040 C CB  . GLN A 1 144 ? 26.976  7.800   24.725  1.00 31.01  ? 144 GLN A CB  1 
ATOM   1041 C CG  . GLN A 1 144 ? 26.278  6.968   25.780  1.00 30.67  ? 144 GLN A CG  1 
ATOM   1042 C CD  . GLN A 1 144 ? 27.160  6.843   27.006  1.00 37.65  ? 144 GLN A CD  1 
ATOM   1043 O OE1 . GLN A 1 144 ? 28.365  6.663   26.876  1.00 38.15  ? 144 GLN A OE1 1 
ATOM   1044 N NE2 . GLN A 1 144 ? 26.573  6.965   28.191  1.00 35.41  ? 144 GLN A NE2 1 
ATOM   1045 N N   . LYS A 1 145 ? 27.911  9.091   22.075  1.00 33.80  ? 145 LYS A N   1 
ATOM   1046 C CA  . LYS A 1 145 ? 28.457  10.241  21.357  1.00 35.35  ? 145 LYS A CA  1 
ATOM   1047 C C   . LYS A 1 145 ? 27.602  10.589  20.153  1.00 35.64  ? 145 LYS A C   1 
ATOM   1048 O O   . LYS A 1 145 ? 27.353  11.765  19.873  1.00 33.09  ? 145 LYS A O   1 
ATOM   1049 C CB  . LYS A 1 145 ? 29.888  9.965   20.889  1.00 40.70  ? 145 LYS A CB  1 
ATOM   1050 C CG  . LYS A 1 145 ? 30.939  9.938   21.972  1.00 55.45  ? 145 LYS A CG  1 
ATOM   1051 C CD  . LYS A 1 145 ? 31.983  8.864   21.695  1.00 61.06  ? 145 LYS A CD  1 
ATOM   1052 C CE  . LYS A 1 145 ? 33.367  9.470   21.509  1.00 68.65  ? 145 LYS A CE  1 
ATOM   1053 N NZ  . LYS A 1 145 ? 34.193  8.697   20.531  1.00 67.87  ? 145 LYS A NZ  1 
ATOM   1054 N N   . SER A 1 146 ? 27.163  9.575   19.410  1.00 32.64  ? 146 SER A N   1 
ATOM   1055 C CA  . SER A 1 146 ? 26.402  9.845   18.197  1.00 30.62  ? 146 SER A CA  1 
ATOM   1056 C C   . SER A 1 146 ? 24.995  10.314  18.516  1.00 30.73  ? 146 SER A C   1 
ATOM   1057 O O   . SER A 1 146 ? 24.511  11.279  17.907  1.00 32.22  ? 146 SER A O   1 
ATOM   1058 C CB  . SER A 1 146 ? 26.381  8.606   17.308  1.00 32.34  ? 146 SER A CB  1 
ATOM   1059 O OG  . SER A 1 146 ? 27.699  8.279   16.925  1.00 36.70  ? 146 SER A OG  1 
ATOM   1060 N N   . LEU A 1 147 ? 24.331  9.662   19.470  1.00 28.69  ? 147 LEU A N   1 
ATOM   1061 C CA  . LEU A 1 147 ? 23.004  10.108  19.874  1.00 28.48  ? 147 LEU A CA  1 
ATOM   1062 C C   . LEU A 1 147 ? 23.047  11.547  20.372  1.00 30.28  ? 147 LEU A C   1 
ATOM   1063 O O   . LEU A 1 147 ? 22.194  12.364  20.012  1.00 30.89  ? 147 LEU A O   1 
ATOM   1064 C CB  . LEU A 1 147 ? 22.440  9.183   20.957  1.00 28.29  ? 147 LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 147 ? 21.013  9.502   21.402  1.00 27.69  ? 147 LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 147 ? 20.061  9.602   20.187  1.00 30.82  ? 147 LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 147 ? 20.485  8.484   22.395  1.00 31.92  ? 147 LEU A CD2 1 
ATOM   1068 N N   . ALA A 1 148 ? 24.053  11.888  21.180  1.00 28.13  ? 148 ALA A N   1 
ATOM   1069 C CA  . ALA A 1 148 ? 24.120  13.253  21.691  1.00 30.28  ? 148 ALA A CA  1 
ATOM   1070 C C   . ALA A 1 148 ? 24.191  14.275  20.566  1.00 29.67  ? 148 ALA A C   1 
ATOM   1071 O O   . ALA A 1 148 ? 23.514  15.311  20.616  1.00 32.33  ? 148 ALA A O   1 
ATOM   1072 C CB  . ALA A 1 148 ? 25.321  13.402  22.618  1.00 28.74  ? 148 ALA A CB  1 
ATOM   1073 N N   . VAL A 1 149 ? 25.010  14.014  19.543  1.00 30.99  ? 149 VAL A N   1 
ATOM   1074 C CA  . VAL A 1 149 ? 25.166  14.983  18.460  1.00 28.94  ? 149 VAL A CA  1 
ATOM   1075 C C   . VAL A 1 149 ? 23.869  15.146  17.673  1.00 30.68  ? 149 VAL A C   1 
ATOM   1076 O O   . VAL A 1 149 ? 23.463  16.269  17.353  1.00 29.12  ? 149 VAL A O   1 
ATOM   1077 C CB  . VAL A 1 149 ? 26.343  14.595  17.550  1.00 29.37  ? 149 VAL A CB  1 
ATOM   1078 C CG1 . VAL A 1 149 ? 26.343  15.448  16.272  1.00 34.02  ? 149 VAL A CG1 1 
ATOM   1079 C CG2 . VAL A 1 149 ? 27.648  14.838  18.292  1.00 33.55  ? 149 VAL A CG2 1 
ATOM   1080 N N   . VAL A 1 150 ? 23.205  14.040  17.326  1.00 27.92  ? 150 VAL A N   1 
ATOM   1081 C CA  . VAL A 1 150 ? 21.992  14.190  16.527  1.00 29.14  ? 150 VAL A CA  1 
ATOM   1082 C C   . VAL A 1 150 ? 20.828  14.691  17.388  1.00 29.01  ? 150 VAL A C   1 
ATOM   1083 O O   . VAL A 1 150 ? 19.959  15.429  16.901  1.00 29.02  ? 150 VAL A O   1 
ATOM   1084 C CB  . VAL A 1 150 ? 21.647  12.875  15.792  1.00 27.29  ? 150 VAL A CB  1 
ATOM   1085 C CG1 . VAL A 1 150 ? 21.272  11.769  16.776  1.00 31.83  ? 150 VAL A CG1 1 
ATOM   1086 C CG2 . VAL A 1 150 ? 20.524  13.125  14.781  1.00 30.08  ? 150 VAL A CG2 1 
ATOM   1087 N N   . LEU A 1 151 ? 20.792  14.320  18.669  1.00 28.84  ? 151 LEU A N   1 
ATOM   1088 C CA  . LEU A 1 151 ? 19.741  14.830  19.548  1.00 29.54  ? 151 LEU A CA  1 
ATOM   1089 C C   . LEU A 1 151 ? 19.855  16.340  19.708  1.00 29.21  ? 151 LEU A C   1 
ATOM   1090 O O   . LEU A 1 151 ? 18.842  17.052  19.681  1.00 28.00  ? 151 LEU A O   1 
ATOM   1091 C CB  . LEU A 1 151 ? 19.809  14.155  20.919  1.00 29.87  ? 151 LEU A CB  1 
ATOM   1092 C CG  . LEU A 1 151 ? 18.808  14.677  21.950  1.00 29.43  ? 151 LEU A CG  1 
ATOM   1093 C CD1 . LEU A 1 151 ? 17.401  14.194  21.587  1.00 31.52  ? 151 LEU A CD1 1 
ATOM   1094 C CD2 . LEU A 1 151 ? 19.191  14.217  23.349  1.00 31.68  ? 151 LEU A CD2 1 
ATOM   1095 N N   . ARG A 1 152 ? 21.081  16.837  19.890  1.00 27.96  ? 152 ARG A N   1 
ATOM   1096 C CA  . ARG A 1 152 ? 21.322  18.283  19.917  1.00 29.00  ? 152 ARG A CA  1 
ATOM   1097 C C   . ARG A 1 152 ? 20.670  18.969  18.727  1.00 30.19  ? 152 ARG A C   1 
ATOM   1098 O O   . ARG A 1 152 ? 19.996  20.001  18.869  1.00 30.10  ? 152 ARG A O   1 
ATOM   1099 C CB  . ARG A 1 152 ? 22.833  18.559  19.918  1.00 31.07  ? 152 ARG A CB  1 
ATOM   1100 C CG  . ARG A 1 152 ? 23.229  20.051  20.091  1.00 32.16  ? 152 ARG A CG  1 
ATOM   1101 C CD  . ARG A 1 152 ? 22.788  20.604  21.430  1.00 33.63  ? 152 ARG A CD  1 
ATOM   1102 N NE  . ARG A 1 152 ? 21.510  21.291  21.368  1.00 30.54  ? 152 ARG A NE  1 
ATOM   1103 C CZ  . ARG A 1 152 ? 20.835  21.695  22.435  1.00 32.99  ? 152 ARG A CZ  1 
ATOM   1104 N NH1 . ARG A 1 152 ? 21.280  21.466  23.663  1.00 34.88  ? 152 ARG A NH1 1 
ATOM   1105 N NH2 . ARG A 1 152 ? 19.690  22.352  22.269  1.00 31.81  ? 152 ARG A NH2 1 
ATOM   1106 N N   . LYS A 1 153 ? 20.887  18.421  17.534  1.00 29.32  ? 153 LYS A N   1 
ATOM   1107 C CA  . LYS A 1 153 ? 20.352  19.038  16.325  1.00 29.33  ? 153 LYS A CA  1 
ATOM   1108 C C   . LYS A 1 153 ? 18.835  18.939  16.264  1.00 27.33  ? 153 LYS A C   1 
ATOM   1109 O O   . LYS A 1 153 ? 18.165  19.874  15.803  1.00 28.05  ? 153 LYS A O   1 
ATOM   1110 C CB  . LYS A 1 153 ? 20.973  18.397  15.082  1.00 30.91  ? 153 LYS A CB  1 
ATOM   1111 C CG  . LYS A 1 153 ? 22.468  18.670  14.914  1.00 35.43  ? 153 LYS A CG  1 
ATOM   1112 C CD  . LYS A 1 153 ? 23.015  17.851  13.761  1.00 40.65  ? 153 LYS A CD  1 
ATOM   1113 C CE  . LYS A 1 153 ? 24.516  17.844  13.751  1.00 44.37  ? 153 LYS A CE  1 
ATOM   1114 N NZ  . LYS A 1 153 ? 25.024  16.910  12.698  1.00 51.35  ? 153 LYS A NZ  1 
ATOM   1115 N N   . ALA A 1 154 ? 18.275  17.810  16.711  1.00 26.98  ? 154 ALA A N   1 
ATOM   1116 C CA  . ALA A 1 154 ? 16.828  17.639  16.700  1.00 29.70  ? 154 ALA A CA  1 
ATOM   1117 C C   . ALA A 1 154 ? 16.154  18.559  17.706  1.00 26.78  ? 154 ALA A C   1 
ATOM   1118 O O   . ALA A 1 154 ? 15.041  19.037  17.459  1.00 30.94  ? 154 ALA A O   1 
ATOM   1119 C CB  . ALA A 1 154 ? 16.471  16.174  16.977  1.00 26.65  ? 154 ALA A CB  1 
ATOM   1120 N N   . ILE A 1 155 ? 16.823  18.854  18.827  1.00 26.03  ? 155 ILE A N   1 
ATOM   1121 C CA  . ILE A 1 155 ? 16.317  19.887  19.726  1.00 25.71  ? 155 ILE A CA  1 
ATOM   1122 C C   . ILE A 1 155 ? 16.355  21.238  19.035  1.00 27.78  ? 155 ILE A C   1 
ATOM   1123 O O   . ILE A 1 155 ? 15.366  21.976  19.037  1.00 29.33  ? 155 ILE A O   1 
ATOM   1124 C CB  . ILE A 1 155 ? 17.129  19.928  21.032  1.00 26.15  ? 155 ILE A CB  1 
ATOM   1125 C CG1 . ILE A 1 155 ? 17.037  18.602  21.772  1.00 28.23  ? 155 ILE A CG1 1 
ATOM   1126 C CG2 . ILE A 1 155 ? 16.626  21.076  21.926  1.00 28.64  ? 155 ILE A CG2 1 
ATOM   1127 C CD1 . ILE A 1 155 ? 18.086  18.455  22.871  1.00 30.06  ? 155 ILE A CD1 1 
ATOM   1128 N N   . ASP A 1 156 ? 17.501  21.576  18.428  1.00 28.12  ? 156 ASP A N   1 
ATOM   1129 C CA  . ASP A 1 156 ? 17.688  22.914  17.854  1.00 28.41  ? 156 ASP A CA  1 
ATOM   1130 C C   . ASP A 1 156 ? 16.648  23.213  16.785  1.00 32.52  ? 156 ASP A C   1 
ATOM   1131 O O   . ASP A 1 156 ? 16.190  24.355  16.654  1.00 31.79  ? 156 ASP A O   1 
ATOM   1132 C CB  . ASP A 1 156 ? 19.083  23.058  17.230  1.00 28.61  ? 156 ASP A CB  1 
ATOM   1133 C CG  . ASP A 1 156 ? 20.229  22.963  18.254  1.00 32.24  ? 156 ASP A CG  1 
ATOM   1134 O OD1 . ASP A 1 156 ? 20.023  23.183  19.467  1.00 32.49  ? 156 ASP A OD1 1 
ATOM   1135 O OD2 . ASP A 1 156 ? 21.360  22.673  17.815  1.00 30.77  ? 156 ASP A OD2 1 
ATOM   1136 N N   . ILE A 1 157 ? 16.309  22.215  15.967  1.00 29.86  ? 157 ILE A N   1 
ATOM   1137 C CA  . ILE A 1 157 ? 15.404  22.467  14.846  1.00 30.25  ? 157 ILE A CA  1 
ATOM   1138 C C   . ILE A 1 157 ? 13.964  22.682  15.290  1.00 29.34  ? 157 ILE A C   1 
ATOM   1139 O O   . ILE A 1 157 ? 13.179  23.285  14.547  1.00 33.17  ? 157 ILE A O   1 
ATOM   1140 C CB  . ILE A 1 157 ? 15.527  21.323  13.819  1.00 31.32  ? 157 ILE A CB  1 
ATOM   1141 C CG1 . ILE A 1 157 ? 15.271  21.846  12.394  1.00 31.80  ? 157 ILE A CG1 1 
ATOM   1142 C CG2 . ILE A 1 157 ? 14.665  20.126  14.219  1.00 32.42  ? 157 ILE A CG2 1 
ATOM   1143 C CD1 . ILE A 1 157 ? 15.357  20.775  11.301  1.00 33.28  ? 157 ILE A CD1 1 
ATOM   1144 N N   . ASP A 1 158 ? 13.585  22.224  16.482  1.00 29.21  ? 158 ASP A N   1 
ATOM   1145 C CA  . ASP A 1 158 ? 12.211  22.373  16.970  1.00 29.37  ? 158 ASP A CA  1 
ATOM   1146 C C   . ASP A 1 158 ? 12.232  22.395  18.491  1.00 32.14  ? 158 ASP A C   1 
ATOM   1147 O O   . ASP A 1 158 ? 11.845  21.428  19.157  1.00 31.91  ? 158 ASP A O   1 
ATOM   1148 C CB  . ASP A 1 158 ? 11.316  21.246  16.447  1.00 29.33  ? 158 ASP A CB  1 
ATOM   1149 C CG  . ASP A 1 158 ? 9.831   21.556  16.619  1.00 34.77  ? 158 ASP A CG  1 
ATOM   1150 O OD1 . ASP A 1 158 ? 9.482   22.378  17.509  1.00 32.78  ? 158 ASP A OD1 1 
ATOM   1151 O OD2 . ASP A 1 158 ? 9.002   20.975  15.869  1.00 33.11  ? 158 ASP A OD2 1 
ATOM   1152 N N   . PRO A 1 159 ? 12.678  23.502  19.081  1.00 31.20  ? 159 PRO A N   1 
ATOM   1153 C CA  . PRO A 1 159 ? 12.785  23.545  20.544  1.00 32.97  ? 159 PRO A CA  1 
ATOM   1154 C C   . PRO A 1 159 ? 11.449  23.415  21.245  1.00 30.07  ? 159 PRO A C   1 
ATOM   1155 O O   . PRO A 1 159 ? 11.408  22.884  22.361  1.00 33.24  ? 159 PRO A O   1 
ATOM   1156 C CB  . PRO A 1 159 ? 13.446  24.911  20.809  1.00 34.24  ? 159 PRO A CB  1 
ATOM   1157 C CG  . PRO A 1 159 ? 13.196  25.694  19.595  1.00 32.22  ? 159 PRO A CG  1 
ATOM   1158 C CD  . PRO A 1 159 ? 13.191  24.727  18.450  1.00 33.49  ? 159 PRO A CD  1 
ATOM   1159 N N   . LYS A 1 160 ? 10.352  23.839  20.614  1.00 30.27  ? 160 LYS A N   1 
ATOM   1160 C CA  . LYS A 1 160 ? 9.048   23.738  21.266  1.00 33.58  ? 160 LYS A CA  1 
ATOM   1161 C C   . LYS A 1 160 ? 8.666   22.281  21.497  1.00 34.82  ? 160 LYS A C   1 
ATOM   1162 O O   . LYS A 1 160 ? 8.098   21.940  22.538  1.00 33.66  ? 160 LYS A O   1 
ATOM   1163 C CB  . LYS A 1 160 ? 7.976   24.440  20.429  1.00 38.05  ? 160 LYS A CB  1 
ATOM   1164 C CG  . LYS A 1 160 ? 6.562   24.315  20.989  1.00 43.64  ? 160 LYS A CG  1 
ATOM   1165 C CD  . LYS A 1 160 ? 5.686   25.504  20.630  1.00 53.31  ? 160 LYS A CD  1 
ATOM   1166 C CE  . LYS A 1 160 ? 5.818   25.870  19.155  1.00 54.72  ? 160 LYS A CE  1 
ATOM   1167 N NZ  . LYS A 1 160 ? 5.918   27.345  18.957  1.00 61.39  ? 160 LYS A NZ  1 
ATOM   1168 N N   . GLN A 1 161 ? 8.957   21.419  20.525  1.00 34.53  ? 161 GLN A N   1 
ATOM   1169 C CA  . GLN A 1 161 ? 8.654   19.993  20.622  1.00 30.82  ? 161 GLN A CA  1 
ATOM   1170 C C   . GLN A 1 161 ? 9.708   19.201  21.385  1.00 33.14  ? 161 GLN A C   1 
ATOM   1171 O O   . GLN A 1 161 ? 9.440   18.042  21.736  1.00 31.57  ? 161 GLN A O   1 
ATOM   1172 C CB  . GLN A 1 161 ? 8.486   19.415  19.214  1.00 28.76  ? 161 GLN A CB  1 
ATOM   1173 C CG  . GLN A 1 161 ? 7.146   19.838  18.565  1.00 32.68  ? 161 GLN A CG  1 
ATOM   1174 C CD  . GLN A 1 161 ? 6.640   18.844  17.526  1.00 41.79  ? 161 GLN A CD  1 
ATOM   1175 O OE1 . GLN A 1 161 ? 6.562   19.143  16.318  1.00 43.30  ? 161 GLN A OE1 1 
ATOM   1176 N NE2 . GLN A 1 161 ? 6.369   17.624  17.978  1.00 37.61  ? 161 GLN A NE2 1 
ATOM   1177 N N   . ALA A 1 162 ? 10.877  19.786  21.661  1.00 30.39  ? 162 ALA A N   1 
ATOM   1178 C CA  . ALA A 1 162 ? 11.970  19.003  22.246  1.00 32.06  ? 162 ALA A CA  1 
ATOM   1179 C C   . ALA A 1 162 ? 11.648  18.380  23.603  1.00 33.59  ? 162 ALA A C   1 
ATOM   1180 O O   . ALA A 1 162 ? 12.077  17.232  23.833  1.00 30.15  ? 162 ALA A O   1 
ATOM   1181 C CB  . ALA A 1 162 ? 13.238  19.858  22.335  1.00 31.55  ? 162 ALA A CB  1 
ATOM   1182 N N   . PRO A 1 163 ? 10.930  19.034  24.531  1.00 30.50  ? 163 PRO A N   1 
ATOM   1183 C CA  . PRO A 1 163 ? 10.614  18.339  25.792  1.00 31.46  ? 163 PRO A CA  1 
ATOM   1184 C C   . PRO A 1 163 ? 9.813   17.066  25.585  1.00 32.93  ? 163 PRO A C   1 
ATOM   1185 O O   . PRO A 1 163 ? 10.094  16.041  26.227  1.00 33.57  ? 163 PRO A O   1 
ATOM   1186 C CB  . PRO A 1 163 ? 9.824   19.389  26.580  1.00 35.33  ? 163 PRO A CB  1 
ATOM   1187 C CG  . PRO A 1 163 ? 10.390  20.698  26.079  1.00 34.53  ? 163 PRO A CG  1 
ATOM   1188 C CD  . PRO A 1 163 ? 10.562  20.467  24.600  1.00 32.53  ? 163 PRO A CD  1 
ATOM   1189 N N   . ALA A 1 164 ? 8.819   17.108  24.695  1.00 30.52  ? 164 ALA A N   1 
ATOM   1190 C CA  . ALA A 1 164 ? 8.026   15.920  24.410  1.00 32.80  ? 164 ALA A CA  1 
ATOM   1191 C C   . ALA A 1 164 ? 8.874   14.844  23.744  1.00 31.50  ? 164 ALA A C   1 
ATOM   1192 O O   . ALA A 1 164 ? 8.744   13.657  24.072  1.00 32.26  ? 164 ALA A O   1 
ATOM   1193 C CB  . ALA A 1 164 ? 6.835   16.284  23.529  1.00 32.93  ? 164 ALA A CB  1 
ATOM   1194 N N   . MET A 1 165 ? 9.722   15.238  22.784  1.00 30.19  ? 165 MET A N   1 
ATOM   1195 C CA  . MET A 1 165 ? 10.655  14.297  22.155  1.00 28.35  ? 165 MET A CA  1 
ATOM   1196 C C   . MET A 1 165 ? 11.497  13.574  23.193  1.00 30.73  ? 165 MET A C   1 
ATOM   1197 O O   . MET A 1 165 ? 11.652  12.338  23.164  1.00 29.74  ? 165 MET A O   1 
ATOM   1198 C CB  . MET A 1 165 ? 11.596  15.038  21.213  1.00 27.11  ? 165 MET A CB  1 
ATOM   1199 C CG  . MET A 1 165 ? 12.529  14.104  20.458  1.00 27.75  ? 165 MET A CG  1 
ATOM   1200 S SD  . MET A 1 165 ? 13.505  14.878  19.173  1.00 29.09  ? 165 MET A SD  1 
ATOM   1201 C CE  . MET A 1 165 ? 14.402  16.104  20.133  1.00 29.83  ? 165 MET A CE  1 
ATOM   1202 N N   . ILE A 1 166 ? 12.073  14.353  24.105  1.00 29.54  ? 166 ILE A N   1 
ATOM   1203 C CA  . ILE A 1 166 ? 12.987  13.764  25.120  1.00 29.28  ? 166 ILE A CA  1 
ATOM   1204 C C   . ILE A 1 166 ? 12.181  12.837  26.021  1.00 29.16  ? 166 ILE A C   1 
ATOM   1205 O O   . ILE A 1 166 ? 12.654  11.743  26.310  1.00 30.69  ? 166 ILE A O   1 
ATOM   1206 C CB  . ILE A 1 166 ? 13.685  14.871  25.925  1.00 29.22  ? 166 ILE A CB  1 
ATOM   1207 C CG1 . ILE A 1 166 ? 14.555  15.762  25.036  1.00 35.97  ? 166 ILE A CG1 1 
ATOM   1208 C CG2 . ILE A 1 166 ? 14.474  14.282  27.083  1.00 32.80  ? 166 ILE A CG2 1 
ATOM   1209 C CD1 . ILE A 1 166 ? 15.964  15.265  24.872  1.00 35.79  ? 166 ILE A CD1 1 
ATOM   1210 N N   . GLU A 1 167 ? 10.993  13.278  26.420  1.00 27.96  ? 167 GLU A N   1 
ATOM   1211 C CA  . GLU A 1 167 ? 10.173  12.390  27.234  1.00 33.55  ? 167 GLU A CA  1 
ATOM   1212 C C   . GLU A 1 167 ? 9.881   11.097  26.501  1.00 31.29  ? 167 GLU A C   1 
ATOM   1213 O O   . GLU A 1 167 ? 9.905   10.013  27.100  1.00 32.43  ? 167 GLU A O   1 
ATOM   1214 C CB  . GLU A 1 167 ? 8.858   13.057  27.636  1.00 35.61  ? 167 GLU A CB  1 
ATOM   1215 C CG  . GLU A 1 167 ? 8.063   12.198  28.623  1.00 40.97  ? 167 GLU A CG  1 
ATOM   1216 C CD  . GLU A 1 167 ? 8.911   11.636  29.780  1.00 47.74  ? 167 GLU A CD  1 
ATOM   1217 O OE1 . GLU A 1 167 ? 9.774   12.360  30.336  1.00 51.80  ? 167 GLU A OE1 1 
ATOM   1218 O OE2 . GLU A 1 167 ? 8.743   10.435  30.106  1.00 50.79  ? 167 GLU A OE2 1 
ATOM   1219 N N   . MET A 1 168 ? 9.586   11.189  25.208  1.00 28.96  ? 168 MET A N   1 
ATOM   1220 C CA  . MET A 1 168 ? 9.271   9.971   24.476  1.00 29.59  ? 168 MET A CA  1 
ATOM   1221 C C   . MET A 1 168 ? 10.487  9.056   24.444  1.00 30.57  ? 168 MET A C   1 
ATOM   1222 O O   . MET A 1 168 ? 10.360  7.832   24.569  1.00 29.83  ? 168 MET A O   1 
ATOM   1223 C CB  . MET A 1 168 ? 8.834   10.312  23.052  1.00 27.92  ? 168 MET A CB  1 
ATOM   1224 C CG  . MET A 1 168 ? 8.682   9.089   22.147  1.00 28.99  ? 168 MET A CG  1 
ATOM   1225 S SD  . MET A 1 168 ? 10.242  8.602   21.384  1.00 28.97  ? 168 MET A SD  1 
ATOM   1226 C CE  . MET A 1 168 ? 10.559  9.951   20.262  1.00 29.08  ? 168 MET A CE  1 
ATOM   1227 N N   . LEU A 1 169 ? 11.683  9.629   24.265  1.00 29.93  ? 169 LEU A N   1 
ATOM   1228 C CA  . LEU A 1 169 ? 12.874  8.798   24.124  1.00 28.13  ? 169 LEU A CA  1 
ATOM   1229 C C   . LEU A 1 169 ? 13.249  8.155   25.450  1.00 28.91  ? 169 LEU A C   1 
ATOM   1230 O O   . LEU A 1 169 ? 13.655  6.986   25.487  1.00 28.68  ? 169 LEU A O   1 
ATOM   1231 C CB  . LEU A 1 169 ? 14.043  9.626   23.576  1.00 28.07  ? 169 LEU A CB  1 
ATOM   1232 C CG  . LEU A 1 169 ? 13.846  10.093  22.124  1.00 27.55  ? 169 LEU A CG  1 
ATOM   1233 C CD1 . LEU A 1 169 ? 14.910  11.122  21.750  1.00 27.02  ? 169 LEU A CD1 1 
ATOM   1234 C CD2 . LEU A 1 169 ? 13.948  8.857   21.201  1.00 26.98  ? 169 LEU A CD2 1 
ATOM   1235 N N   . ARG A 1 170 ? 13.082  8.898   26.532  1.00 30.20  ? 170 ARG A N   1 
ATOM   1236 C CA  . ARG A 1 170 ? 13.381  8.332   27.867  1.00 31.31  ? 170 ARG A CA  1 
ATOM   1237 C C   . ARG A 1 170 ? 12.382  7.206   28.159  1.00 31.44  ? 170 ARG A C   1 
ATOM   1238 O O   . ARG A 1 170 ? 12.792  6.168   28.667  1.00 31.34  ? 170 ARG A O   1 
ATOM   1239 C CB  . ARG A 1 170 ? 13.334  9.429   28.931  1.00 32.92  ? 170 ARG A CB  1 
ATOM   1240 C CG  . ARG A 1 170 ? 14.388  10.514  28.787  1.00 35.59  ? 170 ARG A CG  1 
ATOM   1241 C CD  . ARG A 1 170 ? 14.224  11.489  29.936  1.00 46.67  ? 170 ARG A CD  1 
ATOM   1242 N NE  . ARG A 1 170 ? 15.254  12.508  30.014  1.00 47.03  ? 170 ARG A NE  1 
ATOM   1243 C CZ  . ARG A 1 170 ? 15.089  13.687  30.596  1.00 48.17  ? 170 ARG A CZ  1 
ATOM   1244 N NH1 . ARG A 1 170 ? 13.929  13.991  31.150  1.00 52.45  ? 170 ARG A NH1 1 
ATOM   1245 N NH2 . ARG A 1 170 ? 16.081  14.556  30.624  1.00 48.43  ? 170 ARG A NH2 1 
ATOM   1246 N N   . HIS A 1 171 ? 11.117  7.424   27.818  1.00 33.93  ? 171 HIS A N   1 
ATOM   1247 C CA  . HIS A 1 171 ? 10.119  6.388   28.060  1.00 34.09  ? 171 HIS A CA  1 
ATOM   1248 C C   . HIS A 1 171 ? 10.386  5.157   27.196  1.00 34.53  ? 171 HIS A C   1 
ATOM   1249 O O   . HIS A 1 171 ? 10.220  4.018   27.656  1.00 32.89  ? 171 HIS A O   1 
ATOM   1250 C CB  . HIS A 1 171 ? 8.720   6.954   27.825  1.00 35.89  ? 171 HIS A CB  1 
ATOM   1251 C CG  . HIS A 1 171 ? 7.619   5.967   28.051  1.00 38.65  ? 171 HIS A CG  1 
ATOM   1252 N ND1 . HIS A 1 171 ? 7.187   5.620   29.313  1.00 38.64  ? 171 HIS A ND1 1 
ATOM   1253 C CD2 . HIS A 1 171 ? 6.829   5.293   27.183  1.00 37.38  ? 171 HIS A CD2 1 
ATOM   1254 C CE1 . HIS A 1 171 ? 6.196   4.752   29.212  1.00 41.29  ? 171 HIS A CE1 1 
ATOM   1255 N NE2 . HIS A 1 171 ? 5.957   4.537   27.930  1.00 39.04  ? 171 HIS A NE2 1 
ATOM   1256 N N   . TYR A 1 172 ? 10.822  5.365   25.948  1.00 31.49  ? 172 TYR A N   1 
ATOM   1257 C CA  . TYR A 1 172 ? 11.213  4.238   25.104  1.00 31.50  ? 172 TYR A CA  1 
ATOM   1258 C C   . TYR A 1 172 ? 12.307  3.417   25.780  1.00 32.04  ? 172 TYR A C   1 
ATOM   1259 O O   . TYR A 1 172 ? 12.173  2.201   25.953  1.00 32.03  ? 172 TYR A O   1 
ATOM   1260 C CB  . TYR A 1 172 ? 11.700  4.737   23.744  1.00 31.82  ? 172 TYR A CB  1 
ATOM   1261 C CG  . TYR A 1 172 ? 12.378  3.666   22.893  1.00 28.97  ? 172 TYR A CG  1 
ATOM   1262 C CD1 . TYR A 1 172 ? 11.625  2.674   22.267  1.00 28.95  ? 172 TYR A CD1 1 
ATOM   1263 C CD2 . TYR A 1 172 ? 13.760  3.647   22.725  1.00 28.87  ? 172 TYR A CD2 1 
ATOM   1264 C CE1 . TYR A 1 172 ? 12.236  1.687   21.478  1.00 32.70  ? 172 TYR A CE1 1 
ATOM   1265 C CE2 . TYR A 1 172 ? 14.379  2.653   21.946  1.00 31.14  ? 172 TYR A CE2 1 
ATOM   1266 C CZ  . TYR A 1 172 ? 13.615  1.693   21.327  1.00 30.33  ? 172 TYR A CZ  1 
ATOM   1267 O OH  . TYR A 1 172 ? 14.225  0.719   20.554  1.00 29.78  ? 172 TYR A OH  1 
ATOM   1268 N N   . LEU A 1 173 ? 13.404  4.054   26.174  1.00 28.34  ? 173 LEU A N   1 
ATOM   1269 C CA  . LEU A 1 173 ? 14.541  3.254   26.705  1.00 32.76  ? 173 LEU A CA  1 
ATOM   1270 C C   . LEU A 1 173 ? 14.146  2.603   28.032  1.00 33.58  ? 173 LEU A C   1 
ATOM   1271 O O   . LEU A 1 173 ? 14.670  1.531   28.342  1.00 34.23  ? 173 LEU A O   1 
ATOM   1272 C CB  . LEU A 1 173 ? 15.778  4.146   26.843  1.00 31.84  ? 173 LEU A CB  1 
ATOM   1273 C CG  . LEU A 1 173 ? 16.585  4.351   25.566  1.00 31.91  ? 173 LEU A CG  1 
ATOM   1274 C CD1 . LEU A 1 173 ? 17.774  5.259   25.826  1.00 29.16  ? 173 LEU A CD1 1 
ATOM   1275 C CD2 . LEU A 1 173 ? 17.044  3.018   25.003  1.00 29.84  ? 173 LEU A CD2 1 
ATOM   1276 N N   . ALA A 1 174 ? 13.237  3.236   28.763  1.00 32.97  ? 174 ALA A N   1 
ATOM   1277 C CA  . ALA A 1 174 ? 12.844  2.694   30.055  1.00 37.17  ? 174 ALA A CA  1 
ATOM   1278 C C   . ALA A 1 174 ? 11.906  1.502   29.943  1.00 37.16  ? 174 ALA A C   1 
ATOM   1279 O O   . ALA A 1 174 ? 11.799  0.741   30.908  1.00 37.95  ? 174 ALA A O   1 
ATOM   1280 C CB  . ALA A 1 174 ? 12.172  3.784   30.895  1.00 38.64  ? 174 ALA A CB  1 
ATOM   1281 N N   . THR A 1 175 ? 11.207  1.330   28.807  1.00 35.54  ? 175 THR A N   1 
ATOM   1282 C CA  . THR A 1 175 ? 10.120  0.356   28.723  1.00 35.79  ? 175 THR A CA  1 
ATOM   1283 C C   . THR A 1 175 ? 10.172  -0.605  27.544  1.00 36.02  ? 175 THR A C   1 
ATOM   1284 O O   . THR A 1 175 ? 9.524   -1.654  27.620  1.00 39.55  ? 175 THR A O   1 
ATOM   1285 C CB  . THR A 1 175 ? 8.755   1.064   28.687  1.00 40.26  ? 175 THR A CB  1 
ATOM   1286 O OG1 . THR A 1 175 ? 8.632   1.841   27.482  1.00 38.54  ? 175 THR A OG1 1 
ATOM   1287 C CG2 . THR A 1 175 ? 8.561   1.950   29.909  1.00 40.25  ? 175 THR A CG2 1 
ATOM   1288 N N   . PHE A 1 176 ? 10.906  -0.311  26.469  1.00 33.20  ? 176 PHE A N   1 
ATOM   1289 C CA  . PHE A 1 176 ? 10.730  -1.107  25.259  1.00 30.78  ? 176 PHE A CA  1 
ATOM   1290 C C   . PHE A 1 176 ? 11.241  -2.530  25.414  1.00 36.25  ? 176 PHE A C   1 
ATOM   1291 O O   . PHE A 1 176 ? 10.781  -3.414  24.684  1.00 33.13  ? 176 PHE A O   1 
ATOM   1292 C CB  . PHE A 1 176 ? 11.424  -0.451  24.071  1.00 33.80  ? 176 PHE A CB  1 
ATOM   1293 C CG  . PHE A 1 176 ? 12.867  -0.851  23.897  1.00 31.28  ? 176 PHE A CG  1 
ATOM   1294 C CD1 . PHE A 1 176 ? 13.852  -0.311  24.719  1.00 31.01  ? 176 PHE A CD1 1 
ATOM   1295 C CD2 . PHE A 1 176 ? 13.240  -1.760  22.911  1.00 32.50  ? 176 PHE A CD2 1 
ATOM   1296 C CE1 . PHE A 1 176 ? 15.181  -0.655  24.550  1.00 30.86  ? 176 PHE A CE1 1 
ATOM   1297 C CE2 . PHE A 1 176 ? 14.566  -2.118  22.739  1.00 35.51  ? 176 PHE A CE2 1 
ATOM   1298 C CZ  . PHE A 1 176 ? 15.546  -1.562  23.564  1.00 33.14  ? 176 PHE A CZ  1 
ATOM   1299 N N   . ASP A 1 177 ? 12.175  -2.740  26.345  1.00 32.50  ? 177 ASP A N   1 
ATOM   1300 C CA  . ASP A 1 177 ? 12.878  -3.991  26.604  1.00 39.62  ? 177 ASP A CA  1 
ATOM   1301 C C   . ASP A 1 177 ? 12.566  -4.571  27.979  1.00 41.05  ? 177 ASP A C   1 
ATOM   1302 O O   . ASP A 1 177 ? 13.152  -5.594  28.353  1.00 49.29  ? 177 ASP A O   1 
ATOM   1303 C CB  . ASP A 1 177 ? 14.394  -3.742  26.503  1.00 39.03  ? 177 ASP A CB  1 
ATOM   1304 C CG  . ASP A 1 177 ? 15.167  -4.956  26.074  1.00 43.38  ? 177 ASP A CG  1 
ATOM   1305 O OD1 . ASP A 1 177 ? 14.555  -6.016  25.782  1.00 43.23  ? 177 ASP A OD1 1 
ATOM   1306 O OD2 . ASP A 1 177 ? 16.404  -4.831  26.004  1.00 40.28  ? 177 ASP A OD2 1 
ATOM   1307 N N   . ASN A 1 178 ? 11.661  -3.957  28.735  1.00 40.65  ? 178 ASN A N   1 
ATOM   1308 C CA  . ASN A 1 178 ? 11.515  -4.217  30.167  1.00 43.38  ? 178 ASN A CA  1 
ATOM   1309 C C   . ASN A 1 178 ? 10.608  -5.420  30.412  1.00 47.55  ? 178 ASN A C   1 
ATOM   1310 O O   . ASN A 1 178 ? 9.504   -5.315  30.948  1.00 51.52  ? 178 ASN A O   1 
ATOM   1311 C CB  . ASN A 1 178 ? 10.976  -2.977  30.869  1.00 44.93  ? 178 ASN A CB  1 
ATOM   1312 C CG  . ASN A 1 178 ? 11.591  -2.775  32.236  1.00 52.56  ? 178 ASN A CG  1 
ATOM   1313 O OD1 . ASN A 1 178 ? 12.806  -2.847  32.396  1.00 57.35  ? 178 ASN A OD1 1 
ATOM   1314 N ND2 . ASN A 1 178 ? 10.749  -2.528  33.235  1.00 55.95  ? 178 ASN A ND2 1 
ATOM   1315 N N   . ILE A 1 179 ? 11.105  -6.589  30.020  1.00 42.77  ? 179 ILE A N   1 
ATOM   1316 C CA  . ILE A 1 179 ? 10.370  -7.831  30.218  1.00 42.72  ? 179 ILE A CA  1 
ATOM   1317 C C   . ILE A 1 179 ? 11.324  -8.890  30.754  1.00 42.74  ? 179 ILE A C   1 
ATOM   1318 O O   . ILE A 1 179 ? 12.520  -8.893  30.447  1.00 47.48  ? 179 ILE A O   1 
ATOM   1319 C CB  . ILE A 1 179 ? 9.666   -8.289  28.918  1.00 43.08  ? 179 ILE A CB  1 
ATOM   1320 C CG1 . ILE A 1 179 ? 8.282   -8.847  29.242  1.00 47.68  ? 179 ILE A CG1 1 
ATOM   1321 C CG2 . ILE A 1 179 ? 10.511  -9.275  28.146  1.00 48.19  ? 179 ILE A CG2 1 
ATOM   1322 C CD1 . ILE A 1 179 ? 7.330   -7.812  29.794  1.00 49.36  ? 179 ILE A CD1 1 
ATOM   1323 N N   . GLY A 1 180 ? 10.785  -9.786  31.582  1.00 46.28  ? 180 GLY A N   1 
ATOM   1324 C CA  . GLY A 1 180 ? 11.587  -10.811 32.220  1.00 47.02  ? 180 GLY A CA  1 
ATOM   1325 C C   . GLY A 1 180 ? 11.705  -12.136 31.493  1.00 46.30  ? 180 GLY A C   1 
ATOM   1326 O O   . GLY A 1 180 ? 12.586  -12.928 31.834  1.00 43.03  ? 180 GLY A O   1 
ATOM   1327 N N   . GLY A 1 181 ? 10.869  -12.411 30.498  1.00 43.72  ? 181 GLY A N   1 
ATOM   1328 C CA  . GLY A 1 181 ? 10.953  -13.696 29.825  1.00 36.86  ? 181 GLY A CA  1 
ATOM   1329 C C   . GLY A 1 181 ? 9.924   -13.844 28.729  1.00 43.38  ? 181 GLY A C   1 
ATOM   1330 O O   . GLY A 1 181 ? 9.409   -12.856 28.202  1.00 44.68  ? 181 GLY A O   1 
ATOM   1331 N N   . ASP A 1 182 ? 9.629   -15.101 28.401  1.00 40.09  ? 182 ASP A N   1 
ATOM   1332 C CA  . ASP A 1 182 ? 8.821   -15.441 27.233  1.00 40.02  ? 182 ASP A CA  1 
ATOM   1333 C C   . ASP A 1 182 ? 7.331   -15.230 27.478  1.00 40.75  ? 182 ASP A C   1 
ATOM   1334 O O   . ASP A 1 182 ? 6.843   -15.286 28.610  1.00 35.13  ? 182 ASP A O   1 
ATOM   1335 C CB  . ASP A 1 182 ? 9.061   -16.896 26.831  1.00 43.21  ? 182 ASP A CB  1 
ATOM   1336 C CG  . ASP A 1 182 ? 10.412  -17.110 26.180  1.00 46.76  ? 182 ASP A CG  1 
ATOM   1337 O OD1 . ASP A 1 182 ? 11.278  -16.217 26.280  1.00 56.27  ? 182 ASP A OD1 1 
ATOM   1338 O OD2 . ASP A 1 182 ? 10.609  -18.189 25.582  1.00 53.90  ? 182 ASP A OD2 1 
ATOM   1339 N N   . PHE A 1 183 ? 6.599   -15.005 26.384  1.00 40.86  ? 183 PHE A N   1 
ATOM   1340 C CA  . PHE A 1 183 ? 5.154   -14.838 26.405  1.00 39.97  ? 183 PHE A CA  1 
ATOM   1341 C C   . PHE A 1 183 ? 4.455   -16.094 25.900  1.00 38.92  ? 183 PHE A C   1 
ATOM   1342 O O   . PHE A 1 183 ? 4.964   -16.802 25.025  1.00 42.35  ? 183 PHE A O   1 
ATOM   1343 C CB  . PHE A 1 183 ? 4.729   -13.663 25.524  1.00 37.42  ? 183 PHE A CB  1 
ATOM   1344 C CG  . PHE A 1 183 ? 5.036   -12.323 26.101  1.00 33.61  ? 183 PHE A CG  1 
ATOM   1345 C CD1 . PHE A 1 183 ? 4.143   -11.703 26.955  1.00 34.88  ? 183 PHE A CD1 1 
ATOM   1346 C CD2 . PHE A 1 183 ? 6.197   -11.654 25.750  1.00 39.15  ? 183 PHE A CD2 1 
ATOM   1347 C CE1 . PHE A 1 183 ? 4.405   -10.454 27.467  1.00 36.18  ? 183 PHE A CE1 1 
ATOM   1348 C CE2 . PHE A 1 183 ? 6.469   -10.402 26.263  1.00 39.09  ? 183 PHE A CE2 1 
ATOM   1349 C CZ  . PHE A 1 183 ? 5.567   -9.796  27.126  1.00 39.32  ? 183 PHE A CZ  1 
ATOM   1350 N N   . THR A 1 184 ? 3.256   -16.348 26.442  1.00 34.26  ? 184 THR A N   1 
ATOM   1351 C CA  . THR A 1 184 ? 2.456   -17.491 26.025  1.00 39.54  ? 184 THR A CA  1 
ATOM   1352 C C   . THR A 1 184 ? 1.051   -17.135 25.546  1.00 37.11  ? 184 THR A C   1 
ATOM   1353 O O   . THR A 1 184 ? 0.311   -18.040 25.160  1.00 38.36  ? 184 THR A O   1 
ATOM   1354 C CB  . THR A 1 184 ? 2.341   -18.514 27.165  1.00 45.55  ? 184 THR A CB  1 
ATOM   1355 O OG1 . THR A 1 184 ? 1.345   -18.080 28.100  1.00 49.43  ? 184 THR A OG1 1 
ATOM   1356 C CG2 . THR A 1 184 ? 3.645   -18.608 27.873  1.00 43.27  ? 184 THR A CG2 1 
ATOM   1357 N N   . ARG A 1 185 ? 0.646   -15.867 25.590  1.00 34.75  ? 185 ARG A N   1 
ATOM   1358 C CA  . ARG A 1 185 ? -0.614  -15.461 24.979  1.00 37.41  ? 185 ARG A CA  1 
ATOM   1359 C C   . ARG A 1 185 ? -0.429  -14.153 24.230  1.00 34.50  ? 185 ARG A C   1 
ATOM   1360 O O   . ARG A 1 185 ? 0.257   -13.247 24.701  1.00 36.97  ? 185 ARG A O   1 
ATOM   1361 C CB  . ARG A 1 185 ? -1.754  -15.296 25.998  1.00 42.33  ? 185 ARG A CB  1 
ATOM   1362 C CG  . ARG A 1 185 ? -1.871  -16.402 27.036  1.00 50.40  ? 185 ARG A CG  1 
ATOM   1363 C CD  . ARG A 1 185 ? -3.066  -16.158 27.940  1.00 52.98  ? 185 ARG A CD  1 
ATOM   1364 N NE  . ARG A 1 185 ? -2.945  -14.907 28.678  1.00 60.02  ? 185 ARG A NE  1 
ATOM   1365 C CZ  . ARG A 1 185 ? -3.817  -14.484 29.584  1.00 64.92  ? 185 ARG A CZ  1 
ATOM   1366 N NH1 . ARG A 1 185 ? -4.901  -15.187 29.881  1.00 65.24  ? 185 ARG A NH1 1 
ATOM   1367 N NH2 . ARG A 1 185 ? -3.599  -13.328 30.207  1.00 61.86  ? 185 ARG A NH2 1 
ATOM   1368 N N   . MET A 1 186 ? -1.090  -14.032 23.091  1.00 34.65  ? 186 MET A N   1 
ATOM   1369 C CA  . MET A 1 186 ? -0.969  -12.797 22.292  1.00 32.58  ? 186 MET A CA  1 
ATOM   1370 C C   . MET A 1 186 ? -1.550  -11.617 23.075  1.00 34.23  ? 186 MET A C   1 
ATOM   1371 O O   . MET A 1 186 ? -1.068  -10.505 22.881  1.00 34.87  ? 186 MET A O   1 
ATOM   1372 C CB  . MET A 1 186 ? -1.712  -12.970 20.968  1.00 31.88  ? 186 MET A CB  1 
ATOM   1373 C CG  . MET A 1 186 ? -0.986  -13.863 19.996  1.00 36.20  ? 186 MET A CG  1 
ATOM   1374 S SD  . MET A 1 186 ? 0.577   -13.154 19.446  1.00 35.92  ? 186 MET A SD  1 
ATOM   1375 C CE  . MET A 1 186 ? 0.032   -12.236 18.008  1.00 33.45  ? 186 MET A CE  1 
ATOM   1376 N N   . GLU A 1 187 ? -2.543  -11.869 23.933  1.00 37.28  ? 187 GLU A N   1 
ATOM   1377 C CA  . GLU A 1 187 ? -3.170  -10.790 24.689  1.00 41.85  ? 187 GLU A CA  1 
ATOM   1378 C C   . GLU A 1 187 ? -2.144  -10.022 25.511  1.00 42.00  ? 187 GLU A C   1 
ATOM   1379 O O   . GLU A 1 187 ? -2.301  -8.817  25.742  1.00 38.36  ? 187 GLU A O   1 
ATOM   1380 C CB  . GLU A 1 187 ? -4.262  -11.385 25.579  1.00 47.00  ? 187 GLU A CB  1 
ATOM   1381 C CG  . GLU A 1 187 ? -4.571  -10.637 26.850  1.00 51.85  ? 187 GLU A CG  1 
ATOM   1382 C CD  . GLU A 1 187 ? -5.838  -11.148 27.514  1.00 58.92  ? 187 GLU A CD  1 
ATOM   1383 O OE1 . GLU A 1 187 ? -6.626  -11.843 26.839  1.00 63.22  ? 187 GLU A OE1 1 
ATOM   1384 O OE2 . GLU A 1 187 ? -6.034  -10.876 28.717  1.00 66.09  ? 187 GLU A OE2 1 
ATOM   1385 N N   . GLU A 1 188 ? -1.080  -10.700 25.933  1.00 35.94  ? 188 GLU A N   1 
ATOM   1386 C CA  . GLU A 1 188 ? 0.030   -10.097 26.657  1.00 38.69  ? 188 GLU A CA  1 
ATOM   1387 C C   . GLU A 1 188 ? 1.182   -9.713  25.740  1.00 36.06  ? 188 GLU A C   1 
ATOM   1388 O O   . GLU A 1 188 ? 1.799   -8.658  25.924  1.00 35.85  ? 188 GLU A O   1 
ATOM   1389 C CB  . GLU A 1 188 ? 0.528   -11.071 27.729  1.00 42.53  ? 188 GLU A CB  1 
ATOM   1390 C CG  . GLU A 1 188 ? 0.009   -10.729 29.099  1.00 51.83  ? 188 GLU A CG  1 
ATOM   1391 C CD  . GLU A 1 188 ? -1.415  -11.205 29.285  1.00 58.18  ? 188 GLU A CD  1 
ATOM   1392 O OE1 . GLU A 1 188 ? -1.706  -12.371 28.937  1.00 58.82  ? 188 GLU A OE1 1 
ATOM   1393 O OE2 . GLU A 1 188 ? -2.255  -10.398 29.742  1.00 64.86  ? 188 GLU A OE2 1 
ATOM   1394 N N   . TYR A 1 189 ? 1.466   -10.542 24.735  1.00 34.21  ? 189 TYR A N   1 
ATOM   1395 C CA  . TYR A 1 189 ? 2.571   -10.251 23.831  1.00 32.50  ? 189 TYR A CA  1 
ATOM   1396 C C   . TYR A 1 189 ? 2.307   -8.996  23.006  1.00 32.13  ? 189 TYR A C   1 
ATOM   1397 O O   . TYR A 1 189 ? 3.228   -8.190  22.794  1.00 32.88  ? 189 TYR A O   1 
ATOM   1398 C CB  . TYR A 1 189 ? 2.822   -11.444 22.906  1.00 29.89  ? 189 TYR A CB  1 
ATOM   1399 C CG  . TYR A 1 189 ? 3.916   -11.196 21.894  1.00 30.30  ? 189 TYR A CG  1 
ATOM   1400 C CD1 . TYR A 1 189 ? 5.242   -11.050 22.295  1.00 31.83  ? 189 TYR A CD1 1 
ATOM   1401 C CD2 . TYR A 1 189 ? 3.619   -11.056 20.534  1.00 28.96  ? 189 TYR A CD2 1 
ATOM   1402 C CE1 . TYR A 1 189 ? 6.253   -10.817 21.370  1.00 33.22  ? 189 TYR A CE1 1 
ATOM   1403 C CE2 . TYR A 1 189 ? 4.626   -10.823 19.606  1.00 29.07  ? 189 TYR A CE2 1 
ATOM   1404 C CZ  . TYR A 1 189 ? 5.932   -10.709 20.021  1.00 28.90  ? 189 TYR A CZ  1 
ATOM   1405 O OH  . TYR A 1 189 ? 6.931   -10.481 19.098  1.00 31.58  ? 189 TYR A OH  1 
ATOM   1406 N N   . MET A 1 190 ? 1.072   -8.807  22.509  1.00 32.15  ? 190 MET A N   1 
ATOM   1407 C CA  . MET A 1 190 ? 0.900   -7.710  21.554  1.00 28.99  ? 190 MET A CA  1 
ATOM   1408 C C   . MET A 1 190 ? 1.139   -6.325  22.150  1.00 32.67  ? 190 MET A C   1 
ATOM   1409 O O   . MET A 1 190 ? 1.829   -5.523  21.498  1.00 32.34  ? 190 MET A O   1 
ATOM   1410 C CB  . MET A 1 190 ? -0.447  -7.723  20.809  1.00 32.46  ? 190 MET A CB  1 
ATOM   1411 C CG  . MET A 1 190 ? -0.582  -8.762  19.681  1.00 36.02  ? 190 MET A CG  1 
ATOM   1412 S SD  . MET A 1 190 ? -2.254  -9.390  19.359  1.00 35.42  ? 190 MET A SD  1 
ATOM   1413 C CE  . MET A 1 190 ? -2.889  -7.930  18.523  1.00 37.82  ? 190 MET A CE  1 
ATOM   1414 N N   . PRO A 1 191 ? 0.627   -5.962  23.337  1.00 35.48  ? 191 PRO A N   1 
ATOM   1415 C CA  . PRO A 1 191 ? 0.964   -4.619  23.860  1.00 35.33  ? 191 PRO A CA  1 
ATOM   1416 C C   . PRO A 1 191 ? 2.453   -4.448  24.093  1.00 34.83  ? 191 PRO A C   1 
ATOM   1417 O O   . PRO A 1 191 ? 3.005   -3.373  23.831  1.00 35.63  ? 191 PRO A O   1 
ATOM   1418 C CB  . PRO A 1 191 ? 0.167   -4.532  25.167  1.00 36.39  ? 191 PRO A CB  1 
ATOM   1419 C CG  . PRO A 1 191 ? -0.919  -5.565  25.023  1.00 36.47  ? 191 PRO A CG  1 
ATOM   1420 C CD  . PRO A 1 191 ? -0.302  -6.676  24.237  1.00 36.45  ? 191 PRO A CD  1 
ATOM   1421 N N   . TYR A 1 192 ? 3.122   -5.496  24.571  1.00 31.08  ? 192 TYR A N   1 
ATOM   1422 C CA  . TYR A 1 192 ? 4.571   -5.454  24.715  1.00 32.50  ? 192 TYR A CA  1 
ATOM   1423 C C   . TYR A 1 192 ? 5.241   -5.235  23.365  1.00 32.26  ? 192 TYR A C   1 
ATOM   1424 O O   . TYR A 1 192 ? 6.186   -4.447  23.247  1.00 30.02  ? 192 TYR A O   1 
ATOM   1425 C CB  . TYR A 1 192 ? 5.059   -6.755  25.350  1.00 32.13  ? 192 TYR A CB  1 
ATOM   1426 C CG  . TYR A 1 192 ? 6.512   -7.025  25.109  1.00 32.13  ? 192 TYR A CG  1 
ATOM   1427 C CD1 . TYR A 1 192 ? 7.488   -6.384  25.865  1.00 39.43  ? 192 TYR A CD1 1 
ATOM   1428 C CD2 . TYR A 1 192 ? 6.918   -7.863  24.081  1.00 35.79  ? 192 TYR A CD2 1 
ATOM   1429 C CE1 . TYR A 1 192 ? 8.831   -6.618  25.640  1.00 39.77  ? 192 TYR A CE1 1 
ATOM   1430 C CE2 . TYR A 1 192 ? 8.262   -8.097  23.845  1.00 38.80  ? 192 TYR A CE2 1 
ATOM   1431 C CZ  . TYR A 1 192 ? 9.209   -7.469  24.633  1.00 36.92  ? 192 TYR A CZ  1 
ATOM   1432 O OH  . TYR A 1 192 ? 10.547  -7.689  24.411  1.00 48.53  ? 192 TYR A OH  1 
ATOM   1433 N N   . ARG A 1 193 ? 4.744   -5.899  22.319  1.00 30.65  ? 193 ARG A N   1 
ATOM   1434 C CA  . ARG A 1 193 ? 5.465   -5.842  21.057  1.00 29.39  ? 193 ARG A CA  1 
ATOM   1435 C C   . ARG A 1 193 ? 5.307   -4.480  20.379  1.00 28.71  ? 193 ARG A C   1 
ATOM   1436 O O   . ARG A 1 193 ? 6.232   -4.045  19.688  1.00 28.25  ? 193 ARG A O   1 
ATOM   1437 C CB  . ARG A 1 193 ? 5.015   -6.986  20.135  1.00 28.97  ? 193 ARG A CB  1 
ATOM   1438 C CG  . ARG A 1 193 ? 5.733   -7.021  18.800  1.00 31.28  ? 193 ARG A CG  1 
ATOM   1439 C CD  . ARG A 1 193 ? 7.246   -7.188  18.963  1.00 32.03  ? 193 ARG A CD  1 
ATOM   1440 N NE  . ARG A 1 193 ? 7.878   -7.402  17.667  1.00 32.44  ? 193 ARG A NE  1 
ATOM   1441 C CZ  . ARG A 1 193 ? 9.028   -6.878  17.267  1.00 35.48  ? 193 ARG A CZ  1 
ATOM   1442 N NH1 . ARG A 1 193 ? 9.789   -6.150  18.080  1.00 32.49  ? 193 ARG A NH1 1 
ATOM   1443 N NH2 . ARG A 1 193 ? 9.418   -7.068  16.008  1.00 34.23  ? 193 ARG A NH2 1 
ATOM   1444 N N   . ILE A 1 194 ? 4.170   -3.791  20.558  1.00 27.83  ? 194 ILE A N   1 
ATOM   1445 C CA  . ILE A 1 194 ? 4.047   -2.442  19.999  1.00 29.30  ? 194 ILE A CA  1 
ATOM   1446 C C   . ILE A 1 194 ? 5.170   -1.553  20.507  1.00 31.11  ? 194 ILE A C   1 
ATOM   1447 O O   . ILE A 1 194 ? 5.788   -0.798  19.742  1.00 29.82  ? 194 ILE A O   1 
ATOM   1448 C CB  . ILE A 1 194 ? 2.680   -1.808  20.313  1.00 30.79  ? 194 ILE A CB  1 
ATOM   1449 C CG1 . ILE A 1 194 ? 1.523   -2.619  19.738  1.00 31.89  ? 194 ILE A CG1 1 
ATOM   1450 C CG2 . ILE A 1 194 ? 2.626   -0.382  19.751  1.00 29.97  ? 194 ILE A CG2 1 
ATOM   1451 C CD1 . ILE A 1 194 ? 0.175   -2.012  20.115  1.00 35.48  ? 194 ILE A CD1 1 
ATOM   1452 N N   . ALA A 1 195 ? 5.452   -1.625  21.806  1.00 30.05  ? 195 ALA A N   1 
ATOM   1453 C CA  . ALA A 1 195 ? 6.519   -0.796  22.356  1.00 31.76  ? 195 ALA A CA  1 
ATOM   1454 C C   . ALA A 1 195 ? 7.877   -1.333  21.940  1.00 29.34  ? 195 ALA A C   1 
ATOM   1455 O O   . ALA A 1 195 ? 8.767   -0.569  21.561  1.00 27.77  ? 195 ALA A O   1 
ATOM   1456 C CB  . ALA A 1 195 ? 6.393   -0.734  23.875  1.00 33.26  ? 195 ALA A CB  1 
ATOM   1457 N N   . ASN A 1 196 ? 8.034   -2.663  21.944  1.00 27.65  ? 196 ASN A N   1 
ATOM   1458 C CA  . ASN A 1 196 ? 9.349   -3.241  21.707  1.00 28.74  ? 196 ASN A CA  1 
ATOM   1459 C C   . ASN A 1 196 ? 9.828   -3.019  20.275  1.00 28.38  ? 196 ASN A C   1 
ATOM   1460 O O   . ASN A 1 196 ? 11.034  -2.893  20.039  1.00 31.74  ? 196 ASN A O   1 
ATOM   1461 C CB  . ASN A 1 196 ? 9.315   -4.734  22.035  1.00 30.19  ? 196 ASN A CB  1 
ATOM   1462 C CG  . ASN A 1 196 ? 10.614  -5.418  21.710  1.00 36.04  ? 196 ASN A CG  1 
ATOM   1463 O OD1 . ASN A 1 196 ? 10.744  -6.051  20.668  1.00 34.59  ? 196 ASN A OD1 1 
ATOM   1464 N ND2 . ASN A 1 196 ? 11.588  -5.309  22.618  1.00 33.21  ? 196 ASN A ND2 1 
ATOM   1465 N N   . CYS A 1 197 ? 8.917   -2.966  19.304  1.00 28.21  ? 197 CYS A N   1 
ATOM   1466 C CA  . CYS A 1 197 ? 9.326   -2.709  17.930  1.00 32.07  ? 197 CYS A CA  1 
ATOM   1467 C C   . CYS A 1 197 ? 9.631   -1.242  17.686  1.00 30.68  ? 197 CYS A C   1 
ATOM   1468 O O   . CYS A 1 197 ? 10.046  -0.883  16.574  1.00 31.45  ? 197 CYS A O   1 
ATOM   1469 C CB  . CYS A 1 197 ? 8.248   -3.186  16.947  1.00 31.43  ? 197 CYS A CB  1 
ATOM   1470 S SG  . CYS A 1 197 ? 6.735   -2.175  16.840  1.00 31.05  ? 197 CYS A SG  1 
ATOM   1471 N N   . GLY A 1 198 ? 9.420   -0.399  18.687  1.00 28.34  ? 198 GLY A N   1 
ATOM   1472 C CA  . GLY A 1 198 ? 9.698   1.015   18.567  1.00 28.04  ? 198 GLY A CA  1 
ATOM   1473 C C   . GLY A 1 198 ? 8.562   1.853   18.025  1.00 28.97  ? 198 GLY A C   1 
ATOM   1474 O O   . GLY A 1 198 ? 8.796   3.020   17.670  1.00 28.62  ? 198 GLY A O   1 
ATOM   1475 N N   . TYR A 1 199 ? 7.338   1.312   17.964  1.00 27.11  ? 199 TYR A N   1 
ATOM   1476 C CA  . TYR A 1 199 ? 6.252   2.024   17.289  1.00 26.27  ? 199 TYR A CA  1 
ATOM   1477 C C   . TYR A 1 199 ? 5.949   3.370   17.941  1.00 26.53  ? 199 TYR A C   1 
ATOM   1478 O O   . TYR A 1 199 ? 5.639   4.340   17.243  1.00 27.39  ? 199 TYR A O   1 
ATOM   1479 C CB  . TYR A 1 199 ? 4.982   1.176   17.253  1.00 27.56  ? 199 TYR A CB  1 
ATOM   1480 C CG  . TYR A 1 199 ? 3.823   1.893   16.596  1.00 28.18  ? 199 TYR A CG  1 
ATOM   1481 C CD1 . TYR A 1 199 ? 3.724   1.960   15.209  1.00 29.25  ? 199 TYR A CD1 1 
ATOM   1482 C CD2 . TYR A 1 199 ? 2.819   2.497   17.361  1.00 27.19  ? 199 TYR A CD2 1 
ATOM   1483 C CE1 . TYR A 1 199 ? 2.664   2.617   14.595  1.00 27.68  ? 199 TYR A CE1 1 
ATOM   1484 C CE2 . TYR A 1 199 ? 1.744   3.167   16.740  1.00 28.84  ? 199 TYR A CE2 1 
ATOM   1485 C CZ  . TYR A 1 199 ? 1.681   3.209   15.364  1.00 28.74  ? 199 TYR A CZ  1 
ATOM   1486 O OH  . TYR A 1 199 ? 0.638   3.852   14.737  1.00 29.95  ? 199 TYR A OH  1 
ATOM   1487 N N   . TRP A 1 200 ? 6.025   3.455   19.276  1.00 27.05  ? 200 TRP A N   1 
ATOM   1488 C CA  . TRP A 1 200 ? 5.699   4.731   19.915  1.00 30.56  ? 200 TRP A CA  1 
ATOM   1489 C C   . TRP A 1 200 ? 6.750   5.786   19.606  1.00 30.13  ? 200 TRP A C   1 
ATOM   1490 O O   . TRP A 1 200 ? 6.420   6.977   19.496  1.00 29.02  ? 200 TRP A O   1 
ATOM   1491 C CB  . TRP A 1 200 ? 5.533   4.559   21.428  1.00 28.99  ? 200 TRP A CB  1 
ATOM   1492 C CG  . TRP A 1 200 ? 4.460   3.572   21.795  1.00 29.28  ? 200 TRP A CG  1 
ATOM   1493 C CD1 . TRP A 1 200 ? 4.610   2.459   22.573  1.00 31.05  ? 200 TRP A CD1 1 
ATOM   1494 C CD2 . TRP A 1 200 ? 3.078   3.585   21.383  1.00 29.86  ? 200 TRP A CD2 1 
ATOM   1495 N NE1 . TRP A 1 200 ? 3.414   1.783   22.675  1.00 31.85  ? 200 TRP A NE1 1 
ATOM   1496 C CE2 . TRP A 1 200 ? 2.459   2.452   21.958  1.00 32.67  ? 200 TRP A CE2 1 
ATOM   1497 C CE3 . TRP A 1 200 ? 2.305   4.440   20.586  1.00 29.92  ? 200 TRP A CE3 1 
ATOM   1498 C CZ2 . TRP A 1 200 ? 1.102   2.157   21.760  1.00 32.36  ? 200 TRP A CZ2 1 
ATOM   1499 C CZ3 . TRP A 1 200 ? 0.960   4.143   20.392  1.00 31.76  ? 200 TRP A CZ3 1 
ATOM   1500 C CH2 . TRP A 1 200 ? 0.373   3.017   20.977  1.00 34.71  ? 200 TRP A CH2 1 
ATOM   1501 N N   . MET A 1 201 ? 8.003   5.375   19.418  1.00 27.29  ? 201 MET A N   1 
ATOM   1502 C CA  . MET A 1 201 ? 9.020   6.325   18.989  1.00 25.93  ? 201 MET A CA  1 
ATOM   1503 C C   . MET A 1 201 ? 8.880   6.659   17.509  1.00 27.03  ? 201 MET A C   1 
ATOM   1504 O O   . MET A 1 201 ? 8.951   7.830   17.122  1.00 26.86  ? 201 MET A O   1 
ATOM   1505 C CB  . MET A 1 201 ? 10.414  5.789   19.304  1.00 29.03  ? 201 MET A CB  1 
ATOM   1506 C CG  . MET A 1 201 ? 11.542  6.333   18.434  1.00 25.75  ? 201 MET A CG  1 
ATOM   1507 S SD  . MET A 1 201 ? 13.141  5.817   19.120  1.00 28.39  ? 201 MET A SD  1 
ATOM   1508 C CE  . MET A 1 201 ? 13.288  4.195   18.330  1.00 28.73  ? 201 MET A CE  1 
ATOM   1509 N N   . SER A 1 202 ? 8.664   5.645   16.666  1.00 27.48  ? 202 SER A N   1 
ATOM   1510 C CA  . SER A 1 202 ? 8.532   5.897   15.236  1.00 27.90  ? 202 SER A CA  1 
ATOM   1511 C C   . SER A 1 202 ? 7.300   6.736   14.921  1.00 26.59  ? 202 SER A C   1 
ATOM   1512 O O   . SER A 1 202 ? 7.371   7.672   14.110  1.00 27.08  ? 202 SER A O   1 
ATOM   1513 C CB  . SER A 1 202 ? 8.483   4.566   14.491  1.00 30.15  ? 202 SER A CB  1 
ATOM   1514 O OG  . SER A 1 202 ? 9.723   3.889   14.644  1.00 28.01  ? 202 SER A OG  1 
ATOM   1515 N N   . SER A 1 203 ? 6.159   6.433   15.560  1.00 27.23  ? 203 SER A N   1 
ATOM   1516 C CA  . SER A 1 203 ? 4.955   7.219   15.286  1.00 28.66  ? 203 SER A CA  1 
ATOM   1517 C C   . SER A 1 203 ? 5.071   8.623   15.858  1.00 27.73  ? 203 SER A C   1 
ATOM   1518 O O   . SER A 1 203 ? 4.519   9.564   15.280  1.00 27.08  ? 203 SER A O   1 
ATOM   1519 C CB  . SER A 1 203 ? 3.701   6.519   15.831  1.00 30.27  ? 203 SER A CB  1 
ATOM   1520 O OG  . SER A 1 203 ? 3.791   6.309   17.232  1.00 27.96  ? 203 SER A OG  1 
ATOM   1521 N N   . TYR A 1 204 ? 5.803   8.800   16.961  1.00 25.33  ? 204 TYR A N   1 
ATOM   1522 C CA  . TYR A 1 204 ? 6.114   10.163  17.394  1.00 26.69  ? 204 TYR A CA  1 
ATOM   1523 C C   . TYR A 1 204 ? 6.836   10.912  16.285  1.00 28.01  ? 204 TYR A C   1 
ATOM   1524 O O   . TYR A 1 204 ? 6.490   12.053  15.948  1.00 27.95  ? 204 TYR A O   1 
ATOM   1525 C CB  . TYR A 1 204 ? 6.970   10.150  18.673  1.00 25.40  ? 204 TYR A CB  1 
ATOM   1526 C CG  . TYR A 1 204 ? 7.366   11.570  19.060  1.00 27.38  ? 204 TYR A CG  1 
ATOM   1527 C CD1 . TYR A 1 204 ? 8.503   12.174  18.516  1.00 26.41  ? 204 TYR A CD1 1 
ATOM   1528 C CD2 . TYR A 1 204 ? 6.553   12.333  19.882  1.00 31.86  ? 204 TYR A CD2 1 
ATOM   1529 C CE1 . TYR A 1 204 ? 8.842   13.500  18.816  1.00 25.75  ? 204 TYR A CE1 1 
ATOM   1530 C CE2 . TYR A 1 204 ? 6.896   13.664  20.200  1.00 29.60  ? 204 TYR A CE2 1 
ATOM   1531 C CZ  . TYR A 1 204 ? 8.031   14.233  19.653  1.00 28.57  ? 204 TYR A CZ  1 
ATOM   1532 O OH  . TYR A 1 204 ? 8.374   15.551  19.955  1.00 29.43  ? 204 TYR A OH  1 
ATOM   1533 N N   . PHE A 1 205 ? 7.846   10.282  15.692  1.00 24.56  ? 205 PHE A N   1 
ATOM   1534 C CA  . PHE A 1 205 ? 8.631   10.978  14.682  1.00 25.14  ? 205 PHE A CA  1 
ATOM   1535 C C   . PHE A 1 205 ? 7.866   11.113  13.370  1.00 26.58  ? 205 PHE A C   1 
ATOM   1536 O O   . PHE A 1 205 ? 8.210   11.973  12.554  1.00 27.38  ? 205 PHE A O   1 
ATOM   1537 C CB  . PHE A 1 205 ? 9.967   10.248  14.500  1.00 24.93  ? 205 PHE A CB  1 
ATOM   1538 C CG  . PHE A 1 205 ? 11.016  10.660  15.505  1.00 28.14  ? 205 PHE A CG  1 
ATOM   1539 C CD1 . PHE A 1 205 ? 11.280  12.008  15.744  1.00 28.67  ? 205 PHE A CD1 1 
ATOM   1540 C CD2 . PHE A 1 205 ? 11.681  9.697   16.262  1.00 26.90  ? 205 PHE A CD2 1 
ATOM   1541 C CE1 . PHE A 1 205 ? 12.245  12.388  16.697  1.00 28.18  ? 205 PHE A CE1 1 
ATOM   1542 C CE2 . PHE A 1 205 ? 12.641  10.056  17.214  1.00 27.52  ? 205 PHE A CE2 1 
ATOM   1543 C CZ  . PHE A 1 205 ? 12.927  11.408  17.428  1.00 28.04  ? 205 PHE A CZ  1 
ATOM   1544 N N   . ILE A 1 206 ? 6.812   10.324  13.174  1.00 24.76  ? 206 ILE A N   1 
ATOM   1545 C CA  . ILE A 1 206 ? 5.929   10.578  12.034  1.00 25.51  ? 206 ILE A CA  1 
ATOM   1546 C C   . ILE A 1 206 ? 5.302   11.957  12.161  1.00 28.14  ? 206 ILE A C   1 
ATOM   1547 O O   . ILE A 1 206 ? 5.239   12.724  11.187  1.00 29.21  ? 206 ILE A O   1 
ATOM   1548 C CB  . ILE A 1 206 ? 4.860   9.481   11.919  1.00 25.98  ? 206 ILE A CB  1 
ATOM   1549 C CG1 . ILE A 1 206 ? 5.498   8.215   11.340  1.00 27.78  ? 206 ILE A CG1 1 
ATOM   1550 C CG2 . ILE A 1 206 ? 3.671   9.967   11.058  1.00 27.13  ? 206 ILE A CG2 1 
ATOM   1551 C CD1 . ILE A 1 206 ? 5.820   8.305   9.852   1.00 28.49  ? 206 ILE A CD1 1 
ATOM   1552 N N   . ARG A 1 207 ? 4.818   12.289  13.356  1.00 27.87  ? 207 ARG A N   1 
ATOM   1553 C CA  . ARG A 1 207 ? 4.241   13.612  13.581  1.00 27.90  ? 207 ARG A CA  1 
ATOM   1554 C C   . ARG A 1 207 ? 5.326   14.679  13.557  1.00 27.12  ? 207 ARG A C   1 
ATOM   1555 O O   . ARG A 1 207 ? 5.202   15.701  12.873  1.00 27.39  ? 207 ARG A O   1 
ATOM   1556 C CB  . ARG A 1 207 ? 3.495   13.624  14.916  1.00 29.55  ? 207 ARG A CB  1 
ATOM   1557 C CG  . ARG A 1 207 ? 2.404   12.534  15.030  1.00 29.27  ? 207 ARG A CG  1 
ATOM   1558 C CD  . ARG A 1 207 ? 1.531   12.776  16.257  1.00 33.83  ? 207 ARG A CD  1 
ATOM   1559 N NE  . ARG A 1 207 ? 2.168   12.286  17.480  1.00 32.09  ? 207 ARG A NE  1 
ATOM   1560 C CZ  . ARG A 1 207 ? 2.196   11.022  17.885  1.00 32.03  ? 207 ARG A CZ  1 
ATOM   1561 N NH1 . ARG A 1 207 ? 1.631   10.057  17.183  1.00 30.86  ? 207 ARG A NH1 1 
ATOM   1562 N NH2 . ARG A 1 207 ? 2.809   10.720  19.030  1.00 34.68  ? 207 ARG A NH2 1 
ATOM   1563 N N   . TRP A 1 208 ? 6.405   14.454  14.310  1.00 26.77  ? 208 TRP A N   1 
ATOM   1564 C CA  . TRP A 1 208 ? 7.486   15.433  14.400  1.00 28.57  ? 208 TRP A CA  1 
ATOM   1565 C C   . TRP A 1 208 ? 8.074   15.746  13.035  1.00 29.30  ? 208 TRP A C   1 
ATOM   1566 O O   . TRP A 1 208 ? 8.353   16.911  12.721  1.00 28.10  ? 208 TRP A O   1 
ATOM   1567 C CB  . TRP A 1 208 ? 8.565   14.880  15.336  1.00 27.03  ? 208 TRP A CB  1 
ATOM   1568 C CG  . TRP A 1 208 ? 9.721   15.783  15.699  1.00 27.05  ? 208 TRP A CG  1 
ATOM   1569 C CD1 . TRP A 1 208 ? 9.815   16.630  16.775  1.00 26.64  ? 208 TRP A CD1 1 
ATOM   1570 C CD2 . TRP A 1 208 ? 10.967  15.892  14.991  1.00 26.54  ? 208 TRP A CD2 1 
ATOM   1571 N NE1 . TRP A 1 208 ? 11.045  17.245  16.780  1.00 27.36  ? 208 TRP A NE1 1 
ATOM   1572 C CE2 . TRP A 1 208 ? 11.769  16.821  15.696  1.00 28.03  ? 208 TRP A CE2 1 
ATOM   1573 C CE3 . TRP A 1 208 ? 11.484  15.288  13.831  1.00 28.70  ? 208 TRP A CE3 1 
ATOM   1574 C CZ2 . TRP A 1 208 ? 13.054  17.170  15.278  1.00 26.96  ? 208 TRP A CZ2 1 
ATOM   1575 C CZ3 . TRP A 1 208 ? 12.772  15.636  13.416  1.00 27.78  ? 208 TRP A CZ3 1 
ATOM   1576 C CH2 . TRP A 1 208 ? 13.544  16.570  14.148  1.00 27.52  ? 208 TRP A CH2 1 
ATOM   1577 N N   . GLY A 1 209 ? 8.263   14.722  12.200  1.00 29.42  ? 209 GLY A N   1 
ATOM   1578 C CA  . GLY A 1 209 ? 8.823   14.957  10.879  1.00 27.95  ? 209 GLY A CA  1 
ATOM   1579 C C   . GLY A 1 209 ? 7.944   15.814  9.980   1.00 31.06  ? 209 GLY A C   1 
ATOM   1580 O O   . GLY A 1 209 ? 8.445   16.393  9.017   1.00 29.48  ? 209 GLY A O   1 
ATOM   1581 N N   . MET A 1 210 ? 6.654   15.929  10.297  1.00 27.49  ? 210 MET A N   1 
ATOM   1582 C CA  . MET A 1 210 ? 5.706   16.725  9.534   1.00 27.82  ? 210 MET A CA  1 
ATOM   1583 C C   . MET A 1 210 ? 5.546   18.106  10.159  1.00 28.65  ? 210 MET A C   1 
ATOM   1584 O O   . MET A 1 210 ? 4.707   18.888  9.704   1.00 30.73  ? 210 MET A O   1 
ATOM   1585 C CB  . MET A 1 210 ? 4.370   15.991  9.538   1.00 29.87  ? 210 MET A CB  1 
ATOM   1586 C CG  . MET A 1 210 ? 4.324   14.856  8.535   1.00 32.22  ? 210 MET A CG  1 
ATOM   1587 S SD  . MET A 1 210 ? 2.686   14.330  8.079   1.00 32.03  ? 210 MET A SD  1 
ATOM   1588 C CE  . MET A 1 210 ? 2.224   13.624  9.669   1.00 34.07  ? 210 MET A CE  1 
ATOM   1589 N N   . ASP A 1 211 ? 6.293   18.393  11.237  1.00 29.97  ? 211 ASP A N   1 
ATOM   1590 C CA  . ASP A 1 211 ? 6.197   19.658  11.975  1.00 33.82  ? 211 ASP A CA  1 
ATOM   1591 C C   . ASP A 1 211 ? 4.774   19.886  12.478  1.00 35.89  ? 211 ASP A C   1 
ATOM   1592 O O   . ASP A 1 211 ? 4.177   20.949  12.282  1.00 34.73  ? 211 ASP A O   1 
ATOM   1593 C CB  . ASP A 1 211 ? 6.681   20.840  11.125  1.00 34.81  ? 211 ASP A CB  1 
ATOM   1594 C CG  . ASP A 1 211 ? 6.851   22.129  11.937  1.00 42.02  ? 211 ASP A CG  1 
ATOM   1595 O OD1 . ASP A 1 211 ? 6.893   22.059  13.187  1.00 40.29  ? 211 ASP A OD1 1 
ATOM   1596 O OD2 . ASP A 1 211 ? 6.910   23.216  11.310  1.00 44.42  ? 211 ASP A OD2 1 
ATOM   1597 N N   . MET A 1 212 ? 4.228   18.869  13.135  1.00 32.76  ? 212 MET A N   1 
ATOM   1598 C CA  . MET A 1 212 ? 2.856   18.915  13.611  1.00 35.33  ? 212 MET A CA  1 
ATOM   1599 C C   . MET A 1 212 ? 2.735   18.125  14.898  1.00 35.95  ? 212 MET A C   1 
ATOM   1600 O O   . MET A 1 212 ? 3.604   17.320  15.237  1.00 33.42  ? 212 MET A O   1 
ATOM   1601 C CB  . MET A 1 212 ? 1.892   18.399  12.534  1.00 34.07  ? 212 MET A CB  1 
ATOM   1602 C CG  . MET A 1 212 ? 2.092   16.914  12.236  1.00 35.08  ? 212 MET A CG  1 
ATOM   1603 S SD  . MET A 1 212 ? 1.201   15.749  13.272  1.00 37.89  ? 212 MET A SD  1 
ATOM   1604 C CE  . MET A 1 212 ? -0.480  16.035  12.729  1.00 39.50  ? 212 MET A CE  1 
ATOM   1605 N N   . THR A 1 213 ? 1.653   18.384  15.630  1.00 35.49  ? 213 THR A N   1 
ATOM   1606 C CA  . THR A 1 213 ? 1.303   17.600  16.806  1.00 37.18  ? 213 THR A CA  1 
ATOM   1607 C C   . THR A 1 213 ? -0.195  17.342  16.794  1.00 37.16  ? 213 THR A C   1 
ATOM   1608 O O   . THR A 1 213 ? -0.955  17.998  16.083  1.00 40.24  ? 213 THR A O   1 
ATOM   1609 C CB  . THR A 1 213 ? 1.696   18.286  18.135  1.00 41.16  ? 213 THR A CB  1 
ATOM   1610 O OG1 . THR A 1 213 ? 0.939   19.493  18.308  1.00 41.89  ? 213 THR A OG1 1 
ATOM   1611 C CG2 . THR A 1 213 ? 3.181   18.601  18.184  1.00 39.92  ? 213 THR A CG2 1 
ATOM   1612 N N   . LEU A 1 214 ? -0.610  16.367  17.587  1.00 37.08  ? 214 LEU A N   1 
ATOM   1613 C CA  . LEU A 1 214 ? -2.015  16.170  17.896  1.00 40.52  ? 214 LEU A CA  1 
ATOM   1614 C C   . LEU A 1 214 ? -2.271  16.661  19.312  1.00 42.60  ? 214 LEU A C   1 
ATOM   1615 O O   . LEU A 1 214 ? -1.429  16.487  20.202  1.00 45.37  ? 214 LEU A O   1 
ATOM   1616 C CB  . LEU A 1 214 ? -2.429  14.700  17.768  1.00 39.46  ? 214 LEU A CB  1 
ATOM   1617 C CG  . LEU A 1 214 ? -2.353  14.089  16.371  1.00 38.02  ? 214 LEU A CG  1 
ATOM   1618 C CD1 . LEU A 1 214 ? -2.534  12.567  16.469  1.00 37.43  ? 214 LEU A CD1 1 
ATOM   1619 C CD2 . LEU A 1 214 ? -3.405  14.702  15.450  1.00 37.04  ? 214 LEU A CD2 1 
ATOM   1620 N N   . SER A 1 215 ? -3.426  17.286  19.511  1.00 40.85  ? 215 SER A N   1 
ATOM   1621 C CA  . SER A 1 215 ? -3.837  17.660  20.853  1.00 45.73  ? 215 SER A CA  1 
ATOM   1622 C C   . SER A 1 215 ? -4.164  16.416  21.672  1.00 47.70  ? 215 SER A C   1 
ATOM   1623 O O   . SER A 1 215 ? -4.301  15.308  21.145  1.00 44.66  ? 215 SER A O   1 
ATOM   1624 C CB  . SER A 1 215 ? -5.042  18.597  20.796  1.00 46.39  ? 215 SER A CB  1 
ATOM   1625 O OG  . SER A 1 215 ? -6.257  17.863  20.790  1.00 48.60  ? 215 SER A OG  1 
ATOM   1626 N N   . GLU A 1 216 ? -4.281  16.611  22.985  1.00 48.45  ? 216 GLU A N   1 
ATOM   1627 C CA  . GLU A 1 216 ? -4.665  15.511  23.864  1.00 47.55  ? 216 GLU A CA  1 
ATOM   1628 C C   . GLU A 1 216 ? -6.008  14.923  23.455  1.00 47.59  ? 216 GLU A C   1 
ATOM   1629 O O   . GLU A 1 216 ? -6.189  13.697  23.467  1.00 49.05  ? 216 GLU A O   1 
ATOM   1630 C CB  . GLU A 1 216 ? -4.724  16.000  25.309  1.00 51.93  ? 216 GLU A CB  1 
ATOM   1631 C CG  . GLU A 1 216 ? -4.656  14.908  26.353  1.00 55.96  ? 216 GLU A CG  1 
ATOM   1632 C CD  . GLU A 1 216 ? -3.735  15.278  27.499  1.00 63.86  ? 216 GLU A CD  1 
ATOM   1633 O OE1 . GLU A 1 216 ? -2.668  14.639  27.652  1.00 66.89  ? 216 GLU A OE1 1 
ATOM   1634 O OE2 . GLU A 1 216 ? -4.078  16.226  28.238  1.00 67.05  ? 216 GLU A OE2 1 
ATOM   1635 N N   . GLU A 1 217 ? -6.965  15.786  23.100  1.00 45.77  ? 217 GLU A N   1 
ATOM   1636 C CA  . GLU A 1 217 ? -8.276  15.316  22.666  1.00 48.08  ? 217 GLU A CA  1 
ATOM   1637 C C   . GLU A 1 217 ? -8.191  14.625  21.311  1.00 45.30  ? 217 GLU A C   1 
ATOM   1638 O O   . GLU A 1 217 ? -8.836  13.593  21.093  1.00 44.93  ? 217 GLU A O   1 
ATOM   1639 C CB  . GLU A 1 217 ? -9.263  16.487  22.615  1.00 49.50  ? 217 GLU A CB  1 
ATOM   1640 C CG  . GLU A 1 217 ? -10.668 16.099  22.175  1.00 55.74  ? 217 GLU A CG  1 
ATOM   1641 C CD  . GLU A 1 217 ? -11.653 17.258  22.236  1.00 58.45  ? 217 GLU A CD  1 
ATOM   1642 O OE1 . GLU A 1 217 ? -11.208 18.424  22.261  1.00 58.10  ? 217 GLU A OE1 1 
ATOM   1643 O OE2 . GLU A 1 217 ? -12.875 16.999  22.245  1.00 62.78  ? 217 GLU A OE2 1 
ATOM   1644 N N   . GLU A 1 218 ? -7.390  15.176  20.396  1.00 43.76  ? 218 GLU A N   1 
ATOM   1645 C CA  . GLU A 1 218 ? -7.227  14.571  19.077  1.00 42.99  ? 218 GLU A CA  1 
ATOM   1646 C C   . GLU A 1 218 ? -6.584  13.192  19.183  1.00 39.31  ? 218 GLU A C   1 
ATOM   1647 O O   . GLU A 1 218 ? -7.045  12.230  18.555  1.00 41.73  ? 218 GLU A O   1 
ATOM   1648 C CB  . GLU A 1 218 ? -6.379  15.480  18.186  1.00 41.44  ? 218 GLU A CB  1 
ATOM   1649 C CG  . GLU A 1 218 ? -7.151  16.529  17.411  1.00 45.12  ? 218 GLU A CG  1 
ATOM   1650 C CD  . GLU A 1 218 ? -6.257  17.649  16.913  1.00 44.18  ? 218 GLU A CD  1 
ATOM   1651 O OE1 . GLU A 1 218 ? -5.095  17.732  17.370  1.00 45.88  ? 218 GLU A OE1 1 
ATOM   1652 O OE2 . GLU A 1 218 ? -6.703  18.425  16.042  1.00 49.48  ? 218 GLU A OE2 1 
ATOM   1653 N N   . TYR A 1 219 ? -5.504  13.074  19.967  1.00 37.81  ? 219 TYR A N   1 
ATOM   1654 C CA  . TYR A 1 219 ? -4.857  11.769  20.084  1.00 38.40  ? 219 TYR A CA  1 
ATOM   1655 C C   . TYR A 1 219 ? -5.795  10.750  20.718  1.00 44.68  ? 219 TYR A C   1 
ATOM   1656 O O   . TYR A 1 219 ? -5.888  9.607   20.250  1.00 42.66  ? 219 TYR A O   1 
ATOM   1657 C CB  . TYR A 1 219 ? -3.553  11.825  20.890  1.00 41.05  ? 219 TYR A CB  1 
ATOM   1658 C CG  . TYR A 1 219 ? -2.980  10.428  20.902  1.00 41.75  ? 219 TYR A CG  1 
ATOM   1659 C CD1 . TYR A 1 219 ? -2.332  9.930   19.779  1.00 44.70  ? 219 TYR A CD1 1 
ATOM   1660 C CD2 . TYR A 1 219 ? -3.216  9.556   21.964  1.00 41.63  ? 219 TYR A CD2 1 
ATOM   1661 C CE1 . TYR A 1 219 ? -1.865  8.624   19.738  1.00 38.76  ? 219 TYR A CE1 1 
ATOM   1662 C CE2 . TYR A 1 219 ? -2.755  8.243   21.932  1.00 41.39  ? 219 TYR A CE2 1 
ATOM   1663 C CZ  . TYR A 1 219 ? -2.081  7.791   20.812  1.00 37.99  ? 219 TYR A CZ  1 
ATOM   1664 O OH  . TYR A 1 219 ? -1.611  6.502   20.756  1.00 41.24  ? 219 TYR A OH  1 
ATOM   1665 N N   . ALA A 1 220 ? -6.484  11.139  21.795  1.00 41.71  ? 220 ALA A N   1 
ATOM   1666 C CA  . ALA A 1 220 ? -7.441  10.239  22.434  1.00 43.84  ? 220 ALA A CA  1 
ATOM   1667 C C   . ALA A 1 220 ? -8.450  9.690   21.430  1.00 42.15  ? 220 ALA A C   1 
ATOM   1668 O O   . ALA A 1 220 ? -8.830  8.515   21.497  1.00 45.02  ? 220 ALA A O   1 
ATOM   1669 C CB  . ALA A 1 220 ? -8.167  10.969  23.565  1.00 43.39  ? 220 ALA A CB  1 
ATOM   1670 N N   . SER A 1 221 ? -8.873  10.522  20.482  1.00 41.20  ? 221 SER A N   1 
ATOM   1671 C CA  . SER A 1 221 ? -9.897  10.143  19.514  1.00 42.43  ? 221 SER A CA  1 
ATOM   1672 C C   . SER A 1 221 ? -9.421  9.113   18.496  1.00 41.53  ? 221 SER A C   1 
ATOM   1673 O O   . SER A 1 221 ? -10.258 8.541   17.789  1.00 41.35  ? 221 SER A O   1 
ATOM   1674 C CB  . SER A 1 221 ? -10.403 11.391  18.798  1.00 41.32  ? 221 SER A CB  1 
ATOM   1675 O OG  . SER A 1 221 ? -9.569  11.750  17.712  1.00 42.57  ? 221 SER A OG  1 
ATOM   1676 N N   . ILE A 1 222 ? -8.117  8.855   18.409  1.00 42.76  ? 222 ILE A N   1 
ATOM   1677 C CA  . ILE A 1 222 ? -7.581  7.903   17.438  1.00 40.39  ? 222 ILE A CA  1 
ATOM   1678 C C   . ILE A 1 222 ? -6.669  6.894   18.123  1.00 39.27  ? 222 ILE A C   1 
ATOM   1679 O O   . ILE A 1 222 ? -5.896  6.190   17.457  1.00 38.76  ? 222 ILE A O   1 
ATOM   1680 C CB  . ILE A 1 222 ? -6.834  8.640   16.315  1.00 36.30  ? 222 ILE A CB  1 
ATOM   1681 C CG1 . ILE A 1 222 ? -5.762  9.530   16.934  1.00 41.03  ? 222 ILE A CG1 1 
ATOM   1682 C CG2 . ILE A 1 222 ? -7.815  9.436   15.435  1.00 38.61  ? 222 ILE A CG2 1 
ATOM   1683 C CD1 . ILE A 1 222 ? -4.416  9.413   16.302  1.00 47.78  ? 222 ILE A CD1 1 
ATOM   1684 N N   . GLU A 1 223 ? -6.770  6.790   19.449  1.00 39.36  ? 223 GLU A N   1 
ATOM   1685 C CA  . GLU A 1 223 ? -5.857  5.918   20.184  1.00 39.83  ? 223 GLU A CA  1 
ATOM   1686 C C   . GLU A 1 223 ? -6.050  4.459   19.788  1.00 40.73  ? 223 GLU A C   1 
ATOM   1687 O O   . GLU A 1 223 ? -5.073  3.717   19.625  1.00 36.96  ? 223 GLU A O   1 
ATOM   1688 C CB  . GLU A 1 223 ? -6.061  6.063   21.688  1.00 41.37  ? 223 GLU A CB  1 
ATOM   1689 C CG  . GLU A 1 223 ? -5.208  5.097   22.498  1.00 43.17  ? 223 GLU A CG  1 
ATOM   1690 C CD  . GLU A 1 223 ? -5.103  5.506   23.945  1.00 49.83  ? 223 GLU A CD  1 
ATOM   1691 O OE1 . GLU A 1 223 ? -5.965  6.296   24.375  1.00 50.38  ? 223 GLU A OE1 1 
ATOM   1692 O OE2 . GLU A 1 223 ? -4.156  5.067   24.642  1.00 49.10  ? 223 GLU A OE2 1 
ATOM   1693 N N   . GLN A 1 224 ? -7.305  4.021   19.653  1.00 37.14  ? 224 GLN A N   1 
ATOM   1694 C CA  . GLN A 1 224 ? -7.543  2.631   19.276  1.00 39.63  ? 224 GLN A CA  1 
ATOM   1695 C C   . GLN A 1 224 ? -7.045  2.367   17.862  1.00 33.81  ? 224 GLN A C   1 
ATOM   1696 O O   . GLN A 1 224 ? -6.460  1.310   17.589  1.00 34.02  ? 224 GLN A O   1 
ATOM   1697 C CB  . GLN A 1 224 ? -9.032  2.299   19.408  1.00 38.36  ? 224 GLN A CB  1 
ATOM   1698 C CG  . GLN A 1 224 ? -9.500  2.080   20.849  1.00 42.45  ? 224 GLN A CG  1 
ATOM   1699 C CD  . GLN A 1 224 ? -8.494  1.335   21.702  1.00 48.87  ? 224 GLN A CD  1 
ATOM   1700 O OE1 . GLN A 1 224 ? -8.065  0.229   21.356  1.00 52.52  ? 224 GLN A OE1 1 
ATOM   1701 N NE2 . GLN A 1 224 ? -8.109  1.936   22.830  1.00 49.60  ? 224 GLN A NE2 1 
ATOM   1702 N N   . PHE A 1 225 ? -7.262  3.322   16.957  1.00 33.12  ? 225 PHE A N   1 
ATOM   1703 C CA  . PHE A 1 225 ? -6.673  3.246   15.625  1.00 33.27  ? 225 PHE A CA  1 
ATOM   1704 C C   . PHE A 1 225 ? -5.166  3.091   15.719  1.00 33.88  ? 225 PHE A C   1 
ATOM   1705 O O   . PHE A 1 225 ? -4.554  2.252   15.044  1.00 29.79  ? 225 PHE A O   1 
ATOM   1706 C CB  . PHE A 1 225 ? -7.027  4.504   14.834  1.00 32.29  ? 225 PHE A CB  1 
ATOM   1707 C CG  . PHE A 1 225 ? -6.223  4.678   13.581  1.00 35.07  ? 225 PHE A CG  1 
ATOM   1708 C CD1 . PHE A 1 225 ? -6.609  4.074   12.391  1.00 31.84  ? 225 PHE A CD1 1 
ATOM   1709 C CD2 . PHE A 1 225 ? -5.050  5.418   13.605  1.00 33.49  ? 225 PHE A CD2 1 
ATOM   1710 C CE1 . PHE A 1 225 ? -5.849  4.236   11.240  1.00 32.43  ? 225 PHE A CE1 1 
ATOM   1711 C CE2 . PHE A 1 225 ? -4.285  5.584   12.465  1.00 34.44  ? 225 PHE A CE2 1 
ATOM   1712 C CZ  . PHE A 1 225 ? -4.685  4.986   11.275  1.00 32.70  ? 225 PHE A CZ  1 
ATOM   1713 N N   . ASP A 1 226 ? -4.551  3.889   16.582  1.00 30.89  ? 226 ASP A N   1 
ATOM   1714 C CA  . ASP A 1 226 ? -3.106  3.925   16.625  1.00 31.44  ? 226 ASP A CA  1 
ATOM   1715 C C   . ASP A 1 226 ? -2.550  2.621   17.206  1.00 32.33  ? 226 ASP A C   1 
ATOM   1716 O O   . ASP A 1 226 ? -1.511  2.130   16.743  1.00 31.38  ? 226 ASP A O   1 
ATOM   1717 C CB  . ASP A 1 226 ? -2.732  5.207   17.385  1.00 30.66  ? 226 ASP A CB  1 
ATOM   1718 C CG  . ASP A 1 226 ? -1.290  5.598   17.241  1.00 32.54  ? 226 ASP A CG  1 
ATOM   1719 O OD1 . ASP A 1 226 ? -0.837  5.695   16.091  1.00 31.70  ? 226 ASP A OD1 1 
ATOM   1720 O OD2 . ASP A 1 226 ? -0.679  6.041   18.239  1.00 34.70  ? 226 ASP A OD2 1 
ATOM   1721 N N   . ILE A 1 227 ? -3.275  1.993   18.144  1.00 30.30  ? 227 ILE A N   1 
ATOM   1722 C CA  . ILE A 1 227 ? -2.866  0.690   18.662  1.00 29.41  ? 227 ILE A CA  1 
ATOM   1723 C C   . ILE A 1 227 ? -2.995  -0.381  17.588  1.00 30.68  ? 227 ILE A C   1 
ATOM   1724 O O   . ILE A 1 227 ? -2.133  -1.257  17.461  1.00 30.18  ? 227 ILE A O   1 
ATOM   1725 C CB  . ILE A 1 227 ? -3.680  0.322   19.916  1.00 31.50  ? 227 ILE A CB  1 
ATOM   1726 C CG1 . ILE A 1 227 ? -3.243  1.185   21.108  1.00 36.91  ? 227 ILE A CG1 1 
ATOM   1727 C CG2 . ILE A 1 227 ? -3.505  -1.144  20.276  1.00 32.99  ? 227 ILE A CG2 1 
ATOM   1728 C CD1 . ILE A 1 227 ? -4.342  1.424   22.112  1.00 41.12  ? 227 ILE A CD1 1 
ATOM   1729 N N   . ALA A 1 228 ? -4.073  -0.341  16.809  1.00 31.20  ? 228 ALA A N   1 
ATOM   1730 C CA  . ALA A 1 228 ? -4.214  -1.317  15.740  1.00 30.42  ? 228 ALA A CA  1 
ATOM   1731 C C   . ALA A 1 228 ? -3.066  -1.201  14.747  1.00 28.79  ? 228 ALA A C   1 
ATOM   1732 O O   . ALA A 1 228 ? -2.484  -2.212  14.351  1.00 29.75  ? 228 ALA A O   1 
ATOM   1733 C CB  . ALA A 1 228 ? -5.564  -1.145  15.045  1.00 29.27  ? 228 ALA A CB  1 
ATOM   1734 N N   . MET A 1 229 ? -2.703  0.026   14.352  1.00 27.57  ? 229 MET A N   1 
ATOM   1735 C CA  . MET A 1 229 ? -1.573  0.171   13.436  1.00 28.95  ? 229 MET A CA  1 
ATOM   1736 C C   . MET A 1 229 ? -0.247  -0.224  14.077  1.00 28.86  ? 229 MET A C   1 
ATOM   1737 O O   . MET A 1 229 ? 0.624   -0.765  13.389  1.00 27.98  ? 229 MET A O   1 
ATOM   1738 C CB  . MET A 1 229 ? -1.512  1.588   12.863  1.00 29.48  ? 229 MET A CB  1 
ATOM   1739 C CG  . MET A 1 229 ? -2.823  1.931   12.169  1.00 31.59  ? 229 MET A CG  1 
ATOM   1740 S SD  . MET A 1 229 ? -2.890  1.098   10.549  1.00 31.22  ? 229 MET A SD  1 
ATOM   1741 C CE  . MET A 1 229 ? -1.882  2.160   9.514   1.00 31.87  ? 229 MET A CE  1 
ATOM   1742 N N   . GLY A 1 230 ? -0.062  0.034   15.373  1.00 27.44  ? 230 GLY A N   1 
ATOM   1743 C CA  . GLY A 1 230 ? 1.138   -0.455  16.034  1.00 26.30  ? 230 GLY A CA  1 
ATOM   1744 C C   . GLY A 1 230 ? 1.208   -1.972  16.048  1.00 29.16  ? 230 GLY A C   1 
ATOM   1745 O O   . GLY A 1 230 ? 2.281   -2.553  15.855  1.00 29.17  ? 230 GLY A O   1 
ATOM   1746 N N   . ASN A 1 231 ? 0.067   -2.634  16.268  1.00 28.47  ? 231 ASN A N   1 
ATOM   1747 C CA  . ASN A 1 231 ? 0.026   -4.094  16.156  1.00 27.22  ? 231 ASN A CA  1 
ATOM   1748 C C   . ASN A 1 231 ? 0.438   -4.549  14.763  1.00 28.90  ? 231 ASN A C   1 
ATOM   1749 O O   . ASN A 1 231 ? 1.209   -5.502  14.615  1.00 28.08  ? 231 ASN A O   1 
ATOM   1750 C CB  . ASN A 1 231 ? -1.370  -4.645  16.466  1.00 30.32  ? 231 ASN A CB  1 
ATOM   1751 C CG  . ASN A 1 231 ? -1.734  -4.548  17.926  1.00 32.95  ? 231 ASN A CG  1 
ATOM   1752 O OD1 . ASN A 1 231 ? -0.889  -4.692  18.807  1.00 34.79  ? 231 ASN A OD1 1 
ATOM   1753 N ND2 . ASN A 1 231 ? -3.018  -4.353  18.192  1.00 34.42  ? 231 ASN A ND2 1 
ATOM   1754 N N   . VAL A 1 232 ? -0.120  -3.923  13.717  1.00 27.23  ? 232 VAL A N   1 
ATOM   1755 C CA  . VAL A 1 232 ? 0.247   -4.317  12.358  1.00 26.14  ? 232 VAL A CA  1 
ATOM   1756 C C   . VAL A 1 232 ? 1.752   -4.229  12.161  1.00 30.09  ? 232 VAL A C   1 
ATOM   1757 O O   . VAL A 1 232 ? 2.376   -5.135  11.602  1.00 28.21  ? 232 VAL A O   1 
ATOM   1758 C CB  . VAL A 1 232 ? -0.481  -3.443  11.326  1.00 26.89  ? 232 VAL A CB  1 
ATOM   1759 C CG1 . VAL A 1 232 ? 0.037   -3.789  9.956   1.00 27.28  ? 232 VAL A CG1 1 
ATOM   1760 C CG2 . VAL A 1 232 ? -1.983  -3.638  11.454  1.00 27.43  ? 232 VAL A CG2 1 
ATOM   1761 N N   . LEU A 1 233 ? 2.351   -3.122  12.609  1.00 27.22  ? 233 LEU A N   1 
ATOM   1762 C CA  . LEU A 1 233 ? 3.763   -2.861  12.346  1.00 26.33  ? 233 LEU A CA  1 
ATOM   1763 C C   . LEU A 1 233 ? 4.647   -3.940  12.953  1.00 28.44  ? 233 LEU A C   1 
ATOM   1764 O O   . LEU A 1 233 ? 5.413   -4.599  12.243  1.00 28.32  ? 233 LEU A O   1 
ATOM   1765 C CB  . LEU A 1 233 ? 4.134   -1.476  12.884  1.00 26.79  ? 233 LEU A CB  1 
ATOM   1766 C CG  . LEU A 1 233 ? 5.442   -0.782  12.465  1.00 30.97  ? 233 LEU A CG  1 
ATOM   1767 C CD1 . LEU A 1 233 ? 6.707   -1.527  12.965  1.00 31.79  ? 233 LEU A CD1 1 
ATOM   1768 C CD2 . LEU A 1 233 ? 5.459   -0.583  10.964  1.00 32.78  ? 233 LEU A CD2 1 
ATOM   1769 N N   . GLY A 1 234 ? 4.566   -4.117  14.276  1.00 28.38  ? 234 GLY A N   1 
ATOM   1770 C CA  . GLY A 1 234 ? 5.443   -5.061  14.952  1.00 26.71  ? 234 GLY A CA  1 
ATOM   1771 C C   . GLY A 1 234 ? 5.158   -6.503  14.567  1.00 29.24  ? 234 GLY A C   1 
ATOM   1772 O O   . GLY A 1 234 ? 6.084   -7.296  14.385  1.00 28.13  ? 234 GLY A O   1 
ATOM   1773 N N   . LEU A 1 235 ? 3.879   -6.856  14.410  1.00 27.57  ? 235 LEU A N   1 
ATOM   1774 C CA  . LEU A 1 235 ? 3.563   -8.245  14.074  1.00 28.44  ? 235 LEU A CA  1 
ATOM   1775 C C   . LEU A 1 235 ? 3.952   -8.566  12.634  1.00 28.52  ? 235 LEU A C   1 
ATOM   1776 O O   . LEU A 1 235 ? 4.345   -9.703  12.340  1.00 27.70  ? 235 LEU A O   1 
ATOM   1777 C CB  . LEU A 1 235 ? 2.076   -8.516  14.310  1.00 27.21  ? 235 LEU A CB  1 
ATOM   1778 C CG  . LEU A 1 235 ? 1.627   -8.468  15.778  1.00 28.95  ? 235 LEU A CG  1 
ATOM   1779 C CD1 . LEU A 1 235 ? 0.207   -8.975  15.919  1.00 28.51  ? 235 LEU A CD1 1 
ATOM   1780 C CD2 . LEU A 1 235 ? 2.587   -9.276  16.707  1.00 30.13  ? 235 LEU A CD2 1 
ATOM   1781 N N   . THR A 1 236 ? 3.856   -7.580  11.729  1.00 28.65  ? 236 THR A N   1 
ATOM   1782 C CA  . THR A 1 236 ? 4.380   -7.759  10.378  1.00 29.55  ? 236 THR A CA  1 
ATOM   1783 C C   . THR A 1 236 ? 5.892   -7.917  10.398  1.00 29.48  ? 236 THR A C   1 
ATOM   1784 O O   . THR A 1 236 ? 6.447   -8.744  9.662   1.00 30.10  ? 236 THR A O   1 
ATOM   1785 C CB  . THR A 1 236 ? 3.959   -6.587  9.481   1.00 28.28  ? 236 THR A CB  1 
ATOM   1786 O OG1 . THR A 1 236 ? 2.533   -6.536  9.428   1.00 26.76  ? 236 THR A OG1 1 
ATOM   1787 C CG2 . THR A 1 236 ? 4.515   -6.731  8.084   1.00 27.81  ? 236 THR A CG2 1 
ATOM   1788 N N   . ASN A 1 237 ? 6.571   -7.157  11.257  1.00 26.94  ? 237 ASN A N   1 
ATOM   1789 C CA  . ASN A 1 237 ? 7.999   -7.366  11.450  1.00 29.86  ? 237 ASN A CA  1 
ATOM   1790 C C   . ASN A 1 237 ? 8.264   -8.813  11.885  1.00 28.10  ? 237 ASN A C   1 
ATOM   1791 O O   . ASN A 1 237 ? 9.165   -9.478  11.355  1.00 31.53  ? 237 ASN A O   1 
ATOM   1792 C CB  . ASN A 1 237 ? 8.509   -6.379  12.503  1.00 28.70  ? 237 ASN A CB  1 
ATOM   1793 C CG  . ASN A 1 237 ? 8.665   -4.941  11.966  1.00 33.08  ? 237 ASN A CG  1 
ATOM   1794 O OD1 . ASN A 1 237 ? 8.250   -4.625  10.856  1.00 36.57  ? 237 ASN A OD1 1 
ATOM   1795 N ND2 . ASN A 1 237 ? 9.218   -4.056  12.794  1.00 41.93  ? 237 ASN A ND2 1 
ATOM   1796 N N   . ASP A 1 238 ? 7.447   -9.332  12.819  1.00 27.45  ? 238 ASP A N   1 
ATOM   1797 C CA  . ASP A 1 238 ? 7.597   -10.722 13.250  1.00 28.13  ? 238 ASP A CA  1 
ATOM   1798 C C   . ASP A 1 238 ? 7.389   -11.677 12.093  1.00 28.78  ? 238 ASP A C   1 
ATOM   1799 O O   . ASP A 1 238 ? 8.128   -12.660 11.945  1.00 29.39  ? 238 ASP A O   1 
ATOM   1800 C CB  . ASP A 1 238 ? 6.609   -11.088 14.369  1.00 28.77  ? 238 ASP A CB  1 
ATOM   1801 C CG  . ASP A 1 238 ? 6.936   -10.443 15.703  1.00 32.32  ? 238 ASP A CG  1 
ATOM   1802 O OD1 . ASP A 1 238 ? 7.950   -9.726  15.795  1.00 29.34  ? 238 ASP A OD1 1 
ATOM   1803 O OD2 . ASP A 1 238 ? 6.177   -10.694 16.667  1.00 31.70  ? 238 ASP A OD2 1 
ATOM   1804 N N   . TYR A 1 239 ? 6.375   -11.406 11.266  1.00 26.93  ? 239 TYR A N   1 
ATOM   1805 C CA  . TYR A 1 239 ? 6.011   -12.346 10.217  1.00 28.05  ? 239 TYR A CA  1 
ATOM   1806 C C   . TYR A 1 239 ? 7.161   -12.539 9.235   1.00 29.61  ? 239 TYR A C   1 
ATOM   1807 O O   . TYR A 1 239 ? 7.496   -13.674 8.860   1.00 29.52  ? 239 TYR A O   1 
ATOM   1808 C CB  . TYR A 1 239 ? 4.755   -11.838 9.510   1.00 25.80  ? 239 TYR A CB  1 
ATOM   1809 C CG  . TYR A 1 239 ? 4.340   -12.730 8.386   1.00 28.90  ? 239 TYR A CG  1 
ATOM   1810 C CD1 . TYR A 1 239 ? 3.642   -13.894 8.644   1.00 32.72  ? 239 TYR A CD1 1 
ATOM   1811 C CD2 . TYR A 1 239 ? 4.645   -12.417 7.068   1.00 31.10  ? 239 TYR A CD2 1 
ATOM   1812 C CE1 . TYR A 1 239 ? 3.253   -14.737 7.616   1.00 32.37  ? 239 TYR A CE1 1 
ATOM   1813 C CE2 . TYR A 1 239 ? 4.261   -13.271 6.029   1.00 32.14  ? 239 TYR A CE2 1 
ATOM   1814 C CZ  . TYR A 1 239 ? 3.572   -14.424 6.327   1.00 33.25  ? 239 TYR A CZ  1 
ATOM   1815 O OH  . TYR A 1 239 ? 3.171   -15.283 5.323   1.00 37.53  ? 239 TYR A OH  1 
ATOM   1816 N N   . PHE A 1 240 ? 7.782   -11.442 8.814   1.00 29.20  ? 240 PHE A N   1 
ATOM   1817 C CA  . PHE A 1 240 ? 8.887   -11.519 7.870   1.00 30.62  ? 240 PHE A CA  1 
ATOM   1818 C C   . PHE A 1 240 ? 10.185  -11.987 8.511   1.00 32.64  ? 240 PHE A C   1 
ATOM   1819 O O   . PHE A 1 240 ? 11.000  -12.628 7.839   1.00 34.94  ? 240 PHE A O   1 
ATOM   1820 C CB  . PHE A 1 240 ? 9.084   -10.164 7.207   1.00 31.78  ? 240 PHE A CB  1 
ATOM   1821 C CG  . PHE A 1 240 ? 8.060   -9.886  6.162   1.00 31.62  ? 240 PHE A CG  1 
ATOM   1822 C CD1 . PHE A 1 240 ? 8.060   -10.610 4.988   1.00 37.21  ? 240 PHE A CD1 1 
ATOM   1823 C CD2 . PHE A 1 240 ? 7.078   -8.926  6.361   1.00 29.73  ? 240 PHE A CD2 1 
ATOM   1824 C CE1 . PHE A 1 240 ? 7.112   -10.369 4.016   1.00 36.94  ? 240 PHE A CE1 1 
ATOM   1825 C CE2 . PHE A 1 240 ? 6.121   -8.683  5.377   1.00 28.65  ? 240 PHE A CE2 1 
ATOM   1826 C CZ  . PHE A 1 240 ? 6.149   -9.402  4.214   1.00 34.99  ? 240 PHE A CZ  1 
ATOM   1827 N N   . SER A 1 241 ? 10.390  -11.691 9.789   1.00 32.70  ? 241 SER A N   1 
ATOM   1828 C CA  . SER A 1 241 ? 11.631  -12.108 10.485  1.00 34.27  ? 241 SER A CA  1 
ATOM   1829 C C   . SER A 1 241 ? 11.650  -13.623 10.658  1.00 40.19  ? 241 SER A C   1 
ATOM   1830 O O   . SER A 1 241 ? 12.734  -14.202 10.683  1.00 41.46  ? 241 SER A O   1 
ATOM   1831 C CB  . SER A 1 241 ? 11.743  -11.431 11.809  1.00 39.32  ? 241 SER A CB  1 
ATOM   1832 O OG  . SER A 1 241 ? 11.815  -10.027 11.637  1.00 44.45  ? 241 SER A OG  1 
ATOM   1833 N N   . TRP A 1 242 ? 10.482  -14.244 10.792  1.00 36.29  ? 242 TRP A N   1 
ATOM   1834 C CA  . TRP A 1 242 ? 10.408  -15.707 11.044  1.00 38.50  ? 242 TRP A CA  1 
ATOM   1835 C C   . TRP A 1 242 ? 11.072  -16.483 9.904   1.00 43.00  ? 242 TRP A C   1 
ATOM   1836 O O   . TRP A 1 242 ? 11.539  -17.593 10.143  1.00 46.69  ? 242 TRP A O   1 
ATOM   1837 C CB  . TRP A 1 242 ? 8.955   -16.144 11.225  1.00 37.18  ? 242 TRP A CB  1 
ATOM   1838 C CG  . TRP A 1 242 ? 8.793   -17.592 11.550  1.00 39.63  ? 242 TRP A CG  1 
ATOM   1839 C CD1 . TRP A 1 242 ? 8.271   -18.566 10.752  1.00 42.42  ? 242 TRP A CD1 1 
ATOM   1840 C CD2 . TRP A 1 242 ? 9.165   -18.233 12.778  1.00 40.05  ? 242 TRP A CD2 1 
ATOM   1841 N NE1 . TRP A 1 242 ? 8.291   -19.769 11.402  1.00 41.49  ? 242 TRP A NE1 1 
ATOM   1842 C CE2 . TRP A 1 242 ? 8.835   -19.596 12.646  1.00 40.16  ? 242 TRP A CE2 1 
ATOM   1843 C CE3 . TRP A 1 242 ? 9.741   -17.788 13.971  1.00 38.99  ? 242 TRP A CE3 1 
ATOM   1844 C CZ2 . TRP A 1 242 ? 9.063   -20.516 13.666  1.00 44.73  ? 242 TRP A CZ2 1 
ATOM   1845 C CZ3 . TRP A 1 242 ? 9.970   -18.698 14.975  1.00 43.58  ? 242 TRP A CZ3 1 
ATOM   1846 C CH2 . TRP A 1 242 ? 9.633   -20.042 14.823  1.00 41.10  ? 242 TRP A CH2 1 
ATOM   1847 N N   . ASN A 1 243 ? 11.115  -15.896 8.710   1.00 47.95  ? 243 ASN A N   1 
ATOM   1848 C CA  . ASN A 1 243 ? 11.800  -16.592 7.592   1.00 50.63  ? 243 ASN A CA  1 
ATOM   1849 C C   . ASN A 1 243 ? 13.248  -16.837 8.005   1.00 53.49  ? 243 ASN A C   1 
ATOM   1850 O O   . ASN A 1 243 ? 13.772  -17.905 7.667   1.00 57.63  ? 243 ASN A O   1 
ATOM   1851 C CB  . ASN A 1 243 ? 11.709  -15.773 6.307   1.00 51.65  ? 243 ASN A CB  1 
ATOM   1852 C CG  . ASN A 1 243 ? 10.290  -15.618 5.812   1.00 51.77  ? 243 ASN A CG  1 
ATOM   1853 O OD1 . ASN A 1 243 ? 9.543   -16.588 5.771   1.00 53.73  ? 243 ASN A OD1 1 
ATOM   1854 N ND2 . ASN A 1 243 ? 9.914   -14.408 5.435   1.00 49.97  ? 243 ASN A ND2 1 
ATOM   1855 N N   . ARG A 1 254 ? 11.906  -13.902 20.298  1.00 44.29  ? 254 ARG A N   1 
ATOM   1856 C CA  . ARG A 1 254 ? 10.743  -13.028 20.554  1.00 38.32  ? 254 ARG A CA  1 
ATOM   1857 C C   . ARG A 1 254 ? 9.992   -12.879 19.238  1.00 39.81  ? 254 ARG A C   1 
ATOM   1858 O O   . ARG A 1 254 ? 10.461  -12.132 18.378  1.00 40.16  ? 254 ARG A O   1 
ATOM   1859 C CB  . ARG A 1 254 ? 11.214  -11.670 21.068  1.00 46.66  ? 254 ARG A CB  1 
ATOM   1860 C CG  . ARG A 1 254 ? 10.128  -10.607 21.142  1.00 45.77  ? 254 ARG A CG  1 
ATOM   1861 C CD  . ARG A 1 254 ? 10.636  -9.251  20.697  1.00 48.00  ? 254 ARG A CD  1 
ATOM   1862 N NE  . ARG A 1 254 ? 11.265  -9.328  19.388  1.00 51.01  ? 254 ARG A NE  1 
ATOM   1863 C CZ  . ARG A 1 254 ? 12.282  -8.578  18.986  1.00 53.43  ? 254 ARG A CZ  1 
ATOM   1864 N NH1 . ARG A 1 254 ? 12.805  -7.671  19.793  1.00 49.71  ? 254 ARG A NH1 1 
ATOM   1865 N NH2 . ARG A 1 254 ? 12.774  -8.738  17.772  1.00 57.49  ? 254 ARG A NH2 1 
ATOM   1866 N N   . ASN A 1 255 ? 8.885   -13.593 19.098  1.00 33.21  ? 255 ASN A N   1 
ATOM   1867 C CA  . ASN A 1 255 ? 8.180   -13.564 17.816  1.00 30.54  ? 255 ASN A CA  1 
ATOM   1868 C C   . ASN A 1 255 ? 6.754   -14.058 17.983  1.00 32.59  ? 255 ASN A C   1 
ATOM   1869 O O   . ASN A 1 255 ? 6.526   -15.084 18.631  1.00 32.46  ? 255 ASN A O   1 
ATOM   1870 C CB  . ASN A 1 255 ? 8.941   -14.418 16.788  1.00 32.06  ? 255 ASN A CB  1 
ATOM   1871 C CG  . ASN A 1 255 ? 8.420   -14.246 15.358  1.00 30.74  ? 255 ASN A CG  1 
ATOM   1872 O OD1 . ASN A 1 255 ? 7.261   -14.532 15.069  1.00 31.99  ? 255 ASN A OD1 1 
ATOM   1873 N ND2 . ASN A 1 255 ? 9.279   -13.758 14.473  1.00 31.94  ? 255 ASN A ND2 1 
ATOM   1874 N N   . GLY A 1 256 ? 5.795   -13.369 17.355  1.00 30.56  ? 256 GLY A N   1 
ATOM   1875 C CA  . GLY A 1 256 ? 4.411   -13.787 17.465  1.00 29.01  ? 256 GLY A CA  1 
ATOM   1876 C C   . GLY A 1 256 ? 4.167   -15.207 17.001  1.00 29.00  ? 256 GLY A C   1 
ATOM   1877 O O   . GLY A 1 256 ? 3.214   -15.846 17.447  1.00 29.15  ? 256 GLY A O   1 
ATOM   1878 N N   . VAL A 1 257 ? 4.987   -15.708 16.072  1.00 28.39  ? 257 VAL A N   1 
ATOM   1879 C CA  . VAL A 1 257 ? 4.802   -17.091 15.617  1.00 28.29  ? 257 VAL A CA  1 
ATOM   1880 C C   . VAL A 1 257 ? 4.988   -18.059 16.776  1.00 31.81  ? 257 VAL A C   1 
ATOM   1881 O O   . VAL A 1 257 ? 4.202   -18.999 16.942  1.00 32.52  ? 257 VAL A O   1 
ATOM   1882 C CB  . VAL A 1 257 ? 5.747   -17.431 14.448  1.00 32.64  ? 257 VAL A CB  1 
ATOM   1883 C CG1 . VAL A 1 257 ? 5.558   -18.905 14.030  1.00 31.42  ? 257 VAL A CG1 1 
ATOM   1884 C CG2 . VAL A 1 257 ? 5.454   -16.535 13.246  1.00 32.49  ? 257 VAL A CG2 1 
ATOM   1885 N N   . VAL A 1 258 ? 6.018   -17.833 17.596  1.00 34.27  ? 258 VAL A N   1 
ATOM   1886 C CA  . VAL A 1 258 ? 6.277   -18.688 18.757  1.00 32.86  ? 258 VAL A CA  1 
ATOM   1887 C C   . VAL A 1 258 ? 5.183   -18.536 19.804  1.00 33.04  ? 258 VAL A C   1 
ATOM   1888 O O   . VAL A 1 258 ? 4.734   -19.525 20.398  1.00 33.12  ? 258 VAL A O   1 
ATOM   1889 C CB  . VAL A 1 258 ? 7.670   -18.385 19.340  1.00 35.83  ? 258 VAL A CB  1 
ATOM   1890 C CG1 . VAL A 1 258 ? 7.988   -19.344 20.469  1.00 40.96  ? 258 VAL A CG1 1 
ATOM   1891 C CG2 . VAL A 1 258 ? 8.723   -18.553 18.245  1.00 37.51  ? 258 VAL A CG2 1 
ATOM   1892 N N   . VAL A 1 259 ? 4.763   -17.299 20.078  1.00 29.92  ? 259 VAL A N   1 
ATOM   1893 C CA  . VAL A 1 259 ? 3.674   -17.084 21.030  1.00 29.68  ? 259 VAL A CA  1 
ATOM   1894 C C   . VAL A 1 259 ? 2.431   -17.851 20.606  1.00 33.20  ? 259 VAL A C   1 
ATOM   1895 O O   . VAL A 1 259 ? 1.801   -18.548 21.409  1.00 34.33  ? 259 VAL A O   1 
ATOM   1896 C CB  . VAL A 1 259 ? 3.378   -15.583 21.186  1.00 32.87  ? 259 VAL A CB  1 
ATOM   1897 C CG1 . VAL A 1 259 ? 2.322   -15.384 22.270  1.00 32.59  ? 259 VAL A CG1 1 
ATOM   1898 C CG2 . VAL A 1 259 ? 4.656   -14.830 21.536  1.00 31.24  ? 259 VAL A CG2 1 
ATOM   1899 N N   . LEU A 1 260 ? 2.084   -17.756 19.331  1.00 30.83  ? 260 LEU A N   1 
ATOM   1900 C CA  . LEU A 1 260 ? 0.860   -18.439 18.855  1.00 30.83  ? 260 LEU A CA  1 
ATOM   1901 C C   . LEU A 1 260 ? 1.043   -19.961 18.940  1.00 31.38  ? 260 LEU A C   1 
ATOM   1902 O O   . LEU A 1 260 ? 0.092   -20.644 19.315  1.00 31.89  ? 260 LEU A O   1 
ATOM   1903 C CB  . LEU A 1 260 ? 0.562   -17.971 17.430  1.00 29.19  ? 260 LEU A CB  1 
ATOM   1904 C CG  . LEU A 1 260 ? -0.064  -16.583 17.341  1.00 30.81  ? 260 LEU A CG  1 
ATOM   1905 C CD1 . LEU A 1 260 ? -0.092  -16.087 15.906  1.00 29.50  ? 260 LEU A CD1 1 
ATOM   1906 C CD2 . LEU A 1 260 ? -1.461  -16.587 17.934  1.00 32.63  ? 260 LEU A CD2 1 
ATOM   1907 N N   . MET A 1 261 ? 2.231   -20.452 18.599  1.00 31.63  ? 261 MET A N   1 
ATOM   1908 C CA  . MET A 1 261 ? 2.507   -21.908 18.674  1.00 33.88  ? 261 MET A CA  1 
ATOM   1909 C C   . MET A 1 261 ? 2.278   -22.380 20.109  1.00 37.14  ? 261 MET A C   1 
ATOM   1910 O O   . MET A 1 261 ? 1.676   -23.434 20.289  1.00 36.94  ? 261 MET A O   1 
ATOM   1911 C CB  . MET A 1 261 ? 3.959   -22.215 18.306  1.00 36.78  ? 261 MET A CB  1 
ATOM   1912 C CG  . MET A 1 261 ? 4.263   -22.250 16.834  1.00 37.22  ? 261 MET A CG  1 
ATOM   1913 S SD  . MET A 1 261 ? 6.033   -22.533 16.588  1.00 41.35  ? 261 MET A SD  1 
ATOM   1914 C CE  . MET A 1 261 ? 6.134   -24.283 16.951  1.00 33.91  ? 261 MET A CE  1 
ATOM   1915 N N   . LYS A 1 262 ? 2.755   -21.608 21.085  1.00 36.10  ? 262 LYS A N   1 
ATOM   1916 C CA  . LYS A 1 262 ? 2.608   -21.999 22.483  1.00 38.08  ? 262 LYS A CA  1 
ATOM   1917 C C   . LYS A 1 262 ? 1.172   -21.827 22.960  1.00 39.22  ? 262 LYS A C   1 
ATOM   1918 O O   . LYS A 1 262 ? 0.651   -22.680 23.690  1.00 40.19  ? 262 LYS A O   1 
ATOM   1919 C CB  . LYS A 1 262 ? 3.549   -21.168 23.360  1.00 36.44  ? 262 LYS A CB  1 
ATOM   1920 C CG  . LYS A 1 262 ? 5.016   -21.356 23.049  1.00 40.94  ? 262 LYS A CG  1 
ATOM   1921 C CD  . LYS A 1 262 ? 5.854   -20.598 24.065  1.00 43.76  ? 262 LYS A CD  1 
ATOM   1922 C CE  . LYS A 1 262 ? 7.314   -21.006 24.042  1.00 48.16  ? 262 LYS A CE  1 
ATOM   1923 N NZ  . LYS A 1 262 ? 8.172   -19.842 24.463  1.00 48.84  ? 262 LYS A NZ  1 
ATOM   1924 N N   . GLU A 1 263 ? 0.515   -20.738 22.546  1.00 34.67  ? 263 GLU A N   1 
ATOM   1925 C CA  . GLU A 1 263 ? -0.848  -20.478 22.998  1.00 33.94  ? 263 GLU A CA  1 
ATOM   1926 C C   . GLU A 1 263 ? -1.826  -21.514 22.467  1.00 37.26  ? 263 GLU A C   1 
ATOM   1927 O O   . GLU A 1 263 ? -2.762  -21.902 23.174  1.00 39.55  ? 263 GLU A O   1 
ATOM   1928 C CB  . GLU A 1 263 ? -1.304  -19.080 22.583  1.00 36.35  ? 263 GLU A CB  1 
ATOM   1929 C CG  . GLU A 1 263 ? -2.513  -18.593 23.380  1.00 38.60  ? 263 GLU A CG  1 
ATOM   1930 C CD  . GLU A 1 263 ? -2.973  -17.193 23.000  1.00 42.59  ? 263 GLU A CD  1 
ATOM   1931 O OE1 . GLU A 1 263 ? -2.294  -16.536 22.177  1.00 39.26  ? 263 GLU A OE1 1 
ATOM   1932 O OE2 . GLU A 1 263 ? -4.028  -16.752 23.516  1.00 44.47  ? 263 GLU A OE2 1 
ATOM   1933 N N   . HIS A 1 264 ? -1.643  -21.956 21.222  1.00 37.42  ? 264 HIS A N   1 
ATOM   1934 C CA  . HIS A 1 264 ? -2.614  -22.824 20.567  1.00 36.05  ? 264 HIS A CA  1 
ATOM   1935 C C   . HIS A 1 264 ? -2.078  -24.223 20.314  1.00 41.33  ? 264 HIS A C   1 
ATOM   1936 O O   . HIS A 1 264 ? -2.807  -25.064 19.777  1.00 40.11  ? 264 HIS A O   1 
ATOM   1937 C CB  . HIS A 1 264 ? -3.085  -22.173 19.258  1.00 35.18  ? 264 HIS A CB  1 
ATOM   1938 C CG  . HIS A 1 264 ? -3.772  -20.859 19.476  1.00 32.84  ? 264 HIS A CG  1 
ATOM   1939 N ND1 . HIS A 1 264 ? -5.067  -20.771 19.934  1.00 35.45  ? 264 HIS A ND1 1 
ATOM   1940 C CD2 . HIS A 1 264 ? -3.345  -19.583 19.308  1.00 34.83  ? 264 HIS A CD2 1 
ATOM   1941 C CE1 . HIS A 1 264 ? -5.405  -19.499 20.053  1.00 39.65  ? 264 HIS A CE1 1 
ATOM   1942 N NE2 . HIS A 1 264 ? -4.379  -18.758 19.674  1.00 33.66  ? 264 HIS A NE2 1 
ATOM   1943 N N   . HIS A 1 265 ? -0.829  -24.492 20.697  1.00 40.82  ? 265 HIS A N   1 
ATOM   1944 C CA  . HIS A 1 265 ? -0.195  -25.806 20.564  1.00 41.97  ? 265 HIS A CA  1 
ATOM   1945 C C   . HIS A 1 265 ? -0.240  -26.304 19.118  1.00 44.40  ? 265 HIS A C   1 
ATOM   1946 O O   . HIS A 1 265 ? -0.732  -27.399 18.825  1.00 40.25  ? 265 HIS A O   1 
ATOM   1947 C CB  . HIS A 1 265 ? -0.837  -26.823 21.518  1.00 44.27  ? 265 HIS A CB  1 
ATOM   1948 C CG  . HIS A 1 265 ? -1.036  -26.300 22.903  1.00 46.12  ? 265 HIS A CG  1 
ATOM   1949 N ND1 . HIS A 1 265 ? 0.014   -26.059 23.765  1.00 51.79  ? 265 HIS A ND1 1 
ATOM   1950 C CD2 . HIS A 1 265 ? -2.160  -25.942 23.568  1.00 50.33  ? 265 HIS A CD2 1 
ATOM   1951 C CE1 . HIS A 1 265 ? -0.456  -25.592 24.908  1.00 50.39  ? 265 HIS A CE1 1 
ATOM   1952 N NE2 . HIS A 1 265 ? -1.771  -25.507 24.814  1.00 52.91  ? 265 HIS A NE2 1 
ATOM   1953 N N   . THR A 1 266 ? 0.294   -25.483 18.209  1.00 37.48  ? 266 THR A N   1 
ATOM   1954 C CA  . THR A 1 266 ? 0.290   -25.819 16.794  1.00 36.64  ? 266 THR A CA  1 
ATOM   1955 C C   . THR A 1 266 ? 1.714   -25.869 16.265  1.00 35.10  ? 266 THR A C   1 
ATOM   1956 O O   . THR A 1 266 ? 2.674   -25.489 16.942  1.00 37.53  ? 266 THR A O   1 
ATOM   1957 C CB  . THR A 1 266 ? -0.510  -24.807 15.961  1.00 36.33  ? 266 THR A CB  1 
ATOM   1958 O OG1 . THR A 1 266 ? 0.187   -23.559 15.946  1.00 37.82  ? 266 THR A OG1 1 
ATOM   1959 C CG2 . THR A 1 266 ? -1.913  -24.597 16.541  1.00 36.97  ? 266 THR A CG2 1 
ATOM   1960 N N   . THR A 1 267 ? 1.837   -26.355 15.033  1.00 33.19  ? 267 THR A N   1 
ATOM   1961 C CA  . THR A 1 267 ? 3.096   -26.279 14.314  1.00 34.56  ? 267 THR A CA  1 
ATOM   1962 C C   . THR A 1 267 ? 3.434   -24.822 14.008  1.00 35.40  ? 267 THR A C   1 
ATOM   1963 O O   . THR A 1 267 ? 2.589   -23.928 14.110  1.00 34.28  ? 267 THR A O   1 
ATOM   1964 C CB  . THR A 1 267 ? 3.019   -27.052 13.003  1.00 38.13  ? 267 THR A CB  1 
ATOM   1965 O OG1 . THR A 1 267 ? 2.018   -26.456 12.158  1.00 36.02  ? 267 THR A OG1 1 
ATOM   1966 C CG2 . THR A 1 267 ? 2.658   -28.507 13.260  1.00 41.95  ? 267 THR A CG2 1 
ATOM   1967 N N   . ALA A 1 268 ? 4.686   -24.599 13.599  1.00 35.12  ? 268 ALA A N   1 
ATOM   1968 C CA  . ALA A 1 268 ? 5.106   -23.252 13.225  1.00 36.30  ? 268 ALA A CA  1 
ATOM   1969 C C   . ALA A 1 268 ? 4.410   -22.790 11.952  1.00 38.35  ? 268 ALA A C   1 
ATOM   1970 O O   . ALA A 1 268 ? 4.064   -21.613 11.830  1.00 35.09  ? 268 ALA A O   1 
ATOM   1971 C CB  . ALA A 1 268 ? 6.623   -23.184 13.061  1.00 39.85  ? 268 ALA A CB  1 
ATOM   1972 N N   . ASP A 1 269 ? 4.201   -23.686 10.983  1.00 39.09  ? 269 ASP A N   1 
ATOM   1973 C CA  . ASP A 1 269 ? 3.508   -23.267 9.764   1.00 38.60  ? 269 ASP A CA  1 
ATOM   1974 C C   . ASP A 1 269 ? 2.072   -22.853 10.051  1.00 36.75  ? 269 ASP A C   1 
ATOM   1975 O O   . ASP A 1 269 ? 1.565   -21.901 9.448   1.00 36.34  ? 269 ASP A O   1 
ATOM   1976 C CB  . ASP A 1 269 ? 3.537   -24.366 8.700   1.00 44.82  ? 269 ASP A CB  1 
ATOM   1977 C CG  . ASP A 1 269 ? 4.932   -24.630 8.167   1.00 49.80  ? 269 ASP A CG  1 
ATOM   1978 O OD1 . ASP A 1 269 ? 5.832   -23.792 8.396   1.00 54.41  ? 269 ASP A OD1 1 
ATOM   1979 O OD2 . ASP A 1 269 ? 5.119   -25.663 7.489   1.00 56.56  ? 269 ASP A OD2 1 
ATOM   1980 N N   . ALA A 1 270 ? 1.390   -23.562 10.954  1.00 34.16  ? 270 ALA A N   1 
ATOM   1981 C CA  . ALA A 1 270 ? 0.025   -23.173 11.291  1.00 32.22  ? 270 ALA A CA  1 
ATOM   1982 C C   . ALA A 1 270 ? 0.006   -21.841 12.025  1.00 29.15  ? 270 ALA A C   1 
ATOM   1983 O O   . ALA A 1 270 ? -0.870  -21.003 11.790  1.00 30.08  ? 270 ALA A O   1 
ATOM   1984 C CB  . ALA A 1 270 ? -0.647  -24.258 12.131  1.00 32.87  ? 270 ALA A CB  1 
ATOM   1985 N N   . ALA A 1 271 ? 0.968   -21.638 12.926  1.00 30.60  ? 271 ALA A N   1 
ATOM   1986 C CA  . ALA A 1 271 ? 1.021   -20.396 13.688  1.00 29.91  ? 271 ALA A CA  1 
ATOM   1987 C C   . ALA A 1 271 ? 1.403   -19.217 12.804  1.00 29.75  ? 271 ALA A C   1 
ATOM   1988 O O   . ALA A 1 271 ? 0.935   -18.095 13.025  1.00 29.58  ? 271 ALA A O   1 
ATOM   1989 C CB  . ALA A 1 271 ? 2.011   -20.535 14.844  1.00 29.29  ? 271 ALA A CB  1 
ATOM   1990 N N   . LYS A 1 272 ? 2.278   -19.440 11.828  1.00 31.40  ? 272 LYS A N   1 
ATOM   1991 C CA  . LYS A 1 272 ? 2.638   -18.347 10.890  1.00 31.48  ? 272 LYS A CA  1 
ATOM   1992 C C   . LYS A 1 272 ? 1.407   -17.937 10.077  1.00 30.97  ? 272 LYS A C   1 
ATOM   1993 O O   . LYS A 1 272 ? 1.234   -16.749 9.812   1.00 27.34  ? 272 LYS A O   1 
ATOM   1994 C CB  . LYS A 1 272 ? 3.751   -18.771 9.932   1.00 34.71  ? 272 LYS A CB  1 
ATOM   1995 C CG  . LYS A 1 272 ? 4.299   -17.651 9.063   1.00 41.14  ? 272 LYS A CG  1 
ATOM   1996 C CD  . LYS A 1 272 ? 5.601   -17.992 8.385   1.00 45.05  ? 272 LYS A CD  1 
ATOM   1997 C CE  . LYS A 1 272 ? 6.272   -16.783 7.772   1.00 45.57  ? 272 LYS A CE  1 
ATOM   1998 N NZ  . LYS A 1 272 ? 7.213   -17.177 6.699   1.00 53.65  ? 272 LYS A NZ  1 
ATOM   1999 N N   . MET A 1 273 ? 0.584   -18.911 9.714   1.00 30.68  ? 273 MET A N   1 
ATOM   2000 C CA  . MET A 1 273 ? -0.621  -18.578 8.976   1.00 29.85  ? 273 MET A CA  1 
ATOM   2001 C C   . MET A 1 273 ? -1.587  -17.832 9.889   1.00 31.16  ? 273 MET A C   1 
ATOM   2002 O O   . MET A 1 273 ? -2.182  -16.828 9.491   1.00 30.95  ? 273 MET A O   1 
ATOM   2003 C CB  . MET A 1 273 ? -1.247  -19.870 8.440   1.00 31.26  ? 273 MET A CB  1 
ATOM   2004 C CG  . MET A 1 273 ? -0.733  -20.297 7.059   1.00 36.77  ? 273 MET A CG  1 
ATOM   2005 S SD  . MET A 1 273 ? -0.500  -19.040 5.805   1.00 33.27  ? 273 MET A SD  1 
ATOM   2006 C CE  . MET A 1 273 ? 1.232   -18.568 6.021   1.00 42.36  ? 273 MET A CE  1 
ATOM   2007 N N   . MET A 1 274 ? -1.671  -18.251 11.147  1.00 30.33  ? 274 MET A N   1 
ATOM   2008 C CA  . MET A 1 274 ? -2.517  -17.529 12.129  1.00 29.64  ? 274 MET A CA  1 
ATOM   2009 C C   . MET A 1 274 ? -1.988  -16.094 12.313  1.00 27.54  ? 274 MET A C   1 
ATOM   2010 O O   . MET A 1 274 ? -2.804  -15.183 12.374  1.00 29.63  ? 274 MET A O   1 
ATOM   2011 C CB  . MET A 1 274 ? -2.518  -18.248 13.481  1.00 32.73  ? 274 MET A CB  1 
ATOM   2012 C CG  . MET A 1 274 ? -3.805  -18.142 14.247  1.00 37.14  ? 274 MET A CG  1 
ATOM   2013 S SD  . MET A 1 274 ? -3.629  -19.032 15.807  1.00 44.79  ? 274 MET A SD  1 
ATOM   2014 C CE  . MET A 1 274 ? -2.951  -20.584 15.229  1.00 35.56  ? 274 MET A CE  1 
ATOM   2015 N N   . LEU A 1 275 ? -0.666  -15.925 12.411  1.00 29.52  ? 275 LEU A N   1 
ATOM   2016 C CA  . LEU A 1 275 ? -0.125  -14.574 12.581  1.00 28.67  ? 275 LEU A CA  1 
ATOM   2017 C C   . LEU A 1 275 ? -0.511  -13.675 11.416  1.00 28.52  ? 275 LEU A C   1 
ATOM   2018 O O   . LEU A 1 275 ? -0.916  -12.525 11.617  1.00 26.18  ? 275 LEU A O   1 
ATOM   2019 C CB  . LEU A 1 275 ? 1.396   -14.613 12.713  1.00 29.51  ? 275 LEU A CB  1 
ATOM   2020 C CG  . LEU A 1 275 ? 2.049   -13.250 12.959  1.00 29.44  ? 275 LEU A CG  1 
ATOM   2021 C CD1 . LEU A 1 275 ? 1.499   -12.568 14.226  1.00 30.05  ? 275 LEU A CD1 1 
ATOM   2022 C CD2 . LEU A 1 275 ? 3.572   -13.441 13.041  1.00 31.06  ? 275 LEU A CD2 1 
ATOM   2023 N N   . LEU A 1 276 ? -0.405  -14.190 10.190  1.00 28.79  ? 276 LEU A N   1 
ATOM   2024 C CA  . LEU A 1 276 ? -0.802  -13.406 9.023   1.00 26.39  ? 276 LEU A CA  1 
ATOM   2025 C C   . LEU A 1 276 ? -2.271  -13.013 9.106   1.00 26.91  ? 276 LEU A C   1 
ATOM   2026 O O   . LEU A 1 276 ? -2.636  -11.870 8.805   1.00 27.01  ? 276 LEU A O   1 
ATOM   2027 C CB  . LEU A 1 276 ? -0.536  -14.205 7.748   1.00 28.01  ? 276 LEU A CB  1 
ATOM   2028 C CG  . LEU A 1 276 ? -0.683  -13.463 6.410   1.00 26.24  ? 276 LEU A CG  1 
ATOM   2029 C CD1 . LEU A 1 276 ? 0.040   -12.116 6.416   1.00 26.24  ? 276 LEU A CD1 1 
ATOM   2030 C CD2 . LEU A 1 276 ? -0.226  -14.338 5.253   1.00 27.75  ? 276 LEU A CD2 1 
ATOM   2031 N N   . GLY A 1 277 ? -3.132  -13.950 9.507   1.00 26.69  ? 277 GLY A N   1 
ATOM   2032 C CA  . GLY A 1 277 ? -4.536  -13.617 9.687   1.00 27.61  ? 277 GLY A CA  1 
ATOM   2033 C C   . GLY A 1 277 ? -4.733  -12.519 10.712  1.00 28.10  ? 277 GLY A C   1 
ATOM   2034 O O   . GLY A 1 277 ? -5.494  -11.574 10.499  1.00 29.12  ? 277 GLY A O   1 
ATOM   2035 N N   . VAL A 1 278 ? -4.034  -12.624 11.843  1.00 25.46  ? 278 VAL A N   1 
ATOM   2036 C CA  . VAL A 1 278 ? -4.119  -11.583 12.863  1.00 26.17  ? 278 VAL A CA  1 
ATOM   2037 C C   . VAL A 1 278 ? -3.725  -10.228 12.292  1.00 26.68  ? 278 VAL A C   1 
ATOM   2038 O O   . VAL A 1 278 ? -4.376  -9.216  12.564  1.00 27.27  ? 278 VAL A O   1 
ATOM   2039 C CB  . VAL A 1 278 ? -3.257  -11.960 14.082  1.00 30.25  ? 278 VAL A CB  1 
ATOM   2040 C CG1 . VAL A 1 278 ? -3.115  -10.755 15.014  1.00 29.19  ? 278 VAL A CG1 1 
ATOM   2041 C CG2 . VAL A 1 278 ? -3.873  -13.144 14.819  1.00 29.89  ? 278 VAL A CG2 1 
ATOM   2042 N N   . ILE A 1 279 ? -2.644  -10.180 11.516  1.00 25.74  ? 279 ILE A N   1 
ATOM   2043 C CA  . ILE A 1 279 ? -2.173  -8.913  10.959  1.00 25.33  ? 279 ILE A CA  1 
ATOM   2044 C C   . ILE A 1 279 ? -3.221  -8.311  10.031  1.00 26.53  ? 279 ILE A C   1 
ATOM   2045 O O   . ILE A 1 279 ? -3.521  -7.103  10.083  1.00 26.19  ? 279 ILE A O   1 
ATOM   2046 C CB  . ILE A 1 279 ? -0.849  -9.123  10.205  1.00 25.37  ? 279 ILE A CB  1 
ATOM   2047 C CG1 . ILE A 1 279 ? 0.289   -9.510  11.152  1.00 29.95  ? 279 ILE A CG1 1 
ATOM   2048 C CG2 . ILE A 1 279 ? -0.485  -7.875  9.402   1.00 26.15  ? 279 ILE A CG2 1 
ATOM   2049 C CD1 . ILE A 1 279 ? 1.447   -10.172 10.400  1.00 29.25  ? 279 ILE A CD1 1 
ATOM   2050 N N   . VAL A 1 280 ? -3.780  -9.143  9.161   1.00 26.48  ? 280 VAL A N   1 
ATOM   2051 C CA  . VAL A 1 280 ? -4.741  -8.612  8.149   1.00 25.55  ? 280 VAL A CA  1 
ATOM   2052 C C   . VAL A 1 280 ? -5.993  -8.088  8.866   1.00 29.16  ? 280 VAL A C   1 
ATOM   2053 O O   . VAL A 1 280 ? -6.502  -7.038  8.483   1.00 29.04  ? 280 VAL A O   1 
ATOM   2054 C CB  . VAL A 1 280 ? -5.072  -9.681  7.091   1.00 27.13  ? 280 VAL A CB  1 
ATOM   2055 C CG1 . VAL A 1 280 ? -6.200  -9.251  6.171   1.00 30.11  ? 280 VAL A CG1 1 
ATOM   2056 C CG2 . VAL A 1 280 ? -3.840  -10.060 6.288   1.00 29.85  ? 280 VAL A CG2 1 
ATOM   2057 N N   . GLU A 1 281 ? -6.437  -8.802  9.887   1.00 27.57  ? 281 GLU A N   1 
ATOM   2058 C CA  . GLU A 1 281 ? -7.604  -8.352  10.677  1.00 29.17  ? 281 GLU A CA  1 
ATOM   2059 C C   . GLU A 1 281 ? -7.282  -7.029  11.383  1.00 29.83  ? 281 GLU A C   1 
ATOM   2060 O O   . GLU A 1 281 ? -8.142  -6.163  11.426  1.00 31.11  ? 281 GLU A O   1 
ATOM   2061 C CB  . GLU A 1 281 ? -7.977  -9.436  11.684  1.00 36.32  ? 281 GLU A CB  1 
ATOM   2062 C CG  . GLU A 1 281 ? -9.190  -9.090  12.524  1.00 41.17  ? 281 GLU A CG  1 
ATOM   2063 C CD  . GLU A 1 281 ? -10.350 -8.534  11.721  1.00 49.32  ? 281 GLU A CD  1 
ATOM   2064 O OE1 . GLU A 1 281 ? -11.032 -9.324  11.051  1.00 54.03  ? 281 GLU A OE1 1 
ATOM   2065 O OE2 . GLU A 1 281 ? -10.564 -7.311  11.763  1.00 54.90  ? 281 GLU A OE2 1 
ATOM   2066 N N   . GLN A 1 282 ? -6.068  -6.887  11.897  1.00 27.66  ? 282 GLN A N   1 
ATOM   2067 C CA  . GLN A 1 282 ? -5.683  -5.608  12.545  1.00 27.64  ? 282 GLN A CA  1 
ATOM   2068 C C   . GLN A 1 282 ? -5.656  -4.496  11.496  1.00 29.57  ? 282 GLN A C   1 
ATOM   2069 O O   . GLN A 1 282 ? -6.042  -3.375  11.832  1.00 30.02  ? 282 GLN A O   1 
ATOM   2070 C CB  . GLN A 1 282 ? -4.344  -5.694  13.275  1.00 26.91  ? 282 GLN A CB  1 
ATOM   2071 C CG  . GLN A 1 282 ? -4.400  -6.495  14.564  1.00 33.17  ? 282 GLN A CG  1 
ATOM   2072 C CD  . GLN A 1 282 ? -5.279  -5.836  15.596  1.00 37.03  ? 282 GLN A CD  1 
ATOM   2073 O OE1 . GLN A 1 282 ? -5.008  -4.733  16.057  1.00 33.07  ? 282 GLN A OE1 1 
ATOM   2074 N NE2 . GLN A 1 282 ? -6.348  -6.518  15.967  1.00 36.37  ? 282 GLN A NE2 1 
ATOM   2075 N N   . GLU A 1 283 ? -5.221  -4.816  10.281  1.00 28.71  ? 283 GLU A N   1 
ATOM   2076 C CA  . GLU A 1 283 ? -5.255  -3.791  9.246   1.00 28.74  ? 283 GLU A CA  1 
ATOM   2077 C C   . GLU A 1 283 ? -6.698  -3.395  8.944   1.00 29.52  ? 283 GLU A C   1 
ATOM   2078 O O   . GLU A 1 283 ? -7.001  -2.212  8.740   1.00 29.82  ? 283 GLU A O   1 
ATOM   2079 C CB  . GLU A 1 283 ? -4.552  -4.284  7.972   1.00 29.10  ? 283 GLU A CB  1 
ATOM   2080 C CG  . GLU A 1 283 ? -3.011  -4.216  8.031   1.00 27.34  ? 283 GLU A CG  1 
ATOM   2081 C CD  . GLU A 1 283 ? -2.334  -4.259  6.665   1.00 30.14  ? 283 GLU A CD  1 
ATOM   2082 O OE1 . GLU A 1 283 ? -3.025  -4.487  5.642   1.00 30.45  ? 283 GLU A OE1 1 
ATOM   2083 O OE2 . GLU A 1 283 ? -1.109  -3.990  6.595   1.00 28.43  ? 283 GLU A OE2 1 
ATOM   2084 N N   . SER A 1 284 ? -7.606  -4.380  8.929   1.00 29.33  ? 284 SER A N   1 
ATOM   2085 C CA  . SER A 1 284 ? -9.030  -4.099  8.766   1.00 29.16  ? 284 SER A CA  1 
ATOM   2086 C C   . SER A 1 284 ? -9.591  -3.319  9.950   1.00 32.08  ? 284 SER A C   1 
ATOM   2087 O O   . SER A 1 284 ? -10.361 -2.367  9.766   1.00 31.80  ? 284 SER A O   1 
ATOM   2088 C CB  . SER A 1 284 ? -9.792  -5.415  8.586   1.00 34.93  ? 284 SER A CB  1 
ATOM   2089 O OG  . SER A 1 284 ? -11.063 -5.168  8.035   1.00 43.67  ? 284 SER A OG  1 
ATOM   2090 N N   . LEU A 1 285 ? -9.228  -3.721  11.172  1.00 31.72  ? 285 LEU A N   1 
ATOM   2091 C CA  . LEU A 1 285 ? -9.686  -3.013  12.362  1.00 32.00  ? 285 LEU A CA  1 
ATOM   2092 C C   . LEU A 1 285 ? -9.289  -1.547  12.319  1.00 32.11  ? 285 LEU A C   1 
ATOM   2093 O O   . LEU A 1 285 ? -10.101 -0.668  12.628  1.00 31.47  ? 285 LEU A O   1 
ATOM   2094 C CB  . LEU A 1 285 ? -9.113  -3.669  13.621  1.00 28.73  ? 285 LEU A CB  1 
ATOM   2095 C CG  . LEU A 1 285 ? -9.597  -3.064  14.947  1.00 32.60  ? 285 LEU A CG  1 
ATOM   2096 C CD1 . LEU A 1 285 ? -11.116 -3.039  15.083  1.00 38.62  ? 285 LEU A CD1 1 
ATOM   2097 C CD2 . LEU A 1 285 ? -8.920  -3.761  16.131  1.00 34.36  ? 285 LEU A CD2 1 
ATOM   2098 N N   . ALA A 1 286 ? -8.036  -1.268  11.941  1.00 32.37  ? 286 ALA A N   1 
ATOM   2099 C CA  . ALA A 1 286 ? -7.592  0.113   11.818  1.00 30.50  ? 286 ALA A CA  1 
ATOM   2100 C C   . ALA A 1 286 ? -8.455  0.866   10.822  1.00 30.81  ? 286 ALA A C   1 
ATOM   2101 O O   . ALA A 1 286 ? -8.855  2.006   11.076  1.00 31.96  ? 286 ALA A O   1 
ATOM   2102 C CB  . ALA A 1 286 ? -6.120  0.166   11.405  1.00 29.91  ? 286 ALA A CB  1 
ATOM   2103 N N   . ALA A 1 287 ? -8.774  0.234   9.690   1.00 28.71  ? 287 ALA A N   1 
ATOM   2104 C CA  . ALA A 1 287 ? -9.618  0.889   8.700   1.00 32.61  ? 287 ALA A CA  1 
ATOM   2105 C C   . ALA A 1 287 ? -11.015 1.156   9.255   1.00 33.59  ? 287 ALA A C   1 
ATOM   2106 O O   . ALA A 1 287 ? -11.604 2.211   8.976   1.00 34.65  ? 287 ALA A O   1 
ATOM   2107 C CB  . ALA A 1 287 ? -9.680  0.047   7.425   1.00 34.28  ? 287 ALA A CB  1 
ATOM   2108 N N   . LYS A 1 288 ? -11.536 0.246   10.065  1.00 32.04  ? 288 LYS A N   1 
ATOM   2109 C CA  . LYS A 1 288 ? -12.872 0.468   10.665  1.00 35.79  ? 288 LYS A CA  1 
ATOM   2110 C C   . LYS A 1 288 ? -12.785 1.640   11.642  1.00 36.19  ? 288 LYS A C   1 
ATOM   2111 O O   . LYS A 1 288 ? -13.633 2.526   11.573  1.00 37.34  ? 288 LYS A O   1 
ATOM   2112 C CB  . LYS A 1 288 ? -13.382 -0.793  11.360  1.00 36.46  ? 288 LYS A CB  1 
ATOM   2113 C CG  . LYS A 1 288 ? -13.482 -2.034  10.489  1.00 42.60  ? 288 LYS A CG  1 
ATOM   2114 C CD  . LYS A 1 288 ? -13.491 -3.311  11.294  1.00 48.04  ? 288 LYS A CD  1 
ATOM   2115 C CE  . LYS A 1 288 ? -13.724 -4.545  10.451  1.00 48.72  ? 288 LYS A CE  1 
ATOM   2116 N NZ  . LYS A 1 288 ? -14.874 -5.331  10.950  1.00 54.10  ? 288 LYS A NZ  1 
ATOM   2117 N N   . LEU A 1 289 ? -11.766 1.639   12.496  1.00 35.78  ? 289 LEU A N   1 
ATOM   2118 C CA  . LEU A 1 289 ? -11.640 2.701   13.486  1.00 35.50  ? 289 LEU A CA  1 
ATOM   2119 C C   . LEU A 1 289 ? -11.452 4.065   12.831  1.00 35.96  ? 289 LEU A C   1 
ATOM   2120 O O   . LEU A 1 289 ? -11.959 5.075   13.333  1.00 37.32  ? 289 LEU A O   1 
ATOM   2121 C CB  . LEU A 1 289 ? -10.483 2.370   14.421  1.00 33.32  ? 289 LEU A CB  1 
ATOM   2122 C CG  . LEU A 1 289 ? -10.749 1.122   15.253  1.00 36.60  ? 289 LEU A CG  1 
ATOM   2123 C CD1 . LEU A 1 289 ? -9.506  0.663   15.987  1.00 34.42  ? 289 LEU A CD1 1 
ATOM   2124 C CD2 . LEU A 1 289 ? -11.859 1.430   16.243  1.00 39.84  ? 289 LEU A CD2 1 
ATOM   2125 N N   . LYS A 1 290 ? -10.710 4.125   11.723  1.00 31.50  ? 290 LYS A N   1 
ATOM   2126 C CA  . LYS A 1 290 ? -10.565 5.387   11.008  1.00 32.90  ? 290 LYS A CA  1 
ATOM   2127 C C   . LYS A 1 290 ? -11.896 5.844   10.426  1.00 39.63  ? 290 LYS A C   1 
ATOM   2128 O O   . LYS A 1 290 ? -12.236 7.031   10.477  1.00 39.72  ? 290 LYS A O   1 
ATOM   2129 C CB  . LYS A 1 290 ? -9.532  5.239   9.897   1.00 35.35  ? 290 LYS A CB  1 
ATOM   2130 C CG  . LYS A 1 290 ? -9.421  6.432   8.983   1.00 33.36  ? 290 LYS A CG  1 
ATOM   2131 C CD  . LYS A 1 290 ? -8.466  6.125   7.855   1.00 38.18  ? 290 LYS A CD  1 
ATOM   2132 C CE  . LYS A 1 290 ? -8.373  7.227   6.848   1.00 39.63  ? 290 LYS A CE  1 
ATOM   2133 N NZ  . LYS A 1 290 ? -7.518  6.802   5.709   1.00 43.45  ? 290 LYS A NZ  1 
ATOM   2134 N N   . GLU A 1 291 ? -12.654 4.910   9.854   1.00 39.14  ? 291 GLU A N   1 
ATOM   2135 C CA  . GLU A 1 291 ? -13.963 5.259   9.311   1.00 39.58  ? 291 GLU A CA  1 
ATOM   2136 C C   . GLU A 1 291 ? -14.902 5.735   10.416  1.00 42.29  ? 291 GLU A C   1 
ATOM   2137 O O   . GLU A 1 291 ? -15.690 6.666   10.209  1.00 42.62  ? 291 GLU A O   1 
ATOM   2138 C CB  . GLU A 1 291 ? -14.531 4.058   8.552   1.00 41.25  ? 291 GLU A CB  1 
ATOM   2139 C CG  . GLU A 1 291 ? -16.010 3.764   8.746   1.00 49.03  ? 291 GLU A CG  1 
ATOM   2140 C CD  . GLU A 1 291 ? -16.445 2.515   7.981   1.00 48.83  ? 291 GLU A CD  1 
ATOM   2141 O OE1 . GLU A 1 291 ? -16.461 2.554   6.731   1.00 48.47  ? 291 GLU A OE1 1 
ATOM   2142 O OE2 . GLU A 1 291 ? -16.740 1.485   8.633   1.00 54.08  ? 291 GLU A OE2 1 
ATOM   2143 N N   . GLU A 1 292 ? -14.767 5.154   11.603  1.00 40.63  ? 292 GLU A N   1 
ATOM   2144 C CA  . GLU A 1 292 ? -15.594 5.597   12.752  1.00 44.34  ? 292 GLU A CA  1 
ATOM   2145 C C   . GLU A 1 292 ? -15.207 7.031   13.135  1.00 45.11  ? 292 GLU A C   1 
ATOM   2146 O O   . GLU A 1 292 ? -16.116 7.836   13.352  1.00 45.19  ? 292 GLU A O   1 
ATOM   2147 C CB  . GLU A 1 292 ? -15.447 4.639   13.928  1.00 43.08  ? 292 GLU A CB  1 
ATOM   2148 C CG  . GLU A 1 292 ? -16.178 3.328   13.729  1.00 49.09  ? 292 GLU A CG  1 
ATOM   2149 C CD  . GLU A 1 292 ? -17.650 3.481   13.390  1.00 58.06  ? 292 GLU A CD  1 
ATOM   2150 O OE1 . GLU A 1 292 ? -18.348 4.211   14.117  1.00 54.45  ? 292 GLU A OE1 1 
ATOM   2151 O OE2 . GLU A 1 292 ? -18.093 2.872   12.398  1.00 60.22  ? 292 GLU A OE2 1 
ATOM   2152 N N   . ARG A 1 293 ? -13.911 7.336   13.211  1.00 40.21  ? 293 ARG A N   1 
ATOM   2153 C CA  . ARG A 1 293 ? -13.488 8.676   13.615  1.00 38.96  ? 293 ARG A CA  1 
ATOM   2154 C C   . ARG A 1 293 ? -13.909 9.728   12.595  1.00 42.13  ? 293 ARG A C   1 
ATOM   2155 O O   . ARG A 1 293 ? -14.303 10.841  12.968  1.00 41.81  ? 293 ARG A O   1 
ATOM   2156 C CB  . ARG A 1 293 ? -11.973 8.713   13.817  1.00 39.87  ? 293 ARG A CB  1 
ATOM   2157 C CG  . ARG A 1 293 ? -11.414 10.111  14.093  1.00 39.59  ? 293 ARG A CG  1 
ATOM   2158 C CD  . ARG A 1 293 ? -11.960 10.661  15.403  1.00 41.37  ? 293 ARG A CD  1 
ATOM   2159 N NE  . ARG A 1 293 ? -11.464 11.998  15.727  1.00 38.51  ? 293 ARG A NE  1 
ATOM   2160 C CZ  . ARG A 1 293 ? -11.784 13.112  15.082  1.00 43.53  ? 293 ARG A CZ  1 
ATOM   2161 N NH1 . ARG A 1 293 ? -12.621 13.105  14.056  1.00 44.17  ? 293 ARG A NH1 1 
ATOM   2162 N NH2 . ARG A 1 293 ? -11.271 14.270  15.492  1.00 42.27  ? 293 ARG A NH2 1 
ATOM   2163 N N   . LEU A 1 294 ? -13.844 9.395   11.303  1.00 42.38  ? 294 LEU A N   1 
ATOM   2164 C CA  . LEU A 1 294 ? -14.147 10.348  10.239  1.00 43.86  ? 294 LEU A CA  1 
ATOM   2165 C C   . LEU A 1 294 ? -15.640 10.623  10.087  1.00 43.09  ? 294 LEU A C   1 
ATOM   2166 O O   . LEU A 1 294 ? -16.010 11.433  9.233   1.00 45.39  ? 294 LEU A O   1 
ATOM   2167 C CB  . LEU A 1 294 ? -13.558 9.851   8.914   1.00 41.89  ? 294 LEU A CB  1 
ATOM   2168 C CG  . LEU A 1 294 ? -12.025 9.909   8.804   1.00 39.99  ? 294 LEU A CG  1 
ATOM   2169 C CD1 . LEU A 1 294 ? -11.567 9.915   7.354   1.00 47.01  ? 294 LEU A CD1 1 
ATOM   2170 C CD2 . LEU A 1 294 ? -11.497 11.147  9.516   1.00 43.81  ? 294 LEU A CD2 1 
ATOM   2171 N N   . LYS A 1 295 ? -16.464 10.048  10.954  1.00 43.81  ? 295 LYS A N   1 
ATOM   2172 C CA  . LYS A 1 295 ? -17.905 10.402  10.953  1.00 48.17  ? 295 LYS A CA  1 
ATOM   2173 C C   . LYS A 1 295 ? -18.052 11.740  11.688  1.00 50.23  ? 295 LYS A C   1 
ATOM   2174 O O   . LYS A 1 295 ? -19.081 12.394  11.483  1.00 53.54  ? 295 LYS A O   1 
ATOM   2175 C CB  . LYS A 1 295 ? -18.706 9.293   11.627  1.00 48.11  ? 295 LYS A CB  1 
ATOM   2176 C CG  . LYS A 1 295 ? -18.671 7.936   10.944  1.00 49.48  ? 295 LYS A CG  1 
ATOM   2177 C CD  . LYS A 1 295 ? -18.976 6.814   11.908  1.00 49.34  ? 295 LYS A CD  1 
ATOM   2178 C CE  . LYS A 1 295 ? -20.011 5.842   11.388  1.00 54.20  ? 295 LYS A CE  1 
ATOM   2179 N NZ  . LYS A 1 295 ? -20.500 4.944   12.460  1.00 57.92  ? 295 LYS A NZ  1 
ATOM   2180 N N   . LYS A 1 296 ? -17.074 12.117  12.516  1.00 45.69  ? 296 LYS A N   1 
ATOM   2181 C CA  . LYS A 1 296 ? -17.044 13.379  13.236  1.00 47.26  ? 296 LYS A CA  1 
ATOM   2182 C C   . LYS A 1 296 ? -16.062 14.333  12.575  1.00 49.21  ? 296 LYS A C   1 
ATOM   2183 O O   . LYS A 1 296 ? -15.172 13.908  11.833  1.00 46.31  ? 296 LYS A O   1 
ATOM   2184 C CB  . LYS A 1 296 ? -16.645 13.145  14.700  1.00 51.98  ? 296 LYS A CB  1 
ATOM   2185 C CG  . LYS A 1 296 ? -17.781 12.592  15.562  1.00 54.06  ? 296 LYS A CG  1 
ATOM   2186 C CD  . LYS A 1 296 ? -17.731 13.126  16.993  1.00 58.89  ? 296 LYS A CD  1 
ATOM   2187 C CE  . LYS A 1 296 ? -17.289 12.060  17.984  1.00 56.20  ? 296 LYS A CE  1 
ATOM   2188 N NZ  . LYS A 1 296 ? -17.087 12.628  19.353  1.00 58.34  ? 296 LYS A NZ  1 
ATOM   2189 N N   . PRO A 1 297 ? -16.212 15.641  12.791  1.00 51.06  ? 297 PRO A N   1 
ATOM   2190 C CA  . PRO A 1 297 ? -15.256 16.590  12.209  1.00 46.94  ? 297 PRO A CA  1 
ATOM   2191 C C   . PRO A 1 297 ? -13.825 16.252  12.600  1.00 44.50  ? 297 PRO A C   1 
ATOM   2192 O O   . PRO A 1 297 ? -13.543 15.878  13.741  1.00 41.41  ? 297 PRO A O   1 
ATOM   2193 C CB  . PRO A 1 297 ? -15.699 17.932  12.797  1.00 48.24  ? 297 PRO A CB  1 
ATOM   2194 C CG  . PRO A 1 297 ? -17.194 17.771  12.888  1.00 52.02  ? 297 PRO A CG  1 
ATOM   2195 C CD  . PRO A 1 297 ? -17.401 16.332  13.328  1.00 50.95  ? 297 PRO A CD  1 
ATOM   2196 N N   . ALA A 1 298 ? -12.921 16.394  11.632  1.00 45.69  ? 298 ALA A N   1 
ATOM   2197 C CA  . ALA A 1 298 ? -11.527 16.012  11.795  1.00 43.52  ? 298 ALA A CA  1 
ATOM   2198 C C   . ALA A 1 298 ? -10.627 17.140  11.315  1.00 42.90  ? 298 ALA A C   1 
ATOM   2199 O O   . ALA A 1 298 ? -10.744 17.589  10.168  1.00 44.08  ? 298 ALA A O   1 
ATOM   2200 C CB  . ALA A 1 298 ? -11.221 14.717  11.027  1.00 45.08  ? 298 ALA A CB  1 
ATOM   2201 N N   . SER A 1 299 ? -9.726  17.583  12.190  1.00 41.92  ? 299 SER A N   1 
ATOM   2202 C CA  . SER A 1 299 ? -8.787  18.631  11.829  1.00 41.97  ? 299 SER A CA  1 
ATOM   2203 C C   . SER A 1 299 ? -7.827  18.143  10.750  1.00 42.52  ? 299 SER A C   1 
ATOM   2204 O O   . SER A 1 299 ? -7.680  16.940  10.499  1.00 40.07  ? 299 SER A O   1 
ATOM   2205 C CB  . SER A 1 299 ? -7.985  19.081  13.050  1.00 41.37  ? 299 SER A CB  1 
ATOM   2206 O OG  . SER A 1 299 ? -7.227  18.000  13.577  1.00 43.65  ? 299 SER A OG  1 
ATOM   2207 N N   . LYS A 1 300 ? -7.156  19.103  10.114  1.00 40.80  ? 300 LYS A N   1 
ATOM   2208 C CA  . LYS A 1 300 ? -6.104  18.758  9.166   1.00 39.58  ? 300 LYS A CA  1 
ATOM   2209 C C   . LYS A 1 300 ? -5.030  17.901  9.838   1.00 37.88  ? 300 LYS A C   1 
ATOM   2210 O O   . LYS A 1 300 ? -4.464  16.997  9.215   1.00 38.41  ? 300 LYS A O   1 
ATOM   2211 C CB  . LYS A 1 300 ? -5.496  20.032  8.586   1.00 41.02  ? 300 LYS A CB  1 
ATOM   2212 C CG  . LYS A 1 300 ? -4.150  19.841  7.918   1.00 48.46  ? 300 LYS A CG  1 
ATOM   2213 C CD  . LYS A 1 300 ? -3.324  21.118  7.950   1.00 52.38  ? 300 LYS A CD  1 
ATOM   2214 C CE  . LYS A 1 300 ? -2.359  21.182  6.773   1.00 52.84  ? 300 LYS A CE  1 
ATOM   2215 N NZ  . LYS A 1 300 ? -1.097  21.886  7.158   1.00 62.09  ? 300 LYS A NZ  1 
ATOM   2216 N N   . GLU A 1 301 ? -4.750  18.162  11.115  1.00 38.66  ? 301 GLU A N   1 
ATOM   2217 C CA  . GLU A 1 301 ? -3.759  17.360  11.829  1.00 37.59  ? 301 GLU A CA  1 
ATOM   2218 C C   . GLU A 1 301 ? -4.190  15.899  11.933  1.00 36.06  ? 301 GLU A C   1 
ATOM   2219 O O   . GLU A 1 301 ? -3.378  14.988  11.721  1.00 34.30  ? 301 GLU A O   1 
ATOM   2220 C CB  . GLU A 1 301 ? -3.521  17.961  13.211  1.00 36.02  ? 301 GLU A CB  1 
ATOM   2221 C CG  . GLU A 1 301 ? -2.707  19.249  13.189  1.00 36.87  ? 301 GLU A CG  1 
ATOM   2222 C CD  . GLU A 1 301 ? -3.493  20.417  12.585  1.00 47.59  ? 301 GLU A CD  1 
ATOM   2223 O OE1 . GLU A 1 301 ? -4.708  20.537  12.869  1.00 45.22  ? 301 GLU A OE1 1 
ATOM   2224 O OE2 . GLU A 1 301 ? -2.889  21.228  11.847  1.00 48.20  ? 301 GLU A OE2 1 
ATOM   2225 N N   . ILE A 1 302 ? -5.468  15.651  12.245  1.00 36.95  ? 302 ILE A N   1 
ATOM   2226 C CA  . ILE A 1 302 ? -5.964  14.275  12.291  1.00 38.91  ? 302 ILE A CA  1 
ATOM   2227 C C   . ILE A 1 302 ? -5.839  13.624  10.916  1.00 37.37  ? 302 ILE A C   1 
ATOM   2228 O O   . ILE A 1 302 ? -5.384  12.477  10.793  1.00 34.85  ? 302 ILE A O   1 
ATOM   2229 C CB  . ILE A 1 302 ? -7.421  14.242  12.797  1.00 39.80  ? 302 ILE A CB  1 
ATOM   2230 C CG1 . ILE A 1 302 ? -7.481  14.426  14.316  1.00 37.67  ? 302 ILE A CG1 1 
ATOM   2231 C CG2 . ILE A 1 302 ? -8.088  12.920  12.415  1.00 39.95  ? 302 ILE A CG2 1 
ATOM   2232 C CD1 . ILE A 1 302 ? -7.261  13.174  15.108  1.00 43.27  ? 302 ILE A CD1 1 
ATOM   2233 N N   . LEU A 1 303 ? -6.157  14.376  9.873   1.00 36.54  ? 303 LEU A N   1 
ATOM   2234 C CA  . LEU A 1 303 ? -6.112  13.793  8.512   1.00 35.54  ? 303 LEU A CA  1 
ATOM   2235 C C   . LEU A 1 303 ? -4.656  13.530  8.104   1.00 34.89  ? 303 LEU A C   1 
ATOM   2236 O O   . LEU A 1 303 ? -4.406  12.507  7.475   1.00 32.29  ? 303 LEU A O   1 
ATOM   2237 C CB  . LEU A 1 303 ? -6.833  14.733  7.543   1.00 36.00  ? 303 LEU A CB  1 
ATOM   2238 C CG  . LEU A 1 303 ? -8.289  15.007  7.906   1.00 39.25  ? 303 LEU A CG  1 
ATOM   2239 C CD1 . LEU A 1 303 ? -8.852  16.150  7.081   1.00 44.57  ? 303 LEU A CD1 1 
ATOM   2240 C CD2 . LEU A 1 303 ? -9.126  13.752  7.729   1.00 41.64  ? 303 LEU A CD2 1 
ATOM   2241 N N   . GLN A 1 304 ? -3.743  14.416  8.487   1.00 35.46  ? 304 GLN A N   1 
ATOM   2242 C CA  . GLN A 1 304 ? -2.315  14.246  8.118   1.00 35.12  ? 304 GLN A CA  1 
ATOM   2243 C C   . GLN A 1 304 ? -1.768  12.989  8.800   1.00 30.31  ? 304 GLN A C   1 
ATOM   2244 O O   . GLN A 1 304 ? -1.028  12.252  8.166   1.00 32.14  ? 304 GLN A O   1 
ATOM   2245 C CB  . GLN A 1 304 ? -1.458  15.429  8.558   1.00 40.13  ? 304 GLN A CB  1 
ATOM   2246 C CG  . GLN A 1 304 ? -1.642  16.711  7.770   1.00 43.99  ? 304 GLN A CG  1 
ATOM   2247 C CD  . GLN A 1 304 ? -0.762  17.781  8.367   1.00 47.94  ? 304 GLN A CD  1 
ATOM   2248 O OE1 . GLN A 1 304 ? -0.891  18.133  9.536   1.00 51.75  ? 304 GLN A OE1 1 
ATOM   2249 N NE2 . GLN A 1 304 ? 0.166   18.284  7.573   1.00 39.66  ? 304 GLN A NE2 1 
ATOM   2250 N N   . TYR A 1 305 ? -2.122  12.787  10.061  1.00 30.19  ? 305 TYR A N   1 
ATOM   2251 C CA  . TYR A 1 305 ? -1.578  11.624  10.803  1.00 30.40  ? 305 TYR A CA  1 
ATOM   2252 C C   . TYR A 1 305 ? -2.095  10.327  10.177  1.00 31.82  ? 305 TYR A C   1 
ATOM   2253 O O   . TYR A 1 305 ? -1.325  9.389   10.017  1.00 29.81  ? 305 TYR A O   1 
ATOM   2254 C CB  . TYR A 1 305 ? -1.943  11.678  12.284  1.00 31.98  ? 305 TYR A CB  1 
ATOM   2255 C CG  . TYR A 1 305 ? -1.286  10.594  13.097  1.00 29.84  ? 305 TYR A CG  1 
ATOM   2256 C CD1 . TYR A 1 305 ? 0.085   10.573  13.271  1.00 33.62  ? 305 TYR A CD1 1 
ATOM   2257 C CD2 . TYR A 1 305 ? -2.025  9.569   13.659  1.00 28.14  ? 305 TYR A CD2 1 
ATOM   2258 C CE1 . TYR A 1 305 ? 0.705   9.576   14.001  1.00 30.75  ? 305 TYR A CE1 1 
ATOM   2259 C CE2 . TYR A 1 305 ? -1.421  8.563   14.394  1.00 28.80  ? 305 TYR A CE2 1 
ATOM   2260 C CZ  . TYR A 1 305 ? -0.051  8.568   14.566  1.00 32.29  ? 305 TYR A CZ  1 
ATOM   2261 O OH  . TYR A 1 305 ? 0.560   7.586   15.286  1.00 31.82  ? 305 TYR A OH  1 
ATOM   2262 N N   . PHE A 1 306 ? -3.388  10.299  9.863   1.00 29.95  ? 306 PHE A N   1 
ATOM   2263 C CA  . PHE A 1 306 ? -3.950  9.104   9.197   1.00 31.78  ? 306 PHE A CA  1 
ATOM   2264 C C   . PHE A 1 306 ? -3.133  8.823   7.937   1.00 31.10  ? 306 PHE A C   1 
ATOM   2265 O O   . PHE A 1 306 ? -2.682  7.694   7.771   1.00 31.66  ? 306 PHE A O   1 
ATOM   2266 C CB  . PHE A 1 306 ? -5.424  9.301   8.847   1.00 29.33  ? 306 PHE A CB  1 
ATOM   2267 C CG  . PHE A 1 306 ? -6.409  9.074   9.963   1.00 31.35  ? 306 PHE A CG  1 
ATOM   2268 C CD1 . PHE A 1 306 ? -6.226  8.054   10.879  1.00 35.38  ? 306 PHE A CD1 1 
ATOM   2269 C CD2 . PHE A 1 306 ? -7.534  9.871   10.079  1.00 33.55  ? 306 PHE A CD2 1 
ATOM   2270 C CE1 . PHE A 1 306 ? -7.141  7.846   11.897  1.00 35.34  ? 306 PHE A CE1 1 
ATOM   2271 C CE2 . PHE A 1 306 ? -8.449  9.660   11.095  1.00 34.40  ? 306 PHE A CE2 1 
ATOM   2272 C CZ  . PHE A 1 306 ? -8.251  8.649   12.003  1.00 37.00  ? 306 PHE A CZ  1 
ATOM   2273 N N   . GLU A 1 307 ? -2.947  9.833   7.088   1.00 30.08  ? 307 GLU A N   1 
ATOM   2274 C CA  . GLU A 1 307 ? -2.262  9.569   5.829   1.00 32.22  ? 307 GLU A CA  1 
ATOM   2275 C C   . GLU A 1 307 ? -0.820  9.129   6.070   1.00 33.28  ? 307 GLU A C   1 
ATOM   2276 O O   . GLU A 1 307 ? -0.337  8.172   5.449   1.00 31.80  ? 307 GLU A O   1 
ATOM   2277 C CB  . GLU A 1 307 ? -2.314  10.813  4.952   1.00 35.76  ? 307 GLU A CB  1 
ATOM   2278 C CG  . GLU A 1 307 ? -1.877  10.594  3.524   1.00 42.84  ? 307 GLU A CG  1 
ATOM   2279 C CD  . GLU A 1 307 ? -1.926  11.884  2.720   1.00 46.99  ? 307 GLU A CD  1 
ATOM   2280 O OE1 . GLU A 1 307 ? -2.763  12.745  3.058   1.00 44.93  ? 307 GLU A OE1 1 
ATOM   2281 O OE2 . GLU A 1 307 ? -1.136  12.030  1.762   1.00 49.64  ? 307 GLU A OE2 1 
ATOM   2282 N N   . ALA A 1 308 ? -0.132  9.793   7.001   1.00 28.86  ? 308 ALA A N   1 
ATOM   2283 C CA  . ALA A 1 308 ? 1.289   9.530   7.193   1.00 29.74  ? 308 ALA A CA  1 
ATOM   2284 C C   . ALA A 1 308 ? 1.528   8.200   7.887   1.00 27.55  ? 308 ALA A C   1 
ATOM   2285 O O   . ALA A 1 308 ? 2.517   7.519   7.593   1.00 26.68  ? 308 ALA A O   1 
ATOM   2286 C CB  . ALA A 1 308 ? 1.935   10.644  8.007   1.00 28.63  ? 308 ALA A CB  1 
ATOM   2287 N N   . ILE A 1 309 ? 0.664   7.834   8.836   1.00 27.20  ? 309 ILE A N   1 
ATOM   2288 C CA  . ILE A 1 309 ? 0.863   6.568   9.539   1.00 27.06  ? 309 ILE A CA  1 
ATOM   2289 C C   . ILE A 1 309 ? 0.469   5.398   8.638   1.00 25.73  ? 309 ILE A C   1 
ATOM   2290 O O   . ILE A 1 309 ? 1.036   4.309   8.748   1.00 28.28  ? 309 ILE A O   1 
ATOM   2291 C CB  . ILE A 1 309 ? 0.095   6.563   10.881  1.00 30.86  ? 309 ILE A CB  1 
ATOM   2292 C CG1 . ILE A 1 309 ? 0.744   5.641   11.924  1.00 38.14  ? 309 ILE A CG1 1 
ATOM   2293 C CG2 . ILE A 1 309 ? -1.360  6.217   10.703  1.00 33.57  ? 309 ILE A CG2 1 
ATOM   2294 C CD1 . ILE A 1 309 ? 2.188   6.012   12.296  1.00 30.05  ? 309 ILE A CD1 1 
ATOM   2295 N N   . GLU A 1 310 ? -0.439  5.610   7.697   1.00 28.13  ? 310 GLU A N   1 
ATOM   2296 C CA  . GLU A 1 310 ? -0.720  4.507   6.745   1.00 26.68  ? 310 GLU A CA  1 
ATOM   2297 C C   . GLU A 1 310 ? 0.512   4.316   5.850   1.00 26.41  ? 310 GLU A C   1 
ATOM   2298 O O   . GLU A 1 310 ? 0.864   3.172   5.581   1.00 27.59  ? 310 GLU A O   1 
ATOM   2299 C CB  . GLU A 1 310 ? -2.002  4.785   5.963   1.00 29.53  ? 310 GLU A CB  1 
ATOM   2300 C CG  . GLU A 1 310 ? -3.240  4.703   6.835   1.00 31.77  ? 310 GLU A CG  1 
ATOM   2301 C CD  . GLU A 1 310 ? -4.556  4.973   6.131   1.00 38.07  ? 310 GLU A CD  1 
ATOM   2302 O OE1 . GLU A 1 310 ? -4.536  5.173   4.916   1.00 39.85  ? 310 GLU A OE1 1 
ATOM   2303 O OE2 . GLU A 1 310 ? -5.595  4.972   6.805   1.00 37.16  ? 310 GLU A OE2 1 
ATOM   2304 N N   . LEU A 1 311 ? 1.136   5.404   5.409   1.00 25.41  ? 311 LEU A N   1 
ATOM   2305 C CA  . LEU A 1 311 ? 2.369   5.265   4.630   1.00 26.37  ? 311 LEU A CA  1 
ATOM   2306 C C   . LEU A 1 311 ? 3.469   4.598   5.447   1.00 27.11  ? 311 LEU A C   1 
ATOM   2307 O O   . LEU A 1 311 ? 4.287   3.842   4.902   1.00 26.59  ? 311 LEU A O   1 
ATOM   2308 C CB  . LEU A 1 311 ? 2.850   6.634   4.144   1.00 24.20  ? 311 LEU A CB  1 
ATOM   2309 C CG  . LEU A 1 311 ? 2.004   7.146   2.975   1.00 27.75  ? 311 LEU A CG  1 
ATOM   2310 C CD1 . LEU A 1 311 ? 2.100   8.671   2.909   1.00 32.12  ? 311 LEU A CD1 1 
ATOM   2311 C CD2 . LEU A 1 311 ? 2.455   6.472   1.691   1.00 30.38  ? 311 LEU A CD2 1 
ATOM   2312 N N   . TYR A 1 312 ? 3.510   4.870   6.744   1.00 26.22  ? 312 TYR A N   1 
ATOM   2313 C CA  . TYR A 1 312 ? 4.547   4.257   7.608   1.00 25.53  ? 312 TYR A CA  1 
ATOM   2314 C C   . TYR A 1 312 ? 4.321   2.748   7.667   1.00 26.99  ? 312 TYR A C   1 
ATOM   2315 O O   . TYR A 1 312 ? 5.268   1.990   7.487   1.00 27.67  ? 312 TYR A O   1 
ATOM   2316 C CB  . TYR A 1 312 ? 4.537   4.866   9.009   1.00 26.31  ? 312 TYR A CB  1 
ATOM   2317 C CG  . TYR A 1 312 ? 5.422   4.161   9.999   1.00 26.75  ? 312 TYR A CG  1 
ATOM   2318 C CD1 . TYR A 1 312 ? 6.797   4.283   9.934   1.00 30.74  ? 312 TYR A CD1 1 
ATOM   2319 C CD2 . TYR A 1 312 ? 4.884   3.361   10.988  1.00 30.51  ? 312 TYR A CD2 1 
ATOM   2320 C CE1 . TYR A 1 312 ? 7.620   3.629   10.832  1.00 31.91  ? 312 TYR A CE1 1 
ATOM   2321 C CE2 . TYR A 1 312 ? 5.692   2.702   11.895  1.00 30.42  ? 312 TYR A CE2 1 
ATOM   2322 C CZ  . TYR A 1 312 ? 7.065   2.831   11.813  1.00 28.63  ? 312 TYR A CZ  1 
ATOM   2323 O OH  . TYR A 1 312 ? 7.864   2.180   12.702  1.00 32.85  ? 312 TYR A OH  1 
ATOM   2324 N N   . VAL A 1 313 ? 3.078   2.342   7.896   1.00 25.48  ? 313 VAL A N   1 
ATOM   2325 C CA  . VAL A 1 313 ? 2.807   0.908   8.045   1.00 26.79  ? 313 VAL A CA  1 
ATOM   2326 C C   . VAL A 1 313 ? 2.888   0.195   6.700   1.00 27.33  ? 313 VAL A C   1 
ATOM   2327 O O   . VAL A 1 313 ? 3.466   -0.895  6.591   1.00 27.29  ? 313 VAL A O   1 
ATOM   2328 C CB  . VAL A 1 313 ? 1.437   0.693   8.715   1.00 28.39  ? 313 VAL A CB  1 
ATOM   2329 C CG1 . VAL A 1 313 ? 0.992   -0.768  8.588   1.00 31.99  ? 313 VAL A CG1 1 
ATOM   2330 C CG2 . VAL A 1 313 ? 1.494   1.133   10.167  1.00 30.08  ? 313 VAL A CG2 1 
ATOM   2331 N N   . GLY A 1 314 ? 2.268   0.762   5.661   1.00 28.98  ? 314 GLY A N   1 
ATOM   2332 C CA  . GLY A 1 314 ? 2.383   0.153   4.344   1.00 28.70  ? 314 GLY A CA  1 
ATOM   2333 C C   . GLY A 1 314 ? 3.818   0.154   3.854   1.00 28.06  ? 314 GLY A C   1 
ATOM   2334 O O   . GLY A 1 314 ? 4.296   -0.832  3.283   1.00 26.97  ? 314 GLY A O   1 
ATOM   2335 N N   . GLY A 1 315 ? 4.540   1.244   4.111   1.00 27.46  ? 315 GLY A N   1 
ATOM   2336 C CA  . GLY A 1 315 ? 5.939   1.295   3.720   1.00 29.63  ? 315 GLY A CA  1 
ATOM   2337 C C   . GLY A 1 315 ? 6.791   0.262   4.434   1.00 29.00  ? 315 GLY A C   1 
ATOM   2338 O O   . GLY A 1 315 ? 7.692   -0.334  3.835   1.00 28.59  ? 315 GLY A O   1 
ATOM   2339 N N   . SER A 1 316 ? 6.537   0.049   5.726   1.00 27.28  ? 316 SER A N   1 
ATOM   2340 C CA  . SER A 1 316 ? 7.270   -0.996  6.434   1.00 27.07  ? 316 SER A CA  1 
ATOM   2341 C C   . SER A 1 316 ? 7.000   -2.362  5.823   1.00 28.00  ? 316 SER A C   1 
ATOM   2342 O O   . SER A 1 316 ? 7.929   -3.148  5.613   1.00 29.83  ? 316 SER A O   1 
ATOM   2343 C CB  . SER A 1 316 ? 6.909   -0.986  7.912   1.00 29.83  ? 316 SER A CB  1 
ATOM   2344 O OG  . SER A 1 316 ? 7.718   -1.921  8.610   1.00 27.47  ? 316 SER A OG  1 
ATOM   2345 N N   . CYS A 1 317 ? 5.737   -2.655  5.501   1.00 25.54  ? 317 CYS A N   1 
ATOM   2346 C CA  . CYS A 1 317 ? 5.439   -3.922  4.829   1.00 27.19  ? 317 CYS A CA  1 
ATOM   2347 C C   . CYS A 1 317 ? 6.176   -4.023  3.499   1.00 29.46  ? 317 CYS A C   1 
ATOM   2348 O O   . CYS A 1 317 ? 6.749   -5.072  3.173   1.00 30.27  ? 317 CYS A O   1 
ATOM   2349 C CB  . CYS A 1 317 ? 3.937   -4.070  4.613   1.00 27.13  ? 317 CYS A CB  1 
ATOM   2350 S SG  . CYS A 1 317 ? 3.505   -5.790  4.105   1.00 28.97  ? 317 CYS A SG  1 
ATOM   2351 N N   . TYR A 1 318 ? 6.175   -2.936  2.721   1.00 28.50  ? 318 TYR A N   1 
ATOM   2352 C CA  . TYR A 1 318 ? 6.884   -2.924  1.445   1.00 29.43  ? 318 TYR A CA  1 
ATOM   2353 C C   . TYR A 1 318 ? 8.375   -3.172  1.631   1.00 30.59  ? 318 TYR A C   1 
ATOM   2354 O O   . TYR A 1 318 ? 8.979   -3.960  0.892   1.00 31.10  ? 318 TYR A O   1 
ATOM   2355 C CB  . TYR A 1 318 ? 6.651   -1.593  0.741   1.00 29.95  ? 318 TYR A CB  1 
ATOM   2356 C CG  . TYR A 1 318 ? 7.291   -1.485  -0.615  1.00 31.72  ? 318 TYR A CG  1 
ATOM   2357 C CD1 . TYR A 1 318 ? 6.615   -1.896  -1.759  1.00 35.73  ? 318 TYR A CD1 1 
ATOM   2358 C CD2 . TYR A 1 318 ? 8.580   -0.994  -0.756  1.00 32.11  ? 318 TYR A CD2 1 
ATOM   2359 C CE1 . TYR A 1 318 ? 7.198   -1.786  -3.010  1.00 37.61  ? 318 TYR A CE1 1 
ATOM   2360 C CE2 . TYR A 1 318 ? 9.174   -0.885  -2.003  1.00 35.73  ? 318 TYR A CE2 1 
ATOM   2361 C CZ  . TYR A 1 318 ? 8.476   -1.284  -3.126  1.00 40.00  ? 318 TYR A CZ  1 
ATOM   2362 O OH  . TYR A 1 318 ? 9.060   -1.175  -4.370  1.00 42.91  ? 318 TYR A OH  1 
ATOM   2363 N N   . TRP A 1 319 ? 9.002   -2.491  2.599   1.00 29.09  ? 319 TRP A N   1 
ATOM   2364 C CA  . TRP A 1 319 ? 10.431  -2.696  2.805   1.00 30.82  ? 319 TRP A CA  1 
ATOM   2365 C C   . TRP A 1 319 ? 10.739  -4.145  3.169   1.00 32.70  ? 319 TRP A C   1 
ATOM   2366 O O   . TRP A 1 319 ? 11.656  -4.760  2.612   1.00 34.44  ? 319 TRP A O   1 
ATOM   2367 C CB  . TRP A 1 319 ? 10.962  -1.745  3.885   1.00 30.10  ? 319 TRP A CB  1 
ATOM   2368 C CG  . TRP A 1 319 ? 12.458  -1.809  3.926   1.00 30.88  ? 319 TRP A CG  1 
ATOM   2369 C CD1 . TRP A 1 319 ? 13.320  -1.125  3.123   1.00 35.51  ? 319 TRP A CD1 1 
ATOM   2370 C CD2 . TRP A 1 319 ? 13.266  -2.600  4.803   1.00 33.73  ? 319 TRP A CD2 1 
ATOM   2371 N NE1 . TRP A 1 319 ? 14.616  -1.452  3.439   1.00 35.13  ? 319 TRP A NE1 1 
ATOM   2372 C CE2 . TRP A 1 319 ? 14.607  -2.358  4.462   1.00 32.78  ? 319 TRP A CE2 1 
ATOM   2373 C CE3 . TRP A 1 319 ? 12.982  -3.511  5.823   1.00 38.31  ? 319 TRP A CE3 1 
ATOM   2374 C CZ2 . TRP A 1 319 ? 15.672  -2.969  5.124   1.00 42.10  ? 319 TRP A CZ2 1 
ATOM   2375 C CZ3 . TRP A 1 319 ? 14.041  -4.125  6.479   1.00 46.27  ? 319 TRP A CZ3 1 
ATOM   2376 C CH2 . TRP A 1 319 ? 15.369  -3.850  6.123   1.00 43.50  ? 319 TRP A CH2 1 
ATOM   2377 N N   . HIS A 1 320 ? 9.992   -4.710  4.113   1.00 30.18  ? 320 HIS A N   1 
ATOM   2378 C CA  . HIS A 1 320 ? 10.221  -6.107  4.472   1.00 33.38  ? 320 HIS A CA  1 
ATOM   2379 C C   . HIS A 1 320 ? 9.945   -7.047  3.308   1.00 35.38  ? 320 HIS A C   1 
ATOM   2380 O O   . HIS A 1 320 ? 10.590  -8.096  3.194   1.00 36.98  ? 320 HIS A O   1 
ATOM   2381 C CB  . HIS A 1 320 ? 9.369   -6.479  5.678   1.00 33.36  ? 320 HIS A CB  1 
ATOM   2382 C CG  . HIS A 1 320 ? 9.873   -5.906  6.962   1.00 34.26  ? 320 HIS A CG  1 
ATOM   2383 N ND1 . HIS A 1 320 ? 9.316   -4.790  7.549   1.00 38.20  ? 320 HIS A ND1 1 
ATOM   2384 C CD2 . HIS A 1 320 ? 10.855  -6.319  7.796   1.00 37.62  ? 320 HIS A CD2 1 
ATOM   2385 C CE1 . HIS A 1 320 ? 9.964   -4.513  8.666   1.00 39.46  ? 320 HIS A CE1 1 
ATOM   2386 N NE2 . HIS A 1 320 ? 10.895  -5.432  8.847   1.00 40.35  ? 320 HIS A NE2 1 
ATOM   2387 N N   . SER A 1 321 ? 9.013   -6.682  2.430   1.00 32.90  ? 321 SER A N   1 
ATOM   2388 C CA  . SER A 1 321 ? 8.619   -7.546  1.318   1.00 36.02  ? 321 SER A CA  1 
ATOM   2389 C C   . SER A 1 321 ? 9.661   -7.584  0.213   1.00 39.37  ? 321 SER A C   1 
ATOM   2390 O O   . SER A 1 321 ? 9.643   -8.501  -0.617  1.00 40.93  ? 321 SER A O   1 
ATOM   2391 C CB  . SER A 1 321 ? 7.295   -7.056  0.738   1.00 33.61  ? 321 SER A CB  1 
ATOM   2392 O OG  . SER A 1 321 ? 6.249   -7.311  1.648   1.00 34.44  ? 321 SER A OG  1 
ATOM   2393 N N   . THR A 1 322 ? 10.550  -6.594  0.167   1.00 39.23  ? 322 THR A N   1 
ATOM   2394 C CA  . THR A 1 322 ? 11.535  -6.473  -0.894  1.00 40.03  ? 322 THR A CA  1 
ATOM   2395 C C   . THR A 1 322 ? 12.954  -6.700  -0.406  1.00 43.79  ? 322 THR A C   1 
ATOM   2396 O O   . THR A 1 322 ? 13.845  -6.931  -1.230  1.00 47.77  ? 322 THR A O   1 
ATOM   2397 C CB  . THR A 1 322 ? 11.468  -5.080  -1.529  1.00 40.30  ? 322 THR A CB  1 
ATOM   2398 O OG1 . THR A 1 322 ? 11.460  -4.095  -0.489  1.00 38.57  ? 322 THR A OG1 1 
ATOM   2399 C CG2 . THR A 1 322 ? 10.202  -4.920  -2.363  1.00 39.86  ? 322 THR A CG2 1 
ATOM   2400 N N   . ALA A 1 323 ? 13.180  -6.621  0.895   1.00 40.54  ? 323 ALA A N   1 
ATOM   2401 C CA  . ALA A 1 323 ? 14.522  -6.751  1.455   1.00 43.88  ? 323 ALA A CA  1 
ATOM   2402 C C   . ALA A 1 323 ? 15.039  -8.172  1.272   1.00 47.99  ? 323 ALA A C   1 
ATOM   2403 O O   . ALA A 1 323 ? 14.401  -9.120  1.749   1.00 49.57  ? 323 ALA A O   1 
ATOM   2404 C CB  . ALA A 1 323 ? 14.510  -6.374  2.935   1.00 44.21  ? 323 ALA A CB  1 
ATOM   2405 N N   . PRO A 1 324 ? 16.192  -8.369  0.616   1.00 50.08  ? 324 PRO A N   1 
ATOM   2406 C CA  . PRO A 1 324 ? 16.787  -9.684  0.333   1.00 50.19  ? 324 PRO A CA  1 
ATOM   2407 C C   . PRO A 1 324 ? 17.009  -10.557 1.574   1.00 56.08  ? 324 PRO A C   1 
ATOM   2408 O O   . PRO A 1 324 ? 17.333  -10.042 2.650   1.00 63.14  ? 324 PRO A O   1 
ATOM   2409 C CB  . PRO A 1 324 ? 18.131  -9.325  -0.324  1.00 53.68  ? 324 PRO A CB  1 
ATOM   2410 C CG  . PRO A 1 324 ? 18.389  -7.900  0.040   1.00 57.39  ? 324 PRO A CG  1 
ATOM   2411 C CD  . PRO A 1 324 ? 17.037  -7.265  0.133   1.00 48.52  ? 324 PRO A CD  1 
ATOM   2412 N N   . VAL B 1 13  ? -2.437  0.012   -19.009 1.00 61.92  ? 13  VAL B N   1 
ATOM   2413 C CA  . VAL B 1 13  ? -3.437  -0.015  -20.119 1.00 55.56  ? 13  VAL B CA  1 
ATOM   2414 C C   . VAL B 1 13  ? -4.204  -1.343  -20.073 1.00 53.34  ? 13  VAL B C   1 
ATOM   2415 O O   . VAL B 1 13  ? -3.556  -2.395  -20.066 1.00 52.20  ? 13  VAL B O   1 
ATOM   2416 C CB  . VAL B 1 13  ? -2.770  0.179   -21.491 1.00 55.55  ? 13  VAL B CB  1 
ATOM   2417 C CG1 . VAL B 1 13  ? -1.516  -0.667  -21.637 1.00 56.26  ? 13  VAL B CG1 1 
ATOM   2418 C CG2 . VAL B 1 13  ? -3.737  -0.093  -22.630 1.00 55.64  ? 13  VAL B CG2 1 
ATOM   2419 N N   . SER B 1 14  ? -5.534  -1.285  -20.069 1.00 47.82  ? 14  SER B N   1 
ATOM   2420 C CA  . SER B 1 14  ? -6.331  -2.529  -19.943 1.00 41.37  ? 14  SER B CA  1 
ATOM   2421 C C   . SER B 1 14  ? -6.233  -3.387  -21.198 1.00 42.90  ? 14  SER B C   1 
ATOM   2422 O O   . SER B 1 14  ? -6.183  -2.828  -22.296 1.00 44.54  ? 14  SER B O   1 
ATOM   2423 C CB  . SER B 1 14  ? -7.767  -2.266  -19.599 1.00 41.51  ? 14  SER B CB  1 
ATOM   2424 O OG  . SER B 1 14  ? -8.491  -3.479  -19.519 1.00 35.33  ? 14  SER B OG  1 
ATOM   2425 N N   . ALA B 1 15  ? -6.168  -4.696  -21.010 1.00 37.18  ? 15  ALA B N   1 
ATOM   2426 C CA  . ALA B 1 15  ? -6.154  -5.648  -22.114 1.00 36.38  ? 15  ALA B CA  1 
ATOM   2427 C C   . ALA B 1 15  ? -7.525  -6.243  -22.402 1.00 35.91  ? 15  ALA B C   1 
ATOM   2428 O O   . ALA B 1 15  ? -7.636  -7.107  -23.280 1.00 36.26  ? 15  ALA B O   1 
ATOM   2429 C CB  . ALA B 1 15  ? -5.169  -6.788  -21.820 1.00 38.24  ? 15  ALA B CB  1 
ATOM   2430 N N   . ILE B 1 16  ? -8.557  -5.829  -21.671 1.00 32.71  ? 16  ILE B N   1 
ATOM   2431 C CA  . ILE B 1 16  ? -9.878  -6.452  -21.747 1.00 34.09  ? 16  ILE B CA  1 
ATOM   2432 C C   . ILE B 1 16  ? -10.924 -5.406  -22.138 1.00 37.69  ? 16  ILE B C   1 
ATOM   2433 O O   . ILE B 1 16  ? -10.601 -4.214  -22.213 1.00 38.62  ? 16  ILE B O   1 
ATOM   2434 C CB  . ILE B 1 16  ? -10.211 -7.167  -20.422 1.00 34.90  ? 16  ILE B CB  1 
ATOM   2435 C CG1 . ILE B 1 16  ? -10.268 -6.172  -19.256 1.00 33.09  ? 16  ILE B CG1 1 
ATOM   2436 C CG2 . ILE B 1 16  ? -9.192  -8.269  -20.145 1.00 31.47  ? 16  ILE B CG2 1 
ATOM   2437 C CD1 . ILE B 1 16  ? -10.785 -6.805  -17.978 1.00 34.38  ? 16  ILE B CD1 1 
ATOM   2438 N N   . PRO B 1 17  ? -12.167 -5.803  -22.439 1.00 37.96  ? 17  PRO B N   1 
ATOM   2439 C CA  . PRO B 1 17  ? -13.148 -4.841  -22.965 1.00 38.96  ? 17  PRO B CA  1 
ATOM   2440 C C   . PRO B 1 17  ? -13.441 -3.699  -21.998 1.00 37.44  ? 17  PRO B C   1 
ATOM   2441 O O   . PRO B 1 17  ? -13.405 -3.864  -20.775 1.00 36.02  ? 17  PRO B O   1 
ATOM   2442 C CB  . PRO B 1 17  ? -14.392 -5.709  -23.188 1.00 37.71  ? 17  PRO B CB  1 
ATOM   2443 C CG  . PRO B 1 17  ? -13.852 -7.064  -23.465 1.00 37.77  ? 17  PRO B CG  1 
ATOM   2444 C CD  . PRO B 1 17  ? -12.671 -7.188  -22.528 1.00 38.30  ? 17  PRO B CD  1 
ATOM   2445 N N   . SER B 1 18  ? -13.732 -2.517  -22.557 1.00 37.20  ? 18  SER B N   1 
ATOM   2446 C CA  . SER B 1 18  ? -14.096 -1.355  -21.732 1.00 38.03  ? 18  SER B CA  1 
ATOM   2447 C C   . SER B 1 18  ? -15.586 -1.418  -21.399 1.00 39.51  ? 18  SER B C   1 
ATOM   2448 O O   . SER B 1 18  ? -16.411 -0.639  -21.886 1.00 37.53  ? 18  SER B O   1 
ATOM   2449 C CB  . SER B 1 18  ? -13.737 -0.040  -22.416 1.00 43.81  ? 18  SER B CB  1 
ATOM   2450 O OG  . SER B 1 18  ? -12.524 -0.144  -23.132 1.00 48.50  ? 18  SER B OG  1 
ATOM   2451 N N   . VAL B 1 19  ? -15.922 -2.375  -20.533 1.00 32.06  ? 19  VAL B N   1 
ATOM   2452 C CA  . VAL B 1 19  ? -17.306 -2.689  -20.213 1.00 29.85  ? 19  VAL B CA  1 
ATOM   2453 C C   . VAL B 1 19  ? -17.575 -2.658  -18.716 1.00 30.99  ? 19  VAL B C   1 
ATOM   2454 O O   . VAL B 1 19  ? -18.605 -3.169  -18.262 1.00 34.70  ? 19  VAL B O   1 
ATOM   2455 C CB  . VAL B 1 19  ? -17.704 -4.060  -20.802 1.00 31.68  ? 19  VAL B CB  1 
ATOM   2456 C CG1 . VAL B 1 19  ? -17.530 -4.073  -22.312 1.00 35.88  ? 19  VAL B CG1 1 
ATOM   2457 C CG2 . VAL B 1 19  ? -16.829 -5.164  -20.165 1.00 31.71  ? 19  VAL B CG2 1 
ATOM   2458 N N   . PHE B 1 20  ? -16.680 -2.051  -17.934 1.00 31.36  ? 20  PHE B N   1 
ATOM   2459 C CA  . PHE B 1 20  ? -16.881 -1.995  -16.494 1.00 31.76  ? 20  PHE B CA  1 
ATOM   2460 C C   . PHE B 1 20  ? -16.246 -0.732  -15.930 1.00 35.85  ? 20  PHE B C   1 
ATOM   2461 O O   . PHE B 1 20  ? -15.320 -0.155  -16.509 1.00 38.40  ? 20  PHE B O   1 
ATOM   2462 C CB  . PHE B 1 20  ? -16.297 -3.240  -15.792 1.00 31.69  ? 20  PHE B CB  1 
ATOM   2463 C CG  . PHE B 1 20  ? -14.819 -3.365  -15.951 1.00 32.07  ? 20  PHE B CG  1 
ATOM   2464 C CD1 . PHE B 1 20  ? -14.287 -4.033  -17.045 1.00 32.44  ? 20  PHE B CD1 1 
ATOM   2465 C CD2 . PHE B 1 20  ? -13.951 -2.808  -15.015 1.00 32.79  ? 20  PHE B CD2 1 
ATOM   2466 C CE1 . PHE B 1 20  ? -12.920 -4.141  -17.206 1.00 33.84  ? 20  PHE B CE1 1 
ATOM   2467 C CE2 . PHE B 1 20  ? -12.588 -2.907  -15.172 1.00 33.28  ? 20  PHE B CE2 1 
ATOM   2468 C CZ  . PHE B 1 20  ? -12.066 -3.582  -16.265 1.00 34.97  ? 20  PHE B CZ  1 
ATOM   2469 N N   . GLU B 1 21  ? -16.746 -0.324  -14.773 1.00 33.90  ? 21  GLU B N   1 
ATOM   2470 C CA  . GLU B 1 21  ? -16.171 0.767   -14.001 1.00 38.48  ? 21  GLU B CA  1 
ATOM   2471 C C   . GLU B 1 21  ? -15.496 0.178   -12.771 1.00 37.33  ? 21  GLU B C   1 
ATOM   2472 O O   . GLU B 1 21  ? -15.980 -0.800  -12.203 1.00 35.36  ? 21  GLU B O   1 
ATOM   2473 C CB  . GLU B 1 21  ? -17.252 1.760   -13.580 1.00 41.46  ? 21  GLU B CB  1 
ATOM   2474 C CG  . GLU B 1 21  ? -18.071 2.324   -14.746 1.00 44.60  ? 21  GLU B CG  1 
ATOM   2475 C CD  . GLU B 1 21  ? -17.274 3.233   -15.685 1.00 54.70  ? 21  GLU B CD  1 
ATOM   2476 O OE1 . GLU B 1 21  ? -16.204 3.744   -15.278 1.00 54.04  ? 21  GLU B OE1 1 
ATOM   2477 O OE2 . GLU B 1 21  ? -17.718 3.430   -16.844 1.00 59.27  ? 21  GLU B OE2 1 
ATOM   2478 N N   . THR B 1 22  ? -14.390 0.778   -12.347 1.00 36.75  ? 22  THR B N   1 
ATOM   2479 C CA  . THR B 1 22  ? -13.676 0.261   -11.186 1.00 40.20  ? 22  THR B CA  1 
ATOM   2480 C C   . THR B 1 22  ? -14.405 0.607   -9.888  1.00 45.39  ? 22  THR B C   1 
ATOM   2481 O O   . THR B 1 22  ? -15.063 1.644   -9.770  1.00 45.37  ? 22  THR B O   1 
ATOM   2482 C CB  . THR B 1 22  ? -12.238 0.793   -11.173 1.00 45.84  ? 22  THR B CB  1 
ATOM   2483 O OG1 . THR B 1 22  ? -11.634 0.525   -12.445 1.00 49.29  ? 22  THR B OG1 1 
ATOM   2484 C CG2 . THR B 1 22  ? -11.395 0.167   -10.059 1.00 43.50  ? 22  THR B CG2 1 
ATOM   2485 N N   . LEU B 1 23  ? -14.309 -0.301  -8.918  1.00 40.68  ? 23  LEU B N   1 
ATOM   2486 C CA  . LEU B 1 23  ? -14.834 -0.091  -7.577  1.00 40.69  ? 23  LEU B CA  1 
ATOM   2487 C C   . LEU B 1 23  ? -13.661 0.156   -6.634  1.00 45.03  ? 23  LEU B C   1 
ATOM   2488 O O   . LEU B 1 23  ? -12.594 -0.447  -6.782  1.00 44.48  ? 23  LEU B O   1 
ATOM   2489 C CB  . LEU B 1 23  ? -15.661 -1.300  -7.113  1.00 39.69  ? 23  LEU B CB  1 
ATOM   2490 C CG  . LEU B 1 23  ? -16.992 -1.590  -7.825  1.00 38.58  ? 23  LEU B CG  1 
ATOM   2491 C CD1 . LEU B 1 23  ? -17.445 -3.006  -7.499  1.00 41.02  ? 23  LEU B CD1 1 
ATOM   2492 C CD2 . LEU B 1 23  ? -18.079 -0.598  -7.464  1.00 43.89  ? 23  LEU B CD2 1 
ATOM   2493 N N   . GLN B 1 24  ? -13.867 1.048   -5.662  1.00 46.93  ? 24  GLN B N   1 
ATOM   2494 C CA  . GLN B 1 24  ? -12.790 1.420   -4.710  1.00 51.38  ? 24  GLN B CA  1 
ATOM   2495 C C   . GLN B 1 24  ? -12.940 0.594   -3.427  1.00 49.55  ? 24  GLN B C   1 
ATOM   2496 O O   . GLN B 1 24  ? -13.545 1.090   -2.479  1.00 48.88  ? 24  GLN B O   1 
ATOM   2497 C CB  . GLN B 1 24  ? -12.865 2.925   -4.449  1.00 54.17  ? 24  GLN B CB  1 
ATOM   2498 C CG  . GLN B 1 24  ? -13.186 3.757   -5.680  1.00 56.22  ? 24  GLN B CG  1 
ATOM   2499 C CD  . GLN B 1 24  ? -13.491 5.192   -5.325  1.00 66.43  ? 24  GLN B CD  1 
ATOM   2500 O OE1 . GLN B 1 24  ? -12.594 6.018   -5.170  1.00 69.25  ? 24  GLN B OE1 1 
ATOM   2501 N NE2 . GLN B 1 24  ? -14.770 5.500   -5.188  1.00 61.31  ? 24  GLN B NE2 1 
ATOM   2502 N N   . GLY B 1 25  ? -12.406 -0.627  -3.416  1.00 43.18  ? 25  GLY B N   1 
ATOM   2503 C CA  . GLY B 1 25  ? -12.561 -1.515  -2.251  1.00 42.70  ? 25  GLY B CA  1 
ATOM   2504 C C   . GLY B 1 25  ? -11.838 -0.991  -1.028  1.00 42.68  ? 25  GLY B C   1 
ATOM   2505 O O   . GLY B 1 25  ? -12.201 -1.388  0.075   1.00 40.97  ? 25  GLY B O   1 
ATOM   2506 N N   . TYR B 1 26  ? -10.848 -0.130  -1.233  1.00 47.08  ? 26  TYR B N   1 
ATOM   2507 C CA  . TYR B 1 26  ? -10.118 0.478   -0.093  1.00 52.22  ? 26  TYR B CA  1 
ATOM   2508 C C   . TYR B 1 26  ? -11.109 1.132   0.871   1.00 51.62  ? 26  TYR B C   1 
ATOM   2509 O O   . TYR B 1 26  ? -10.783 1.270   2.055   1.00 54.80  ? 26  TYR B O   1 
ATOM   2510 C CB  . TYR B 1 26  ? -9.065  1.481   -0.579  1.00 53.23  ? 26  TYR B CB  1 
ATOM   2511 C CG  . TYR B 1 26  ? -9.581  2.768   -1.168  1.00 56.70  ? 26  TYR B CG  1 
ATOM   2512 C CD1 . TYR B 1 26  ? -9.817  3.876   -0.373  1.00 56.92  ? 26  TYR B CD1 1 
ATOM   2513 C CD2 . TYR B 1 26  ? -9.798  2.891   -2.528  1.00 55.80  ? 26  TYR B CD2 1 
ATOM   2514 C CE1 . TYR B 1 26  ? -10.277 5.067   -0.910  1.00 60.23  ? 26  TYR B CE1 1 
ATOM   2515 C CE2 . TYR B 1 26  ? -10.253 4.075   -3.082  1.00 60.16  ? 26  TYR B CE2 1 
ATOM   2516 C CZ  . TYR B 1 26  ? -10.498 5.166   -2.270  1.00 63.17  ? 26  TYR B CZ  1 
ATOM   2517 O OH  . TYR B 1 26  ? -10.951 6.331   -2.815  1.00 66.83  ? 26  TYR B OH  1 
ATOM   2518 N N   . LYS B 1 27  ? -12.276 1.515   0.373   1.00 48.87  ? 27  LYS B N   1 
ATOM   2519 C CA  . LYS B 1 27  ? -13.284 2.200   1.215   1.00 47.61  ? 27  LYS B CA  1 
ATOM   2520 C C   . LYS B 1 27  ? -14.071 1.182   2.049   1.00 48.65  ? 27  LYS B C   1 
ATOM   2521 O O   . LYS B 1 27  ? -14.882 1.623   2.868   1.00 49.57  ? 27  LYS B O   1 
ATOM   2522 C CB  . LYS B 1 27  ? -14.187 3.024   0.299   1.00 49.57  ? 27  LYS B CB  1 
ATOM   2523 C CG  . LYS B 1 27  ? -13.480 4.121   -0.482  1.00 55.00  ? 27  LYS B CG  1 
ATOM   2524 C CD  . LYS B 1 27  ? -14.303 4.656   -1.629  1.00 57.41  ? 27  LYS B CD  1 
ATOM   2525 C CE  . LYS B 1 27  ? -14.002 6.104   -1.949  1.00 60.18  ? 27  LYS B CE  1 
ATOM   2526 N NZ  . LYS B 1 27  ? -15.234 6.858   -2.278  1.00 62.14  ? 27  LYS B NZ  1 
ATOM   2527 N N   . VAL B 1 28  ? -13.847 -0.120  1.844   1.00 40.38  ? 28  VAL B N   1 
ATOM   2528 C CA  . VAL B 1 28  ? -14.550 -1.168  2.577   1.00 35.72  ? 28  VAL B CA  1 
ATOM   2529 C C   . VAL B 1 28  ? -13.555 -1.803  3.541   1.00 36.15  ? 28  VAL B C   1 
ATOM   2530 O O   . VAL B 1 28  ? -12.663 -2.545  3.104   1.00 33.03  ? 28  VAL B O   1 
ATOM   2531 C CB  . VAL B 1 28  ? -15.157 -2.215  1.634   1.00 37.42  ? 28  VAL B CB  1 
ATOM   2532 C CG1 . VAL B 1 28  ? -16.047 -3.167  2.407   1.00 37.54  ? 28  VAL B CG1 1 
ATOM   2533 C CG2 . VAL B 1 28  ? -15.962 -1.520  0.524   1.00 43.61  ? 28  VAL B CG2 1 
ATOM   2534 N N   . PRO B 1 29  ? -13.656 -1.541  4.846   1.00 35.30  ? 29  PRO B N   1 
ATOM   2535 C CA  . PRO B 1 29  ? -12.634 -2.046  5.773   1.00 34.90  ? 29  PRO B CA  1 
ATOM   2536 C C   . PRO B 1 29  ? -12.509 -3.566  5.811   1.00 34.60  ? 29  PRO B C   1 
ATOM   2537 O O   . PRO B 1 29  ? -11.400 -4.073  6.011   1.00 37.86  ? 29  PRO B O   1 
ATOM   2538 C CB  . PRO B 1 29  ? -13.084 -1.473  7.123   1.00 34.90  ? 29  PRO B CB  1 
ATOM   2539 C CG  . PRO B 1 29  ? -13.766 -0.190  6.761   1.00 35.37  ? 29  PRO B CG  1 
ATOM   2540 C CD  . PRO B 1 29  ? -14.537 -0.544  5.485   1.00 37.36  ? 29  PRO B CD  1 
ATOM   2541 N N   . VAL B 1 30  ? -13.579 -4.305  5.542   1.00 35.91  ? 30  VAL B N   1 
ATOM   2542 C CA  . VAL B 1 30  ? -13.529 -5.796  5.634   1.00 37.95  ? 30  VAL B CA  1 
ATOM   2543 C C   . VAL B 1 30  ? -12.920 -6.373  4.352   1.00 36.77  ? 30  VAL B C   1 
ATOM   2544 O O   . VAL B 1 30  ? -12.501 -7.521  4.371   1.00 34.91  ? 30  VAL B O   1 
ATOM   2545 C CB  . VAL B 1 30  ? -14.922 -6.395  5.899   1.00 42.14  ? 30  VAL B CB  1 
ATOM   2546 C CG1 . VAL B 1 30  ? -15.415 -6.055  7.294   1.00 47.37  ? 30  VAL B CG1 1 
ATOM   2547 C CG2 . VAL B 1 30  ? -15.922 -5.948  4.854   1.00 44.32  ? 30  VAL B CG2 1 
ATOM   2548 N N   . PHE B 1 31  ? -12.894 -5.584  3.286   1.00 33.72  ? 31  PHE B N   1 
ATOM   2549 C CA  . PHE B 1 31  ? -12.315 -6.034  2.024   1.00 34.38  ? 31  PHE B CA  1 
ATOM   2550 C C   . PHE B 1 31  ? -10.795 -6.097  2.149   1.00 34.73  ? 31  PHE B C   1 
ATOM   2551 O O   . PHE B 1 31  ? -10.146 -5.067  2.339   1.00 35.21  ? 31  PHE B O   1 
ATOM   2552 C CB  . PHE B 1 31  ? -12.743 -5.076  0.909   1.00 32.74  ? 31  PHE B CB  1 
ATOM   2553 C CG  . PHE B 1 31  ? -12.094 -5.346  -0.415  1.00 31.74  ? 31  PHE B CG  1 
ATOM   2554 C CD1 . PHE B 1 31  ? -12.515 -6.402  -1.207  1.00 31.41  ? 31  PHE B CD1 1 
ATOM   2555 C CD2 . PHE B 1 31  ? -11.041 -4.552  -0.859  1.00 36.41  ? 31  PHE B CD2 1 
ATOM   2556 C CE1 . PHE B 1 31  ? -11.920 -6.645  -2.430  1.00 31.26  ? 31  PHE B CE1 1 
ATOM   2557 C CE2 . PHE B 1 31  ? -10.435 -4.799  -2.080  1.00 37.25  ? 31  PHE B CE2 1 
ATOM   2558 C CZ  . PHE B 1 31  ? -10.888 -5.856  -2.873  1.00 32.98  ? 31  PHE B CZ  1 
ATOM   2559 N N   . PHE B 1 32  ? -10.218 -7.303  2.047   1.00 29.82  ? 32  PHE B N   1 
ATOM   2560 C CA  . PHE B 1 32  ? -8.786  -7.480  2.255   1.00 31.11  ? 32  PHE B CA  1 
ATOM   2561 C C   . PHE B 1 32  ? -8.004  -7.878  1.005   1.00 32.24  ? 32  PHE B C   1 
ATOM   2562 O O   . PHE B 1 32  ? -6.768  -7.954  1.064   1.00 31.08  ? 32  PHE B O   1 
ATOM   2563 C CB  . PHE B 1 32  ? -8.549  -8.537  3.341   1.00 31.53  ? 32  PHE B CB  1 
ATOM   2564 C CG  . PHE B 1 32  ? -9.046  -9.906  2.962   1.00 27.08  ? 32  PHE B CG  1 
ATOM   2565 C CD1 . PHE B 1 32  ? -8.265  -10.757 2.198   1.00 29.09  ? 32  PHE B CD1 1 
ATOM   2566 C CD2 . PHE B 1 32  ? -10.279 -10.349 3.403   1.00 29.04  ? 32  PHE B CD2 1 
ATOM   2567 C CE1 . PHE B 1 32  ? -8.724  -12.020 1.857   1.00 29.87  ? 32  PHE B CE1 1 
ATOM   2568 C CE2 . PHE B 1 32  ? -10.748 -11.615 3.070   1.00 29.89  ? 32  PHE B CE2 1 
ATOM   2569 C CZ  . PHE B 1 32  ? -9.969  -12.453 2.296   1.00 29.41  ? 32  PHE B CZ  1 
ATOM   2570 N N   . SER B 1 33  ? -8.673  -8.161  -0.105  1.00 29.49  ? 33  SER B N   1 
ATOM   2571 C CA  . SER B 1 33  ? -7.978  -8.703  -1.260  1.00 27.26  ? 33  SER B CA  1 
ATOM   2572 C C   . SER B 1 33  ? -7.018  -7.692  -1.860  1.00 26.65  ? 33  SER B C   1 
ATOM   2573 O O   . SER B 1 33  ? -7.275  -6.485  -1.863  1.00 29.72  ? 33  SER B O   1 
ATOM   2574 C CB  . SER B 1 33  ? -8.983  -9.124  -2.338  1.00 28.67  ? 33  SER B CB  1 
ATOM   2575 O OG  . SER B 1 33  ? -8.304  -9.728  -3.424  1.00 28.68  ? 33  SER B OG  1 
ATOM   2576 N N   . ARG B 1 34  ? -5.930  -8.206  -2.431  1.00 27.09  ? 34  ARG B N   1 
ATOM   2577 C CA  . ARG B 1 34  ? -5.026  -7.392  -3.232  1.00 30.35  ? 34  ARG B CA  1 
ATOM   2578 C C   . ARG B 1 34  ? -5.528  -7.185  -4.654  1.00 29.22  ? 34  ARG B C   1 
ATOM   2579 O O   . ARG B 1 34  ? -4.977  -6.347  -5.382  1.00 28.50  ? 34  ARG B O   1 
ATOM   2580 C CB  . ARG B 1 34  ? -3.644  -8.043  -3.293  1.00 31.27  ? 34  ARG B CB  1 
ATOM   2581 C CG  . ARG B 1 34  ? -3.618  -9.285  -4.162  1.00 28.84  ? 34  ARG B CG  1 
ATOM   2582 C CD  . ARG B 1 34  ? -2.356  -10.133 -3.998  1.00 34.72  ? 34  ARG B CD  1 
ATOM   2583 N NE  . ARG B 1 34  ? -1.166  -9.492  -4.537  1.00 35.11  ? 34  ARG B NE  1 
ATOM   2584 C CZ  . ARG B 1 34  ? -0.072  -9.228  -3.831  1.00 39.68  ? 34  ARG B CZ  1 
ATOM   2585 N NH1 . ARG B 1 34  ? 0.056   -9.637  -2.577  1.00 37.89  ? 34  ARG B NH1 1 
ATOM   2586 N NH2 . ARG B 1 34  ? 0.942   -8.598  -4.418  1.00 37.38  ? 34  ARG B NH2 1 
ATOM   2587 N N   . TYR B 1 35  ? -6.562  -7.920  -5.066  1.00 26.93  ? 35  TYR B N   1 
ATOM   2588 C CA  . TYR B 1 35  ? -7.031  -7.882  -6.444  1.00 26.78  ? 35  TYR B CA  1 
ATOM   2589 C C   . TYR B 1 35  ? -8.166  -6.876  -6.594  1.00 29.88  ? 35  TYR B C   1 
ATOM   2590 O O   . TYR B 1 35  ? -8.878  -6.585  -5.627  1.00 30.17  ? 35  TYR B O   1 
ATOM   2591 C CB  . TYR B 1 35  ? -7.460  -9.294  -6.880  1.00 27.98  ? 35  TYR B CB  1 
ATOM   2592 C CG  . TYR B 1 35  ? -6.237  -10.183 -6.916  1.00 27.18  ? 35  TYR B CG  1 
ATOM   2593 C CD1 . TYR B 1 35  ? -5.182  -9.870  -7.760  1.00 29.25  ? 35  TYR B CD1 1 
ATOM   2594 C CD2 . TYR B 1 35  ? -6.090  -11.285 -6.059  1.00 28.01  ? 35  TYR B CD2 1 
ATOM   2595 C CE1 . TYR B 1 35  ? -4.031  -10.610 -7.778  1.00 28.25  ? 35  TYR B CE1 1 
ATOM   2596 C CE2 . TYR B 1 35  ? -4.919  -12.042 -6.075  1.00 27.52  ? 35  TYR B CE2 1 
ATOM   2597 C CZ  . TYR B 1 35  ? -3.903  -11.692 -6.943  1.00 30.28  ? 35  TYR B CZ  1 
ATOM   2598 O OH  . TYR B 1 35  ? -2.732  -12.408 -6.995  1.00 30.78  ? 35  TYR B OH  1 
ATOM   2599 N N   . PRO B 1 36  ? -8.321  -6.299  -7.787  1.00 30.90  ? 36  PRO B N   1 
ATOM   2600 C CA  . PRO B 1 36  ? -9.307  -5.231  -7.984  1.00 30.87  ? 36  PRO B CA  1 
ATOM   2601 C C   . PRO B 1 36  ? -10.728 -5.745  -8.162  1.00 31.83  ? 36  PRO B C   1 
ATOM   2602 O O   . PRO B 1 36  ? -10.992 -6.938  -8.350  1.00 28.25  ? 36  PRO B O   1 
ATOM   2603 C CB  . PRO B 1 36  ? -8.840  -4.536  -9.265  1.00 34.34  ? 36  PRO B CB  1 
ATOM   2604 C CG  . PRO B 1 36  ? -8.001  -5.547  -10.000 1.00 34.53  ? 36  PRO B CG  1 
ATOM   2605 C CD  . PRO B 1 36  ? -7.678  -6.697  -9.051  1.00 31.33  ? 36  PRO B CD  1 
ATOM   2606 N N   . ALA B 1 37  ? -11.654 -4.790  -8.128  1.00 29.13  ? 37  ALA B N   1 
ATOM   2607 C CA  . ALA B 1 37  ? -13.070 -5.059  -8.299  1.00 30.02  ? 37  ALA B CA  1 
ATOM   2608 C C   . ALA B 1 37  ? -13.657 -4.038  -9.255  1.00 33.57  ? 37  ALA B C   1 
ATOM   2609 O O   . ALA B 1 37  ? -13.242 -2.871  -9.274  1.00 33.65  ? 37  ALA B O   1 
ATOM   2610 C CB  . ALA B 1 37  ? -13.821 -5.019  -6.962  1.00 30.75  ? 37  ALA B CB  1 
ATOM   2611 N N   . GLY B 1 38  ? -14.624 -4.486  -10.052 1.00 30.77  ? 38  GLY B N   1 
ATOM   2612 C CA  . GLY B 1 38  ? -15.283 -3.617  -11.005 1.00 30.51  ? 38  GLY B CA  1 
ATOM   2613 C C   . GLY B 1 38  ? -16.749 -3.979  -11.119 1.00 31.37  ? 38  GLY B C   1 
ATOM   2614 O O   . GLY B 1 38  ? -17.209 -4.955  -10.531 1.00 30.75  ? 38  GLY B O   1 
ATOM   2615 N N   . ILE B 1 39  ? -17.520 -3.319  -11.863 1.00 29.85  ? 39  ILE B N   1 
ATOM   2616 C CA  . ILE B 1 39  ? -18.994 -3.393  -12.029 1.00 32.37  ? 39  ILE B CA  1 
ATOM   2617 C C   . ILE B 1 39  ? -19.352 -3.200  -13.499 1.00 32.08  ? 39  ILE B C   1 
ATOM   2618 O O   . ILE B 1 39  ? -18.847 -2.266  -14.113 1.00 32.26  ? 39  ILE B O   1 
ATOM   2619 C CB  . ILE B 1 39  ? -19.706 -2.373  -11.119 1.00 37.63  ? 39  ILE B CB  1 
ATOM   2620 C CG1 . ILE B 1 39  ? -21.215 -2.617  -11.073 1.00 39.38  ? 39  ILE B CG1 1 
ATOM   2621 C CG2 . ILE B 1 39  ? -19.375 -0.950  -11.534 1.00 36.47  ? 39  ILE B CG2 1 
ATOM   2622 C CD1 . ILE B 1 39  ? -21.601 -3.917  -10.422 1.00 38.79  ? 39  ILE B CD1 1 
ATOM   2623 N N   . SER B 1 40  ? -20.040 -4.127  -14.081 1.00 30.59  ? 40  SER B N   1 
ATOM   2624 C CA  . SER B 1 40  ? -20.512 -4.052  -15.459 1.00 30.81  ? 40  SER B CA  1 
ATOM   2625 C C   . SER B 1 40  ? -21.290 -2.780  -15.761 1.00 32.08  ? 40  SER B C   1 
ATOM   2626 O O   . SER B 1 40  ? -22.186 -2.389  -15.012 1.00 33.62  ? 40  SER B O   1 
ATOM   2627 C CB  . SER B 1 40  ? -21.430 -5.225  -15.783 1.00 34.57  ? 40  SER B CB  1 
ATOM   2628 O OG  . SER B 1 40  ? -21.652 -5.305  -17.195 1.00 34.09  ? 40  SER B OG  1 
ATOM   2629 N N   . ILE B 1 41  ? -21.008 -2.203  -16.929 1.00 31.54  ? 41  ILE B N   1 
ATOM   2630 C CA  . ILE B 1 41  ? -21.872 -1.139  -17.438 1.00 37.15  ? 41  ILE B CA  1 
ATOM   2631 C C   . ILE B 1 41  ? -23.270 -1.648  -17.746 1.00 36.51  ? 41  ILE B C   1 
ATOM   2632 O O   . ILE B 1 41  ? -24.203 -0.848  -17.866 1.00 40.43  ? 41  ILE B O   1 
ATOM   2633 C CB  . ILE B 1 41  ? -21.258 -0.466  -18.685 1.00 36.19  ? 41  ILE B CB  1 
ATOM   2634 C CG1 . ILE B 1 41  ? -21.225 -1.437  -19.870 1.00 41.18  ? 41  ILE B CG1 1 
ATOM   2635 C CG2 . ILE B 1 41  ? -19.909 0.151   -18.353 1.00 37.91  ? 41  ILE B CG2 1 
ATOM   2636 C CD1 . ILE B 1 41  ? -20.477 -0.893  -21.070 1.00 43.78  ? 41  ILE B CD1 1 
ATOM   2637 N N   . ALA B 1 42  ? -23.447 -2.965  -17.866 1.00 37.25  ? 42  ALA B N   1 
ATOM   2638 C CA  . ALA B 1 42  ? -24.742 -3.562  -18.153 1.00 37.36  ? 42  ALA B CA  1 
ATOM   2639 C C   . ALA B 1 42  ? -25.412 -4.121  -16.913 1.00 35.01  ? 42  ALA B C   1 
ATOM   2640 O O   . ALA B 1 42  ? -26.250 -5.018  -17.032 1.00 37.86  ? 42  ALA B O   1 
ATOM   2641 C CB  . ALA B 1 42  ? -24.600 -4.665  -19.202 1.00 38.59  ? 42  ALA B CB  1 
ATOM   2642 N N   . ALA B 1 43  ? -25.068 -3.609  -15.727 1.00 31.76  ? 43  ALA B N   1 
ATOM   2643 C CA  . ALA B 1 43  ? -25.519 -4.232  -14.485 1.00 34.56  ? 43  ALA B CA  1 
ATOM   2644 C C   . ALA B 1 43  ? -27.042 -4.321  -14.403 1.00 39.33  ? 43  ALA B C   1 
ATOM   2645 O O   . ALA B 1 43  ? -27.588 -5.360  -14.022 1.00 35.82  ? 43  ALA B O   1 
ATOM   2646 C CB  . ALA B 1 43  ? -24.959 -3.480  -13.276 1.00 36.40  ? 43  ALA B CB  1 
ATOM   2647 N N   . GLN B 1 44  ? -27.754 -3.258  -14.768 1.00 39.83  ? 44  GLN B N   1 
ATOM   2648 C CA  . GLN B 1 44  ? -29.230 -3.301  -14.576 1.00 42.53  ? 44  GLN B CA  1 
ATOM   2649 C C   . GLN B 1 44  ? -29.837 -4.382  -15.470 1.00 37.95  ? 44  GLN B C   1 
ATOM   2650 O O   . GLN B 1 44  ? -30.683 -5.138  -14.984 1.00 40.72  ? 44  GLN B O   1 
ATOM   2651 C CB  . GLN B 1 44  ? -29.877 -1.942  -14.852 1.00 40.71  ? 44  GLN B CB  1 
ATOM   2652 C CG  . GLN B 1 44  ? -31.380 -1.929  -14.619 1.00 43.93  ? 44  GLN B CG  1 
ATOM   2653 C CD  . GLN B 1 44  ? -31.740 -2.285  -13.198 1.00 46.99  ? 44  GLN B CD  1 
ATOM   2654 O OE1 . GLN B 1 44  ? -31.468 -1.539  -12.262 1.00 55.13  ? 44  GLN B OE1 1 
ATOM   2655 N NE2 . GLN B 1 44  ? -32.363 -3.438  -13.026 1.00 53.60  ? 44  GLN B NE2 1 
ATOM   2656 N N   . GLU B 1 45  ? -29.406 -4.447  -16.721 1.00 35.89  ? 45  GLU B N   1 
ATOM   2657 C CA  . GLU B 1 45  ? -30.041 -5.417  -17.643 1.00 37.78  ? 45  GLU B CA  1 
ATOM   2658 C C   . GLU B 1 45  ? -29.766 -6.855  -17.177 1.00 37.91  ? 45  GLU B C   1 
ATOM   2659 O O   . GLU B 1 45  ? -30.663 -7.694  -17.279 1.00 35.38  ? 45  GLU B O   1 
ATOM   2660 C CB  . GLU B 1 45  ? -29.530 -5.173  -19.059 1.00 43.01  ? 45  GLU B CB  1 
ATOM   2661 C CG  . GLU B 1 45  ? -29.593 -3.713  -19.470 1.00 50.03  ? 45  GLU B CG  1 
ATOM   2662 C CD  . GLU B 1 45  ? -28.343 -2.893  -19.189 1.00 52.39  ? 45  GLU B CD  1 
ATOM   2663 O OE1 . GLU B 1 45  ? -28.143 -2.493  -18.029 1.00 46.32  ? 45  GLU B OE1 1 
ATOM   2664 O OE2 . GLU B 1 45  ? -27.577 -2.651  -20.138 1.00 62.21  ? 45  GLU B OE2 1 
ATOM   2665 N N   . VAL B 1 46  ? -28.568 -7.107  -16.657 1.00 34.81  ? 46  VAL B N   1 
ATOM   2666 C CA  . VAL B 1 46  ? -28.196 -8.487  -16.241 1.00 32.64  ? 46  VAL B CA  1 
ATOM   2667 C C   . VAL B 1 46  ? -28.997 -8.848  -14.989 1.00 34.02  ? 46  VAL B C   1 
ATOM   2668 O O   . VAL B 1 46  ? -29.515 -9.960  -14.919 1.00 37.07  ? 46  VAL B O   1 
ATOM   2669 C CB  . VAL B 1 46  ? -26.670 -8.595  -16.040 1.00 34.07  ? 46  VAL B CB  1 
ATOM   2670 C CG1 . VAL B 1 46  ? -26.270 -9.912  -15.397 1.00 35.88  ? 46  VAL B CG1 1 
ATOM   2671 C CG2 . VAL B 1 46  ? -25.924 -8.384  -17.346 1.00 33.55  ? 46  VAL B CG2 1 
ATOM   2672 N N   . GLU B 1 47  ? -29.112 -7.911  -14.053 1.00 35.61  ? 47  GLU B N   1 
ATOM   2673 C CA  . GLU B 1 47  ? -29.862 -8.162  -12.800 1.00 35.47  ? 47  GLU B CA  1 
ATOM   2674 C C   . GLU B 1 47  ? -31.331 -8.467  -13.115 1.00 38.88  ? 47  GLU B C   1 
ATOM   2675 O O   . GLU B 1 47  ? -31.913 -9.309  -12.434 1.00 37.33  ? 47  GLU B O   1 
ATOM   2676 C CB  . GLU B 1 47  ? -29.760 -6.946  -11.887 1.00 37.71  ? 47  GLU B CB  1 
ATOM   2677 C CG  . GLU B 1 47  ? -28.386 -6.728  -11.294 1.00 42.02  ? 47  GLU B CG  1 
ATOM   2678 C CD  . GLU B 1 47  ? -28.275 -5.401  -10.568 1.00 46.31  ? 47  GLU B CD  1 
ATOM   2679 O OE1 . GLU B 1 47  ? -27.599 -5.351  -9.530  1.00 51.58  ? 47  GLU B OE1 1 
ATOM   2680 O OE2 . GLU B 1 47  ? -28.882 -4.426  -11.038 1.00 52.04  ? 47  GLU B OE2 1 
ATOM   2681 N N   . ASP B 1 48  ? -31.899 -7.771  -14.099 1.00 39.41  ? 48  ASP B N   1 
ATOM   2682 C CA  . ASP B 1 48  ? -33.311 -8.007  -14.490 1.00 41.54  ? 48  ASP B CA  1 
ATOM   2683 C C   . ASP B 1 48  ? -33.443 -9.428  -15.034 1.00 38.79  ? 48  ASP B C   1 
ATOM   2684 O O   . ASP B 1 48  ? -34.400 -10.110 -14.681 1.00 39.44  ? 48  ASP B O   1 
ATOM   2685 C CB  . ASP B 1 48  ? -33.762 -6.963  -15.510 1.00 40.77  ? 48  ASP B CB  1 
ATOM   2686 C CG  . ASP B 1 48  ? -33.923 -5.572  -14.927 1.00 43.82  ? 48  ASP B CG  1 
ATOM   2687 O OD1 . ASP B 1 48  ? -34.043 -5.465  -13.696 1.00 48.25  ? 48  ASP B OD1 1 
ATOM   2688 O OD2 . ASP B 1 48  ? -33.930 -4.612  -15.714 1.00 44.88  ? 48  ASP B OD2 1 
ATOM   2689 N N   . ALA B 1 49  ? -32.500 -9.830  -15.874 1.00 37.22  ? 49  ALA B N   1 
ATOM   2690 C CA  . ALA B 1 49  ? -32.508 -11.191 -16.444 1.00 33.59  ? 49  ALA B CA  1 
ATOM   2691 C C   . ALA B 1 49  ? -32.384 -12.220 -15.323 1.00 37.39  ? 49  ALA B C   1 
ATOM   2692 O O   . ALA B 1 49  ? -33.058 -13.242 -15.381 1.00 38.73  ? 49  ALA B O   1 
ATOM   2693 C CB  . ALA B 1 49  ? -31.384 -11.307 -17.431 1.00 34.82  ? 49  ALA B CB  1 
ATOM   2694 N N   . LEU B 1 50  ? -31.539 -11.937 -14.341 1.00 35.77  ? 50  LEU B N   1 
ATOM   2695 C CA  . LEU B 1 50  ? -31.325 -12.892 -13.235 1.00 33.18  ? 50  LEU B CA  1 
ATOM   2696 C C   . LEU B 1 50  ? -32.602 -12.960 -12.396 1.00 39.12  ? 50  LEU B C   1 
ATOM   2697 O O   . LEU B 1 50  ? -32.975 -14.062 -11.996 1.00 37.69  ? 50  LEU B O   1 
ATOM   2698 C CB  . LEU B 1 50  ? -30.128 -12.436 -12.395 1.00 33.45  ? 50  LEU B CB  1 
ATOM   2699 C CG  . LEU B 1 50  ? -28.751 -12.701 -12.996 1.00 35.45  ? 50  LEU B CG  1 
ATOM   2700 C CD1 . LEU B 1 50  ? -27.715 -11.758 -12.405 1.00 32.36  ? 50  LEU B CD1 1 
ATOM   2701 C CD2 . LEU B 1 50  ? -28.345 -14.145 -12.768 1.00 29.73  ? 50  LEU B CD2 1 
ATOM   2702 N N   . ARG B 1 51  ? -33.256 -11.826 -12.199 1.00 40.48  ? 51  ARG B N   1 
ATOM   2703 C CA  . ARG B 1 51  ? -34.493 -11.829 -11.395 1.00 43.45  ? 51  ARG B CA  1 
ATOM   2704 C C   . ARG B 1 51  ? -35.514 -12.679 -12.146 1.00 39.19  ? 51  ARG B C   1 
ATOM   2705 O O   . ARG B 1 51  ? -36.267 -13.410 -11.501 1.00 41.74  ? 51  ARG B O   1 
ATOM   2706 C CB  . ARG B 1 51  ? -34.972 -10.398 -11.141 1.00 42.63  ? 51  ARG B CB  1 
ATOM   2707 C CG  . ARG B 1 51  ? -34.107 -9.638  -10.147 1.00 50.32  ? 51  ARG B CG  1 
ATOM   2708 C CD  . ARG B 1 51  ? -34.749 -8.370  -9.618  1.00 58.14  ? 51  ARG B CD  1 
ATOM   2709 N NE  . ARG B 1 51  ? -34.361 -7.198  -10.386 1.00 60.09  ? 51  ARG B NE  1 
ATOM   2710 C CZ  . ARG B 1 51  ? -33.260 -6.490  -10.170 1.00 58.80  ? 51  ARG B CZ  1 
ATOM   2711 N NH1 . ARG B 1 51  ? -32.435 -6.832  -9.196  1.00 55.67  ? 51  ARG B NH1 1 
ATOM   2712 N NH2 . ARG B 1 51  ? -32.994 -5.439  -10.923 1.00 60.07  ? 51  ARG B NH2 1 
ATOM   2713 N N   . LYS B 1 52  ? -35.505 -12.623 -13.468 1.00 40.67  ? 52  LYS B N   1 
ATOM   2714 C CA  . LYS B 1 52  ? -36.513 -13.372 -14.257 1.00 42.49  ? 52  LYS B CA  1 
ATOM   2715 C C   . LYS B 1 52  ? -36.231 -14.873 -14.142 1.00 44.51  ? 52  LYS B C   1 
ATOM   2716 O O   . LYS B 1 52  ? -37.148 -15.628 -13.813 1.00 46.24  ? 52  LYS B O   1 
ATOM   2717 C CB  . LYS B 1 52  ? -36.481 -12.911 -15.712 1.00 46.39  ? 52  LYS B CB  1 
ATOM   2718 C CG  . LYS B 1 52  ? -37.415 -13.655 -16.652 1.00 55.81  ? 52  LYS B CG  1 
ATOM   2719 C CD  . LYS B 1 52  ? -37.807 -12.836 -17.857 1.00 57.97  ? 52  LYS B CD  1 
ATOM   2720 C CE  . LYS B 1 52  ? -38.784 -13.554 -18.763 1.00 61.35  ? 52  LYS B CE  1 
ATOM   2721 N NZ  . LYS B 1 52  ? -38.313 -14.916 -19.105 1.00 58.60  ? 52  LYS B NZ  1 
ATOM   2722 N N   . ILE B 1 53  ? -34.987 -15.271 -14.390 1.00 40.48  ? 53  ILE B N   1 
ATOM   2723 C CA  . ILE B 1 53  ? -34.628 -16.720 -14.334 1.00 41.23  ? 53  ILE B CA  1 
ATOM   2724 C C   . ILE B 1 53  ? -34.831 -17.239 -12.907 1.00 38.53  ? 53  ILE B C   1 
ATOM   2725 O O   . ILE B 1 53  ? -35.188 -18.404 -12.767 1.00 41.33  ? 53  ILE B O   1 
ATOM   2726 C CB  . ILE B 1 53  ? -33.202 -16.989 -14.862 1.00 37.67  ? 53  ILE B CB  1 
ATOM   2727 C CG1 . ILE B 1 53  ? -33.080 -18.411 -15.413 1.00 37.64  ? 53  ILE B CG1 1 
ATOM   2728 C CG2 . ILE B 1 53  ? -32.154 -16.706 -13.802 1.00 37.84  ? 53  ILE B CG2 1 
ATOM   2729 C CD1 . ILE B 1 53  ? -32.393 -18.499 -16.750 1.00 38.02  ? 53  ILE B CD1 1 
ATOM   2730 N N   . ASP B 1 54  ? -34.653 -16.385 -11.902 1.00 39.83  ? 54  ASP B N   1 
ATOM   2731 C CA  . ASP B 1 54  ? -34.867 -16.835 -10.528 1.00 38.95  ? 54  ASP B CA  1 
ATOM   2732 C C   . ASP B 1 54  ? -36.330 -17.201 -10.286 1.00 44.90  ? 54  ASP B C   1 
ATOM   2733 O O   . ASP B 1 54  ? -36.628 -18.165 -9.569  1.00 42.59  ? 54  ASP B O   1 
ATOM   2734 C CB  . ASP B 1 54  ? -34.418 -15.757 -9.547  1.00 41.16  ? 54  ASP B CB  1 
ATOM   2735 C CG  . ASP B 1 54  ? -32.930 -15.826 -9.243  1.00 43.26  ? 54  ASP B CG  1 
ATOM   2736 O OD1 . ASP B 1 54  ? -32.314 -16.883 -9.524  1.00 37.87  ? 54  ASP B OD1 1 
ATOM   2737 O OD2 . ASP B 1 54  ? -32.383 -14.826 -8.724  1.00 40.47  ? 54  ASP B OD2 1 
ATOM   2738 N N   . GLU B 1 55  ? -37.259 -16.437 -10.868 1.00 42.82  ? 55  GLU B N   1 
ATOM   2739 C CA  . GLU B 1 55  ? -38.675 -16.784 -10.752 1.00 45.36  ? 55  GLU B CA  1 
ATOM   2740 C C   . GLU B 1 55  ? -38.994 -18.095 -11.452 1.00 46.96  ? 55  GLU B C   1 
ATOM   2741 O O   . GLU B 1 55  ? -39.883 -18.833 -11.014 1.00 49.90  ? 55  GLU B O   1 
ATOM   2742 C CB  . GLU B 1 55  ? -39.555 -15.679 -11.340 1.00 48.14  ? 55  GLU B CB  1 
ATOM   2743 C CG  . GLU B 1 55  ? -39.996 -14.640 -10.341 1.00 54.89  ? 55  GLU B CG  1 
ATOM   2744 C CD  . GLU B 1 55  ? -40.175 -13.276 -10.973 1.00 59.93  ? 55  GLU B CD  1 
ATOM   2745 O OE1 . GLU B 1 55  ? -39.995 -12.267 -10.260 1.00 64.93  ? 55  GLU B OE1 1 
ATOM   2746 O OE2 . GLU B 1 55  ? -40.517 -13.219 -12.178 1.00 59.78  ? 55  GLU B OE2 1 
ATOM   2747 N N   . GLU B 1 56  ? -38.288 -18.390 -12.542 1.00 42.96  ? 56  GLU B N   1 
ATOM   2748 C CA  . GLU B 1 56  ? -38.636 -19.575 -13.361 1.00 41.72  ? 56  GLU B CA  1 
ATOM   2749 C C   . GLU B 1 56  ? -37.894 -20.832 -12.919 1.00 43.07  ? 56  GLU B C   1 
ATOM   2750 O O   . GLU B 1 56  ? -38.441 -21.918 -13.121 1.00 40.59  ? 56  GLU B O   1 
ATOM   2751 C CB  . GLU B 1 56  ? -38.296 -19.252 -14.811 1.00 44.07  ? 56  GLU B CB  1 
ATOM   2752 C CG  . GLU B 1 56  ? -38.992 -18.006 -15.318 1.00 47.04  ? 56  GLU B CG  1 
ATOM   2753 C CD  . GLU B 1 56  ? -38.333 -17.346 -16.514 1.00 53.68  ? 56  GLU B CD  1 
ATOM   2754 O OE1 . GLU B 1 56  ? -37.222 -17.765 -16.882 1.00 51.16  ? 56  GLU B OE1 1 
ATOM   2755 O OE2 . GLU B 1 56  ? -38.936 -16.416 -17.073 1.00 56.29  ? 56  GLU B OE2 1 
ATOM   2756 N N   . ALA B 1 57  ? -36.712 -20.690 -12.331 1.00 39.61  ? 57  ALA B N   1 
ATOM   2757 C CA  . ALA B 1 57  ? -35.883 -21.842 -12.022 1.00 40.88  ? 57  ALA B CA  1 
ATOM   2758 C C   . ALA B 1 57  ? -35.939 -22.230 -10.557 1.00 40.84  ? 57  ALA B C   1 
ATOM   2759 O O   . ALA B 1 57  ? -35.324 -23.231 -10.172 1.00 38.68  ? 57  ALA B O   1 
ATOM   2760 C CB  . ALA B 1 57  ? -34.433 -21.570 -12.438 1.00 38.55  ? 57  ALA B CB  1 
ATOM   2761 N N   . SER B 1 58  ? -36.646 -21.465 -9.731  1.00 38.73  ? 58  SER B N   1 
ATOM   2762 C CA  . SER B 1 58  ? -36.907 -21.859 -8.356  1.00 44.13  ? 58  SER B CA  1 
ATOM   2763 C C   . SER B 1 58  ? -38.363 -21.559 -8.032  1.00 47.78  ? 58  SER B C   1 
ATOM   2764 O O   . SER B 1 58  ? -38.891 -20.515 -8.424  1.00 48.81  ? 58  SER B O   1 
ATOM   2765 C CB  . SER B 1 58  ? -35.984 -21.136 -7.371  1.00 42.77  ? 58  SER B CB  1 
ATOM   2766 O OG  . SER B 1 58  ? -36.207 -19.737 -7.414  1.00 43.44  ? 58  SER B OG  1 
ATOM   2767 N N   . GLU B 1 59  ? -39.007 -22.479 -7.325  1.00 50.73  ? 59  GLU B N   1 
ATOM   2768 C CA  . GLU B 1 59  ? -40.418 -22.319 -7.016  1.00 53.27  ? 59  GLU B CA  1 
ATOM   2769 C C   . GLU B 1 59  ? -40.607 -21.389 -5.827  1.00 51.70  ? 59  GLU B C   1 
ATOM   2770 O O   . GLU B 1 59  ? -39.781 -21.335 -4.912  1.00 49.70  ? 59  GLU B O   1 
ATOM   2771 C CB  . GLU B 1 59  ? -41.074 -23.675 -6.741  1.00 54.21  ? 59  GLU B CB  1 
ATOM   2772 C CG  . GLU B 1 59  ? -41.420 -24.449 -8.012  1.00 58.05  ? 59  GLU B CG  1 
ATOM   2773 C CD  . GLU B 1 59  ? -40.934 -25.887 -7.987  1.00 62.68  ? 59  GLU B CD  1 
ATOM   2774 O OE1 . GLU B 1 59  ? -40.031 -26.203 -7.181  1.00 65.17  ? 59  GLU B OE1 1 
ATOM   2775 O OE2 . GLU B 1 59  ? -41.447 -26.702 -8.789  1.00 65.44  ? 59  GLU B OE2 1 
ATOM   2776 N N   . GLU B 1 60  ? -41.707 -20.641 -5.861  1.00 50.91  ? 60  GLU B N   1 
ATOM   2777 C CA  . GLU B 1 60  ? -42.055 -19.761 -4.756  1.00 54.60  ? 60  GLU B CA  1 
ATOM   2778 C C   . GLU B 1 60  ? -42.134 -20.546 -3.450  1.00 54.06  ? 60  GLU B C   1 
ATOM   2779 O O   . GLU B 1 60  ? -42.452 -21.740 -3.432  1.00 56.56  ? 60  GLU B O   1 
ATOM   2780 C CB  . GLU B 1 60  ? -43.389 -19.072 -5.039  1.00 56.72  ? 60  GLU B CB  1 
ATOM   2781 C CG  . GLU B 1 60  ? -43.474 -17.631 -4.572  1.00 59.38  ? 60  GLU B CG  1 
ATOM   2782 C CD  . GLU B 1 60  ? -44.879 -17.069 -4.717  1.00 68.44  ? 60  GLU B CD  1 
ATOM   2783 O OE1 . GLU B 1 60  ? -45.717 -17.307 -3.818  1.00 68.29  ? 60  GLU B OE1 1 
ATOM   2784 O OE2 . GLU B 1 60  ? -45.148 -16.397 -5.738  1.00 69.18  ? 60  GLU B OE2 1 
ATOM   2785 N N   . GLY B 1 61  ? -41.818 -19.865 -2.347  1.00 52.87  ? 61  GLY B N   1 
ATOM   2786 C CA  . GLY B 1 61  ? -41.915 -20.452 -1.027  1.00 53.04  ? 61  GLY B CA  1 
ATOM   2787 C C   . GLY B 1 61  ? -40.788 -21.382 -0.635  1.00 56.17  ? 61  GLY B C   1 
ATOM   2788 O O   . GLY B 1 61  ? -40.702 -21.756 0.542   1.00 59.61  ? 61  GLY B O   1 
ATOM   2789 N N   . THR B 1 62  ? -39.916 -21.762 -1.564  1.00 54.08  ? 62  THR B N   1 
ATOM   2790 C CA  . THR B 1 62  ? -38.841 -22.694 -1.263  1.00 54.05  ? 62  THR B CA  1 
ATOM   2791 C C   . THR B 1 62  ? -37.629 -21.961 -0.690  1.00 54.58  ? 62  THR B C   1 
ATOM   2792 O O   . THR B 1 62  ? -37.467 -20.747 -0.853  1.00 53.53  ? 62  THR B O   1 
ATOM   2793 C CB  . THR B 1 62  ? -38.439 -23.461 -2.520  1.00 52.38  ? 62  THR B CB  1 
ATOM   2794 O OG1 . THR B 1 62  ? -37.871 -22.550 -3.471  1.00 50.28  ? 62  THR B OG1 1 
ATOM   2795 C CG2 . THR B 1 62  ? -39.649 -24.137 -3.145  1.00 51.35  ? 62  THR B CG2 1 
ATOM   2796 N N   . ARG B 1 63  ? -36.766 -22.720 -0.008  1.00 53.26  ? 63  ARG B N   1 
ATOM   2797 C CA  . ARG B 1 63  ? -35.539 -22.133 0.522   1.00 51.56  ? 63  ARG B CA  1 
ATOM   2798 C C   . ARG B 1 63  ? -34.621 -21.661 -0.600  1.00 49.12  ? 63  ARG B C   1 
ATOM   2799 O O   . ARG B 1 63  ? -33.965 -20.620 -0.471  1.00 49.21  ? 63  ARG B O   1 
ATOM   2800 C CB  . ARG B 1 63  ? -34.805 -23.129 1.423   1.00 57.27  ? 63  ARG B CB  1 
ATOM   2801 C CG  . ARG B 1 63  ? -35.643 -23.685 2.559   1.00 62.45  ? 63  ARG B CG  1 
ATOM   2802 C CD  . ARG B 1 63  ? -34.884 -23.681 3.882   1.00 71.45  ? 63  ARG B CD  1 
ATOM   2803 N NE  . ARG B 1 63  ? -35.586 -24.440 4.912   1.00 76.05  ? 63  ARG B NE  1 
ATOM   2804 C CZ  . ARG B 1 63  ? -36.348 -23.902 5.856   1.00 77.50  ? 63  ARG B CZ  1 
ATOM   2805 N NH1 . ARG B 1 63  ? -36.551 -22.595 5.920   1.00 76.18  ? 63  ARG B NH1 1 
ATOM   2806 N NH2 . ARG B 1 63  ? -36.932 -24.696 6.751   1.00 76.22  ? 63  ARG B NH2 1 
ATOM   2807 N N   . GLU B 1 64  ? -34.568 -22.403 -1.711  1.00 48.57  ? 64  GLU B N   1 
ATOM   2808 C CA  . GLU B 1 64  ? -33.686 -22.016 -2.807  1.00 46.41  ? 64  GLU B CA  1 
ATOM   2809 C C   . GLU B 1 64  ? -34.128 -20.691 -3.416  1.00 45.92  ? 64  GLU B C   1 
ATOM   2810 O O   . GLU B 1 64  ? -33.291 -19.865 -3.800  1.00 43.89  ? 64  GLU B O   1 
ATOM   2811 C CB  . GLU B 1 64  ? -33.654 -23.103 -3.879  1.00 43.53  ? 64  GLU B CB  1 
ATOM   2812 C CG  . GLU B 1 64  ? -35.030 -23.563 -4.322  1.00 46.06  ? 64  GLU B CG  1 
ATOM   2813 C CD  . GLU B 1 64  ? -35.559 -24.750 -3.546  1.00 47.69  ? 64  GLU B CD  1 
ATOM   2814 O OE1 . GLU B 1 64  ? -35.279 -24.869 -2.332  1.00 47.69  ? 64  GLU B OE1 1 
ATOM   2815 O OE2 . GLU B 1 64  ? -36.319 -25.529 -4.153  1.00 49.59  ? 64  GLU B OE2 1 
ATOM   2816 N N   . ARG B 1 65  ? -35.443 -20.473 -3.515  1.00 47.09  ? 65  ARG B N   1 
ATOM   2817 C CA  . ARG B 1 65  ? -35.954 -19.191 -3.990  1.00 46.62  ? 65  ARG B CA  1 
ATOM   2818 C C   . ARG B 1 65  ? -35.501 -18.067 -3.074  1.00 44.09  ? 65  ARG B C   1 
ATOM   2819 O O   . ARG B 1 65  ? -35.022 -17.026 -3.533  1.00 45.24  ? 65  ARG B O   1 
ATOM   2820 C CB  . ARG B 1 65  ? -37.480 -19.235 -4.061  1.00 47.17  ? 65  ARG B CB  1 
ATOM   2821 C CG  . ARG B 1 65  ? -38.149 -17.885 -4.198  1.00 48.34  ? 65  ARG B CG  1 
ATOM   2822 C CD  . ARG B 1 65  ? -37.838 -17.279 -5.546  1.00 45.96  ? 65  ARG B CD  1 
ATOM   2823 N NE  . ARG B 1 65  ? -38.607 -17.904 -6.615  1.00 49.87  ? 65  ARG B NE  1 
ATOM   2824 C CZ  . ARG B 1 65  ? -39.788 -17.478 -7.046  1.00 51.67  ? 65  ARG B CZ  1 
ATOM   2825 N NH1 . ARG B 1 65  ? -40.384 -16.426 -6.507  1.00 51.92  ? 65  ARG B NH1 1 
ATOM   2826 N NH2 . ARG B 1 65  ? -40.383 -18.120 -8.047  1.00 52.33  ? 65  ARG B NH2 1 
ATOM   2827 N N   . ARG B 1 66  ? -35.642 -18.272 -1.765  1.00 44.55  ? 66  ARG B N   1 
ATOM   2828 C CA  . ARG B 1 66  ? -35.222 -17.271 -0.795  1.00 46.69  ? 66  ARG B CA  1 
ATOM   2829 C C   . ARG B 1 66  ? -33.725 -16.997 -0.891  1.00 47.85  ? 66  ARG B C   1 
ATOM   2830 O O   . ARG B 1 66  ? -33.296 -15.836 -0.866  1.00 43.54  ? 66  ARG B O   1 
ATOM   2831 C CB  . ARG B 1 66  ? -35.619 -17.741 0.603   1.00 49.97  ? 66  ARG B CB  1 
ATOM   2832 C CG  . ARG B 1 66  ? -36.174 -16.670 1.524   1.00 57.28  ? 66  ARG B CG  1 
ATOM   2833 C CD  . ARG B 1 66  ? -36.414 -17.272 2.893   1.00 61.47  ? 66  ARG B CD  1 
ATOM   2834 N NE  . ARG B 1 66  ? -36.839 -18.659 2.738   1.00 64.29  ? 66  ARG B NE  1 
ATOM   2835 C CZ  . ARG B 1 66  ? -37.146 -19.480 3.733   1.00 67.81  ? 66  ARG B CZ  1 
ATOM   2836 N NH1 . ARG B 1 66  ? -37.120 -19.078 4.994   1.00 68.16  ? 66  ARG B NH1 1 
ATOM   2837 N NH2 . ARG B 1 66  ? -37.495 -20.734 3.454   1.00 64.98  ? 66  ARG B NH2 1 
ATOM   2838 N N   . ARG B 1 67  ? -32.915 -18.053 -1.018  1.00 46.09  ? 67  ARG B N   1 
ATOM   2839 C CA  . ARG B 1 67  ? -31.472 -17.871 -1.145  1.00 42.62  ? 67  ARG B CA  1 
ATOM   2840 C C   . ARG B 1 67  ? -31.120 -17.115 -2.417  1.00 40.08  ? 67  ARG B C   1 
ATOM   2841 O O   . ARG B 1 67  ? -30.158 -16.339 -2.435  1.00 42.70  ? 67  ARG B O   1 
ATOM   2842 C CB  . ARG B 1 67  ? -30.777 -19.232 -1.126  1.00 44.86  ? 67  ARG B CB  1 
ATOM   2843 C CG  . ARG B 1 67  ? -30.643 -19.839 0.254   1.00 46.60  ? 67  ARG B CG  1 
ATOM   2844 C CD  . ARG B 1 67  ? -29.470 -20.797 0.298   1.00 49.29  ? 67  ARG B CD  1 
ATOM   2845 N NE  . ARG B 1 67  ? -29.428 -21.555 1.541   1.00 54.87  ? 67  ARG B NE  1 
ATOM   2846 C CZ  . ARG B 1 67  ? -28.664 -22.621 1.739   1.00 59.03  ? 67  ARG B CZ  1 
ATOM   2847 N NH1 . ARG B 1 67  ? -27.897 -23.109 0.776   1.00 55.65  ? 67  ARG B NH1 1 
ATOM   2848 N NH2 . ARG B 1 67  ? -28.678 -23.218 2.928   1.00 63.53  ? 67  ARG B NH2 1 
ATOM   2849 N N   . ALA B 1 68  ? -31.893 -17.320 -3.482  1.00 39.99  ? 68  ALA B N   1 
ATOM   2850 C CA  . ALA B 1 68  ? -31.646 -16.601 -4.724  1.00 41.65  ? 68  ALA B CA  1 
ATOM   2851 C C   . ALA B 1 68  ? -31.895 -15.107 -4.555  1.00 44.91  ? 68  ALA B C   1 
ATOM   2852 O O   . ALA B 1 68  ? -31.177 -14.286 -5.136  1.00 43.47  ? 68  ALA B O   1 
ATOM   2853 C CB  . ALA B 1 68  ? -32.520 -17.170 -5.840  1.00 39.28  ? 68  ALA B CB  1 
ATOM   2854 N N   . LEU B 1 69  ? -32.906 -14.729 -3.766  1.00 46.39  ? 69  LEU B N   1 
ATOM   2855 C CA  . LEU B 1 69  ? -33.163 -13.302 -3.573  1.00 49.14  ? 69  LEU B CA  1 
ATOM   2856 C C   . LEU B 1 69  ? -32.079 -12.653 -2.722  1.00 48.14  ? 69  LEU B C   1 
ATOM   2857 O O   . LEU B 1 69  ? -31.618 -11.553 -3.045  1.00 51.32  ? 69  LEU B O   1 
ATOM   2858 C CB  . LEU B 1 69  ? -34.546 -13.069 -2.959  1.00 51.30  ? 69  LEU B CB  1 
ATOM   2859 C CG  . LEU B 1 69  ? -35.715 -14.005 -3.284  1.00 55.45  ? 69  LEU B CG  1 
ATOM   2860 C CD1 . LEU B 1 69  ? -36.989 -13.525 -2.588  1.00 57.73  ? 69  LEU B CD1 1 
ATOM   2861 C CD2 . LEU B 1 69  ? -35.961 -14.156 -4.791  1.00 53.17  ? 69  LEU B CD2 1 
ATOM   2862 N N   . ILE B 1 70  ? -31.662 -13.309 -1.631  1.00 48.53  ? 70  ILE B N   1 
ATOM   2863 C CA  . ILE B 1 70  ? -30.554 -12.786 -0.826  1.00 49.33  ? 70  ILE B CA  1 
ATOM   2864 C C   . ILE B 1 70  ? -29.317 -12.590 -1.686  1.00 49.99  ? 70  ILE B C   1 
ATOM   2865 O O   . ILE B 1 70  ? -28.621 -11.572 -1.583  1.00 49.07  ? 70  ILE B O   1 
ATOM   2866 C CB  . ILE B 1 70  ? -30.253 -13.713 0.367   1.00 51.00  ? 70  ILE B CB  1 
ATOM   2867 C CG1 . ILE B 1 70  ? -31.528 -14.063 1.137   1.00 53.30  ? 70  ILE B CG1 1 
ATOM   2868 C CG2 . ILE B 1 70  ? -29.189 -13.103 1.267   1.00 53.74  ? 70  ILE B CG2 1 
ATOM   2869 C CD1 . ILE B 1 70  ? -31.410 -15.347 1.943   1.00 55.78  ? 70  ILE B CD1 1 
ATOM   2870 N N   . ARG B 1 71  ? -29.035 -13.555 -2.560  1.00 49.75  ? 71  ARG B N   1 
ATOM   2871 C CA  . ARG B 1 71  ? -27.851 -13.512 -3.406  1.00 44.24  ? 71  ARG B CA  1 
ATOM   2872 C C   . ARG B 1 71  ? -27.895 -12.353 -4.398  1.00 43.93  ? 71  ARG B C   1 
ATOM   2873 O O   . ARG B 1 71  ? -26.840 -11.910 -4.867  1.00 44.89  ? 71  ARG B O   1 
ATOM   2874 C CB  . ARG B 1 71  ? -27.715 -14.874 -4.112  1.00 44.97  ? 71  ARG B CB  1 
ATOM   2875 C CG  . ARG B 1 71  ? -26.729 -14.952 -5.247  1.00 42.00  ? 71  ARG B CG  1 
ATOM   2876 C CD  . ARG B 1 71  ? -26.456 -16.413 -5.602  1.00 33.09  ? 71  ARG B CD  1 
ATOM   2877 N NE  . ARG B 1 71  ? -27.599 -17.090 -6.216  1.00 34.72  ? 71  ARG B NE  1 
ATOM   2878 C CZ  . ARG B 1 71  ? -28.256 -18.119 -5.692  1.00 32.78  ? 71  ARG B CZ  1 
ATOM   2879 N NH1 . ARG B 1 71  ? -27.978 -18.579 -4.481  1.00 36.85  ? 71  ARG B NH1 1 
ATOM   2880 N NH2 . ARG B 1 71  ? -29.224 -18.697 -6.399  1.00 32.94  ? 71  ARG B NH2 1 
ATOM   2881 N N   . HIS B 1 72  ? -29.081 -11.812 -4.686  1.00 44.35  ? 72  HIS B N   1 
ATOM   2882 C CA  . HIS B 1 72  ? -29.235 -10.709 -5.628  1.00 46.62  ? 72  HIS B CA  1 
ATOM   2883 C C   . HIS B 1 72  ? -29.821 -9.456  -4.973  1.00 49.35  ? 72  HIS B C   1 
ATOM   2884 O O   . HIS B 1 72  ? -30.530 -8.688  -5.623  1.00 48.91  ? 72  HIS B O   1 
ATOM   2885 C CB  . HIS B 1 72  ? -30.080 -11.154 -6.823  1.00 44.87  ? 72  HIS B CB  1 
ATOM   2886 C CG  . HIS B 1 72  ? -29.468 -12.286 -7.591  1.00 41.31  ? 72  HIS B CG  1 
ATOM   2887 N ND1 . HIS B 1 72  ? -28.318 -12.139 -8.339  1.00 38.89  ? 72  HIS B ND1 1 
ATOM   2888 C CD2 . HIS B 1 72  ? -29.788 -13.601 -7.649  1.00 41.53  ? 72  HIS B CD2 1 
ATOM   2889 C CE1 . HIS B 1 72  ? -27.986 -13.306 -8.866  1.00 39.46  ? 72  HIS B CE1 1 
ATOM   2890 N NE2 . HIS B 1 72  ? -28.853 -14.212 -8.451  1.00 39.63  ? 72  HIS B NE2 1 
ATOM   2891 N N   . THR B 1 73  ? -29.484 -9.217  -3.702  1.00 51.35  ? 73  THR B N   1 
ATOM   2892 C CA  . THR B 1 73  ? -29.986 -8.019  -2.972  1.00 50.79  ? 73  THR B CA  1 
ATOM   2893 C C   . THR B 1 73  ? -28.858 -7.216  -2.311  1.00 53.43  ? 73  THR B C   1 
ATOM   2894 O O   . THR B 1 73  ? -29.175 -6.219  -1.660  1.00 56.20  ? 73  THR B O   1 
ATOM   2895 C CB  . THR B 1 73  ? -31.012 -8.411  -1.900  1.00 52.83  ? 73  THR B CB  1 
ATOM   2896 O OG1 . THR B 1 73  ? -30.508 -9.520  -1.157  1.00 57.17  ? 73  THR B OG1 1 
ATOM   2897 C CG2 . THR B 1 73  ? -32.368 -8.742  -2.483  1.00 51.39  ? 73  THR B CG2 1 
ATOM   2898 N N   . ASN B 1 74  ? -27.598 -7.615  -2.458  1.00 49.09  ? 74  ASN B N   1 
ATOM   2899 C CA  . ASN B 1 74  ? -26.495 -6.784  -1.898  1.00 53.91  ? 74  ASN B CA  1 
ATOM   2900 C C   . ASN B 1 74  ? -26.584 -5.387  -2.518  1.00 54.06  ? 74  ASN B C   1 
ATOM   2901 O O   . ASN B 1 74  ? -26.485 -5.277  -3.744  1.00 52.26  ? 74  ASN B O   1 
ATOM   2902 C CB  . ASN B 1 74  ? -25.127 -7.441  -2.101  1.00 52.49  ? 74  ASN B CB  1 
ATOM   2903 C CG  . ASN B 1 74  ? -23.953 -6.641  -1.573  1.00 53.90  ? 74  ASN B CG  1 
ATOM   2904 O OD1 . ASN B 1 74  ? -24.105 -5.511  -1.118  1.00 52.55  ? 74  ASN B OD1 1 
ATOM   2905 N ND2 . ASN B 1 74  ? -22.770 -7.230  -1.624  1.00 49.64  ? 74  ASN B ND2 1 
ATOM   2906 N N   . PRO B 1 75  ? -26.775 -4.319  -1.715  1.00 55.79  ? 75  PRO B N   1 
ATOM   2907 C CA  . PRO B 1 75  ? -26.933 -2.980  -2.249  1.00 53.37  ? 75  PRO B CA  1 
ATOM   2908 C C   . PRO B 1 75  ? -25.643 -2.512  -2.922  1.00 54.88  ? 75  PRO B C   1 
ATOM   2909 O O   . PRO B 1 75  ? -25.692 -1.583  -3.690  1.00 55.18  ? 75  PRO B O   1 
ATOM   2910 C CB  . PRO B 1 75  ? -27.166 -2.134  -0.996  1.00 55.27  ? 75  PRO B CB  1 
ATOM   2911 C CG  . PRO B 1 75  ? -26.535 -2.927  0.115   1.00 58.31  ? 75  PRO B CG  1 
ATOM   2912 C CD  . PRO B 1 75  ? -26.833 -4.362  -0.257  1.00 60.13  ? 75  PRO B CD  1 
ATOM   2913 N N   . TYR B 1 76  ? -24.529 -3.176  -2.618  1.00 53.13  ? 76  TYR B N   1 
ATOM   2914 C CA  . TYR B 1 76  ? -23.226 -2.762  -3.192  1.00 52.75  ? 76  TYR B CA  1 
ATOM   2915 C C   . TYR B 1 76  ? -23.039 -3.420  -4.551  1.00 49.65  ? 76  TYR B C   1 
ATOM   2916 O O   . TYR B 1 76  ? -22.112 -3.061  -5.283  1.00 46.23  ? 76  TYR B O   1 
ATOM   2917 C CB  . TYR B 1 76  ? -22.085 -3.132  -2.248  1.00 52.13  ? 76  TYR B CB  1 
ATOM   2918 C CG  . TYR B 1 76  ? -22.009 -2.248  -1.033  1.00 54.72  ? 76  TYR B CG  1 
ATOM   2919 C CD1 . TYR B 1 76  ? -22.832 -2.467  0.056   1.00 56.73  ? 76  TYR B CD1 1 
ATOM   2920 C CD2 . TYR B 1 76  ? -21.133 -1.178  -0.985  1.00 56.18  ? 76  TYR B CD2 1 
ATOM   2921 C CE1 . TYR B 1 76  ? -22.777 -1.652  1.173   1.00 59.19  ? 76  TYR B CE1 1 
ATOM   2922 C CE2 . TYR B 1 76  ? -21.063 -0.355  0.125   1.00 55.91  ? 76  TYR B CE2 1 
ATOM   2923 C CZ  . TYR B 1 76  ? -21.889 -0.594  1.207   1.00 59.90  ? 76  TYR B CZ  1 
ATOM   2924 O OH  . TYR B 1 76  ? -21.830 0.210   2.307   1.00 64.97  ? 76  TYR B OH  1 
ATOM   2925 N N   . GLY B 1 77  ? -23.922 -4.357  -4.868  1.00 48.83  ? 77  GLY B N   1 
ATOM   2926 C CA  . GLY B 1 77  ? -23.822 -4.960  -6.199  1.00 45.80  ? 77  GLY B CA  1 
ATOM   2927 C C   . GLY B 1 77  ? -24.126 -6.436  -6.262  1.00 43.55  ? 77  GLY B C   1 
ATOM   2928 O O   . GLY B 1 77  ? -24.158 -7.081  -5.212  1.00 44.08  ? 77  GLY B O   1 
ATOM   2929 N N   . ASP B 1 78  ? -24.309 -6.935  -7.468  1.00 36.36  ? 78  ASP B N   1 
ATOM   2930 C CA  . ASP B 1 78  ? -24.672 -8.309  -7.760  1.00 35.11  ? 78  ASP B CA  1 
ATOM   2931 C C   . ASP B 1 78  ? -23.419 -9.149  -7.983  1.00 34.37  ? 78  ASP B C   1 
ATOM   2932 O O   . ASP B 1 78  ? -22.448 -8.661  -8.569  1.00 32.33  ? 78  ASP B O   1 
ATOM   2933 C CB  . ASP B 1 78  ? -25.557 -8.346  -9.000  1.00 34.17  ? 78  ASP B CB  1 
ATOM   2934 C CG  . ASP B 1 78  ? -26.183 -9.689  -9.217  1.00 37.06  ? 78  ASP B CG  1 
ATOM   2935 O OD1 . ASP B 1 78  ? -25.520 -10.547 -9.829  1.00 34.08  ? 78  ASP B OD1 1 
ATOM   2936 O OD2 . ASP B 1 78  ? -27.313 -9.900  -8.728  1.00 38.38  ? 78  ASP B OD2 1 
ATOM   2937 N N   . PRO B 1 79  ? -23.412 -10.414 -7.532  1.00 34.00  ? 79  PRO B N   1 
ATOM   2938 C CA  . PRO B 1 79  ? -22.209 -11.243 -7.729  1.00 31.24  ? 79  PRO B CA  1 
ATOM   2939 C C   . PRO B 1 79  ? -21.816 -11.389 -9.183  1.00 30.66  ? 79  PRO B C   1 
ATOM   2940 O O   . PRO B 1 79  ? -20.621 -11.420 -9.492  1.00 31.59  ? 79  PRO B O   1 
ATOM   2941 C CB  . PRO B 1 79  ? -22.602 -12.597 -7.113  1.00 35.37  ? 79  PRO B CB  1 
ATOM   2942 C CG  . PRO B 1 79  ? -24.101 -12.559 -7.011  1.00 38.70  ? 79  PRO B CG  1 
ATOM   2943 C CD  . PRO B 1 79  ? -24.432 -11.123 -6.744  1.00 33.53  ? 79  PRO B CD  1 
ATOM   2944 N N   . PHE B 1 80  ? -22.788 -11.455 -10.103 1.00 28.38  ? 80  PHE B N   1 
ATOM   2945 C CA  . PHE B 1 80  ? -22.429 -11.598 -11.507 1.00 29.65  ? 80  PHE B CA  1 
ATOM   2946 C C   . PHE B 1 80  ? -21.946 -10.296 -12.128 1.00 28.88  ? 80  PHE B C   1 
ATOM   2947 O O   . PHE B 1 80  ? -20.977 -10.299 -12.897 1.00 27.83  ? 80  PHE B O   1 
ATOM   2948 C CB  . PHE B 1 80  ? -23.609 -12.175 -12.290 1.00 29.08  ? 80  PHE B CB  1 
ATOM   2949 C CG  . PHE B 1 80  ? -23.851 -13.611 -11.971 1.00 29.37  ? 80  PHE B CG  1 
ATOM   2950 C CD1 . PHE B 1 80  ? -23.007 -14.583 -12.481 1.00 28.31  ? 80  PHE B CD1 1 
ATOM   2951 C CD2 . PHE B 1 80  ? -24.866 -13.988 -11.104 1.00 31.04  ? 80  PHE B CD2 1 
ATOM   2952 C CE1 . PHE B 1 80  ? -23.201 -15.917 -12.163 1.00 29.61  ? 80  PHE B CE1 1 
ATOM   2953 C CE2 . PHE B 1 80  ? -25.070 -15.316 -10.796 1.00 32.00  ? 80  PHE B CE2 1 
ATOM   2954 C CZ  . PHE B 1 80  ? -24.233 -16.279 -11.321 1.00 30.62  ? 80  PHE B CZ  1 
ATOM   2955 N N   . THR B 1 81  ? -22.610 -9.174  -11.854 1.00 28.64  ? 81  THR B N   1 
ATOM   2956 C CA  . THR B 1 81  ? -22.184 -7.949  -12.501 1.00 29.98  ? 81  THR B CA  1 
ATOM   2957 C C   . THR B 1 81  ? -20.871 -7.431  -11.934 1.00 30.00  ? 81  THR B C   1 
ATOM   2958 O O   . THR B 1 81  ? -20.211 -6.622  -12.590 1.00 31.82  ? 81  THR B O   1 
ATOM   2959 C CB  . THR B 1 81  ? -23.271 -6.890  -12.368 1.00 32.83  ? 81  THR B CB  1 
ATOM   2960 O OG1 . THR B 1 81  ? -23.527 -6.671  -10.976 1.00 33.67  ? 81  THR B OG1 1 
ATOM   2961 C CG2 . THR B 1 81  ? -24.539 -7.397  -13.048 1.00 33.54  ? 81  THR B CG2 1 
ATOM   2962 N N   . ILE B 1 82  ? -20.473 -7.892  -10.748 1.00 29.81  ? 82  ILE B N   1 
ATOM   2963 C CA  . ILE B 1 82  ? -19.169 -7.539  -10.189 1.00 28.53  ? 82  ILE B CA  1 
ATOM   2964 C C   . ILE B 1 82  ? -18.121 -8.546  -10.652 1.00 27.50  ? 82  ILE B C   1 
ATOM   2965 O O   . ILE B 1 82  ? -17.173 -8.184  -11.358 1.00 28.34  ? 82  ILE B O   1 
ATOM   2966 C CB  . ILE B 1 82  ? -19.232 -7.429  -8.652  1.00 29.32  ? 82  ILE B CB  1 
ATOM   2967 C CG1 . ILE B 1 82  ? -20.053 -6.193  -8.260  1.00 31.18  ? 82  ILE B CG1 1 
ATOM   2968 C CG2 . ILE B 1 82  ? -17.837 -7.360  -8.035  1.00 28.41  ? 82  ILE B CG2 1 
ATOM   2969 C CD1 . ILE B 1 82  ? -20.397 -6.116  -6.811  1.00 34.59  ? 82  ILE B CD1 1 
ATOM   2970 N N   . CYS B 1 83  ? -18.274 -9.810  -10.280 1.00 29.50  ? 83  CYS B N   1 
ATOM   2971 C CA  . CYS B 1 83  ? -17.205 -10.805 -10.570 1.00 30.09  ? 83  CYS B CA  1 
ATOM   2972 C C   . CYS B 1 83  ? -16.985 -11.023 -12.069 1.00 28.12  ? 83  CYS B C   1 
ATOM   2973 O O   . CYS B 1 83  ? -15.853 -11.303 -12.449 1.00 27.26  ? 83  CYS B O   1 
ATOM   2974 C CB  . CYS B 1 83  ? -17.536 -12.121 -9.883  1.00 30.27  ? 83  CYS B CB  1 
ATOM   2975 S SG  . CYS B 1 83  ? -17.754 -11.962 -8.094  1.00 31.82  ? 83  CYS B SG  1 
ATOM   2976 N N   . HIS B 1 84  ? -18.036 -10.906 -12.872 1.00 26.10  ? 84  HIS B N   1 
ATOM   2977 C CA  . HIS B 1 84  ? -17.916 -11.139 -14.306 1.00 27.56  ? 84  HIS B CA  1 
ATOM   2978 C C   . HIS B 1 84  ? -17.998 -9.822  -15.077 1.00 26.29  ? 84  HIS B C   1 
ATOM   2979 O O   . HIS B 1 84  ? -18.436 -9.781  -16.232 1.00 28.47  ? 84  HIS B O   1 
ATOM   2980 C CB  . HIS B 1 84  ? -18.986 -12.123 -14.776 1.00 27.44  ? 84  HIS B CB  1 
ATOM   2981 C CG  . HIS B 1 84  ? -18.807 -13.503 -14.206 1.00 28.20  ? 84  HIS B CG  1 
ATOM   2982 N ND1 . HIS B 1 84  ? -18.080 -14.487 -14.836 1.00 29.64  ? 84  HIS B ND1 1 
ATOM   2983 C CD2 . HIS B 1 84  ? -19.270 -14.053 -13.059 1.00 26.46  ? 84  HIS B CD2 1 
ATOM   2984 C CE1 . HIS B 1 84  ? -18.100 -15.589 -14.097 1.00 28.62  ? 84  HIS B CE1 1 
ATOM   2985 N NE2 . HIS B 1 84  ? -18.820 -15.352 -13.015 1.00 28.41  ? 84  HIS B NE2 1 
ATOM   2986 N N   . CYS B 1 85  ? -17.574 -8.736  -14.425 1.00 28.62  ? 85  CYS B N   1 
ATOM   2987 C CA  . CYS B 1 85  ? -17.662 -7.405  -15.021 1.00 28.32  ? 85  CYS B CA  1 
ATOM   2988 C C   . CYS B 1 85  ? -16.823 -7.257  -16.281 1.00 30.61  ? 85  CYS B C   1 
ATOM   2989 O O   . CYS B 1 85  ? -17.025 -6.296  -17.040 1.00 30.50  ? 85  CYS B O   1 
ATOM   2990 C CB  . CYS B 1 85  ? -17.252 -6.378  -13.958 1.00 29.31  ? 85  CYS B CB  1 
ATOM   2991 S SG  . CYS B 1 85  ? -15.481 -6.370  -13.591 1.00 29.47  ? 85  CYS B SG  1 
ATOM   2992 N N   . SER B 1 86  ? -15.893 -8.174  -16.524 1.00 26.92  ? 86  SER B N   1 
ATOM   2993 C CA  . SER B 1 86  ? -15.069 -8.145  -17.723 1.00 28.58  ? 86  SER B CA  1 
ATOM   2994 C C   . SER B 1 86  ? -15.807 -8.627  -18.968 1.00 26.51  ? 86  SER B C   1 
ATOM   2995 O O   . SER B 1 86  ? -15.275 -8.452  -20.067 1.00 28.41  ? 86  SER B O   1 
ATOM   2996 C CB  . SER B 1 86  ? -13.832 -9.020  -17.527 1.00 28.46  ? 86  SER B CB  1 
ATOM   2997 O OG  . SER B 1 86  ? -14.232 -10.316 -17.114 1.00 29.55  ? 86  SER B OG  1 
ATOM   2998 N N   . ALA B 1 87  ? -16.987 -9.242  -18.821 1.00 26.90  ? 87  ALA B N   1 
ATOM   2999 C CA  . ALA B 1 87  ? -17.659 -9.924  -19.933 1.00 25.98  ? 87  ALA B CA  1 
ATOM   3000 C C   . ALA B 1 87  ? -18.366 -8.940  -20.861 1.00 30.04  ? 87  ALA B C   1 
ATOM   3001 O O   . ALA B 1 87  ? -18.926 -7.937  -20.413 1.00 32.00  ? 87  ALA B O   1 
ATOM   3002 C CB  . ALA B 1 87  ? -18.692 -10.931 -19.409 1.00 27.17  ? 87  ALA B CB  1 
ATOM   3003 N N   . PHE B 1 88  ? -18.359 -9.247  -22.156 1.00 29.99  ? 88  PHE B N   1 
ATOM   3004 C CA  . PHE B 1 88  ? -19.214 -8.493  -23.070 1.00 30.63  ? 88  PHE B CA  1 
ATOM   3005 C C   . PHE B 1 88  ? -20.668 -8.619  -22.622 1.00 31.72  ? 88  PHE B C   1 
ATOM   3006 O O   . PHE B 1 88  ? -21.121 -9.724  -22.285 1.00 29.56  ? 88  PHE B O   1 
ATOM   3007 C CB  . PHE B 1 88  ? -19.073 -8.995  -24.501 1.00 30.44  ? 88  PHE B CB  1 
ATOM   3008 C CG  . PHE B 1 88  ? -17.763 -8.653  -25.141 1.00 29.20  ? 88  PHE B CG  1 
ATOM   3009 C CD1 . PHE B 1 88  ? -17.472 -7.342  -25.493 1.00 31.72  ? 88  PHE B CD1 1 
ATOM   3010 C CD2 . PHE B 1 88  ? -16.834 -9.639  -25.412 1.00 30.93  ? 88  PHE B CD2 1 
ATOM   3011 C CE1 . PHE B 1 88  ? -16.277 -7.027  -26.102 1.00 33.86  ? 88  PHE B CE1 1 
ATOM   3012 C CE2 . PHE B 1 88  ? -15.630 -9.329  -26.004 1.00 30.81  ? 88  PHE B CE2 1 
ATOM   3013 C CZ  . PHE B 1 88  ? -15.350 -8.031  -26.352 1.00 36.31  ? 88  PHE B CZ  1 
ATOM   3014 N N   . PRO B 1 89  ? -21.433 -7.527  -22.641 1.00 30.94  ? 89  PRO B N   1 
ATOM   3015 C CA  . PRO B 1 89  ? -22.740 -7.526  -21.957 1.00 30.07  ? 89  PRO B CA  1 
ATOM   3016 C C   . PRO B 1 89  ? -23.742 -8.560  -22.451 1.00 33.32  ? 89  PRO B C   1 
ATOM   3017 O O   . PRO B 1 89  ? -24.497 -9.088  -21.622 1.00 36.88  ? 89  PRO B O   1 
ATOM   3018 C CB  . PRO B 1 89  ? -23.237 -6.093  -22.199 1.00 33.75  ? 89  PRO B CB  1 
ATOM   3019 C CG  . PRO B 1 89  ? -21.976 -5.297  -22.196 1.00 35.67  ? 89  PRO B CG  1 
ATOM   3020 C CD  . PRO B 1 89  ? -20.955 -6.157  -22.912 1.00 32.06  ? 89  PRO B CD  1 
ATOM   3021 N N   . ASP B 1 90  ? -23.808 -8.861  -23.753 1.00 31.85  ? 90  ASP B N   1 
ATOM   3022 C CA  . ASP B 1 90  ? -24.772 -9.873  -24.172 1.00 34.52  ? 90  ASP B CA  1 
ATOM   3023 C C   . ASP B 1 90  ? -24.348 -11.255 -23.691 1.00 35.05  ? 90  ASP B C   1 
ATOM   3024 O O   . ASP B 1 90  ? -25.192 -12.047 -23.251 1.00 35.08  ? 90  ASP B O   1 
ATOM   3025 C CB  . ASP B 1 90  ? -25.002 -9.867  -25.694 1.00 37.31  ? 90  ASP B CB  1 
ATOM   3026 C CG  . ASP B 1 90  ? -23.717 -9.906  -26.515 1.00 39.91  ? 90  ASP B CG  1 
ATOM   3027 O OD1 . ASP B 1 90  ? -22.614 -9.903  -25.955 1.00 38.96  ? 90  ASP B OD1 1 
ATOM   3028 O OD2 . ASP B 1 90  ? -23.823 -9.963  -27.759 1.00 43.76  ? 90  ASP B OD2 1 
ATOM   3029 N N   . ARG B 1 91  ? -23.046 -11.551 -23.735 1.00 32.97  ? 91  ARG B N   1 
ATOM   3030 C CA  . ARG B 1 91  ? -22.559 -12.804 -23.157 1.00 34.05  ? 91  ARG B CA  1 
ATOM   3031 C C   . ARG B 1 91  ? -22.767 -12.828 -21.649 1.00 33.77  ? 91  ARG B C   1 
ATOM   3032 O O   . ARG B 1 91  ? -23.109 -13.873 -21.081 1.00 29.82  ? 91  ARG B O   1 
ATOM   3033 C CB  . ARG B 1 91  ? -21.084 -13.005 -23.491 1.00 33.15  ? 91  ARG B CB  1 
ATOM   3034 C CG  . ARG B 1 91  ? -20.840 -13.260 -24.942 1.00 37.75  ? 91  ARG B CG  1 
ATOM   3035 C CD  . ARG B 1 91  ? -19.488 -13.886 -25.189 1.00 35.99  ? 91  ARG B CD  1 
ATOM   3036 N NE  . ARG B 1 91  ? -19.367 -14.172 -26.610 1.00 39.85  ? 91  ARG B NE  1 
ATOM   3037 C CZ  . ARG B 1 91  ? -18.912 -15.305 -27.124 1.00 36.22  ? 91  ARG B CZ  1 
ATOM   3038 N NH1 . ARG B 1 91  ? -18.424 -16.278 -26.356 1.00 30.39  ? 91  ARG B NH1 1 
ATOM   3039 N NH2 . ARG B 1 91  ? -18.972 -15.478 -28.441 1.00 32.84  ? 91  ARG B NH2 1 
ATOM   3040 N N   . LEU B 1 92  ? -22.580 -11.681 -20.985 1.00 30.28  ? 92  LEU B N   1 
ATOM   3041 C CA  . LEU B 1 92  ? -22.712 -11.637 -19.533 1.00 29.13  ? 92  LEU B CA  1 
ATOM   3042 C C   . LEU B 1 92  ? -24.122 -12.020 -19.097 1.00 29.08  ? 92  LEU B C   1 
ATOM   3043 O O   . LEU B 1 92  ? -24.303 -12.746 -18.121 1.00 28.15  ? 92  LEU B O   1 
ATOM   3044 C CB  . LEU B 1 92  ? -22.346 -10.239 -19.016 1.00 28.75  ? 92  LEU B CB  1 
ATOM   3045 C CG  . LEU B 1 92  ? -22.601 -10.012 -17.529 1.00 30.50  ? 92  LEU B CG  1 
ATOM   3046 C CD1 . LEU B 1 92  ? -21.736 -10.964 -16.718 1.00 28.41  ? 92  LEU B CD1 1 
ATOM   3047 C CD2 . LEU B 1 92  ? -22.259 -8.589  -17.139 1.00 30.35  ? 92  LEU B CD2 1 
ATOM   3048 N N   . ALA B 1 93  ? -25.142 -11.541 -19.809 1.00 29.71  ? 93  ALA B N   1 
ATOM   3049 C CA  . ALA B 1 93  ? -26.513 -11.915 -19.470 1.00 30.55  ? 93  ALA B CA  1 
ATOM   3050 C C   . ALA B 1 93  ? -26.721 -13.422 -19.571 1.00 30.47  ? 93  ALA B C   1 
ATOM   3051 O O   . ALA B 1 93  ? -27.366 -14.032 -18.709 1.00 30.37  ? 93  ALA B O   1 
ATOM   3052 C CB  . ALA B 1 93  ? -27.489 -11.187 -20.398 1.00 29.52  ? 93  ALA B CB  1 
ATOM   3053 N N   . LEU B 1 94  ? -26.173 -14.032 -20.616 1.00 28.19  ? 94  LEU B N   1 
ATOM   3054 C CA  . LEU B 1 94  ? -26.351 -15.460 -20.846 1.00 31.35  ? 94  LEU B CA  1 
ATOM   3055 C C   . LEU B 1 94  ? -25.613 -16.276 -19.792 1.00 32.19  ? 94  LEU B C   1 
ATOM   3056 O O   . LEU B 1 94  ? -26.202 -17.155 -19.148 1.00 29.18  ? 94  LEU B O   1 
ATOM   3057 C CB  . LEU B 1 94  ? -25.845 -15.802 -22.247 1.00 33.13  ? 94  LEU B CB  1 
ATOM   3058 C CG  . LEU B 1 94  ? -26.750 -15.407 -23.426 1.00 34.74  ? 94  LEU B CG  1 
ATOM   3059 C CD1 . LEU B 1 94  ? -26.290 -16.114 -24.661 1.00 33.93  ? 94  LEU B CD1 1 
ATOM   3060 C CD2 . LEU B 1 94  ? -28.207 -15.748 -23.135 1.00 37.60  ? 94  LEU B CD2 1 
ATOM   3061 N N   . LEU B 1 95  ? -24.318 -15.999 -19.596 1.00 30.78  ? 95  LEU B N   1 
ATOM   3062 C CA  . LEU B 1 95  ? -23.563 -16.823 -18.656 1.00 30.57  ? 95  LEU B CA  1 
ATOM   3063 C C   . LEU B 1 95  ? -24.054 -16.628 -17.230 1.00 29.78  ? 95  LEU B C   1 
ATOM   3064 O O   . LEU B 1 95  ? -24.039 -17.578 -16.433 1.00 29.22  ? 95  LEU B O   1 
ATOM   3065 C CB  . LEU B 1 95  ? -22.065 -16.530 -18.738 1.00 31.51  ? 95  LEU B CB  1 
ATOM   3066 C CG  . LEU B 1 95  ? -21.544 -15.144 -18.334 1.00 27.62  ? 95  LEU B CG  1 
ATOM   3067 C CD1 . LEU B 1 95  ? -21.126 -15.162 -16.847 1.00 27.39  ? 95  LEU B CD1 1 
ATOM   3068 C CD2 . LEU B 1 95  ? -20.360 -14.777 -19.195 1.00 28.59  ? 95  LEU B CD2 1 
ATOM   3069 N N   . SER B 1 96  ? -24.500 -15.409 -16.893 1.00 26.83  ? 96  SER B N   1 
ATOM   3070 C CA  . SER B 1 96  ? -24.984 -15.145 -15.545 1.00 27.53  ? 96  SER B CA  1 
ATOM   3071 C C   . SER B 1 96  ? -26.222 -15.966 -15.236 1.00 27.28  ? 96  SER B C   1 
ATOM   3072 O O   . SER B 1 96  ? -26.327 -16.570 -14.168 1.00 30.86  ? 96  SER B O   1 
ATOM   3073 C CB  . SER B 1 96  ? -25.279 -13.652 -15.366 1.00 28.94  ? 96  SER B CB  1 
ATOM   3074 O OG  . SER B 1 96  ? -24.085 -12.880 -15.464 1.00 30.55  ? 96  SER B OG  1 
ATOM   3075 N N   . CYS B 1 97  ? -27.193 -15.982 -16.154 1.00 29.87  ? 97  CYS B N   1 
ATOM   3076 C CA  . CYS B 1 97  ? -28.382 -16.784 -15.902 1.00 27.99  ? 97  CYS B CA  1 
ATOM   3077 C C   . CYS B 1 97  ? -28.102 -18.277 -15.952 1.00 28.29  ? 97  CYS B C   1 
ATOM   3078 O O   . CYS B 1 97  ? -28.741 -19.031 -15.220 1.00 30.87  ? 97  CYS B O   1 
ATOM   3079 C CB  . CYS B 1 97  ? -29.515 -16.436 -16.872 1.00 28.37  ? 97  CYS B CB  1 
ATOM   3080 S SG  . CYS B 1 97  ? -30.078 -14.726 -16.755 1.00 33.45  ? 97  CYS B SG  1 
ATOM   3081 N N   . LEU B 1 98  ? -27.181 -18.726 -16.807 1.00 27.55  ? 98  LEU B N   1 
ATOM   3082 C CA  . LEU B 1 98  ? -26.845 -20.147 -16.823 1.00 27.94  ? 98  LEU B CA  1 
ATOM   3083 C C   . LEU B 1 98  ? -26.223 -20.565 -15.494 1.00 28.97  ? 98  LEU B C   1 
ATOM   3084 O O   . LEU B 1 98  ? -26.668 -21.528 -14.853 1.00 29.36  ? 98  LEU B O   1 
ATOM   3085 C CB  . LEU B 1 98  ? -25.887 -20.462 -17.970 1.00 30.26  ? 98  LEU B CB  1 
ATOM   3086 C CG  . LEU B 1 98  ? -25.758 -21.941 -18.377 1.00 27.97  ? 98  LEU B CG  1 
ATOM   3087 C CD1 . LEU B 1 98  ? -25.315 -22.059 -19.803 1.00 28.98  ? 98  LEU B CD1 1 
ATOM   3088 C CD2 . LEU B 1 98  ? -24.770 -22.678 -17.469 1.00 30.16  ? 98  LEU B CD2 1 
ATOM   3089 N N   . VAL B 1 99  ? -25.183 -19.849 -15.066 1.00 30.11  ? 99  VAL B N   1 
ATOM   3090 C CA  . VAL B 1 99  ? -24.545 -20.167 -13.790 1.00 27.85  ? 99  VAL B CA  1 
ATOM   3091 C C   . VAL B 1 99  ? -25.539 -20.016 -12.648 1.00 29.97  ? 99  VAL B C   1 
ATOM   3092 O O   . VAL B 1 99  ? -25.525 -20.798 -11.689 1.00 29.86  ? 99  VAL B O   1 
ATOM   3093 C CB  . VAL B 1 99  ? -23.288 -19.295 -13.601 1.00 30.07  ? 99  VAL B CB  1 
ATOM   3094 C CG1 . VAL B 1 99  ? -22.640 -19.519 -12.222 1.00 27.46  ? 99  VAL B CG1 1 
ATOM   3095 C CG2 . VAL B 1 99  ? -22.287 -19.637 -14.699 1.00 28.95  ? 99  VAL B CG2 1 
ATOM   3096 N N   . GLU B 1 100 ? -26.445 -19.033 -12.745 1.00 28.48  ? 100 GLU B N   1 
ATOM   3097 C CA  . GLU B 1 100 ? -27.432 -18.871 -11.682 1.00 28.39  ? 100 GLU B CA  1 
ATOM   3098 C C   . GLU B 1 100 ? -28.300 -20.114 -11.525 1.00 31.01  ? 100 GLU B C   1 
ATOM   3099 O O   . GLU B 1 100 ? -28.628 -20.503 -10.399 1.00 32.26  ? 100 GLU B O   1 
ATOM   3100 C CB  . GLU B 1 100 ? -28.303 -17.638 -11.930 1.00 31.77  ? 100 GLU B CB  1 
ATOM   3101 C CG  . GLU B 1 100 ? -29.458 -17.514 -10.930 1.00 32.38  ? 100 GLU B CG  1 
ATOM   3102 C CD  . GLU B 1 100 ? -29.022 -17.091 -9.539  1.00 38.27  ? 100 GLU B CD  1 
ATOM   3103 O OE1 . GLU B 1 100 ? -27.813 -16.868 -9.307  1.00 36.22  ? 100 GLU B OE1 1 
ATOM   3104 O OE2 . GLU B 1 100 ? -29.895 -17.007 -8.647  1.00 39.64  ? 100 GLU B OE2 1 
ATOM   3105 N N   . VAL B 1 101 ? -28.694 -20.747 -12.637 1.00 30.83  ? 101 VAL B N   1 
ATOM   3106 C CA  . VAL B 1 101 ? -29.461 -21.987 -12.521 1.00 29.09  ? 101 VAL B CA  1 
ATOM   3107 C C   . VAL B 1 101 ? -28.630 -23.055 -11.816 1.00 32.60  ? 101 VAL B C   1 
ATOM   3108 O O   . VAL B 1 101 ? -29.135 -23.780 -10.952 1.00 32.89  ? 101 VAL B O   1 
ATOM   3109 C CB  . VAL B 1 101 ? -29.953 -22.458 -13.901 1.00 33.59  ? 101 VAL B CB  1 
ATOM   3110 C CG1 . VAL B 1 101 ? -30.650 -23.811 -13.777 1.00 30.63  ? 101 VAL B CG1 1 
ATOM   3111 C CG2 . VAL B 1 101 ? -30.900 -21.439 -14.503 1.00 33.91  ? 101 VAL B CG2 1 
ATOM   3112 N N   . MET B 1 102 ? -27.336 -23.150 -12.151 1.00 30.52  ? 102 MET B N   1 
ATOM   3113 C CA  . MET B 1 102 ? -26.444 -24.070 -11.429 1.00 32.67  ? 102 MET B CA  1 
ATOM   3114 C C   . MET B 1 102 ? -26.355 -23.711 -9.949  1.00 31.07  ? 102 MET B C   1 
ATOM   3115 O O   . MET B 1 102 ? -26.238 -24.593 -9.087  1.00 32.81  ? 102 MET B O   1 
ATOM   3116 C CB  . MET B 1 102 ? -25.037 -24.044 -12.035 1.00 30.74  ? 102 MET B CB  1 
ATOM   3117 C CG  . MET B 1 102 ? -24.897 -24.393 -13.513 1.00 29.28  ? 102 MET B CG  1 
ATOM   3118 S SD  . MET B 1 102 ? -25.874 -25.799 -14.116 1.00 36.25  ? 102 MET B SD  1 
ATOM   3119 C CE  . MET B 1 102 ? -24.952 -27.082 -13.350 1.00 32.70  ? 102 MET B CE  1 
ATOM   3120 N N   . TRP B 1 103 ? -26.368 -22.414 -9.634  1.00 30.97  ? 103 TRP B N   1 
ATOM   3121 C CA  . TRP B 1 103 ? -26.291 -21.995 -8.240  1.00 31.54  ? 103 TRP B CA  1 
ATOM   3122 C C   . TRP B 1 103 ? -27.546 -22.395 -7.482  1.00 31.62  ? 103 TRP B C   1 
ATOM   3123 O O   . TRP B 1 103 ? -27.469 -22.849 -6.336  1.00 33.49  ? 103 TRP B O   1 
ATOM   3124 C CB  . TRP B 1 103 ? -26.088 -20.484 -8.176  1.00 31.22  ? 103 TRP B CB  1 
ATOM   3125 C CG  . TRP B 1 103 ? -25.313 -19.983 -7.027  1.00 33.52  ? 103 TRP B CG  1 
ATOM   3126 C CD1 . TRP B 1 103 ? -25.269 -20.493 -5.757  1.00 33.19  ? 103 TRP B CD1 1 
ATOM   3127 C CD2 . TRP B 1 103 ? -24.513 -18.798 -7.016  1.00 33.37  ? 103 TRP B CD2 1 
ATOM   3128 N NE1 . TRP B 1 103 ? -24.457 -19.699 -4.959  1.00 32.27  ? 103 TRP B NE1 1 
ATOM   3129 C CE2 . TRP B 1 103 ? -23.973 -18.664 -5.717  1.00 34.83  ? 103 TRP B CE2 1 
ATOM   3130 C CE3 . TRP B 1 103 ? -24.176 -17.851 -7.991  1.00 36.15  ? 103 TRP B CE3 1 
ATOM   3131 C CZ2 . TRP B 1 103 ? -23.129 -17.611 -5.364  1.00 36.73  ? 103 TRP B CZ2 1 
ATOM   3132 C CZ3 . TRP B 1 103 ? -23.333 -16.795 -7.634  1.00 38.59  ? 103 TRP B CZ3 1 
ATOM   3133 C CH2 . TRP B 1 103 ? -22.815 -16.697 -6.330  1.00 39.13  ? 103 TRP B CH2 1 
ATOM   3134 N N   . ILE B 1 104 ? -28.712 -22.224 -8.110  1.00 31.11  ? 104 ILE B N   1 
ATOM   3135 C CA  . ILE B 1 104 ? -29.956 -22.707 -7.519  1.00 32.07  ? 104 ILE B CA  1 
ATOM   3136 C C   . ILE B 1 104 ? -29.879 -24.210 -7.298  1.00 32.19  ? 104 ILE B C   1 
ATOM   3137 O O   . ILE B 1 104 ? -30.311 -24.726 -6.263  1.00 35.76  ? 104 ILE B O   1 
ATOM   3138 C CB  . ILE B 1 104 ? -31.156 -22.336 -8.416  1.00 33.78  ? 104 ILE B CB  1 
ATOM   3139 C CG1 . ILE B 1 104 ? -31.352 -20.820 -8.480  1.00 33.12  ? 104 ILE B CG1 1 
ATOM   3140 C CG2 . ILE B 1 104 ? -32.433 -23.028 -7.930  1.00 34.60  ? 104 ILE B CG2 1 
ATOM   3141 C CD1 . ILE B 1 104 ? -32.271 -20.398 -9.621  1.00 33.69  ? 104 ILE B CD1 1 
ATOM   3142 N N   . HIS B 1 105 ? -29.325 -24.932 -8.275  1.00 31.38  ? 105 HIS B N   1 
ATOM   3143 C CA  . HIS B 1 105 ? -29.190 -26.379 -8.155  1.00 33.06  ? 105 HIS B CA  1 
ATOM   3144 C C   . HIS B 1 105 ? -28.282 -26.753 -6.992  1.00 34.22  ? 105 HIS B C   1 
ATOM   3145 O O   . HIS B 1 105 ? -28.549 -27.718 -6.264  1.00 34.46  ? 105 HIS B O   1 
ATOM   3146 C CB  . HIS B 1 105 ? -28.641 -26.949 -9.456  1.00 32.08  ? 105 HIS B CB  1 
ATOM   3147 C CG  . HIS B 1 105 ? -28.566 -28.440 -9.467  1.00 33.27  ? 105 HIS B CG  1 
ATOM   3148 N ND1 . HIS B 1 105 ? -29.686 -29.239 -9.544  1.00 35.40  ? 105 HIS B ND1 1 
ATOM   3149 C CD2 . HIS B 1 105 ? -27.512 -29.278 -9.329  1.00 35.27  ? 105 HIS B CD2 1 
ATOM   3150 C CE1 . HIS B 1 105 ? -29.319 -30.509 -9.519  1.00 31.88  ? 105 HIS B CE1 1 
ATOM   3151 N NE2 . HIS B 1 105 ? -28.006 -30.561 -9.380  1.00 34.74  ? 105 HIS B NE2 1 
ATOM   3152 N N   . ASP B 1 106 ? -27.197 -26.004 -6.808  1.00 31.17  ? 106 ASP B N   1 
ATOM   3153 C CA  . ASP B 1 106 ? -26.322 -26.230 -5.669  1.00 34.87  ? 106 ASP B CA  1 
ATOM   3154 C C   . ASP B 1 106 ? -27.097 -26.035 -4.369  1.00 36.51  ? 106 ASP B C   1 
ATOM   3155 O O   . ASP B 1 106 ? -27.045 -26.880 -3.467  1.00 36.12  ? 106 ASP B O   1 
ATOM   3156 C CB  . ASP B 1 106 ? -25.110 -25.292 -5.793  1.00 34.69  ? 106 ASP B CB  1 
ATOM   3157 C CG  . ASP B 1 106 ? -24.119 -25.412 -4.645  1.00 40.28  ? 106 ASP B CG  1 
ATOM   3158 O OD1 . ASP B 1 106 ? -24.392 -26.077 -3.625  1.00 44.50  ? 106 ASP B OD1 1 
ATOM   3159 O OD2 . ASP B 1 106 ? -23.004 -24.871 -4.809  1.00 43.91  ? 106 ASP B OD2 1 
ATOM   3160 N N   . ASP B 1 107 ? -27.874 -24.948 -4.279  1.00 35.82  ? 107 ASP B N   1 
ATOM   3161 C CA  . ASP B 1 107 ? -28.648 -24.707 -3.066  1.00 38.60  ? 107 ASP B CA  1 
ATOM   3162 C C   . ASP B 1 107 ? -29.651 -25.827 -2.818  1.00 37.99  ? 107 ASP B C   1 
ATOM   3163 O O   . ASP B 1 107 ? -29.838 -26.262 -1.676  1.00 42.10  ? 107 ASP B O   1 
ATOM   3164 C CB  . ASP B 1 107 ? -29.373 -23.362 -3.150  1.00 34.32  ? 107 ASP B CB  1 
ATOM   3165 C CG  . ASP B 1 107 ? -28.446 -22.191 -2.915  1.00 40.49  ? 107 ASP B CG  1 
ATOM   3166 O OD1 . ASP B 1 107 ? -27.428 -22.370 -2.210  1.00 41.26  ? 107 ASP B OD1 1 
ATOM   3167 O OD2 . ASP B 1 107 ? -28.760 -21.085 -3.391  1.00 39.63  ? 107 ASP B OD2 1 
ATOM   3168 N N   . VAL B 1 108 ? -30.294 -26.314 -3.880  1.00 35.82  ? 108 VAL B N   1 
ATOM   3169 C CA  . VAL B 1 108 ? -31.313 -27.348 -3.734  1.00 37.91  ? 108 VAL B CA  1 
ATOM   3170 C C   . VAL B 1 108 ? -30.690 -28.653 -3.252  1.00 41.77  ? 108 VAL B C   1 
ATOM   3171 O O   . VAL B 1 108 ? -31.232 -29.326 -2.363  1.00 40.63  ? 108 VAL B O   1 
ATOM   3172 C CB  . VAL B 1 108 ? -32.064 -27.524 -5.068  1.00 36.70  ? 108 VAL B CB  1 
ATOM   3173 C CG1 . VAL B 1 108 ? -32.825 -28.852 -5.107  1.00 42.33  ? 108 VAL B CG1 1 
ATOM   3174 C CG2 . VAL B 1 108 ? -32.999 -26.345 -5.301  1.00 40.82  ? 108 VAL B CG2 1 
ATOM   3175 N N   . THR B 1 109 ? -29.538 -29.005 -3.819  1.00 37.74  ? 109 THR B N   1 
ATOM   3176 C CA  . THR B 1 109 ? -28.911 -30.318 -3.533  1.00 40.22  ? 109 THR B CA  1 
ATOM   3177 C C   . THR B 1 109 ? -28.106 -30.303 -2.228  1.00 41.63  ? 109 THR B C   1 
ATOM   3178 O O   . THR B 1 109 ? -27.805 -31.384 -1.718  1.00 38.73  ? 109 THR B O   1 
ATOM   3179 C CB  . THR B 1 109 ? -28.076 -30.745 -4.748  1.00 36.59  ? 109 THR B CB  1 
ATOM   3180 O OG1 . THR B 1 109 ? -27.147 -29.708 -5.064  1.00 35.46  ? 109 THR B OG1 1 
ATOM   3181 C CG2 . THR B 1 109 ? -28.935 -31.053 -5.954  1.00 37.64  ? 109 THR B CG2 1 
ATOM   3182 N N   . GLU B 1 110 ? -27.764 -29.127 -1.722  1.00 40.93  ? 110 GLU B N   1 
ATOM   3183 C CA  . GLU B 1 110 ? -27.023 -29.028 -0.443  1.00 45.30  ? 110 GLU B CA  1 
ATOM   3184 C C   . GLU B 1 110 ? -27.910 -29.534 0.698   1.00 48.64  ? 110 GLU B C   1 
ATOM   3185 O O   . GLU B 1 110 ? -27.361 -30.123 1.632   1.00 53.07  ? 110 GLU B O   1 
ATOM   3186 C CB  . GLU B 1 110 ? -26.594 -27.580 -0.206  1.00 46.21  ? 110 GLU B CB  1 
ATOM   3187 C CG  . GLU B 1 110 ? -25.455 -27.435 0.775   1.00 51.45  ? 110 GLU B CG  1 
ATOM   3188 C CD  . GLU B 1 110 ? -25.312 -26.023 1.309   1.00 58.41  ? 110 GLU B CD  1 
ATOM   3189 O OE1 . GLU B 1 110 ? -26.343 -25.425 1.666   1.00 60.12  ? 110 GLU B OE1 1 
ATOM   3190 O OE2 . GLU B 1 110 ? -24.175 -25.527 1.360   1.00 64.82  ? 110 GLU B OE2 1 
ATOM   3191 N N   . GLU B 1 111 ? -29.226 -29.340 0.597   1.00 53.27  ? 111 GLU B N   1 
ATOM   3192 C CA  . GLU B 1 111 ? -30.125 -29.708 1.720   1.00 54.91  ? 111 GLU B CA  1 
ATOM   3193 C C   . GLU B 1 111 ? -30.509 -31.191 1.660   1.00 55.10  ? 111 GLU B C   1 
ATOM   3194 O O   . GLU B 1 111 ? -31.261 -31.619 2.541   1.00 58.46  ? 111 GLU B O   1 
ATOM   3195 C CB  . GLU B 1 111 ? -31.353 -28.799 1.671   1.00 55.36  ? 111 GLU B CB  1 
ATOM   3196 C CG  . GLU B 1 111 ? -31.238 -27.596 2.589   1.00 62.11  ? 111 GLU B CG  1 
ATOM   3197 C CD  . GLU B 1 111 ? -31.199 -26.251 1.886   1.00 67.41  ? 111 GLU B CD  1 
ATOM   3198 O OE1 . GLU B 1 111 ? -31.660 -26.177 0.731   1.00 65.04  ? 111 GLU B OE1 1 
ATOM   3199 O OE2 . GLU B 1 111 ? -30.715 -25.277 2.499   1.00 68.84  ? 111 GLU B OE2 1 
ATOM   3200 N N   . MET B 1 112 ? -30.025 -31.934 0.667   1.00 51.31  ? 112 MET B N   1 
ATOM   3201 C CA  . MET B 1 112 ? -30.354 -33.343 0.493   1.00 48.63  ? 112 MET B CA  1 
ATOM   3202 C C   . MET B 1 112 ? -29.245 -34.229 1.041   1.00 49.91  ? 112 MET B C   1 
ATOM   3203 O O   . MET B 1 112 ? -28.127 -33.782 1.298   1.00 51.49  ? 112 MET B O   1 
ATOM   3204 C CB  . MET B 1 112 ? -30.593 -33.673 -0.986  1.00 46.18  ? 112 MET B CB  1 
ATOM   3205 C CG  . MET B 1 112 ? -31.690 -32.877 -1.668  1.00 46.03  ? 112 MET B CG  1 
ATOM   3206 S SD  . MET B 1 112 ? -31.820 -33.298 -3.420  1.00 45.95  ? 112 MET B SD  1 
ATOM   3207 C CE  . MET B 1 112 ? -33.208 -32.291 -3.924  1.00 47.85  ? 112 MET B CE  1 
ATOM   3208 N N   . ASP B 1 113 ? -29.571 -35.508 1.223   1.00 47.15  ? 113 ASP B N   1 
ATOM   3209 C CA  . ASP B 1 113 ? -28.523 -36.483 1.465   1.00 46.44  ? 113 ASP B CA  1 
ATOM   3210 C C   . ASP B 1 113 ? -27.697 -36.655 0.194   1.00 46.18  ? 113 ASP B C   1 
ATOM   3211 O O   . ASP B 1 113 ? -28.140 -36.338 -0.914  1.00 45.22  ? 113 ASP B O   1 
ATOM   3212 C CB  . ASP B 1 113 ? -29.107 -37.829 1.901   1.00 49.96  ? 113 ASP B CB  1 
ATOM   3213 C CG  . ASP B 1 113 ? -29.967 -38.462 0.834   1.00 51.85  ? 113 ASP B CG  1 
ATOM   3214 O OD1 . ASP B 1 113 ? -31.181 -38.169 0.793   1.00 55.83  ? 113 ASP B OD1 1 
ATOM   3215 O OD2 . ASP B 1 113 ? -29.431 -39.263 0.037   1.00 52.28  ? 113 ASP B OD2 1 
ATOM   3216 N N   . HIS B 1 114 ? -26.472 -37.142 0.347   1.00 45.27  ? 114 HIS B N   1 
ATOM   3217 C CA  . HIS B 1 114 ? -25.548 -37.207 -0.812  1.00 46.00  ? 114 HIS B CA  1 
ATOM   3218 C C   . HIS B 1 114 ? -26.122 -38.054 -1.946  1.00 47.23  ? 114 HIS B C   1 
ATOM   3219 O O   . HIS B 1 114 ? -26.012 -37.635 -3.097  1.00 42.87  ? 114 HIS B O   1 
ATOM   3220 C CB  . HIS B 1 114 ? -24.186 -37.716 -0.349  1.00 45.43  ? 114 HIS B CB  1 
ATOM   3221 C CG  . HIS B 1 114 ? -23.120 -37.634 -1.384  1.00 47.98  ? 114 HIS B CG  1 
ATOM   3222 N ND1 . HIS B 1 114 ? -22.776 -36.449 -1.992  1.00 48.21  ? 114 HIS B ND1 1 
ATOM   3223 C CD2 . HIS B 1 114 ? -22.320 -38.581 -1.912  1.00 49.81  ? 114 HIS B CD2 1 
ATOM   3224 C CE1 . HIS B 1 114 ? -21.810 -36.671 -2.852  1.00 44.83  ? 114 HIS B CE1 1 
ATOM   3225 N NE2 . HIS B 1 114 ? -21.512 -37.967 -2.825  1.00 51.64  ? 114 HIS B NE2 1 
ATOM   3226 N N   . ILE B 1 115 ? -26.681 -39.214 -1.626  1.00 43.41  ? 115 ILE B N   1 
ATOM   3227 C CA  . ILE B 1 115 ? -27.151 -40.060 -2.719  1.00 43.81  ? 115 ILE B CA  1 
ATOM   3228 C C   . ILE B 1 115 ? -28.285 -39.373 -3.478  1.00 44.02  ? 115 ILE B C   1 
ATOM   3229 O O   . ILE B 1 115 ? -28.359 -39.444 -4.713  1.00 41.67  ? 115 ILE B O   1 
ATOM   3230 C CB  . ILE B 1 115 ? -27.562 -41.448 -2.188  1.00 48.39  ? 115 ILE B CB  1 
ATOM   3231 C CG1 . ILE B 1 115 ? -26.406 -42.443 -2.341  1.00 52.43  ? 115 ILE B CG1 1 
ATOM   3232 C CG2 . ILE B 1 115 ? -28.767 -41.983 -2.931  1.00 48.67  ? 115 ILE B CG2 1 
ATOM   3233 C CD1 . ILE B 1 115 ? -25.060 -41.931 -1.830  1.00 50.89  ? 115 ILE B CD1 1 
ATOM   3234 N N   . SER B 1 116 ? -29.173 -38.681 -2.762  1.00 43.04  ? 116 SER B N   1 
ATOM   3235 C CA  . SER B 1 116 ? -30.250 -37.965 -3.439  1.00 43.09  ? 116 SER B CA  1 
ATOM   3236 C C   . SER B 1 116 ? -29.708 -36.791 -4.242  1.00 41.12  ? 116 SER B C   1 
ATOM   3237 O O   . SER B 1 116 ? -30.196 -36.506 -5.342  1.00 38.23  ? 116 SER B O   1 
ATOM   3238 C CB  . SER B 1 116 ? -31.286 -37.478 -2.429  1.00 46.21  ? 116 SER B CB  1 
ATOM   3239 O OG  . SER B 1 116 ? -31.944 -38.568 -1.813  1.00 46.84  ? 116 SER B OG  1 
ATOM   3240 N N   . ALA B 1 117 ? -28.703 -36.097 -3.707  1.00 39.52  ? 117 ALA B N   1 
ATOM   3241 C CA  . ALA B 1 117 ? -28.119 -34.984 -4.450  1.00 41.48  ? 117 ALA B CA  1 
ATOM   3242 C C   . ALA B 1 117 ? -27.515 -35.475 -5.755  1.00 36.96  ? 117 ALA B C   1 
ATOM   3243 O O   . ALA B 1 117 ? -27.742 -34.884 -6.819  1.00 36.64  ? 117 ALA B O   1 
ATOM   3244 C CB  . ALA B 1 117 ? -27.064 -34.274 -3.599  1.00 37.13  ? 117 ALA B CB  1 
ATOM   3245 N N   . CYS B 1 118 ? -26.781 -36.589 -5.695  1.00 37.26  ? 118 CYS B N   1 
ATOM   3246 C CA  . CYS B 1 118 ? -26.147 -37.128 -6.889  1.00 37.28  ? 118 CYS B CA  1 
ATOM   3247 C C   . CYS B 1 118 ? -27.174 -37.553 -7.924  1.00 37.15  ? 118 CYS B C   1 
ATOM   3248 O O   . CYS B 1 118 ? -26.924 -37.441 -9.126  1.00 37.31  ? 118 CYS B O   1 
ATOM   3249 C CB  . CYS B 1 118 ? -25.259 -38.312 -6.513  1.00 38.92  ? 118 CYS B CB  1 
ATOM   3250 S SG  . CYS B 1 118 ? -23.771 -37.794 -5.635  1.00 47.53  ? 118 CYS B SG  1 
ATOM   3251 N N   . ARG B 1 119 ? -28.331 -38.025 -7.478  1.00 36.99  ? 119 ARG B N   1 
ATOM   3252 C CA  . ARG B 1 119 ? -29.404 -38.379 -8.435  1.00 39.43  ? 119 ARG B CA  1 
ATOM   3253 C C   . ARG B 1 119 ? -29.854 -37.107 -9.155  1.00 37.32  ? 119 ARG B C   1 
ATOM   3254 O O   . ARG B 1 119 ? -30.071 -37.154 -10.362 1.00 36.93  ? 119 ARG B O   1 
ATOM   3255 C CB  . ARG B 1 119 ? -30.569 -39.049 -7.700  1.00 42.86  ? 119 ARG B CB  1 
ATOM   3256 C CG  . ARG B 1 119 ? -31.705 -39.503 -8.602  1.00 49.16  ? 119 ARG B CG  1 
ATOM   3257 C CD  . ARG B 1 119 ? -32.688 -40.351 -7.821  1.00 53.38  ? 119 ARG B CD  1 
ATOM   3258 N NE  . ARG B 1 119 ? -33.134 -39.688 -6.604  1.00 57.58  ? 119 ARG B NE  1 
ATOM   3259 C CZ  . ARG B 1 119 ? -32.950 -40.160 -5.376  1.00 56.27  ? 119 ARG B CZ  1 
ATOM   3260 N NH1 . ARG B 1 119 ? -32.319 -41.306 -5.191  1.00 55.12  ? 119 ARG B NH1 1 
ATOM   3261 N NH2 . ARG B 1 119 ? -33.397 -39.483 -4.335  1.00 54.95  ? 119 ARG B NH2 1 
ATOM   3262 N N   . GLU B 1 120 ? -29.982 -36.019 -8.407  1.00 37.59  ? 120 GLU B N   1 
ATOM   3263 C CA  . GLU B 1 120 ? -30.419 -34.773 -9.028  1.00 35.21  ? 120 GLU B CA  1 
ATOM   3264 C C   . GLU B 1 120 ? -29.361 -34.227 -9.982  1.00 35.42  ? 120 GLU B C   1 
ATOM   3265 O O   . GLU B 1 120 ? -29.701 -33.634 -11.015 1.00 34.91  ? 120 GLU B O   1 
ATOM   3266 C CB  . GLU B 1 120 ? -30.766 -33.739 -7.962  1.00 38.49  ? 120 GLU B CB  1 
ATOM   3267 C CG  . GLU B 1 120 ? -31.914 -34.138 -7.040  1.00 40.49  ? 120 GLU B CG  1 
ATOM   3268 C CD  . GLU B 1 120 ? -33.259 -34.231 -7.754  1.00 47.16  ? 120 GLU B CD  1 
ATOM   3269 O OE1 . GLU B 1 120 ? -33.404 -33.711 -8.885  1.00 45.87  ? 120 GLU B OE1 1 
ATOM   3270 O OE2 . GLU B 1 120 ? -34.190 -34.820 -7.167  1.00 52.78  ? 120 GLU B OE2 1 
ATOM   3271 N N   . HIS B 1 121 ? -28.076 -34.405 -9.654  1.00 33.60  ? 121 HIS B N   1 
ATOM   3272 C CA  . HIS B 1 121 ? -27.019 -34.038 -10.595 1.00 31.59  ? 121 HIS B CA  1 
ATOM   3273 C C   . HIS B 1 121 ? -27.165 -34.811 -11.899 1.00 33.92  ? 121 HIS B C   1 
ATOM   3274 O O   . HIS B 1 121 ? -27.059 -34.238 -12.987 1.00 30.94  ? 121 HIS B O   1 
ATOM   3275 C CB  . HIS B 1 121 ? -25.639 -34.287 -9.983  1.00 32.27  ? 121 HIS B CB  1 
ATOM   3276 C CG  . HIS B 1 121 ? -25.404 -33.572 -8.691  1.00 32.14  ? 121 HIS B CG  1 
ATOM   3277 N ND1 . HIS B 1 121 ? -26.080 -32.424 -8.332  1.00 32.42  ? 121 HIS B ND1 1 
ATOM   3278 C CD2 . HIS B 1 121 ? -24.573 -33.856 -7.660  1.00 31.83  ? 121 HIS B CD2 1 
ATOM   3279 C CE1 . HIS B 1 121 ? -25.674 -32.033 -7.138  1.00 33.89  ? 121 HIS B CE1 1 
ATOM   3280 N NE2 . HIS B 1 121 ? -24.756 -32.881 -6.710  1.00 33.33  ? 121 HIS B NE2 1 
ATOM   3281 N N   . ASP B 1 122 ? -27.418 -36.124 -11.809 1.00 33.73  ? 122 ASP B N   1 
ATOM   3282 C CA  . ASP B 1 122 ? -27.614 -36.924 -13.016 1.00 33.56  ? 122 ASP B CA  1 
ATOM   3283 C C   . ASP B 1 122 ? -28.822 -36.440 -13.809 1.00 33.46  ? 122 ASP B C   1 
ATOM   3284 O O   . ASP B 1 122 ? -28.781 -36.390 -15.041 1.00 32.27  ? 122 ASP B O   1 
ATOM   3285 C CB  . ASP B 1 122 ? -27.774 -38.410 -12.655 1.00 35.63  ? 122 ASP B CB  1 
ATOM   3286 C CG  . ASP B 1 122 ? -26.532 -39.008 -11.993 1.00 42.25  ? 122 ASP B CG  1 
ATOM   3287 O OD1 . ASP B 1 122 ? -25.431 -38.448 -12.145 1.00 37.05  ? 122 ASP B OD1 1 
ATOM   3288 O OD2 . ASP B 1 122 ? -26.656 -40.067 -11.320 1.00 43.01  ? 122 ASP B OD2 1 
ATOM   3289 N N   . GLU B 1 123 ? -29.878 -36.045 -13.117 1.00 34.38  ? 123 GLU B N   1 
ATOM   3290 C CA  . GLU B 1 123 ? -31.102 -35.583 -13.810 1.00 35.36  ? 123 GLU B CA  1 
ATOM   3291 C C   . GLU B 1 123 ? -30.822 -34.253 -14.524 1.00 33.80  ? 123 GLU B C   1 
ATOM   3292 O O   . GLU B 1 123 ? -31.220 -34.102 -15.678 1.00 32.63  ? 123 GLU B O   1 
ATOM   3293 C CB  . GLU B 1 123 ? -32.253 -35.466 -12.816 1.00 34.77  ? 123 GLU B CB  1 
ATOM   3294 C CG  . GLU B 1 123 ? -32.672 -36.791 -12.215 1.00 45.45  ? 123 GLU B CG  1 
ATOM   3295 C CD  . GLU B 1 123 ? -33.203 -37.795 -13.219 1.00 46.23  ? 123 GLU B CD  1 
ATOM   3296 O OE1 . GLU B 1 123 ? -33.913 -37.378 -14.139 1.00 49.39  ? 123 GLU B OE1 1 
ATOM   3297 O OE2 . GLU B 1 123 ? -32.901 -38.990 -13.074 1.00 55.84  ? 123 GLU B OE2 1 
ATOM   3298 N N   . LEU B 1 124 ? -30.155 -33.329 -13.841 1.00 33.21  ? 124 LEU B N   1 
ATOM   3299 C CA  . LEU B 1 124 ? -29.859 -32.054 -14.480 1.00 31.08  ? 124 LEU B CA  1 
ATOM   3300 C C   . LEU B 1 124 ? -28.923 -32.238 -15.665 1.00 32.24  ? 124 LEU B C   1 
ATOM   3301 O O   . LEU B 1 124 ? -29.064 -31.556 -16.689 1.00 30.55  ? 124 LEU B O   1 
ATOM   3302 C CB  . LEU B 1 124 ? -29.265 -31.076 -13.465 1.00 30.57  ? 124 LEU B CB  1 
ATOM   3303 C CG  . LEU B 1 124 ? -29.184 -29.649 -14.010 1.00 30.24  ? 124 LEU B CG  1 
ATOM   3304 C CD1 . LEU B 1 124 ? -30.568 -29.089 -14.389 1.00 32.00  ? 124 LEU B CD1 1 
ATOM   3305 C CD2 . LEU B 1 124 ? -28.484 -28.760 -12.982 1.00 29.20  ? 124 LEU B CD2 1 
ATOM   3306 N N   . ALA B 1 125 ? -27.974 -33.172 -15.558 1.00 30.10  ? 125 ALA B N   1 
ATOM   3307 C CA  . ALA B 1 125 ? -27.030 -33.399 -16.646 1.00 29.50  ? 125 ALA B CA  1 
ATOM   3308 C C   . ALA B 1 125 ? -27.724 -33.833 -17.934 1.00 31.20  ? 125 ALA B C   1 
ATOM   3309 O O   . ALA B 1 125 ? -27.161 -33.646 -19.020 1.00 30.54  ? 125 ALA B O   1 
ATOM   3310 C CB  . ALA B 1 125 ? -25.988 -34.448 -16.232 1.00 33.60  ? 125 ALA B CB  1 
ATOM   3311 N N   . LYS B 1 126 ? -28.933 -34.384 -17.844 1.00 32.47  ? 126 LYS B N   1 
ATOM   3312 C CA  . LYS B 1 126 ? -29.624 -34.794 -19.067 1.00 33.38  ? 126 LYS B CA  1 
ATOM   3313 C C   . LYS B 1 126 ? -29.840 -33.644 -20.040 1.00 35.36  ? 126 LYS B C   1 
ATOM   3314 O O   . LYS B 1 126 ? -29.989 -33.892 -21.246 1.00 36.62  ? 126 LYS B O   1 
ATOM   3315 C CB  . LYS B 1 126 ? -30.953 -35.463 -18.726 1.00 35.95  ? 126 LYS B CB  1 
ATOM   3316 C CG  . LYS B 1 126 ? -30.783 -36.849 -18.111 1.00 37.12  ? 126 LYS B CG  1 
ATOM   3317 C CD  . LYS B 1 126 ? -32.087 -37.380 -17.524 1.00 40.90  ? 126 LYS B CD  1 
ATOM   3318 C CE  . LYS B 1 126 ? -31.825 -38.610 -16.675 1.00 45.90  ? 126 LYS B CE  1 
ATOM   3319 N NZ  . LYS B 1 126 ? -33.052 -39.415 -16.438 1.00 49.36  ? 126 LYS B NZ  1 
ATOM   3320 N N   . VAL B 1 127 ? -29.843 -32.397 -19.551 1.00 33.35  ? 127 VAL B N   1 
ATOM   3321 C CA  . VAL B 1 127 ? -30.047 -31.229 -20.405 1.00 32.54  ? 127 VAL B CA  1 
ATOM   3322 C C   . VAL B 1 127 ? -28.770 -30.806 -21.129 1.00 33.02  ? 127 VAL B C   1 
ATOM   3323 O O   . VAL B 1 127 ? -28.835 -30.108 -22.152 1.00 33.09  ? 127 VAL B O   1 
ATOM   3324 C CB  . VAL B 1 127 ? -30.617 -30.093 -19.532 1.00 38.87  ? 127 VAL B CB  1 
ATOM   3325 C CG1 . VAL B 1 127 ? -30.566 -28.772 -20.237 1.00 42.40  ? 127 VAL B CG1 1 
ATOM   3326 C CG2 . VAL B 1 127 ? -32.044 -30.414 -19.119 1.00 38.33  ? 127 VAL B CG2 1 
ATOM   3327 N N   . LEU B 1 128 ? -27.599 -31.204 -20.624 1.00 30.25  ? 128 LEU B N   1 
ATOM   3328 C CA  . LEU B 1 128 ? -26.318 -30.738 -21.156 1.00 29.17  ? 128 LEU B CA  1 
ATOM   3329 C C   . LEU B 1 128 ? -25.963 -31.523 -22.413 1.00 34.44  ? 128 LEU B C   1 
ATOM   3330 O O   . LEU B 1 128 ? -25.136 -32.441 -22.407 1.00 33.46  ? 128 LEU B O   1 
ATOM   3331 C CB  . LEU B 1 128 ? -25.239 -30.864 -20.087 1.00 26.67  ? 128 LEU B CB  1 
ATOM   3332 C CG  . LEU B 1 128 ? -25.552 -30.064 -18.834 1.00 29.12  ? 128 LEU B CG  1 
ATOM   3333 C CD1 . LEU B 1 128 ? -24.480 -30.317 -17.796 1.00 27.37  ? 128 LEU B CD1 1 
ATOM   3334 C CD2 . LEU B 1 128 ? -25.601 -28.574 -19.172 1.00 28.70  ? 128 LEU B CD2 1 
ATOM   3335 N N   . GLN B 1 129 ? -26.597 -31.133 -23.524 1.00 33.94  ? 129 GLN B N   1 
ATOM   3336 C CA  . GLN B 1 129 ? -26.441 -31.799 -24.810 1.00 37.11  ? 129 GLN B CA  1 
ATOM   3337 C C   . GLN B 1 129 ? -26.283 -30.731 -25.882 1.00 32.47  ? 129 GLN B C   1 
ATOM   3338 O O   . GLN B 1 129 ? -26.982 -29.717 -25.848 1.00 34.76  ? 129 GLN B O   1 
ATOM   3339 C CB  . GLN B 1 129 ? -27.666 -32.680 -25.130 1.00 39.49  ? 129 GLN B CB  1 
ATOM   3340 C CG  . GLN B 1 129 ? -28.175 -33.440 -23.918 1.00 40.50  ? 129 GLN B CG  1 
ATOM   3341 C CD  . GLN B 1 129 ? -27.370 -34.688 -23.628 1.00 44.52  ? 129 GLN B CD  1 
ATOM   3342 O OE1 . GLN B 1 129 ? -26.496 -35.073 -24.408 1.00 46.95  ? 129 GLN B OE1 1 
ATOM   3343 N NE2 . GLN B 1 129 ? -27.595 -35.278 -22.455 1.00 45.70  ? 129 GLN B NE2 1 
ATOM   3344 N N   . LEU B 1 130 ? -25.372 -30.958 -26.832 1.00 31.54  ? 130 LEU B N   1 
ATOM   3345 C CA  . LEU B 1 130 ? -25.161 -29.982 -27.902 1.00 35.45  ? 130 LEU B CA  1 
ATOM   3346 C C   . LEU B 1 130 ? -26.422 -29.760 -28.740 1.00 38.88  ? 130 LEU B C   1 
ATOM   3347 O O   . LEU B 1 130 ? -26.652 -28.655 -29.247 1.00 37.09  ? 130 LEU B O   1 
ATOM   3348 C CB  . LEU B 1 130 ? -24.000 -30.439 -28.788 1.00 34.62  ? 130 LEU B CB  1 
ATOM   3349 C CG  . LEU B 1 130 ? -23.496 -29.491 -29.876 1.00 39.80  ? 130 LEU B CG  1 
ATOM   3350 C CD1 . LEU B 1 130 ? -23.238 -28.100 -29.318 1.00 38.90  ? 130 LEU B CD1 1 
ATOM   3351 C CD2 . LEU B 1 130 ? -22.243 -30.057 -30.515 1.00 43.88  ? 130 LEU B CD2 1 
ATOM   3352 N N   . ASP B 1 131 ? -27.250 -30.791 -28.897 1.00 41.44  ? 131 ASP B N   1 
ATOM   3353 C CA  . ASP B 1 131 ? -28.493 -30.691 -29.650 1.00 40.42  ? 131 ASP B CA  1 
ATOM   3354 C C   . ASP B 1 131 ? -29.718 -30.483 -28.756 1.00 43.53  ? 131 ASP B C   1 
ATOM   3355 O O   . ASP B 1 131 ? -30.838 -30.806 -29.162 1.00 42.83  ? 131 ASP B O   1 
ATOM   3356 C CB  . ASP B 1 131 ? -28.654 -31.925 -30.541 1.00 45.10  ? 131 ASP B CB  1 
ATOM   3357 C CG  . ASP B 1 131 ? -28.943 -33.194 -29.752 1.00 51.20  ? 131 ASP B CG  1 
ATOM   3358 O OD1 . ASP B 1 131 ? -28.929 -33.162 -28.498 1.00 51.95  ? 131 ASP B OD1 1 
ATOM   3359 O OD2 . ASP B 1 131 ? -29.102 -34.259 -30.384 1.00 56.14  ? 131 ASP B OD2 1 
ATOM   3360 N N   . ILE B 1 132 ? -29.525 -29.939 -27.550 1.00 37.05  ? 132 ILE B N   1 
ATOM   3361 C CA  . ILE B 1 132 ? -30.627 -29.739 -26.609 1.00 36.82  ? 132 ILE B CA  1 
ATOM   3362 C C   . ILE B 1 132 ? -31.807 -29.061 -27.296 1.00 38.24  ? 132 ILE B C   1 
ATOM   3363 O O   . ILE B 1 132 ? -31.677 -28.003 -27.923 1.00 41.13  ? 132 ILE B O   1 
ATOM   3364 C CB  . ILE B 1 132 ? -30.142 -28.937 -25.381 1.00 35.03  ? 132 ILE B CB  1 
ATOM   3365 C CG1 . ILE B 1 132 ? -31.273 -28.705 -24.365 1.00 32.55  ? 132 ILE B CG1 1 
ATOM   3366 C CG2 . ILE B 1 132 ? -29.545 -27.602 -25.802 1.00 34.70  ? 132 ILE B CG2 1 
ATOM   3367 C CD1 . ILE B 1 132 ? -31.829 -29.962 -23.745 1.00 35.10  ? 132 ILE B CD1 1 
ATOM   3368 N N   . ASP B 1 133 ? -32.967 -29.695 -27.198 1.00 41.06  ? 133 ASP B N   1 
ATOM   3369 C CA  . ASP B 1 133 ? -34.215 -29.093 -27.636 1.00 40.02  ? 133 ASP B CA  1 
ATOM   3370 C C   . ASP B 1 133 ? -34.991 -28.741 -26.378 1.00 39.19  ? 133 ASP B C   1 
ATOM   3371 O O   . ASP B 1 133 ? -35.482 -29.650 -25.691 1.00 42.82  ? 133 ASP B O   1 
ATOM   3372 C CB  . ASP B 1 133 ? -34.999 -30.066 -28.527 1.00 45.19  ? 133 ASP B CB  1 
ATOM   3373 C CG  . ASP B 1 133 ? -36.448 -29.651 -28.751 1.00 45.45  ? 133 ASP B CG  1 
ATOM   3374 O OD1 . ASP B 1 133 ? -36.823 -28.503 -28.439 1.00 45.87  ? 133 ASP B OD1 1 
ATOM   3375 O OD2 . ASP B 1 133 ? -37.217 -30.488 -29.278 1.00 51.24  ? 133 ASP B OD2 1 
ATOM   3376 N N   . PRO B 1 134 ? -35.088 -27.462 -26.010 1.00 41.26  ? 134 PRO B N   1 
ATOM   3377 C CA  . PRO B 1 134 ? -35.694 -27.116 -24.717 1.00 42.09  ? 134 PRO B CA  1 
ATOM   3378 C C   . PRO B 1 134 ? -37.110 -27.631 -24.530 1.00 45.99  ? 134 PRO B C   1 
ATOM   3379 O O   . PRO B 1 134 ? -37.494 -27.931 -23.392 1.00 44.61  ? 134 PRO B O   1 
ATOM   3380 C CB  . PRO B 1 134 ? -35.654 -25.584 -24.727 1.00 44.41  ? 134 PRO B CB  1 
ATOM   3381 C CG  . PRO B 1 134 ? -34.427 -25.279 -25.501 1.00 43.38  ? 134 PRO B CG  1 
ATOM   3382 C CD  . PRO B 1 134 ? -34.404 -26.305 -26.616 1.00 41.39  ? 134 PRO B CD  1 
ATOM   3383 N N   . SER B 1 135 ? -37.906 -27.731 -25.601 1.00 48.04  ? 135 SER B N   1 
ATOM   3384 C CA  . SER B 1 135 ? -39.278 -28.203 -25.442 1.00 50.54  ? 135 SER B CA  1 
ATOM   3385 C C   . SER B 1 135 ? -39.315 -29.623 -24.900 1.00 50.70  ? 135 SER B C   1 
ATOM   3386 O O   . SER B 1 135 ? -40.252 -29.991 -24.183 1.00 52.89  ? 135 SER B O   1 
ATOM   3387 C CB  . SER B 1 135 ? -40.030 -28.136 -26.773 1.00 48.82  ? 135 SER B CB  1 
ATOM   3388 O OG  . SER B 1 135 ? -39.478 -29.037 -27.718 1.00 48.39  ? 135 SER B OG  1 
ATOM   3389 N N   . LYS B 1 136 ? -38.299 -30.427 -25.219 1.00 45.69  ? 136 LYS B N   1 
ATOM   3390 C CA  . LYS B 1 136 ? -38.262 -31.815 -24.783 1.00 49.05  ? 136 LYS B CA  1 
ATOM   3391 C C   . LYS B 1 136 ? -38.110 -31.946 -23.275 1.00 49.30  ? 136 LYS B C   1 
ATOM   3392 O O   . LYS B 1 136 ? -38.157 -33.068 -22.756 1.00 51.57  ? 136 LYS B O   1 
ATOM   3393 C CB  . LYS B 1 136 ? -37.123 -32.542 -25.502 1.00 47.31  ? 136 LYS B CB  1 
ATOM   3394 C CG  . LYS B 1 136 ? -37.580 -33.354 -26.708 1.00 53.02  ? 136 LYS B CG  1 
ATOM   3395 C CD  . LYS B 1 136 ? -36.399 -33.783 -27.575 1.00 55.43  ? 136 LYS B CD  1 
ATOM   3396 C CE  . LYS B 1 136 ? -36.855 -34.170 -28.984 1.00 56.32  ? 136 LYS B CE  1 
ATOM   3397 N NZ  . LYS B 1 136 ? -36.564 -33.108 -30.004 1.00 57.27  ? 136 LYS B NZ  1 
ATOM   3398 N N   . PHE B 1 137 ? -37.931 -30.833 -22.563 1.00 51.15  ? 137 PHE B N   1 
ATOM   3399 C CA  . PHE B 1 137 ? -37.796 -30.833 -21.113 1.00 48.14  ? 137 PHE B CA  1 
ATOM   3400 C C   . PHE B 1 137 ? -38.888 -29.998 -20.463 1.00 54.91  ? 137 PHE B C   1 
ATOM   3401 O O   . PHE B 1 137 ? -38.731 -29.533 -19.328 1.00 53.76  ? 137 PHE B O   1 
ATOM   3402 C CB  . PHE B 1 137 ? -36.409 -30.331 -20.713 1.00 47.24  ? 137 PHE B CB  1 
ATOM   3403 C CG  . PHE B 1 137 ? -35.370 -31.392 -20.791 1.00 42.64  ? 137 PHE B CG  1 
ATOM   3404 C CD1 . PHE B 1 137 ? -35.164 -32.259 -19.733 1.00 42.84  ? 137 PHE B CD1 1 
ATOM   3405 C CD2 . PHE B 1 137 ? -34.635 -31.562 -21.950 1.00 42.15  ? 137 PHE B CD2 1 
ATOM   3406 C CE1 . PHE B 1 137 ? -34.220 -33.260 -19.817 1.00 42.68  ? 137 PHE B CE1 1 
ATOM   3407 C CE2 . PHE B 1 137 ? -33.687 -32.565 -22.040 1.00 44.37  ? 137 PHE B CE2 1 
ATOM   3408 C CZ  . PHE B 1 137 ? -33.478 -33.412 -20.973 1.00 41.37  ? 137 PHE B CZ  1 
ATOM   3409 N N   . GLU B 1 138 ? -40.006 -29.828 -21.159 1.00 58.19  ? 138 GLU B N   1 
ATOM   3410 C CA  . GLU B 1 138 ? -41.105 -28.988 -20.617 1.00 60.54  ? 138 GLU B CA  1 
ATOM   3411 C C   . GLU B 1 138 ? -41.856 -29.739 -19.510 1.00 58.79  ? 138 GLU B C   1 
ATOM   3412 O O   . GLU B 1 138 ? -42.752 -29.146 -18.924 1.00 67.13  ? 138 GLU B O   1 
ATOM   3413 C CB  . GLU B 1 138 ? -42.039 -28.583 -21.756 1.00 61.12  ? 138 GLU B CB  1 
ATOM   3414 C CG  . GLU B 1 138 ? -41.702 -27.234 -22.359 1.00 61.91  ? 138 GLU B CG  1 
ATOM   3415 C CD  . GLU B 1 138 ? -42.379 -26.954 -23.688 1.00 63.30  ? 138 GLU B CD  1 
ATOM   3416 O OE1 . GLU B 1 138 ? -43.211 -27.779 -24.112 1.00 65.89  ? 138 GLU B OE1 1 
ATOM   3417 O OE2 . GLU B 1 138 ? -42.072 -25.913 -24.296 1.00 64.17  ? 138 GLU B OE2 1 
ATOM   3418 N N   . SER B 1 139 ? -41.535 -31.008 -19.272 1.00 57.55  ? 139 SER B N   1 
ATOM   3419 C CA  . SER B 1 139 ? -42.185 -31.761 -18.208 1.00 56.98  ? 139 SER B CA  1 
ATOM   3420 C C   . SER B 1 139 ? -41.232 -32.099 -17.069 1.00 55.79  ? 139 SER B C   1 
ATOM   3421 O O   . SER B 1 139 ? -41.623 -32.814 -16.140 1.00 56.86  ? 139 SER B O   1 
ATOM   3422 C CB  . SER B 1 139 ? -42.806 -33.043 -18.769 1.00 60.45  ? 139 SER B CB  1 
ATOM   3423 O OG  . SER B 1 139 ? -44.156 -32.822 -19.142 1.00 66.44  ? 139 SER B OG  1 
ATOM   3424 N N   . GLY B 1 140 ? -39.994 -31.609 -17.116 1.00 53.23  ? 140 GLY B N   1 
ATOM   3425 C CA  . GLY B 1 140 ? -39.012 -31.884 -16.088 1.00 48.78  ? 140 GLY B CA  1 
ATOM   3426 C C   . GLY B 1 140 ? -39.111 -30.916 -14.925 1.00 47.58  ? 140 GLY B C   1 
ATOM   3427 O O   . GLY B 1 140 ? -40.079 -30.170 -14.774 1.00 48.38  ? 140 GLY B O   1 
ATOM   3428 N N   . ASN B 1 141 ? -38.051 -30.921 -14.122 1.00 41.88  ? 141 ASN B N   1 
ATOM   3429 C CA  . ASN B 1 141 ? -38.006 -30.005 -12.967 1.00 39.33  ? 141 ASN B CA  1 
ATOM   3430 C C   . ASN B 1 141 ? -37.716 -28.601 -13.486 1.00 39.80  ? 141 ASN B C   1 
ATOM   3431 O O   . ASN B 1 141 ? -37.242 -28.471 -14.609 1.00 38.00  ? 141 ASN B O   1 
ATOM   3432 C CB  . ASN B 1 141 ? -37.030 -30.490 -11.893 1.00 42.68  ? 141 ASN B CB  1 
ATOM   3433 C CG  . ASN B 1 141 ? -35.578 -30.451 -12.314 1.00 42.28  ? 141 ASN B CG  1 
ATOM   3434 O OD1 . ASN B 1 141 ? -35.057 -29.400 -12.670 1.00 38.35  ? 141 ASN B OD1 1 
ATOM   3435 N ND2 . ASN B 1 141 ? -34.914 -31.591 -12.255 1.00 43.18  ? 141 ASN B ND2 1 
ATOM   3436 N N   . VAL B 1 142 ? -37.960 -27.601 -12.650 1.00 41.01  ? 142 VAL B N   1 
ATOM   3437 C CA  . VAL B 1 142 ? -37.829 -26.230 -13.136 1.00 38.63  ? 142 VAL B CA  1 
ATOM   3438 C C   . VAL B 1 142 ? -36.385 -25.867 -13.455 1.00 40.47  ? 142 VAL B C   1 
ATOM   3439 O O   . VAL B 1 142 ? -36.147 -24.967 -14.276 1.00 39.89  ? 142 VAL B O   1 
ATOM   3440 C CB  . VAL B 1 142 ? -38.407 -25.227 -12.124 1.00 43.46  ? 142 VAL B CB  1 
ATOM   3441 C CG1 . VAL B 1 142 ? -39.928 -25.281 -12.131 1.00 43.96  ? 142 VAL B CG1 1 
ATOM   3442 C CG2 . VAL B 1 142 ? -37.837 -25.481 -10.733 1.00 44.13  ? 142 VAL B CG2 1 
ATOM   3443 N N   . ARG B 1 143 ? -35.410 -26.542 -12.831 1.00 37.01  ? 143 ARG B N   1 
ATOM   3444 C CA  . ARG B 1 143 ? -34.015 -26.287 -13.171 1.00 34.05  ? 143 ARG B CA  1 
ATOM   3445 C C   . ARG B 1 143 ? -33.675 -26.867 -14.535 1.00 35.57  ? 143 ARG B C   1 
ATOM   3446 O O   . ARG B 1 143 ? -33.008 -26.218 -15.348 1.00 34.64  ? 143 ARG B O   1 
ATOM   3447 C CB  . ARG B 1 143 ? -33.101 -26.859 -12.082 1.00 36.46  ? 143 ARG B CB  1 
ATOM   3448 C CG  . ARG B 1 143 ? -33.128 -26.018 -10.826 1.00 36.53  ? 143 ARG B CG  1 
ATOM   3449 C CD  . ARG B 1 143 ? -32.326 -26.593 -9.671  1.00 35.40  ? 143 ARG B CD  1 
ATOM   3450 N NE  . ARG B 1 143 ? -32.418 -28.042 -9.551  1.00 41.70  ? 143 ARG B NE  1 
ATOM   3451 C CZ  . ARG B 1 143 ? -33.427 -28.680 -8.976  1.00 43.81  ? 143 ARG B CZ  1 
ATOM   3452 N NH1 . ARG B 1 143 ? -34.478 -28.029 -8.504  1.00 41.79  ? 143 ARG B NH1 1 
ATOM   3453 N NH2 . ARG B 1 143 ? -33.387 -30.006 -8.885  1.00 42.27  ? 143 ARG B NH2 1 
ATOM   3454 N N   . GLN B 1 144 ? -34.128 -28.093 -14.810 1.00 35.24  ? 144 GLN B N   1 
ATOM   3455 C CA  . GLN B 1 144 ? -33.964 -28.652 -16.145 1.00 35.56  ? 144 GLN B CA  1 
ATOM   3456 C C   . GLN B 1 144 ? -34.571 -27.731 -17.193 1.00 35.22  ? 144 GLN B C   1 
ATOM   3457 O O   . GLN B 1 144 ? -33.956 -27.461 -18.232 1.00 34.35  ? 144 GLN B O   1 
ATOM   3458 C CB  . GLN B 1 144 ? -34.628 -30.025 -16.209 1.00 36.80  ? 144 GLN B CB  1 
ATOM   3459 C CG  . GLN B 1 144 ? -33.805 -31.166 -15.672 1.00 38.36  ? 144 GLN B CG  1 
ATOM   3460 C CD  . GLN B 1 144 ? -34.620 -32.443 -15.623 1.00 41.75  ? 144 GLN B CD  1 
ATOM   3461 O OE1 . GLN B 1 144 ? -35.821 -32.404 -15.354 1.00 38.62  ? 144 GLN B OE1 1 
ATOM   3462 N NE2 . GLN B 1 144 ? -33.986 -33.573 -15.926 1.00 37.89  ? 144 GLN B NE2 1 
ATOM   3463 N N   . LYS B 1 145 ? -35.773 -27.251 -16.923 1.00 35.96  ? 145 LYS B N   1 
ATOM   3464 C CA  . LYS B 1 145 ? -36.492 -26.423 -17.919 1.00 40.93  ? 145 LYS B CA  1 
ATOM   3465 C C   . LYS B 1 145 ? -35.726 -25.128 -18.191 1.00 36.36  ? 145 LYS B C   1 
ATOM   3466 O O   . LYS B 1 145 ? -35.560 -24.786 -19.357 1.00 37.16  ? 145 LYS B O   1 
ATOM   3467 C CB  . LYS B 1 145 ? -37.909 -26.152 -17.404 1.00 44.95  ? 145 LYS B CB  1 
ATOM   3468 C CG  . LYS B 1 145 ? -38.696 -27.392 -17.014 1.00 49.18  ? 145 LYS B CG  1 
ATOM   3469 C CD  . LYS B 1 145 ? -40.043 -27.074 -16.417 1.00 53.44  ? 145 LYS B CD  1 
ATOM   3470 C CE  . LYS B 1 145 ? -41.122 -26.926 -17.468 1.00 59.79  ? 145 LYS B CE  1 
ATOM   3471 N NZ  . LYS B 1 145 ? -42.322 -27.726 -17.130 1.00 62.28  ? 145 LYS B NZ  1 
ATOM   3472 N N   . SER B 1 146 ? -35.275 -24.447 -17.141 1.00 38.28  ? 146 SER B N   1 
ATOM   3473 C CA  . SER B 1 146 ? -34.619 -23.160 -17.352 1.00 36.50  ? 146 SER B CA  1 
ATOM   3474 C C   . SER B 1 146 ? -33.208 -23.338 -17.888 1.00 35.87  ? 146 SER B C   1 
ATOM   3475 O O   . SER B 1 146 ? -32.769 -22.570 -18.750 1.00 35.69  ? 146 SER B O   1 
ATOM   3476 C CB  . SER B 1 146 ? -34.612 -22.345 -16.061 1.00 42.70  ? 146 SER B CB  1 
ATOM   3477 O OG  . SER B 1 146 ? -35.897 -22.334 -15.462 1.00 42.57  ? 146 SER B OG  1 
ATOM   3478 N N   . LEU B 1 147 ? -32.474 -24.343 -17.393 1.00 34.92  ? 147 LEU B N   1 
ATOM   3479 C CA  . LEU B 1 147 ? -31.134 -24.558 -17.922 1.00 34.26  ? 147 LEU B CA  1 
ATOM   3480 C C   . LEU B 1 147 ? -31.196 -24.909 -19.403 1.00 33.64  ? 147 LEU B C   1 
ATOM   3481 O O   . LEU B 1 147 ? -30.356 -24.455 -20.187 1.00 32.99  ? 147 LEU B O   1 
ATOM   3482 C CB  . LEU B 1 147 ? -30.402 -25.652 -17.130 1.00 31.13  ? 147 LEU B CB  1 
ATOM   3483 C CG  . LEU B 1 147 ? -28.973 -25.958 -17.590 1.00 31.70  ? 147 LEU B CG  1 
ATOM   3484 C CD1 . LEU B 1 147 ? -28.092 -24.711 -17.395 1.00 33.93  ? 147 LEU B CD1 1 
ATOM   3485 C CD2 . LEU B 1 147 ? -28.376 -27.160 -16.838 1.00 34.20  ? 147 LEU B CD2 1 
ATOM   3486 N N   . ALA B 1 148 ? -32.197 -25.703 -19.812 1.00 34.74  ? 148 ALA B N   1 
ATOM   3487 C CA  . ALA B 1 148 ? -32.338 -26.045 -21.226 1.00 35.99  ? 148 ALA B CA  1 
ATOM   3488 C C   . ALA B 1 148 ? -32.478 -24.798 -22.085 1.00 32.28  ? 148 ALA B C   1 
ATOM   3489 O O   . ALA B 1 148 ? -31.815 -24.669 -23.122 1.00 33.84  ? 148 ALA B O   1 
ATOM   3490 C CB  . ALA B 1 148 ? -33.539 -26.977 -21.438 1.00 35.72  ? 148 ALA B CB  1 
ATOM   3491 N N   . VAL B 1 149 ? -33.323 -23.859 -21.656 1.00 35.58  ? 149 VAL B N   1 
ATOM   3492 C CA  . VAL B 1 149 ? -33.569 -22.650 -22.442 1.00 35.64  ? 149 VAL B CA  1 
ATOM   3493 C C   . VAL B 1 149 ? -32.305 -21.809 -22.541 1.00 37.62  ? 149 VAL B C   1 
ATOM   3494 O O   . VAL B 1 149 ? -31.938 -21.339 -23.626 1.00 35.73  ? 149 VAL B O   1 
ATOM   3495 C CB  . VAL B 1 149 ? -34.730 -21.840 -21.838 1.00 36.92  ? 149 VAL B CB  1 
ATOM   3496 C CG1 . VAL B 1 149 ? -34.882 -20.501 -22.571 1.00 38.56  ? 149 VAL B CG1 1 
ATOM   3497 C CG2 . VAL B 1 149 ? -36.024 -22.651 -21.915 1.00 40.82  ? 149 VAL B CG2 1 
ATOM   3498 N N   . VAL B 1 150 ? -31.626 -21.592 -21.409 1.00 35.51  ? 150 VAL B N   1 
ATOM   3499 C CA  . VAL B 1 150 ? -30.468 -20.705 -21.462 1.00 31.59  ? 150 VAL B CA  1 
ATOM   3500 C C   . VAL B 1 150 ? -29.297 -21.396 -22.141 1.00 31.55  ? 150 VAL B C   1 
ATOM   3501 O O   . VAL B 1 150 ? -28.534 -20.748 -22.867 1.00 32.01  ? 150 VAL B O   1 
ATOM   3502 C CB  . VAL B 1 150 ? -30.104 -20.181 -20.057 1.00 33.46  ? 150 VAL B CB  1 
ATOM   3503 C CG1 . VAL B 1 150 ? -29.472 -21.266 -19.208 1.00 36.55  ? 150 VAL B CG1 1 
ATOM   3504 C CG2 . VAL B 1 150 ? -29.152 -19.003 -20.166 1.00 34.84  ? 150 VAL B CG2 1 
ATOM   3505 N N   . LEU B 1 151 ? -29.154 -22.718 -21.956 1.00 31.48  ? 151 LEU B N   1 
ATOM   3506 C CA  . LEU B 1 151 ? -28.080 -23.443 -22.626 1.00 30.87  ? 151 LEU B CA  1 
ATOM   3507 C C   . LEU B 1 151 ? -28.216 -23.345 -24.133 1.00 30.53  ? 151 LEU B C   1 
ATOM   3508 O O   . LEU B 1 151 ? -27.228 -23.122 -24.842 1.00 30.71  ? 151 LEU B O   1 
ATOM   3509 C CB  . LEU B 1 151 ? -28.076 -24.917 -22.202 1.00 32.81  ? 151 LEU B CB  1 
ATOM   3510 C CG  . LEU B 1 151 ? -26.974 -25.735 -22.873 1.00 30.54  ? 151 LEU B CG  1 
ATOM   3511 C CD1 . LEU B 1 151 ? -25.587 -25.265 -22.408 1.00 32.58  ? 151 LEU B CD1 1 
ATOM   3512 C CD2 . LEU B 1 151 ? -27.147 -27.238 -22.618 1.00 30.17  ? 151 LEU B CD2 1 
ATOM   3513 N N   . ARG B 1 152 ? -29.437 -23.528 -24.641 1.00 31.90  ? 152 ARG B N   1 
ATOM   3514 C CA  . ARG B 1 152 ? -29.660 -23.416 -26.072 1.00 37.27  ? 152 ARG B CA  1 
ATOM   3515 C C   . ARG B 1 152 ? -29.198 -22.053 -26.579 1.00 32.39  ? 152 ARG B C   1 
ATOM   3516 O O   . ARG B 1 152 ? -28.489 -21.967 -27.589 1.00 34.14  ? 152 ARG B O   1 
ATOM   3517 C CB  . ARG B 1 152 ? -31.137 -23.668 -26.355 1.00 34.51  ? 152 ARG B CB  1 
ATOM   3518 C CG  . ARG B 1 152 ? -31.605 -23.390 -27.764 1.00 35.48  ? 152 ARG B CG  1 
ATOM   3519 C CD  . ARG B 1 152 ? -31.366 -24.581 -28.677 1.00 41.83  ? 152 ARG B CD  1 
ATOM   3520 N NE  . ARG B 1 152 ? -30.065 -24.505 -29.327 1.00 38.78  ? 152 ARG B NE  1 
ATOM   3521 C CZ  . ARG B 1 152 ? -29.269 -25.530 -29.587 1.00 33.73  ? 152 ARG B CZ  1 
ATOM   3522 N NH1 . ARG B 1 152 ? -29.591 -26.769 -29.244 1.00 42.03  ? 152 ARG B NH1 1 
ATOM   3523 N NH2 . ARG B 1 152 ? -28.131 -25.311 -30.242 1.00 36.96  ? 152 ARG B NH2 1 
ATOM   3524 N N   . LYS B 1 153 ? -29.524 -20.987 -25.839 1.00 31.60  ? 153 LYS B N   1 
ATOM   3525 C CA  . LYS B 1 153 ? -29.090 -19.644 -26.223 1.00 30.38  ? 153 LYS B CA  1 
ATOM   3526 C C   . LYS B 1 153 ? -27.577 -19.494 -26.132 1.00 34.13  ? 153 LYS B C   1 
ATOM   3527 O O   . LYS B 1 153 ? -26.959 -18.862 -26.998 1.00 34.51  ? 153 LYS B O   1 
ATOM   3528 C CB  . LYS B 1 153 ? -29.776 -18.590 -25.356 1.00 36.31  ? 153 LYS B CB  1 
ATOM   3529 C CG  . LYS B 1 153 ? -31.294 -18.632 -25.385 1.00 37.15  ? 153 LYS B CG  1 
ATOM   3530 C CD  . LYS B 1 153 ? -31.882 -17.607 -24.440 1.00 39.64  ? 153 LYS B CD  1 
ATOM   3531 C CE  . LYS B 1 153 ? -33.391 -17.516 -24.582 1.00 46.87  ? 153 LYS B CE  1 
ATOM   3532 N NZ  . LYS B 1 153 ? -34.008 -16.840 -23.410 1.00 46.27  ? 153 LYS B NZ  1 
ATOM   3533 N N   . ALA B 1 154 ? -26.959 -20.071 -25.092 1.00 31.02  ? 154 ALA B N   1 
ATOM   3534 C CA  . ALA B 1 154 ? -25.512 -19.964 -24.963 1.00 31.35  ? 154 ALA B CA  1 
ATOM   3535 C C   . ALA B 1 154 ? -24.776 -20.788 -26.013 1.00 30.98  ? 154 ALA B C   1 
ATOM   3536 O O   . ALA B 1 154 ? -23.697 -20.382 -26.460 1.00 29.25  ? 154 ALA B O   1 
ATOM   3537 C CB  . ALA B 1 154 ? -25.072 -20.370 -23.552 1.00 28.63  ? 154 ALA B CB  1 
ATOM   3538 N N   . ILE B 1 155 ? -25.328 -21.940 -26.429 1.00 30.72  ? 155 ILE B N   1 
ATOM   3539 C CA  . ILE B 1 155 ? -24.753 -22.661 -27.567 1.00 32.01  ? 155 ILE B CA  1 
ATOM   3540 C C   . ILE B 1 155 ? -24.835 -21.803 -28.827 1.00 32.83  ? 155 ILE B C   1 
ATOM   3541 O O   . ILE B 1 155 ? -23.861 -21.666 -29.580 1.00 30.48  ? 155 ILE B O   1 
ATOM   3542 C CB  . ILE B 1 155 ? -25.474 -24.008 -27.779 1.00 32.16  ? 155 ILE B CB  1 
ATOM   3543 C CG1 . ILE B 1 155 ? -25.219 -24.968 -26.609 1.00 31.27  ? 155 ILE B CG1 1 
ATOM   3544 C CG2 . ILE B 1 155 ? -25.041 -24.654 -29.084 1.00 32.99  ? 155 ILE B CG2 1 
ATOM   3545 C CD1 . ILE B 1 155 ? -26.278 -26.075 -26.556 1.00 32.58  ? 155 ILE B CD1 1 
ATOM   3546 N N   . ASP B 1 156 ? -26.006 -21.219 -29.071 1.00 32.32  ? 156 ASP B N   1 
ATOM   3547 C CA  . ASP B 1 156 ? -26.259 -20.575 -30.360 1.00 36.01  ? 156 ASP B CA  1 
ATOM   3548 C C   . ASP B 1 156 ? -25.465 -19.287 -30.533 1.00 39.69  ? 156 ASP B C   1 
ATOM   3549 O O   . ASP B 1 156 ? -25.138 -18.922 -31.672 1.00 35.53  ? 156 ASP B O   1 
ATOM   3550 C CB  . ASP B 1 156 ? -27.752 -20.319 -30.528 1.00 35.95  ? 156 ASP B CB  1 
ATOM   3551 C CG  . ASP B 1 156 ? -28.546 -21.604 -30.715 1.00 38.38  ? 156 ASP B CG  1 
ATOM   3552 O OD1 . ASP B 1 156 ? -27.955 -22.596 -31.192 1.00 37.29  ? 156 ASP B OD1 1 
ATOM   3553 O OD2 . ASP B 1 156 ? -29.748 -21.620 -30.368 1.00 41.95  ? 156 ASP B OD2 1 
ATOM   3554 N N   . ILE B 1 157 ? -25.127 -18.597 -29.435 1.00 34.71  ? 157 ILE B N   1 
ATOM   3555 C CA  . ILE B 1 157 ? -24.347 -17.367 -29.563 1.00 33.88  ? 157 ILE B CA  1 
ATOM   3556 C C   . ILE B 1 157 ? -22.896 -17.678 -29.902 1.00 34.75  ? 157 ILE B C   1 
ATOM   3557 O O   . ILE B 1 157 ? -22.198 -16.822 -30.456 1.00 35.00  ? 157 ILE B O   1 
ATOM   3558 C CB  . ILE B 1 157 ? -24.440 -16.494 -28.291 1.00 33.65  ? 157 ILE B CB  1 
ATOM   3559 C CG1 . ILE B 1 157 ? -23.932 -15.063 -28.553 1.00 34.40  ? 157 ILE B CG1 1 
ATOM   3560 C CG2 . ILE B 1 157 ? -23.651 -17.100 -27.137 1.00 28.87  ? 157 ILE B CG2 1 
ATOM   3561 C CD1 . ILE B 1 157 ? -24.297 -14.067 -27.455 1.00 33.95  ? 157 ILE B CD1 1 
ATOM   3562 N N   . ASP B 1 158 ? -22.414 -18.884 -29.585 1.00 31.38  ? 158 ASP B N   1 
ATOM   3563 C CA  . ASP B 1 158 ? -21.027 -19.260 -29.862 1.00 34.07  ? 158 ASP B CA  1 
ATOM   3564 C C   . ASP B 1 158 ? -20.947 -20.759 -30.108 1.00 32.38  ? 158 ASP B C   1 
ATOM   3565 O O   . ASP B 1 158 ? -20.537 -21.538 -29.235 1.00 32.28  ? 158 ASP B O   1 
ATOM   3566 C CB  . ASP B 1 158 ? -20.108 -18.845 -28.709 1.00 30.00  ? 158 ASP B CB  1 
ATOM   3567 C CG  . ASP B 1 158 ? -18.639 -18.884 -29.084 1.00 36.93  ? 158 ASP B CG  1 
ATOM   3568 O OD1 . ASP B 1 158 ? -18.283 -19.569 -30.063 1.00 36.06  ? 158 ASP B OD1 1 
ATOM   3569 O OD2 . ASP B 1 158 ? -17.819 -18.241 -28.383 1.00 33.60  ? 158 ASP B OD2 1 
ATOM   3570 N N   . PRO B 1 159 ? -21.329 -21.210 -31.300 1.00 30.37  ? 159 PRO B N   1 
ATOM   3571 C CA  . PRO B 1 159 ? -21.319 -22.659 -31.545 1.00 32.32  ? 159 PRO B CA  1 
ATOM   3572 C C   . PRO B 1 159 ? -19.924 -23.248 -31.548 1.00 35.01  ? 159 PRO B C   1 
ATOM   3573 O O   . PRO B 1 159 ? -19.755 -24.418 -31.180 1.00 34.19  ? 159 PRO B O   1 
ATOM   3574 C CB  . PRO B 1 159 ? -22.013 -22.783 -32.913 1.00 31.99  ? 159 PRO B CB  1 
ATOM   3575 C CG  . PRO B 1 159 ? -21.849 -21.417 -33.540 1.00 35.31  ? 159 PRO B CG  1 
ATOM   3576 C CD  . PRO B 1 159 ? -21.998 -20.469 -32.384 1.00 36.44  ? 159 PRO B CD  1 
ATOM   3577 N N   . LYS B 1 160 ? -18.911 -22.457 -31.912 1.00 33.30  ? 160 LYS B N   1 
ATOM   3578 C CA  . LYS B 1 160 ? -17.544 -22.957 -31.929 1.00 35.69  ? 160 LYS B CA  1 
ATOM   3579 C C   . LYS B 1 160 ? -17.098 -23.370 -30.527 1.00 32.93  ? 160 LYS B C   1 
ATOM   3580 O O   . LYS B 1 160 ? -16.450 -24.412 -30.351 1.00 36.94  ? 160 LYS B O   1 
ATOM   3581 C CB  . LYS B 1 160 ? -16.621 -21.880 -32.505 1.00 38.33  ? 160 LYS B CB  1 
ATOM   3582 C CG  . LYS B 1 160 ? -15.174 -22.300 -32.712 1.00 45.00  ? 160 LYS B CG  1 
ATOM   3583 C CD  . LYS B 1 160 ? -14.324 -21.089 -33.116 1.00 51.84  ? 160 LYS B CD  1 
ATOM   3584 C CE  . LYS B 1 160 ? -12.834 -21.404 -33.104 1.00 53.57  ? 160 LYS B CE  1 
ATOM   3585 N NZ  . LYS B 1 160 ? -12.582 -22.807 -33.540 1.00 54.69  ? 160 LYS B NZ  1 
ATOM   3586 N N   . GLN B 1 161 ? -17.469 -22.585 -29.514 1.00 33.28  ? 161 GLN B N   1 
ATOM   3587 C CA  . GLN B 1 161 ? -17.043 -22.879 -28.151 1.00 33.23  ? 161 GLN B CA  1 
ATOM   3588 C C   . GLN B 1 161 ? -18.020 -23.785 -27.416 1.00 30.93  ? 161 GLN B C   1 
ATOM   3589 O O   . GLN B 1 161 ? -17.719 -24.226 -26.299 1.00 30.70  ? 161 GLN B O   1 
ATOM   3590 C CB  . GLN B 1 161 ? -16.884 -21.584 -27.348 1.00 32.17  ? 161 GLN B CB  1 
ATOM   3591 C CG  . GLN B 1 161 ? -15.612 -20.811 -27.652 1.00 37.20  ? 161 GLN B CG  1 
ATOM   3592 C CD  . GLN B 1 161 ? -15.229 -19.863 -26.523 1.00 39.97  ? 161 GLN B CD  1 
ATOM   3593 O OE1 . GLN B 1 161 ? -15.104 -20.290 -25.372 1.00 38.94  ? 161 GLN B OE1 1 
ATOM   3594 N NE2 . GLN B 1 161 ? -15.073 -18.565 -26.837 1.00 38.50  ? 161 GLN B NE2 1 
ATOM   3595 N N   . ALA B 1 162 ? -19.178 -24.077 -28.012 1.00 32.64  ? 162 ALA B N   1 
ATOM   3596 C CA  . ALA B 1 162 ? -20.218 -24.786 -27.274 1.00 30.99  ? 162 ALA B CA  1 
ATOM   3597 C C   . ALA B 1 162 ? -19.819 -26.200 -26.852 1.00 30.25  ? 162 ALA B C   1 
ATOM   3598 O O   . ALA B 1 162 ? -20.209 -26.603 -25.744 1.00 31.58  ? 162 ALA B O   1 
ATOM   3599 C CB  . ALA B 1 162 ? -21.523 -24.802 -28.087 1.00 33.15  ? 162 ALA B CB  1 
ATOM   3600 N N   . PRO B 1 163 ? -19.104 -27.006 -27.654 1.00 32.04  ? 163 PRO B N   1 
ATOM   3601 C CA  . PRO B 1 163 ? -18.705 -28.328 -27.141 1.00 33.70  ? 163 PRO B CA  1 
ATOM   3602 C C   . PRO B 1 163 ? -17.840 -28.231 -25.903 1.00 33.09  ? 163 PRO B C   1 
ATOM   3603 O O   . PRO B 1 163 ? -18.015 -29.010 -24.960 1.00 31.85  ? 163 PRO B O   1 
ATOM   3604 C CB  . PRO B 1 163 ? -17.953 -28.952 -28.324 1.00 36.64  ? 163 PRO B CB  1 
ATOM   3605 C CG  . PRO B 1 163 ? -18.600 -28.337 -29.509 1.00 33.22  ? 163 PRO B CG  1 
ATOM   3606 C CD  . PRO B 1 163 ? -18.839 -26.898 -29.103 1.00 34.70  ? 163 PRO B CD  1 
ATOM   3607 N N   . ALA B 1 164 ? -16.924 -27.268 -25.878 1.00 28.70  ? 164 ALA B N   1 
ATOM   3608 C CA  . ALA B 1 164 ? -16.089 -27.081 -24.697 1.00 32.26  ? 164 ALA B CA  1 
ATOM   3609 C C   . ALA B 1 164 ? -16.918 -26.640 -23.500 1.00 29.12  ? 164 ALA B C   1 
ATOM   3610 O O   . ALA B 1 164 ? -16.626 -27.042 -22.360 1.00 29.86  ? 164 ALA B O   1 
ATOM   3611 C CB  . ALA B 1 164 ? -14.981 -26.074 -24.991 1.00 34.27  ? 164 ALA B CB  1 
ATOM   3612 N N   . MET B 1 165 ? -17.923 -25.807 -23.726 1.00 28.56  ? 165 MET B N   1 
ATOM   3613 C CA  . MET B 1 165 ? -18.736 -25.285 -22.605 1.00 30.66  ? 165 MET B CA  1 
ATOM   3614 C C   . MET B 1 165 ? -19.548 -26.435 -22.009 1.00 31.76  ? 165 MET B C   1 
ATOM   3615 O O   . MET B 1 165 ? -19.617 -26.557 -20.788 1.00 28.96  ? 165 MET B O   1 
ATOM   3616 C CB  . MET B 1 165 ? -19.679 -24.187 -23.101 1.00 35.21  ? 165 MET B CB  1 
ATOM   3617 C CG  . MET B 1 165 ? -20.666 -23.715 -22.061 1.00 29.77  ? 165 MET B CG  1 
ATOM   3618 S SD  . MET B 1 165 ? -21.823 -22.518 -22.757 1.00 29.14  ? 165 MET B SD  1 
ATOM   3619 C CE  . MET B 1 165 ? -22.514 -23.471 -24.107 1.00 25.13  ? 165 MET B CE  1 
ATOM   3620 N N   . ILE B 1 166 ? -20.147 -27.237 -22.878 1.00 28.84  ? 166 ILE B N   1 
ATOM   3621 C CA  . ILE B 1 166 ? -20.921 -28.380 -22.409 1.00 28.11  ? 166 ILE B CA  1 
ATOM   3622 C C   . ILE B 1 166 ? -20.029 -29.375 -21.683 1.00 29.79  ? 166 ILE B C   1 
ATOM   3623 O O   . ILE B 1 166 ? -20.411 -29.915 -20.642 1.00 29.55  ? 166 ILE B O   1 
ATOM   3624 C CB  . ILE B 1 166 ? -21.664 -29.039 -23.583 1.00 30.17  ? 166 ILE B CB  1 
ATOM   3625 C CG1 . ILE B 1 166 ? -22.724 -28.080 -24.103 1.00 30.74  ? 166 ILE B CG1 1 
ATOM   3626 C CG2 . ILE B 1 166 ? -22.289 -30.357 -23.137 1.00 28.63  ? 166 ILE B CG2 1 
ATOM   3627 C CD1 . ILE B 1 166 ? -23.185 -28.412 -25.478 1.00 34.19  ? 166 ILE B CD1 1 
ATOM   3628 N N   . GLU B 1 167 ? -18.831 -29.633 -22.212 1.00 27.94  ? 167 GLU B N   1 
ATOM   3629 C CA  . GLU B 1 167 ? -17.912 -30.542 -21.539 1.00 28.04  ? 167 GLU B CA  1 
ATOM   3630 C C   . GLU B 1 167 ? -17.568 -30.020 -20.157 1.00 30.56  ? 167 GLU B C   1 
ATOM   3631 O O   . GLU B 1 167 ? -17.517 -30.781 -19.185 1.00 29.68  ? 167 GLU B O   1 
ATOM   3632 C CB  . GLU B 1 167 ? -16.647 -30.708 -22.373 1.00 29.24  ? 167 GLU B CB  1 
ATOM   3633 C CG  . GLU B 1 167 ? -15.559 -31.501 -21.688 1.00 34.57  ? 167 GLU B CG  1 
ATOM   3634 C CD  . GLU B 1 167 ? -14.342 -31.611 -22.561 1.00 40.09  ? 167 GLU B CD  1 
ATOM   3635 O OE1 . GLU B 1 167 ? -14.309 -32.516 -23.417 1.00 41.06  ? 167 GLU B OE1 1 
ATOM   3636 O OE2 . GLU B 1 167 ? -13.440 -30.766 -22.420 1.00 42.09  ? 167 GLU B OE2 1 
ATOM   3637 N N   . MET B 1 168 ? -17.356 -28.709 -20.052 1.00 27.00  ? 168 MET B N   1 
ATOM   3638 C CA  . MET B 1 168 ? -17.114 -28.103 -18.750 1.00 29.71  ? 168 MET B CA  1 
ATOM   3639 C C   . MET B 1 168 ? -18.291 -28.324 -17.807 1.00 28.45  ? 168 MET B C   1 
ATOM   3640 O O   . MET B 1 168 ? -18.099 -28.660 -16.634 1.00 27.78  ? 168 MET B O   1 
ATOM   3641 C CB  . MET B 1 168 ? -16.837 -26.603 -18.901 1.00 30.73  ? 168 MET B CB  1 
ATOM   3642 C CG  . MET B 1 168 ? -16.627 -26.002 -17.522 1.00 28.60  ? 168 MET B CG  1 
ATOM   3643 S SD  . MET B 1 168 ? -18.166 -25.352 -16.819 1.00 27.43  ? 168 MET B SD  1 
ATOM   3644 C CE  . MET B 1 168 ? -18.801 -24.332 -18.166 1.00 29.19  ? 168 MET B CE  1 
ATOM   3645 N N   . LEU B 1 169 ? -19.519 -28.094 -18.289 1.00 26.21  ? 169 LEU B N   1 
ATOM   3646 C CA  . LEU B 1 169 ? -20.674 -28.167 -17.396 1.00 26.19  ? 169 LEU B CA  1 
ATOM   3647 C C   . LEU B 1 169 ? -20.914 -29.601 -16.929 1.00 24.41  ? 169 LEU B C   1 
ATOM   3648 O O   . LEU B 1 169 ? -21.256 -29.828 -15.764 1.00 26.54  ? 169 LEU B O   1 
ATOM   3649 C CB  . LEU B 1 169 ? -21.922 -27.611 -18.075 1.00 25.67  ? 169 LEU B CB  1 
ATOM   3650 C CG  . LEU B 1 169 ? -21.875 -26.094 -18.315 1.00 23.75  ? 169 LEU B CG  1 
ATOM   3651 C CD1 . LEU B 1 169 ? -22.885 -25.697 -19.407 1.00 26.28  ? 169 LEU B CD1 1 
ATOM   3652 C CD2 . LEU B 1 169 ? -22.102 -25.314 -17.025 1.00 26.62  ? 169 LEU B CD2 1 
ATOM   3653 N N   . ARG B 1 170 ? -20.771 -30.573 -17.836 1.00 27.36  ? 170 ARG B N   1 
ATOM   3654 C CA  . ARG B 1 170 ? -20.892 -31.978 -17.447 1.00 26.32  ? 170 ARG B CA  1 
ATOM   3655 C C   . ARG B 1 170 ? -19.811 -32.359 -16.442 1.00 28.51  ? 170 ARG B C   1 
ATOM   3656 O O   . ARG B 1 170 ? -20.074 -33.087 -15.476 1.00 27.69  ? 170 ARG B O   1 
ATOM   3657 C CB  . ARG B 1 170 ? -20.804 -32.863 -18.690 1.00 27.02  ? 170 ARG B CB  1 
ATOM   3658 C CG  . ARG B 1 170 ? -21.932 -32.572 -19.732 1.00 28.46  ? 170 ARG B CG  1 
ATOM   3659 C CD  . ARG B 1 170 ? -22.099 -33.676 -20.784 1.00 31.29  ? 170 ARG B CD  1 
ATOM   3660 N NE  . ARG B 1 170 ? -22.488 -34.942 -20.167 1.00 29.92  ? 170 ARG B NE  1 
ATOM   3661 C CZ  . ARG B 1 170 ? -23.738 -35.279 -19.888 1.00 30.82  ? 170 ARG B CZ  1 
ATOM   3662 N NH1 . ARG B 1 170 ? -24.768 -34.564 -20.339 1.00 30.50  ? 170 ARG B NH1 1 
ATOM   3663 N NH2 . ARG B 1 170 ? -23.964 -36.333 -19.106 1.00 31.99  ? 170 ARG B NH2 1 
ATOM   3664 N N   . HIS B 1 171 ? -18.689 -31.893 -16.594 1.00 26.93  ? 171 HIS B N   1 
ATOM   3665 C CA  . HIS B 1 171 ? -17.564 -32.147 -15.697 1.00 26.91  ? 171 HIS B CA  1 
ATOM   3666 C C   . HIS B 1 171 ? -17.803 -31.541 -14.318 1.00 28.16  ? 171 HIS B C   1 
ATOM   3667 O O   . HIS B 1 171 ? -17.464 -32.151 -13.293 1.00 28.83  ? 171 HIS B O   1 
ATOM   3668 C CB  . HIS B 1 171 ? -16.281 -31.593 -16.317 1.00 30.36  ? 171 HIS B CB  1 
ATOM   3669 C CG  . HIS B 1 171 ? -15.058 -31.847 -15.490 1.00 30.19  ? 171 HIS B CG  1 
ATOM   3670 N ND1 . HIS B 1 171 ? -14.610 -33.118 -15.198 1.00 30.47  ? 171 HIS B ND1 1 
ATOM   3671 C CD2 . HIS B 1 171 ? -14.191 -30.996 -14.889 1.00 34.12  ? 171 HIS B CD2 1 
ATOM   3672 C CE1 . HIS B 1 171 ? -13.518 -33.039 -14.456 1.00 32.26  ? 171 HIS B CE1 1 
ATOM   3673 N NE2 . HIS B 1 171 ? -13.245 -31.763 -14.249 1.00 32.10  ? 171 HIS B NE2 1 
ATOM   3674 N N   . TYR B 1 172 ? -18.305 -30.329 -14.349 1.00 26.55  ? 172 TYR B N   1 
ATOM   3675 C CA  . TYR B 1 172 ? -18.697 -29.723 -13.081 1.00 28.14  ? 172 TYR B CA  1 
ATOM   3676 C C   . TYR B 1 172 ? -19.682 -30.619 -12.329 1.00 27.60  ? 172 TYR B C   1 
ATOM   3677 O O   . TYR B 1 172 ? -19.437 -31.008 -11.184 1.00 29.19  ? 172 TYR B O   1 
ATOM   3678 C CB  . TYR B 1 172 ? -19.277 -28.327 -13.341 1.00 25.76  ? 172 TYR B CB  1 
ATOM   3679 C CG  . TYR B 1 172 ? -20.026 -27.736 -12.173 1.00 26.18  ? 172 TYR B CG  1 
ATOM   3680 C CD1 . TYR B 1 172 ? -19.331 -27.200 -11.075 1.00 26.28  ? 172 TYR B CD1 1 
ATOM   3681 C CD2 . TYR B 1 172 ? -21.411 -27.723 -12.142 1.00 26.72  ? 172 TYR B CD2 1 
ATOM   3682 C CE1 . TYR B 1 172 ? -20.006 -26.654 -10.000 1.00 27.99  ? 172 TYR B CE1 1 
ATOM   3683 C CE2 . TYR B 1 172 ? -22.093 -27.196 -11.058 1.00 29.30  ? 172 TYR B CE2 1 
ATOM   3684 C CZ  . TYR B 1 172 ? -21.378 -26.656 -9.990  1.00 28.84  ? 172 TYR B CZ  1 
ATOM   3685 O OH  . TYR B 1 172 ? -22.040 -26.121 -8.913  1.00 30.03  ? 172 TYR B OH  1 
ATOM   3686 N N   . LEU B 1 173 ? -20.774 -31.020 -12.986 1.00 27.78  ? 173 LEU B N   1 
ATOM   3687 C CA  . LEU B 1 173 ? -21.765 -31.837 -12.289 1.00 26.05  ? 173 LEU B CA  1 
ATOM   3688 C C   . LEU B 1 173 ? -21.190 -33.191 -11.891 1.00 28.47  ? 173 LEU B C   1 
ATOM   3689 O O   . LEU B 1 173 ? -21.662 -33.804 -10.930 1.00 29.82  ? 173 LEU B O   1 
ATOM   3690 C CB  . LEU B 1 173 ? -23.007 -32.022 -13.170 1.00 26.44  ? 173 LEU B CB  1 
ATOM   3691 C CG  . LEU B 1 173 ? -23.961 -30.816 -13.182 1.00 27.08  ? 173 LEU B CG  1 
ATOM   3692 C CD1 . LEU B 1 173 ? -25.213 -31.129 -14.002 1.00 30.61  ? 173 LEU B CD1 1 
ATOM   3693 C CD2 . LEU B 1 173 ? -24.339 -30.385 -11.787 1.00 30.00  ? 173 LEU B CD2 1 
ATOM   3694 N N   . ALA B 1 174 ? -20.182 -33.674 -12.619 1.00 29.56  ? 174 ALA B N   1 
ATOM   3695 C CA  . ALA B 1 174 ? -19.556 -34.955 -12.312 1.00 28.94  ? 174 ALA B CA  1 
ATOM   3696 C C   . ALA B 1 174 ? -18.559 -34.884 -11.160 1.00 30.48  ? 174 ALA B C   1 
ATOM   3697 O O   . ALA B 1 174 ? -18.191 -35.936 -10.621 1.00 30.82  ? 174 ALA B O   1 
ATOM   3698 C CB  . ALA B 1 174 ? -18.828 -35.500 -13.542 1.00 28.97  ? 174 ALA B CB  1 
ATOM   3699 N N   . THR B 1 175 ? -18.095 -33.690 -10.785 1.00 29.73  ? 175 THR B N   1 
ATOM   3700 C CA  . THR B 1 175 ? -16.974 -33.570 -9.854  1.00 29.00  ? 175 THR B CA  1 
ATOM   3701 C C   . THR B 1 175 ? -17.212 -32.667 -8.648  1.00 32.15  ? 175 THR B C   1 
ATOM   3702 O O   . THR B 1 175 ? -16.505 -32.830 -7.641  1.00 30.32  ? 175 THR B O   1 
ATOM   3703 C CB  . THR B 1 175 ? -15.711 -33.049 -10.570 1.00 31.21  ? 175 THR B CB  1 
ATOM   3704 O OG1 . THR B 1 175 ? -15.968 -31.757 -11.146 1.00 30.42  ? 175 THR B OG1 1 
ATOM   3705 C CG2 . THR B 1 175 ? -15.223 -34.014 -11.630 1.00 31.52  ? 175 THR B CG2 1 
ATOM   3706 N N   . PHE B 1 176 ? -18.149 -31.724 -8.702  1.00 29.93  ? 176 PHE B N   1 
ATOM   3707 C CA  . PHE B 1 176 ? -18.170 -30.671 -7.681  1.00 30.29  ? 176 PHE B CA  1 
ATOM   3708 C C   . PHE B 1 176 ? -18.682 -31.149 -6.327  1.00 32.34  ? 176 PHE B C   1 
ATOM   3709 O O   . PHE B 1 176 ? -18.329 -30.548 -5.305  1.00 32.20  ? 176 PHE B O   1 
ATOM   3710 C CB  . PHE B 1 176 ? -18.987 -29.482 -8.202  1.00 29.95  ? 176 PHE B CB  1 
ATOM   3711 C CG  . PHE B 1 176 ? -20.451 -29.481 -7.774  1.00 31.19  ? 176 PHE B CG  1 
ATOM   3712 C CD1 . PHE B 1 176 ? -21.383 -30.242 -8.471  1.00 30.08  ? 176 PHE B CD1 1 
ATOM   3713 C CD2 . PHE B 1 176 ? -20.900 -28.673 -6.739  1.00 33.83  ? 176 PHE B CD2 1 
ATOM   3714 C CE1 . PHE B 1 176 ? -22.728 -30.233 -8.114  1.00 32.05  ? 176 PHE B CE1 1 
ATOM   3715 C CE2 . PHE B 1 176 ? -22.248 -28.653 -6.378  1.00 33.70  ? 176 PHE B CE2 1 
ATOM   3716 C CZ  . PHE B 1 176 ? -23.160 -29.434 -7.065  1.00 32.46  ? 176 PHE B CZ  1 
ATOM   3717 N N   . ASP B 1 177 ? -19.507 -32.190 -6.322  1.00 32.09  ? 177 ASP B N   1 
ATOM   3718 C CA  . ASP B 1 177 ? -20.171 -32.621 -5.069  1.00 30.78  ? 177 ASP B CA  1 
ATOM   3719 C C   . ASP B 1 177 ? -20.109 -34.143 -4.924  1.00 38.15  ? 177 ASP B C   1 
ATOM   3720 O O   . ASP B 1 177 ? -21.156 -34.746 -4.708  1.00 38.10  ? 177 ASP B O   1 
ATOM   3721 C CB  . ASP B 1 177 ? -21.604 -32.096 -5.083  1.00 33.39  ? 177 ASP B CB  1 
ATOM   3722 C CG  . ASP B 1 177 ? -22.421 -32.340 -3.832  1.00 36.46  ? 177 ASP B CG  1 
ATOM   3723 O OD1 . ASP B 1 177 ? -21.849 -32.271 -2.738  1.00 35.36  ? 177 ASP B OD1 1 
ATOM   3724 O OD2 . ASP B 1 177 ? -23.628 -32.576 -3.975  1.00 36.68  ? 177 ASP B OD2 1 
ATOM   3725 N N   . ASN B 1 178 ? -18.919 -34.725 -5.014  1.00 37.78  ? 178 ASN B N   1 
ATOM   3726 C CA  . ASN B 1 178 ? -18.776 -36.202 -4.959  1.00 42.87  ? 178 ASN B CA  1 
ATOM   3727 C C   . ASN B 1 178 ? -18.434 -36.673 -3.541  1.00 43.41  ? 178 ASN B C   1 
ATOM   3728 O O   . ASN B 1 178 ? -18.239 -37.877 -3.364  1.00 49.37  ? 178 ASN B O   1 
ATOM   3729 C CB  . ASN B 1 178 ? -17.699 -36.688 -5.923  1.00 46.15  ? 178 ASN B CB  1 
ATOM   3730 C CG  . ASN B 1 178 ? -18.062 -36.500 -7.375  1.00 45.86  ? 178 ASN B CG  1 
ATOM   3731 O OD1 . ASN B 1 178 ? -19.226 -36.305 -7.706  1.00 50.81  ? 178 ASN B OD1 1 
ATOM   3732 N ND2 . ASN B 1 178 ? -17.066 -36.564 -8.241  1.00 33.78  ? 178 ASN B ND2 1 
ATOM   3733 N N   . ILE B 1 179 ? -18.362 -35.763 -2.577  1.00 40.41  ? 179 ILE B N   1 
ATOM   3734 C CA  . ILE B 1 179 ? -17.930 -36.165 -1.207  1.00 47.21  ? 179 ILE B CA  1 
ATOM   3735 C C   . ILE B 1 179 ? -19.063 -35.946 -0.202  1.00 49.36  ? 179 ILE B C   1 
ATOM   3736 O O   . ILE B 1 179 ? -19.465 -34.797 -0.005  1.00 52.25  ? 179 ILE B O   1 
ATOM   3737 C CB  . ILE B 1 179 ? -16.637 -35.439 -0.790  1.00 45.89  ? 179 ILE B CB  1 
ATOM   3738 C CG1 . ILE B 1 179 ? -15.404 -36.102 -1.405  1.00 45.98  ? 179 ILE B CG1 1 
ATOM   3739 C CG2 . ILE B 1 179 ? -16.529 -35.360 0.723   1.00 50.27  ? 179 ILE B CG2 1 
ATOM   3740 C CD1 . ILE B 1 179 ? -14.601 -35.193 -2.288  1.00 49.52  ? 179 ILE B CD1 1 
ATOM   3741 N N   . GLY B 1 180 ? -19.555 -37.028 0.396   1.00 51.99  ? 180 GLY B N   1 
ATOM   3742 C CA  . GLY B 1 180 ? -20.611 -36.929 1.418   1.00 52.42  ? 180 GLY B CA  1 
ATOM   3743 C C   . GLY B 1 180 ? -20.002 -36.956 2.799   1.00 59.70  ? 180 GLY B C   1 
ATOM   3744 O O   . GLY B 1 180 ? -20.716 -36.651 3.765   1.00 63.18  ? 180 GLY B O   1 
ATOM   3745 N N   . GLY B 1 181 ? -18.714 -37.278 2.876   1.00 59.53  ? 181 GLY B N   1 
ATOM   3746 C CA  . GLY B 1 181 ? -18.033 -37.400 4.173   1.00 59.81  ? 181 GLY B CA  1 
ATOM   3747 C C   . GLY B 1 181 ? -17.427 -36.109 4.678   1.00 61.65  ? 181 GLY B C   1 
ATOM   3748 O O   . GLY B 1 181 ? -17.959 -35.035 4.360   1.00 60.76  ? 181 GLY B O   1 
ATOM   3749 N N   . ASP B 1 182 ? -16.308 -36.213 5.389   1.00 60.57  ? 182 ASP B N   1 
ATOM   3750 C CA  . ASP B 1 182 ? -15.756 -35.036 6.042   1.00 59.34  ? 182 ASP B CA  1 
ATOM   3751 C C   . ASP B 1 182 ? -14.263 -34.956 5.772   1.00 56.27  ? 182 ASP B C   1 
ATOM   3752 O O   . ASP B 1 182 ? -13.602 -35.971 5.540   1.00 54.72  ? 182 ASP B O   1 
ATOM   3753 C CB  . ASP B 1 182 ? -15.999 -35.073 7.556   1.00 62.97  ? 182 ASP B CB  1 
ATOM   3754 C CG  . ASP B 1 182 ? -17.413 -34.676 7.925   1.00 67.09  ? 182 ASP B CG  1 
ATOM   3755 O OD1 . ASP B 1 182 ? -17.825 -33.551 7.567   1.00 67.56  ? 182 ASP B OD1 1 
ATOM   3756 O OD2 . ASP B 1 182 ? -18.113 -35.491 8.566   1.00 68.06  ? 182 ASP B OD2 1 
ATOM   3757 N N   . PHE B 1 183 ? -13.756 -33.722 5.834   1.00 52.23  ? 183 PHE B N   1 
ATOM   3758 C CA  . PHE B 1 183 ? -12.313 -33.499 5.576   1.00 47.79  ? 183 PHE B CA  1 
ATOM   3759 C C   . PHE B 1 183 ? -11.568 -33.220 6.879   1.00 45.28  ? 183 PHE B C   1 
ATOM   3760 O O   . PHE B 1 183 ? -12.080 -32.458 7.692   1.00 48.21  ? 183 PHE B O   1 
ATOM   3761 C CB  . PHE B 1 183 ? -12.130 -32.357 4.579   1.00 42.07  ? 183 PHE B CB  1 
ATOM   3762 C CG  . PHE B 1 183 ? -12.318 -32.737 3.136   1.00 41.36  ? 183 PHE B CG  1 
ATOM   3763 C CD1 . PHE B 1 183 ? -11.284 -33.307 2.415   1.00 40.01  ? 183 PHE B CD1 1 
ATOM   3764 C CD2 . PHE B 1 183 ? -13.527 -32.520 2.499   1.00 42.89  ? 183 PHE B CD2 1 
ATOM   3765 C CE1 . PHE B 1 183 ? -11.457 -33.653 1.086   1.00 40.13  ? 183 PHE B CE1 1 
ATOM   3766 C CE2 . PHE B 1 183 ? -13.699 -32.871 1.171   1.00 39.14  ? 183 PHE B CE2 1 
ATOM   3767 C CZ  . PHE B 1 183 ? -12.663 -33.433 0.468   1.00 39.17  ? 183 PHE B CZ  1 
ATOM   3768 N N   . THR B 1 184 ? -10.391 -33.815 7.035   1.00 43.04  ? 184 THR B N   1 
ATOM   3769 C CA  . THR B 1 184 ? -9.574  -33.642 8.226   1.00 46.30  ? 184 THR B CA  1 
ATOM   3770 C C   . THR B 1 184 ? -8.233  -32.966 7.972   1.00 46.05  ? 184 THR B C   1 
ATOM   3771 O O   . THR B 1 184 ? -7.527  -32.669 8.942   1.00 42.32  ? 184 THR B O   1 
ATOM   3772 C CB  . THR B 1 184 ? -9.319  -34.997 8.913   1.00 48.55  ? 184 THR B CB  1 
ATOM   3773 O OG1 . THR B 1 184 ? -8.488  -35.818 8.075   1.00 51.73  ? 184 THR B OG1 1 
ATOM   3774 C CG2 . THR B 1 184 ? -10.627 -35.715 9.178   1.00 49.46  ? 184 THR B CG2 1 
ATOM   3775 N N   . ARG B 1 185 ? -7.926  -32.709 6.698   1.00 41.10  ? 185 ARG B N   1 
ATOM   3776 C CA  . ARG B 1 185 ? -6.682  -31.998 6.327   1.00 39.74  ? 185 ARG B CA  1 
ATOM   3777 C C   . ARG B 1 185 ? -6.964  -31.029 5.171   1.00 39.69  ? 185 ARG B C   1 
ATOM   3778 O O   . ARG B 1 185 ? -7.747  -31.378 4.294   1.00 37.65  ? 185 ARG B O   1 
ATOM   3779 C CB  . ARG B 1 185 ? -5.586  -32.981 5.919   1.00 47.69  ? 185 ARG B CB  1 
ATOM   3780 C CG  . ARG B 1 185 ? -5.430  -34.181 6.838   1.00 50.45  ? 185 ARG B CG  1 
ATOM   3781 C CD  . ARG B 1 185 ? -3.974  -34.577 6.964   1.00 55.23  ? 185 ARG B CD  1 
ATOM   3782 N NE  . ARG B 1 185 ? -3.180  -34.290 5.778   1.00 55.57  ? 185 ARG B NE  1 
ATOM   3783 C CZ  . ARG B 1 185 ? -3.079  -35.096 4.729   1.00 56.47  ? 185 ARG B CZ  1 
ATOM   3784 N NH1 . ARG B 1 185 ? -3.743  -36.238 4.706   1.00 60.29  ? 185 ARG B NH1 1 
ATOM   3785 N NH2 . ARG B 1 185 ? -2.327  -34.755 3.700   1.00 58.65  ? 185 ARG B NH2 1 
ATOM   3786 N N   . MET B 1 186 ? -6.319  -29.866 5.186   1.00 39.42  ? 186 MET B N   1 
ATOM   3787 C CA  . MET B 1 186 ? -6.525  -28.833 4.145   1.00 36.95  ? 186 MET B CA  1 
ATOM   3788 C C   . MET B 1 186 ? -5.933  -29.328 2.831   1.00 38.89  ? 186 MET B C   1 
ATOM   3789 O O   . MET B 1 186 ? -6.468  -28.973 1.780   1.00 37.89  ? 186 MET B O   1 
ATOM   3790 C CB  . MET B 1 186 ? -5.831  -27.538 4.564   1.00 34.99  ? 186 MET B CB  1 
ATOM   3791 C CG  . MET B 1 186 ? -6.638  -26.722 5.534   1.00 39.59  ? 186 MET B CG  1 
ATOM   3792 S SD  . MET B 1 186 ? -8.126  -26.074 4.760   1.00 35.06  ? 186 MET B SD  1 
ATOM   3793 C CE  . MET B 1 186 ? -7.535  -24.486 4.181   1.00 33.92  ? 186 MET B CE  1 
ATOM   3794 N N   . GLU B 1 187 ? -4.878  -30.133 2.913   1.00 40.16  ? 187 GLU B N   1 
ATOM   3795 C CA  . GLU B 1 187 ? -4.224  -30.691 1.704   1.00 40.30  ? 187 GLU B CA  1 
ATOM   3796 C C   . GLU B 1 187 ? -5.265  -31.413 0.846   1.00 39.18  ? 187 GLU B C   1 
ATOM   3797 O O   . GLU B 1 187 ? -5.163  -31.337 -0.374  1.00 42.62  ? 187 GLU B O   1 
ATOM   3798 C CB  . GLU B 1 187 ? -3.090  -31.627 2.113   1.00 47.58  ? 187 GLU B CB  1 
ATOM   3799 C CG  . GLU B 1 187 ? -2.463  -32.368 0.950   1.00 51.21  ? 187 GLU B CG  1 
ATOM   3800 C CD  . GLU B 1 187 ? -1.049  -32.858 1.210   1.00 61.52  ? 187 GLU B CD  1 
ATOM   3801 O OE1 . GLU B 1 187 ? -0.723  -33.120 2.381   1.00 61.23  ? 187 GLU B OE1 1 
ATOM   3802 O OE2 . GLU B 1 187 ? -0.277  -32.972 0.241   1.00 65.21  ? 187 GLU B OE2 1 
ATOM   3803 N N   . GLU B 1 188 ? -6.222  -32.087 1.470   1.00 35.70  ? 188 GLU B N   1 
ATOM   3804 C CA  . GLU B 1 188 ? -7.294  -32.702 0.693   1.00 40.35  ? 188 GLU B CA  1 
ATOM   3805 C C   . GLU B 1 188 ? -8.507  -31.797 0.508   1.00 36.82  ? 188 GLU B C   1 
ATOM   3806 O O   . GLU B 1 188 ? -9.175  -31.881 -0.531  1.00 37.93  ? 188 GLU B O   1 
ATOM   3807 C CB  . GLU B 1 188 ? -7.752  -34.007 1.345   1.00 42.40  ? 188 GLU B CB  1 
ATOM   3808 C CG  . GLU B 1 188 ? -6.728  -35.111 1.231   1.00 42.71  ? 188 GLU B CG  1 
ATOM   3809 C CD  . GLU B 1 188 ? -6.169  -35.470 2.572   1.00 53.78  ? 188 GLU B CD  1 
ATOM   3810 O OE1 . GLU B 1 188 ? -5.390  -34.660 3.096   1.00 52.20  ? 188 GLU B OE1 1 
ATOM   3811 O OE2 . GLU B 1 188 ? -6.487  -36.561 3.095   1.00 61.55  ? 188 GLU B OE2 1 
ATOM   3812 N N   . TYR B 1 189 ? -8.833  -30.957 1.493   1.00 35.78  ? 189 TYR B N   1 
ATOM   3813 C CA  . TYR B 1 189 ? -10.008 -30.100 1.354   1.00 33.65  ? 189 TYR B CA  1 
ATOM   3814 C C   . TYR B 1 189 ? -9.823  -29.086 0.236   1.00 33.78  ? 189 TYR B C   1 
ATOM   3815 O O   . TYR B 1 189 ? -10.772 -28.777 -0.493  1.00 33.47  ? 189 TYR B O   1 
ATOM   3816 C CB  . TYR B 1 189 ? -10.302 -29.370 2.665   1.00 34.70  ? 189 TYR B CB  1 
ATOM   3817 C CG  . TYR B 1 189 ? -11.445 -28.381 2.567   1.00 31.32  ? 189 TYR B CG  1 
ATOM   3818 C CD1 . TYR B 1 189 ? -12.757 -28.825 2.470   1.00 34.12  ? 189 TYR B CD1 1 
ATOM   3819 C CD2 . TYR B 1 189 ? -11.215 -27.006 2.569   1.00 27.25  ? 189 TYR B CD2 1 
ATOM   3820 C CE1 . TYR B 1 189 ? -13.813 -27.944 2.388   1.00 32.84  ? 189 TYR B CE1 1 
ATOM   3821 C CE2 . TYR B 1 189 ? -12.271 -26.103 2.496   1.00 31.50  ? 189 TYR B CE2 1 
ATOM   3822 C CZ  . TYR B 1 189 ? -13.571 -26.582 2.391   1.00 32.05  ? 189 TYR B CZ  1 
ATOM   3823 O OH  . TYR B 1 189 ? -14.633 -25.717 2.313   1.00 33.39  ? 189 TYR B OH  1 
ATOM   3824 N N   . MET B 1 190 ? -8.614  -28.551 0.088   1.00 32.17  ? 190 MET B N   1 
ATOM   3825 C CA  . MET B 1 190 ? -8.413  -27.444 -0.852  1.00 29.36  ? 190 MET B CA  1 
ATOM   3826 C C   . MET B 1 190 ? -8.679  -27.832 -2.303  1.00 32.75  ? 190 MET B C   1 
ATOM   3827 O O   . MET B 1 190 ? -9.429  -27.104 -2.985  1.00 30.07  ? 190 MET B O   1 
ATOM   3828 C CB  . MET B 1 190 ? -7.009  -26.866 -0.627  1.00 32.61  ? 190 MET B CB  1 
ATOM   3829 C CG  . MET B 1 190 ? -6.952  -26.062 0.651   1.00 35.99  ? 190 MET B CG  1 
ATOM   3830 S SD  . MET B 1 190 ? -5.388  -25.242 1.044   1.00 35.87  ? 190 MET B SD  1 
ATOM   3831 C CE  . MET B 1 190 ? -5.139  -24.133 -0.336  1.00 38.63  ? 190 MET B CE  1 
ATOM   3832 N N   . PRO B 1 191 ? -8.141  -28.935 -2.842  1.00 32.32  ? 191 PRO B N   1 
ATOM   3833 C CA  . PRO B 1 191 ? -8.507  -29.298 -4.225  1.00 34.46  ? 191 PRO B CA  1 
ATOM   3834 C C   . PRO B 1 191 ? -9.992  -29.554 -4.389  1.00 33.02  ? 191 PRO B C   1 
ATOM   3835 O O   . PRO B 1 191 ? -10.586 -29.176 -5.406  1.00 35.11  ? 191 PRO B O   1 
ATOM   3836 C CB  . PRO B 1 191 ? -7.686  -30.571 -4.483  1.00 35.49  ? 191 PRO B CB  1 
ATOM   3837 C CG  . PRO B 1 191 ? -6.555  -30.485 -3.514  1.00 36.48  ? 191 PRO B CG  1 
ATOM   3838 C CD  . PRO B 1 191 ? -7.140  -29.864 -2.285  1.00 35.04  ? 191 PRO B CD  1 
ATOM   3839 N N   . TYR B 1 192 ? -10.613 -30.177 -3.389  1.00 32.71  ? 192 TYR B N   1 
ATOM   3840 C CA  . TYR B 1 192 ? -12.050 -30.394 -3.437  1.00 33.74  ? 192 TYR B CA  1 
ATOM   3841 C C   . TYR B 1 192 ? -12.801 -29.075 -3.471  1.00 30.33  ? 192 TYR B C   1 
ATOM   3842 O O   . TYR B 1 192 ? -13.741 -28.905 -4.254  1.00 30.83  ? 192 TYR B O   1 
ATOM   3843 C CB  . TYR B 1 192 ? -12.489 -31.222 -2.235  1.00 33.43  ? 192 TYR B CB  1 
ATOM   3844 C CG  . TYR B 1 192 ? -13.942 -31.067 -1.858  1.00 32.99  ? 192 TYR B CG  1 
ATOM   3845 C CD1 . TYR B 1 192 ? -14.905 -31.848 -2.463  1.00 33.15  ? 192 TYR B CD1 1 
ATOM   3846 C CD2 . TYR B 1 192 ? -14.350 -30.176 -0.875  1.00 35.22  ? 192 TYR B CD2 1 
ATOM   3847 C CE1 . TYR B 1 192 ? -16.230 -31.740 -2.130  1.00 31.66  ? 192 TYR B CE1 1 
ATOM   3848 C CE2 . TYR B 1 192 ? -15.685 -30.067 -0.530  1.00 33.96  ? 192 TYR B CE2 1 
ATOM   3849 C CZ  . TYR B 1 192 ? -16.619 -30.865 -1.166  1.00 34.44  ? 192 TYR B CZ  1 
ATOM   3850 O OH  . TYR B 1 192 ? -17.949 -30.787 -0.834  1.00 38.95  ? 192 TYR B OH  1 
ATOM   3851 N N   . ARG B 1 193 ? -12.408 -28.133 -2.616  1.00 28.78  ? 193 ARG B N   1 
ATOM   3852 C CA  . ARG B 1 193 ? -13.164 -26.894 -2.509  1.00 28.32  ? 193 ARG B CA  1 
ATOM   3853 C C   . ARG B 1 193 ? -13.089 -26.058 -3.779  1.00 28.54  ? 193 ARG B C   1 
ATOM   3854 O O   . ARG B 1 193 ? -14.046 -25.352 -4.084  1.00 29.11  ? 193 ARG B O   1 
ATOM   3855 C CB  . ARG B 1 193 ? -12.665 -26.067 -1.324  1.00 29.88  ? 193 ARG B CB  1 
ATOM   3856 C CG  . ARG B 1 193 ? -13.548 -24.874 -0.983  1.00 30.91  ? 193 ARG B CG  1 
ATOM   3857 C CD  . ARG B 1 193 ? -15.042 -25.235 -0.880  1.00 31.71  ? 193 ARG B CD  1 
ATOM   3858 N NE  . ARG B 1 193 ? -15.792 -24.084 -0.383  1.00 32.58  ? 193 ARG B NE  1 
ATOM   3859 C CZ  . ARG B 1 193 ? -16.920 -23.593 -0.883  1.00 33.32  ? 193 ARG B CZ  1 
ATOM   3860 N NH1 . ARG B 1 193 ? -17.609 -24.228 -1.827  1.00 31.55  ? 193 ARG B NH1 1 
ATOM   3861 N NH2 . ARG B 1 193 ? -17.383 -22.441 -0.409  1.00 33.61  ? 193 ARG B NH2 1 
ATOM   3862 N N   . ILE B 1 194 ? -11.975 -26.106 -4.522  1.00 29.64  ? 194 ILE B N   1 
ATOM   3863 C CA  . ILE B 1 194 ? -11.924 -25.339 -5.767  1.00 26.19  ? 194 ILE B CA  1 
ATOM   3864 C C   . ILE B 1 194 ? -13.016 -25.809 -6.707  1.00 27.72  ? 194 ILE B C   1 
ATOM   3865 O O   . ILE B 1 194 ? -13.688 -25.003 -7.354  1.00 28.69  ? 194 ILE B O   1 
ATOM   3866 C CB  . ILE B 1 194 ? -10.553 -25.438 -6.463  1.00 29.28  ? 194 ILE B CB  1 
ATOM   3867 C CG1 . ILE B 1 194 ? -9.437  -24.912 -5.582  1.00 29.44  ? 194 ILE B CG1 1 
ATOM   3868 C CG2 . ILE B 1 194 ? -10.547 -24.618 -7.759  1.00 28.00  ? 194 ILE B CG2 1 
ATOM   3869 C CD1 . ILE B 1 194 ? -8.067  -25.122 -6.199  1.00 32.89  ? 194 ILE B CD1 1 
ATOM   3870 N N   . ALA B 1 195 ? -13.196 -27.124 -6.819  1.00 27.16  ? 195 ALA B N   1 
ATOM   3871 C CA  . ALA B 1 195 ? -14.256 -27.608 -7.694  1.00 27.47  ? 195 ALA B CA  1 
ATOM   3872 C C   . ALA B 1 195 ? -15.626 -27.321 -7.095  1.00 28.07  ? 195 ALA B C   1 
ATOM   3873 O O   . ALA B 1 195 ? -16.562 -26.924 -7.811  1.00 28.06  ? 195 ALA B O   1 
ATOM   3874 C CB  . ALA B 1 195 ? -14.071 -29.109 -7.943  1.00 28.09  ? 195 ALA B CB  1 
ATOM   3875 N N   . ASN B 1 196 ? -15.756 -27.525 -5.781  1.00 27.53  ? 196 ASN B N   1 
ATOM   3876 C CA  . ASN B 1 196 ? -17.056 -27.474 -5.122  1.00 26.98  ? 196 ASN B CA  1 
ATOM   3877 C C   . ASN B 1 196 ? -17.620 -26.061 -5.106  1.00 28.64  ? 196 ASN B C   1 
ATOM   3878 O O   . ASN B 1 196 ? -18.838 -25.884 -5.129  1.00 31.78  ? 196 ASN B O   1 
ATOM   3879 C CB  . ASN B 1 196 ? -16.931 -28.028 -3.699  1.00 28.55  ? 196 ASN B CB  1 
ATOM   3880 C CG  . ASN B 1 196 ? -18.213 -27.902 -2.907  1.00 35.08  ? 196 ASN B CG  1 
ATOM   3881 O OD1 . ASN B 1 196 ? -18.366 -27.001 -2.087  1.00 31.08  ? 196 ASN B OD1 1 
ATOM   3882 N ND2 . ASN B 1 196 ? -19.165 -28.799 -3.174  1.00 33.15  ? 196 ASN B ND2 1 
ATOM   3883 N N   . CYS B 1 197 ? -16.760 -25.051 -5.095  1.00 27.86  ? 197 CYS B N   1 
ATOM   3884 C CA  . CYS B 1 197 ? -17.239 -23.676 -5.146  1.00 26.11  ? 197 CYS B CA  1 
ATOM   3885 C C   . CYS B 1 197 ? -17.585 -23.210 -6.551  1.00 27.30  ? 197 CYS B C   1 
ATOM   3886 O O   . CYS B 1 197 ? -18.061 -22.082 -6.701  1.00 32.06  ? 197 CYS B O   1 
ATOM   3887 C CB  . CYS B 1 197 ? -16.201 -22.750 -4.500  1.00 26.82  ? 197 CYS B CB  1 
ATOM   3888 S SG  . CYS B 1 197 ? -14.821 -22.316 -5.542  1.00 29.99  ? 197 CYS B SG  1 
ATOM   3889 N N   . GLY B 1 198 ? -17.348 -24.037 -7.567  1.00 25.72  ? 198 GLY B N   1 
ATOM   3890 C CA  . GLY B 1 198 ? -17.708 -23.683 -8.921  1.00 28.14  ? 198 GLY B CA  1 
ATOM   3891 C C   . GLY B 1 198 ? -16.624 -22.958 -9.676  1.00 28.94  ? 198 GLY B C   1 
ATOM   3892 O O   . GLY B 1 198 ? -16.891 -22.471 -10.776 1.00 26.40  ? 198 GLY B O   1 
ATOM   3893 N N   . TYR B 1 199 ? -15.408 -22.864 -9.123  1.00 25.98  ? 199 TYR B N   1 
ATOM   3894 C CA  . TYR B 1 199 ? -14.384 -22.026 -9.748  1.00 27.69  ? 199 TYR B CA  1 
ATOM   3895 C C   . TYR B 1 199 ? -14.076 -22.480 -11.170 1.00 27.04  ? 199 TYR B C   1 
ATOM   3896 O O   . TYR B 1 199 ? -13.826 -21.649 -12.054 1.00 27.17  ? 199 TYR B O   1 
ATOM   3897 C CB  . TYR B 1 199 ? -13.096 -22.012 -8.901  1.00 25.89  ? 199 TYR B CB  1 
ATOM   3898 C CG  . TYR B 1 199 ? -11.974 -21.201 -9.522  1.00 23.85  ? 199 TYR B CG  1 
ATOM   3899 C CD1 . TYR B 1 199 ? -11.947 -19.818 -9.394  1.00 24.04  ? 199 TYR B CD1 1 
ATOM   3900 C CD2 . TYR B 1 199 ? -10.975 -21.814 -10.292 1.00 24.76  ? 199 TYR B CD2 1 
ATOM   3901 C CE1 . TYR B 1 199 ? -10.930 -19.065 -9.959  1.00 23.68  ? 199 TYR B CE1 1 
ATOM   3902 C CE2 . TYR B 1 199 ? -9.959  -21.070 -10.865 1.00 23.90  ? 199 TYR B CE2 1 
ATOM   3903 C CZ  . TYR B 1 199 ? -9.966  -19.677 -10.710 1.00 23.46  ? 199 TYR B CZ  1 
ATOM   3904 O OH  . TYR B 1 199 ? -8.977  -18.910 -11.268 1.00 25.63  ? 199 TYR B OH  1 
ATOM   3905 N N   . TRP B 1 200 ? -14.063 -23.790 -11.424 1.00 27.12  ? 200 TRP B N   1 
ATOM   3906 C CA  . TRP B 1 200 ? -13.724 -24.199 -12.782 1.00 28.13  ? 200 TRP B CA  1 
ATOM   3907 C C   . TRP B 1 200 ? -14.808 -23.794 -13.769 1.00 26.87  ? 200 TRP B C   1 
ATOM   3908 O O   . TRP B 1 200 ? -14.501 -23.492 -14.921 1.00 27.07  ? 200 TRP B O   1 
ATOM   3909 C CB  . TRP B 1 200 ? -13.479 -25.706 -12.860 1.00 26.68  ? 200 TRP B CB  1 
ATOM   3910 C CG  . TRP B 1 200 ? -12.373 -26.142 -11.937 1.00 26.95  ? 200 TRP B CG  1 
ATOM   3911 C CD1 . TRP B 1 200 ? -12.454 -27.095 -10.960 1.00 32.53  ? 200 TRP B CD1 1 
ATOM   3912 C CD2 . TRP B 1 200 ? -11.024 -25.649 -11.904 1.00 29.06  ? 200 TRP B CD2 1 
ATOM   3913 N NE1 . TRP B 1 200 ? -11.243 -27.219 -10.317 1.00 30.56  ? 200 TRP B NE1 1 
ATOM   3914 C CE2 . TRP B 1 200 ? -10.351 -26.342 -10.877 1.00 30.23  ? 200 TRP B CE2 1 
ATOM   3915 C CE3 . TRP B 1 200 ? -10.324 -24.680 -12.632 1.00 29.37  ? 200 TRP B CE3 1 
ATOM   3916 C CZ2 . TRP B 1 200 ? -9.008  -26.104 -10.569 1.00 32.33  ? 200 TRP B CZ2 1 
ATOM   3917 C CZ3 . TRP B 1 200 ? -9.001  -24.441 -12.323 1.00 28.95  ? 200 TRP B CZ3 1 
ATOM   3918 C CH2 . TRP B 1 200 ? -8.352  -25.154 -11.299 1.00 29.17  ? 200 TRP B CH2 1 
ATOM   3919 N N   . MET B 1 201 ? -16.070 -23.820 -13.342 1.00 24.33  ? 201 MET B N   1 
ATOM   3920 C CA  . MET B 1 201 ? -17.167 -23.266 -14.140 1.00 24.38  ? 201 MET B CA  1 
ATOM   3921 C C   . MET B 1 201 ? -17.052 -21.755 -14.295 1.00 26.10  ? 201 MET B C   1 
ATOM   3922 O O   . MET B 1 201 ? -17.152 -21.224 -15.404 1.00 26.01  ? 201 MET B O   1 
ATOM   3923 C CB  . MET B 1 201 ? -18.500 -23.582 -13.482 1.00 25.73  ? 201 MET B CB  1 
ATOM   3924 C CG  . MET B 1 201 ? -19.700 -23.045 -14.289 1.00 27.04  ? 201 MET B CG  1 
ATOM   3925 S SD  . MET B 1 201 ? -21.235 -23.766 -13.713 1.00 29.51  ? 201 MET B SD  1 
ATOM   3926 C CE  . MET B 1 201 ? -21.220 -23.336 -11.982 1.00 31.58  ? 201 MET B CE  1 
ATOM   3927 N N   . SER B 1 202 ? -16.907 -21.042 -13.179 1.00 25.41  ? 202 SER B N   1 
ATOM   3928 C CA  . SER B 1 202 ? -16.891 -19.581 -13.248 1.00 25.99  ? 202 SER B CA  1 
ATOM   3929 C C   . SER B 1 202 ? -15.721 -19.074 -14.079 1.00 26.94  ? 202 SER B C   1 
ATOM   3930 O O   . SER B 1 202 ? -15.870 -18.119 -14.865 1.00 25.91  ? 202 SER B O   1 
ATOM   3931 C CB  . SER B 1 202 ? -16.835 -18.999 -11.836 1.00 26.69  ? 202 SER B CB  1 
ATOM   3932 O OG  . SER B 1 202 ? -18.017 -19.306 -11.110 1.00 27.40  ? 202 SER B OG  1 
ATOM   3933 N N   . SER B 1 203 ? -14.541 -19.676 -13.895 1.00 25.86  ? 203 SER B N   1 
ATOM   3934 C CA  . SER B 1 203 ? -13.356 -19.212 -14.606 1.00 26.34  ? 203 SER B CA  1 
ATOM   3935 C C   . SER B 1 203 ? -13.434 -19.554 -16.086 1.00 28.87  ? 203 SER B C   1 
ATOM   3936 O O   . SER B 1 203 ? -12.928 -18.789 -16.913 1.00 27.80  ? 203 SER B O   1 
ATOM   3937 C CB  . SER B 1 203 ? -12.078 -19.788 -13.991 1.00 24.96  ? 203 SER B CB  1 
ATOM   3938 O OG  . SER B 1 203 ? -12.089 -21.219 -13.952 1.00 27.46  ? 203 SER B OG  1 
ATOM   3939 N N   . TYR B 1 204 ? -14.035 -20.700 -16.437 1.00 26.07  ? 204 TYR B N   1 
ATOM   3940 C CA  . TYR B 1 204 ? -14.346 -20.958 -17.838 1.00 25.21  ? 204 TYR B CA  1 
ATOM   3941 C C   . TYR B 1 204 ? -15.176 -19.815 -18.401 1.00 27.54  ? 204 TYR B C   1 
ATOM   3942 O O   . TYR B 1 204 ? -14.860 -19.269 -19.463 1.00 26.86  ? 204 TYR B O   1 
ATOM   3943 C CB  . TYR B 1 204 ? -15.088 -22.289 -18.013 1.00 26.82  ? 204 TYR B CB  1 
ATOM   3944 C CG  . TYR B 1 204 ? -15.523 -22.477 -19.457 1.00 27.29  ? 204 TYR B CG  1 
ATOM   3945 C CD1 . TYR B 1 204 ? -14.683 -23.098 -20.374 1.00 29.30  ? 204 TYR B CD1 1 
ATOM   3946 C CD2 . TYR B 1 204 ? -16.723 -21.946 -19.918 1.00 28.00  ? 204 TYR B CD2 1 
ATOM   3947 C CE1 . TYR B 1 204 ? -15.058 -23.230 -21.713 1.00 29.38  ? 204 TYR B CE1 1 
ATOM   3948 C CE2 . TYR B 1 204 ? -17.093 -22.056 -21.243 1.00 27.83  ? 204 TYR B CE2 1 
ATOM   3949 C CZ  . TYR B 1 204 ? -16.248 -22.705 -22.131 1.00 30.03  ? 204 TYR B CZ  1 
ATOM   3950 O OH  . TYR B 1 204 ? -16.604 -22.824 -23.455 1.00 29.20  ? 204 TYR B OH  1 
ATOM   3951 N N   . PHE B 1 205 ? -16.220 -19.403 -17.676 1.00 24.00  ? 205 PHE B N   1 
ATOM   3952 C CA  . PHE B 1 205 ? -17.081 -18.363 -18.243 1.00 25.63  ? 205 PHE B CA  1 
ATOM   3953 C C   . PHE B 1 205 ? -16.419 -16.991 -18.225 1.00 28.77  ? 205 PHE B C   1 
ATOM   3954 O O   . PHE B 1 205 ? -16.867 -16.092 -18.944 1.00 25.63  ? 205 PHE B O   1 
ATOM   3955 C CB  . PHE B 1 205 ? -18.417 -18.339 -17.504 1.00 23.77  ? 205 PHE B CB  1 
ATOM   3956 C CG  . PHE B 1 205 ? -19.413 -19.337 -18.046 1.00 27.38  ? 205 PHE B CG  1 
ATOM   3957 C CD1 . PHE B 1 205 ? -19.788 -19.312 -19.383 1.00 27.55  ? 205 PHE B CD1 1 
ATOM   3958 C CD2 . PHE B 1 205 ? -19.935 -20.328 -17.226 1.00 27.40  ? 205 PHE B CD2 1 
ATOM   3959 C CE1 . PHE B 1 205 ? -20.703 -20.242 -19.896 1.00 28.28  ? 205 PHE B CE1 1 
ATOM   3960 C CE2 . PHE B 1 205 ? -20.834 -21.271 -17.727 1.00 26.88  ? 205 PHE B CE2 1 
ATOM   3961 C CZ  . PHE B 1 205 ? -21.230 -21.213 -19.064 1.00 27.02  ? 205 PHE B CZ  1 
ATOM   3962 N N   . ILE B 1 206 ? -15.363 -16.803 -17.431 1.00 26.96  ? 206 ILE B N   1 
ATOM   3963 C CA  . ILE B 1 206 ? -14.595 -15.563 -17.523 1.00 25.76  ? 206 ILE B CA  1 
ATOM   3964 C C   . ILE B 1 206 ? -13.938 -15.459 -18.895 1.00 27.94  ? 206 ILE B C   1 
ATOM   3965 O O   . ILE B 1 206 ? -13.921 -14.387 -19.514 1.00 27.72  ? 206 ILE B O   1 
ATOM   3966 C CB  . ILE B 1 206 ? -13.567 -15.481 -16.365 1.00 25.18  ? 206 ILE B CB  1 
ATOM   3967 C CG1 . ILE B 1 206 ? -14.311 -15.108 -15.085 1.00 27.63  ? 206 ILE B CG1 1 
ATOM   3968 C CG2 . ILE B 1 206 ? -12.419 -14.534 -16.691 1.00 27.70  ? 206 ILE B CG2 1 
ATOM   3969 C CD1 . ILE B 1 206 ? -14.565 -13.620 -14.934 1.00 24.57  ? 206 ILE B CD1 1 
ATOM   3970 N N   . ARG B 1 207 ? -13.429 -16.577 -19.418 1.00 27.60  ? 207 ARG B N   1 
ATOM   3971 C CA  . ARG B 1 207 ? -12.892 -16.568 -20.779 1.00 27.19  ? 207 ARG B CA  1 
ATOM   3972 C C   . ARG B 1 207 ? -14.005 -16.510 -21.819 1.00 28.37  ? 207 ARG B C   1 
ATOM   3973 O O   . ARG B 1 207 ? -13.960 -15.693 -22.745 1.00 28.49  ? 207 ARG B O   1 
ATOM   3974 C CB  . ARG B 1 207 ? -12.018 -17.798 -21.006 1.00 29.89  ? 207 ARG B CB  1 
ATOM   3975 C CG  . ARG B 1 207 ? -11.040 -18.034 -19.851 1.00 26.68  ? 207 ARG B CG  1 
ATOM   3976 C CD  . ARG B 1 207 ? -10.004 -19.055 -20.247 1.00 30.83  ? 207 ARG B CD  1 
ATOM   3977 N NE  . ARG B 1 207 ? -10.476 -20.418 -20.004 1.00 30.28  ? 207 ARG B NE  1 
ATOM   3978 C CZ  . ARG B 1 207 ? -10.449 -21.037 -18.829 1.00 30.07  ? 207 ARG B CZ  1 
ATOM   3979 N NH1 . ARG B 1 207 ? -9.993  -20.439 -17.739 1.00 30.46  ? 207 ARG B NH1 1 
ATOM   3980 N NH2 . ARG B 1 207 ? -10.865 -22.301 -18.750 1.00 29.45  ? 207 ARG B NH2 1 
ATOM   3981 N N   . TRP B 1 208 ? -15.005 -17.378 -21.683 1.00 25.90  ? 208 TRP B N   1 
ATOM   3982 C CA  . TRP B 1 208 ? -16.125 -17.388 -22.629 1.00 24.18  ? 208 TRP B CA  1 
ATOM   3983 C C   . TRP B 1 208 ? -16.792 -16.018 -22.717 1.00 27.19  ? 208 TRP B C   1 
ATOM   3984 O O   . TRP B 1 208 ? -17.198 -15.580 -23.806 1.00 28.36  ? 208 TRP B O   1 
ATOM   3985 C CB  . TRP B 1 208 ? -17.125 -18.448 -22.189 1.00 26.98  ? 208 TRP B CB  1 
ATOM   3986 C CG  . TRP B 1 208 ? -18.259 -18.769 -23.129 1.00 28.59  ? 208 TRP B CG  1 
ATOM   3987 C CD1 . TRP B 1 208 ? -18.302 -19.760 -24.075 1.00 29.34  ? 208 TRP B CD1 1 
ATOM   3988 C CD2 . TRP B 1 208 ? -19.530 -18.125 -23.155 1.00 25.83  ? 208 TRP B CD2 1 
ATOM   3989 N NE1 . TRP B 1 208 ? -19.539 -19.754 -24.712 1.00 27.41  ? 208 TRP B NE1 1 
ATOM   3990 C CE2 . TRP B 1 208 ? -20.310 -18.763 -24.158 1.00 26.67  ? 208 TRP B CE2 1 
ATOM   3991 C CE3 . TRP B 1 208 ? -20.094 -17.076 -22.426 1.00 28.71  ? 208 TRP B CE3 1 
ATOM   3992 C CZ2 . TRP B 1 208 ? -21.613 -18.377 -24.437 1.00 28.90  ? 208 TRP B CZ2 1 
ATOM   3993 C CZ3 . TRP B 1 208 ? -21.373 -16.681 -22.715 1.00 28.13  ? 208 TRP B CZ3 1 
ATOM   3994 C CH2 . TRP B 1 208 ? -22.129 -17.327 -23.716 1.00 29.38  ? 208 TRP B CH2 1 
ATOM   3995 N N   . GLY B 1 209 ? -16.925 -15.331 -21.575 1.00 27.25  ? 209 GLY B N   1 
ATOM   3996 C CA  . GLY B 1 209 ? -17.579 -14.028 -21.537 1.00 26.76  ? 209 GLY B CA  1 
ATOM   3997 C C   . GLY B 1 209 ? -16.842 -12.967 -22.311 1.00 29.66  ? 209 GLY B C   1 
ATOM   3998 O O   . GLY B 1 209 ? -17.462 -11.981 -22.732 1.00 29.73  ? 209 GLY B O   1 
ATOM   3999 N N   . MET B 1 210 ? -15.545 -13.161 -22.533 1.00 28.36  ? 210 MET B N   1 
ATOM   4000 C CA  . MET B 1 210 ? -14.722 -12.261 -23.329 1.00 29.64  ? 210 MET B CA  1 
ATOM   4001 C C   . MET B 1 210 ? -14.546 -12.746 -24.764 1.00 33.95  ? 210 MET B C   1 
ATOM   4002 O O   . MET B 1 210 ? -13.736 -12.177 -25.502 1.00 32.29  ? 210 MET B O   1 
ATOM   4003 C CB  . MET B 1 210 ? -13.360 -12.083 -22.660 1.00 29.83  ? 210 MET B CB  1 
ATOM   4004 C CG  . MET B 1 210 ? -13.407 -11.144 -21.465 1.00 32.75  ? 210 MET B CG  1 
ATOM   4005 S SD  . MET B 1 210 ? -11.792 -10.720 -20.763 1.00 32.98  ? 210 MET B SD  1 
ATOM   4006 C CE  . MET B 1 210 ? -11.048 -12.336 -20.580 1.00 32.36  ? 210 MET B CE  1 
ATOM   4007 N N   . ASP B 1 211 ? -15.252 -13.807 -25.161 1.00 33.66  ? 211 ASP B N   1 
ATOM   4008 C CA  . ASP B 1 211 ? -15.120 -14.372 -26.508 1.00 32.99  ? 211 ASP B CA  1 
ATOM   4009 C C   . ASP B 1 211 ? -13.672 -14.770 -26.805 1.00 35.25  ? 211 ASP B C   1 
ATOM   4010 O O   . ASP B 1 211 ? -13.118 -14.453 -27.858 1.00 37.30  ? 211 ASP B O   1 
ATOM   4011 C CB  . ASP B 1 211 ? -15.651 -13.384 -27.554 1.00 36.18  ? 211 ASP B CB  1 
ATOM   4012 C CG  . ASP B 1 211 ? -15.874 -14.025 -28.915 1.00 40.45  ? 211 ASP B CG  1 
ATOM   4013 O OD1 . ASP B 1 211 ? -16.054 -15.255 -28.979 1.00 41.67  ? 211 ASP B OD1 1 
ATOM   4014 O OD2 . ASP B 1 211 ? -15.860 -13.281 -29.922 1.00 44.71  ? 211 ASP B OD2 1 
ATOM   4015 N N   . MET B 1 212 ? -13.035 -15.461 -25.859 1.00 32.33  ? 212 MET B N   1 
ATOM   4016 C CA  . MET B 1 212 ? -11.661 -15.875 -26.103 1.00 33.90  ? 212 MET B CA  1 
ATOM   4017 C C   . MET B 1 212 ? -11.417 -17.227 -25.458 1.00 33.56  ? 212 MET B C   1 
ATOM   4018 O O   . MET B 1 212 ? -12.215 -17.704 -24.650 1.00 32.73  ? 212 MET B O   1 
ATOM   4019 C CB  . MET B 1 212 ? -10.650 -14.825 -25.615 1.00 37.75  ? 212 MET B CB  1 
ATOM   4020 C CG  . MET B 1 212 ? -10.698 -14.400 -24.170 1.00 36.50  ? 212 MET B CG  1 
ATOM   4021 S SD  . MET B 1 212 ? -10.159 -15.657 -23.000 1.00 41.26  ? 212 MET B SD  1 
ATOM   4022 C CE  . MET B 1 212 ? -8.426  -15.263 -22.966 1.00 36.50  ? 212 MET B CE  1 
ATOM   4023 N N   . THR B 1 213 ? -10.319 -17.859 -25.856 1.00 34.06  ? 213 THR B N   1 
ATOM   4024 C CA  . THR B 1 213 ? -9.942  -19.131 -25.267 1.00 34.66  ? 213 THR B CA  1 
ATOM   4025 C C   . THR B 1 213 ? -8.460  -19.081 -24.952 1.00 36.02  ? 213 THR B C   1 
ATOM   4026 O O   . THR B 1 213 ? -7.719  -18.229 -25.449 1.00 36.47  ? 213 THR B O   1 
ATOM   4027 C CB  . THR B 1 213 ? -10.183 -20.329 -26.195 1.00 36.86  ? 213 THR B CB  1 
ATOM   4028 O OG1 . THR B 1 213 ? -9.617  -20.061 -27.481 1.00 39.58  ? 213 THR B OG1 1 
ATOM   4029 C CG2 . THR B 1 213 ? -11.679 -20.524 -26.377 1.00 37.35  ? 213 THR B CG2 1 
ATOM   4030 N N   . LEU B 1 214 ? -8.036  -20.018 -24.121 1.00 35.64  ? 214 LEU B N   1 
ATOM   4031 C CA  . LEU B 1 214 ? -6.634  -20.317 -23.927 1.00 36.37  ? 214 LEU B CA  1 
ATOM   4032 C C   . LEU B 1 214 ? -6.345  -21.636 -24.633 1.00 34.77  ? 214 LEU B C   1 
ATOM   4033 O O   . LEU B 1 214 ? -7.147  -22.571 -24.568 1.00 37.61  ? 214 LEU B O   1 
ATOM   4034 C CB  . LEU B 1 214 ? -6.317  -20.420 -22.432 1.00 34.98  ? 214 LEU B CB  1 
ATOM   4035 C CG  . LEU B 1 214 ? -6.228  -19.095 -21.655 1.00 32.56  ? 214 LEU B CG  1 
ATOM   4036 C CD1 . LEU B 1 214 ? -5.748  -19.392 -20.254 1.00 32.57  ? 214 LEU B CD1 1 
ATOM   4037 C CD2 . LEU B 1 214 ? -5.297  -18.076 -22.300 1.00 35.45  ? 214 LEU B CD2 1 
ATOM   4038 N N   . SER B 1 215 ? -5.215  -21.698 -25.322 1.00 35.65  ? 215 SER B N   1 
ATOM   4039 C CA  . SER B 1 215 ? -4.743  -22.949 -25.897 1.00 41.51  ? 215 SER B CA  1 
ATOM   4040 C C   . SER B 1 215 ? -4.330  -23.930 -24.794 1.00 41.69  ? 215 SER B C   1 
ATOM   4041 O O   . SER B 1 215 ? -4.177  -23.568 -23.627 1.00 37.56  ? 215 SER B O   1 
ATOM   4042 C CB  . SER B 1 215 ? -3.588  -22.665 -26.853 1.00 44.19  ? 215 SER B CB  1 
ATOM   4043 O OG  . SER B 1 215 ? -2.350  -22.691 -26.179 1.00 44.34  ? 215 SER B OG  1 
ATOM   4044 N N   . GLU B 1 216 ? -4.157  -25.201 -25.170 1.00 42.45  ? 216 GLU B N   1 
ATOM   4045 C CA  . GLU B 1 216 ? -3.739  -26.197 -24.185 1.00 43.81  ? 216 GLU B CA  1 
ATOM   4046 C C   . GLU B 1 216 ? -2.396  -25.827 -23.574 1.00 39.16  ? 216 GLU B C   1 
ATOM   4047 O O   . GLU B 1 216 ? -2.217  -25.886 -22.352 1.00 40.56  ? 216 GLU B O   1 
ATOM   4048 C CB  . GLU B 1 216 ? -3.677  -27.582 -24.829 1.00 47.61  ? 216 GLU B CB  1 
ATOM   4049 C CG  . GLU B 1 216 ? -4.788  -28.505 -24.393 1.00 53.91  ? 216 GLU B CG  1 
ATOM   4050 C CD  . GLU B 1 216 ? -4.517  -29.947 -24.784 1.00 59.97  ? 216 GLU B CD  1 
ATOM   4051 O OE1 . GLU B 1 216 ? -4.405  -30.213 -25.999 1.00 61.96  ? 216 GLU B OE1 1 
ATOM   4052 O OE2 . GLU B 1 216 ? -4.403  -30.808 -23.883 1.00 62.28  ? 216 GLU B OE2 1 
ATOM   4053 N N   . GLU B 1 217 ? -1.442  -25.419 -24.412 1.00 42.85  ? 217 GLU B N   1 
ATOM   4054 C CA  . GLU B 1 217 ? -0.133  -25.034 -23.905 1.00 43.64  ? 217 GLU B CA  1 
ATOM   4055 C C   . GLU B 1 217 ? -0.210  -23.735 -23.111 1.00 39.50  ? 217 GLU B C   1 
ATOM   4056 O O   . GLU B 1 217 ? 0.452   -23.598 -22.077 1.00 41.04  ? 217 GLU B O   1 
ATOM   4057 C CB  . GLU B 1 217 ? 0.865   -24.920 -25.060 1.00 47.93  ? 217 GLU B CB  1 
ATOM   4058 C CG  . GLU B 1 217 ? 0.355   -24.159 -26.288 1.00 52.75  ? 217 GLU B CG  1 
ATOM   4059 C CD  . GLU B 1 217 ? -0.371  -25.025 -27.340 1.00 58.61  ? 217 GLU B CD  1 
ATOM   4060 O OE1 . GLU B 1 217 ? -1.164  -25.934 -26.988 1.00 53.52  ? 217 GLU B OE1 1 
ATOM   4061 O OE2 . GLU B 1 217 ? -0.154  -24.771 -28.548 1.00 61.50  ? 217 GLU B OE2 1 
ATOM   4062 N N   . GLU B 1 218 ? -1.016  -22.777 -23.574 1.00 41.72  ? 218 GLU B N   1 
ATOM   4063 C CA  . GLU B 1 218 ? -1.201  -21.533 -22.829 1.00 40.85  ? 218 GLU B CA  1 
ATOM   4064 C C   . GLU B 1 218 ? -1.752  -21.816 -21.439 1.00 38.45  ? 218 GLU B C   1 
ATOM   4065 O O   . GLU B 1 218 ? -1.241  -21.296 -20.438 1.00 36.74  ? 218 GLU B O   1 
ATOM   4066 C CB  . GLU B 1 218 ? -2.143  -20.604 -23.596 1.00 40.74  ? 218 GLU B CB  1 
ATOM   4067 C CG  . GLU B 1 218 ? -1.511  -19.967 -24.821 1.00 41.56  ? 218 GLU B CG  1 
ATOM   4068 C CD  . GLU B 1 218 ? -2.451  -19.028 -25.549 1.00 42.21  ? 218 GLU B CD  1 
ATOM   4069 O OE1 . GLU B 1 218 ? -3.661  -19.322 -25.612 1.00 40.89  ? 218 GLU B OE1 1 
ATOM   4070 O OE2 . GLU B 1 218 ? -1.971  -18.021 -26.105 1.00 43.47  ? 218 GLU B OE2 1 
ATOM   4071 N N   . TYR B 1 219 ? -2.807  -22.635 -21.361 1.00 35.08  ? 219 TYR B N   1 
ATOM   4072 C CA  . TYR B 1 219 ? -3.397  -22.940 -20.062 1.00 36.24  ? 219 TYR B CA  1 
ATOM   4073 C C   . TYR B 1 219 ? -2.408  -23.676 -19.170 1.00 36.75  ? 219 TYR B C   1 
ATOM   4074 O O   . TYR B 1 219 ? -2.323  -23.404 -17.966 1.00 34.45  ? 219 TYR B O   1 
ATOM   4075 C CB  . TYR B 1 219 ? -4.661  -23.793 -20.185 1.00 35.63  ? 219 TYR B CB  1 
ATOM   4076 C CG  . TYR B 1 219 ? -5.243  -23.959 -18.805 1.00 37.22  ? 219 TYR B CG  1 
ATOM   4077 C CD1 . TYR B 1 219 ? -5.876  -22.894 -18.176 1.00 36.39  ? 219 TYR B CD1 1 
ATOM   4078 C CD2 . TYR B 1 219 ? -4.974  -25.106 -18.042 1.00 35.15  ? 219 TYR B CD2 1 
ATOM   4079 C CE1 . TYR B 1 219 ? -6.348  -23.008 -16.880 1.00 36.43  ? 219 TYR B CE1 1 
ATOM   4080 C CE2 . TYR B 1 219 ? -5.414  -25.218 -16.737 1.00 36.71  ? 219 TYR B CE2 1 
ATOM   4081 C CZ  . TYR B 1 219 ? -6.102  -24.168 -16.157 1.00 36.17  ? 219 TYR B CZ  1 
ATOM   4082 O OH  . TYR B 1 219 ? -6.560  -24.276 -14.865 1.00 34.76  ? 219 TYR B OH  1 
ATOM   4083 N N   . ALA B 1 220 ? -1.687  -24.651 -19.728 1.00 36.88  ? 220 ALA B N   1 
ATOM   4084 C CA  . ALA B 1 220 ? -0.717  -25.384 -18.921 1.00 36.97  ? 220 ALA B CA  1 
ATOM   4085 C C   . ALA B 1 220 ? 0.322   -24.448 -18.318 1.00 36.87  ? 220 ALA B C   1 
ATOM   4086 O O   . ALA B 1 220 ? 0.772   -24.662 -17.185 1.00 36.52  ? 220 ALA B O   1 
ATOM   4087 C CB  . ALA B 1 220 ? -0.044  -26.471 -19.763 1.00 37.72  ? 220 ALA B CB  1 
ATOM   4088 N N   . SER B 1 221 ? 0.685   -23.386 -19.039 1.00 35.00  ? 221 SER B N   1 
ATOM   4089 C CA  . SER B 1 221 ? 1.695   -22.452 -18.566 1.00 36.53  ? 221 SER B CA  1 
ATOM   4090 C C   . SER B 1 221 ? 1.222   -21.591 -17.399 1.00 36.87  ? 221 SER B C   1 
ATOM   4091 O O   . SER B 1 221 ? 2.057   -20.930 -16.768 1.00 35.78  ? 221 SER B O   1 
ATOM   4092 C CB  . SER B 1 221 ? 2.153   -21.571 -19.731 1.00 39.06  ? 221 SER B CB  1 
ATOM   4093 O OG  . SER B 1 221 ? 1.259   -20.502 -19.952 1.00 40.17  ? 221 SER B OG  1 
ATOM   4094 N N   . ILE B 1 222 ? -0.077  -21.582 -17.091 1.00 34.98  ? 222 ILE B N   1 
ATOM   4095 C CA  . ILE B 1 222 ? -0.602  -20.779 -15.989 1.00 35.48  ? 222 ILE B CA  1 
ATOM   4096 C C   . ILE B 1 222 ? -1.510  -21.613 -15.085 1.00 31.92  ? 222 ILE B C   1 
ATOM   4097 O O   . ILE B 1 222 ? -2.277  -21.063 -14.289 1.00 31.04  ? 222 ILE B O   1 
ATOM   4098 C CB  . ILE B 1 222 ? -1.337  -19.530 -16.514 1.00 33.73  ? 222 ILE B CB  1 
ATOM   4099 C CG1 . ILE B 1 222 ? -2.455  -19.930 -17.481 1.00 36.70  ? 222 ILE B CG1 1 
ATOM   4100 C CG2 . ILE B 1 222 ? -0.380  -18.588 -17.230 1.00 33.77  ? 222 ILE B CG2 1 
ATOM   4101 C CD1 . ILE B 1 222 ? -3.840  -19.786 -16.928 1.00 40.73  ? 222 ILE B CD1 1 
ATOM   4102 N N   . GLU B 1 223 ? -1.423  -22.944 -15.184 1.00 30.74  ? 223 GLU B N   1 
ATOM   4103 C CA  . GLU B 1 223 ? -2.290  -23.798 -14.373 1.00 31.97  ? 223 GLU B CA  1 
ATOM   4104 C C   . GLU B 1 223 ? -2.052  -23.608 -12.875 1.00 30.66  ? 223 GLU B C   1 
ATOM   4105 O O   . GLU B 1 223 ? -3.007  -23.593 -12.091 1.00 31.37  ? 223 GLU B O   1 
ATOM   4106 C CB  . GLU B 1 223 ? -2.095  -25.266 -14.746 1.00 36.70  ? 223 GLU B CB  1 
ATOM   4107 C CG  . GLU B 1 223 ? -3.163  -26.146 -14.135 1.00 37.18  ? 223 GLU B CG  1 
ATOM   4108 C CD  . GLU B 1 223 ? -3.003  -27.615 -14.479 1.00 46.25  ? 223 GLU B CD  1 
ATOM   4109 O OE1 . GLU B 1 223 ? -1.913  -28.014 -14.941 1.00 48.08  ? 223 GLU B OE1 1 
ATOM   4110 O OE2 . GLU B 1 223 ? -3.995  -28.355 -14.319 1.00 49.13  ? 223 GLU B OE2 1 
ATOM   4111 N N   . GLN B 1 224 ? -0.793  -23.488 -12.444 1.00 30.38  ? 224 GLN B N   1 
ATOM   4112 C CA  . GLN B 1 224 ? -0.562  -23.333 -11.007 1.00 30.55  ? 224 GLN B CA  1 
ATOM   4113 C C   . GLN B 1 224 ? -1.071  -21.983 -10.521 1.00 28.87  ? 224 GLN B C   1 
ATOM   4114 O O   . GLN B 1 224 ? -1.644  -21.885 -9.429  1.00 30.02  ? 224 GLN B O   1 
ATOM   4115 C CB  . GLN B 1 224 ? 0.913   -23.513 -10.655 1.00 34.42  ? 224 GLN B CB  1 
ATOM   4116 C CG  . GLN B 1 224 ? 1.457   -24.877 -11.027 1.00 36.69  ? 224 GLN B CG  1 
ATOM   4117 C CD  . GLN B 1 224 ? 0.655   -25.993 -10.384 1.00 41.47  ? 224 GLN B CD  1 
ATOM   4118 O OE1 . GLN B 1 224 ? 0.131   -26.875 -11.073 1.00 48.31  ? 224 GLN B OE1 1 
ATOM   4119 N NE2 . GLN B 1 224 ? 0.470   -25.908 -9.079  1.00 42.58  ? 224 GLN B NE2 1 
ATOM   4120 N N   . PHE B 1 225 ? -0.887  -20.939 -11.330 1.00 28.31  ? 225 PHE B N   1 
ATOM   4121 C CA  . PHE B 1 225 ? -1.508  -19.650 -11.034 1.00 28.27  ? 225 PHE B CA  1 
ATOM   4122 C C   . PHE B 1 225 ? -3.013  -19.802 -10.868 1.00 27.70  ? 225 PHE B C   1 
ATOM   4123 O O   . PHE B 1 225 ? -3.606  -19.297 -9.908  1.00 27.44  ? 225 PHE B O   1 
ATOM   4124 C CB  . PHE B 1 225 ? -1.194  -18.662 -12.156 1.00 28.79  ? 225 PHE B CB  1 
ATOM   4125 C CG  . PHE B 1 225 ? -2.085  -17.448 -12.179 1.00 30.66  ? 225 PHE B CG  1 
ATOM   4126 C CD1 . PHE B 1 225 ? -1.809  -16.344 -11.381 1.00 28.90  ? 225 PHE B CD1 1 
ATOM   4127 C CD2 . PHE B 1 225 ? -3.214  -17.418 -13.003 1.00 28.25  ? 225 PHE B CD2 1 
ATOM   4128 C CE1 . PHE B 1 225 ? -2.625  -15.224 -11.397 1.00 28.59  ? 225 PHE B CE1 1 
ATOM   4129 C CE2 . PHE B 1 225 ? -4.046  -16.315 -13.027 1.00 30.93  ? 225 PHE B CE2 1 
ATOM   4130 C CZ  . PHE B 1 225 ? -3.755  -15.198 -12.236 1.00 28.58  ? 225 PHE B CZ  1 
ATOM   4131 N N   . ASP B 1 226 ? -3.654  -20.477 -11.826 1.00 27.52  ? 226 ASP B N   1 
ATOM   4132 C CA  . ASP B 1 226 ? -5.104  -20.647 -11.793 1.00 28.85  ? 226 ASP B CA  1 
ATOM   4133 C C   . ASP B 1 226 ? -5.554  -21.380 -10.536 1.00 27.68  ? 226 ASP B C   1 
ATOM   4134 O O   . ASP B 1 226 ? -6.591  -21.041 -9.949  1.00 27.30  ? 226 ASP B O   1 
ATOM   4135 C CB  . ASP B 1 226 ? -5.540  -21.437 -13.022 1.00 27.15  ? 226 ASP B CB  1 
ATOM   4136 C CG  . ASP B 1 226 ? -6.893  -21.040 -13.538 1.00 28.02  ? 226 ASP B CG  1 
ATOM   4137 O OD1 . ASP B 1 226 ? -7.375  -19.928 -13.262 1.00 30.97  ? 226 ASP B OD1 1 
ATOM   4138 O OD2 . ASP B 1 226 ? -7.509  -21.917 -14.172 1.00 29.26  ? 226 ASP B OD2 1 
ATOM   4139 N N   . ILE B 1 227 ? -4.813  -22.417 -10.138 1.00 25.70  ? 227 ILE B N   1 
ATOM   4140 C CA  . ILE B 1 227 ? -5.172  -23.169 -8.940  1.00 27.84  ? 227 ILE B CA  1 
ATOM   4141 C C   . ILE B 1 227 ? -5.082  -22.267 -7.717  1.00 27.46  ? 227 ILE B C   1 
ATOM   4142 O O   . ILE B 1 227 ? -5.953  -22.301 -6.837  1.00 27.84  ? 227 ILE B O   1 
ATOM   4143 C CB  . ILE B 1 227 ? -4.276  -24.416 -8.787  1.00 29.35  ? 227 ILE B CB  1 
ATOM   4144 C CG1 . ILE B 1 227 ? -4.706  -25.507 -9.767  1.00 30.31  ? 227 ILE B CG1 1 
ATOM   4145 C CG2 . ILE B 1 227 ? -4.337  -24.971 -7.363  1.00 28.65  ? 227 ILE B CG2 1 
ATOM   4146 C CD1 . ILE B 1 227 ? -3.577  -26.471 -10.142 1.00 34.63  ? 227 ILE B CD1 1 
ATOM   4147 N N   . ALA B 1 228 ? -4.038  -21.439 -7.648  1.00 28.03  ? 228 ALA B N   1 
ATOM   4148 C CA  . ALA B 1 228 ? -3.915  -20.524 -6.519  1.00 27.69  ? 228 ALA B CA  1 
ATOM   4149 C C   . ALA B 1 228 ? -5.106  -19.579 -6.459  1.00 25.88  ? 228 ALA B C   1 
ATOM   4150 O O   . ALA B 1 228 ? -5.689  -19.369 -5.387  1.00 25.93  ? 228 ALA B O   1 
ATOM   4151 C CB  . ALA B 1 228 ? -2.594  -19.742 -6.595  1.00 29.12  ? 228 ALA B CB  1 
ATOM   4152 N N   . MET B 1 229 ? -5.493  -18.999 -7.611  1.00 26.25  ? 229 MET B N   1 
ATOM   4153 C CA  . MET B 1 229 ? -6.671  -18.139 -7.640  1.00 26.42  ? 229 MET B CA  1 
ATOM   4154 C C   . MET B 1 229 ? -7.928  -18.900 -7.245  1.00 25.48  ? 229 MET B C   1 
ATOM   4155 O O   . MET B 1 229 ? -8.787  -18.358 -6.545  1.00 27.69  ? 229 MET B O   1 
ATOM   4156 C CB  . MET B 1 229 ? -6.829  -17.492 -9.024  1.00 25.09  ? 229 MET B CB  1 
ATOM   4157 C CG  . MET B 1 229 ? -5.660  -16.552 -9.351  1.00 28.40  ? 229 MET B CG  1 
ATOM   4158 S SD  . MET B 1 229 ? -5.602  -15.098 -8.252  1.00 27.92  ? 229 MET B SD  1 
ATOM   4159 C CE  . MET B 1 229 ? -6.467  -13.891 -9.279  1.00 29.60  ? 229 MET B CE  1 
ATOM   4160 N N   . GLY B 1 230 ? -8.061  -20.156 -7.689  1.00 23.08  ? 230 GLY B N   1 
ATOM   4161 C CA  . GLY B 1 230 ? -9.210  -20.952 -7.290  1.00 26.74  ? 230 GLY B CA  1 
ATOM   4162 C C   . GLY B 1 230 ? -9.252  -21.208 -5.797  1.00 28.05  ? 230 GLY B C   1 
ATOM   4163 O O   . GLY B 1 230 ? -10.329 -21.232 -5.192  1.00 26.92  ? 230 GLY B O   1 
ATOM   4164 N N   . ASN B 1 231 ? -8.080  -21.420 -5.186  1.00 24.85  ? 231 ASN B N   1 
ATOM   4165 C CA  . ASN B 1 231 ? -8.001  -21.537 -3.726  1.00 27.69  ? 231 ASN B CA  1 
ATOM   4166 C C   . ASN B 1 231 ? -8.491  -20.261 -3.052  1.00 27.60  ? 231 ASN B C   1 
ATOM   4167 O O   . ASN B 1 231 ? -9.262  -20.307 -2.086  1.00 27.71  ? 231 ASN B O   1 
ATOM   4168 C CB  . ASN B 1 231 ? -6.567  -21.840 -3.298  1.00 26.48  ? 231 ASN B CB  1 
ATOM   4169 C CG  . ASN B 1 231 ? -6.191  -23.288 -3.492  1.00 30.57  ? 231 ASN B CG  1 
ATOM   4170 O OD1 . ASN B 1 231 ? -7.022  -24.179 -3.351  1.00 32.37  ? 231 ASN B OD1 1 
ATOM   4171 N ND2 . ASN B 1 231 ? -4.925  -23.532 -3.822  1.00 33.89  ? 231 ASN B ND2 1 
ATOM   4172 N N   . VAL B 1 232 ? -8.047  -19.108 -3.550  1.00 25.58  ? 232 VAL B N   1 
ATOM   4173 C CA  . VAL B 1 232 ? -8.493  -17.833 -2.990  1.00 27.00  ? 232 VAL B CA  1 
ATOM   4174 C C   . VAL B 1 232 ? -10.011 -17.729 -3.028  1.00 28.88  ? 232 VAL B C   1 
ATOM   4175 O O   . VAL B 1 232 ? -10.658 -17.350 -2.044  1.00 27.87  ? 232 VAL B O   1 
ATOM   4176 C CB  . VAL B 1 232 ? -7.849  -16.662 -3.748  1.00 26.78  ? 232 VAL B CB  1 
ATOM   4177 C CG1 . VAL B 1 232 ? -8.407  -15.348 -3.221  1.00 26.63  ? 232 VAL B CG1 1 
ATOM   4178 C CG2 . VAL B 1 232 ? -6.324  -16.701 -3.584  1.00 29.56  ? 232 VAL B CG2 1 
ATOM   4179 N N   . LEU B 1 233 ? -10.601 -18.038 -4.180  1.00 26.42  ? 233 LEU B N   1 
ATOM   4180 C CA  . LEU B 1 233 ? -12.032 -17.836 -4.365  1.00 26.97  ? 233 LEU B CA  1 
ATOM   4181 C C   . LEU B 1 233 ? -12.844 -18.626 -3.344  1.00 27.31  ? 233 LEU B C   1 
ATOM   4182 O O   . LEU B 1 233 ? -13.655 -18.060 -2.608  1.00 29.14  ? 233 LEU B O   1 
ATOM   4183 C CB  . LEU B 1 233 ? -12.411 -18.243 -5.790  1.00 25.77  ? 233 LEU B CB  1 
ATOM   4184 C CG  . LEU B 1 233 ? -13.687 -17.703 -6.434  1.00 26.77  ? 233 LEU B CG  1 
ATOM   4185 C CD1 . LEU B 1 233 ? -14.935 -18.339 -5.832  1.00 32.99  ? 233 LEU B CD1 1 
ATOM   4186 C CD2 . LEU B 1 233 ? -13.727 -16.166 -6.314  1.00 29.83  ? 233 LEU B CD2 1 
ATOM   4187 N N   . GLY B 1 234 ? -12.669 -19.950 -3.314  1.00 28.02  ? 234 GLY B N   1 
ATOM   4188 C CA  . GLY B 1 234 ? -13.509 -20.770 -2.457  1.00 27.79  ? 234 GLY B CA  1 
ATOM   4189 C C   . GLY B 1 234 ? -13.212 -20.586 -0.977  1.00 28.56  ? 234 GLY B C   1 
ATOM   4190 O O   . GLY B 1 234 ? -14.127 -20.563 -0.150  1.00 28.43  ? 234 GLY B O   1 
ATOM   4191 N N   . LEU B 1 235 ? -11.939 -20.443 -0.621  1.00 27.24  ? 235 LEU B N   1 
ATOM   4192 C CA  . LEU B 1 235 ? -11.629 -20.264 0.794   1.00 27.40  ? 235 LEU B CA  1 
ATOM   4193 C C   . LEU B 1 235 ? -12.078 -18.896 1.296   1.00 30.14  ? 235 LEU B C   1 
ATOM   4194 O O   . LEU B 1 235 ? -12.419 -18.752 2.477   1.00 30.54  ? 235 LEU B O   1 
ATOM   4195 C CB  . LEU B 1 235 ? -10.134 -20.481 1.062   1.00 25.65  ? 235 LEU B CB  1 
ATOM   4196 C CG  . LEU B 1 235 ? -9.554  -21.852 0.672   1.00 27.48  ? 235 LEU B CG  1 
ATOM   4197 C CD1 . LEU B 1 235 ? -8.065  -21.890 0.999   1.00 30.42  ? 235 LEU B CD1 1 
ATOM   4198 C CD2 . LEU B 1 235 ? -10.281 -22.986 1.397   1.00 29.47  ? 235 LEU B CD2 1 
ATOM   4199 N N   . THR B 1 236 ? -12.099 -17.888 0.425   1.00 27.72  ? 236 THR B N   1 
ATOM   4200 C CA  . THR B 1 236 ? -12.651 -16.600 0.832   1.00 27.25  ? 236 THR B CA  1 
ATOM   4201 C C   . THR B 1 236 ? -14.154 -16.707 1.056   1.00 29.62  ? 236 THR B C   1 
ATOM   4202 O O   . THR B 1 236 ? -14.681 -16.128 2.013   1.00 29.79  ? 236 THR B O   1 
ATOM   4203 C CB  . THR B 1 236 ? -12.307 -15.530 -0.205  1.00 28.26  ? 236 THR B CB  1 
ATOM   4204 O OG1 . THR B 1 236 ? -10.878 -15.369 -0.254  1.00 27.09  ? 236 THR B OG1 1 
ATOM   4205 C CG2 . THR B 1 236 ? -12.956 -14.197 0.151   1.00 29.31  ? 236 THR B CG2 1 
ATOM   4206 N N   . ASN B 1 237 ? -14.862 -17.448 0.186   1.00 29.98  ? 237 ASN B N   1 
ATOM   4207 C CA  . ASN B 1 237 ? -16.263 -17.779 0.454   1.00 31.47  ? 237 ASN B CA  1 
ATOM   4208 C C   . ASN B 1 237 ? -16.415 -18.422 1.832   1.00 31.28  ? 237 ASN B C   1 
ATOM   4209 O O   . ASN B 1 237 ? -17.287 -18.037 2.619   1.00 34.64  ? 237 ASN B O   1 
ATOM   4210 C CB  . ASN B 1 237 ? -16.813 -18.711 -0.642  1.00 31.25  ? 237 ASN B CB  1 
ATOM   4211 C CG  . ASN B 1 237 ? -16.908 -18.044 -2.011  1.00 41.56  ? 237 ASN B CG  1 
ATOM   4212 O OD1 . ASN B 1 237 ? -16.352 -16.969 -2.237  1.00 41.86  ? 237 ASN B OD1 1 
ATOM   4213 N ND2 . ASN B 1 237 ? -17.577 -18.717 -2.952  1.00 46.96  ? 237 ASN B ND2 1 
ATOM   4214 N N   . ASP B 1 238 ? -15.549 -19.387 2.154   1.00 31.72  ? 238 ASP B N   1 
ATOM   4215 C CA  . ASP B 1 238 ? -15.597 -20.023 3.470   1.00 32.09  ? 238 ASP B CA  1 
ATOM   4216 C C   . ASP B 1 238 ? -15.369 -19.008 4.579   1.00 35.10  ? 238 ASP B C   1 
ATOM   4217 O O   . ASP B 1 238 ? -16.070 -19.015 5.597   1.00 33.33  ? 238 ASP B O   1 
ATOM   4218 C CB  . ASP B 1 238 ? -14.542 -21.126 3.598   1.00 30.97  ? 238 ASP B CB  1 
ATOM   4219 C CG  . ASP B 1 238 ? -14.838 -22.339 2.755   1.00 35.22  ? 238 ASP B CG  1 
ATOM   4220 O OD1 . ASP B 1 238 ? -15.884 -22.359 2.074   1.00 33.99  ? 238 ASP B OD1 1 
ATOM   4221 O OD2 . ASP B 1 238 ? -14.018 -23.287 2.814   1.00 33.52  ? 238 ASP B OD2 1 
ATOM   4222 N N   . TYR B 1 239 ? -14.368 -18.147 4.406   1.00 31.17  ? 239 TYR B N   1 
ATOM   4223 C CA  . TYR B 1 239 ? -14.030 -17.194 5.457   1.00 32.62  ? 239 TYR B CA  1 
ATOM   4224 C C   . TYR B 1 239 ? -15.233 -16.327 5.803   1.00 33.44  ? 239 TYR B C   1 
ATOM   4225 O O   . TYR B 1 239 ? -15.577 -16.162 6.978   1.00 33.39  ? 239 TYR B O   1 
ATOM   4226 C CB  . TYR B 1 239 ? -12.837 -16.336 5.032   1.00 29.69  ? 239 TYR B CB  1 
ATOM   4227 C CG  . TYR B 1 239 ? -12.456 -15.296 6.062   1.00 28.13  ? 239 TYR B CG  1 
ATOM   4228 C CD1 . TYR B 1 239 ? -11.645 -15.639 7.135   1.00 32.33  ? 239 TYR B CD1 1 
ATOM   4229 C CD2 . TYR B 1 239 ? -12.893 -13.980 5.953   1.00 31.77  ? 239 TYR B CD2 1 
ATOM   4230 C CE1 . TYR B 1 239 ? -11.281 -14.699 8.084   1.00 31.00  ? 239 TYR B CE1 1 
ATOM   4231 C CE2 . TYR B 1 239 ? -12.539 -13.035 6.900   1.00 32.69  ? 239 TYR B CE2 1 
ATOM   4232 C CZ  . TYR B 1 239 ? -11.736 -13.409 7.957   1.00 33.76  ? 239 TYR B CZ  1 
ATOM   4233 O OH  . TYR B 1 239 ? -11.380 -12.467 8.899   1.00 37.56  ? 239 TYR B OH  1 
ATOM   4234 N N   . PHE B 1 240 ? -15.923 -15.804 4.784   1.00 33.05  ? 240 PHE B N   1 
ATOM   4235 C CA  . PHE B 1 240 ? -17.029 -14.903 5.057   1.00 34.63  ? 240 PHE B CA  1 
ATOM   4236 C C   . PHE B 1 240 ? -18.306 -15.624 5.443   1.00 38.07  ? 240 PHE B C   1 
ATOM   4237 O O   . PHE B 1 240 ? -19.191 -15.001 6.036   1.00 42.92  ? 240 PHE B O   1 
ATOM   4238 C CB  . PHE B 1 240 ? -17.283 -13.993 3.859   1.00 36.45  ? 240 PHE B CB  1 
ATOM   4239 C CG  . PHE B 1 240 ? -16.278 -12.901 3.734   1.00 35.25  ? 240 PHE B CG  1 
ATOM   4240 C CD1 . PHE B 1 240 ? -16.299 -11.825 4.612   1.00 38.82  ? 240 PHE B CD1 1 
ATOM   4241 C CD2 . PHE B 1 240 ? -15.310 -12.939 2.750   1.00 35.89  ? 240 PHE B CD2 1 
ATOM   4242 C CE1 . PHE B 1 240 ? -15.364 -10.823 4.511   1.00 38.59  ? 240 PHE B CE1 1 
ATOM   4243 C CE2 . PHE B 1 240 ? -14.379 -11.927 2.636   1.00 34.32  ? 240 PHE B CE2 1 
ATOM   4244 C CZ  . PHE B 1 240 ? -14.405 -10.869 3.516   1.00 36.19  ? 240 PHE B CZ  1 
ATOM   4245 N N   . SER B 1 241 ? -18.429 -16.909 5.128   1.00 35.93  ? 241 SER B N   1 
ATOM   4246 C CA  . SER B 1 241 ? -19.638 -17.638 5.469   1.00 42.37  ? 241 SER B CA  1 
ATOM   4247 C C   . SER B 1 241 ? -19.580 -18.275 6.848   1.00 44.32  ? 241 SER B C   1 
ATOM   4248 O O   . SER B 1 241 ? -20.598 -18.795 7.315   1.00 47.56  ? 241 SER B O   1 
ATOM   4249 C CB  . SER B 1 241 ? -19.916 -18.695 4.391   1.00 39.23  ? 241 SER B CB  1 
ATOM   4250 O OG  . SER B 1 241 ? -19.465 -19.955 4.813   1.00 48.08  ? 241 SER B OG  1 
ATOM   4251 N N   . TRP B 1 242 ? -18.432 -18.211 7.526   1.00 42.78  ? 242 TRP B N   1 
ATOM   4252 C CA  . TRP B 1 242 ? -18.285 -18.897 8.807   1.00 48.42  ? 242 TRP B CA  1 
ATOM   4253 C C   . TRP B 1 242 ? -19.177 -18.291 9.888   1.00 52.24  ? 242 TRP B C   1 
ATOM   4254 O O   . TRP B 1 242 ? -19.751 -19.023 10.705  1.00 56.69  ? 242 TRP B O   1 
ATOM   4255 C CB  . TRP B 1 242 ? -16.824 -18.873 9.250   1.00 44.12  ? 242 TRP B CB  1 
ATOM   4256 C CG  . TRP B 1 242 ? -16.658 -19.480 10.593  1.00 46.96  ? 242 TRP B CG  1 
ATOM   4257 C CD1 . TRP B 1 242 ? -16.262 -18.858 11.739  1.00 49.04  ? 242 TRP B CD1 1 
ATOM   4258 C CD2 . TRP B 1 242 ? -16.927 -20.836 10.943  1.00 45.85  ? 242 TRP B CD2 1 
ATOM   4259 N NE1 . TRP B 1 242 ? -16.251 -19.755 12.782  1.00 49.97  ? 242 TRP B NE1 1 
ATOM   4260 C CE2 . TRP B 1 242 ? -16.664 -20.975 12.318  1.00 48.50  ? 242 TRP B CE2 1 
ATOM   4261 C CE3 . TRP B 1 242 ? -17.366 -21.950 10.224  1.00 46.02  ? 242 TRP B CE3 1 
ATOM   4262 C CZ2 . TRP B 1 242 ? -16.817 -22.186 12.986  1.00 51.93  ? 242 TRP B CZ2 1 
ATOM   4263 C CZ3 . TRP B 1 242 ? -17.520 -23.142 10.887  1.00 49.31  ? 242 TRP B CZ3 1 
ATOM   4264 C CH2 . TRP B 1 242 ? -17.243 -23.254 12.255  1.00 49.60  ? 242 TRP B CH2 1 
ATOM   4265 N N   . ASN B 1 243 ? -19.303 -16.967 9.918   1.00 52.98  ? 243 ASN B N   1 
ATOM   4266 C CA  . ASN B 1 243 ? -20.156 -16.280 10.896  1.00 58.29  ? 243 ASN B CA  1 
ATOM   4267 C C   . ASN B 1 243 ? -21.579 -16.841 10.916  1.00 60.97  ? 243 ASN B C   1 
ATOM   4268 O O   . ASN B 1 243 ? -21.974 -17.531 11.857  1.00 66.61  ? 243 ASN B O   1 
ATOM   4269 C CB  . ASN B 1 243 ? -20.218 -14.779 10.604  1.00 58.76  ? 243 ASN B CB  1 
ATOM   4270 C CG  . ASN B 1 243 ? -20.310 -14.478 9.121   1.00 59.13  ? 243 ASN B CG  1 
ATOM   4271 O OD1 . ASN B 1 243 ? -21.045 -15.146 8.391   1.00 62.10  ? 243 ASN B OD1 1 
ATOM   4272 N ND2 . ASN B 1 243 ? -19.585 -13.452 8.669   1.00 59.63  ? 243 ASN B ND2 1 
ATOM   4273 N N   . ASN B 1 255 ? -16.579 -26.202 5.220   1.00 43.00  ? 255 ASN B N   1 
ATOM   4274 C CA  . ASN B 1 255 ? -15.941 -24.920 5.504   1.00 37.83  ? 255 ASN B CA  1 
ATOM   4275 C C   . ASN B 1 255 ? -14.509 -25.107 6.011   1.00 34.59  ? 255 ASN B C   1 
ATOM   4276 O O   . ASN B 1 255 ? -14.252 -25.908 6.908   1.00 35.52  ? 255 ASN B O   1 
ATOM   4277 C CB  . ASN B 1 255 ? -16.769 -24.132 6.515   1.00 37.98  ? 255 ASN B CB  1 
ATOM   4278 C CG  . ASN B 1 255 ? -16.356 -22.675 6.592   1.00 37.31  ? 255 ASN B CG  1 
ATOM   4279 O OD1 . ASN B 1 255 ? -15.220 -22.361 6.957   1.00 36.65  ? 255 ASN B OD1 1 
ATOM   4280 N ND2 . ASN B 1 255 ? -17.262 -21.784 6.236   1.00 35.56  ? 255 ASN B ND2 1 
ATOM   4281 N N   . GLY B 1 256 ? -13.576 -24.344 5.433   1.00 33.59  ? 256 GLY B N   1 
ATOM   4282 C CA  . GLY B 1 256 ? -12.176 -24.505 5.783   1.00 33.01  ? 256 GLY B CA  1 
ATOM   4283 C C   . GLY B 1 256 ? -11.878 -24.223 7.244   1.00 33.67  ? 256 GLY B C   1 
ATOM   4284 O O   . GLY B 1 256 ? -10.913 -24.760 7.795   1.00 33.85  ? 256 GLY B O   1 
ATOM   4285 N N   . VAL B 1 257 ? -12.672 -23.379 7.891   1.00 34.17  ? 257 VAL B N   1 
ATOM   4286 C CA  . VAL B 1 257 ? -12.465 -23.138 9.348   1.00 34.09  ? 257 VAL B CA  1 
ATOM   4287 C C   . VAL B 1 257 ? -12.618 -24.466 10.094  1.00 36.76  ? 257 VAL B C   1 
ATOM   4288 O O   . VAL B 1 257 ? -11.768 -24.770 10.932  1.00 35.32  ? 257 VAL B O   1 
ATOM   4289 C CB  . VAL B 1 257 ? -13.421 -22.067 9.896   1.00 37.35  ? 257 VAL B CB  1 
ATOM   4290 C CG1 . VAL B 1 257 ? -13.338 -21.958 11.409  1.00 39.06  ? 257 VAL B CG1 1 
ATOM   4291 C CG2 . VAL B 1 257 ? -13.180 -20.715 9.246   1.00 33.99  ? 257 VAL B CG2 1 
ATOM   4292 N N   . VAL B 1 258 ? -13.660 -25.227 9.754   1.00 36.82  ? 258 VAL B N   1 
ATOM   4293 C CA  . VAL B 1 258 ? -13.869 -26.518 10.417  1.00 37.32  ? 258 VAL B CA  1 
ATOM   4294 C C   . VAL B 1 258 ? -12.723 -27.477 10.131  1.00 38.38  ? 258 VAL B C   1 
ATOM   4295 O O   . VAL B 1 258 ? -12.237 -28.171 11.038  1.00 37.58  ? 258 VAL B O   1 
ATOM   4296 C CB  . VAL B 1 258 ? -15.222 -27.121 9.996   1.00 42.63  ? 258 VAL B CB  1 
ATOM   4297 C CG1 . VAL B 1 258 ? -15.345 -28.559 10.491  1.00 46.01  ? 258 VAL B CG1 1 
ATOM   4298 C CG2 . VAL B 1 258 ? -16.352 -26.271 10.535  1.00 42.79  ? 258 VAL B CG2 1 
ATOM   4299 N N   . VAL B 1 259 ? -12.289 -27.558 8.872   1.00 33.93  ? 259 VAL B N   1 
ATOM   4300 C CA  . VAL B 1 259 ? -11.153 -28.409 8.539   1.00 36.72  ? 259 VAL B CA  1 
ATOM   4301 C C   . VAL B 1 259 ? -9.951  -28.034 9.394   1.00 36.30  ? 259 VAL B C   1 
ATOM   4302 O O   . VAL B 1 259 ? -9.257  -28.901 9.941   1.00 36.77  ? 259 VAL B O   1 
ATOM   4303 C CB  . VAL B 1 259 ? -10.829 -28.304 7.039   1.00 35.36  ? 259 VAL B CB  1 
ATOM   4304 C CG1 . VAL B 1 259 ? -9.650  -29.192 6.681   1.00 37.21  ? 259 VAL B CG1 1 
ATOM   4305 C CG2 . VAL B 1 259 ? -12.055 -28.661 6.196   1.00 34.37  ? 259 VAL B CG2 1 
ATOM   4306 N N   . LEU B 1 260 ? -9.704  -26.735 9.533   1.00 34.84  ? 260 LEU B N   1 
ATOM   4307 C CA  . LEU B 1 260 ? -8.492  -26.292 10.262  1.00 34.34  ? 260 LEU B CA  1 
ATOM   4308 C C   . LEU B 1 260 ? -8.631  -26.588 11.761  1.00 36.35  ? 260 LEU B C   1 
ATOM   4309 O O   . LEU B 1 260 ? -7.630  -27.002 12.348  1.00 37.58  ? 260 LEU B O   1 
ATOM   4310 C CB  . LEU B 1 260 ? -8.269  -24.804 9.979   1.00 32.76  ? 260 LEU B CB  1 
ATOM   4311 C CG  . LEU B 1 260 ? -7.706  -24.490 8.597   1.00 29.93  ? 260 LEU B CG  1 
ATOM   4312 C CD1 . LEU B 1 260 ? -7.738  -22.997 8.328   1.00 32.82  ? 260 LEU B CD1 1 
ATOM   4313 C CD2 . LEU B 1 260 ? -6.293  -25.025 8.461   1.00 32.61  ? 260 LEU B CD2 1 
ATOM   4314 N N   . MET B 1 261 ? -9.810  -26.379 12.350  1.00 37.26  ? 261 MET B N   1 
ATOM   4315 C CA  . MET B 1 261 ? -9.942  -26.764 13.757  1.00 43.17  ? 261 MET B CA  1 
ATOM   4316 C C   . MET B 1 261 ? -9.687  -28.249 13.953  1.00 41.21  ? 261 MET B C   1 
ATOM   4317 O O   . MET B 1 261 ? -9.077  -28.651 14.952  1.00 40.89  ? 261 MET B O   1 
ATOM   4318 C CB  . MET B 1 261 ? -11.304 -26.403 14.371  1.00 40.34  ? 261 MET B CB  1 
ATOM   4319 C CG  . MET B 1 261 ? -11.879 -25.044 14.113  1.00 42.04  ? 261 MET B CG  1 
ATOM   4320 S SD  . MET B 1 261 ? -13.635 -24.996 14.528  1.00 49.23  ? 261 MET B SD  1 
ATOM   4321 C CE  . MET B 1 261 ? -13.602 -25.570 16.228  1.00 48.31  ? 261 MET B CE  1 
ATOM   4322 N N   . LYS B 1 262 ? -10.143 -29.084 13.020  1.00 39.41  ? 262 LYS B N   1 
ATOM   4323 C CA  . LYS B 1 262 ? -9.948  -30.519 13.194  1.00 38.93  ? 262 LYS B CA  1 
ATOM   4324 C C   . LYS B 1 262 ? -8.499  -30.915 12.921  1.00 40.64  ? 262 LYS B C   1 
ATOM   4325 O O   . LYS B 1 262 ? -7.954  -31.795 13.598  1.00 43.91  ? 262 LYS B O   1 
ATOM   4326 C CB  . LYS B 1 262 ? -10.921 -31.298 12.300  1.00 40.53  ? 262 LYS B CB  1 
ATOM   4327 C CG  . LYS B 1 262 ? -12.391 -30.957 12.563  1.00 46.40  ? 262 LYS B CG  1 
ATOM   4328 C CD  . LYS B 1 262 ? -13.361 -32.023 12.034  1.00 48.98  ? 262 LYS B CD  1 
ATOM   4329 C CE  . LYS B 1 262 ? -12.989 -32.511 10.645  1.00 54.09  ? 262 LYS B CE  1 
ATOM   4330 N NZ  . LYS B 1 262 ? -13.761 -31.823 9.551   1.00 56.87  ? 262 LYS B NZ  1 
ATOM   4331 N N   . GLU B 1 263 ? -7.849  -30.257 11.957  1.00 34.88  ? 263 GLU B N   1 
ATOM   4332 C CA  . GLU B 1 263 ? -6.484  -30.626 11.599  1.00 36.69  ? 263 GLU B CA  1 
ATOM   4333 C C   . GLU B 1 263 ? -5.486  -30.210 12.670  1.00 35.99  ? 263 GLU B C   1 
ATOM   4334 O O   . GLU B 1 263 ? -4.543  -30.951 12.969  1.00 39.04  ? 263 GLU B O   1 
ATOM   4335 C CB  . GLU B 1 263 ? -6.090  -30.008 10.262  1.00 37.84  ? 263 GLU B CB  1 
ATOM   4336 C CG  . GLU B 1 263 ? -4.729  -30.481 9.790   1.00 37.33  ? 263 GLU B CG  1 
ATOM   4337 C CD  . GLU B 1 263 ? -4.345  -29.982 8.416   1.00 42.38  ? 263 GLU B CD  1 
ATOM   4338 O OE1 . GLU B 1 263 ? -5.084  -29.136 7.850   1.00 39.58  ? 263 GLU B OE1 1 
ATOM   4339 O OE2 . GLU B 1 263 ? -3.285  -30.421 7.909   1.00 43.48  ? 263 GLU B OE2 1 
ATOM   4340 N N   . HIS B 1 264 ? -5.654  -29.015 13.228  1.00 34.73  ? 264 HIS B N   1 
ATOM   4341 C CA  . HIS B 1 264 ? -4.716  -28.476 14.200  1.00 35.77  ? 264 HIS B CA  1 
ATOM   4342 C C   . HIS B 1 264 ? -5.243  -28.443 15.626  1.00 40.86  ? 264 HIS B C   1 
ATOM   4343 O O   . HIS B 1 264 ? -4.507  -28.015 16.525  1.00 42.79  ? 264 HIS B O   1 
ATOM   4344 C CB  . HIS B 1 264 ? -4.262  -27.076 13.762  1.00 36.04  ? 264 HIS B CB  1 
ATOM   4345 C CG  . HIS B 1 264 ? -3.545  -27.076 12.453  1.00 30.34  ? 264 HIS B CG  1 
ATOM   4346 N ND1 . HIS B 1 264 ? -4.160  -26.793 11.250  1.00 38.39  ? 264 HIS B ND1 1 
ATOM   4347 C CD2 . HIS B 1 264 ? -2.271  -27.417 12.151  1.00 33.45  ? 264 HIS B CD2 1 
ATOM   4348 C CE1 . HIS B 1 264 ? -3.278  -26.912 10.272  1.00 32.96  ? 264 HIS B CE1 1 
ATOM   4349 N NE2 . HIS B 1 264 ? -2.124  -27.284 10.793  1.00 40.09  ? 264 HIS B NE2 1 
ATOM   4350 N N   . HIS B 1 265 ? -6.478  -28.894 15.862  1.00 42.76  ? 265 HIS B N   1 
ATOM   4351 C CA  . HIS B 1 265 ? -7.056  -28.993 17.204  1.00 45.33  ? 265 HIS B CA  1 
ATOM   4352 C C   . HIS B 1 265 ? -7.036  -27.636 17.913  1.00 45.17  ? 265 HIS B C   1 
ATOM   4353 O O   . HIS B 1 265 ? -6.474  -27.480 18.998  1.00 43.24  ? 265 HIS B O   1 
ATOM   4354 C CB  . HIS B 1 265 ? -6.322  -30.053 18.032  1.00 42.98  ? 265 HIS B CB  1 
ATOM   4355 C CG  . HIS B 1 265 ? -6.111  -31.350 17.310  1.00 47.42  ? 265 HIS B CG  1 
ATOM   4356 N ND1 . HIS B 1 265 ? -7.146  -32.199 16.978  1.00 52.59  ? 265 HIS B ND1 1 
ATOM   4357 C CD2 . HIS B 1 265 ? -4.982  -31.934 16.842  1.00 48.66  ? 265 HIS B CD2 1 
ATOM   4358 C CE1 . HIS B 1 265 ? -6.662  -33.256 16.350  1.00 52.27  ? 265 HIS B CE1 1 
ATOM   4359 N NE2 . HIS B 1 265 ? -5.351  -33.120 16.253  1.00 53.75  ? 265 HIS B NE2 1 
ATOM   4360 N N   . THR B 1 266 ? -7.646  -26.646 17.267  1.00 41.06  ? 266 THR B N   1 
ATOM   4361 C CA  . THR B 1 266 ? -7.682  -25.276 17.756  1.00 40.52  ? 266 THR B CA  1 
ATOM   4362 C C   . THR B 1 266 ? -9.121  -24.810 17.914  1.00 42.20  ? 266 THR B C   1 
ATOM   4363 O O   . THR B 1 266 ? -10.070 -25.487 17.514  1.00 42.50  ? 266 THR B O   1 
ATOM   4364 C CB  . THR B 1 266 ? -6.939  -24.324 16.808  1.00 40.51  ? 266 THR B CB  1 
ATOM   4365 O OG1 . THR B 1 266 ? -7.768  -24.089 15.659  1.00 40.37  ? 266 THR B OG1 1 
ATOM   4366 C CG2 . THR B 1 266 ? -5.607  -24.897 16.378  1.00 40.02  ? 266 THR B CG2 1 
ATOM   4367 N N   . THR B 1 267 ? -9.277  -23.622 18.492  1.00 41.64  ? 267 THR B N   1 
ATOM   4368 C CA  . THR B 1 267 ? -10.590 -23.005 18.541  1.00 41.50  ? 267 THR B CA  1 
ATOM   4369 C C   . THR B 1 267 ? -11.003 -22.522 17.149  1.00 44.33  ? 267 THR B C   1 
ATOM   4370 O O   . THR B 1 267 ? -10.191 -22.433 16.221  1.00 41.15  ? 267 THR B O   1 
ATOM   4371 C CB  . THR B 1 267 ? -10.603 -21.823 19.497  1.00 43.13  ? 267 THR B CB  1 
ATOM   4372 O OG1 . THR B 1 267 ? -9.635  -20.859 19.063  1.00 43.83  ? 267 THR B OG1 1 
ATOM   4373 C CG2 . THR B 1 267 ? -10.265 -22.283 20.905  1.00 47.04  ? 267 THR B CG2 1 
ATOM   4374 N N   . ALA B 1 268 ? -12.291 -22.196 17.024  1.00 43.35  ? 268 ALA B N   1 
ATOM   4375 C CA  . ALA B 1 268 ? -12.803 -21.640 15.775  1.00 42.46  ? 268 ALA B CA  1 
ATOM   4376 C C   . ALA B 1 268 ? -12.150 -20.303 15.461  1.00 43.17  ? 268 ALA B C   1 
ATOM   4377 O O   . ALA B 1 268 ? -11.843 -20.012 14.297  1.00 40.87  ? 268 ALA B O   1 
ATOM   4378 C CB  . ALA B 1 268 ? -14.321 -21.479 15.849  1.00 44.38  ? 268 ALA B CB  1 
ATOM   4379 N N   . ASP B 1 269 ? -11.948 -19.466 16.484  1.00 40.71  ? 269 ASP B N   1 
ATOM   4380 C CA  . ASP B 1 269 ? -11.351 -18.156 16.252  1.00 44.20  ? 269 ASP B CA  1 
ATOM   4381 C C   . ASP B 1 269 ? -9.928  -18.302 15.741  1.00 40.57  ? 269 ASP B C   1 
ATOM   4382 O O   . ASP B 1 269 ? -9.499  -17.563 14.849  1.00 36.98  ? 269 ASP B O   1 
ATOM   4383 C CB  . ASP B 1 269 ? -11.365 -17.333 17.540  1.00 46.50  ? 269 ASP B CB  1 
ATOM   4384 C CG  . ASP B 1 269 ? -12.678 -16.624 17.769  1.00 51.96  ? 269 ASP B CG  1 
ATOM   4385 O OD1 . ASP B 1 269 ? -13.530 -16.618 16.859  1.00 55.71  ? 269 ASP B OD1 1 
ATOM   4386 O OD2 . ASP B 1 269 ? -12.856 -16.064 18.872  1.00 58.41  ? 269 ASP B OD2 1 
ATOM   4387 N N   . ALA B 1 270 ? -9.181  -19.252 16.301  1.00 39.41  ? 270 ALA B N   1 
ATOM   4388 C CA  . ALA B 1 270 ? -7.819  -19.497 15.843  1.00 40.41  ? 270 ALA B CA  1 
ATOM   4389 C C   . ALA B 1 270 ? -7.808  -20.034 14.414  1.00 37.89  ? 270 ALA B C   1 
ATOM   4390 O O   . ALA B 1 270 ? -7.013  -19.584 13.581  1.00 32.60  ? 270 ALA B O   1 
ATOM   4391 C CB  . ALA B 1 270 ? -7.114  -20.463 16.797  1.00 39.32  ? 270 ALA B CB  1 
ATOM   4392 N N   . ALA B 1 271 ? -8.692  -20.993 14.111  1.00 34.82  ? 271 ALA B N   1 
ATOM   4393 C CA  . ALA B 1 271 ? -8.750  -21.537 12.755  1.00 34.41  ? 271 ALA B CA  1 
ATOM   4394 C C   . ALA B 1 271 ? -9.204  -20.496 11.742  1.00 31.60  ? 271 ALA B C   1 
ATOM   4395 O O   . ALA B 1 271 ? -8.755  -20.520 10.587  1.00 33.29  ? 271 ALA B O   1 
ATOM   4396 C CB  . ALA B 1 271 ? -9.682  -22.747 12.698  1.00 33.77  ? 271 ALA B CB  1 
ATOM   4397 N N   . LYS B 1 272 ? -10.099 -19.589 12.138  1.00 33.31  ? 272 LYS B N   1 
ATOM   4398 C CA  . LYS B 1 272 ? -10.510 -18.538 11.214  1.00 34.24  ? 272 LYS B CA  1 
ATOM   4399 C C   . LYS B 1 272 ? -9.346  -17.606 10.902  1.00 34.49  ? 272 LYS B C   1 
ATOM   4400 O O   . LYS B 1 272 ? -9.174  -17.170 9.760   1.00 30.24  ? 272 LYS B O   1 
ATOM   4401 C CB  . LYS B 1 272 ? -11.694 -17.759 11.789  1.00 38.94  ? 272 LYS B CB  1 
ATOM   4402 C CG  . LYS B 1 272 ? -12.226 -16.716 10.831  1.00 43.43  ? 272 LYS B CG  1 
ATOM   4403 C CD  . LYS B 1 272 ? -13.264 -15.793 11.458  1.00 46.94  ? 272 LYS B CD  1 
ATOM   4404 C CE  . LYS B 1 272 ? -14.299 -15.376 10.425  1.00 45.51  ? 272 LYS B CE  1 
ATOM   4405 N NZ  . LYS B 1 272 ? -15.419 -14.583 11.004  1.00 51.49  ? 272 LYS B NZ  1 
ATOM   4406 N N   . MET B 1 273 ? -8.503  -17.316 11.894  1.00 29.51  ? 273 MET B N   1 
ATOM   4407 C CA  . MET B 1 273 ? -7.334  -16.510 11.585  1.00 28.73  ? 273 MET B CA  1 
ATOM   4408 C C   . MET B 1 273 ? -6.361  -17.281 10.705  1.00 28.36  ? 273 MET B C   1 
ATOM   4409 O O   . MET B 1 273 ? -5.759  -16.702 9.794   1.00 29.54  ? 273 MET B O   1 
ATOM   4410 C CB  . MET B 1 273 ? -6.660  -16.030 12.876  1.00 29.74  ? 273 MET B CB  1 
ATOM   4411 C CG  . MET B 1 273 ? -7.482  -14.958 13.562  1.00 33.52  ? 273 MET B CG  1 
ATOM   4412 S SD  . MET B 1 273 ? -7.531  -13.418 12.632  1.00 37.47  ? 273 MET B SD  1 
ATOM   4413 C CE  . MET B 1 273 ? -9.160  -13.537 11.870  1.00 40.64  ? 273 MET B CE  1 
ATOM   4414 N N   . MET B 1 274 ? -6.226  -18.580 10.943  1.00 26.70  ? 274 MET B N   1 
ATOM   4415 C CA  . MET B 1 274 ? -5.353  -19.416 10.081  1.00 27.18  ? 274 MET B CA  1 
ATOM   4416 C C   . MET B 1 274 ? -5.884  -19.422 8.638   1.00 29.07  ? 274 MET B C   1 
ATOM   4417 O O   . MET B 1 274 ? -5.073  -19.328 7.716   1.00 29.21  ? 274 MET B O   1 
ATOM   4418 C CB  . MET B 1 274 ? -5.297  -20.848 10.616  1.00 30.76  ? 274 MET B CB  1 
ATOM   4419 C CG  . MET B 1 274 ? -3.955  -21.515 10.491  1.00 37.80  ? 274 MET B CG  1 
ATOM   4420 S SD  . MET B 1 274 ? -4.039  -23.189 11.171  1.00 45.09  ? 274 MET B SD  1 
ATOM   4421 C CE  . MET B 1 274 ? -4.667  -22.845 12.811  1.00 33.46  ? 274 MET B CE  1 
ATOM   4422 N N   . LEU B 1 275 ? -7.202  -19.515 8.469   1.00 29.76  ? 275 LEU B N   1 
ATOM   4423 C CA  . LEU B 1 275 ? -7.779  -19.525 7.129   1.00 25.95  ? 275 LEU B CA  1 
ATOM   4424 C C   . LEU B 1 275 ? -7.471  -18.226 6.398   1.00 26.76  ? 275 LEU B C   1 
ATOM   4425 O O   . LEU B 1 275 ? -7.116  -18.231 5.216   1.00 29.25  ? 275 LEU B O   1 
ATOM   4426 C CB  . LEU B 1 275 ? -9.288  -19.716 7.211   1.00 27.67  ? 275 LEU B CB  1 
ATOM   4427 C CG  . LEU B 1 275 ? -9.985  -19.845 5.854   1.00 27.32  ? 275 LEU B CG  1 
ATOM   4428 C CD1 . LEU B 1 275 ? -9.361  -20.969 5.021   1.00 33.21  ? 275 LEU B CD1 1 
ATOM   4429 C CD2 . LEU B 1 275 ? -11.470 -20.039 6.039   1.00 29.36  ? 275 LEU B CD2 1 
ATOM   4430 N N   . LEU B 1 276 ? -7.647  -17.092 7.082   1.00 27.14  ? 276 LEU B N   1 
ATOM   4431 C CA  . LEU B 1 276 ? -7.347  -15.810 6.457   1.00 24.84  ? 276 LEU B CA  1 
ATOM   4432 C C   . LEU B 1 276 ? -5.889  -15.754 6.016   1.00 26.90  ? 276 LEU B C   1 
ATOM   4433 O O   . LEU B 1 276 ? -5.585  -15.281 4.919   1.00 27.37  ? 276 LEU B O   1 
ATOM   4434 C CB  . LEU B 1 276 ? -7.672  -14.676 7.434   1.00 27.25  ? 276 LEU B CB  1 
ATOM   4435 C CG  . LEU B 1 276 ? -7.489  -13.246 6.925   1.00 26.40  ? 276 LEU B CG  1 
ATOM   4436 C CD1 . LEU B 1 276 ? -8.369  -13.055 5.670   1.00 25.85  ? 276 LEU B CD1 1 
ATOM   4437 C CD2 . LEU B 1 276 ? -7.857  -12.238 7.984   1.00 28.83  ? 276 LEU B CD2 1 
ATOM   4438 N N   . GLY B 1 277 ? -4.960  -16.206 6.874   1.00 26.38  ? 277 GLY B N   1 
ATOM   4439 C CA  . GLY B 1 277 ? -3.568  -16.288 6.452   1.00 29.04  ? 277 GLY B CA  1 
ATOM   4440 C C   . GLY B 1 277 ? -3.379  -17.161 5.218   1.00 29.01  ? 277 GLY B C   1 
ATOM   4441 O O   . GLY B 1 277 ? -2.647  -16.800 4.295   1.00 27.94  ? 277 GLY B O   1 
ATOM   4442 N N   . VAL B 1 278 ? -4.028  -18.326 5.188   1.00 26.64  ? 278 VAL B N   1 
ATOM   4443 C CA  . VAL B 1 278 ? -3.897  -19.203 4.022   1.00 27.18  ? 278 VAL B CA  1 
ATOM   4444 C C   . VAL B 1 278 ? -4.378  -18.491 2.763   1.00 26.29  ? 278 VAL B C   1 
ATOM   4445 O O   . VAL B 1 278 ? -3.724  -18.548 1.714   1.00 28.42  ? 278 VAL B O   1 
ATOM   4446 C CB  . VAL B 1 278 ? -4.653  -20.522 4.265   1.00 27.37  ? 278 VAL B CB  1 
ATOM   4447 C CG1 . VAL B 1 278 ? -4.764  -21.336 2.978   1.00 27.63  ? 278 VAL B CG1 1 
ATOM   4448 C CG2 . VAL B 1 278 ? -3.961  -21.337 5.353   1.00 29.69  ? 278 VAL B CG2 1 
ATOM   4449 N N   . ILE B 1 279 ? -5.503  -17.773 2.860   1.00 27.28  ? 279 ILE B N   1 
ATOM   4450 C CA  . ILE B 1 279 ? -6.031  -17.027 1.713   1.00 26.38  ? 279 ILE B CA  1 
ATOM   4451 C C   . ILE B 1 279 ? -5.032  -15.981 1.239   1.00 28.22  ? 279 ILE B C   1 
ATOM   4452 O O   . ILE B 1 279 ? -4.732  -15.877 0.045   1.00 27.71  ? 279 ILE B O   1 
ATOM   4453 C CB  . ILE B 1 279 ? -7.382  -16.372 2.063   1.00 26.46  ? 279 ILE B CB  1 
ATOM   4454 C CG1 . ILE B 1 279 ? -8.437  -17.432 2.373   1.00 29.19  ? 279 ILE B CG1 1 
ATOM   4455 C CG2 . ILE B 1 279 ? -7.857  -15.447 0.928   1.00 27.15  ? 279 ILE B CG2 1 
ATOM   4456 C CD1 . ILE B 1 279 ? -9.614  -16.875 3.164   1.00 26.77  ? 279 ILE B CD1 1 
ATOM   4457 N N   . VAL B 1 280 ? -4.517  -15.169 2.168   1.00 26.12  ? 280 VAL B N   1 
ATOM   4458 C CA  . VAL B 1 280 ? -3.600  -14.100 1.780   1.00 27.90  ? 280 VAL B CA  1 
ATOM   4459 C C   . VAL B 1 280 ? -2.335  -14.677 1.157   1.00 27.87  ? 280 VAL B C   1 
ATOM   4460 O O   . VAL B 1 280 ? -1.814  -14.146 0.172   1.00 28.17  ? 280 VAL B O   1 
ATOM   4461 C CB  . VAL B 1 280 ? -3.291  -13.210 2.999   1.00 29.30  ? 280 VAL B CB  1 
ATOM   4462 C CG1 . VAL B 1 280 ? -2.248  -12.155 2.658   1.00 28.98  ? 280 VAL B CG1 1 
ATOM   4463 C CG2 . VAL B 1 280 ? -4.583  -12.558 3.466   1.00 29.51  ? 280 VAL B CG2 1 
ATOM   4464 N N   . GLU B 1 281 ? -1.817  -15.765 1.731   1.00 28.96  ? 281 GLU B N   1 
ATOM   4465 C CA  . GLU B 1 281 ? -0.659  -16.443 1.151   1.00 27.89  ? 281 GLU B CA  1 
ATOM   4466 C C   . GLU B 1 281 ? -0.968  -16.942 -0.261  1.00 29.53  ? 281 GLU B C   1 
ATOM   4467 O O   . GLU B 1 281 ? -0.115  -16.873 -1.158  1.00 30.03  ? 281 GLU B O   1 
ATOM   4468 C CB  . GLU B 1 281 ? -0.272  -17.617 2.039   1.00 31.15  ? 281 GLU B CB  1 
ATOM   4469 C CG  . GLU B 1 281 ? 0.576   -18.656 1.345   1.00 39.31  ? 281 GLU B CG  1 
ATOM   4470 C CD  . GLU B 1 281 ? 0.211   -20.047 1.826   1.00 47.73  ? 281 GLU B CD  1 
ATOM   4471 O OE1 . GLU B 1 281 ? -0.891  -20.541 1.408   1.00 43.40  ? 281 GLU B OE1 1 
ATOM   4472 O OE2 . GLU B 1 281 ? 0.960   -20.621 2.642   1.00 49.09  ? 281 GLU B OE2 1 
ATOM   4473 N N   . GLN B 1 282 ? -2.190  -17.439 -0.483  1.00 27.67  ? 282 GLN B N   1 
ATOM   4474 C CA  . GLN B 1 282 ? -2.556  -17.909 -1.823  1.00 26.68  ? 282 GLN B CA  1 
ATOM   4475 C C   . GLN B 1 282 ? -2.666  -16.748 -2.811  1.00 27.34  ? 282 GLN B C   1 
ATOM   4476 O O   . GLN B 1 282 ? -2.288  -16.882 -3.983  1.00 27.65  ? 282 GLN B O   1 
ATOM   4477 C CB  . GLN B 1 282 ? -3.874  -18.700 -1.779  1.00 28.34  ? 282 GLN B CB  1 
ATOM   4478 C CG  . GLN B 1 282 ? -3.763  -20.122 -1.232  1.00 29.66  ? 282 GLN B CG  1 
ATOM   4479 C CD  . GLN B 1 282 ? -2.776  -20.985 -2.003  1.00 31.44  ? 282 GLN B CD  1 
ATOM   4480 O OE1 . GLN B 1 282 ? -2.998  -21.308 -3.172  1.00 28.72  ? 282 GLN B OE1 1 
ATOM   4481 N NE2 . GLN B 1 282 ? -1.692  -21.392 -1.334  1.00 29.33  ? 282 GLN B NE2 1 
ATOM   4482 N N   . GLU B 1 283 ? -3.171  -15.597 -2.356  1.00 25.75  ? 283 GLU B N   1 
ATOM   4483 C CA  . GLU B 1 283 ? -3.171  -14.414 -3.214  1.00 26.79  ? 283 GLU B CA  1 
ATOM   4484 C C   . GLU B 1 283 ? -1.745  -14.026 -3.589  1.00 28.50  ? 283 GLU B C   1 
ATOM   4485 O O   . GLU B 1 283 ? -1.474  -13.692 -4.742  1.00 28.71  ? 283 GLU B O   1 
ATOM   4486 C CB  . GLU B 1 283 ? -3.889  -13.252 -2.519  1.00 26.62  ? 283 GLU B CB  1 
ATOM   4487 C CG  . GLU B 1 283 ? -5.408  -13.405 -2.438  1.00 29.72  ? 283 GLU B CG  1 
ATOM   4488 C CD  . GLU B 1 283 ? -6.163  -12.083 -2.314  1.00 29.26  ? 283 GLU B CD  1 
ATOM   4489 O OE1 . GLU B 1 283 ? -5.542  -11.047 -1.969  1.00 29.79  ? 283 GLU B OE1 1 
ATOM   4490 O OE2 . GLU B 1 283 ? -7.394  -12.086 -2.561  1.00 29.63  ? 283 GLU B OE2 1 
ATOM   4491 N N   . SER B 1 284 ? -0.806  -14.061 -2.624  1.00 26.42  ? 284 SER B N   1 
ATOM   4492 C CA  . SER B 1 284 ? 0.584   -13.753 -2.963  1.00 27.63  ? 284 SER B CA  1 
ATOM   4493 C C   . SER B 1 284 ? 1.186   -14.807 -3.873  1.00 25.36  ? 284 SER B C   1 
ATOM   4494 O O   . SER B 1 284 ? 1.995   -14.483 -4.749  1.00 29.31  ? 284 SER B O   1 
ATOM   4495 C CB  . SER B 1 284 ? 1.465   -13.636 -1.699  1.00 30.72  ? 284 SER B CB  1 
ATOM   4496 O OG  . SER B 1 284 ? 0.867   -12.786 -0.741  1.00 39.83  ? 284 SER B OG  1 
ATOM   4497 N N   . LEU B 1 285 ? 0.847   -16.077 -3.646  1.00 27.38  ? 285 LEU B N   1 
ATOM   4498 C CA  . LEU B 1 285 ? 1.376   -17.144 -4.484  1.00 28.86  ? 285 LEU B CA  1 
ATOM   4499 C C   . LEU B 1 285 ? 0.919   -16.971 -5.928  1.00 27.62  ? 285 LEU B C   1 
ATOM   4500 O O   . LEU B 1 285 ? 1.722   -17.084 -6.863  1.00 27.12  ? 285 LEU B O   1 
ATOM   4501 C CB  . LEU B 1 285 ? 0.933   -18.500 -3.936  1.00 27.49  ? 285 LEU B CB  1 
ATOM   4502 C CG  . LEU B 1 285 ? 1.251   -19.697 -4.831  1.00 30.52  ? 285 LEU B CG  1 
ATOM   4503 C CD1 . LEU B 1 285 ? 2.759   -19.777 -5.100  1.00 34.10  ? 285 LEU B CD1 1 
ATOM   4504 C CD2 . LEU B 1 285 ? 0.713   -20.999 -4.232  1.00 32.38  ? 285 LEU B CD2 1 
ATOM   4505 N N   . ALA B 1 286 ? -0.362  -16.660 -6.126  1.00 28.89  ? 286 ALA B N   1 
ATOM   4506 C CA  . ALA B 1 286 ? -0.832  -16.329 -7.470  1.00 26.66  ? 286 ALA B CA  1 
ATOM   4507 C C   . ALA B 1 286 ? -0.005  -15.197 -8.077  1.00 28.03  ? 286 ALA B C   1 
ATOM   4508 O O   . ALA B 1 286 ? 0.460   -15.294 -9.215  1.00 28.36  ? 286 ALA B O   1 
ATOM   4509 C CB  . ALA B 1 286 ? -2.319  -15.962 -7.435  1.00 29.23  ? 286 ALA B CB  1 
ATOM   4510 N N   . ALA B 1 287 ? 0.203   -14.114 -7.322  1.00 26.33  ? 287 ALA B N   1 
ATOM   4511 C CA  . ALA B 1 287 ? 1.004   -13.009 -7.840  1.00 27.95  ? 287 ALA B CA  1 
ATOM   4512 C C   . ALA B 1 287 ? 2.417   -13.462 -8.202  1.00 29.04  ? 287 ALA B C   1 
ATOM   4513 O O   . ALA B 1 287 ? 2.978   -13.014 -9.210  1.00 30.04  ? 287 ALA B O   1 
ATOM   4514 C CB  . ALA B 1 287 ? 1.046   -11.873 -6.819  1.00 29.54  ? 287 ALA B CB  1 
ATOM   4515 N N   . LYS B 1 288 ? 3.016   -14.334 -7.381  1.00 28.78  ? 288 LYS B N   1 
ATOM   4516 C CA  . LYS B 1 288 ? 4.342   -14.866 -7.690  1.00 29.25  ? 288 LYS B CA  1 
ATOM   4517 C C   . LYS B 1 288 ? 4.322   -15.669 -8.981  1.00 33.17  ? 288 LYS B C   1 
ATOM   4518 O O   . LYS B 1 288 ? 5.203   -15.519 -9.836  1.00 32.13  ? 288 LYS B O   1 
ATOM   4519 C CB  . LYS B 1 288 ? 4.822   -15.747 -6.541  1.00 31.75  ? 288 LYS B CB  1 
ATOM   4520 C CG  . LYS B 1 288 ? 6.270   -16.170 -6.630  1.00 44.18  ? 288 LYS B CG  1 
ATOM   4521 C CD  . LYS B 1 288 ? 6.697   -16.927 -5.369  1.00 46.69  ? 288 LYS B CD  1 
ATOM   4522 C CE  . LYS B 1 288 ? 5.842   -16.517 -4.155  1.00 49.73  ? 288 LYS B CE  1 
ATOM   4523 N NZ  . LYS B 1 288 ? 6.601   -16.547 -2.865  1.00 56.28  ? 288 LYS B NZ  1 
ATOM   4524 N N   . LEU B 1 289 ? 3.321   -16.531 -9.128  1.00 30.00  ? 289 LEU B N   1 
ATOM   4525 C CA  . LEU B 1 289 ? 3.234   -17.388 -10.303 1.00 29.84  ? 289 LEU B CA  1 
ATOM   4526 C C   . LEU B 1 289 ? 2.976   -16.573 -11.563 1.00 33.39  ? 289 LEU B C   1 
ATOM   4527 O O   . LEU B 1 289 ? 3.543   -16.866 -12.625 1.00 32.44  ? 289 LEU B O   1 
ATOM   4528 C CB  . LEU B 1 289 ? 2.153   -18.437 -10.077 1.00 28.33  ? 289 LEU B CB  1 
ATOM   4529 C CG  . LEU B 1 289 ? 2.563   -19.439 -8.990  1.00 30.10  ? 289 LEU B CG  1 
ATOM   4530 C CD1 . LEU B 1 289 ? 1.365   -20.268 -8.515  1.00 28.01  ? 289 LEU B CD1 1 
ATOM   4531 C CD2 . LEU B 1 289 ? 3.659   -20.365 -9.501  1.00 33.31  ? 289 LEU B CD2 1 
ATOM   4532 N N   . LYS B 1 290 ? 2.149   -15.525 -11.462 1.00 30.76  ? 290 LYS B N   1 
ATOM   4533 C CA  . LYS B 1 290 ? 1.963   -14.629 -12.600 1.00 30.24  ? 290 LYS B CA  1 
ATOM   4534 C C   . LYS B 1 290 ? 3.262   -13.927 -12.959 1.00 34.70  ? 290 LYS B C   1 
ATOM   4535 O O   . LYS B 1 290 ? 3.609   -13.811 -14.143 1.00 33.40  ? 290 LYS B O   1 
ATOM   4536 C CB  . LYS B 1 290 ? 0.861   -13.611 -12.306 1.00 29.21  ? 290 LYS B CB  1 
ATOM   4537 C CG  . LYS B 1 290 ? 0.595   -12.668 -13.468 1.00 34.14  ? 290 LYS B CG  1 
ATOM   4538 C CD  . LYS B 1 290 ? 0.179   -11.310 -12.964 1.00 37.53  ? 290 LYS B CD  1 
ATOM   4539 C CE  . LYS B 1 290 ? -1.071  -10.814 -13.611 1.00 41.11  ? 290 LYS B CE  1 
ATOM   4540 N NZ  . LYS B 1 290 ? -1.316  -9.387  -13.290 1.00 36.14  ? 290 LYS B NZ  1 
ATOM   4541 N N   . GLU B 1 291 ? 4.009   -13.470 -11.945 1.00 34.01  ? 291 GLU B N   1 
ATOM   4542 C CA  . GLU B 1 291 ? 5.265   -12.788 -12.226 1.00 34.33  ? 291 GLU B CA  1 
ATOM   4543 C C   . GLU B 1 291 ? 6.244   -13.736 -12.901 1.00 34.92  ? 291 GLU B C   1 
ATOM   4544 O O   . GLU B 1 291 ? 6.962   -13.332 -13.822 1.00 39.11  ? 291 GLU B O   1 
ATOM   4545 C CB  . GLU B 1 291 ? 5.867   -12.224 -10.936 1.00 34.96  ? 291 GLU B CB  1 
ATOM   4546 C CG  . GLU B 1 291 ? 7.152   -11.442 -11.154 1.00 37.96  ? 291 GLU B CG  1 
ATOM   4547 C CD  . GLU B 1 291 ? 7.780   -10.954 -9.857  1.00 42.63  ? 291 GLU B CD  1 
ATOM   4548 O OE1 . GLU B 1 291 ? 7.806   -11.708 -8.865  1.00 46.09  ? 291 GLU B OE1 1 
ATOM   4549 O OE2 . GLU B 1 291 ? 8.172   -9.776  -9.813  1.00 52.31  ? 291 GLU B OE2 1 
ATOM   4550 N N   . GLU B 1 292 ? 6.244   -14.996 -12.481 1.00 33.14  ? 292 GLU B N   1 
ATOM   4551 C CA  . GLU B 1 292 ? 7.122   -16.006 -13.122 1.00 36.08  ? 292 GLU B CA  1 
ATOM   4552 C C   . GLU B 1 292 ? 6.700   -16.209 -14.583 1.00 38.06  ? 292 GLU B C   1 
ATOM   4553 O O   . GLU B 1 292 ? 7.573   -16.195 -15.450 1.00 38.85  ? 292 GLU B O   1 
ATOM   4554 C CB  . GLU B 1 292 ? 7.083   -17.325 -12.354 1.00 37.32  ? 292 GLU B CB  1 
ATOM   4555 C CG  . GLU B 1 292 ? 7.777   -17.261 -11.006 1.00 42.78  ? 292 GLU B CG  1 
ATOM   4556 C CD  . GLU B 1 292 ? 7.606   -18.489 -10.129 1.00 48.56  ? 292 GLU B CD  1 
ATOM   4557 O OE1 . GLU B 1 292 ? 7.170   -19.528 -10.650 1.00 51.60  ? 292 GLU B OE1 1 
ATOM   4558 O OE2 . GLU B 1 292 ? 7.915   -18.404 -8.926  1.00 54.51  ? 292 GLU B OE2 1 
ATOM   4559 N N   . ARG B 1 293 ? 5.406   -16.395 -14.826 1.00 33.34  ? 293 ARG B N   1 
ATOM   4560 C CA  . ARG B 1 293 ? 4.943   -16.582 -16.200 1.00 36.13  ? 293 ARG B CA  1 
ATOM   4561 C C   . ARG B 1 293 ? 5.362   -15.420 -17.085 1.00 37.78  ? 293 ARG B C   1 
ATOM   4562 O O   . ARG B 1 293 ? 5.781   -15.624 -18.231 1.00 40.03  ? 293 ARG B O   1 
ATOM   4563 C CB  . ARG B 1 293 ? 3.424   -16.730 -16.245 1.00 33.85  ? 293 ARG B CB  1 
ATOM   4564 C CG  . ARG B 1 293 ? 2.856   -16.973 -17.659 1.00 34.46  ? 293 ARG B CG  1 
ATOM   4565 C CD  . ARG B 1 293 ? 3.561   -18.127 -18.390 1.00 36.30  ? 293 ARG B CD  1 
ATOM   4566 N NE  . ARG B 1 293 ? 3.109   -18.259 -19.774 1.00 40.97  ? 293 ARG B NE  1 
ATOM   4567 C CZ  . ARG B 1 293 ? 3.507   -17.482 -20.772 1.00 38.28  ? 293 ARG B CZ  1 
ATOM   4568 N NH1 . ARG B 1 293 ? 4.442   -16.563 -20.598 1.00 39.77  ? 293 ARG B NH1 1 
ATOM   4569 N NH2 . ARG B 1 293 ? 2.981   -17.654 -21.982 1.00 41.19  ? 293 ARG B NH2 1 
ATOM   4570 N N   . LEU B 1 294 ? 5.259   -14.192 -16.571 1.00 34.36  ? 294 LEU B N   1 
ATOM   4571 C CA  . LEU B 1 294 ? 5.527   -13.019 -17.391 1.00 37.31  ? 294 LEU B CA  1 
ATOM   4572 C C   . LEU B 1 294 ? 7.009   -12.797 -17.648 1.00 39.27  ? 294 LEU B C   1 
ATOM   4573 O O   . LEU B 1 294 ? 7.357   -11.834 -18.345 1.00 41.39  ? 294 LEU B O   1 
ATOM   4574 C CB  . LEU B 1 294 ? 4.904   -11.779 -16.754 1.00 39.62  ? 294 LEU B CB  1 
ATOM   4575 C CG  . LEU B 1 294 ? 3.374   -11.822 -16.811 1.00 39.91  ? 294 LEU B CG  1 
ATOM   4576 C CD1 . LEU B 1 294 ? 2.750   -10.668 -16.022 1.00 40.19  ? 294 LEU B CD1 1 
ATOM   4577 C CD2 . LEU B 1 294 ? 2.877   -11.863 -18.270 1.00 40.71  ? 294 LEU B CD2 1 
ATOM   4578 N N   . LYS B 1 295 ? 7.880   -13.656 -17.129 1.00 41.15  ? 295 LYS B N   1 
ATOM   4579 C CA  . LYS B 1 295 ? 9.284   -13.617 -17.514 1.00 44.32  ? 295 LYS B CA  1 
ATOM   4580 C C   . LYS B 1 295 ? 9.504   -14.177 -18.918 1.00 45.83  ? 295 LYS B C   1 
ATOM   4581 O O   . LYS B 1 295 ? 10.528  -13.879 -19.542 1.00 47.64  ? 295 LYS B O   1 
ATOM   4582 C CB  . LYS B 1 295 ? 10.118  -14.386 -16.487 1.00 45.09  ? 295 LYS B CB  1 
ATOM   4583 C CG  . LYS B 1 295 ? 10.101  -13.750 -15.085 1.00 47.12  ? 295 LYS B CG  1 
ATOM   4584 C CD  . LYS B 1 295 ? 10.408  -12.249 -15.122 1.00 52.99  ? 295 LYS B CD  1 
ATOM   4585 C CE  . LYS B 1 295 ? 9.477   -11.384 -14.220 1.00 54.68  ? 295 LYS B CE  1 
ATOM   4586 N NZ  . LYS B 1 295 ? 8.079   -11.100 -14.753 1.00 38.91  ? 295 LYS B NZ  1 
ATOM   4587 N N   . LYS B 1 296 ? 8.561   -14.956 -19.433 1.00 46.37  ? 296 LYS B N   1 
ATOM   4588 C CA  . LYS B 1 296 ? 8.574   -15.441 -20.805 1.00 44.74  ? 296 LYS B CA  1 
ATOM   4589 C C   . LYS B 1 296 ? 7.492   -14.752 -21.633 1.00 46.67  ? 296 LYS B C   1 
ATOM   4590 O O   . LYS B 1 296 ? 6.543   -14.182 -21.082 1.00 44.46  ? 296 LYS B O   1 
ATOM   4591 C CB  . LYS B 1 296 ? 8.387   -16.966 -20.846 1.00 46.03  ? 296 LYS B CB  1 
ATOM   4592 C CG  . LYS B 1 296 ? 9.510   -17.739 -20.157 1.00 50.64  ? 296 LYS B CG  1 
ATOM   4593 C CD  . LYS B 1 296 ? 9.320   -19.249 -20.246 1.00 52.74  ? 296 LYS B CD  1 
ATOM   4594 C CE  . LYS B 1 296 ? 10.424  -19.992 -19.482 1.00 54.55  ? 296 LYS B CE  1 
ATOM   4595 N NZ  . LYS B 1 296 ? 10.211  -21.477 -19.461 1.00 58.72  ? 296 LYS B NZ  1 
ATOM   4596 N N   . PRO B 1 297 ? 7.621   -14.754 -22.963 1.00 47.01  ? 297 PRO B N   1 
ATOM   4597 C CA  . PRO B 1 297 ? 6.602   -14.109 -23.804 1.00 48.41  ? 297 PRO B CA  1 
ATOM   4598 C C   . PRO B 1 297 ? 5.212   -14.672 -23.541 1.00 42.18  ? 297 PRO B C   1 
ATOM   4599 O O   . PRO B 1 297 ? 5.025   -15.881 -23.390 1.00 45.13  ? 297 PRO B O   1 
ATOM   4600 C CB  . PRO B 1 297 ? 7.073   -14.416 -25.229 1.00 47.98  ? 297 PRO B CB  1 
ATOM   4601 C CG  . PRO B 1 297 ? 8.549   -14.594 -25.094 1.00 51.20  ? 297 PRO B CG  1 
ATOM   4602 C CD  . PRO B 1 297 ? 8.745   -15.272 -23.767 1.00 48.71  ? 297 PRO B CD  1 
ATOM   4603 N N   . ALA B 1 298 ? 4.235   -13.773 -23.473 1.00 44.16  ? 298 ALA B N   1 
ATOM   4604 C CA  . ALA B 1 298 ? 2.856   -14.139 -23.180 1.00 43.11  ? 298 ALA B CA  1 
ATOM   4605 C C   . ALA B 1 298 ? 1.932   -13.507 -24.211 1.00 41.50  ? 298 ALA B C   1 
ATOM   4606 O O   . ALA B 1 298 ? 2.021   -12.304 -24.485 1.00 43.48  ? 298 ALA B O   1 
ATOM   4607 C CB  . ALA B 1 298 ? 2.453   -13.703 -21.766 1.00 44.57  ? 298 ALA B CB  1 
ATOM   4608 N N   . SER B 1 299 ? 1.047   -14.321 -24.769 1.00 40.85  ? 299 SER B N   1 
ATOM   4609 C CA  . SER B 1 299 ? 0.089   -13.864 -25.759 1.00 41.94  ? 299 SER B CA  1 
ATOM   4610 C C   . SER B 1 299 ? -0.917  -12.907 -25.132 1.00 39.68  ? 299 SER B C   1 
ATOM   4611 O O   . SER B 1 299 ? -1.110  -12.881 -23.917 1.00 36.88  ? 299 SER B O   1 
ATOM   4612 C CB  . SER B 1 299 ? -0.653  -15.053 -26.355 1.00 40.30  ? 299 SER B CB  1 
ATOM   4613 O OG  . SER B 1 299 ? -1.348  -15.747 -25.328 1.00 41.58  ? 299 SER B OG  1 
ATOM   4614 N N   . LYS B 1 300 ? -1.598  -12.139 -25.989 1.00 36.93  ? 300 LYS B N   1 
ATOM   4615 C CA  . LYS B 1 300 ? -2.635  -11.250 -25.479 1.00 35.03  ? 300 LYS B CA  1 
ATOM   4616 C C   . LYS B 1 300 ? -3.729  -12.032 -24.771 1.00 34.36  ? 300 LYS B C   1 
ATOM   4617 O O   . LYS B 1 300 ? -4.358  -11.515 -23.844 1.00 36.80  ? 300 LYS B O   1 
ATOM   4618 C CB  . LYS B 1 300 ? -3.240  -10.417 -26.607 1.00 39.72  ? 300 LYS B CB  1 
ATOM   4619 C CG  . LYS B 1 300 ? -3.764  -11.232 -27.763 1.00 42.18  ? 300 LYS B CG  1 
ATOM   4620 C CD  . LYS B 1 300 ? -4.121  -10.331 -28.959 1.00 45.57  ? 300 LYS B CD  1 
ATOM   4621 C CE  . LYS B 1 300 ? -4.467  -11.151 -30.194 1.00 48.09  ? 300 LYS B CE  1 
ATOM   4622 N NZ  . LYS B 1 300 ? -5.795  -11.823 -30.103 1.00 48.74  ? 300 LYS B NZ  1 
ATOM   4623 N N   . GLU B 1 301 ? -3.969  -13.279 -25.186 1.00 35.80  ? 301 GLU B N   1 
ATOM   4624 C CA  . GLU B 1 301 ? -4.978  -14.092 -24.513 1.00 34.00  ? 301 GLU B CA  1 
ATOM   4625 C C   . GLU B 1 301 ? -4.570  -14.393 -23.071 1.00 34.15  ? 301 GLU B C   1 
ATOM   4626 O O   . GLU B 1 301 ? -5.411  -14.343 -22.165 1.00 31.85  ? 301 GLU B O   1 
ATOM   4627 C CB  . GLU B 1 301 ? -5.205  -15.376 -25.307 1.00 34.32  ? 301 GLU B CB  1 
ATOM   4628 C CG  . GLU B 1 301 ? -6.119  -15.136 -26.514 1.00 37.33  ? 301 GLU B CG  1 
ATOM   4629 C CD  . GLU B 1 301 ? -5.331  -14.636 -27.717 1.00 43.12  ? 301 GLU B CD  1 
ATOM   4630 O OE1 . GLU B 1 301 ? -5.947  -14.052 -28.647 1.00 48.38  ? 301 GLU B OE1 1 
ATOM   4631 O OE2 . GLU B 1 301 ? -4.085  -14.769 -27.699 1.00 40.49  ? 301 GLU B OE2 1 
ATOM   4632 N N   . ILE B 1 302 ? -3.289  -14.696 -22.844 1.00 34.84  ? 302 ILE B N   1 
ATOM   4633 C CA  . ILE B 1 302 ? -2.794  -14.870 -21.476 1.00 33.96  ? 302 ILE B CA  1 
ATOM   4634 C C   . ILE B 1 302 ? -3.029  -13.598 -20.665 1.00 32.45  ? 302 ILE B C   1 
ATOM   4635 O O   . ILE B 1 302 ? -3.542  -13.643 -19.539 1.00 30.78  ? 302 ILE B O   1 
ATOM   4636 C CB  . ILE B 1 302 ? -1.303  -15.264 -21.480 1.00 35.21  ? 302 ILE B CB  1 
ATOM   4637 C CG1 . ILE B 1 302 ? -1.087  -16.670 -22.044 1.00 38.40  ? 302 ILE B CG1 1 
ATOM   4638 C CG2 . ILE B 1 302 ? -0.714  -15.188 -20.057 1.00 36.15  ? 302 ILE B CG2 1 
ATOM   4639 C CD1 . ILE B 1 302 ? -1.335  -17.763 -21.061 1.00 41.61  ? 302 ILE B CD1 1 
ATOM   4640 N N   . LEU B 1 303 ? -2.673  -12.439 -21.232 1.00 31.82  ? 303 LEU B N   1 
ATOM   4641 C CA  . LEU B 1 303 ? -2.811  -11.186 -20.489 1.00 31.09  ? 303 LEU B CA  1 
ATOM   4642 C C   . LEU B 1 303 ? -4.271  -10.852 -20.231 1.00 31.36  ? 303 LEU B C   1 
ATOM   4643 O O   . LEU B 1 303 ? -4.616  -10.296 -19.184 1.00 31.62  ? 303 LEU B O   1 
ATOM   4644 C CB  . LEU B 1 303 ? -2.129  -10.041 -21.242 1.00 33.30  ? 303 LEU B CB  1 
ATOM   4645 C CG  . LEU B 1 303 ? -0.690  -10.345 -21.651 1.00 37.18  ? 303 LEU B CG  1 
ATOM   4646 C CD1 . LEU B 1 303 ? -0.100  -9.194  -22.443 1.00 41.22  ? 303 LEU B CD1 1 
ATOM   4647 C CD2 . LEU B 1 303 ? 0.139   -10.629 -20.412 1.00 37.85  ? 303 LEU B CD2 1 
ATOM   4648 N N   . GLN B 1 304 ? -5.140  -11.156 -21.193 1.00 31.25  ? 304 GLN B N   1 
ATOM   4649 C CA  . GLN B 1 304 ? -6.566  -10.951 -20.996 1.00 29.47  ? 304 GLN B CA  1 
ATOM   4650 C C   . GLN B 1 304 ? -7.082  -11.781 -19.829 1.00 27.90  ? 304 GLN B C   1 
ATOM   4651 O O   . GLN B 1 304 ? -7.880  -11.302 -19.016 1.00 28.29  ? 304 GLN B O   1 
ATOM   4652 C CB  . GLN B 1 304 ? -7.308  -11.325 -22.273 1.00 29.80  ? 304 GLN B CB  1 
ATOM   4653 C CG  . GLN B 1 304 ? -7.212  -10.278 -23.368 1.00 32.17  ? 304 GLN B CG  1 
ATOM   4654 C CD  . GLN B 1 304 ? -7.469  -10.875 -24.745 1.00 35.15  ? 304 GLN B CD  1 
ATOM   4655 O OE1 . GLN B 1 304 ? -8.012  -11.976 -24.866 1.00 33.40  ? 304 GLN B OE1 1 
ATOM   4656 N NE2 . GLN B 1 304 ? -7.097  -10.138 -25.790 1.00 37.46  ? 304 GLN B NE2 1 
ATOM   4657 N N   . TYR B 1 305 ? -6.681  -13.051 -19.765 1.00 26.98  ? 305 TYR B N   1 
ATOM   4658 C CA  . TYR B 1 305 ? -7.162  -13.900 -18.685 1.00 26.68  ? 305 TYR B CA  1 
ATOM   4659 C C   . TYR B 1 305 ? -6.631  -13.421 -17.337 1.00 27.17  ? 305 TYR B C   1 
ATOM   4660 O O   . TYR B 1 305 ? -7.388  -13.372 -16.363 1.00 28.35  ? 305 TYR B O   1 
ATOM   4661 C CB  . TYR B 1 305 ? -6.765  -15.359 -18.913 1.00 28.18  ? 305 TYR B CB  1 
ATOM   4662 C CG  . TYR B 1 305 ? -7.345  -16.278 -17.854 1.00 29.00  ? 305 TYR B CG  1 
ATOM   4663 C CD1 . TYR B 1 305 ? -8.721  -16.429 -17.740 1.00 29.93  ? 305 TYR B CD1 1 
ATOM   4664 C CD2 . TYR B 1 305 ? -6.528  -16.956 -16.950 1.00 29.12  ? 305 TYR B CD2 1 
ATOM   4665 C CE1 . TYR B 1 305 ? -9.280  -17.268 -16.789 1.00 28.92  ? 305 TYR B CE1 1 
ATOM   4666 C CE2 . TYR B 1 305 ? -7.077  -17.796 -15.973 1.00 28.92  ? 305 TYR B CE2 1 
ATOM   4667 C CZ  . TYR B 1 305 ? -8.453  -17.942 -15.901 1.00 28.20  ? 305 TYR B CZ  1 
ATOM   4668 O OH  . TYR B 1 305 ? -9.021  -18.760 -14.956 1.00 28.75  ? 305 TYR B OH  1 
ATOM   4669 N N   . PHE B 1 306 ? -5.349  -13.043 -17.267 1.00 28.57  ? 306 PHE B N   1 
ATOM   4670 C CA  . PHE B 1 306 ? -4.806  -12.539 -16.004 1.00 28.70  ? 306 PHE B CA  1 
ATOM   4671 C C   . PHE B 1 306 ? -5.654  -11.390 -15.486 1.00 28.08  ? 306 PHE B C   1 
ATOM   4672 O O   . PHE B 1 306 ? -6.042  -11.355 -14.312 1.00 30.18  ? 306 PHE B O   1 
ATOM   4673 C CB  . PHE B 1 306 ? -3.354  -12.051 -16.162 1.00 29.51  ? 306 PHE B CB  1 
ATOM   4674 C CG  . PHE B 1 306 ? -2.326  -13.137 -16.120 1.00 30.52  ? 306 PHE B CG  1 
ATOM   4675 C CD1 . PHE B 1 306 ? -2.529  -14.281 -15.373 1.00 30.75  ? 306 PHE B CD1 1 
ATOM   4676 C CD2 . PHE B 1 306 ? -1.125  -12.991 -16.802 1.00 32.54  ? 306 PHE B CD2 1 
ATOM   4677 C CE1 . PHE B 1 306 ? -1.561  -15.284 -15.331 1.00 33.86  ? 306 PHE B CE1 1 
ATOM   4678 C CE2 . PHE B 1 306 ? -0.154  -13.981 -16.756 1.00 31.56  ? 306 PHE B CE2 1 
ATOM   4679 C CZ  . PHE B 1 306 ? -0.371  -15.122 -16.030 1.00 33.29  ? 306 PHE B CZ  1 
ATOM   4680 N N   . GLU B 1 307 ? -5.945  -10.419 -16.348 1.00 27.59  ? 307 GLU B N   1 
ATOM   4681 C CA  . GLU B 1 307 ? -6.592  -9.233  -15.814 1.00 27.14  ? 307 GLU B CA  1 
ATOM   4682 C C   . GLU B 1 307 ? -8.046  -9.539  -15.461 1.00 28.65  ? 307 GLU B C   1 
ATOM   4683 O O   . GLU B 1 307 ? -8.561  -9.054  -14.450 1.00 30.09  ? 307 GLU B O   1 
ATOM   4684 C CB  . GLU B 1 307 ? -6.460  -8.067  -16.801 1.00 29.77  ? 307 GLU B CB  1 
ATOM   4685 C CG  . GLU B 1 307 ? -7.473  -6.949  -16.610 1.00 35.36  ? 307 GLU B CG  1 
ATOM   4686 C CD  . GLU B 1 307 ? -7.185  -5.736  -17.489 1.00 35.64  ? 307 GLU B CD  1 
ATOM   4687 O OE1 . GLU B 1 307 ? -6.359  -5.850  -18.423 1.00 35.97  ? 307 GLU B OE1 1 
ATOM   4688 O OE2 . GLU B 1 307 ? -7.809  -4.681  -17.254 1.00 36.15  ? 307 GLU B OE2 1 
ATOM   4689 N N   . ALA B 1 308 ? -8.724  -10.370 -16.262 1.00 26.56  ? 308 ALA B N   1 
ATOM   4690 C CA  . ALA B 1 308 ? -10.128 -10.644 -15.974 1.00 26.97  ? 308 ALA B CA  1 
ATOM   4691 C C   . ALA B 1 308 ? -10.283 -11.564 -14.766 1.00 26.56  ? 308 ALA B C   1 
ATOM   4692 O O   . ALA B 1 308 ? -11.223 -11.404 -13.979 1.00 26.36  ? 308 ALA B O   1 
ATOM   4693 C CB  . ALA B 1 308 ? -10.822 -11.254 -17.201 1.00 27.08  ? 308 ALA B CB  1 
ATOM   4694 N N   . ILE B 1 309 ? -9.388  -12.541 -14.601 1.00 26.45  ? 309 ILE B N   1 
ATOM   4695 C CA  . ILE B 1 309 ? -9.531  -13.442 -13.456 1.00 26.43  ? 309 ILE B CA  1 
ATOM   4696 C C   . ILE B 1 309 ? -9.166  -12.734 -12.154 1.00 28.21  ? 309 ILE B C   1 
ATOM   4697 O O   . ILE B 1 309 ? -9.724  -13.056 -11.099 1.00 26.53  ? 309 ILE B O   1 
ATOM   4698 C CB  . ILE B 1 309 ? -8.707  -14.738 -13.653 1.00 26.85  ? 309 ILE B CB  1 
ATOM   4699 C CG1 . ILE B 1 309 ? -9.285  -15.914 -12.841 1.00 29.22  ? 309 ILE B CG1 1 
ATOM   4700 C CG2 . ILE B 1 309 ? -7.226  -14.539 -13.350 1.00 26.89  ? 309 ILE B CG2 1 
ATOM   4701 C CD1 . ILE B 1 309 ? -10.778 -16.191 -13.085 1.00 29.21  ? 309 ILE B CD1 1 
ATOM   4702 N N   . GLU B 1 310 ? -8.279  -11.732 -12.204 1.00 26.47  ? 310 GLU B N   1 
ATOM   4703 C CA  . GLU B 1 310 ? -8.021  -10.939 -11.001 1.00 26.74  ? 310 GLU B CA  1 
ATOM   4704 C C   . GLU B 1 310 ? -9.246  -10.118 -10.621 1.00 28.57  ? 310 GLU B C   1 
ATOM   4705 O O   . GLU B 1 310 ? -9.571  -9.996  -9.439  1.00 28.51  ? 310 GLU B O   1 
ATOM   4706 C CB  . GLU B 1 310 ? -6.799  -10.043 -11.204 1.00 29.01  ? 310 GLU B CB  1 
ATOM   4707 C CG  . GLU B 1 310 ? -5.536  -10.868 -11.314 1.00 28.20  ? 310 GLU B CG  1 
ATOM   4708 C CD  . GLU B 1 310 ? -4.298  -10.050 -11.451 1.00 35.76  ? 310 GLU B CD  1 
ATOM   4709 O OE1 . GLU B 1 310 ? -4.400  -8.804  -11.502 1.00 37.36  ? 310 GLU B OE1 1 
ATOM   4710 O OE2 . GLU B 1 310 ? -3.222  -10.664 -11.517 1.00 34.24  ? 310 GLU B OE2 1 
ATOM   4711 N N   . LEU B 1 311 ? -9.975  -9.597  -11.613 1.00 26.13  ? 311 LEU B N   1 
ATOM   4712 C CA  . LEU B 1 311 ? -11.216 -8.894  -11.309 1.00 27.20  ? 311 LEU B CA  1 
ATOM   4713 C C   . LEU B 1 311 ? -12.259 -9.853  -10.761 1.00 25.70  ? 311 LEU B C   1 
ATOM   4714 O O   . LEU B 1 311 ? -13.087 -9.464  -9.932  1.00 27.48  ? 311 LEU B O   1 
ATOM   4715 C CB  . LEU B 1 311 ? -11.745 -8.201  -12.569 1.00 25.43  ? 311 LEU B CB  1 
ATOM   4716 C CG  . LEU B 1 311 ? -11.087 -6.861  -12.906 1.00 28.94  ? 311 LEU B CG  1 
ATOM   4717 C CD1 . LEU B 1 311 ? -11.300 -6.519  -14.360 1.00 31.74  ? 311 LEU B CD1 1 
ATOM   4718 C CD2 . LEU B 1 311 ? -11.606 -5.735  -11.974 1.00 29.38  ? 311 LEU B CD2 1 
ATOM   4719 N N   . TYR B 1 312 ? -12.244 -11.095 -11.210 1.00 25.83  ? 312 TYR B N   1 
ATOM   4720 C CA  . TYR B 1 312 ? -13.224 -12.080 -10.703 1.00 27.41  ? 312 TYR B CA  1 
ATOM   4721 C C   . TYR B 1 312 ? -12.960 -12.354 -9.225  1.00 27.06  ? 312 TYR B C   1 
ATOM   4722 O O   . TYR B 1 312 ? -13.903 -12.353 -8.437  1.00 25.88  ? 312 TYR B O   1 
ATOM   4723 C CB  . TYR B 1 312 ? -13.144 -13.377 -11.505 1.00 28.52  ? 312 TYR B CB  1 
ATOM   4724 C CG  . TYR B 1 312 ? -13.947 -14.506 -10.917 1.00 26.29  ? 312 TYR B CG  1 
ATOM   4725 C CD1 . TYR B 1 312 ? -15.327 -14.509 -10.998 1.00 29.22  ? 312 TYR B CD1 1 
ATOM   4726 C CD2 . TYR B 1 312 ? -13.331 -15.557 -10.265 1.00 27.64  ? 312 TYR B CD2 1 
ATOM   4727 C CE1 . TYR B 1 312 ? -16.080 -15.530 -10.447 1.00 28.28  ? 312 TYR B CE1 1 
ATOM   4728 C CE2 . TYR B 1 312 ? -14.068 -16.589 -9.714  1.00 28.15  ? 312 TYR B CE2 1 
ATOM   4729 C CZ  . TYR B 1 312 ? -15.447 -16.574 -9.801  1.00 30.68  ? 312 TYR B CZ  1 
ATOM   4730 O OH  . TYR B 1 312 ? -16.178 -17.584 -9.251  1.00 32.96  ? 312 TYR B OH  1 
ATOM   4731 N N   . VAL B 1 313 ? -11.694 -12.550 -8.879  1.00 25.89  ? 313 VAL B N   1 
ATOM   4732 C CA  . VAL B 1 313 ? -11.338 -12.917 -7.509  1.00 27.12  ? 313 VAL B CA  1 
ATOM   4733 C C   . VAL B 1 313 ? -11.461 -11.721 -6.575  1.00 24.87  ? 313 VAL B C   1 
ATOM   4734 O O   . VAL B 1 313 ? -12.054 -11.815 -5.496  1.00 25.91  ? 313 VAL B O   1 
ATOM   4735 C CB  . VAL B 1 313 ? -9.929  -13.520 -7.479  1.00 25.98  ? 313 VAL B CB  1 
ATOM   4736 C CG1 . VAL B 1 313 ? -9.442  -13.642 -6.037  1.00 26.37  ? 313 VAL B CG1 1 
ATOM   4737 C CG2 . VAL B 1 313 ? -9.953  -14.904 -8.171  1.00 29.61  ? 313 VAL B CG2 1 
ATOM   4738 N N   . GLY B 1 314 ? -10.923 -10.575 -6.981  1.00 24.73  ? 314 GLY B N   1 
ATOM   4739 C CA  . GLY B 1 314 ? -11.097 -9.380  -6.172  1.00 26.59  ? 314 GLY B CA  1 
ATOM   4740 C C   . GLY B 1 314 ? -12.555 -8.984  -6.039  1.00 28.24  ? 314 GLY B C   1 
ATOM   4741 O O   . GLY B 1 314 ? -13.020 -8.640  -4.951  1.00 28.71  ? 314 GLY B O   1 
ATOM   4742 N N   . GLY B 1 315 ? -13.301 -9.028  -7.146  1.00 27.35  ? 315 GLY B N   1 
ATOM   4743 C CA  . GLY B 1 315 ? -14.720 -8.723  -7.069  1.00 27.92  ? 315 GLY B CA  1 
ATOM   4744 C C   . GLY B 1 315 ? -15.471 -9.660  -6.144  1.00 26.75  ? 315 GLY B C   1 
ATOM   4745 O O   . GLY B 1 315 ? -16.400 -9.249  -5.448  1.00 27.39  ? 315 GLY B O   1 
ATOM   4746 N N   . SER B 1 316 ? -15.100 -10.946 -6.137  1.00 27.36  ? 316 SER B N   1 
ATOM   4747 C CA  . SER B 1 316 ? -15.780 -11.863 -5.229  1.00 26.09  ? 316 SER B CA  1 
ATOM   4748 C C   . SER B 1 316 ? -15.484 -11.509 -3.781  1.00 28.78  ? 316 SER B C   1 
ATOM   4749 O O   . SER B 1 316 ? -16.375 -11.565 -2.922  1.00 29.52  ? 316 SER B O   1 
ATOM   4750 C CB  . SER B 1 316 ? -15.365 -13.300 -5.522  1.00 28.65  ? 316 SER B CB  1 
ATOM   4751 O OG  . SER B 1 316 ? -16.131 -14.205 -4.741  1.00 28.81  ? 316 SER B OG  1 
ATOM   4752 N N   . CYS B 1 317 ? -14.241 -11.134 -3.490  1.00 26.61  ? 317 CYS B N   1 
ATOM   4753 C CA  . CYS B 1 317 ? -13.931 -10.693 -2.133  1.00 29.58  ? 317 CYS B CA  1 
ATOM   4754 C C   . CYS B 1 317 ? -14.750 -9.466  -1.760  1.00 31.79  ? 317 CYS B C   1 
ATOM   4755 O O   . CYS B 1 317 ? -15.299 -9.384  -0.654  1.00 32.68  ? 317 CYS B O   1 
ATOM   4756 C CB  . CYS B 1 317 ? -12.440 -10.399 -1.999  1.00 25.45  ? 317 CYS B CB  1 
ATOM   4757 S SG  . CYS B 1 317 ? -12.014 -10.043 -0.277  1.00 31.01  ? 317 CYS B SG  1 
ATOM   4758 N N   . TYR B 1 318 ? -14.881 -8.530  -2.699  1.00 28.59  ? 318 TYR B N   1 
ATOM   4759 C CA  . TYR B 1 318 ? -15.656 -7.319  -2.472  1.00 33.10  ? 318 TYR B CA  1 
ATOM   4760 C C   . TYR B 1 318 ? -17.122 -7.637  -2.221  1.00 34.60  ? 318 TYR B C   1 
ATOM   4761 O O   . TYR B 1 318 ? -17.737 -7.088  -1.298  1.00 35.57  ? 318 TYR B O   1 
ATOM   4762 C CB  . TYR B 1 318 ? -15.482 -6.399  -3.674  1.00 31.18  ? 318 TYR B CB  1 
ATOM   4763 C CG  . TYR B 1 318 ? -16.196 -5.072  -3.585  1.00 33.29  ? 318 TYR B CG  1 
ATOM   4764 C CD1 . TYR B 1 318 ? -17.505 -4.935  -4.037  1.00 36.85  ? 318 TYR B CD1 1 
ATOM   4765 C CD2 . TYR B 1 318 ? -15.566 -3.963  -3.032  1.00 36.46  ? 318 TYR B CD2 1 
ATOM   4766 C CE1 . TYR B 1 318 ? -18.161 -3.719  -3.958  1.00 42.50  ? 318 TYR B CE1 1 
ATOM   4767 C CE2 . TYR B 1 318 ? -16.213 -2.745  -2.949  1.00 40.60  ? 318 TYR B CE2 1 
ATOM   4768 C CZ  . TYR B 1 318 ? -17.506 -2.631  -3.413  1.00 41.22  ? 318 TYR B CZ  1 
ATOM   4769 O OH  . TYR B 1 318 ? -18.153 -1.418  -3.325  1.00 42.64  ? 318 TYR B OH  1 
ATOM   4770 N N   . TRP B 1 319 ? -17.707 -8.521  -3.033  1.00 32.39  ? 319 TRP B N   1 
ATOM   4771 C CA  . TRP B 1 319 ? -19.111 -8.852  -2.836  1.00 31.82  ? 319 TRP B CA  1 
ATOM   4772 C C   . TRP B 1 319 ? -19.334 -9.528  -1.490  1.00 37.91  ? 319 TRP B C   1 
ATOM   4773 O O   . TRP B 1 319 ? -20.263 -9.168  -0.760  1.00 37.37  ? 319 TRP B O   1 
ATOM   4774 C CB  . TRP B 1 319 ? -19.624 -9.732  -3.983  1.00 33.77  ? 319 TRP B CB  1 
ATOM   4775 C CG  . TRP B 1 319 ? -21.084 -10.022 -3.860  1.00 33.23  ? 319 TRP B CG  1 
ATOM   4776 C CD1 . TRP B 1 319 ? -22.116 -9.153  -4.101  1.00 40.06  ? 319 TRP B CD1 1 
ATOM   4777 C CD2 . TRP B 1 319 ? -21.685 -11.254 -3.454  1.00 41.68  ? 319 TRP B CD2 1 
ATOM   4778 N NE1 . TRP B 1 319 ? -23.317 -9.770  -3.862  1.00 39.55  ? 319 TRP B NE1 1 
ATOM   4779 C CE2 . TRP B 1 319 ? -23.083 -11.060 -3.463  1.00 43.19  ? 319 TRP B CE2 1 
ATOM   4780 C CE3 . TRP B 1 319 ? -21.179 -12.501 -3.077  1.00 45.47  ? 319 TRP B CE3 1 
ATOM   4781 C CZ2 . TRP B 1 319 ? -23.981 -12.073 -3.126  1.00 49.85  ? 319 TRP B CZ2 1 
ATOM   4782 C CZ3 . TRP B 1 319 ? -22.074 -13.511 -2.740  1.00 50.34  ? 319 TRP B CZ3 1 
ATOM   4783 C CH2 . TRP B 1 319 ? -23.458 -13.291 -2.768  1.00 50.24  ? 319 TRP B CH2 1 
ATOM   4784 N N   . HIS B 1 320 ? -18.489 -10.507 -1.129  1.00 33.80  ? 320 HIS B N   1 
ATOM   4785 C CA  . HIS B 1 320 ? -18.642 -11.140 0.179   1.00 39.97  ? 320 HIS B CA  1 
ATOM   4786 C C   . HIS B 1 320 ? -18.370 -10.161 1.309   1.00 42.74  ? 320 HIS B C   1 
ATOM   4787 O O   . HIS B 1 320 ? -18.923 -10.310 2.404   1.00 49.71  ? 320 HIS B O   1 
ATOM   4788 C CB  . HIS B 1 320 ? -17.723 -12.356 0.311   1.00 39.33  ? 320 HIS B CB  1 
ATOM   4789 C CG  . HIS B 1 320 ? -18.172 -13.535 -0.484  1.00 36.52  ? 320 HIS B CG  1 
ATOM   4790 N ND1 . HIS B 1 320 ? -17.723 -13.791 -1.760  1.00 45.84  ? 320 HIS B ND1 1 
ATOM   4791 C CD2 . HIS B 1 320 ? -19.053 -14.518 -0.191  1.00 40.69  ? 320 HIS B CD2 1 
ATOM   4792 C CE1 . HIS B 1 320 ? -18.297 -14.891 -2.213  1.00 44.06  ? 320 HIS B CE1 1 
ATOM   4793 N NE2 . HIS B 1 320 ? -19.100 -15.359 -1.275  1.00 44.82  ? 320 HIS B NE2 1 
ATOM   4794 N N   . SER B 1 321 ? -17.533 -9.154  1.060   1.00 40.36  ? 321 SER B N   1 
ATOM   4795 C CA  . SER B 1 321 ? -17.187 -8.185  2.096   1.00 43.45  ? 321 SER B CA  1 
ATOM   4796 C C   . SER B 1 321 ? -18.342 -7.245  2.404   1.00 47.17  ? 321 SER B C   1 
ATOM   4797 O O   . SER B 1 321 ? -18.473 -6.778  3.542   1.00 50.20  ? 321 SER B O   1 
ATOM   4798 C CB  . SER B 1 321 ? -15.972 -7.371  1.660   1.00 38.39  ? 321 SER B CB  1 
ATOM   4799 O OG  . SER B 1 321 ? -14.807 -8.170  1.661   1.00 38.98  ? 321 SER B OG  1 
ATOM   4800 N N   . THR B 1 322 ? -19.170 -6.943  1.408   1.00 46.42  ? 322 THR B N   1 
ATOM   4801 C CA  . THR B 1 322 ? -20.233 -5.955  1.529   1.00 47.69  ? 322 THR B CA  1 
ATOM   4802 C C   . THR B 1 322 ? -21.620 -6.569  1.660   1.00 54.35  ? 322 THR B C   1 
ATOM   4803 O O   . THR B 1 322 ? -22.595 -5.823  1.793   1.00 57.77  ? 322 THR B O   1 
ATOM   4804 C CB  . THR B 1 322 ? -20.216 -5.020  0.317   1.00 50.84  ? 322 THR B CB  1 
ATOM   4805 O OG1 . THR B 1 322 ? -20.279 -5.805  -0.878  1.00 47.52  ? 322 THR B OG1 1 
ATOM   4806 C CG2 . THR B 1 322 ? -18.950 -4.183  0.287   1.00 43.74  ? 322 THR B CG2 1 
ATOM   4807 N N   . ALA B 1 323 ? -21.736 -7.895  1.626   1.00 51.45  ? 323 ALA B N   1 
ATOM   4808 C CA  . ALA B 1 323 ? -23.036 -8.566  1.579   1.00 56.88  ? 323 ALA B CA  1 
ATOM   4809 C C   . ALA B 1 323 ? -23.825 -8.371  2.872   1.00 59.27  ? 323 ALA B C   1 
ATOM   4810 O O   . ALA B 1 323 ? -23.342 -8.689  3.960   1.00 62.82  ? 323 ALA B O   1 
ATOM   4811 C CB  . ALA B 1 323 ? -22.849 -10.043 1.292   1.00 52.40  ? 323 ALA B CB  1 
HETATM 4812 O O   . HOH C 2 .   ? 30.011  -0.562  17.924  1.00 43.34  ? 401 HOH A O   1 
HETATM 4813 O O   . HOH C 2 .   ? -5.702  -18.007 24.651  1.00 59.77  ? 402 HOH A O   1 
HETATM 4814 O O   . HOH C 2 .   ? -12.179 -6.045  12.970  1.00 50.30  ? 403 HOH A O   1 
HETATM 4815 O O   . HOH C 2 .   ? 16.076  4.970   -0.327  1.00 38.83  ? 404 HOH A O   1 
HETATM 4816 O O   . HOH C 2 .   ? 1.435   -27.696 10.059  1.00 43.77  ? 405 HOH A O   1 
HETATM 4817 O O   . HOH C 2 .   ? -8.116  19.486  20.305  1.00 54.73  ? 406 HOH A O   1 
HETATM 4818 O O   . HOH C 2 .   ? 17.744  -5.075  23.300  1.00 46.80  ? 407 HOH A O   1 
HETATM 4819 O O   . HOH C 2 .   ? 23.189  13.836  3.089   1.00 44.27  ? 408 HOH A O   1 
HETATM 4820 O O   . HOH C 2 .   ? 4.821   -16.047 29.947  1.00 43.85  ? 409 HOH A O   1 
HETATM 4821 O O   . HOH C 2 .   ? 24.857  2.102   26.202  1.00 35.97  ? 410 HOH A O   1 
HETATM 4822 O O   . HOH C 2 .   ? 10.316  -10.063 -2.522  1.00 48.76  ? 411 HOH A O   1 
HETATM 4823 O O   . HOH C 2 .   ? 5.135   15.561  17.094  1.00 38.93  ? 412 HOH A O   1 
HETATM 4824 O O   . HOH C 2 .   ? 5.955   16.984  20.426  1.00 34.14  ? 413 HOH A O   1 
HETATM 4825 O O   . HOH C 2 .   ? -0.196  20.545  10.124  1.00 46.85  ? 414 HOH A O   1 
HETATM 4826 O O   . HOH C 2 .   ? -4.611  -6.372  4.881   1.00 38.98  ? 415 HOH A O   1 
HETATM 4827 O O   . HOH C 2 .   ? 20.211  -5.696  9.643   1.00 48.15  ? 416 HOH A O   1 
HETATM 4828 O O   . HOH C 2 .   ? 28.081  10.778  15.168  1.00 44.88  ? 417 HOH A O   1 
HETATM 4829 O O   . HOH C 2 .   ? 1.293   14.679  -0.433  1.00 51.38  ? 418 HOH A O   1 
HETATM 4830 O O   . HOH C 2 .   ? 11.255  0.224   -4.622  1.00 43.93  ? 419 HOH A O   1 
HETATM 4831 O O   . HOH C 2 .   ? 13.278  23.064  24.158  1.00 42.67  ? 420 HOH A O   1 
HETATM 4832 O O   . HOH C 2 .   ? 17.995  -5.530  13.535  1.00 47.36  ? 421 HOH A O   1 
HETATM 4833 O O   . HOH C 2 .   ? 20.575  8.849   -6.205  1.00 57.34  ? 422 HOH A O   1 
HETATM 4834 O O   . HOH C 2 .   ? -4.405  -14.202 23.969  1.00 43.77  ? 423 HOH A O   1 
HETATM 4835 O O   . HOH C 2 .   ? 12.712  -0.906  19.137  1.00 37.46  ? 424 HOH A O   1 
HETATM 4836 O O   . HOH C 2 .   ? 9.033   1.147   14.830  1.00 37.85  ? 425 HOH A O   1 
HETATM 4837 O O   . HOH C 2 .   ? 6.560   12.218  8.955   1.00 26.00  ? 426 HOH A O   1 
HETATM 4838 O O   . HOH C 2 .   ? -6.881  2.972   7.959   1.00 37.20  ? 427 HOH A O   1 
HETATM 4839 O O   . HOH C 2 .   ? -3.369  19.595  16.598  1.00 49.86  ? 428 HOH A O   1 
HETATM 4840 O O   . HOH C 2 .   ? 6.089   -3.931  9.240   1.00 29.00  ? 429 HOH A O   1 
HETATM 4841 O O   . HOH C 2 .   ? 26.407  -6.830  21.993  1.00 44.39  ? 430 HOH A O   1 
HETATM 4842 O O   . HOH C 2 .   ? 23.055  -2.068  13.894  1.00 33.49  ? 431 HOH A O   1 
HETATM 4843 O O   . HOH C 2 .   ? 1.637   -6.046  18.877  1.00 32.87  ? 432 HOH A O   1 
HETATM 4844 O O   . HOH C 2 .   ? 1.626   7.391   18.454  1.00 31.75  ? 433 HOH A O   1 
HETATM 4845 O O   . HOH C 2 .   ? 10.366  13.029  2.557   1.00 35.07  ? 434 HOH A O   1 
HETATM 4846 O O   . HOH C 2 .   ? 5.071   8.250   6.491   1.00 26.77  ? 435 HOH A O   1 
HETATM 4847 O O   . HOH C 2 .   ? 26.947  12.072  11.346  1.00 42.19  ? 436 HOH A O   1 
HETATM 4848 O O   . HOH C 2 .   ? 26.305  -9.839  27.797  1.00 49.66  ? 437 HOH A O   1 
HETATM 4849 O O   . HOH C 2 .   ? 11.085  4.192   12.336  1.00 34.53  ? 438 HOH A O   1 
HETATM 4850 O O   . HOH C 2 .   ? 17.541  -1.022  3.008   1.00 38.09  ? 439 HOH A O   1 
HETATM 4851 O O   . HOH C 2 .   ? 2.023   -7.024  28.083  1.00 41.42  ? 440 HOH A O   1 
HETATM 4852 O O   . HOH C 2 .   ? 6.718   2.231   25.589  1.00 35.98  ? 441 HOH A O   1 
HETATM 4853 O O   . HOH C 2 .   ? 2.532   -0.709  24.161  1.00 40.36  ? 442 HOH A O   1 
HETATM 4854 O O   . HOH C 2 .   ? 16.073  17.427  29.985  1.00 42.46  ? 443 HOH A O   1 
HETATM 4855 O O   . HOH C 2 .   ? 8.649   10.985  10.050  1.00 29.15  ? 444 HOH A O   1 
HETATM 4856 O O   . HOH C 2 .   ? 5.816   4.433   2.720   1.00 29.05  ? 445 HOH A O   1 
HETATM 4857 O O   . HOH C 2 .   ? -6.681  -22.961 20.175  1.00 43.19  ? 446 HOH A O   1 
HETATM 4858 O O   . HOH C 2 .   ? 18.612  23.309  24.880  1.00 42.60  ? 447 HOH A O   1 
HETATM 4859 O O   . HOH C 2 .   ? 12.604  18.819  18.813  1.00 27.43  ? 448 HOH A O   1 
HETATM 4860 O O   . HOH C 2 .   ? 11.716  -2.615  35.796  1.00 58.39  ? 449 HOH A O   1 
HETATM 4861 O O   . HOH C 2 .   ? 15.174  6.122   30.046  1.00 39.81  ? 450 HOH A O   1 
HETATM 4862 O O   . HOH C 2 .   ? 3.485   14.452  18.563  1.00 47.01  ? 451 HOH A O   1 
HETATM 4863 O O   . HOH C 2 .   ? 6.306   12.593  24.801  1.00 39.58  ? 452 HOH A O   1 
HETATM 4864 O O   . HOH C 2 .   ? 7.701   -22.061 9.454   1.00 47.63  ? 453 HOH A O   1 
HETATM 4865 O O   . HOH C 2 .   ? 24.472  2.763   6.085   1.00 44.40  ? 454 HOH A O   1 
HETATM 4866 O O   . HOH C 2 .   ? -1.588  -4.372  21.461  1.00 39.88  ? 455 HOH A O   1 
HETATM 4867 O O   . HOH C 2 .   ? 9.640   -1.032  10.389  1.00 40.70  ? 456 HOH A O   1 
HETATM 4868 O O   . HOH C 2 .   ? 1.456   2.407   -2.578  1.00 39.25  ? 457 HOH A O   1 
HETATM 4869 O O   . HOH C 2 .   ? 13.320  -4.679  19.566  1.00 43.68  ? 458 HOH A O   1 
HETATM 4870 O O   . HOH C 2 .   ? 13.646  9.661   -4.263  1.00 47.68  ? 459 HOH A O   1 
HETATM 4871 O O   . HOH C 2 .   ? -11.259 3.364   6.476   1.00 37.25  ? 460 HOH A O   1 
HETATM 4872 O O   . HOH C 2 .   ? 24.828  11.758  9.496   1.00 38.34  ? 461 HOH A O   1 
HETATM 4873 O O   . HOH C 2 .   ? -12.801 7.487   17.423  1.00 46.29  ? 462 HOH A O   1 
HETATM 4874 O O   . HOH C 2 .   ? -5.814  8.822   4.855   1.00 45.68  ? 463 HOH A O   1 
HETATM 4875 O O   . HOH C 2 .   ? -1.223  -1.082  -0.738  1.00 39.17  ? 464 HOH A O   1 
HETATM 4876 O O   . HOH C 2 .   ? -8.974  7.048   23.854  1.00 46.86  ? 465 HOH A O   1 
HETATM 4877 O O   . HOH C 2 .   ? -7.198  -5.860  5.643   1.00 37.49  ? 466 HOH A O   1 
HETATM 4878 O O   . HOH C 2 .   ? -6.086  -3.697  18.414  1.00 40.14  ? 467 HOH A O   1 
HETATM 4879 O O   . HOH C 2 .   ? -7.293  -1.083  18.781  1.00 39.00  ? 468 HOH A O   1 
HETATM 4880 O O   . HOH C 2 .   ? 20.089  7.046   33.087  1.00 41.82  ? 469 HOH A O   1 
HETATM 4881 O O   . HOH C 2 .   ? 6.795   23.097  17.142  1.00 43.51  ? 470 HOH A O   1 
HETATM 4882 O O   . HOH C 2 .   ? 4.794   8.423   21.276  1.00 40.57  ? 471 HOH A O   1 
HETATM 4883 O O   . HOH C 2 .   ? 27.949  9.407   3.668   1.00 49.42  ? 472 HOH A O   1 
HETATM 4884 O O   . HOH C 2 .   ? -2.555  -24.034 27.079  1.00 61.33  ? 473 HOH A O   1 
HETATM 4885 O O   . HOH C 2 .   ? 26.353  -3.586  30.046  1.00 47.01  ? 474 HOH A O   1 
HETATM 4886 O O   . HOH C 2 .   ? 23.742  13.148  31.828  1.00 46.15  ? 475 HOH A O   1 
HETATM 4887 O O   . HOH C 2 .   ? 8.139   6.187   24.003  1.00 30.13  ? 476 HOH A O   1 
HETATM 4888 O O   . HOH C 2 .   ? 13.592  -1.076  28.402  1.00 33.13  ? 477 HOH A O   1 
HETATM 4889 O O   . HOH C 2 .   ? 18.489  11.847  33.174  1.00 53.95  ? 478 HOH A O   1 
HETATM 4890 O O   . HOH C 2 .   ? 10.031  25.124  17.877  1.00 36.51  ? 479 HOH A O   1 
HETATM 4891 O O   . HOH C 2 .   ? -11.049 12.797  22.671  1.00 54.26  ? 480 HOH A O   1 
HETATM 4892 O O   . HOH C 2 .   ? 23.326  17.813  29.852  1.00 51.03  ? 481 HOH A O   1 
HETATM 4893 O O   . HOH C 2 .   ? -9.180  4.193   24.168  1.00 56.96  ? 482 HOH A O   1 
HETATM 4894 O O   . HOH C 2 .   ? -4.524  11.781  24.730  1.00 49.08  ? 483 HOH A O   1 
HETATM 4895 O O   . HOH C 2 .   ? 27.520  0.573   18.716  1.00 36.46  ? 484 HOH A O   1 
HETATM 4896 O O   . HOH C 2 .   ? 1.183   14.901  19.227  1.00 43.04  ? 485 HOH A O   1 
HETATM 4897 O O   . HOH C 2 .   ? 1.549   -4.849  7.114   1.00 25.95  ? 486 HOH A O   1 
HETATM 4898 O O   . HOH C 2 .   ? 30.783  8.238   17.839  1.00 49.72  ? 487 HOH A O   1 
HETATM 4899 O O   . HOH C 2 .   ? 11.215  16.292  28.831  1.00 40.27  ? 488 HOH A O   1 
HETATM 4900 O O   . HOH C 2 .   ? 8.889   6.226   31.516  1.00 53.46  ? 489 HOH A O   1 
HETATM 4901 O O   . HOH C 2 .   ? -1.653  7.333   3.058   1.00 40.15  ? 490 HOH A O   1 
HETATM 4902 O O   . HOH C 2 .   ? 7.501   23.504  24.858  1.00 48.93  ? 491 HOH A O   1 
HETATM 4903 O O   . HOH C 2 .   ? 7.089   -15.126 4.702   1.00 53.14  ? 492 HOH A O   1 
HETATM 4904 O O   . HOH C 2 .   ? -7.017  18.524  23.952  1.00 50.27  ? 493 HOH A O   1 
HETATM 4905 O O   . HOH C 2 .   ? 7.131   19.644  23.964  1.00 34.97  ? 494 HOH A O   1 
HETATM 4906 O O   . HOH C 2 .   ? -4.227  -7.084  24.497  1.00 46.79  ? 495 HOH A O   1 
HETATM 4907 O O   . HOH C 2 .   ? 3.588   -3.132  8.396   1.00 27.38  ? 496 HOH A O   1 
HETATM 4908 O O   . HOH C 2 .   ? 20.996  -3.600  34.984  1.00 42.10  ? 497 HOH A O   1 
HETATM 4909 O O   . HOH C 2 .   ? -21.664 11.929  10.295  1.00 58.89  ? 498 HOH A O   1 
HETATM 4910 O O   . HOH C 2 .   ? -5.594  -0.987  -0.733  1.00 54.50  ? 499 HOH A O   1 
HETATM 4911 O O   . HOH C 2 .   ? 3.481   -4.680  17.387  1.00 32.92  ? 500 HOH A O   1 
HETATM 4912 O O   . HOH C 2 .   ? 6.666   -26.667 13.975  1.00 40.29  ? 501 HOH A O   1 
HETATM 4913 O O   . HOH C 2 .   ? 12.578  -16.449 19.098  1.00 52.86  ? 502 HOH A O   1 
HETATM 4914 O O   . HOH C 2 .   ? -4.410  -15.893 20.303  1.00 40.54  ? 503 HOH A O   1 
HETATM 4915 O O   . HOH C 2 .   ? 22.122  22.876  15.021  1.00 38.88  ? 504 HOH A O   1 
HETATM 4916 O O   . HOH C 2 .   ? 11.916  -12.875 15.310  1.00 46.47  ? 505 HOH A O   1 
HETATM 4917 O O   . HOH C 2 .   ? 16.107  3.967   31.103  1.00 48.48  ? 506 HOH A O   1 
HETATM 4918 O O   . HOH C 2 .   ? 14.297  -6.324  22.292  1.00 47.15  ? 507 HOH A O   1 
HETATM 4919 O O   . HOH C 2 .   ? -8.070  -6.463  18.317  1.00 54.30  ? 508 HOH A O   1 
HETATM 4920 O O   . HOH C 2 .   ? -9.506  5.136   17.393  1.00 37.86  ? 509 HOH A O   1 
HETATM 4921 O O   . HOH C 2 .   ? -6.428  11.257  5.778   1.00 39.62  ? 510 HOH A O   1 
HETATM 4922 O O   . HOH C 2 .   ? -12.167 5.260   16.242  1.00 45.04  ? 511 HOH A O   1 
HETATM 4923 O O   . HOH C 2 .   ? 13.006  23.501  9.440   1.00 44.74  ? 512 HOH A O   1 
HETATM 4924 O O   . HOH C 2 .   ? -1.366  4.839   23.157  1.00 47.02  ? 513 HOH A O   1 
HETATM 4925 O O   . HOH C 2 .   ? 30.393  -7.652  17.647  1.00 54.33  ? 514 HOH A O   1 
HETATM 4926 O O   . HOH C 2 .   ? 18.406  0.922   0.858   1.00 50.50  ? 515 HOH A O   1 
HETATM 4927 O O   . HOH C 2 .   ? 25.660  11.995  15.284  1.00 39.95  ? 516 HOH A O   1 
HETATM 4928 O O   . HOH C 2 .   ? -6.450  -9.251  14.851  1.00 36.52  ? 517 HOH A O   1 
HETATM 4929 O O   . HOH C 2 .   ? 22.742  4.219   4.078   1.00 45.47  ? 518 HOH A O   1 
HETATM 4930 O O   . HOH C 2 .   ? -16.299 7.973   7.627   1.00 47.70  ? 519 HOH A O   1 
HETATM 4931 O O   . HOH C 2 .   ? 16.672  10.857  -3.786  1.00 46.78  ? 520 HOH A O   1 
HETATM 4932 O O   . HOH C 2 .   ? 8.032   2.268   21.128  1.00 28.72  ? 521 HOH A O   1 
HETATM 4933 O O   . HOH C 2 .   ? 25.224  18.653  17.438  1.00 33.47  ? 522 HOH A O   1 
HETATM 4934 O O   . HOH C 2 .   ? 5.728   -26.217 10.713  1.00 45.22  ? 523 HOH A O   1 
HETATM 4935 O O   . HOH C 2 .   ? 25.280  17.942  28.799  1.00 42.82  ? 524 HOH A O   1 
HETATM 4936 O O   . HOH C 2 .   ? 7.724   -10.607 -3.816  1.00 41.78  ? 525 HOH A O   1 
HETATM 4937 O O   . HOH C 2 .   ? 31.859  2.382   22.176  1.00 48.63  ? 526 HOH A O   1 
HETATM 4938 O O   . HOH C 2 .   ? -16.522 -7.829  10.970  1.00 57.76  ? 527 HOH A O   1 
HETATM 4939 O O   . HOH C 2 .   ? -10.589 14.996  18.341  1.00 47.61  ? 528 HOH A O   1 
HETATM 4940 O O   . HOH C 2 .   ? 1.723   -14.565 28.347  1.00 46.74  ? 529 HOH A O   1 
HETATM 4941 O O   . HOH C 2 .   ? 17.959  -4.407  10.861  1.00 40.15  ? 530 HOH A O   1 
HETATM 4942 O O   . HOH C 2 .   ? 8.061   -14.018 23.910  1.00 49.18  ? 531 HOH A O   1 
HETATM 4943 O O   . HOH C 2 .   ? 3.063   12.912  21.126  1.00 46.28  ? 532 HOH A O   1 
HETATM 4944 O O   . HOH C 2 .   ? 20.967  19.965  34.003  1.00 57.49  ? 533 HOH A O   1 
HETATM 4945 O O   . HOH C 2 .   ? -9.739  5.808   20.122  1.00 44.79  ? 534 HOH A O   1 
HETATM 4946 O O   . HOH C 2 .   ? 13.300  20.217  4.102   1.00 43.38  ? 535 HOH A O   1 
HETATM 4947 O O   . HOH C 2 .   ? -1.256  -5.491  -1.570  1.00 48.18  ? 536 HOH A O   1 
HETATM 4948 O O   . HOH C 2 .   ? 0.194   20.937  14.668  1.00 44.41  ? 537 HOH A O   1 
HETATM 4949 O O   . HOH C 2 .   ? 10.834  21.394  8.541   1.00 40.99  ? 538 HOH A O   1 
HETATM 4950 O O   . HOH C 2 .   ? 2.772   10.878  -4.880  1.00 62.84  ? 539 HOH A O   1 
HETATM 4951 O O   . HOH C 2 .   ? 18.008  24.902  21.676  1.00 36.28  ? 540 HOH A O   1 
HETATM 4952 O O   . HOH C 2 .   ? 0.988   0.125   -2.899  1.00 51.58  ? 541 HOH A O   1 
HETATM 4953 O O   . HOH C 2 .   ? -6.283  1.546   2.322   1.00 47.48  ? 542 HOH A O   1 
HETATM 4954 O O   . HOH C 2 .   ? -7.986  22.103  10.562  1.00 48.84  ? 543 HOH A O   1 
HETATM 4955 O O   . HOH C 2 .   ? 12.606  -2.384  15.337  1.00 45.54  ? 544 HOH A O   1 
HETATM 4956 O O   . HOH C 2 .   ? 8.185   -15.125 21.869  1.00 48.34  ? 545 HOH A O   1 
HETATM 4957 O O   . HOH C 2 .   ? -5.039  -4.603  20.777  1.00 51.19  ? 546 HOH A O   1 
HETATM 4958 O O   . HOH C 2 .   ? 19.877  -13.122 25.935  1.00 55.66  ? 547 HOH A O   1 
HETATM 4959 O O   . HOH C 2 .   ? 24.952  13.620  13.404  1.00 43.54  ? 548 HOH A O   1 
HETATM 4960 O O   . HOH C 2 .   ? 4.117   -28.268 9.384   1.00 58.61  ? 549 HOH A O   1 
HETATM 4961 O O   . HOH C 2 .   ? 12.660  -9.817  5.267   1.00 52.84  ? 550 HOH A O   1 
HETATM 4962 O O   . HOH C 2 .   ? 11.253  -8.469  -5.088  1.00 59.51  ? 551 HOH A O   1 
HETATM 4963 O O   . HOH C 2 .   ? 8.802   -13.223 2.280   1.00 45.12  ? 552 HOH A O   1 
HETATM 4964 O O   . HOH C 2 .   ? 30.093  10.903  16.859  1.00 50.81  ? 553 HOH A O   1 
HETATM 4965 O O   . HOH C 2 .   ? -10.251 -1.382  19.059  1.00 45.01  ? 554 HOH A O   1 
HETATM 4966 O O   . HOH C 2 .   ? 0.344   13.445  20.999  1.00 53.88  ? 555 HOH A O   1 
HETATM 4967 O O   . HOH C 2 .   ? 25.356  13.485  5.029   1.00 49.00  ? 556 HOH A O   1 
HETATM 4968 O O   . HOH C 2 .   ? -8.466  2.994   5.838   1.00 38.41  ? 557 HOH A O   1 
HETATM 4969 O O   . HOH C 2 .   ? -1.049  -4.772  -3.643  1.00 49.95  ? 558 HOH A O   1 
HETATM 4970 O O   . HOH C 2 .   ? 18.258  6.626   -3.516  1.00 54.46  ? 559 HOH A O   1 
HETATM 4971 O O   . HOH C 2 .   ? 12.121  -4.619  15.409  1.00 33.43  ? 560 HOH A O   1 
HETATM 4972 O O   . HOH C 2 .   ? 15.953  4.939   -3.094  1.00 51.10  ? 561 HOH A O   1 
HETATM 4973 O O   . HOH C 2 .   ? 6.191   9.787   25.943  1.00 43.60  ? 562 HOH A O   1 
HETATM 4974 O O   . HOH C 2 .   ? -7.116  -21.921 22.858  1.00 48.26  ? 563 HOH A O   1 
HETATM 4975 O O   . HOH C 2 .   ? 4.138   0.589   26.186  1.00 50.60  ? 564 HOH A O   1 
HETATM 4976 O O   . HOH C 2 .   ? 20.572  20.987  13.100  1.00 39.00  ? 565 HOH A O   1 
HETATM 4977 O O   . HOH C 2 .   ? -10.705 17.843  18.479  1.00 53.04  ? 566 HOH A O   1 
HETATM 4978 O O   . HOH C 2 .   ? 3.583   5.677   25.084  1.00 52.65  ? 567 HOH A O   1 
HETATM 4979 O O   . HOH C 2 .   ? 5.398   9.289   28.493  1.00 54.67  ? 568 HOH A O   1 
HETATM 4980 O O   . HOH C 2 .   ? -1.100  -1.501  -3.492  1.00 58.43  ? 569 HOH A O   1 
HETATM 4981 O O   . HOH C 2 .   ? 19.857  9.903   33.232  1.00 53.25  ? 570 HOH A O   1 
HETATM 4982 O O   . HOH C 2 .   ? 17.610  6.300   33.362  1.00 48.76  ? 571 HOH A O   1 
HETATM 4983 O O   . HOH C 2 .   ? -1.422  2.243   24.694  1.00 49.98  ? 572 HOH A O   1 
HETATM 4984 O O   . HOH C 2 .   ? 2.779   -27.659 20.582  1.00 54.09  ? 573 HOH A O   1 
HETATM 4985 O O   . HOH C 2 .   ? 29.687  19.051  19.871  1.00 46.06  ? 574 HOH A O   1 
HETATM 4986 O O   . HOH C 2 .   ? -0.882  8.337   0.369   1.00 51.57  ? 575 HOH A O   1 
HETATM 4987 O O   . HOH C 2 .   ? 8.697   17.180  29.748  1.00 56.60  ? 576 HOH A O   1 
HETATM 4988 O O   . HOH C 2 .   ? -6.148  -10.118 17.613  1.00 53.10  ? 577 HOH A O   1 
HETATM 4989 O O   . HOH C 2 .   ? -6.531  -8.117  19.595  1.00 64.62  ? 578 HOH A O   1 
HETATM 4990 O O   . HOH C 2 .   ? -1.302  -24.185 7.816   1.00 53.10  ? 579 HOH A O   1 
HETATM 4991 O O   . HOH C 2 .   ? 8.194   3.408   23.618  1.00 30.85  ? 580 HOH A O   1 
HETATM 4992 O O   . HOH C 2 .   ? -2.595  1.523   -1.886  1.00 50.50  ? 581 HOH A O   1 
HETATM 4993 O O   . HOH C 2 .   ? 4.690   -2.087  27.393  1.00 61.00  ? 582 HOH A O   1 
HETATM 4994 O O   . HOH C 2 .   ? 27.675  -7.888  27.546  1.00 52.34  ? 583 HOH A O   1 
HETATM 4995 O O   . HOH C 2 .   ? 5.163   19.031  21.840  1.00 39.20  ? 584 HOH A O   1 
HETATM 4996 O O   . HOH C 2 .   ? 28.054  12.573  4.086   1.00 57.74  ? 585 HOH A O   1 
HETATM 4997 O O   . HOH C 2 .   ? 14.240  -7.971  8.440   1.00 57.10  ? 586 HOH A O   1 
HETATM 4998 O O   . HOH C 2 .   ? -5.230  8.708   2.649   1.00 61.25  ? 587 HOH A O   1 
HETATM 4999 O O   . HOH C 2 .   ? 6.549   -14.135 2.737   1.00 53.71  ? 588 HOH A O   1 
HETATM 5000 O O   . HOH C 2 .   ? -0.302  -0.407  24.125  1.00 47.03  ? 589 HOH A O   1 
HETATM 5001 O O   . HOH C 2 .   ? 5.571   14.157  27.178  1.00 55.71  ? 590 HOH A O   1 
HETATM 5002 O O   . HOH C 2 .   ? 13.826  1.624   15.959  1.00 42.37  ? 591 HOH A O   1 
HETATM 5003 O O   . HOH C 2 .   ? 5.843   7.782   24.252  1.00 38.72  ? 592 HOH A O   1 
HETATM 5004 O O   . HOH C 2 .   ? 2.508   17.310  22.299  1.00 63.53  ? 593 HOH A O   1 
HETATM 5005 O O   . HOH C 2 .   ? -1.757  -2.073  23.283  1.00 43.37  ? 594 HOH A O   1 
HETATM 5006 O O   . HOH C 2 .   ? -1.634  5.998   -2.517  1.00 54.25  ? 595 HOH A O   1 
HETATM 5007 O O   . HOH C 2 .   ? 1.122   5.325   24.602  1.00 57.62  ? 596 HOH A O   1 
HETATM 5008 O O   . HOH C 2 .   ? 15.812  8.200   31.644  1.00 46.18  ? 597 HOH A O   1 
HETATM 5009 O O   . HOH C 2 .   ? -4.665  -14.381 18.061  1.00 52.76  ? 598 HOH A O   1 
HETATM 5010 O O   . HOH C 2 .   ? 3.722   15.558  21.240  1.00 44.57  ? 599 HOH A O   1 
HETATM 5011 O O   . HOH C 2 .   ? 12.430  -17.147 16.951  1.00 59.22  ? 600 HOH A O   1 
HETATM 5012 O O   . HOH C 2 .   ? -11.134 13.299  25.198  1.00 61.06  ? 601 HOH A O   1 
HETATM 5013 O O   . HOH C 2 .   ? 4.096   12.906  23.280  1.00 64.24  ? 602 HOH A O   1 
HETATM 5014 O O   . HOH C 2 .   ? -13.943 3.947   17.634  1.00 51.40  ? 603 HOH A O   1 
HETATM 5015 O O   . HOH C 2 .   ? -1.125  3.863   -3.309  1.00 47.10  ? 604 HOH A O   1 
HETATM 5016 O O   . HOH C 2 .   ? -4.167  -2.315  24.478  1.00 50.65  ? 605 HOH A O   1 
HETATM 5017 O O   . HOH D 2 .   ? -9.625  -35.148 5.321   1.00 50.27  ? 401 HOH B O   1 
HETATM 5018 O O   . HOH D 2 .   ? -30.286 -33.713 -26.696 1.00 47.31  ? 402 HOH B O   1 
HETATM 5019 O O   . HOH D 2 .   ? -25.912 -19.793 -33.867 1.00 46.16  ? 403 HOH B O   1 
HETATM 5020 O O   . HOH D 2 .   ? 6.216   -21.354 -12.047 1.00 48.57  ? 404 HOH B O   1 
HETATM 5021 O O   . HOH D 2 .   ? -25.170 -4.909  -9.930  1.00 41.06  ? 405 HOH B O   1 
HETATM 5022 O O   . HOH D 2 .   ? -26.618 -26.955 -31.372 1.00 42.04  ? 406 HOH B O   1 
HETATM 5023 O O   . HOH D 2 .   ? -35.378 -35.937 -15.618 1.00 48.62  ? 407 HOH B O   1 
HETATM 5024 O O   . HOH D 2 .   ? -19.528 -32.928 -1.861  1.00 38.51  ? 408 HOH B O   1 
HETATM 5025 O O   . HOH D 2 .   ? -19.596 -6.280  -18.383 1.00 32.10  ? 409 HOH B O   1 
HETATM 5026 O O   . HOH D 2 .   ? -5.422  -18.694 -27.378 1.00 44.68  ? 410 HOH B O   1 
HETATM 5027 O O   . HOH D 2 .   ? -33.361 -37.139 -5.469  1.00 52.17  ? 411 HOH B O   1 
HETATM 5028 O O   . HOH D 2 .   ? -28.194 -17.037 -28.398 1.00 41.56  ? 412 HOH B O   1 
HETATM 5029 O O   . HOH D 2 .   ? -3.178  -30.348 5.293   1.00 45.05  ? 413 HOH B O   1 
HETATM 5030 O O   . HOH D 2 .   ? 4.506   -20.648 -15.874 1.00 43.12  ? 414 HOH B O   1 
HETATM 5031 O O   . HOH D 2 .   ? -9.857  -22.146 -15.338 1.00 28.43  ? 415 HOH B O   1 
HETATM 5032 O O   . HOH D 2 .   ? -14.345 -22.796 -25.036 1.00 32.45  ? 416 HOH B O   1 
HETATM 5033 O O   . HOH D 2 .   ? -20.770 -24.934 -6.925  1.00 34.60  ? 417 HOH B O   1 
HETATM 5034 O O   . HOH D 2 .   ? -18.712 -27.758 5.105   1.00 54.67  ? 418 HOH B O   1 
HETATM 5035 O O   . HOH D 2 .   ? -14.391 -15.031 -2.929  1.00 30.31  ? 419 HOH B O   1 
HETATM 5036 O O   . HOH D 2 .   ? -5.994  -7.548  -25.308 1.00 39.37  ? 420 HOH B O   1 
HETATM 5037 O O   . HOH D 2 .   ? -20.966 -21.544 -26.623 1.00 28.28  ? 421 HOH B O   1 
HETATM 5038 O O   . HOH D 2 .   ? -3.437  -30.120 -1.994  1.00 47.18  ? 422 HOH B O   1 
HETATM 5039 O O   . HOH D 2 .   ? -13.683 -19.863 -23.160 1.00 36.06  ? 423 HOH B O   1 
HETATM 5040 O O   . HOH D 2 .   ? -13.992 -29.969 -11.276 1.00 35.01  ? 424 HOH B O   1 
HETATM 5041 O O   . HOH D 2 .   ? -35.750 -16.195 -18.470 1.00 51.57  ? 425 HOH B O   1 
HETATM 5042 O O   . HOH D 2 .   ? -40.885 -17.354 -2.263  1.00 55.99  ? 426 HOH B O   1 
HETATM 5043 O O   . HOH D 2 .   ? -13.316 -12.565 -30.368 1.00 42.87  ? 427 HOH B O   1 
HETATM 5044 O O   . HOH D 2 .   ? -20.440 -1.016  -4.824  1.00 47.75  ? 428 HOH B O   1 
HETATM 5045 O O   . HOH D 2 .   ? -9.593  -33.856 -2.302  1.00 42.33  ? 429 HOH B O   1 
HETATM 5046 O O   . HOH D 2 .   ? -10.483 -2.009  -7.350  1.00 40.77  ? 430 HOH B O   1 
HETATM 5047 O O   . HOH D 2 .   ? -16.173 -33.651 -5.102  1.00 39.18  ? 431 HOH B O   1 
HETATM 5048 O O   . HOH D 2 .   ? -16.237 1.044   -2.456  1.00 58.20  ? 432 HOH B O   1 
HETATM 5049 O O   . HOH D 2 .   ? -1.273  -11.141 -0.777  1.00 33.81  ? 433 HOH B O   1 
HETATM 5050 O O   . HOH D 2 .   ? -30.959 -20.539 -4.994  1.00 33.84  ? 434 HOH B O   1 
HETATM 5051 O O   . HOH D 2 .   ? -24.139 -37.118 -14.120 1.00 37.74  ? 435 HOH B O   1 
HETATM 5052 O O   . HOH D 2 .   ? -32.161 -32.234 -10.801 1.00 38.82  ? 436 HOH B O   1 
HETATM 5053 O O   . HOH D 2 .   ? -31.025 -19.462 -29.310 1.00 45.91  ? 437 HOH B O   1 
HETATM 5054 O O   . HOH D 2 .   ? -3.838  -10.209 -0.011  1.00 36.86  ? 438 HOH B O   1 
HETATM 5055 O O   . HOH D 2 .   ? -18.797 -31.592 -25.366 1.00 33.91  ? 439 HOH B O   1 
HETATM 5056 O O   . HOH D 2 .   ? 6.365   -18.231 -23.781 1.00 51.50  ? 440 HOH B O   1 
HETATM 5057 O O   . HOH D 2 .   ? -17.972 -15.903 -5.837  1.00 39.46  ? 441 HOH B O   1 
HETATM 5058 O O   . HOH D 2 .   ? -14.150 -27.735 -21.416 1.00 41.09  ? 442 HOH B O   1 
HETATM 5059 O O   . HOH D 2 .   ? -15.497 -12.293 -18.715 1.00 26.34  ? 443 HOH B O   1 
HETATM 5060 O O   . HOH D 2 .   ? -12.893 -24.948 -16.600 1.00 35.93  ? 444 HOH B O   1 
HETATM 5061 O O   . HOH D 2 .   ? -3.202  -8.381  -15.012 1.00 36.74  ? 445 HOH B O   1 
HETATM 5062 O O   . HOH D 2 .   ? -20.575 -33.966 -8.242  1.00 30.59  ? 446 HOH B O   1 
HETATM 5063 O O   . HOH D 2 .   ? -14.845 -7.323  -10.165 1.00 27.54  ? 447 HOH B O   1 
HETATM 5064 O O   . HOH D 2 .   ? 2.492   -10.441 -10.066 1.00 37.36  ? 448 HOH B O   1 
HETATM 5065 O O   . HOH D 2 .   ? -26.210 -9.258  -4.467  1.00 44.80  ? 449 HOH B O   1 
HETATM 5066 O O   . HOH D 2 .   ? -27.304 -37.890 -16.823 1.00 38.55  ? 450 HOH B O   1 
HETATM 5067 O O   . HOH D 2 .   ? -19.108 -38.489 -11.125 1.00 37.33  ? 451 HOH B O   1 
HETATM 5068 O O   . HOH D 2 .   ? -26.661 -36.915 -19.199 1.00 35.76  ? 452 HOH B O   1 
HETATM 5069 O O   . HOH D 2 .   ? -2.783  -13.968 -29.998 1.00 48.79  ? 453 HOH B O   1 
HETATM 5070 O O   . HOH D 2 .   ? -14.046 -10.326 -14.359 1.00 26.16  ? 454 HOH B O   1 
HETATM 5071 O O   . HOH D 2 .   ? -1.745  -12.191 -9.746  1.00 32.42  ? 455 HOH B O   1 
HETATM 5072 O O   . HOH D 2 .   ? -7.701  -4.512  -4.224  1.00 38.10  ? 456 HOH B O   1 
HETATM 5073 O O   . HOH D 2 .   ? -3.624  -6.089  -18.774 1.00 45.07  ? 457 HOH B O   1 
HETATM 5074 O O   . HOH D 2 .   ? -33.890 -29.389 -1.589  1.00 59.97  ? 458 HOH B O   1 
HETATM 5075 O O   . HOH D 2 .   ? -25.094 -24.036 -1.888  1.00 50.48  ? 459 HOH B O   1 
HETATM 5076 O O   . HOH D 2 .   ? -3.171  -27.196 7.334   1.00 42.78  ? 460 HOH B O   1 
HETATM 5077 O O   . HOH D 2 .   ? -13.406 -0.873  -18.384 1.00 49.48  ? 461 HOH B O   1 
HETATM 5078 O O   . HOH D 2 .   ? -6.743  -26.882 -13.928 1.00 46.03  ? 462 HOH B O   1 
HETATM 5079 O O   . HOH D 2 .   ? -37.733 -25.142 0.946   1.00 54.60  ? 463 HOH B O   1 
HETATM 5080 O O   . HOH D 2 .   ? -1.822  -28.718 16.414  1.00 44.35  ? 464 HOH B O   1 
HETATM 5081 O O   . HOH D 2 .   ? -9.424  -24.523 -1.947  1.00 32.51  ? 465 HOH B O   1 
HETATM 5082 O O   . HOH D 2 .   ? -11.600 1.203   -15.148 1.00 55.03  ? 466 HOH B O   1 
HETATM 5083 O O   . HOH D 2 .   ? -17.497 -19.995 -8.460  1.00 35.91  ? 467 HOH B O   1 
HETATM 5084 O O   . HOH D 2 .   ? -19.613 -16.987 -10.900 1.00 32.45  ? 468 HOH B O   1 
HETATM 5085 O O   . HOH D 2 .   ? -21.044 -25.859 -3.081  1.00 45.76  ? 469 HOH B O   1 
HETATM 5086 O O   . HOH D 2 .   ? -30.967 -36.294 -22.291 1.00 43.68  ? 470 HOH B O   1 
HETATM 5087 O O   . HOH D 2 .   ? -33.796 -21.302 -25.718 1.00 42.28  ? 471 HOH B O   1 
HETATM 5088 O O   . HOH D 2 .   ? -37.393 -25.054 -6.693  1.00 48.04  ? 472 HOH B O   1 
HETATM 5089 O O   . HOH D 2 .   ? -11.402 -22.979 -3.284  1.00 30.02  ? 473 HOH B O   1 
HETATM 5090 O O   . HOH D 2 .   ? -2.720  -8.749  -17.812 1.00 35.35  ? 474 HOH B O   1 
HETATM 5091 O O   . HOH D 2 .   ? 2.928   -24.801 -21.531 1.00 47.77  ? 475 HOH B O   1 
HETATM 5092 O O   . HOH D 2 .   ? 1.211   -10.041 -25.936 1.00 48.63  ? 476 HOH B O   1 
HETATM 5093 O O   . HOH D 2 .   ? -7.139  -21.082 -28.336 1.00 57.43  ? 477 HOH B O   1 
HETATM 5094 O O   . HOH D 2 .   ? -37.434 -25.739 -21.228 1.00 47.71  ? 478 HOH B O   1 
HETATM 5095 O O   . HOH D 2 .   ? -32.961 -17.582 -20.903 1.00 47.06  ? 479 HOH B O   1 
HETATM 5096 O O   . HOH D 2 .   ? -34.173 -20.152 -19.117 1.00 42.31  ? 480 HOH B O   1 
HETATM 5097 O O   . HOH D 2 .   ? -17.489 -13.731 -17.532 1.00 27.51  ? 481 HOH B O   1 
HETATM 5098 O O   . HOH D 2 .   ? -1.831  -23.358 -4.725  1.00 36.59  ? 482 HOH B O   1 
HETATM 5099 O O   . HOH D 2 .   ? -27.915 -16.690 -0.752  1.00 47.18  ? 483 HOH B O   1 
HETATM 5100 O O   . HOH D 2 .   ? -36.440 -20.306 -17.846 1.00 44.85  ? 484 HOH B O   1 
HETATM 5101 O O   . HOH D 2 .   ? 3.923   -19.578 -13.343 1.00 35.36  ? 485 HOH B O   1 
HETATM 5102 O O   . HOH D 2 .   ? -11.269 -21.242 -22.594 1.00 38.65  ? 486 HOH B O   1 
HETATM 5103 O O   . HOH D 2 .   ? -0.711  -23.309 -7.165  1.00 33.52  ? 487 HOH B O   1 
HETATM 5104 O O   . HOH D 2 .   ? -37.078 -34.716 -14.300 1.00 58.77  ? 488 HOH B O   1 
HETATM 5105 O O   . HOH D 2 .   ? -12.496 -29.312 -24.665 1.00 55.89  ? 489 HOH B O   1 
HETATM 5106 O O   . HOH D 2 .   ? -35.134 -25.285 -8.184  1.00 40.64  ? 490 HOH B O   1 
HETATM 5107 O O   . HOH D 2 .   ? -15.592 -35.033 -23.715 1.00 38.10  ? 491 HOH B O   1 
HETATM 5108 O O   . HOH D 2 .   ? -11.164 -2.483  -19.692 1.00 38.22  ? 492 HOH B O   1 
HETATM 5109 O O   . HOH D 2 .   ? -12.265 -11.373 -27.804 1.00 41.35  ? 493 HOH B O   1 
HETATM 5110 O O   . HOH D 2 .   ? -18.628 -22.144 2.805   1.00 48.63  ? 494 HOH B O   1 
HETATM 5111 O O   . HOH D 2 .   ? -7.323  -6.816  -13.187 1.00 37.93  ? 495 HOH B O   1 
HETATM 5112 O O   . HOH D 2 .   ? -27.067 -41.293 -6.463  1.00 49.71  ? 496 HOH B O   1 
HETATM 5113 O O   . HOH D 2 .   ? 1.298   -21.006 -13.167 1.00 32.40  ? 497 HOH B O   1 
HETATM 5114 O O   . HOH D 2 .   ? -29.232 -41.309 -11.352 1.00 46.55  ? 498 HOH B O   1 
HETATM 5115 O O   . HOH D 2 .   ? -7.422  -4.548  0.241   1.00 40.45  ? 499 HOH B O   1 
HETATM 5116 O O   . HOH D 2 .   ? -37.047 -9.175  -14.112 1.00 51.92  ? 500 HOH B O   1 
HETATM 5117 O O   . HOH D 2 .   ? -23.657 -0.066  -14.208 1.00 46.10  ? 501 HOH B O   1 
HETATM 5118 O O   . HOH D 2 .   ? -3.756  -27.963 19.774  1.00 46.37  ? 502 HOH B O   1 
HETATM 5119 O O   . HOH D 2 .   ? -20.291 -20.455 13.131  1.00 58.28  ? 503 HOH B O   1 
HETATM 5120 O O   . HOH D 2 .   ? -9.253  -12.331 -27.428 1.00 39.40  ? 504 HOH B O   1 
HETATM 5121 O O   . HOH D 2 .   ? -15.892 -26.619 -32.097 1.00 54.99  ? 505 HOH B O   1 
HETATM 5122 O O   . HOH D 2 .   ? -10.114 -29.050 -8.235  1.00 33.83  ? 506 HOH B O   1 
HETATM 5123 O O   . HOH D 2 .   ? -26.804 -7.399  -21.330 1.00 46.08  ? 507 HOH B O   1 
HETATM 5124 O O   . HOH D 2 .   ? -3.760  -27.520 -20.560 1.00 43.57  ? 508 HOH B O   1 
HETATM 5125 O O   . HOH D 2 .   ? -16.854 -33.580 -19.311 1.00 36.99  ? 509 HOH B O   1 
HETATM 5126 O O   . HOH D 2 .   ? -24.907 -27.136 -8.857  1.00 38.01  ? 510 HOH B O   1 
HETATM 5127 O O   . HOH D 2 .   ? 0.646   -27.355 -16.163 1.00 46.58  ? 511 HOH B O   1 
HETATM 5128 O O   . HOH D 2 .   ? -10.048 -12.809 -1.695  1.00 27.26  ? 512 HOH B O   1 
HETATM 5129 O O   . HOH D 2 .   ? -32.731 -8.051  -19.263 1.00 44.34  ? 513 HOH B O   1 
HETATM 5130 O O   . HOH D 2 .   ? -12.025 -13.904 -3.500  1.00 27.94  ? 514 HOH B O   1 
HETATM 5131 O O   . HOH D 2 .   ? -27.952 -11.772 -24.066 1.00 37.72  ? 515 HOH B O   1 
HETATM 5132 O O   . HOH D 2 .   ? -21.851 -26.296 -31.851 1.00 42.83  ? 516 HOH B O   1 
HETATM 5133 O O   . HOH D 2 .   ? 0.696   -18.641 -27.042 1.00 51.71  ? 517 HOH B O   1 
HETATM 5134 O O   . HOH D 2 .   ? -10.943 -23.884 -21.172 1.00 42.77  ? 518 HOH B O   1 
HETATM 5135 O O   . HOH D 2 .   ? 5.859   -11.372 -20.920 1.00 45.53  ? 519 HOH B O   1 
HETATM 5136 O O   . HOH D 2 .   ? -26.177 -17.818 -2.337  1.00 39.95  ? 520 HOH B O   1 
HETATM 5137 O O   . HOH D 2 .   ? -15.850 -25.988 -10.465 1.00 27.43  ? 521 HOH B O   1 
HETATM 5138 O O   . HOH D 2 .   ? -33.724 -14.237 -18.027 1.00 43.01  ? 522 HOH B O   1 
HETATM 5139 O O   . HOH D 2 .   ? -11.115 -30.326 -12.895 1.00 59.93  ? 523 HOH B O   1 
HETATM 5140 O O   . HOH D 2 .   ? -39.539 -28.606 -10.426 1.00 50.19  ? 524 HOH B O   1 
HETATM 5141 O O   . HOH D 2 .   ? -5.305  -26.198 -27.649 1.00 47.31  ? 525 HOH B O   1 
HETATM 5142 O O   . HOH D 2 .   ? -23.108 -32.766 -26.471 1.00 38.71  ? 526 HOH B O   1 
HETATM 5143 O O   . HOH D 2 .   ? -0.568  -12.326 -28.716 1.00 42.95  ? 527 HOH B O   1 
HETATM 5144 O O   . HOH D 2 .   ? -15.364 -26.125 -28.243 1.00 35.93  ? 528 HOH B O   1 
HETATM 5145 O O   . HOH D 2 .   ? -15.803 -28.056 -14.905 1.00 29.22  ? 529 HOH B O   1 
HETATM 5146 O O   . HOH D 2 .   ? -26.613 -40.509 1.013   1.00 51.69  ? 530 HOH B O   1 
HETATM 5147 O O   . HOH D 2 .   ? -27.748 -7.860  -6.111  1.00 47.37  ? 531 HOH B O   1 
HETATM 5148 O O   . HOH D 2 .   ? -24.688 -29.817 -3.431  1.00 45.01  ? 532 HOH B O   1 
HETATM 5149 O O   . HOH D 2 .   ? -6.005  -26.849 -4.171  1.00 38.04  ? 533 HOH B O   1 
HETATM 5150 O O   . HOH D 2 .   ? -18.698 -4.264  5.147   1.00 50.15  ? 534 HOH B O   1 
HETATM 5151 O O   . HOH D 2 .   ? -23.714 2.032   -17.172 1.00 54.71  ? 535 HOH B O   1 
HETATM 5152 O O   . HOH D 2 .   ? -18.886 -16.457 -8.588  1.00 39.10  ? 536 HOH B O   1 
HETATM 5153 O O   . HOH D 2 .   ? 2.163   -17.112 -24.863 1.00 45.32  ? 537 HOH B O   1 
HETATM 5154 O O   . HOH D 2 .   ? -20.575 -25.867 -0.387  1.00 53.24  ? 538 HOH B O   1 
HETATM 5155 O O   . HOH D 2 .   ? -26.550 -0.727  -15.870 1.00 46.49  ? 539 HOH B O   1 
HETATM 5156 O O   . HOH D 2 .   ? -0.541  -8.280  -7.225  1.00 42.31  ? 540 HOH B O   1 
HETATM 5157 O O   . HOH D 2 .   ? 1.551   -23.580 -14.352 1.00 35.57  ? 541 HOH B O   1 
HETATM 5158 O O   . HOH D 2 .   ? -8.285  -3.751  -14.405 1.00 51.96  ? 542 HOH B O   1 
HETATM 5159 O O   . HOH D 2 .   ? -13.529 -19.737 19.061  1.00 52.29  ? 543 HOH B O   1 
HETATM 5160 O O   . HOH D 2 .   ? -14.300 -22.865 19.200  1.00 51.14  ? 544 HOH B O   1 
HETATM 5161 O O   . HOH D 2 .   ? -13.290 3.087   -14.017 1.00 45.70  ? 545 HOH B O   1 
HETATM 5162 O O   . HOH D 2 .   ? -5.754  -25.000 20.631  1.00 46.11  ? 546 HOH B O   1 
HETATM 5163 O O   . HOH D 2 .   ? -35.959 -34.162 -10.499 1.00 46.43  ? 547 HOH B O   1 
HETATM 5164 O O   . HOH D 2 .   ? -32.948 -32.643 -26.380 1.00 44.76  ? 548 HOH B O   1 
HETATM 5165 O O   . HOH D 2 .   ? -22.287 -6.850  -26.276 1.00 45.99  ? 549 HOH B O   1 
HETATM 5166 O O   . HOH D 2 .   ? -9.003  -16.637 -28.373 1.00 40.56  ? 550 HOH B O   1 
HETATM 5167 O O   . HOH D 2 .   ? -35.740 -31.378 -7.388  1.00 52.36  ? 551 HOH B O   1 
HETATM 5168 O O   . HOH D 2 .   ? -9.011  -14.467 -28.965 1.00 54.19  ? 552 HOH B O   1 
HETATM 5169 O O   . HOH D 2 .   ? -1.700  -23.477 2.090   1.00 56.00  ? 553 HOH B O   1 
HETATM 5170 O O   . HOH D 2 .   ? -2.846  -6.839  -7.617  1.00 43.84  ? 554 HOH B O   1 
HETATM 5171 O O   . HOH D 2 .   ? -13.390 -33.233 -7.511  1.00 44.52  ? 555 HOH B O   1 
HETATM 5172 O O   . HOH D 2 .   ? -9.959  -24.503 -16.685 1.00 38.56  ? 556 HOH B O   1 
HETATM 5173 O O   . HOH D 2 .   ? -16.293 -28.954 6.756   1.00 51.81  ? 557 HOH B O   1 
HETATM 5174 O O   . HOH D 2 .   ? -17.142 2.638   -19.857 1.00 67.34  ? 558 HOH B O   1 
HETATM 5175 O O   . HOH D 2 .   ? -16.480 -3.172  6.179   1.00 41.73  ? 559 HOH B O   1 
HETATM 5176 O O   . HOH D 2 .   ? -33.599 -34.014 -29.263 1.00 54.29  ? 560 HOH B O   1 
HETATM 5177 O O   . HOH D 2 .   ? -24.645 -38.361 -16.695 1.00 36.27  ? 561 HOH B O   1 
HETATM 5178 O O   . HOH D 2 .   ? -28.314 -42.215 -13.143 1.00 49.13  ? 562 HOH B O   1 
HETATM 5179 O O   . HOH D 2 .   ? 5.587   -9.182  -13.774 1.00 46.06  ? 563 HOH B O   1 
HETATM 5180 O O   . HOH D 2 .   ? -20.887 -20.547 -7.412  1.00 47.82  ? 564 HOH B O   1 
HETATM 5181 O O   . HOH D 2 .   ? 1.979   -23.745 -7.024  1.00 45.10  ? 565 HOH B O   1 
HETATM 5182 O O   . HOH D 2 .   ? -33.466 -2.300  -9.489  1.00 58.89  ? 566 HOH B O   1 
HETATM 5183 O O   . HOH D 2 .   ? -34.828 -9.768  -18.536 1.00 51.50  ? 567 HOH B O   1 
HETATM 5184 O O   . HOH D 2 .   ? -22.844 -4.429  5.050   1.00 57.33  ? 568 HOH B O   1 
HETATM 5185 O O   . HOH D 2 .   ? -10.514 -33.462 -4.748  1.00 52.35  ? 569 HOH B O   1 
HETATM 5186 O O   . HOH D 2 .   ? -8.489  -24.118 -21.599 1.00 55.44  ? 570 HOH B O   1 
HETATM 5187 O O   . HOH D 2 .   ? -14.591 -29.945 -26.612 1.00 55.69  ? 571 HOH B O   1 
HETATM 5188 O O   . HOH D 2 .   ? -7.957  -2.099  -0.063  1.00 47.02  ? 572 HOH B O   1 
HETATM 5189 O O   . HOH D 2 .   ? 3.264   -9.932  -12.689 1.00 52.03  ? 573 HOH B O   1 
HETATM 5190 O O   . HOH D 2 .   ? -19.556 -33.186 -23.259 1.00 36.74  ? 574 HOH B O   1 
HETATM 5191 O O   . HOH D 2 .   ? -0.136  -9.813  -9.509  1.00 33.60  ? 575 HOH B O   1 
HETATM 5192 O O   . HOH D 2 .   ? -15.839 -28.097 -12.103 1.00 29.74  ? 576 HOH B O   1 
HETATM 5193 O O   . HOH D 2 .   ? -7.456  -16.576 18.354  1.00 49.20  ? 577 HOH B O   1 
HETATM 5194 O O   . HOH D 2 .   ? -11.026 -28.669 -14.504 1.00 48.22  ? 578 HOH B O   1 
HETATM 5195 O O   . HOH D 2 .   ? -12.503 -25.718 -19.253 1.00 51.02  ? 579 HOH B O   1 
HETATM 5196 O O   . HOH D 2 .   ? -6.532  -28.850 -11.500 1.00 44.14  ? 580 HOH B O   1 
HETATM 5197 O O   . HOH D 2 .   ? -13.659 -29.385 -18.837 1.00 47.96  ? 581 HOH B O   1 
HETATM 5198 O O   . HOH D 2 .   ? -0.316  -8.776  -17.020 1.00 46.33  ? 582 HOH B O   1 
HETATM 5199 O O   . HOH D 2 .   ? -18.491 -28.936 7.319   1.00 68.47  ? 583 HOH B O   1 
HETATM 5200 O O   . HOH D 2 .   ? -13.669 -24.220 -27.429 1.00 42.92  ? 584 HOH B O   1 
HETATM 5201 O O   . HOH D 2 .   ? -31.884 -15.754 -20.097 1.00 47.10  ? 585 HOH B O   1 
HETATM 5202 O O   . HOH D 2 .   ? -14.458 -28.345 -28.970 1.00 48.58  ? 586 HOH B O   1 
HETATM 5203 O O   . HOH D 2 .   ? -1.043  -25.282 0.023   1.00 55.39  ? 587 HOH B O   1 
HETATM 5204 O O   . HOH D 2 .   ? -11.669 -31.420 -10.047 1.00 50.46  ? 588 HOH B O   1 
HETATM 5205 O O   . HOH D 2 .   ? -20.587 -3.013  4.871   1.00 59.21  ? 589 HOH B O   1 
HETATM 5206 O O   . HOH D 2 .   ? -22.098 -21.416 -9.130  1.00 40.74  ? 590 HOH B O   1 
HETATM 5207 O O   . HOH D 2 .   ? -3.610  -27.508 -2.731  1.00 57.71  ? 591 HOH B O   1 
HETATM 5208 O O   . HOH D 2 .   ? -33.204 -20.154 -28.191 1.00 46.07  ? 592 HOH B O   1 
HETATM 5209 O O   . HOH D 2 .   ? -19.804 -28.333 -33.053 1.00 54.28  ? 593 HOH B O   1 
HETATM 5210 O O   . HOH D 2 .   ? 2.061   -20.674 -25.871 1.00 55.33  ? 594 HOH B O   1 
HETATM 5211 O O   . HOH D 2 .   ? -11.798 -30.955 -18.307 1.00 61.92  ? 595 HOH B O   1 
HETATM 5212 O O   . HOH D 2 .   ? -20.885 -31.435 -27.219 1.00 39.67  ? 596 HOH B O   1 
HETATM 5213 O O   . HOH D 2 .   ? -13.659 -27.735 -16.221 1.00 32.28  ? 597 HOH B O   1 
HETATM 5214 O O   . HOH D 2 .   ? -35.929 -29.896 -3.084  1.00 59.70  ? 598 HOH B O   1 
HETATM 5215 O O   . HOH D 2 .   ? -5.662  -28.179 -6.609  1.00 41.27  ? 599 HOH B O   1 
HETATM 5216 O O   . HOH D 2 .   ? -34.222 -12.155 -19.668 1.00 46.81  ? 600 HOH B O   1 
HETATM 5217 O O   . HOH D 2 .   ? -7.280  -28.881 -8.614  1.00 43.78  ? 601 HOH B O   1 
HETATM 5218 O O   . HOH D 2 .   ? -29.012 -8.265  -22.193 1.00 48.83  ? 602 HOH B O   1 
HETATM 5219 O O   . HOH D 2 .   ? -29.025 -41.451 -15.203 1.00 54.96  ? 603 HOH B O   1 
HETATM 5220 O O   . HOH D 2 .   ? -8.257  -1.166  -8.456  1.00 48.03  ? 604 HOH B O   1 
HETATM 5221 O O   . HOH D 2 .   ? -24.003 -26.048 -32.488 1.00 47.51  ? 605 HOH B O   1 
HETATM 5222 O O   . HOH D 2 .   ? -7.525  -1.323  -10.888 1.00 62.31  ? 606 HOH B O   1 
HETATM 5223 O O   . HOH D 2 .   ? -11.803 -23.493 -23.863 1.00 40.30  ? 607 HOH B O   1 
HETATM 5224 O O   . HOH D 2 .   ? -27.904 -40.466 -17.679 1.00 43.02  ? 608 HOH B O   1 
HETATM 5225 O O   . HOH D 2 .   ? -16.292 -11.959 -34.725 1.00 53.18  ? 609 HOH B O   1 
HETATM 5226 O O   . HOH D 2 .   ? -2.932  -24.842 6.292   1.00 50.31  ? 610 HOH B O   1 
HETATM 5227 O O   . HOH D 2 .   ? -20.270 -27.793 8.353   1.00 67.91  ? 611 HOH B O   1 
HETATM 5228 O O   . HOH D 2 .   ? -2.186  -25.346 3.657   1.00 53.38  ? 612 HOH B O   1 
HETATM 5229 O O   . HOH D 2 .   ? -20.078 -32.160 -29.619 1.00 44.03  ? 613 HOH B O   1 
# 
