data_9UPA
# 
_entry.id   9UPA 
# 
_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   9UPA         pdb_00009upa 10.2210/pdb9upa/pdb 
WWPDB D_1300058949 ?            ?                   
# 
_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                        9UPA 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-28 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 2684195429@qq.com   panpan Dong ? 'principal investigator/group leader' 0000-0003-0449-0345 
3 porterlu@zju.edu.cn Peng   Lu   ? 'principal investigator/group leader' 0000-0002-1405-5294 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, P.P.' 1 0000-0003-0449-0345 
'Lu, P.'     2 0000-0002-1405-5294 
# 
_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                     'Improved thermostability of a GH10 xylanase based on its X-ray crystal structure' 
_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 'Dong, P.P.' 1 ? 
primary 'Lu, P.'     2 ? 
# 
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 Beta-xylanase 39489.535 2  3.2.1.8 ? ? ? 
2 water   nat water         18.015    81 ?       ? ? ? 
# 
_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       
;PALKDLAKAKGMRFGSAIGLLEDQDTRKSFRDPAYRALMARECNMIVAENETKWQALQPKPGPYQWGPADEMFAWARKEG
MAIRGHALIWQDPKWLPAWVNALDLKSKPVAHAEAILREHAKTVCTHLKDVISHDVVNEAVSPKDGSLIQNVFTKRMGAV
EQIEFAFRQAHEHAPKAQLVYNDFMGPGLGDRAKHRAGVLKLLAELKKRGAPIHALGLQSHISAGDMMSGPANAAVLREW
RKFLDEVTGMGLDLLITEFDVNDKAFPADFAKRDAATAALARDYLDVTLSYPTCRDFLLWGMADHVNWLQVWPDAKRPDG
LAQRPTPYDSQLRPKPMREAIAASLRAMPMRKA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PALKDLAKAKGMRFGSAIGLLEDQDTRKSFRDPAYRALMARECNMIVAENETKWQALQPKPGPYQWGPADEMFAWARKEG
MAIRGHALIWQDPKWLPAWVNALDLKSKPVAHAEAILREHAKTVCTHLKDVISHDVVNEAVSPKDGSLIQNVFTKRMGAV
EQIEFAFRQAHEHAPKAQLVYNDFMGPGLGDRAKHRAGVLKLLAELKKRGAPIHALGLQSHISAGDMMSGPANAAVLREW
RKFLDEVTGMGLDLLITEFDVNDKAFPADFAKRDAATAALARDYLDVTLSYPTCRDFLLWGMADHVNWLQVWPDAKRPDG
LAQRPTPYDSQLRPKPMREAIAASLRAMPMRKA
;
_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   PRO n 
1 2   ALA n 
1 3   LEU n 
1 4   LYS n 
1 5   ASP n 
1 6   LEU n 
1 7   ALA n 
1 8   LYS n 
1 9   ALA n 
1 10  LYS n 
1 11  GLY n 
1 12  MET n 
1 13  ARG n 
1 14  PHE n 
1 15  GLY n 
1 16  SER n 
1 17  ALA n 
1 18  ILE n 
1 19  GLY n 
1 20  LEU n 
1 21  LEU n 
1 22  GLU n 
1 23  ASP n 
1 24  GLN n 
1 25  ASP n 
1 26  THR n 
1 27  ARG n 
1 28  LYS n 
1 29  SER n 
1 30  PHE n 
1 31  ARG n 
1 32  ASP n 
1 33  PRO n 
1 34  ALA n 
1 35  TYR n 
1 36  ARG n 
1 37  ALA n 
1 38  LEU n 
1 39  MET n 
1 40  ALA n 
1 41  ARG n 
1 42  GLU n 
1 43  CYS n 
1 44  ASN n 
1 45  MET n 
1 46  ILE n 
1 47  VAL n 
1 48  ALA n 
1 49  GLU n 
1 50  ASN n 
1 51  GLU n 
1 52  THR n 
1 53  LYS n 
1 54  TRP n 
1 55  GLN n 
1 56  ALA n 
1 57  LEU n 
1 58  GLN n 
1 59  PRO n 
1 60  LYS n 
1 61  PRO n 
1 62  GLY n 
1 63  PRO n 
1 64  TYR n 
1 65  GLN n 
1 66  TRP n 
1 67  GLY n 
1 68  PRO n 
1 69  ALA n 
1 70  ASP n 
1 71  GLU n 
1 72  MET n 
1 73  PHE n 
1 74  ALA n 
1 75  TRP n 
1 76  ALA n 
1 77  ARG n 
1 78  LYS n 
1 79  GLU n 
1 80  GLY n 
1 81  MET n 
1 82  ALA n 
1 83  ILE n 
1 84  ARG n 
1 85  GLY n 
1 86  HIS n 
1 87  ALA n 
1 88  LEU n 
1 89  ILE n 
1 90  TRP n 
1 91  GLN n 
1 92  ASP n 
1 93  PRO n 
1 94  LYS n 
1 95  TRP n 
1 96  LEU n 
1 97  PRO n 
1 98  ALA n 
1 99  TRP n 
1 100 VAL n 
1 101 ASN n 
1 102 ALA n 
1 103 LEU n 
1 104 ASP n 
1 105 LEU n 
1 106 LYS n 
1 107 SER n 
1 108 LYS n 
1 109 PRO n 
1 110 VAL n 
1 111 ALA n 
1 112 HIS n 
1 113 ALA n 
1 114 GLU n 
1 115 ALA n 
1 116 ILE n 
1 117 LEU n 
1 118 ARG n 
1 119 GLU n 
1 120 HIS n 
1 121 ALA n 
1 122 LYS n 
1 123 THR n 
1 124 VAL n 
1 125 CYS n 
1 126 THR n 
1 127 HIS n 
1 128 LEU n 
1 129 LYS n 
1 130 ASP n 
1 131 VAL n 
1 132 ILE n 
1 133 SER n 
1 134 HIS n 
1 135 ASP n 
1 136 VAL n 
1 137 VAL n 
1 138 ASN n 
1 139 GLU n 
1 140 ALA n 
1 141 VAL n 
1 142 SER n 
1 143 PRO n 
1 144 LYS n 
1 145 ASP n 
1 146 GLY n 
1 147 SER n 
1 148 LEU n 
1 149 ILE n 
1 150 GLN n 
1 151 ASN n 
1 152 VAL n 
1 153 PHE n 
1 154 THR n 
1 155 LYS n 
1 156 ARG n 
1 157 MET n 
1 158 GLY n 
1 159 ALA n 
1 160 VAL n 
1 161 GLU n 
1 162 GLN n 
1 163 ILE n 
1 164 GLU n 
1 165 PHE n 
1 166 ALA n 
1 167 PHE n 
1 168 ARG n 
1 169 GLN n 
1 170 ALA n 
1 171 HIS n 
1 172 GLU n 
1 173 HIS n 
1 174 ALA n 
1 175 PRO n 
1 176 LYS n 
1 177 ALA n 
1 178 GLN n 
1 179 LEU n 
1 180 VAL n 
1 181 TYR n 
1 182 ASN n 
1 183 ASP n 
1 184 PHE n 
1 185 MET n 
1 186 GLY n 
1 187 PRO n 
1 188 GLY n 
1 189 LEU n 
1 190 GLY n 
1 191 ASP n 
1 192 ARG n 
1 193 ALA n 
1 194 LYS n 
1 195 HIS n 
1 196 ARG n 
1 197 ALA n 
1 198 GLY n 
1 199 VAL n 
1 200 LEU n 
1 201 LYS n 
1 202 LEU n 
1 203 LEU n 
1 204 ALA n 
1 205 GLU n 
1 206 LEU n 
1 207 LYS n 
1 208 LYS n 
1 209 ARG n 
1 210 GLY n 
1 211 ALA n 
1 212 PRO n 
1 213 ILE n 
1 214 HIS n 
1 215 ALA n 
1 216 LEU n 
1 217 GLY n 
1 218 LEU n 
1 219 GLN n 
1 220 SER n 
1 221 HIS n 
1 222 ILE n 
1 223 SER n 
1 224 ALA n 
1 225 GLY n 
1 226 ASP n 
1 227 MET n 
1 228 MET n 
1 229 SER n 
1 230 GLY n 
1 231 PRO n 
1 232 ALA n 
1 233 ASN n 
1 234 ALA n 
1 235 ALA n 
1 236 VAL n 
1 237 LEU n 
1 238 ARG n 
1 239 GLU n 
1 240 TRP n 
1 241 ARG n 
1 242 LYS n 
1 243 PHE n 
1 244 LEU n 
1 245 ASP n 
1 246 GLU n 
1 247 VAL n 
1 248 THR n 
1 249 GLY n 
1 250 MET n 
1 251 GLY n 
1 252 LEU n 
1 253 ASP n 
1 254 LEU n 
1 255 LEU n 
1 256 ILE n 
1 257 THR n 
1 258 GLU n 
1 259 PHE n 
1 260 ASP n 
1 261 VAL n 
1 262 ASN n 
1 263 ASP n 
1 264 LYS n 
1 265 ALA n 
1 266 PHE n 
1 267 PRO n 
1 268 ALA n 
1 269 ASP n 
1 270 PHE n 
1 271 ALA n 
1 272 LYS n 
1 273 ARG n 
1 274 ASP n 
1 275 ALA n 
1 276 ALA n 
1 277 THR n 
1 278 ALA n 
1 279 ALA n 
1 280 LEU n 
1 281 ALA n 
1 282 ARG n 
1 283 ASP n 
1 284 TYR n 
1 285 LEU n 
1 286 ASP n 
1 287 VAL n 
1 288 THR n 
1 289 LEU n 
1 290 SER n 
1 291 TYR n 
1 292 PRO n 
1 293 THR n 
1 294 CYS n 
1 295 ARG n 
1 296 ASP n 
1 297 PHE n 
1 298 LEU n 
1 299 LEU n 
1 300 TRP n 
1 301 GLY n 
1 302 MET n 
1 303 ALA n 
1 304 ASP n 
1 305 HIS n 
1 306 VAL n 
1 307 ASN n 
1 308 TRP n 
1 309 LEU n 
1 310 GLN n 
1 311 VAL n 
1 312 TRP n 
1 313 PRO n 
1 314 ASP n 
1 315 ALA n 
1 316 LYS n 
1 317 ARG n 
1 318 PRO n 
1 319 ASP n 
1 320 GLY n 
1 321 LEU n 
1 322 ALA n 
1 323 GLN n 
1 324 ARG n 
1 325 PRO n 
1 326 THR n 
1 327 PRO n 
1 328 TYR n 
1 329 ASP n 
1 330 SER n 
1 331 GLN n 
1 332 LEU n 
1 333 ARG n 
1 334 PRO n 
1 335 LYS n 
1 336 PRO n 
1 337 MET n 
1 338 ARG n 
1 339 GLU n 
1 340 ALA n 
1 341 ILE n 
1 342 ALA n 
1 343 ALA n 
1 344 SER n 
1 345 LEU n 
1 346 ARG n 
1 347 ALA n 
1 348 MET n 
1 349 PRO n 
1 350 MET n 
1 351 ARG n 
1 352 LYS n 
1 353 ALA 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                   353 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Massilia sp. RBM26' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1756047 
_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   PRO 1   1   1   PRO PRO A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   ASP 5   5   5   ASP ASP A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  ARG 13  13  13  ARG ARG A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PHE 30  30  30  PHE PHE A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  MET 39  39  39  MET MET A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  CYS 43  43  43  CYS CYS A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  MET 45  45  45  MET MET A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  ALA 48  48  48  ALA ALA A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  THR 52  52  52  THR THR A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  TRP 54  54  54  TRP TRP A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  TRP 66  66  66  TRP TRP A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  GLU 71  71  71  GLU GLU A . n 
A 1 72  MET 72  72  72  MET MET A . n 
A 1 73  PHE 73  73  73  PHE PHE A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ARG 77  77  77  ARG ARG A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  MET 81  81  81  MET MET A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  TRP 90  90  90  TRP TRP A . n 
A 1 91  GLN 91  91  91  GLN GLN A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  TRP 95  95  95  TRP TRP A . n 
A 1 96  LEU 96  96  96  LEU LEU A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  TRP 99  99  99  TRP TRP A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 PRO 109 109 109 PRO PRO A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 CYS 125 125 125 CYS CYS A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 HIS 127 127 127 HIS HIS A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 VAL 131 131 131 VAL VAL A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 GLU 139 139 139 GLU GLU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 GLY 158 158 158 GLY GLY A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 GLN 162 162 162 GLN GLN A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 GLU 164 164 164 GLU GLU A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 PHE 167 167 167 PHE PHE A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 GLN 169 169 169 GLN GLN A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 HIS 171 171 171 HIS HIS A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 ASN 182 182 182 ASN ASN A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 HIS 195 195 195 HIS HIS A . n 
A 1 196 ARG 196 196 196 ARG ARG A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 HIS 214 214 214 HIS HIS A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 SER 223 223 223 SER SER A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 MET 227 227 227 MET MET A . n 
A 1 228 MET 228 228 228 MET MET A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 ALA 235 235 235 ALA ALA A . n 
A 1 236 VAL 236 236 236 VAL VAL A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 TRP 240 240 240 TRP TRP A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 MET 250 250 250 MET MET A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 ILE 256 256 256 ILE ILE A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLU 258 258 258 GLU GLU A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 ALA 265 265 265 ALA ALA A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 PRO 267 267 267 PRO PRO 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 PHE 270 270 270 PHE PHE 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 ARG 273 273 273 ARG ARG A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 LEU 280 280 280 LEU LEU A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 ASP 283 283 283 ASP ASP A . n 
A 1 284 TYR 284 284 284 TYR TYR A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 VAL 287 287 287 VAL VAL A . n 
A 1 288 THR 288 288 288 THR THR A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 TYR 291 291 291 TYR TYR A . n 
A 1 292 PRO 292 292 292 PRO PRO A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 CYS 294 294 294 CYS CYS A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 ASP 296 296 296 ASP ASP A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 TRP 300 300 300 TRP TRP A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 MET 302 302 302 MET MET A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 ASP 304 304 304 ASP ASP A . n 
A 1 305 HIS 305 305 305 HIS HIS A . n 
A 1 306 VAL 306 306 306 VAL VAL A . n 
A 1 307 ASN 307 307 307 ASN ASN A . n 
A 1 308 TRP 308 308 308 TRP TRP A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 GLN 310 310 310 GLN GLN A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 TRP 312 312 312 TRP TRP A . n 
A 1 313 PRO 313 313 313 PRO PRO A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 ALA 315 315 315 ALA ALA A . n 
A 1 316 LYS 316 316 316 LYS LYS A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 PRO 318 318 318 PRO PRO A . n 
A 1 319 ASP 319 319 319 ASP ASP A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 ALA 322 322 322 ALA ALA A . n 
A 1 323 GLN 323 323 323 GLN GLN A . n 
A 1 324 ARG 324 324 324 ARG ARG A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 THR 326 326 326 THR THR A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 TYR 328 328 328 TYR TYR A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 SER 330 330 330 SER SER A . n 
A 1 331 GLN 331 331 331 GLN GLN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 PRO 334 334 334 PRO PRO A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 PRO 336 336 336 PRO PRO A . n 
A 1 337 MET 337 337 337 MET MET A . n 
A 1 338 ARG 338 338 338 ARG ARG A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 ALA 340 340 340 ALA ALA A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 SER 344 344 344 SER SER A . n 
A 1 345 LEU 345 345 345 LEU LEU A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 MET 348 348 348 MET MET A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 MET 350 350 350 MET MET A . n 
A 1 351 ARG 351 351 351 ARG ARG A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
B 1 1   PRO 1   1   1   PRO PRO B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   LEU 3   3   3   LEU LEU B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   ASP 5   5   5   ASP ASP B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   LYS 8   8   8   LYS LYS B . n 
B 1 9   ALA 9   9   9   ALA ALA B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  ARG 13  13  13  ARG ARG B . n 
B 1 14  PHE 14  14  14  PHE PHE B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  GLY 19  19  19  GLY GLY B . n 
B 1 20  LEU 20  20  20  LEU LEU B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  GLN 24  24  24  GLN GLN B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  ARG 27  27  27  ARG ARG B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  SER 29  29  29  SER SER B . n 
B 1 30  PHE 30  30  30  PHE PHE B . n 
B 1 31  ARG 31  31  31  ARG ARG B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  ARG 36  36  36  ARG ARG B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  MET 39  39  39  MET MET B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  ARG 41  41  41  ARG ARG B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  CYS 43  43  43  CYS CYS B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  MET 45  45  45  MET MET B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  ALA 48  48  48  ALA ALA B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ASN 50  50  50  ASN ASN B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  THR 52  52  52  THR THR B . n 
B 1 53  LYS 53  53  53  LYS LYS B . n 
B 1 54  TRP 54  54  54  TRP TRP B . n 
B 1 55  GLN 55  55  55  GLN GLN B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  LYS 60  60  60  LYS LYS B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  PRO 63  63  63  PRO PRO B . n 
B 1 64  TYR 64  64  64  TYR TYR B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  TRP 66  66  66  TRP TRP B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  ALA 69  69  69  ALA ALA B . n 
B 1 70  ASP 70  70  70  ASP ASP B . n 
B 1 71  GLU 71  71  71  GLU GLU B . n 
B 1 72  MET 72  72  72  MET MET B . n 
B 1 73  PHE 73  73  73  PHE PHE B . n 
B 1 74  ALA 74  74  74  ALA ALA B . n 
B 1 75  TRP 75  75  75  TRP TRP B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  ARG 77  77  77  ARG ARG B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  MET 81  81  81  MET MET B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  TRP 90  90  90  TRP TRP B . n 
B 1 91  GLN 91  91  91  GLN GLN B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  TRP 95  95  95  TRP TRP B . n 
B 1 96  LEU 96  96  96  LEU LEU B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  TRP 99  99  99  TRP TRP B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 LEU 105 105 105 LEU LEU B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 LYS 108 108 108 LYS LYS B . n 
B 1 109 PRO 109 109 109 PRO PRO B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 ALA 111 111 111 ALA ALA B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ALA 115 115 115 ALA ALA B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 GLU 119 119 119 GLU GLU B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 CYS 125 125 125 CYS CYS B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 HIS 127 127 127 HIS HIS B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 LYS 129 129 129 LYS LYS B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 VAL 131 131 131 VAL VAL B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 HIS 134 134 134 HIS HIS B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 VAL 136 136 136 VAL VAL B . n 
B 1 137 VAL 137 137 137 VAL VAL B . n 
B 1 138 ASN 138 138 138 ASN ASN B . n 
B 1 139 GLU 139 139 139 GLU GLU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 PRO 143 143 143 PRO PRO B . n 
B 1 144 LYS 144 144 144 LYS LYS B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLN 150 150 150 GLN GLN B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 VAL 152 152 152 VAL VAL B . n 
B 1 153 PHE 153 153 153 PHE PHE B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 LYS 155 155 155 LYS LYS B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 MET 157 157 157 MET MET B . n 
B 1 158 GLY 158 158 158 GLY GLY B . n 
B 1 159 ALA 159 159 159 ALA ALA B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 GLN 162 162 162 GLN GLN B . n 
B 1 163 ILE 163 163 163 ILE ILE B . n 
B 1 164 GLU 164 164 164 GLU GLU B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 PHE 167 167 167 PHE PHE B . n 
B 1 168 ARG 168 168 168 ARG ARG B . n 
B 1 169 GLN 169 169 169 GLN GLN B . n 
B 1 170 ALA 170 170 170 ALA ALA B . n 
B 1 171 HIS 171 171 171 HIS HIS B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 HIS 173 173 173 HIS HIS B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 GLN 178 178 178 GLN GLN B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 VAL 180 180 180 VAL VAL B . n 
B 1 181 TYR 181 181 181 TYR TYR B . n 
B 1 182 ASN 182 182 182 ASN ASN B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 PRO 187 187 187 PRO PRO B . n 
B 1 188 GLY 188 188 188 GLY GLY B . n 
B 1 189 LEU 189 189 189 LEU LEU B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 HIS 195 195 195 HIS HIS B . n 
B 1 196 ARG 196 196 196 ARG ARG B . n 
B 1 197 ALA 197 197 197 ALA ALA B . n 
B 1 198 GLY 198 198 198 GLY GLY B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 LYS 201 201 201 LYS LYS B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 LEU 203 203 203 LEU LEU B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 LYS 207 207 207 LYS LYS B . n 
B 1 208 LYS 208 208 208 LYS LYS B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 GLY 210 210 210 GLY GLY B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 PRO 212 212 212 PRO PRO B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 HIS 214 214 214 HIS HIS B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 SER 220 220 220 SER SER B . n 
B 1 221 HIS 221 221 221 HIS HIS B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 SER 223 223 223 SER SER B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 MET 227 227 227 MET MET B . n 
B 1 228 MET 228 228 228 MET MET B . n 
B 1 229 SER 229 229 229 SER SER B . n 
B 1 230 GLY 230 230 230 GLY GLY B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ASN 233 233 233 ASN ASN B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 ALA 235 235 235 ALA ALA B . n 
B 1 236 VAL 236 236 236 VAL VAL B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 TRP 240 240 240 TRP TRP B . n 
B 1 241 ARG 241 241 241 ARG ARG B . n 
B 1 242 LYS 242 242 242 LYS LYS B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 GLU 246 246 246 GLU GLU B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 THR 248 248 248 THR THR B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 MET 250 250 250 MET MET B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 LEU 252 252 252 LEU LEU B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 LEU 255 255 255 LEU LEU B . n 
B 1 256 ILE 256 256 256 ILE ILE B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLU 258 258 258 GLU GLU B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 ALA 265 265 265 ALA ALA B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 PRO 267 267 267 PRO PRO 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 PHE 270 270 270 PHE PHE 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 ARG 273 273 273 ARG ARG B . n 
B 1 274 ASP 274 274 274 ASP ASP B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 LEU 280 280 280 LEU LEU B . n 
B 1 281 ALA 281 281 281 ALA ALA B . n 
B 1 282 ARG 282 282 282 ARG ARG B . n 
B 1 283 ASP 283 283 283 ASP ASP B . n 
B 1 284 TYR 284 284 284 TYR TYR B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 VAL 287 287 287 VAL VAL B . n 
B 1 288 THR 288 288 288 THR THR B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 TYR 291 291 291 TYR TYR B . n 
B 1 292 PRO 292 292 292 PRO PRO B . n 
B 1 293 THR 293 293 293 THR THR B . n 
B 1 294 CYS 294 294 294 CYS CYS B . n 
B 1 295 ARG 295 295 295 ARG ARG B . n 
B 1 296 ASP 296 296 296 ASP ASP B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 LEU 298 298 298 LEU LEU B . n 
B 1 299 LEU 299 299 299 LEU LEU B . n 
B 1 300 TRP 300 300 300 TRP TRP B . n 
B 1 301 GLY 301 301 301 GLY GLY B . n 
B 1 302 MET 302 302 302 MET MET B . n 
B 1 303 ALA 303 303 303 ALA ALA B . n 
B 1 304 ASP 304 304 304 ASP ASP B . n 
B 1 305 HIS 305 305 305 HIS HIS B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 ASN 307 307 307 ASN ASN B . n 
B 1 308 TRP 308 308 308 TRP TRP B . n 
B 1 309 LEU 309 309 309 LEU LEU B . n 
B 1 310 GLN 310 310 310 GLN GLN B . n 
B 1 311 VAL 311 311 311 VAL VAL B . n 
B 1 312 TRP 312 312 312 TRP TRP B . n 
B 1 313 PRO 313 313 313 PRO PRO B . n 
B 1 314 ASP 314 314 314 ASP ASP B . n 
B 1 315 ALA 315 315 315 ALA ALA B . n 
B 1 316 LYS 316 316 316 LYS LYS B . n 
B 1 317 ARG 317 317 317 ARG ARG B . n 
B 1 318 PRO 318 318 318 PRO PRO B . n 
B 1 319 ASP 319 319 319 ASP ASP B . n 
B 1 320 GLY 320 320 320 GLY GLY B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 ALA 322 322 322 ALA ALA B . n 
B 1 323 GLN 323 323 323 GLN GLN B . n 
B 1 324 ARG 324 324 324 ARG ARG B . n 
B 1 325 PRO 325 325 325 PRO PRO B . n 
B 1 326 THR 326 326 326 THR THR B . n 
B 1 327 PRO 327 327 327 PRO PRO B . n 
B 1 328 TYR 328 328 328 TYR TYR B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 SER 330 330 330 SER SER B . n 
B 1 331 GLN 331 331 331 GLN GLN B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 PRO 334 334 334 PRO PRO B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 PRO 336 336 336 PRO PRO B . n 
B 1 337 MET 337 337 337 MET MET B . n 
B 1 338 ARG 338 338 338 ARG ARG B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 ALA 340 340 340 ALA ALA B . n 
B 1 341 ILE 341 341 341 ILE ILE B . n 
B 1 342 ALA 342 342 342 ALA ALA B . n 
B 1 343 ALA 343 343 343 ALA ALA B . n 
B 1 344 SER 344 344 344 SER SER B . n 
B 1 345 LEU 345 345 345 LEU LEU B . n 
B 1 346 ARG 346 346 346 ARG ARG B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 MET 348 348 348 MET MET B . n 
B 1 349 PRO 349 349 349 PRO PRO B . n 
B 1 350 MET 350 350 350 MET MET B . n 
B 1 351 ARG 351 351 351 ARG ARG B . n 
B 1 352 LYS 352 352 352 LYS LYS B . n 
B 1 353 ALA 353 353 353 ALA ALA 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 72 HOH HOH A . 
C 2 HOH 2  402 76 HOH HOH A . 
C 2 HOH 3  403 11 HOH HOH A . 
C 2 HOH 4  404 4  HOH HOH A . 
C 2 HOH 5  405 37 HOH HOH A . 
C 2 HOH 6  406 19 HOH HOH A . 
C 2 HOH 7  407 34 HOH HOH A . 
C 2 HOH 8  408 23 HOH HOH A . 
C 2 HOH 9  409 8  HOH HOH A . 
C 2 HOH 10 410 10 HOH HOH A . 
C 2 HOH 11 411 3  HOH HOH A . 
C 2 HOH 12 412 39 HOH HOH A . 
C 2 HOH 13 413 16 HOH HOH A . 
C 2 HOH 14 414 58 HOH HOH A . 
C 2 HOH 15 415 54 HOH HOH A . 
C 2 HOH 16 416 70 HOH HOH A . 
C 2 HOH 17 417 38 HOH HOH A . 
C 2 HOH 18 418 6  HOH HOH A . 
C 2 HOH 19 419 24 HOH HOH A . 
C 2 HOH 20 420 50 HOH HOH A . 
C 2 HOH 21 421 46 HOH HOH A . 
C 2 HOH 22 422 28 HOH HOH A . 
C 2 HOH 23 423 45 HOH HOH A . 
C 2 HOH 24 424 85 HOH HOH A . 
C 2 HOH 25 425 17 HOH HOH A . 
C 2 HOH 26 426 62 HOH HOH A . 
C 2 HOH 27 427 87 HOH HOH A . 
C 2 HOH 28 428 68 HOH HOH A . 
C 2 HOH 29 429 43 HOH HOH A . 
C 2 HOH 30 430 44 HOH HOH A . 
C 2 HOH 31 431 57 HOH HOH A . 
C 2 HOH 32 432 25 HOH HOH A . 
C 2 HOH 33 433 29 HOH HOH A . 
C 2 HOH 34 434 82 HOH HOH A . 
C 2 HOH 35 435 51 HOH HOH A . 
C 2 HOH 36 436 73 HOH HOH A . 
C 2 HOH 37 437 2  HOH HOH A . 
D 2 HOH 1  401 26 HOH HOH B . 
D 2 HOH 2  402 47 HOH HOH B . 
D 2 HOH 3  403 27 HOH HOH B . 
D 2 HOH 4  404 69 HOH HOH B . 
D 2 HOH 5  405 41 HOH HOH B . 
D 2 HOH 6  406 78 HOH HOH B . 
D 2 HOH 7  407 13 HOH HOH B . 
D 2 HOH 8  408 66 HOH HOH B . 
D 2 HOH 9  409 81 HOH HOH B . 
D 2 HOH 10 410 42 HOH HOH B . 
D 2 HOH 11 411 7  HOH HOH B . 
D 2 HOH 12 412 35 HOH HOH B . 
D 2 HOH 13 413 1  HOH HOH B . 
D 2 HOH 14 414 14 HOH HOH B . 
D 2 HOH 15 415 83 HOH HOH B . 
D 2 HOH 16 416 80 HOH HOH B . 
D 2 HOH 17 417 79 HOH HOH B . 
D 2 HOH 18 418 60 HOH HOH B . 
D 2 HOH 19 419 65 HOH HOH B . 
D 2 HOH 20 420 9  HOH HOH B . 
D 2 HOH 21 421 89 HOH HOH B . 
D 2 HOH 22 422 71 HOH HOH B . 
D 2 HOH 23 423 32 HOH HOH B . 
D 2 HOH 24 424 22 HOH HOH B . 
D 2 HOH 25 425 36 HOH HOH B . 
D 2 HOH 26 426 49 HOH HOH B . 
D 2 HOH 27 427 31 HOH HOH B . 
D 2 HOH 28 428 21 HOH HOH B . 
D 2 HOH 29 429 61 HOH HOH B . 
D 2 HOH 30 430 63 HOH HOH B . 
D 2 HOH 31 431 77 HOH HOH B . 
D 2 HOH 32 432 67 HOH HOH B . 
D 2 HOH 33 433 52 HOH HOH B . 
D 2 HOH 34 434 20 HOH HOH B . 
D 2 HOH 35 435 59 HOH HOH B . 
D 2 HOH 36 436 88 HOH HOH B . 
D 2 HOH 37 437 56 HOH HOH B . 
D 2 HOH 38 438 18 HOH HOH B . 
D 2 HOH 39 439 12 HOH HOH B . 
D 2 HOH 40 440 30 HOH HOH B . 
D 2 HOH 41 441 48 HOH HOH B . 
D 2 HOH 42 442 40 HOH HOH B . 
D 2 HOH 43 443 84 HOH HOH B . 
D 2 HOH 44 444 15 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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.914 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9UPA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     53.350 
_cell.length_a_esd                 ? 
_cell.length_b                     69.300 
_cell.length_b_esd                 ? 
_cell.length_c                     91.080 
_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                         9UPA 
_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                   9UPA 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.27 
_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    '0.1MBis-TrispH 7.0,25%(W/V) MPD' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-07 
_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   0.97918 
_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        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9UPA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.6 
_reflns.d_resolution_low                               46.694 
_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                                     39554 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.43 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          5.64 
_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                                   0.961 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.60 
_reflns_shell.d_res_low                                     2.76 
_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                             6333 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.665 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.006 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.027 
_refine.aniso_B[2][2]                            -0.004 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.008 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               31.269 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.903 
_refine.correlation_coeff_Fo_to_Fc_free          0.832 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9UPA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.600 
_refine.ls_d_res_low                             46.694 
_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                     20575 
_refine.ls_number_reflns_R_free                  1023 
_refine.ls_number_reflns_R_work                  19552 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.835 
_refine.ls_percent_reflns_R_free                 4.972 
_refine.ls_R_factor_all                          0.245 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2947 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2420 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.344 
_refine.pdbx_overall_ESU_R_Free                  0.418 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             0.006 
_refine.overall_SU_ML                            0.000 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.600 
_refine_hist.d_res_low                        46.694 
_refine_hist.number_atoms_solvent             81 
_refine_hist.number_atoms_total               5629 
_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        5548 
_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_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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.600  2.667  1526 . 72 1444 99.3447  . 0.333 . . 0.328 . . . . . 0.321 . . . . . 20 . 0.919 0.870 0.431 
'X-RAY DIFFRACTION' 2.667  2.740  1440 . 55 1385 100.0000 . 0.330 . . 0.328 . . . . . 0.313 . . . . . 20 . 0.925 0.900 0.385 
'X-RAY DIFFRACTION' 2.740  2.819  1449 . 73 1376 100.0000 . 0.333 . . 0.329 . . . . . 0.306 . . . . . 20 . 0.923 0.896 0.393 
'X-RAY DIFFRACTION' 2.819  2.905  1379 . 71 1307 99.9275  . 0.313 . . 0.312 . . . . . 0.286 . . . . . 20 . 0.930 0.924 0.324 
'X-RAY DIFFRACTION' 2.905  3.000  1331 . 63 1268 100.0000 . 0.310 . . 0.307 . . . . . 0.278 . . . . . 20 . 0.934 0.902 0.367 
'X-RAY DIFFRACTION' 3.000  3.105  1319 . 49 1268 99.8484  . 0.289 . . 0.288 . . . . . 0.267 . . . . . 20 . 0.941 0.938 0.320 
'X-RAY DIFFRACTION' 3.105  3.222  1235 . 76 1159 100.0000 . 0.283 . . 0.281 . . . . . 0.247 . . . . . 20 . 0.944 0.919 0.320 
'X-RAY DIFFRACTION' 3.222  3.353  1259 . 57 1200 99.8411  . 0.272 . . 0.272 . . . . . 0.250 . . . . . 20 . 0.951 0.956 0.271 
'X-RAY DIFFRACTION' 3.353  3.501  1143 . 61 1082 100.0000 . 0.247 . . 0.243 . . . . . 0.228 . . . . . 20 . 0.961 0.939 0.318 
'X-RAY DIFFRACTION' 3.501  3.671  1123 . 54 1069 100.0000 . 0.234 . . 0.231 . . . . . 0.209 . . . . . 20 . 0.966 0.955 0.288 
'X-RAY DIFFRACTION' 3.671  3.868  1063 . 51 1012 100.0000 . 0.226 . . 0.226 . . . . . 0.211 . . . . . 20 . 0.970 0.966 0.238 
'X-RAY DIFFRACTION' 3.868  4.101  1002 . 61 939  99.8004  . 0.203 . . 0.200 . . . . . 0.186 . . . . . 20 . 0.975 0.956 0.260 
'X-RAY DIFFRACTION' 4.101  4.382  962  . 67 895  100.0000 . 0.200 . . 0.193 . . . . . 0.179 . . . . . 20 . 0.977 0.956 0.284 
'X-RAY DIFFRACTION' 4.382  4.729  873  . 49 824  100.0000 . 0.189 . . 0.186 . . . . . 0.174 . . . . . 20 . 0.979 0.965 0.250 
'X-RAY DIFFRACTION' 4.729  5.175  817  . 45 772  100.0000 . 0.188 . . 0.188 . . . . . 0.178 . . . . . 20 . 0.980 0.977 0.185 
'X-RAY DIFFRACTION' 5.175  5.777  752  . 33 719  100.0000 . 0.212 . . 0.208 . . . . . 0.192 . . . . . 20 . 0.973 0.945 0.301 
'X-RAY DIFFRACTION' 5.777  6.654  660  . 38 622  100.0000 . 0.227 . . 0.227 . . . . . 0.210 . . . . . 20 . 0.970 0.975 0.228 
'X-RAY DIFFRACTION' 6.654  8.108  553  . 15 538  100.0000 . 0.197 . . 0.196 . . . . . 0.190 . . . . . 20 . 0.975 0.974 0.216 
'X-RAY DIFFRACTION' 8.108  11.298 450  . 20 430  100.0000 . 0.166 . . 0.164 . . . . . 0.168 . . . . . 20 . 0.983 0.973 0.215 
'X-RAY DIFFRACTION' 11.298 46.694 270  . 13 243  94.8148  . 0.282 . . 0.268 . . . . . 0.279 . . . . . 20 . 0.953 0.784 0.602 
# 
_struct.entry_id                     9UPA 
_struct.title                        'Improved thermostability of a GH10 xylanase based on its X-ray crystal structure' 
_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        9UPA 
_struct_keywords.text            'glycosidase, crystal, thermostability, HYDROLASE, CARBOHYDRATE' 
_struct_keywords.pdbx_keywords   CARBOHYDRATE 
# 
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                    A0A0S2I9J6_9BURK 
_struct_ref.pdbx_db_accession          A0A0S2I9J6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PALKDLAKAKGMRFGNAIGLLEDQDTRKSFRDPAYRALMARECNMIVAENETKWQALQPKPGPYQWGPADEMFAWARKEG
MAIRGHALIWQDPKWLPAWVNALDLKSKPVAHAEAILREHAKTVCTHLKDVISHDVVNEAVSPKDGSLIQNVFTKRMGAV
EQIEFAFRQAHEHAPKAQLVYNDFMGPGLGDDAKHRAGVLKLLAELKKRGAPIHALGLQSHVSAGDMMSGPANAAVLREW
RKFLDEVTGMGLDLLITEFDVNDKAFPADFAKRDAATAALARDYLDVTLSYPTCRDFLLWGMADHVNWLQVWADAKRPDG
LAQRPTPYDSQLRAKPMREAIAASLRAMPMRKA
;
_struct_ref.pdbx_align_begin           31 
# 
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 9UPA A 1 ? 353 ? A0A0S2I9J6 31 ? 383 ? 1 353 
2 1 9UPA B 1 ? 353 ? A0A0S2I9J6 31 ? 383 ? 1 353 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9UPA SER A 16  ? UNP A0A0S2I9J6 ASN 46  conflict 16  1  
1 9UPA ARG A 192 ? UNP A0A0S2I9J6 ASP 222 conflict 192 2  
1 9UPA ILE A 222 ? UNP A0A0S2I9J6 VAL 252 conflict 222 3  
1 9UPA PRO A 313 ? UNP A0A0S2I9J6 ALA 343 conflict 313 4  
1 9UPA PRO A 334 ? UNP A0A0S2I9J6 ALA 364 conflict 334 5  
2 9UPA SER B 16  ? UNP A0A0S2I9J6 ASN 46  conflict 16  6  
2 9UPA ARG B 192 ? UNP A0A0S2I9J6 ASP 222 conflict 192 7  
2 9UPA ILE B 222 ? UNP A0A0S2I9J6 VAL 252 conflict 222 8  
2 9UPA PRO B 313 ? UNP A0A0S2I9J6 ALA 343 conflict 313 9  
2 9UPA PRO B 334 ? UNP A0A0S2I9J6 ALA 364 conflict 334 10 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,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 ALA A 2   ? LYS A 10  ? ALA A 2   LYS A 10  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 32  ? CYS A 43  ? ASP A 32  CYS A 43  1 ? 12 
HELX_P HELX_P3  AA3 LYS A 53  ? GLN A 58  ? LYS A 53  GLN A 58  1 ? 6  
HELX_P HELX_P4  AA4 TRP A 66  ? GLU A 79  ? TRP A 66  GLU A 79  1 ? 14 
HELX_P HELX_P5  AA5 ASP A 92  ? LEU A 96  ? ASP A 92  LEU A 96  5 ? 5  
HELX_P HELX_P6  AA6 PRO A 97  ? ALA A 102 ? PRO A 97  ALA A 102 1 ? 6  
HELX_P HELX_P7  AA7 PRO A 109 ? LEU A 128 ? PRO A 109 LEU A 128 1 ? 20 
HELX_P HELX_P8  AA8 PHE A 153 ? GLY A 158 ? PHE A 153 GLY A 158 1 ? 6  
HELX_P HELX_P9  AA9 GLY A 158 ? ALA A 174 ? GLY A 158 ALA A 174 1 ? 17 
HELX_P HELX_P10 AB1 GLY A 190 ? ARG A 209 ? GLY A 190 ARG A 209 1 ? 20 
HELX_P HELX_P11 AB2 SER A 223 ? MET A 227 ? SER A 223 MET A 227 5 ? 5  
HELX_P HELX_P12 AB3 GLY A 230 ? ALA A 232 ? GLY A 230 ALA A 232 5 ? 3  
HELX_P HELX_P13 AB4 ASN A 233 ? MET A 250 ? ASN A 233 MET A 250 1 ? 18 
HELX_P HELX_P14 AB5 ASP A 269 ? SER A 290 ? ASP A 269 SER A 290 1 ? 22 
HELX_P HELX_P15 AB6 ALA A 303 ? VAL A 311 ? ALA A 303 VAL A 311 5 ? 9  
HELX_P HELX_P16 AB7 TRP A 312 ? LYS A 316 ? TRP A 312 LYS A 316 5 ? 5  
HELX_P HELX_P17 AB8 LYS A 335 ? MET A 348 ? LYS A 335 MET A 348 1 ? 14 
HELX_P HELX_P18 AB9 ALA B 2   ? LYS B 10  ? ALA B 2   LYS B 10  1 ? 9  
HELX_P HELX_P19 AC1 ASP B 32  ? CYS B 43  ? ASP B 32  CYS B 43  1 ? 12 
HELX_P HELX_P20 AC2 LYS B 53  ? GLN B 58  ? LYS B 53  GLN B 58  1 ? 6  
HELX_P HELX_P21 AC3 TRP B 66  ? GLU B 79  ? TRP B 66  GLU B 79  1 ? 14 
HELX_P HELX_P22 AC4 ASP B 92  ? LEU B 96  ? ASP B 92  LEU B 96  5 ? 5  
HELX_P HELX_P23 AC5 PRO B 97  ? ALA B 102 ? PRO B 97  ALA B 102 1 ? 6  
HELX_P HELX_P24 AC6 PRO B 109 ? LEU B 128 ? PRO B 109 LEU B 128 1 ? 20 
HELX_P HELX_P25 AC7 PHE B 153 ? GLY B 158 ? PHE B 153 GLY B 158 1 ? 6  
HELX_P HELX_P26 AC8 GLY B 158 ? ALA B 174 ? GLY B 158 ALA B 174 1 ? 17 
HELX_P HELX_P27 AC9 GLY B 190 ? ARG B 209 ? GLY B 190 ARG B 209 1 ? 20 
HELX_P HELX_P28 AD1 SER B 223 ? MET B 227 ? SER B 223 MET B 227 5 ? 5  
HELX_P HELX_P29 AD2 GLY B 230 ? ALA B 232 ? GLY B 230 ALA B 232 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 233 ? MET B 250 ? ASN B 233 MET B 250 1 ? 18 
HELX_P HELX_P31 AD4 ASP B 269 ? LEU B 289 ? ASP B 269 LEU B 289 1 ? 21 
HELX_P HELX_P32 AD5 ALA B 303 ? VAL B 311 ? ALA B 303 VAL B 311 5 ? 9  
HELX_P HELX_P33 AD6 TRP B 312 ? LYS B 316 ? TRP B 312 LYS B 316 5 ? 5  
HELX_P HELX_P34 AD7 LYS B 335 ? MET B 348 ? LYS B 335 MET B 348 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 HIS 86 A . ? HIS 86 A ALA 87 A ? ALA 87 A 1 -6.31 
2 HIS 86 B . ? HIS 86 B ALA 87 B ? ALA 87 B 1 -5.84 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 6 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA3 7 8 ? parallel 
AA4 1 2 ? parallel 
AA4 2 3 ? parallel 
AA4 3 4 ? parallel 
AA4 4 5 ? parallel 
AA4 5 6 ? 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 ILE A 89  ? TRP A 90  ? ILE A 89  TRP A 90  
AA1 2 SER A 133 ? ASN A 138 ? SER A 133 ASN A 138 
AA1 3 ALA A 82  ? GLY A 85  ? ALA A 82  GLY A 85  
AA1 4 MET A 45  ? ALA A 48  ? MET A 45  ALA A 48  
AA1 5 ARG A 13  ? ILE A 18  ? ARG A 13  ILE A 18  
AA1 6 CYS A 294 ? LEU A 299 ? CYS A 294 LEU A 299 
AA1 7 ASP A 253 ? VAL A 261 ? ASP A 253 VAL A 261 
AA1 8 HIS A 221 ? ILE A 222 ? HIS A 221 ILE A 222 
AA2 1 ILE A 89  ? TRP A 90  ? ILE A 89  TRP A 90  
AA2 2 SER A 133 ? ASN A 138 ? SER A 133 ASN A 138 
AA2 3 GLN A 178 ? ASP A 183 ? GLN A 178 ASP A 183 
AA2 4 ALA A 215 ? LEU A 218 ? ALA A 215 LEU A 218 
AA2 5 ASP A 253 ? VAL A 261 ? ASP A 253 VAL A 261 
AA2 6 HIS A 221 ? ILE A 222 ? HIS A 221 ILE A 222 
AA3 1 ILE B 89  ? TRP B 90  ? ILE B 89  TRP B 90  
AA3 2 SER B 133 ? ASN B 138 ? SER B 133 ASN B 138 
AA3 3 ALA B 82  ? GLY B 85  ? ALA B 82  GLY B 85  
AA3 4 MET B 45  ? ALA B 48  ? MET B 45  ALA B 48  
AA3 5 ARG B 13  ? ILE B 18  ? ARG B 13  ILE B 18  
AA3 6 CYS B 294 ? LEU B 299 ? CYS B 294 LEU B 299 
AA3 7 ASP B 253 ? VAL B 261 ? ASP B 253 VAL B 261 
AA3 8 HIS B 221 ? ILE B 222 ? HIS B 221 ILE B 222 
AA4 1 ILE B 89  ? TRP B 90  ? ILE B 89  TRP B 90  
AA4 2 SER B 133 ? ASN B 138 ? SER B 133 ASN B 138 
AA4 3 GLN B 178 ? ASP B 183 ? GLN B 178 ASP B 183 
AA4 4 ALA B 215 ? LEU B 218 ? ALA B 215 LEU B 218 
AA4 5 ASP B 253 ? VAL B 261 ? ASP B 253 VAL B 261 
AA4 6 HIS B 221 ? ILE B 222 ? HIS B 221 ILE B 222 
# 
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 ILE A 89  ? N ILE A 89  O ASN A 138 ? O ASN A 138 
AA1 2 3 O ASP A 135 ? O ASP A 135 N GLY A 85  ? N GLY A 85  
AA1 3 4 O ALA A 82  ? O ALA A 82  N ILE A 46  ? N ILE A 46  
AA1 4 5 O VAL A 47  ? O VAL A 47  N ILE A 18  ? N ILE A 18  
AA1 5 6 N ALA A 17  ? N ALA A 17  O LEU A 299 ? O LEU A 299 
AA1 6 7 O LEU A 298 ? O LEU A 298 N PHE A 259 ? N PHE A 259 
AA1 7 8 N ASP A 260 ? N ASP A 260 O ILE A 222 ? O ILE A 222 
AA2 1 2 N ILE A 89  ? N ILE A 89  O ASN A 138 ? O ASN A 138 
AA2 2 3 N HIS A 134 ? N HIS A 134 O VAL A 180 ? O VAL A 180 
AA2 3 4 N TYR A 181 ? N TYR A 181 O GLY A 217 ? O GLY A 217 
AA2 4 5 N LEU A 218 ? N LEU A 218 O LEU A 255 ? O LEU A 255 
AA2 5 6 N ASP A 260 ? N ASP A 260 O ILE A 222 ? O ILE A 222 
AA3 1 2 N ILE B 89  ? N ILE B 89  O ASN B 138 ? O ASN B 138 
AA3 2 3 O SER B 133 ? O SER B 133 N GLY B 85  ? N GLY B 85  
AA3 3 4 O ALA B 82  ? O ALA B 82  N ILE B 46  ? N ILE B 46  
AA3 4 5 O MET B 45  ? O MET B 45  N SER B 16  ? N SER B 16  
AA3 5 6 N ARG B 13  ? N ARG B 13  O ARG B 295 ? O ARG B 295 
AA3 6 7 O LEU B 298 ? O LEU B 298 N PHE B 259 ? N PHE B 259 
AA3 7 8 N ASP B 260 ? N ASP B 260 O ILE B 222 ? O ILE B 222 
AA4 1 2 N ILE B 89  ? N ILE B 89  O ASN B 138 ? O ASN B 138 
AA4 2 3 N HIS B 134 ? N HIS B 134 O GLN B 178 ? O GLN B 178 
AA4 3 4 N TYR B 181 ? N TYR B 181 O GLY B 217 ? O GLY B 217 
AA4 4 5 N LEU B 216 ? N LEU B 216 O ASP B 253 ? O ASP B 253 
AA4 5 6 N ASP B 260 ? N ASP B 260 O ILE B 222 ? O ILE B 222 
# 
_pdbx_entry_details.entry_id                   9UPA 
_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 LEU A 20  ? ? -137.79 -30.85 
2  1 ARG A 27  ? ? -100.12 50.53  
3  1 SER A 29  ? ? -115.28 -71.92 
4  1 ASN A 50  ? ? -146.77 -9.90  
5  1 LEU A 128 ? ? -105.15 63.71  
6  1 GLU A 139 ? ? 51.64   76.20  
7  1 GLU A 258 ? ? -144.15 51.22  
8  1 ARG B 27  ? ? -97.46  50.57  
9  1 SER B 29  ? ? -115.86 -73.18 
10 1 ASN B 50  ? ? -143.77 -12.01 
11 1 LEU B 128 ? ? -104.34 63.98  
12 1 GLU B 139 ? ? 53.66   74.45  
13 1 GLU B 258 ? ? -144.77 51.04  
# 
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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China ?                                                                      
1 
'Other government'                                    China 'Zhejiang Provincial Natural Science Foundation of China LQN25C050002' 
2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5Y3X 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9UPA 
_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]   0.018744 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000626 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014430 
_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]   0.010985 
_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   . PRO A 1 1   ? 18.538  -19.701 9.531  1.000 33.330 0  1   PRO A N   1 
ATOM   2    C CA  . PRO A 1 1   ? 17.218  -19.340 9.004  1.000 32.990 0  1   PRO A CA  1 
ATOM   3    C C   . PRO A 1 1   ? 16.855  -17.884 9.265  1.000 32.470 0  1   PRO A C   1 
ATOM   4    O O   . PRO A 1 1   ? 17.218  -17.336 10.304 1.000 33.250 0  1   PRO A O   1 
ATOM   5    C CB  . PRO A 1 1   ? 16.270  -20.274 9.760  1.000 32.830 0  1   PRO A CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 16.979  -20.583 11.022 1.000 32.840 0  1   PRO A CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 18.442  -20.622 10.675 1.000 33.310 0  1   PRO A CD  1 
ATOM   8    N N   . ALA A 1 2   ? 16.129  -17.276 8.331  1.000 32.790 0  2   ALA A N   1 
ATOM   9    C CA  . ALA A 1 2   ? 15.746  -15.878 8.450  1.000 35.120 0  2   ALA A CA  1 
ATOM   10   C C   . ALA A 1 2   ? 14.494  -15.733 9.308  1.000 34.130 0  2   ALA A C   1 
ATOM   11   O O   . ALA A 1 2   ? 13.660  -16.642 9.384  1.000 35.160 0  2   ALA A O   1 
ATOM   12   C CB  . ALA A 1 2   ? 15.505  -15.264 7.071  1.000 33.520 0  2   ALA A CB  1 
ATOM   13   N N   . LEU A 1 3   ? 14.380  -14.575 9.968  1.000 32.900 0  3   LEU A N   1 
ATOM   14   C CA  . LEU A 1 3   ? 13.229  -14.307 10.826 1.000 32.320 0  3   LEU A CA  1 
ATOM   15   C C   . LEU A 1 3   ? 11.922  -14.519 10.079 1.000 31.700 0  3   LEU A C   1 
ATOM   16   O O   . LEU A 1 3   ? 10.944  -15.015 10.650 1.000 32.080 0  3   LEU A O   1 
ATOM   17   C CB  . LEU A 1 3   ? 13.298  -12.880 11.373 1.000 30.090 0  3   LEU A CB  1 
ATOM   18   C CG  . LEU A 1 3   ? 14.252  -12.662 12.544 1.000 32.050 0  3   LEU A CG  1 
ATOM   19   C CD1 . LEU A 1 3   ? 14.327  -11.191 12.911 1.000 29.680 0  3   LEU A CD1 1 
ATOM   20   C CD2 . LEU A 1 3   ? 13.820  -13.494 13.739 1.000 32.830 0  3   LEU A CD2 1 
ATOM   21   N N   . LYS A 1 4   ? 11.886  -14.153 8.796  1.000 31.310 0  4   LYS A N   1 
ATOM   22   C CA  . LYS A 1 4   ? 10.672  -14.373 8.023  1.000 31.610 0  4   LYS A CA  1 
ATOM   23   C C   . LYS A 1 4   ? 10.369  -15.857 7.881  1.000 32.450 0  4   LYS A C   1 
ATOM   24   O O   . LYS A 1 4   ? 9.199   -16.245 7.857  1.000 33.240 0  4   LYS A O   1 
ATOM   25   C CB  . LYS A 1 4   ? 10.786  -13.711 6.650  1.000 30.710 0  4   LYS A CB  1 
ATOM   26   C CG  . LYS A 1 4   ? 11.954  -14.181 5.804  1.000 31.750 0  4   LYS A CG  1 
ATOM   27   C CD  . LYS A 1 4   ? 12.053  -13.351 4.533  1.000 31.390 0  4   LYS A CD  1 
ATOM   28   C CE  . LYS A 1 4   ? 12.500  -14.189 3.348  1.000 31.960 0  4   LYS A CE  1 
ATOM   29   N NZ  . LYS A 1 4   ? 12.170  -13.535 2.051  1.000 32.090 1  4   LYS A NZ  1 
ATOM   30   N N   . ASP A 1 5   ? 11.394  -16.709 7.866  1.000 33.410 0  5   ASP A N   1 
ATOM   31   C CA  . ASP A 1 5   ? 11.159  -18.142 7.712  1.000 34.570 0  5   ASP A CA  1 
ATOM   32   C C   . ASP A 1 5   ? 10.632  -18.770 8.999  1.000 35.230 0  5   ASP A C   1 
ATOM   33   O O   . ASP A 1 5   ? 9.689   -19.574 8.961  1.000 33.970 0  5   ASP A O   1 
ATOM   34   C CB  . ASP A 1 5   ? 12.439  -18.838 7.249  1.000 37.060 0  5   ASP A CB  1 
ATOM   35   C CG  . ASP A 1 5   ? 12.809  -18.476 5.820  1.000 39.460 0  5   ASP A CG  1 
ATOM   36   O OD1 . ASP A 1 5   ? 11.935  -18.591 4.932  1.000 41.000 0  5   ASP A OD1 1 
ATOM   37   O OD2 . ASP A 1 5   ? 13.968  -18.074 5.580  1.000 39.390 -1 5   ASP A OD2 1 
ATOM   38   N N   . LEU A 1 6   ? 11.231  -18.423 10.142 1.000 34.290 0  6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? 10.688  -18.856 11.425 1.000 30.870 0  6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? 9.251   -18.377 11.593 1.000 31.730 0  6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? 8.368   -19.142 11.997 1.000 31.200 0  6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? 11.559  -18.326 12.563 1.000 30.720 0  6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? 12.896  -19.014 12.836 1.000 32.450 0  6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? 13.692  -18.200 13.832 1.000 30.950 0  6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? 12.688  -20.428 13.347 1.000 31.360 0  6   LEU A CD2 1 
ATOM   46   N N   . ALA A 1 7   ? 9.001   -17.102 11.284 1.000 31.390 0  7   ALA A N   1 
ATOM   47   C CA  . ALA A 1 7   ? 7.659   -16.551 11.423 1.000 31.750 0  7   ALA A CA  1 
ATOM   48   C C   . ALA A 1 7   ? 6.676   -17.230 10.476 1.000 31.810 0  7   ALA A C   1 
ATOM   49   O O   . ALA A 1 7   ? 5.513   -17.456 10.834 1.000 30.910 0  7   ALA A O   1 
ATOM   50   C CB  . ALA A 1 7   ? 7.688   -15.043 11.176 1.000 29.640 0  7   ALA A CB  1 
ATOM   51   N N   . LYS A 1 8   ? 7.125   -17.573 9.268  1.000 31.370 0  8   LYS A N   1 
ATOM   52   C CA  . LYS A 1 8   ? 6.239   -18.147 8.265  1.000 32.420 0  8   LYS A CA  1 
ATOM   53   C C   . LYS A 1 8   ? 5.912   -19.601 8.559  1.000 33.480 0  8   LYS A C   1 
ATOM   54   O O   . LYS A 1 8   ? 4.784   -20.041 8.302  1.000 33.190 0  8   LYS A O   1 
ATOM   55   C CB  . LYS A 1 8   ? 6.874   -18.018 6.879  1.000 30.850 0  8   LYS A CB  1 
ATOM   56   C CG  . LYS A 1 8   ? 6.213   -18.858 5.804  1.000 32.040 0  8   LYS A CG  1 
ATOM   57   C CD  . LYS A 1 8   ? 7.028   -18.866 4.523  1.000 32.720 0  8   LYS A CD  1 
ATOM   58   C CE  . LYS A 1 8   ? 6.890   -20.196 3.807  1.000 34.390 0  8   LYS A CE  1 
ATOM   59   N NZ  . LYS A 1 8   ? 8.124   -20.577 3.065  1.000 36.880 1  8   LYS A NZ  1 
ATOM   60   N N   . ALA A 1 9   ? 6.865   -20.354 9.116  1.000 34.210 0  9   ALA A N   1 
ATOM   61   C CA  . ALA A 1 9   ? 6.576   -21.722 9.524  1.000 32.440 0  9   ALA A CA  1 
ATOM   62   C C   . ALA A 1 9   ? 5.458   -21.799 10.556 1.000 34.320 0  9   ALA A C   1 
ATOM   63   O O   . ALA A 1 9   ? 4.783   -22.830 10.645 1.000 38.000 0  9   ALA A O   1 
ATOM   64   C CB  . ALA A 1 9   ? 7.841   -22.382 10.074 1.000 32.840 0  9   ALA A CB  1 
ATOM   65   N N   . LYS A 1 10  ? 5.239   -20.735 11.327 1.000 32.140 0  10  LYS A N   1 
ATOM   66   C CA  . LYS A 1 10  ? 4.162   -20.693 12.305 1.000 33.010 0  10  LYS A CA  1 
ATOM   67   C C   . LYS A 1 10  ? 2.917   -19.972 11.803 1.000 32.740 0  10  LYS A C   1 
ATOM   68   O O   . LYS A 1 10  ? 1.945   -19.862 12.552 1.000 31.510 0  10  LYS A O   1 
ATOM   69   C CB  . LYS A 1 10  ? 4.650   -20.038 13.597 1.000 33.050 0  10  LYS A CB  1 
ATOM   70   C CG  . LYS A 1 10  ? 5.822   -20.761 14.228 1.000 33.950 0  10  LYS A CG  1 
ATOM   71   C CD  . LYS A 1 10  ? 5.362   -21.741 15.289 1.000 32.840 0  10  LYS A CD  1 
ATOM   72   C CE  . LYS A 1 10  ? 6.492   -22.673 15.684 1.000 33.300 0  10  LYS A CE  1 
ATOM   73   N NZ  . LYS A 1 10  ? 6.378   -23.115 17.098 1.000 34.830 1  10  LYS A NZ  1 
ATOM   74   N N   . GLY A 1 11  ? 2.917   -19.492 10.563 1.000 34.960 0  11  GLY A N   1 
ATOM   75   C CA  . GLY A 1 11  ? 1.765   -18.795 10.033 1.000 30.990 0  11  GLY A CA  1 
ATOM   76   C C   . GLY A 1 11  ? 1.711   -17.316 10.331 1.000 30.450 0  11  GLY A C   1 
ATOM   77   O O   . GLY A 1 11  ? 0.613   -16.755 10.432 1.000 29.680 0  11  GLY A O   1 
ATOM   78   N N   . MET A 1 12  ? 2.859   -16.659 10.463 1.000 30.760 0  12  MET A N   1 
ATOM   79   C CA  . MET A 1 12  ? 2.926   -15.253 10.828 1.000 31.510 0  12  MET A CA  1 
ATOM   80   C C   . MET A 1 12  ? 3.785   -14.522 9.807  1.000 30.580 0  12  MET A C   1 
ATOM   81   O O   . MET A 1 12  ? 4.825   -15.033 9.383  1.000 31.760 0  12  MET A O   1 
ATOM   82   C CB  . MET A 1 12  ? 3.509   -15.069 12.241 1.000 29.460 0  12  MET A CB  1 
ATOM   83   C CG  . MET A 1 12  ? 4.300   -13.781 12.433 1.000 28.540 0  12  MET A CG  1 
ATOM   84   S SD  . MET A 1 12  ? 4.812   -13.481 14.137 1.000 30.150 0  12  MET A SD  1 
ATOM   85   C CE  . MET A 1 12  ? 3.246   -13.503 14.990 1.000 27.970 0  12  MET A CE  1 
ATOM   86   N N   . ARG A 1 13  ? 3.343   -13.334 9.407  1.000 29.970 0  13  ARG A N   1 
ATOM   87   C CA  . ARG A 1 13  ? 4.154   -12.489 8.547  1.000 31.360 0  13  ARG A CA  1 
ATOM   88   C C   . ARG A 1 13  ? 5.130   -11.670 9.381  1.000 33.380 0  13  ARG A C   1 
ATOM   89   O O   . ARG A 1 13  ? 4.813   -11.225 10.489 1.000 30.600 0  13  ARG A O   1 
ATOM   90   C CB  . ARG A 1 13  ? 3.280   -11.541 7.725  1.000 31.390 0  13  ARG A CB  1 
ATOM   91   C CG  . ARG A 1 13  ? 2.463   -12.194 6.634  1.000 34.290 0  13  ARG A CG  1 
ATOM   92   C CD  . ARG A 1 13  ? 1.381   -11.236 6.166  1.000 32.740 0  13  ARG A CD  1 
ATOM   93   N NE  . ARG A 1 13  ? 0.240   -11.238 7.071  1.000 30.760 0  13  ARG A NE  1 
ATOM   94   C CZ  . ARG A 1 13  ? -0.840  -11.990 6.910  1.000 34.350 0  13  ARG A CZ  1 
ATOM   95   N NH1 . ARG A 1 13  ? -0.988  -12.768 5.850  1.000 37.010 1  13  ARG A NH1 1 
ATOM   96   N NH2 . ARG A 1 13  ? -1.802  -11.948 7.828  1.000 33.480 0  13  ARG A NH2 1 
ATOM   97   N N   . PHE A 1 14  ? 6.319   -11.448 8.826  1.000 32.090 0  14  PHE A N   1 
ATOM   98   C CA  . PHE A 1 14  ? 7.348   -10.675 9.502  1.000 30.440 0  14  PHE A CA  1 
ATOM   99   C C   . PHE A 1 14  ? 7.793   -9.530  8.607  1.000 31.370 0  14  PHE A C   1 
ATOM   100  O O   . PHE A 1 14  ? 8.095   -9.732  7.423  1.000 34.070 0  14  PHE A O   1 
ATOM   101  C CB  . PHE A 1 14  ? 8.549   -11.539 9.884  1.000 29.200 0  14  PHE A CB  1 
ATOM   102  C CG  . PHE A 1 14  ? 9.416   -10.923 10.938 1.000 29.030 0  14  PHE A CG  1 
ATOM   103  C CD1 . PHE A 1 14  ? 9.086   -11.036 12.277 1.000 31.800 0  14  PHE A CD1 1 
ATOM   104  C CD2 . PHE A 1 14  ? 10.553  -10.214 10.591 1.000 29.970 0  14  PHE A CD2 1 
ATOM   105  C CE1 . PHE A 1 14  ? 9.882   -10.465 13.251 1.000 33.350 0  14  PHE A CE1 1 
ATOM   106  C CE2 . PHE A 1 14  ? 11.350  -9.638  11.560 1.000 29.950 0  14  PHE A CE2 1 
ATOM   107  C CZ  . PHE A 1 14  ? 11.015  -9.764  12.891 1.000 29.530 0  14  PHE A CZ  1 
ATOM   108  N N   . GLY A 1 15  ? 7.824   -8.331  9.173  1.000 29.100 0  15  GLY A N   1 
ATOM   109  C CA  . GLY A 1 15  ? 8.182   -7.168  8.398  1.000 28.890 0  15  GLY A CA  1 
ATOM   110  C C   . GLY A 1 15  ? 8.862   -6.102  9.220  1.000 28.440 0  15  GLY A C   1 
ATOM   111  O O   . GLY A 1 15  ? 9.215   -6.317  10.383 1.000 28.300 0  15  GLY A O   1 
ATOM   112  N N   . SER A 1 16  ? 9.052   -4.943  8.606  1.000 28.420 0  16  SER A N   1 
ATOM   113  C CA  . SER A 1 16  ? 9.775   -3.866  9.260  1.000 28.240 0  16  SER A CA  1 
ATOM   114  C C   . SER A 1 16  ? 9.419   -2.538  8.606  1.000 30.680 0  16  SER A C   1 
ATOM   115  O O   . SER A 1 16  ? 8.959   -2.484  7.459  1.000 30.580 0  16  SER A O   1 
ATOM   116  C CB  . SER A 1 16  ? 11.286  -4.106  9.223  1.000 30.320 0  16  SER A CB  1 
ATOM   117  O OG  . SER A 1 16  ? 11.977  -3.107  9.954  1.000 33.320 0  16  SER A OG  1 
ATOM   118  N N   . ALA A 1 17  ? 9.627   -1.468  9.363  1.000 28.610 0  17  ALA A N   1 
ATOM   119  C CA  . ALA A 1 17  ? 9.514   -0.126  8.823  1.000 28.470 0  17  ALA A CA  1 
ATOM   120  C C   . ALA A 1 17  ? 10.750  0.254   8.021  1.000 30.130 0  17  ALA A C   1 
ATOM   121  O O   . ALA A 1 17  ? 11.866  -0.190  8.300  1.000 29.260 0  17  ALA A O   1 
ATOM   122  C CB  . ALA A 1 17  ? 9.299   0.888   9.948  1.000 29.230 0  17  ALA A CB  1 
ATOM   123  N N   . ILE A 1 18  ? 10.537  1.112   7.030  1.000 31.290 0  18  ILE A N   1 
ATOM   124  C CA  . ILE A 1 18  ? 11.630  1.667   6.238  1.000 31.370 0  18  ILE A CA  1 
ATOM   125  C C   . ILE A 1 18  ? 11.187  3.035   5.739  1.000 29.660 0  18  ILE A C   1 
ATOM   126  O O   . ILE A 1 18  ? 10.012  3.243   5.427  1.000 32.620 0  18  ILE A O   1 
ATOM   127  C CB  . ILE A 1 18  ? 12.038  0.713   5.090  1.000 31.810 0  18  ILE A CB  1 
ATOM   128  C CG1 . ILE A 1 18  ? 13.431  1.067   4.561  1.000 32.700 0  18  ILE A CG1 1 
ATOM   129  C CG2 . ILE A 1 18  ? 11.007  0.718   3.972  1.000 29.270 0  18  ILE A CG2 1 
ATOM   130  C CD1 . ILE A 1 18  ? 13.900  0.175   3.428  1.000 30.950 0  18  ILE A CD1 1 
ATOM   131  N N   . GLY A 1 19  ? 12.122  3.989   5.708  1.000 29.940 0  19  GLY A N   1 
ATOM   132  C CA  . GLY A 1 19  ? 11.765  5.371   5.479  1.000 30.100 0  19  GLY A CA  1 
ATOM   133  C C   . GLY A 1 19  ? 12.711  6.070   4.525  1.000 31.760 0  19  GLY A C   1 
ATOM   134  O O   . GLY A 1 19  ? 13.793  5.576   4.199  1.000 33.210 0  19  GLY A O   1 
ATOM   135  N N   . LEU A 1 20  ? 12.281  7.257   4.100  1.000 33.300 0  20  LEU A N   1 
ATOM   136  C CA  . LEU A 1 20  ? 13.034  8.081   3.159  1.000 34.390 0  20  LEU A CA  1 
ATOM   137  C C   . LEU A 1 20  ? 13.056  9.563   3.507  1.000 36.680 0  20  LEU A C   1 
ATOM   138  O O   . LEU A 1 20  ? 14.060  10.221  3.216  1.000 37.720 0  20  LEU A O   1 
ATOM   139  C CB  . LEU A 1 20  ? 12.456  7.912   1.743  1.000 30.620 0  20  LEU A CB  1 
ATOM   140  C CG  . LEU A 1 20  ? 13.357  7.907   0.505  1.000 32.240 0  20  LEU A CG  1 
ATOM   141  C CD1 . LEU A 1 20  ? 12.567  7.386   -0.687 1.000 29.960 0  20  LEU A CD1 1 
ATOM   142  C CD2 . LEU A 1 20  ? 13.915  9.293   0.199  1.000 39.930 0  20  LEU A CD2 1 
ATOM   143  N N   . LEU A 1 21  ? 12.021  10.111  4.140  1.000 36.090 0  21  LEU A N   1 
ATOM   144  C CA  . LEU A 1 21  ? 11.891  11.558  4.260  1.000 37.610 0  21  LEU A CA  1 
ATOM   145  C C   . LEU A 1 21  ? 12.612  12.122  5.480  1.000 39.640 0  21  LEU A C   1 
ATOM   146  O O   . LEU A 1 21  ? 13.370  13.090  5.359  1.000 41.170 0  21  LEU A O   1 
ATOM   147  C CB  . LEU A 1 21  ? 10.412  11.947  4.311  1.000 37.240 0  21  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 21  ? 9.655   11.892  2.984  1.000 35.030 0  21  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 21  ? 8.157   11.946  3.231  1.000 34.170 0  21  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 21  ? 10.098  13.022  2.070  1.000 30.910 0  21  LEU A CD2 1 
ATOM   151  N N   . GLU A 1 22  ? 12.390  11.536  6.651  1.000 39.790 0  22  GLU A N   1 
ATOM   152  C CA  . GLU A 1 22  ? 12.783  12.151  7.910  1.000 42.680 0  22  GLU A CA  1 
ATOM   153  C C   . GLU A 1 22  ? 14.118  11.617  8.416  1.000 44.020 0  22  GLU A C   1 
ATOM   154  O O   . GLU A 1 22  ? 14.438  10.436  8.260  1.000 45.160 0  22  GLU A O   1 
ATOM   155  C CB  . GLU A 1 22  ? 11.690  11.941  8.958  1.000 44.130 0  22  GLU A CB  1 
ATOM   156  C CG  . GLU A 1 22  ? 10.296  12.152  8.381  1.000 43.660 0  22  GLU A CG  1 
ATOM   157  C CD  . GLU A 1 22  ? 9.341   12.813  9.354  1.000 46.100 0  22  GLU A CD  1 
ATOM   158  O OE1 . GLU A 1 22  ? 9.639   12.836  10.569 1.000 45.260 0  22  GLU A OE1 1 
ATOM   159  O OE2 . GLU A 1 22  ? 8.301   13.332  8.892  1.000 49.130 -1 22  GLU A OE2 1 
ATOM   160  N N   . ASP A 1 23  ? 14.884  12.515  9.040  1.000 45.220 0  23  ASP A N   1 
ATOM   161  C CA  . ASP A 1 23  ? 16.153  12.200  9.701  1.000 46.650 0  23  ASP A CA  1 
ATOM   162  C C   . ASP A 1 23  ? 17.108  11.473  8.752  1.000 46.420 0  23  ASP A C   1 
ATOM   163  O O   . ASP A 1 23  ? 17.557  10.357  9.010  1.000 47.060 0  23  ASP A O   1 
ATOM   164  C CB  . ASP A 1 23  ? 15.916  11.379  10.974 1.000 45.370 0  23  ASP A CB  1 
ATOM   165  C CG  . ASP A 1 23  ? 15.467  12.233  12.152 1.000 48.490 0  23  ASP A CG  1 
ATOM   166  O OD1 . ASP A 1 23  ? 16.316  12.941  12.735 1.000 51.470 0  23  ASP A OD1 1 
ATOM   167  O OD2 . ASP A 1 23  ? 14.266  12.192  12.498 1.000 47.310 -1 23  ASP A OD2 1 
ATOM   168  N N   . GLN A 1 24  ? 17.422  12.136  7.636  1.000 45.260 0  24  GLN A N   1 
ATOM   169  C CA  . GLN A 1 24  ? 18.129  11.444  6.562  1.000 47.560 0  24  GLN A CA  1 
ATOM   170  C C   . GLN A 1 24  ? 19.638  11.422  6.774  1.000 48.480 0  24  GLN A C   1 
ATOM   171  O O   . GLN A 1 24  ? 20.286  10.406  6.495  1.000 48.930 0  24  GLN A O   1 
ATOM   172  C CB  . GLN A 1 24  ? 17.793  12.080  5.215  1.000 46.570 0  24  GLN A CB  1 
ATOM   173  C CG  . GLN A 1 24  ? 16.687  11.362  4.461  1.000 45.170 0  24  GLN A CG  1 
ATOM   174  C CD  . GLN A 1 24  ? 16.745  9.850   4.624  1.000 43.310 0  24  GLN A CD  1 
ATOM   175  O OE1 . GLN A 1 24  ? 16.158  9.286   5.550  1.000 42.180 0  24  GLN A OE1 1 
ATOM   176  N NE2 . GLN A 1 24  ? 17.456  9.187   3.721  1.000 43.100 0  24  GLN A NE2 1 
ATOM   177  N N   . ASP A 1 25  ? 20.225  12.526  7.245  1.000 47.560 0  25  ASP A N   1 
ATOM   178  C CA  . ASP A 1 25  ? 21.669  12.539  7.445  1.000 48.730 0  25  ASP A CA  1 
ATOM   179  C C   . ASP A 1 25  ? 22.108  11.535  8.503  1.000 48.420 0  25  ASP A C   1 
ATOM   180  O O   . ASP A 1 25  ? 23.261  11.090  8.478  1.000 48.680 0  25  ASP A O   1 
ATOM   181  C CB  . ASP A 1 25  ? 22.162  13.945  7.804  1.000 48.680 0  25  ASP A CB  1 
ATOM   182  C CG  . ASP A 1 25  ? 21.292  14.634  8.834  1.000 51.510 0  25  ASP A CG  1 
ATOM   183  O OD1 . ASP A 1 25  ? 20.223  14.088  9.185  1.000 51.660 0  25  ASP A OD1 1 
ATOM   184  O OD2 . ASP A 1 25  ? 21.682  15.728  9.294  1.000 50.480 -1 25  ASP A OD2 1 
ATOM   185  N N   . THR A 1 26  ? 21.217  11.165  9.425  1.000 47.030 0  26  THR A N   1 
ATOM   186  C CA  . THR A 1 26  ? 21.549  10.267  10.525 1.000 47.750 0  26  THR A CA  1 
ATOM   187  C C   . THR A 1 26  ? 20.864  8.910   10.428 1.000 42.870 0  26  THR A C   1 
ATOM   188  O O   . THR A 1 26  ? 21.526  7.877   10.563 1.000 42.640 0  26  THR A O   1 
ATOM   189  C CB  . THR A 1 26  ? 21.193  10.933  11.863 1.000 44.940 0  26  THR A CB  1 
ATOM   190  O OG1 . THR A 1 26  ? 19.844  11.418  11.815 1.000 47.570 0  26  THR A OG1 1 
ATOM   191  C CG2 . THR A 1 26  ? 22.130  12.101  12.139 1.000 44.410 0  26  THR A CG2 1 
ATOM   192  N N   . ARG A 1 27  ? 19.556  8.879   10.196 1.000 43.750 0  27  ARG A N   1 
ATOM   193  C CA  . ARG A 1 27  ? 18.791  7.628   10.163 1.000 41.620 0  27  ARG A CA  1 
ATOM   194  C C   . ARG A 1 27  ? 18.533  7.159   8.732  1.000 40.790 0  27  ARG A C   1 
ATOM   195  O O   . ARG A 1 27  ? 17.406  6.843   8.350  1.000 40.060 0  27  ARG A O   1 
ATOM   196  C CB  . ARG A 1 27  ? 17.485  7.796   10.931 1.000 41.010 0  27  ARG A CB  1 
ATOM   197  C CG  . ARG A 1 27  ? 17.680  8.272   12.366 1.000 41.150 0  27  ARG A CG  1 
ATOM   198  C CD  . ARG A 1 27  ? 16.498  7.911   13.249 1.000 38.510 0  27  ARG A CD  1 
ATOM   199  N NE  . ARG A 1 27  ? 15.297  8.664   12.906 1.000 41.360 0  27  ARG A NE  1 
ATOM   200  C CZ  . ARG A 1 27  ? 14.254  8.159   12.262 1.000 40.430 0  27  ARG A CZ  1 
ATOM   201  N NH1 . ARG A 1 27  ? 14.223  6.892   11.884 1.000 34.710 1  27  ARG A NH1 1 
ATOM   202  N NH2 . ARG A 1 27  ? 13.212  8.944   11.999 1.000 42.110 0  27  ARG A NH2 1 
ATOM   203  N N   . LYS A 1 28  ? 19.593  7.101   7.931  1.000 41.450 0  28  LYS A N   1 
ATOM   204  C CA  . LYS A 1 28  ? 19.498  6.724   6.523  1.000 42.370 0  28  LYS A CA  1 
ATOM   205  C C   . LYS A 1 28  ? 19.133  5.246   6.408  1.000 40.210 0  28  LYS A C   1 
ATOM   206  O O   . LYS A 1 28  ? 19.926  4.373   6.773  1.000 38.940 0  28  LYS A O   1 
ATOM   207  C CB  . LYS A 1 28  ? 20.830  7.019   5.840  1.000 41.420 0  28  LYS A CB  1 
ATOM   208  C CG  . LYS A 1 28  ? 20.872  6.780   4.348  1.000 40.690 0  28  LYS A CG  1 
ATOM   209  C CD  . LYS A 1 28  ? 22.176  7.327   3.787  1.000 42.330 0  28  LYS A CD  1 
ATOM   210  C CE  . LYS A 1 28  ? 22.147  7.424   2.276  1.000 43.570 0  28  LYS A CE  1 
ATOM   211  N NZ  . LYS A 1 28  ? 22.592  8.767   1.809  1.000 45.990 1  28  LYS A NZ  1 
ATOM   212  N N   . SER A 1 29  ? 17.936  4.957   5.888  1.000 37.830 0  29  SER A N   1 
ATOM   213  C CA  . SER A 1 29  ? 17.423  3.589   5.845  1.000 34.880 0  29  SER A CA  1 
ATOM   214  C C   . SER A 1 29  ? 17.258  3.091   4.414  1.000 35.660 0  29  SER A C   1 
ATOM   215  O O   . SER A 1 29  ? 18.025  2.226   3.983  1.000 34.550 0  29  SER A O   1 
ATOM   216  C CB  . SER A 1 29  ? 16.105  3.493   6.616  1.000 32.470 0  29  SER A CB  1 
ATOM   217  O OG  . SER A 1 29  ? 15.012  3.883   5.804  1.000 32.540 0  29  SER A OG  1 
ATOM   218  N N   . PHE A 1 30  ? 16.268  3.589   3.665  1.000 35.380 0  30  PHE A N   1 
ATOM   219  C CA  . PHE A 1 30  ? 15.999  3.043   2.337  1.000 32.640 0  30  PHE A CA  1 
ATOM   220  C C   . PHE A 1 30  ? 17.135  3.312   1.357  1.000 32.400 0  30  PHE A C   1 
ATOM   221  O O   . PHE A 1 30  ? 17.394  2.486   0.474  1.000 31.590 0  30  PHE A O   1 
ATOM   222  C CB  . PHE A 1 30  ? 14.692  3.616   1.789  1.000 29.990 0  30  PHE A CB  1 
ATOM   223  C CG  . PHE A 1 30  ? 14.372  3.161   0.393  1.000 30.380 0  30  PHE A CG  1 
ATOM   224  C CD1 . PHE A 1 30  ? 13.774  1.933   0.171  1.000 30.460 0  30  PHE A CD1 1 
ATOM   225  C CD2 . PHE A 1 30  ? 14.674  3.960   -0.698 1.000 31.900 0  30  PHE A CD2 1 
ATOM   226  C CE1 . PHE A 1 30  ? 13.481  1.510   -1.111 1.000 30.840 0  30  PHE A CE1 1 
ATOM   227  C CE2 . PHE A 1 30  ? 14.385  3.543   -1.983 1.000 31.210 0  30  PHE A CE2 1 
ATOM   228  C CZ  . PHE A 1 30  ? 13.787  2.317   -2.190 1.000 31.140 0  30  PHE A CZ  1 
ATOM   229  N N   . ARG A 1 31  ? 17.817  4.449   1.488  1.000 33.010 0  31  ARG A N   1 
ATOM   230  C CA  . ARG A 1 31  ? 18.880  4.804   0.554  1.000 33.990 0  31  ARG A CA  1 
ATOM   231  C C   . ARG A 1 31  ? 20.154  3.993   0.765  1.000 34.380 0  31  ARG A C   1 
ATOM   232  O O   . ARG A 1 31  ? 21.091  4.126   -0.028 1.000 33.700 0  31  ARG A O   1 
ATOM   233  C CB  . ARG A 1 31  ? 19.178  6.299   0.656  1.000 36.680 0  31  ARG A CB  1 
ATOM   234  C CG  . ARG A 1 31  ? 17.992  7.190   0.311  1.000 36.060 0  31  ARG A CG  1 
ATOM   235  C CD  . ARG A 1 31  ? 18.102  7.747   -1.102 1.000 40.120 0  31  ARG A CD  1 
ATOM   236  N NE  . ARG A 1 31  ? 16.833  8.279   -1.589 1.000 39.680 0  31  ARG A NE  1 
ATOM   237  C CZ  . ARG A 1 31  ? 16.196  7.837   -2.665 1.000 38.960 0  31  ARG A CZ  1 
ATOM   238  N NH1 . ARG A 1 31  ? 16.685  6.855   -3.404 1.000 38.190 1  31  ARG A NH1 1 
ATOM   239  N NH2 . ARG A 1 31  ? 15.041  8.401   -3.011 1.000 38.250 0  31  ARG A NH2 1 
ATOM   240  N N   . ASP A 1 32  ? 20.211  3.169   1.809  1.000 33.550 0  32  ASP A N   1 
ATOM   241  C CA  . ASP A 1 32  ? 21.372  2.330   2.067  1.000 33.630 0  32  ASP A CA  1 
ATOM   242  C C   . ASP A 1 32  ? 21.126  0.974   1.421  1.000 36.550 0  32  ASP A C   1 
ATOM   243  O O   . ASP A 1 32  ? 20.270  0.219   1.906  1.000 38.130 0  32  ASP A O   1 
ATOM   244  C CB  . ASP A 1 32  ? 21.597  2.178   3.565  1.000 35.690 0  32  ASP A CB  1 
ATOM   245  C CG  . ASP A 1 32  ? 22.850  1.388   3.898  1.000 36.180 0  32  ASP A CG  1 
ATOM   246  O OD1 . ASP A 1 32  ? 23.563  0.955   2.965  1.000 34.010 0  32  ASP A OD1 1 
ATOM   247  O OD2 . ASP A 1 32  ? 23.119  1.199   5.102  1.000 34.440 -1 32  ASP A OD2 1 
ATOM   248  N N   . PRO A 1 33  ? 21.825  0.625   0.336  1.000 36.050 0  33  PRO A N   1 
ATOM   249  C CA  . PRO A 1 33  ? 21.540  -0.662  -0.324 1.000 33.300 0  33  PRO A CA  1 
ATOM   250  C C   . PRO A 1 33  ? 21.761  -1.870  0.570  1.000 36.370 0  33  PRO A C   1 
ATOM   251  O O   . PRO A 1 33  ? 20.994  -2.839  0.495  1.000 38.670 0  33  PRO A O   1 
ATOM   252  C CB  . PRO A 1 33  ? 22.498  -0.667  -1.527 1.000 33.430 0  33  PRO A CB  1 
ATOM   253  C CG  . PRO A 1 33  ? 23.076  0.710   -1.612 1.000 33.430 0  33  PRO A CG  1 
ATOM   254  C CD  . PRO A 1 33  ? 22.974  1.325   -0.259 1.000 34.960 0  33  PRO A CD  1 
ATOM   255  N N   . ALA A 1 34  ? 22.779  -1.832  1.435  1.000 36.880 0  34  ALA A N   1 
ATOM   256  C CA  . ALA A 1 34  ? 23.027  -2.958  2.330  1.000 37.500 0  34  ALA A CA  1 
ATOM   257  C C   . ALA A 1 34  ? 21.886  -3.133  3.326  1.000 34.960 0  34  ALA A C   1 
ATOM   258  O O   . ALA A 1 34  ? 21.501  -4.264  3.650  1.000 36.890 0  34  ALA A O   1 
ATOM   259  C CB  . ALA A 1 34  ? 24.360  -2.771  3.051  1.000 35.800 0  34  ALA A CB  1 
ATOM   260  N N   . TYR A 1 35  ? 21.333  -2.024  3.817  1.000 34.290 0  35  TYR A N   1 
ATOM   261  C CA  . TYR A 1 35  ? 20.192  -2.098  4.724  1.000 35.860 0  35  TYR A CA  1 
ATOM   262  C C   . TYR A 1 35  ? 18.964  -2.653  4.009  1.000 34.740 0  35  TYR A C   1 
ATOM   263  O O   . TYR A 1 35  ? 18.213  -3.459  4.578  1.000 34.500 0  35  TYR A O   1 
ATOM   264  C CB  . TYR A 1 35  ? 19.905  -0.718  5.313  1.000 33.690 0  35  TYR A CB  1 
ATOM   265  C CG  . TYR A 1 35  ? 18.801  -0.720  6.336  1.000 34.760 0  35  TYR A CG  1 
ATOM   266  C CD1 . TYR A 1 35  ? 19.061  -1.029  7.664  1.000 35.460 0  35  TYR A CD1 1 
ATOM   267  C CD2 . TYR A 1 35  ? 17.496  -0.415  5.976  1.000 35.310 0  35  TYR A CD2 1 
ATOM   268  C CE1 . TYR A 1 35  ? 18.049  -1.035  8.607  1.000 36.790 0  35  TYR A CE1 1 
ATOM   269  C CE2 . TYR A 1 35  ? 16.478  -0.420  6.908  1.000 35.630 0  35  TYR A CE2 1 
ATOM   270  C CZ  . TYR A 1 35  ? 16.760  -0.729  8.223  1.000 37.060 0  35  TYR A CZ  1 
ATOM   271  O OH  . TYR A 1 35  ? 15.747  -0.733  9.153  1.000 37.440 0  35  TYR A OH  1 
ATOM   272  N N   . ARG A 1 36  ? 18.743  -2.223  2.763  1.000 34.580 0  36  ARG A N   1 
ATOM   273  C CA  . ARG A 1 36  ? 17.669  -2.785  1.954  1.000 33.860 0  36  ARG A CA  1 
ATOM   274  C C   . ARG A 1 36  ? 17.826  -4.293  1.811  1.000 31.760 0  36  ARG A C   1 
ATOM   275  O O   . ARG A 1 36  ? 16.852  -5.045  1.934  1.000 32.310 0  36  ARG A O   1 
ATOM   276  C CB  . ARG A 1 36  ? 17.667  -2.130  0.572  1.000 33.000 0  36  ARG A CB  1 
ATOM   277  C CG  . ARG A 1 36  ? 16.837  -0.866  0.438  1.000 32.490 0  36  ARG A CG  1 
ATOM   278  C CD  . ARG A 1 36  ? 16.667  -0.513  -1.033 1.000 31.760 0  36  ARG A CD  1 
ATOM   279  N NE  . ARG A 1 36  ? 17.950  -0.473  -1.725 1.000 36.360 0  36  ARG A NE  1 
ATOM   280  C CZ  . ARG A 1 36  ? 18.439  0.594   -2.345 1.000 37.530 0  36  ARG A CZ  1 
ATOM   281  N NH1 . ARG A 1 36  ? 17.764  1.731   -2.401 1.000 38.250 1  36  ARG A NH1 1 
ATOM   282  N NH2 . ARG A 1 36  ? 19.640  0.521   -2.916 1.000 33.910 0  36  ARG A NH2 1 
ATOM   283  N N   . ALA A 1 37  ? 19.056  -4.753  1.563  1.000 32.790 0  37  ALA A N   1 
ATOM   284  C CA  . ALA A 1 37  ? 19.295  -6.180  1.382  1.000 32.810 0  37  ALA A CA  1 
ATOM   285  C C   . ALA A 1 37  ? 19.065  -6.955  2.672  1.000 34.090 0  37  ALA A C   1 
ATOM   286  O O   . ALA A 1 37  ? 18.495  -8.050  2.648  1.000 34.480 0  37  ALA A O   1 
ATOM   287  C CB  . ALA A 1 37  ? 20.714  -6.411  0.867  1.000 37.600 0  37  ALA A CB  1 
ATOM   288  N N   . LEU A 1 38  ? 19.487  -6.400  3.811  1.000 32.650 0  38  LEU A N   1 
ATOM   289  C CA  . LEU A 1 38  ? 19.232  -7.060  5.089  1.000 32.350 0  38  LEU A CA  1 
ATOM   290  C C   . LEU A 1 38  ? 17.736  -7.184  5.347  1.000 35.880 0  38  LEU A C   1 
ATOM   291  O O   . LEU A 1 38  ? 17.242  -8.247  5.757  1.000 36.590 0  38  LEU A O   1 
ATOM   292  C CB  . LEU A 1 38  ? 19.899  -6.289  6.226  1.000 31.940 0  38  LEU A CB  1 
ATOM   293  C CG  . LEU A 1 38  ? 19.459  -6.778  7.607  1.000 31.920 0  38  LEU A CG  1 
ATOM   294  C CD1 . LEU A 1 38  ? 19.907  -8.217  7.833  1.000 32.710 0  38  LEU A CD1 1 
ATOM   295  C CD2 . LEU A 1 38  ? 19.965  -5.863  8.708  1.000 32.530 0  38  LEU A CD2 1 
ATOM   296  N N   . MET A 1 39  ? 16.997  -6.094  5.121  1.000 33.130 0  39  MET A N   1 
ATOM   297  C CA  . MET A 1 39  ? 15.553  -6.137  5.306  1.000 31.740 0  39  MET A CA  1 
ATOM   298  C C   . MET A 1 39  ? 14.926  -7.192  4.410  1.000 33.090 0  39  MET A C   1 
ATOM   299  O O   . MET A 1 39  ? 14.090  -7.984  4.860  1.000 33.420 0  39  MET A O   1 
ATOM   300  C CB  . MET A 1 39  ? 14.945  -4.771  5.003  1.000 30.320 0  39  MET A CB  1 
ATOM   301  C CG  . MET A 1 39  ? 13.437  -4.773  5.064  1.000 32.460 0  39  MET A CG  1 
ATOM   302  S SD  . MET A 1 39  ? 12.754  -3.118  4.948  1.000 34.770 0  39  MET A SD  1 
ATOM   303  C CE  . MET A 1 39  ? 12.969  -2.558  6.629  1.000 32.600 0  39  MET A CE  1 
ATOM   304  N N   . ALA A 1 40  ? 15.335  -7.239  3.139  1.000 34.800 0  40  ALA A N   1 
ATOM   305  C CA  . ALA A 1 40  ? 14.786  -8.231  2.224  1.000 34.090 0  40  ALA A CA  1 
ATOM   306  C C   . ALA A 1 40  ? 15.171  -9.650  2.629  1.000 32.990 0  40  ALA A C   1 
ATOM   307  O O   . ALA A 1 40  ? 14.434  -10.595 2.334  1.000 33.990 0  40  ALA A O   1 
ATOM   308  C CB  . ALA A 1 40  ? 15.248  -7.948  0.795  1.000 34.400 0  40  ALA A CB  1 
ATOM   309  N N   . ARG A 1 41  ? 16.314  -9.821  3.292  1.000 33.300 0  41  ARG A N   1 
ATOM   310  C CA  . ARG A 1 41  ? 16.683  -11.149 3.772  1.000 34.730 0  41  ARG A CA  1 
ATOM   311  C C   . ARG A 1 41  ? 15.781  -11.595 4.913  1.000 34.550 0  41  ARG A C   1 
ATOM   312  O O   . ARG A 1 41  ? 15.205  -12.688 4.869  1.000 32.530 0  41  ARG A O   1 
ATOM   313  C CB  . ARG A 1 41  ? 18.140  -11.178 4.226  1.000 36.360 0  41  ARG A CB  1 
ATOM   314  C CG  . ARG A 1 41  ? 19.156  -11.072 3.120  1.000 40.060 0  41  ARG A CG  1 
ATOM   315  C CD  . ARG A 1 41  ? 20.529  -11.442 3.646  1.000 41.530 0  41  ARG A CD  1 
ATOM   316  N NE  . ARG A 1 41  ? 21.271  -10.254 4.052  1.000 41.080 0  41  ARG A NE  1 
ATOM   317  C CZ  . ARG A 1 41  ? 21.882  -9.429  3.214  1.000 42.640 0  41  ARG A CZ  1 
ATOM   318  N NH1 . ARG A 1 41  ? 21.868  -9.636  1.907  1.000 39.970 1  41  ARG A NH1 1 
ATOM   319  N NH2 . ARG A 1 41  ? 22.513  -8.364  3.697  1.000 40.880 0  41  ARG A NH2 1 
ATOM   320  N N   . GLU A 1 42  ? 15.645  -10.763 5.946  1.000 31.900 0  42  GLU A N   1 
ATOM   321  C CA  . GLU A 1 42  ? 14.986  -11.207 7.168  1.000 31.950 0  42  GLU A CA  1 
ATOM   322  C C   . GLU A 1 42  ? 13.480  -10.974 7.180  1.000 31.870 0  42  GLU A C   1 
ATOM   323  O O   . GLU A 1 42  ? 12.793  -11.533 8.044  1.000 30.370 0  42  GLU A O   1 
ATOM   324  C CB  . GLU A 1 42  ? 15.613  -10.521 8.383  1.000 32.380 0  42  GLU A CB  1 
ATOM   325  C CG  . GLU A 1 42  ? 17.128  -10.593 8.408  1.000 35.620 0  42  GLU A CG  1 
ATOM   326  C CD  . GLU A 1 42  ? 17.647  -12.001 8.649  1.000 35.240 0  42  GLU A CD  1 
ATOM   327  O OE1 . GLU A 1 42  ? 17.083  -12.706 9.512  1.000 32.780 0  42  GLU A OE1 1 
ATOM   328  O OE2 . GLU A 1 42  ? 18.632  -12.396 7.988  1.000 38.250 -1 42  GLU A OE2 1 
ATOM   329  N N   . CYS A 1 43  ? 12.947  -10.188 6.248  1.000 33.390 0  43  CYS A N   1 
ATOM   330  C CA  . CYS A 1 43  ? 11.554  -9.772  6.287  1.000 31.690 0  43  CYS A CA  1 
ATOM   331  C C   . CYS A 1 43  ? 10.871  -10.099 4.971  1.000 31.690 0  43  CYS A C   1 
ATOM   332  O O   . CYS A 1 43  ? 11.505  -10.137 3.913  1.000 33.720 0  43  CYS A O   1 
ATOM   333  C CB  . CYS A 1 43  ? 11.413  -8.268  6.547  1.000 29.990 0  43  CYS A CB  1 
ATOM   334  S SG  . CYS A 1 43  ? 12.120  -7.703  8.094  1.000 35.000 0  43  CYS A SG  1 
ATOM   335  N N   . ASN A 1 44  ? 9.562   -10.326 5.050  1.000 30.400 0  44  ASN A N   1 
ATOM   336  C CA  . ASN A 1 44  ? 8.716   -10.394 3.866  1.000 31.140 0  44  ASN A CA  1 
ATOM   337  C C   . ASN A 1 44  ? 7.592   -9.370  3.927  1.000 32.430 0  44  ASN A C   1 
ATOM   338  O O   . ASN A 1 44  ? 6.619   -9.474  3.173  1.000 31.570 0  44  ASN A O   1 
ATOM   339  C CB  . ASN A 1 44  ? 8.154   -11.806 3.679  1.000 30.540 0  44  ASN A CB  1 
ATOM   340  C CG  . ASN A 1 44  ? 7.265   -12.246 4.831  1.000 32.170 0  44  ASN A CG  1 
ATOM   341  O OD1 . ASN A 1 44  ? 6.841   -11.440 5.659  1.000 29.810 0  44  ASN A OD1 1 
ATOM   342  N ND2 . ASN A 1 44  ? 6.978   -13.540 4.884  1.000 31.250 0  44  ASN A ND2 1 
ATOM   343  N N   . MET A 1 45  ? 7.703   -8.384  4.818  1.000 32.150 0  45  MET A N   1 
ATOM   344  C CA  . MET A 1 45  ? 6.695   -7.343  4.928  1.000 30.180 0  45  MET A CA  1 
ATOM   345  C C   . MET A 1 45  ? 7.340   -5.990  5.177  1.000 32.610 0  45  MET A C   1 
ATOM   346  O O   . MET A 1 45  ? 8.296   -5.870  5.950  1.000 29.020 0  45  MET A O   1 
ATOM   347  C CB  . MET A 1 45  ? 5.701   -7.621  6.051  1.000 28.900 0  45  MET A CB  1 
ATOM   348  C CG  . MET A 1 45  ? 4.380   -6.914  5.870  1.000 28.640 0  45  MET A CG  1 
ATOM   349  S SD  . MET A 1 45  ? 3.144   -7.529  7.017  1.000 28.890 0  45  MET A SD  1 
ATOM   350  C CE  . MET A 1 45  ? 4.186   -8.150  8.337  1.000 28.580 0  45  MET A CE  1 
ATOM   351  N N   . ILE A 1 46  ? 6.769   -4.970  4.549  1.000 33.800 0  46  ILE A N   1 
ATOM   352  C CA  . ILE A 1 46  ? 7.283   -3.610  4.583  1.000 30.020 0  46  ILE A CA  1 
ATOM   353  C C   . ILE A 1 46  ? 6.195   -2.699  5.134  1.000 32.260 0  46  ILE A C   1 
ATOM   354  O O   . ILE A 1 46  ? 5.000   -2.931  4.910  1.000 31.700 0  46  ILE A O   1 
ATOM   355  C CB  . ILE A 1 46  ? 7.730   -3.151  3.179  1.000 29.210 0  46  ILE A CB  1 
ATOM   356  C CG1 . ILE A 1 46  ? 8.610   -1.908  3.262  1.000 30.380 0  46  ILE A CG1 1 
ATOM   357  C CG2 . ILE A 1 46  ? 6.527   -2.881  2.289  1.000 30.470 0  46  ILE A CG2 1 
ATOM   358  C CD1 . ILE A 1 46  ? 8.806   -1.232  1.924  1.000 32.960 0  46  ILE A CD1 1 
ATOM   359  N N   . VAL A 1 47  ? 6.606   -1.684  5.891  1.000 31.990 0  47  VAL A N   1 
ATOM   360  C CA  . VAL A 1 47  ? 5.712   -0.598  6.266  1.000 27.880 0  47  VAL A CA  1 
ATOM   361  C C   . VAL A 1 47  ? 6.477   0.714   6.145  1.000 28.160 0  47  VAL A C   1 
ATOM   362  O O   . VAL A 1 47  ? 7.702   0.763   6.312  1.000 30.430 0  47  VAL A O   1 
ATOM   363  C CB  . VAL A 1 47  ? 5.102   -0.793  7.679  1.000 28.890 0  47  VAL A CB  1 
ATOM   364  C CG1 . VAL A 1 47  ? 6.060   -0.365  8.764  1.000 28.030 0  47  VAL A CG1 1 
ATOM   365  C CG2 . VAL A 1 47  ? 3.789   -0.025  7.798  1.000 29.340 0  47  VAL A CG2 1 
ATOM   366  N N   . ALA A 1 48  ? 5.751   1.765   5.775  1.000 27.740 0  48  ALA A N   1 
ATOM   367  C CA  . ALA A 1 48  ? 6.336   3.083   5.565  1.000 28.140 0  48  ALA A CA  1 
ATOM   368  C C   . ALA A 1 48  ? 6.395   3.824   6.893  1.000 29.370 0  48  ALA A C   1 
ATOM   369  O O   . ALA A 1 48  ? 5.372   3.991   7.564  1.000 27.090 0  48  ALA A O   1 
ATOM   370  C CB  . ALA A 1 48  ? 5.532   3.876   4.537  1.000 27.810 0  48  ALA A CB  1 
ATOM   371  N N   . GLU A 1 49  ? 7.599   4.256   7.273  1.000 31.770 0  49  GLU A N   1 
ATOM   372  C CA  . GLU A 1 49  ? 7.771   4.931   8.554  1.000 30.760 0  49  GLU A CA  1 
ATOM   373  C C   . GLU A 1 49  ? 6.986   6.236   8.605  1.000 29.940 0  49  GLU A C   1 
ATOM   374  O O   . GLU A 1 49  ? 6.388   6.567   9.635  1.000 34.690 0  49  GLU A O   1 
ATOM   375  C CB  . GLU A 1 49  ? 9.259   5.185   8.804  1.000 33.690 0  49  GLU A CB  1 
ATOM   376  C CG  . GLU A 1 49  ? 9.605   5.660   10.205 1.000 34.530 0  49  GLU A CG  1 
ATOM   377  C CD  . GLU A 1 49  ? 11.107  5.741   10.430 1.000 36.330 0  49  GLU A CD  1 
ATOM   378  O OE1 . GLU A 1 49  ? 11.855  5.060   9.697  1.000 34.250 0  49  GLU A OE1 1 
ATOM   379  O OE2 . GLU A 1 49  ? 11.537  6.483   11.339 1.000 35.790 -1 49  GLU A OE2 1 
ATOM   380  N N   . ASN A 1 50  ? 6.975   6.990   7.506  1.000 30.240 0  50  ASN A N   1 
ATOM   381  C CA  . ASN A 1 50  ? 6.325   8.297   7.488  1.000 30.200 0  50  ASN A CA  1 
ATOM   382  C C   . ASN A 1 50  ? 5.712   8.627   6.132  1.000 30.000 0  50  ASN A C   1 
ATOM   383  O O   . ASN A 1 50  ? 4.968   9.604   6.010  1.000 29.880 0  50  ASN A O   1 
ATOM   384  C CB  . ASN A 1 50  ? 7.315   9.396   7.881  1.000 32.980 0  50  ASN A CB  1 
ATOM   385  C CG  . ASN A 1 50  ? 7.671   9.358   9.352  1.000 35.680 0  50  ASN A CG  1 
ATOM   386  O OD1 . ASN A 1 50  ? 6.793   9.384   10.217 1.000 33.610 0  50  ASN A OD1 1 
ATOM   387  N ND2 . ASN A 1 50  ? 8.965   9.304   9.643  1.000 34.540 0  50  ASN A ND2 1 
ATOM   388  N N   . GLU A 1 51  ? 6.007   7.821   5.112  1.000 29.710 0  51  GLU A N   1 
ATOM   389  C CA  . GLU A 1 51  ? 5.745   8.231   3.737  1.000 27.710 0  51  GLU A CA  1 
ATOM   390  C C   . GLU A 1 51  ? 4.282   8.110   3.338  1.000 28.340 0  51  GLU A C   1 
ATOM   391  O O   . GLU A 1 51  ? 3.900   8.648   2.295  1.000 29.030 0  51  GLU A O   1 
ATOM   392  C CB  . GLU A 1 51  ? 6.598   7.407   2.772  1.000 28.110 0  51  GLU A CB  1 
ATOM   393  C CG  . GLU A 1 51  ? 8.039   7.879   2.641  1.000 30.470 0  51  GLU A CG  1 
ATOM   394  C CD  . GLU A 1 51  ? 8.774   7.918   3.968  1.000 32.530 0  51  GLU A CD  1 
ATOM   395  O OE1 . GLU A 1 51  ? 8.536   7.023   4.808  1.000 29.970 0  51  GLU A OE1 1 
ATOM   396  O OE2 . GLU A 1 51  ? 9.591   8.841   4.167  1.000 32.420 -1 51  GLU A OE2 1 
ATOM   397  N N   . THR A 1 52  ? 3.453   7.437   4.138  1.000 27.440 0  52  THR A N   1 
ATOM   398  C CA  . THR A 1 52  ? 2.023   7.350   3.867  1.000 27.400 0  52  THR A CA  1 
ATOM   399  C C   . THR A 1 52  ? 1.202   7.971   4.990  1.000 27.350 0  52  THR A C   1 
ATOM   400  O O   . THR A 1 52  ? 0.009   7.682   5.118  1.000 26.950 0  52  THR A O   1 
ATOM   401  C CB  . THR A 1 52  ? 1.588   5.900   3.630  1.000 27.510 0  52  THR A CB  1 
ATOM   402  O OG1 . THR A 1 52  ? 2.188   5.043   4.610  1.000 28.370 0  52  THR A OG1 1 
ATOM   403  C CG2 . THR A 1 52  ? 1.998   5.437   2.237  1.000 27.920 0  52  THR A CG2 1 
ATOM   404  N N   . LYS A 1 53  ? 1.821   8.812   5.814  1.000 27.990 0  53  LYS A N   1 
ATOM   405  C CA  . LYS A 1 53  ? 1.071   9.638   6.744  1.000 27.850 0  53  LYS A CA  1 
ATOM   406  C C   . LYS A 1 53  ? 0.503   10.849  6.015  1.000 29.080 0  53  LYS A C   1 
ATOM   407  O O   . LYS A 1 53  ? 1.023   11.278  4.980  1.000 28.500 0  53  LYS A O   1 
ATOM   408  C CB  . LYS A 1 53  ? 1.956   10.077  7.911  1.000 28.580 0  53  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 53  ? 1.992   9.075   9.060  1.000 29.970 0  53  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 53  ? 3.212   9.267   9.950  1.000 30.780 0  53  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 53  ? 3.529   7.992   10.720 1.000 29.910 0  53  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 53  ? 4.693   8.136   11.637 1.000 32.200 1  53  LYS A NZ  1 
ATOM   413  N N   . TRP A 1 54  ? -0.588  11.392  6.560  1.000 27.240 0  54  TRP A N   1 
ATOM   414  C CA  . TRP A 1 54  ? -1.256  12.508  5.898  1.000 26.550 0  54  TRP A CA  1 
ATOM   415  C C   . TRP A 1 54  ? -0.317  13.697  5.737  1.000 26.930 0  54  TRP A C   1 
ATOM   416  O O   . TRP A 1 54  ? -0.334  14.374  4.703  1.000 28.230 0  54  TRP A O   1 
ATOM   417  C CB  . TRP A 1 54  ? -2.509  12.906  6.673  1.000 26.340 0  54  TRP A CB  1 
ATOM   418  C CG  . TRP A 1 54  ? -3.564  13.514  5.812  1.000 26.510 0  54  TRP A CG  1 
ATOM   419  C CD1 . TRP A 1 54  ? -3.426  13.949  4.526  1.000 26.800 0  54  TRP A CD1 1 
ATOM   420  C CD2 . TRP A 1 54  ? -4.925  13.759  6.173  1.000 26.430 0  54  TRP A CD2 1 
ATOM   421  N NE1 . TRP A 1 54  ? -4.618  14.451  4.064  1.000 26.910 0  54  TRP A NE1 1 
ATOM   422  C CE2 . TRP A 1 54  ? -5.555  14.345  5.059  1.000 26.680 0  54  TRP A CE2 1 
ATOM   423  C CE3 . TRP A 1 54  ? -5.673  13.540  7.335  1.000 26.310 0  54  TRP A CE3 1 
ATOM   424  C CZ2 . TRP A 1 54  ? -6.898  14.714  5.068  1.000 26.700 0  54  TRP A CZ2 1 
ATOM   425  C CZ3 . TRP A 1 54  ? -7.007  13.908  7.343  1.000 28.150 0  54  TRP A CZ3 1 
ATOM   426  C CH2 . TRP A 1 54  ? -7.605  14.489  6.216  1.000 26.590 0  54  TRP A CH2 1 
ATOM   427  N N   . GLN A 1 55  ? 0.521   13.959  6.742  1.000 27.050 0  55  GLN A N   1 
ATOM   428  C CA  . GLN A 1 55  ? 1.435   15.093  6.680  1.000 28.880 0  55  GLN A CA  1 
ATOM   429  C C   . GLN A 1 55  ? 2.449   14.957  5.553  1.000 28.650 0  55  GLN A C   1 
ATOM   430  O O   . GLN A 1 55  ? 2.973   15.971  5.080  1.000 30.690 0  55  GLN A O   1 
ATOM   431  C CB  . GLN A 1 55  ? 2.171   15.255  8.010  1.000 27.470 0  55  GLN A CB  1 
ATOM   432  C CG  . GLN A 1 55  ? 1.475   16.172  8.994  1.000 27.180 0  55  GLN A CG  1 
ATOM   433  C CD  . GLN A 1 55  ? 2.025   16.036  10.398 1.000 26.970 0  55  GLN A CD  1 
ATOM   434  O OE1 . GLN A 1 55  ? 2.790   15.118  10.692 1.000 26.110 0  55  GLN A OE1 1 
ATOM   435  N NE2 . GLN A 1 55  ? 1.636   16.953  11.274 1.000 26.030 0  55  GLN A NE2 1 
ATOM   436  N N   . ALA A 1 56  ? 2.746   13.734  5.118  1.000 28.490 0  56  ALA A N   1 
ATOM   437  C CA  . ALA A 1 56  ? 3.684   13.538  4.020  1.000 29.720 0  56  ALA A CA  1 
ATOM   438  C C   . ALA A 1 56  ? 3.008   13.548  2.656  1.000 31.790 0  56  ALA A C   1 
ATOM   439  O O   . ALA A 1 56  ? 3.622   13.979  1.673  1.000 31.930 0  56  ALA A O   1 
ATOM   440  C CB  . ALA A 1 56  ? 4.443   12.220  4.202  1.000 27.280 0  56  ALA A CB  1 
ATOM   441  N N   . LEU A 1 57  ? 1.757   13.088  2.574  1.000 31.280 0  57  LEU A N   1 
ATOM   442  C CA  . LEU A 1 57  ? 1.089   12.993  1.280  1.000 29.340 0  57  LEU A CA  1 
ATOM   443  C C   . LEU A 1 57  ? 0.473   14.323  0.866  1.000 29.910 0  57  LEU A C   1 
ATOM   444  O O   . LEU A 1 57  ? 0.563   14.717  -0.301 1.000 31.790 0  57  LEU A O   1 
ATOM   445  C CB  . LEU A 1 57  ? 0.026   11.899  1.328  1.000 28.320 0  57  LEU A CB  1 
ATOM   446  C CG  . LEU A 1 57  ? 0.579   10.479  1.449  1.000 27.950 0  57  LEU A CG  1 
ATOM   447  C CD1 . LEU A 1 57  ? -0.454  9.535   2.041  1.000 27.600 0  57  LEU A CD1 1 
ATOM   448  C CD2 . LEU A 1 57  ? 1.047   9.987   0.095  1.000 28.200 0  57  LEU A CD2 1 
ATOM   449  N N   . GLN A 1 58  ? -0.156  15.026  1.801  1.000 29.160 0  58  GLN A N   1 
ATOM   450  C CA  . GLN A 1 58  ? -0.853  16.277  1.515  1.000 29.320 0  58  GLN A CA  1 
ATOM   451  C C   . GLN A 1 58  ? -0.459  17.307  2.567  1.000 30.190 0  58  GLN A C   1 
ATOM   452  O O   . GLN A 1 58  ? -1.291  17.738  3.375  1.000 29.100 0  58  GLN A O   1 
ATOM   453  C CB  . GLN A 1 58  ? -2.366  16.060  1.484  1.000 27.580 0  58  GLN A CB  1 
ATOM   454  C CG  . GLN A 1 58  ? -3.079  16.750  0.336  1.000 28.690 0  58  GLN A CG  1 
ATOM   455  C CD  . GLN A 1 58  ? -4.567  16.462  0.326  1.000 27.870 0  58  GLN A CD  1 
ATOM   456  O OE1 . GLN A 1 58  ? -5.081  15.772  1.206  1.000 28.390 0  58  GLN A OE1 1 
ATOM   457  N NE2 . GLN A 1 58  ? -5.268  16.993  -0.666 1.000 28.160 0  58  GLN A NE2 1 
ATOM   458  N N   . PRO A 1 59  ? 0.807   17.738  2.575  1.000 29.150 0  59  PRO A N   1 
ATOM   459  C CA  . PRO A 1 59  ? 1.221   18.734  3.573  1.000 29.680 0  59  PRO A CA  1 
ATOM   460  C C   . PRO A 1 59  ? 0.582   20.088  3.341  1.000 30.070 0  59  PRO A C   1 
ATOM   461  O O   . PRO A 1 59  ? 0.489   20.886  4.281  1.000 32.190 0  59  PRO A O   1 
ATOM   462  C CB  . PRO A 1 59  ? 2.746   18.795  3.406  1.000 28.610 0  59  PRO A CB  1 
ATOM   463  C CG  . PRO A 1 59  ? 2.995   18.370  2.002  1.000 27.950 0  59  PRO A CG  1 
ATOM   464  C CD  . PRO A 1 59  ? 1.857   17.477  1.573  1.000 29.300 0  59  PRO A CD  1 
ATOM   465  N N   . LYS A 1 60  ? 0.132   20.356  2.125  1.000 28.140 0  60  LYS A N   1 
ATOM   466  C CA  . LYS A 1 60  ? -0.657  21.523  1.773  1.000 29.400 0  60  LYS A CA  1 
ATOM   467  C C   . LYS A 1 60  ? -1.688  21.072  0.753  1.000 29.160 0  60  LYS A C   1 
ATOM   468  O O   . LYS A 1 60  ? -1.557  19.987  0.175  1.000 31.450 0  60  LYS A O   1 
ATOM   469  C CB  . LYS A 1 60  ? 0.215   22.661  1.221  1.000 29.200 0  60  LYS A CB  1 
ATOM   470  C CG  . LYS A 1 60  ? 0.922   22.360  -0.084 1.000 33.470 0  60  LYS A CG  1 
ATOM   471  C CD  . LYS A 1 60  ? 2.130   23.270  -0.256 1.000 35.690 0  60  LYS A CD  1 
ATOM   472  C CE  . LYS A 1 60  ? 3.345   22.503  -0.747 1.000 38.440 0  60  LYS A CE  1 
ATOM   473  N NZ  . LYS A 1 60  ? 4.564   23.361  -0.790 1.000 41.720 1  60  LYS A NZ  1 
ATOM   474  N N   . PRO A 1 61  ? -2.762  21.854  0.552  1.000 27.970 0  61  PRO A N   1 
ATOM   475  C CA  . PRO A 1 61  ? -3.802  21.439  -0.403 1.000 28.220 0  61  PRO A CA  1 
ATOM   476  C C   . PRO A 1 61  ? -3.268  21.123  -1.795 1.000 28.610 0  61  PRO A C   1 
ATOM   477  O O   . PRO A 1 61  ? -2.170  21.546  -2.174 1.000 31.090 0  61  PRO A O   1 
ATOM   478  C CB  . PRO A 1 61  ? -4.759  22.639  -0.437 1.000 28.290 0  61  PRO A CB  1 
ATOM   479  C CG  . PRO A 1 61  ? -4.305  23.589  0.628  1.000 28.050 0  61  PRO A CG  1 
ATOM   480  C CD  . PRO A 1 61  ? -3.217  22.949  1.422  1.000 27.790 0  61  PRO A CD  1 
ATOM   481  N N   . GLY A 1 62  ? -4.060  20.383  -2.569 1.000 29.720 0  62  GLY A N   1 
ATOM   482  C CA  . GLY A 1 62  ? -3.669  19.928  -3.882 1.000 31.470 0  62  GLY A CA  1 
ATOM   483  C C   . GLY A 1 62  ? -3.375  18.440  -3.908 1.000 33.380 0  62  GLY A C   1 
ATOM   484  O O   . GLY A 1 62  ? -3.776  17.692  -3.010 1.000 31.850 0  62  GLY A O   1 
ATOM   485  N N   . PRO A 1 63  ? -2.660  17.981  -4.933 1.000 32.530 0  63  PRO A N   1 
ATOM   486  C CA  . PRO A 1 63  ? -2.505  16.535  -5.139 1.000 31.590 0  63  PRO A CA  1 
ATOM   487  C C   . PRO A 1 63  ? -1.592  15.916  -4.093 1.000 30.620 0  63  PRO A C   1 
ATOM   488  O O   . PRO A 1 63  ? -0.883  16.600  -3.352 1.000 32.880 0  63  PRO A O   1 
ATOM   489  C CB  . PRO A 1 63  ? -1.904  16.429  -6.543 1.000 30.610 0  63  PRO A CB  1 
ATOM   490  C CG  . PRO A 1 63  ? -1.251  17.741  -6.789 1.000 30.840 0  63  PRO A CG  1 
ATOM   491  C CD  . PRO A 1 63  ? -1.951  18.777  -5.951 1.000 30.090 0  63  PRO A CD  1 
ATOM   492  N N   . TYR A 1 64  ? -1.618  14.585  -4.043 1.000 30.360 0  64  TYR A N   1 
ATOM   493  C CA  . TYR A 1 64  ? -0.872  13.845  -3.035 1.000 31.050 0  64  TYR A CA  1 
ATOM   494  C C   . TYR A 1 64  ? 0.592   13.701  -3.448 1.000 29.120 0  64  TYR A C   1 
ATOM   495  O O   . TYR A 1 64  ? 0.951   13.829  -4.620 1.000 31.590 0  64  TYR A O   1 
ATOM   496  C CB  . TYR A 1 64  ? -1.498  12.465  -2.798 1.000 28.830 0  64  TYR A CB  1 
ATOM   497  C CG  . TYR A 1 64  ? -2.709  12.478  -1.880 1.000 28.950 0  64  TYR A CG  1 
ATOM   498  C CD1 . TYR A 1 64  ? -3.783  13.320  -2.130 1.000 29.160 0  64  TYR A CD1 1 
ATOM   499  C CD2 . TYR A 1 64  ? -2.782  11.642  -0.769 1.000 28.210 0  64  TYR A CD2 1 
ATOM   500  C CE1 . TYR A 1 64  ? -4.890  13.341  -1.300 1.000 29.390 0  64  TYR A CE1 1 
ATOM   501  C CE2 . TYR A 1 64  ? -3.892  11.655  0.068  1.000 27.950 0  64  TYR A CE2 1 
ATOM   502  C CZ  . TYR A 1 64  ? -4.942  12.508  -0.207 1.000 28.000 0  64  TYR A CZ  1 
ATOM   503  O OH  . TYR A 1 64  ? -6.053  12.538  0.609  1.000 27.780 0  64  TYR A OH  1 
ATOM   504  N N   . GLN A 1 65  ? 1.439   13.430  -2.459 1.000 28.870 0  65  GLN A N   1 
ATOM   505  C CA  . GLN A 1 65  ? 2.883   13.315  -2.653 1.000 29.040 0  65  GLN A CA  1 
ATOM   506  C C   . GLN A 1 65  ? 3.246   11.840  -2.516 1.000 29.060 0  65  GLN A C   1 
ATOM   507  O O   . GLN A 1 65  ? 3.707   11.383  -1.469 1.000 28.800 0  65  GLN A O   1 
ATOM   508  C CB  . GLN A 1 65  ? 3.641   14.176  -1.637 1.000 31.450 0  65  GLN A CB  1 
ATOM   509  C CG  . GLN A 1 65  ? 3.371   15.666  -1.735 1.000 30.640 0  65  GLN A CG  1 
ATOM   510  C CD  . GLN A 1 65  ? 3.966   16.286  -2.978 1.000 39.280 0  65  GLN A CD  1 
ATOM   511  O OE1 . GLN A 1 65  ? 5.188   16.400  -3.106 1.000 42.100 0  65  GLN A OE1 1 
ATOM   512  N NE2 . GLN A 1 65  ? 3.106   16.695  -3.907 1.000 39.920 0  65  GLN A NE2 1 
ATOM   513  N N   . TRP A 1 66  ? 3.039   11.092  -3.595 1.000 29.400 0  66  TRP A N   1 
ATOM   514  C CA  . TRP A 1 66  ? 3.248   9.653   -3.577 1.000 29.470 0  66  TRP A CA  1 
ATOM   515  C C   . TRP A 1 66  ? 4.678   9.249   -3.907 1.000 29.740 0  66  TRP A C   1 
ATOM   516  O O   . TRP A 1 66  ? 4.995   8.059   -3.828 1.000 29.810 0  66  TRP A O   1 
ATOM   517  C CB  . TRP A 1 66  ? 2.294   8.965   -4.558 1.000 29.730 0  66  TRP A CB  1 
ATOM   518  C CG  . TRP A 1 66  ? 0.855   8.944   -4.124 1.000 29.470 0  66  TRP A CG  1 
ATOM   519  C CD1 . TRP A 1 66  ? -0.185  9.619   -4.697 1.000 29.560 0  66  TRP A CD1 1 
ATOM   520  C CD2 . TRP A 1 66  ? 0.295   8.199   -3.035 1.000 29.130 0  66  TRP A CD2 1 
ATOM   521  N NE1 . TRP A 1 66  ? -1.356  9.342   -4.032 1.000 29.290 0  66  TRP A NE1 1 
ATOM   522  C CE2 . TRP A 1 66  ? -1.087  8.474   -3.006 1.000 29.020 0  66  TRP A CE2 1 
ATOM   523  C CE3 . TRP A 1 66  ? 0.829   7.326   -2.082 1.000 28.920 0  66  TRP A CE3 1 
ATOM   524  C CZ2 . TRP A 1 66  ? -1.941  7.910   -2.061 1.000 28.720 0  66  TRP A CZ2 1 
ATOM   525  C CZ3 . TRP A 1 66  ? -0.020  6.769   -1.143 1.000 28.620 0  66  TRP A CZ3 1 
ATOM   526  C CH2 . TRP A 1 66  ? -1.390  7.061   -1.141 1.000 28.520 0  66  TRP A CH2 1 
ATOM   527  N N   . GLY A 1 67  ? 5.539   10.204  -4.264 1.000 29.900 0  67  GLY A N   1 
ATOM   528  C CA  . GLY A 1 67  ? 6.879   9.925   -4.736 1.000 30.230 0  67  GLY A CA  1 
ATOM   529  C C   . GLY A 1 67  ? 7.668   8.940   -3.891 1.000 30.110 0  67  GLY A C   1 
ATOM   530  O O   . GLY A 1 67  ? 8.029   7.849   -4.349 1.000 30.370 0  67  GLY A O   1 
ATOM   531  N N   . PRO A 1 68  ? 7.951   9.307   -2.636 1.000 29.720 0  68  PRO A N   1 
ATOM   532  C CA  . PRO A 1 68  ? 8.756   8.409   -1.791 1.000 29.620 0  68  PRO A CA  1 
ATOM   533  C C   . PRO A 1 68  ? 8.072   7.088   -1.504 1.000 29.530 0  68  PRO A C   1 
ATOM   534  O O   . PRO A 1 68  ? 8.722   6.030   -1.543 1.000 29.710 0  68  PRO A O   1 
ATOM   535  C CB  . PRO A 1 68  ? 8.964   9.232   -0.511 1.000 29.210 0  68  PRO A CB  1 
ATOM   536  C CG  . PRO A 1 68  ? 8.690   10.655  -0.913 1.000 29.220 0  68  PRO A CG  1 
ATOM   537  C CD  . PRO A 1 68  ? 7.616   10.560  -1.942 1.000 29.400 0  68  PRO A CD  1 
ATOM   538  N N   . ALA A 1 69  ? 6.770   7.123   -1.204 1.000 29.260 0  69  ALA A N   1 
ATOM   539  C CA  . ALA A 1 69  ? 6.026   5.891   -0.984 1.000 29.190 0  69  ALA A CA  1 
ATOM   540  C C   . ALA A 1 69  ? 6.021   5.020   -2.232 1.000 29.640 0  69  ALA A C   1 
ATOM   541  O O   . ALA A 1 69  ? 6.226   3.805   -2.144 1.000 29.730 0  69  ALA A O   1 
ATOM   542  C CB  . ALA A 1 69  ? 4.597   6.211   -0.548 1.000 28.880 0  69  ALA A CB  1 
ATOM   543  N N   . ASP A 1 70  ? 5.812   5.625   -3.406 1.000 29.930 0  70  ASP A N   1 
ATOM   544  C CA  . ASP A 1 70  ? 5.829   4.854   -4.646 1.000 30.390 0  70  ASP A CA  1 
ATOM   545  C C   . ASP A 1 70  ? 7.186   4.202   -4.866 1.000 30.690 0  70  ASP A C   1 
ATOM   546  O O   . ASP A 1 70  ? 7.265   3.036   -5.262 1.000 30.940 0  70  ASP A O   1 
ATOM   547  C CB  . ASP A 1 70  ? 5.479   5.745   -5.838 1.000 30.670 0  70  ASP A CB  1 
ATOM   548  C CG  . ASP A 1 70  ? 3.994   6.030   -5.943 1.000 30.510 0  70  ASP A CG  1 
ATOM   549  O OD1 . ASP A 1 70  ? 3.204   5.396   -5.212 1.000 30.220 0  70  ASP A OD1 1 
ATOM   550  O OD2 . ASP A 1 70  ? 3.616   6.891   -6.769 1.000 30.700 -1 70  ASP A OD2 1 
ATOM   551  N N   . GLU A 1 71  ? 8.265   4.941   -4.603 1.000 30.700 0  71  GLU A N   1 
ATOM   552  C CA  . GLU A 1 71  ? 9.607   4.390   -4.765 1.000 31.010 0  71  GLU A CA  1 
ATOM   553  C C   . GLU A 1 71  ? 9.827   3.188   -3.851 1.000 30.860 0  71  GLU A C   1 
ATOM   554  O O   . GLU A 1 71  ? 10.170  2.087   -4.314 1.000 31.180 0  71  GLU A O   1 
ATOM   555  C CB  . GLU A 1 71  ? 10.630  5.490   -4.478 1.000 30.990 0  71  GLU A CB  1 
ATOM   556  C CG  . GLU A 1 71  ? 12.070  5.145   -4.783 1.000 31.380 0  71  GLU A CG  1 
ATOM   557  C CD  . GLU A 1 71  ? 13.006  6.296   -4.462 1.000 31.340 0  71  GLU A CD  1 
ATOM   558  O OE1 . GLU A 1 71  ? 12.508  7.379   -4.081 1.000 31.030 0  71  GLU A OE1 1 
ATOM   559  O OE2 . GLU A 1 71  ? 14.236  6.121   -4.596 1.000 32.590 -1 71  GLU A OE2 1 
ATOM   560  N N   . MET A 1 72  ? 9.603   3.374   -2.546 1.000 30.390 0  72  MET A N   1 
ATOM   561  C CA  . MET A 1 72  ? 9.858   2.283   -1.612 1.000 30.250 0  72  MET A CA  1 
ATOM   562  C C   . MET A 1 72  ? 8.932   1.103   -1.855 1.000 30.300 0  72  MET A C   1 
ATOM   563  O O   . MET A 1 72  ? 9.335   -0.048  -1.667 1.000 30.690 0  72  MET A O   1 
ATOM   564  C CB  . MET A 1 72  ? 9.719   2.757   -0.169 1.000 29.750 0  72  MET A CB  1 
ATOM   565  C CG  . MET A 1 72  ? 10.689  3.836   0.237  1.000 29.680 0  72  MET A CG  1 
ATOM   566  S SD  . MET A 1 72  ? 10.614  4.051   2.017  1.000 29.150 0  72  MET A SD  1 
ATOM   567  C CE  . MET A 1 72  ? 8.882   4.455   2.217  1.000 28.790 0  72  MET A CE  1 
ATOM   568  N N   . PHE A 1 73  ? 7.705   1.349   -2.308 1.000 30.220 0  73  PHE A N   1 
ATOM   569  C CA  . PHE A 1 73  ? 6.775   0.243   -2.471 1.000 30.250 0  73  PHE A CA  1 
ATOM   570  C C   . PHE A 1 73  ? 7.014   -0.486  -3.784 1.000 30.770 0  73  PHE A C   1 
ATOM   571  O O   . PHE A 1 73  ? 6.763   -1.691  -3.868 1.000 31.730 0  73  PHE A O   1 
ATOM   572  C CB  . PHE A 1 73  ? 5.332   0.745   -2.368 1.000 29.970 0  73  PHE A CB  1 
ATOM   573  C CG  . PHE A 1 73  ? 4.934   1.164   -0.972 1.000 29.460 0  73  PHE A CG  1 
ATOM   574  C CD1 . PHE A 1 73  ? 5.827   1.054   0.083  1.000 29.280 0  73  PHE A CD1 1 
ATOM   575  C CD2 . PHE A 1 73  ? 3.673   1.682   -0.719 1.000 29.190 0  73  PHE A CD2 1 
ATOM   576  C CE1 . PHE A 1 73  ? 5.472   1.443   1.362  1.000 28.850 0  73  PHE A CE1 1 
ATOM   577  C CE2 . PHE A 1 73  ? 3.311   2.073   0.563  1.000 28.760 0  73  PHE A CE2 1 
ATOM   578  C CZ  . PHE A 1 73  ? 4.213   1.952   1.604  1.000 28.590 0  73  PHE A CZ  1 
ATOM   579  N N   . ALA A 1 74  ? 7.516   0.209   -4.808 1.000 31.110 0  74  ALA A N   1 
ATOM   580  C CA  . ALA A 1 74  ? 8.029   -0.491  -5.979 1.000 31.650 0  74  ALA A CA  1 
ATOM   581  C C   . ALA A 1 74  ? 9.180   -1.408  -5.588 1.000 32.960 0  74  ALA A C   1 
ATOM   582  O O   . ALA A 1 74  ? 9.252   -2.560  -6.043 1.000 35.920 0  74  ALA A O   1 
ATOM   583  C CB  . ALA A 1 74  ? 8.473   0.511   -7.043 1.000 31.980 0  74  ALA A CB  1 
ATOM   584  N N   . TRP A 1 75  ? 10.082  -0.919  -4.729 1.000 31.640 0  75  TRP A N   1 
ATOM   585  C CA  . TRP A 1 75  ? 11.140  -1.792  -4.224 1.000 32.230 0  75  TRP A CA  1 
ATOM   586  C C   . TRP A 1 75  ? 10.554  -2.991  -3.488 1.000 32.370 0  75  TRP A C   1 
ATOM   587  O O   . TRP A 1 75  ? 11.016  -4.124  -3.662 1.000 32.620 0  75  TRP A O   1 
ATOM   588  C CB  . TRP A 1 75  ? 12.087  -1.020  -3.306 1.000 31.560 0  75  TRP A CB  1 
ATOM   589  C CG  . TRP A 1 75  ? 13.046  -1.913  -2.568 1.000 31.640 0  75  TRP A CG  1 
ATOM   590  C CD1 . TRP A 1 75  ? 14.181  -2.483  -3.069 1.000 32.120 0  75  TRP A CD1 1 
ATOM   591  C CD2 . TRP A 1 75  ? 12.957  -2.333  -1.198 1.000 32.250 0  75  TRP A CD2 1 
ATOM   592  N NE1 . TRP A 1 75  ? 14.803  -3.231  -2.098 1.000 32.050 0  75  TRP A NE1 1 
ATOM   593  C CE2 . TRP A 1 75  ? 14.072  -3.156  -0.942 1.000 31.840 0  75  TRP A CE2 1 
ATOM   594  C CE3 . TRP A 1 75  ? 12.043  -2.092  -0.166 1.000 31.700 0  75  TRP A CE3 1 
ATOM   595  C CZ2 . TRP A 1 75  ? 14.300  -3.739  0.305  1.000 31.290 0  75  TRP A CZ2 1 
ATOM   596  C CZ3 . TRP A 1 75  ? 12.271  -2.674  1.072  1.000 31.640 0  75  TRP A CZ3 1 
ATOM   597  C CH2 . TRP A 1 75  ? 13.390  -3.488  1.295  1.000 31.340 0  75  TRP A CH2 1 
ATOM   598  N N   . ALA A 1 76  ? 9.541   -2.754  -2.653 1.000 31.400 0  76  ALA A N   1 
ATOM   599  C CA  . ALA A 1 76  ? 8.913   -3.841  -1.908 1.000 32.440 0  76  ALA A CA  1 
ATOM   600  C C   . ALA A 1 76  ? 8.288   -4.867  -2.846 1.000 33.710 0  76  ALA A C   1 
ATOM   601  O O   . ALA A 1 76  ? 8.350   -6.076  -2.589 1.000 33.130 0  76  ALA A O   1 
ATOM   602  C CB  . ALA A 1 76  ? 7.859   -3.283  -0.953 1.000 30.380 0  76  ALA A CB  1 
ATOM   603  N N   . ARG A 1 77  ? 7.680   -4.404  -3.938 1.000 32.710 0  77  ARG A N   1 
ATOM   604  C CA  . ARG A 1 77  ? 7.051   -5.327  -4.874 1.000 32.850 0  77  ARG A CA  1 
ATOM   605  C C   . ARG A 1 77  ? 8.088   -6.139  -5.633 1.000 32.280 0  77  ARG A C   1 
ATOM   606  O O   . ARG A 1 77  ? 7.856   -7.319  -5.921 1.000 32.520 0  77  ARG A O   1 
ATOM   607  C CB  . ARG A 1 77  ? 6.154   -4.569  -5.852 1.000 32.490 0  77  ARG A CB  1 
ATOM   608  C CG  . ARG A 1 77  ? 4.732   -4.377  -5.359 1.000 32.070 0  77  ARG A CG  1 
ATOM   609  C CD  . ARG A 1 77  ? 4.183   -3.028  -5.786 1.000 34.710 0  77  ARG A CD  1 
ATOM   610  N NE  . ARG A 1 77  ? 3.250   -2.486  -4.807 1.000 35.040 0  77  ARG A NE  1 
ATOM   611  C CZ  . ARG A 1 77  ? 2.975   -1.196  -4.670 1.000 34.790 0  77  ARG A CZ  1 
ATOM   612  N NH1 . ARG A 1 77  ? 3.543   -0.282  -5.441 1.000 34.950 1  77  ARG A NH1 1 
ATOM   613  N NH2 . ARG A 1 77  ? 2.112   -0.812  -3.733 1.000 34.530 0  77  ARG A NH2 1 
ATOM   614  N N   . LYS A 1 78  ? 9.236   -5.542  -5.951 1.000 33.580 0  78  LYS A N   1 
ATOM   615  C CA  . LYS A 1 78  ? 10.254  -6.303  -6.664 1.000 33.060 0  78  LYS A CA  1 
ATOM   616  C C   . LYS A 1 78  ? 11.029  -7.247  -5.753 1.000 33.060 0  78  LYS A C   1 
ATOM   617  O O   . LYS A 1 78  ? 11.702  -8.153  -6.254 1.000 35.070 0  78  LYS A O   1 
ATOM   618  C CB  . LYS A 1 78  ? 11.214  -5.352  -7.384 1.000 35.210 0  78  LYS A CB  1 
ATOM   619  C CG  . LYS A 1 78  ? 12.363  -4.829  -6.537 1.000 36.490 0  78  LYS A CG  1 
ATOM   620  C CD  . LYS A 1 78  ? 13.379  -4.095  -7.406 1.000 35.730 0  78  LYS A CD  1 
ATOM   621  C CE  . LYS A 1 78  ? 12.680  -3.157  -8.385 1.000 39.370 0  78  LYS A CE  1 
ATOM   622  N NZ  . LYS A 1 78  ? 13.629  -2.391  -9.247 1.000 42.870 1  78  LYS A NZ  1 
ATOM   623  N N   . GLU A 1 79  ? 10.942  -7.069  -4.437 1.000 32.570 0  79  GLU A N   1 
ATOM   624  C CA  . GLU A 1 79  ? 11.501  -8.015  -3.481 1.000 32.530 0  79  GLU A CA  1 
ATOM   625  C C   . GLU A 1 79  ? 10.447  -8.915  -2.845 1.000 34.040 0  79  GLU A C   1 
ATOM   626  O O   . GLU A 1 79  ? 10.745  -9.599  -1.862 1.000 35.800 0  79  GLU A O   1 
ATOM   627  C CB  . GLU A 1 79  ? 12.278  -7.268  -2.396 1.000 33.910 0  79  GLU A CB  1 
ATOM   628  C CG  . GLU A 1 79  ? 13.364  -6.354  -2.948 1.000 35.010 0  79  GLU A CG  1 
ATOM   629  C CD  . GLU A 1 79  ? 14.585  -7.122  -3.419 1.000 36.590 0  79  GLU A CD  1 
ATOM   630  O OE1 . GLU A 1 79  ? 15.200  -7.832  -2.593 1.000 38.450 0  79  GLU A OE1 1 
ATOM   631  O OE2 . GLU A 1 79  ? 14.926  -7.020  -4.618 1.000 35.570 -1 79  GLU A OE2 1 
ATOM   632  N N   . GLY A 1 80  ? 9.228   -8.931  -3.381 1.000 34.610 0  80  GLY A N   1 
ATOM   633  C CA  . GLY A 1 80  ? 8.190   -9.824  -2.898 1.000 32.010 0  80  GLY A CA  1 
ATOM   634  C C   . GLY A 1 80  ? 7.816   -9.627  -1.444 1.000 31.480 0  80  GLY A C   1 
ATOM   635  O O   . GLY A 1 80  ? 7.871   -10.571 -0.648 1.000 31.420 0  80  GLY A O   1 
ATOM   636  N N   . MET A 1 81  ? 7.436   -8.406  -1.081 1.000 33.130 0  81  MET A N   1 
ATOM   637  C CA  . MET A 1 81  ? 7.089   -8.066  0.291  1.000 30.600 0  81  MET A CA  1 
ATOM   638  C C   . MET A 1 81  ? 5.685   -7.481  0.341  1.000 30.280 0  81  MET A C   1 
ATOM   639  O O   . MET A 1 81  ? 5.340   -6.611  -0.464 1.000 30.320 0  81  MET A O   1 
ATOM   640  C CB  . MET A 1 81  ? 8.099   -7.080  0.880  1.000 31.200 0  81  MET A CB  1 
ATOM   641  C CG  . MET A 1 81  ? 9.442   -7.710  1.198  1.000 34.150 0  81  MET A CG  1 
ATOM   642  S SD  . MET A 1 81  ? 10.774  -6.507  1.267  1.000 33.710 0  81  MET A SD  1 
ATOM   643  C CE  . MET A 1 81  ? 11.117  -6.522  3.021  1.000 32.510 0  81  MET A CE  1 
ATOM   644  N N   . ALA A 1 82  ? 4.874   -7.980  1.271  1.000 29.990 0  82  ALA A N   1 
ATOM   645  C CA  . ALA A 1 82  ? 3.562   -7.402  1.509  1.000 29.660 0  82  ALA A CA  1 
ATOM   646  C C   . ALA A 1 82  ? 3.704   -6.019  2.136  1.000 30.870 0  82  ALA A C   1 
ATOM   647  O O   . ALA A 1 82  ? 4.710   -5.707  2.779  1.000 31.630 0  82  ALA A O   1 
ATOM   648  C CB  . ALA A 1 82  ? 2.730   -8.311  2.413  1.000 29.540 0  82  ALA A CB  1 
ATOM   649  N N   . ILE A 1 83  ? 2.693   -5.179  1.928  1.000 29.130 0  83  ILE A N   1 
ATOM   650  C CA  . ILE A 1 83  ? 2.764   -3.762  2.268  1.000 29.510 0  83  ILE A CA  1 
ATOM   651  C C   . ILE A 1 83  ? 1.601   -3.402  3.183  1.000 30.320 0  83  ILE A C   1 
ATOM   652  O O   . ILE A 1 83  ? 0.449   -3.753  2.901  1.000 29.170 0  83  ILE A O   1 
ATOM   653  C CB  . ILE A 1 83  ? 2.746   -2.872  1.010  1.000 29.090 0  83  ILE A CB  1 
ATOM   654  C CG1 . ILE A 1 83  ? 3.576   -3.500  -0.114 1.000 31.560 0  83  ILE A CG1 1 
ATOM   655  C CG2 . ILE A 1 83  ? 3.252   -1.481  1.337  1.000 28.900 0  83  ILE A CG2 1 
ATOM   656  C CD1 . ILE A 1 83  ? 3.521   -2.729  -1.419 1.000 29.850 0  83  ILE A CD1 1 
ATOM   657  N N   . ARG A 1 84  ? 1.902   -2.700  4.273  1.000 28.870 0  84  ARG A N   1 
ATOM   658  C CA  . ARG A 1 84  ? 0.894   -2.097  5.131  1.000 27.800 0  84  ARG A CA  1 
ATOM   659  C C   . ARG A 1 84  ? 0.767   -0.610  4.819  1.000 29.170 0  84  ARG A C   1 
ATOM   660  O O   . ARG A 1 84  ? 1.663   0.009   4.240  1.000 27.850 0  84  ARG A O   1 
ATOM   661  C CB  . ARG A 1 84  ? 1.229   -2.277  6.613  1.000 27.520 0  84  ARG A CB  1 
ATOM   662  C CG  . ARG A 1 84  ? 1.837   -3.608  7.004  1.000 27.650 0  84  ARG A CG  1 
ATOM   663  C CD  . ARG A 1 84  ? 1.822   -3.760  8.520  1.000 27.360 0  84  ARG A CD  1 
ATOM   664  N NE  . ARG A 1 84  ? 0.486   -3.542  9.062  1.000 27.110 0  84  ARG A NE  1 
ATOM   665  C CZ  . ARG A 1 84  ? 0.146   -2.525  9.843  1.000 26.820 0  84  ARG A CZ  1 
ATOM   666  N NH1 . ARG A 1 84  ? 1.031   -1.619  10.224 1.000 26.720 1  84  ARG A NH1 1 
ATOM   667  N NH2 . ARG A 1 84  ? -1.118  -2.411  10.249 1.000 26.650 0  84  ARG A NH2 1 
ATOM   668  N N   . GLY A 1 85  ? -0.358  -0.036  5.229  1.000 27.470 0  85  GLY A N   1 
ATOM   669  C CA  . GLY A 1 85  ? -0.553  1.391   5.088  1.000 27.360 0  85  GLY A CA  1 
ATOM   670  C C   . GLY A 1 85  ? -0.565  2.090   6.430  1.000 27.000 0  85  GLY A C   1 
ATOM   671  O O   . GLY A 1 85  ? -1.518  1.945   7.201  1.000 27.520 0  85  GLY A O   1 
ATOM   672  N N   . HIS A 1 86  ? 0.487   2.846   6.729  1.000 26.940 0  86  HIS A N   1 
ATOM   673  C CA  . HIS A 1 86  ? 0.617   3.534   8.008  1.000 26.630 0  86  HIS A CA  1 
ATOM   674  C C   . HIS A 1 86  ? 0.840   5.016   7.760  1.000 26.940 0  86  HIS A C   1 
ATOM   675  O O   . HIS A 1 86  ? 1.866   5.401   7.190  1.000 26.750 0  86  HIS A O   1 
ATOM   676  C CB  . HIS A 1 86  ? 1.775   2.959   8.824  1.000 26.590 0  86  HIS A CB  1 
ATOM   677  C CG  . HIS A 1 86  ? 1.966   3.629   10.149 1.000 26.290 0  86  HIS A CG  1 
ATOM   678  N ND1 . HIS A 1 86  ? 1.380   3.170   11.308 1.000 26.080 0  86  HIS A ND1 1 
ATOM   679  C CD2 . HIS A 1 86  ? 2.673   4.730   10.497 1.000 26.190 0  86  HIS A CD2 1 
ATOM   680  C CE1 . HIS A 1 86  ? 1.723   3.955   12.313 1.000 25.870 0  86  HIS A CE1 1 
ATOM   681  N NE2 . HIS A 1 86  ? 2.507   4.910   11.848 1.000 25.920 0  86  HIS A NE2 1 
ATOM   682  N N   . ALA A 1 87  ? -0.113  5.842   8.183  1.000 26.380 0  87  ALA A N   1 
ATOM   683  C CA  . ALA A 1 87  ? -1.409  5.471   8.746  1.000 26.230 0  87  ALA A CA  1 
ATOM   684  C C   . ALA A 1 87  ? -2.465  6.411   8.178  1.000 26.250 0  87  ALA A C   1 
ATOM   685  O O   . ALA A 1 87  ? -2.146  7.525   7.764  1.000 27.070 0  87  ALA A O   1 
ATOM   686  C CB  . ALA A 1 87  ? -1.385  5.539   10.268 1.000 25.940 0  87  ALA A CB  1 
ATOM   687  N N   . LEU A 1 88  ? -3.726  5.979   8.165  1.000 26.250 0  88  LEU A N   1 
ATOM   688  C CA  . LEU A 1 88  ? -4.755  6.780   7.508  1.000 26.320 0  88  LEU A CA  1 
ATOM   689  C C   . LEU A 1 88  ? -5.020  8.074   8.269  1.000 26.110 0  88  LEU A C   1 
ATOM   690  O O   . LEU A 1 88  ? -4.961  9.166   7.691  1.000 26.300 0  88  LEU A O   1 
ATOM   691  C CB  . LEU A 1 88  ? -6.039  5.971   7.346  1.000 26.380 0  88  LEU A CB  1 
ATOM   692  C CG  . LEU A 1 88  ? -6.993  6.613   6.342  1.000 27.020 0  88  LEU A CG  1 
ATOM   693  C CD1 . LEU A 1 88  ? -6.284  6.819   5.010  1.000 26.840 0  88  LEU A CD1 1 
ATOM   694  C CD2 . LEU A 1 88  ? -8.244  5.772   6.168  1.000 27.260 0  88  LEU A CD2 1 
ATOM   695  N N   . ILE A 1 89  ? -5.316  7.980   9.564  1.000 25.870 0  89  ILE A N   1 
ATOM   696  C CA  . ILE A 1 89  ? -5.542  9.156   10.396 1.000 26.410 0  89  ILE A CA  1 
ATOM   697  C C   . ILE A 1 89  ? -4.711  9.044   11.664 1.000 25.950 0  89  ILE A C   1 
ATOM   698  O O   . ILE A 1 89  ? -4.748  8.016   12.349 1.000 25.540 0  89  ILE A O   1 
ATOM   699  C CB  . ILE A 1 89  ? -7.028  9.329   10.758 1.000 27.320 0  89  ILE A CB  1 
ATOM   700  C CG1 . ILE A 1 89  ? -7.860  9.611   9.510  1.000 25.870 0  89  ILE A CG1 1 
ATOM   701  C CG2 . ILE A 1 89  ? -7.202  10.450  11.773 1.000 25.440 0  89  ILE A CG2 1 
ATOM   702  C CD1 . ILE A 1 89  ? -9.195  10.226  9.818  1.000 26.660 0  89  ILE A CD1 1 
ATOM   703  N N   . TRP A 1 90  ? -3.984  10.110  11.983 1.000 26.440 0  90  TRP A N   1 
ATOM   704  C CA  . TRP A 1 90  ? -3.251  10.247  13.236 1.000 26.860 0  90  TRP A CA  1 
ATOM   705  C C   . TRP A 1 90  ? -3.932  11.379  13.997 1.000 27.070 0  90  TRP A C   1 
ATOM   706  O O   . TRP A 1 90  ? -3.844  12.544  13.594 1.000 27.820 0  90  TRP A O   1 
ATOM   707  C CB  . TRP A 1 90  ? -1.773  10.534  12.976 1.000 25.230 0  90  TRP A CB  1 
ATOM   708  C CG  . TRP A 1 90  ? -0.860  10.106  14.082 1.000 26.030 0  90  TRP A CG  1 
ATOM   709  C CD1 . TRP A 1 90  ? -1.222  9.680   15.327 1.000 25.610 0  90  TRP A CD1 1 
ATOM   710  C CD2 . TRP A 1 90  ? 0.573   10.073  14.047 1.000 25.300 0  90  TRP A CD2 1 
ATOM   711  N NE1 . TRP A 1 90  ? -0.105  9.382   16.067 1.000 24.860 0  90  TRP A NE1 1 
ATOM   712  C CE2 . TRP A 1 90  ? 1.010   9.614   15.304 1.000 25.260 0  90  TRP A CE2 1 
ATOM   713  C CE3 . TRP A 1 90  ? 1.527   10.386  13.075 1.000 26.520 0  90  TRP A CE3 1 
ATOM   714  C CZ2 . TRP A 1 90  ? 2.360   9.459   15.615 1.000 25.470 0  90  TRP A CZ2 1 
ATOM   715  C CZ3 . TRP A 1 90  ? 2.868   10.231  13.384 1.000 26.980 0  90  TRP A CZ3 1 
ATOM   716  C CH2 . TRP A 1 90  ? 3.271   9.772   14.643 1.000 25.210 0  90  TRP A CH2 1 
ATOM   717  N N   . GLN A 1 91  ? -4.605  11.034  15.098 1.000 27.330 0  91  GLN A N   1 
ATOM   718  C CA  . GLN A 1 91  ? -5.691  11.874  15.606 1.000 26.020 0  91  GLN A CA  1 
ATOM   719  C C   . GLN A 1 91  ? -5.198  13.224  16.119 1.000 25.540 0  91  GLN A C   1 
ATOM   720  O O   . GLN A 1 91  ? -5.876  14.241  15.934 1.000 24.760 0  91  GLN A O   1 
ATOM   721  C CB  . GLN A 1 91  ? -6.456  11.132  16.698 1.000 25.260 0  91  GLN A CB  1 
ATOM   722  C CG  . GLN A 1 91  ? -7.438  10.100  16.169 1.000 25.710 0  91  GLN A CG  1 
ATOM   723  C CD  . GLN A 1 91  ? -8.716  10.712  15.623 1.000 25.780 0  91  GLN A CD  1 
ATOM   724  O OE1 . GLN A 1 91  ? -8.719  11.330  14.558 1.000 26.360 0  91  GLN A OE1 1 
ATOM   725  N NE2 . GLN A 1 91  ? -9.812  10.536  16.350 1.000 24.910 0  91  GLN A NE2 1 
ATOM   726  N N   . ASP A 1 92  ? -4.054  13.256  16.791 1.000 25.680 0  92  ASP A N   1 
ATOM   727  C CA  . ASP A 1 92  ? -3.608  14.498  17.408 1.000 26.260 0  92  ASP A CA  1 
ATOM   728  C C   . ASP A 1 92  ? -3.373  15.576  16.351 1.000 26.620 0  92  ASP A C   1 
ATOM   729  O O   . ASP A 1 92  ? -2.781  15.299  15.301 1.000 27.550 0  92  ASP A O   1 
ATOM   730  C CB  . ASP A 1 92  ? -2.329  14.282  18.212 1.000 26.000 0  92  ASP A CB  1 
ATOM   731  C CG  . ASP A 1 92  ? -2.033  15.441  19.142 1.000 27.950 0  92  ASP A CG  1 
ATOM   732  O OD1 . ASP A 1 92  ? -1.522  16.474  18.660 1.000 26.040 0  92  ASP A OD1 1 
ATOM   733  O OD2 . ASP A 1 92  ? -2.314  15.321  20.353 1.000 30.500 -1 92  ASP A OD2 1 
ATOM   734  N N   . PRO A 1 93  ? -3.823  16.812  16.592 1.000 26.700 0  93  PRO A N   1 
ATOM   735  C CA  . PRO A 1 93  ? -3.604  17.881  15.604 1.000 27.190 0  93  PRO A CA  1 
ATOM   736  C C   . PRO A 1 93  ? -2.142  18.101  15.257 1.000 26.280 0  93  PRO A C   1 
ATOM   737  O O   . PRO A 1 93  ? -1.846  18.611  14.168 1.000 27.700 0  93  PRO A O   1 
ATOM   738  C CB  . PRO A 1 93  ? -4.214  19.113  16.283 1.000 24.940 0  93  PRO A CB  1 
ATOM   739  C CG  . PRO A 1 93  ? -5.264  18.548  17.183 1.000 24.610 0  93  PRO A CG  1 
ATOM   740  C CD  . PRO A 1 93  ? -4.699  17.250  17.692 1.000 24.740 0  93  PRO A CD  1 
ATOM   741  N N   . LYS A 1 94  ? -1.215  17.709  16.133 1.000 26.840 0  94  LYS A N   1 
ATOM   742  C CA  . LYS A 1 94  ? 0.201   17.822  15.808 1.000 27.550 0  94  LYS A CA  1 
ATOM   743  C C   . LYS A 1 94  ? 0.622   16.835  14.727 1.000 26.690 0  94  LYS A C   1 
ATOM   744  O O   . LYS A 1 94  ? 1.746   16.928  14.226 1.000 25.880 0  94  LYS A O   1 
ATOM   745  C CB  . LYS A 1 94  ? 1.036   17.644  17.085 1.000 27.220 0  94  LYS A CB  1 
ATOM   746  C CG  . LYS A 1 94  ? 1.767   16.319  17.243 1.000 28.260 0  94  LYS A CG  1 
ATOM   747  C CD  . LYS A 1 94  ? 2.207   16.120  18.695 1.000 29.330 0  94  LYS A CD  1 
ATOM   748  C CE  . LYS A 1 94  ? 3.509   16.854  19.003 1.000 32.660 0  94  LYS A CE  1 
ATOM   749  N NZ  . LYS A 1 94  ? 4.687   16.260  18.307 1.000 30.130 1  94  LYS A NZ  1 
ATOM   750  N N   . TRP A 1 95  ? -0.264  15.911  14.343 1.000 27.670 0  95  TRP A N   1 
ATOM   751  C CA  . TRP A 1 95  ? 0.020   14.943  13.296 1.000 26.340 0  95  TRP A CA  1 
ATOM   752  C C   . TRP A 1 95  ? -0.872  15.096  12.071 1.000 27.450 0  95  TRP A C   1 
ATOM   753  O O   . TRP A 1 95  ? -0.689  14.357  11.097 1.000 27.730 0  95  TRP A O   1 
ATOM   754  C CB  . TRP A 1 95  ? -0.106  13.521  13.851 1.000 25.890 0  95  TRP A CB  1 
ATOM   755  C CG  . TRP A 1 95  ? 0.795   13.279  15.011 1.000 25.930 0  95  TRP A CG  1 
ATOM   756  C CD1 . TRP A 1 95  ? 0.428   12.917  16.273 1.000 24.720 0  95  TRP A CD1 1 
ATOM   757  C CD2 . TRP A 1 95  ? 2.222   13.389  15.023 1.000 26.260 0  95  TRP A CD2 1 
ATOM   758  N NE1 . TRP A 1 95  ? 1.538   12.793  17.071 1.000 25.580 0  95  TRP A NE1 1 
ATOM   759  C CE2 . TRP A 1 95  ? 2.653   13.077  16.326 1.000 27.190 0  95  TRP A CE2 1 
ATOM   760  C CE3 . TRP A 1 95  ? 3.179   13.718  14.057 1.000 26.910 0  95  TRP A CE3 1 
ATOM   761  C CZ2 . TRP A 1 95  ? 3.998   13.086  16.689 1.000 27.930 0  95  TRP A CZ2 1 
ATOM   762  C CZ3 . TRP A 1 95  ? 4.512   13.725  14.418 1.000 25.620 0  95  TRP A CZ3 1 
ATOM   763  C CH2 . TRP A 1 95  ? 4.911   13.412  15.723 1.000 28.590 0  95  TRP A CH2 1 
ATOM   764  N N   . LEU A 1 96  ? -1.830  16.027  12.087 1.000 28.500 0  96  LEU A N   1 
ATOM   765  C CA  . LEU A 1 96  ? -2.597  16.368  10.900 1.000 26.070 0  96  LEU A CA  1 
ATOM   766  C C   . LEU A 1 96  ? -1.949  17.527  10.153 1.000 25.630 0  96  LEU A C   1 
ATOM   767  O O   . LEU A 1 96  ? -1.217  18.328  10.743 1.000 25.540 0  96  LEU A O   1 
ATOM   768  C CB  . LEU A 1 96  ? -4.029  16.730  11.290 1.000 25.520 0  96  LEU A CB  1 
ATOM   769  C CG  . LEU A 1 96  ? -4.895  15.618  11.881 1.000 26.040 0  96  LEU A CG  1 
ATOM   770  C CD1 . LEU A 1 96  ? -6.230  16.184  12.337 1.000 28.000 0  96  LEU A CD1 1 
ATOM   771  C CD2 . LEU A 1 96  ? -5.103  14.496  10.875 1.000 25.510 0  96  LEU A CD2 1 
ATOM   772  N N   . PRO A 1 97  ? -2.203  17.647  8.848  1.000 25.880 0  97  PRO A N   1 
ATOM   773  C CA  . PRO A 1 97  ? -1.684  18.798  8.098  1.000 26.060 0  97  PRO A CA  1 
ATOM   774  C C   . PRO A 1 97  ? -2.218  20.113  8.652  1.000 26.000 0  97  PRO A C   1 
ATOM   775  O O   . PRO A 1 97  ? -3.340  20.190  9.157  1.000 27.430 0  97  PRO A O   1 
ATOM   776  C CB  . PRO A 1 97  ? -2.176  18.560  6.665  1.000 26.360 0  97  PRO A CB  1 
ATOM   777  C CG  . PRO A 1 97  ? -2.725  17.186  6.617  1.000 26.350 0  97  PRO A CG  1 
ATOM   778  C CD  . PRO A 1 97  ? -2.707  16.572  7.975  1.000 26.050 0  97  PRO A CD  1 
ATOM   779  N N   . ALA A 1 98  ? -1.386  21.153  8.555  1.000 26.920 0  98  ALA A N   1 
ATOM   780  C CA  . ALA A 1 98  ? -1.750  22.459  9.101  1.000 26.950 0  98  ALA A CA  1 
ATOM   781  C C   . ALA A 1 98  ? -3.058  22.973  8.511  1.000 26.570 0  98  ALA A C   1 
ATOM   782  O O   . ALA A 1 98  ? -3.885  23.549  9.227  1.000 29.080 0  98  ALA A O   1 
ATOM   783  C CB  . ALA A 1 98  ? -0.625  23.463  8.854  1.000 26.050 0  98  ALA A CB  1 
ATOM   784  N N   . TRP A 1 99  ? -3.257  22.795  7.203  1.000 26.380 0  99  TRP A N   1 
ATOM   785  C CA  . TRP A 1 99  ? -4.491  23.266  6.585  1.000 26.570 0  99  TRP A CA  1 
ATOM   786  C C   . TRP A 1 99  ? -5.694  22.455  7.049  1.000 26.900 0  99  TRP A C   1 
ATOM   787  O O   . TRP A 1 99  ? -6.817  22.972  7.080  1.000 28.600 0  99  TRP A O   1 
ATOM   788  C CB  . TRP A 1 99  ? -4.368  23.221  5.063  1.000 26.900 0  99  TRP A CB  1 
ATOM   789  C CG  . TRP A 1 99  ? -4.167  21.842  4.524  1.000 26.960 0  99  TRP A CG  1 
ATOM   790  C CD1 . TRP A 1 99  ? -2.982  21.178  4.396  1.000 27.150 0  99  TRP A CD1 1 
ATOM   791  C CD2 . TRP A 1 99  ? -5.180  20.954  4.038  1.000 27.060 0  99  TRP A CD2 1 
ATOM   792  N NE1 . TRP A 1 99  ? -3.194  19.931  3.860  1.000 27.230 0  99  TRP A NE1 1 
ATOM   793  C CE2 . TRP A 1 99  ? -4.535  19.768  3.631  1.000 27.100 0  99  TRP A CE2 1 
ATOM   794  C CE3 . TRP A 1 99  ? -6.569  21.045  3.909  1.000 27.130 0  99  TRP A CE3 1 
ATOM   795  C CZ2 . TRP A 1 99  ? -5.232  18.684  3.104  1.000 27.210 0  99  TRP A CZ2 1 
ATOM   796  C CZ3 . TRP A 1 99  ? -7.259  19.967  3.385  1.000 27.230 0  99  TRP A CZ3 1 
ATOM   797  C CH2 . TRP A 1 99  ? -6.590  18.802  2.989  1.000 27.270 0  99  TRP A CH2 1 
ATOM   798  N N   . VAL A 1 100 ? -5.483  21.188  7.408  1.000 26.320 0  100 VAL A N   1 
ATOM   799  C CA  . VAL A 1 100 ? -6.581  20.384  7.931  1.000 26.220 0  100 VAL A CA  1 
ATOM   800  C C   . VAL A 1 100 ? -6.975  20.879  9.315  1.000 29.290 0  100 VAL A C   1 
ATOM   801  O O   . VAL A 1 100 ? -8.165  21.007  9.633  1.000 31.560 0  100 VAL A O   1 
ATOM   802  C CB  . VAL A 1 100 ? -6.191  18.895  7.943  1.000 26.600 0  100 VAL A CB  1 
ATOM   803  C CG1 . VAL A 1 100 ? -6.943  18.145  9.035  1.000 27.940 0  100 VAL A CG1 1 
ATOM   804  C CG2 . VAL A 1 100 ? -6.440  18.268  6.574  1.000 27.010 0  100 VAL A CG2 1 
ATOM   805  N N   . ASN A 1 101 ? -5.982  21.183  10.154 1.000 26.610 0  101 ASN A N   1 
ATOM   806  C CA  . ASN A 1 101 ? -6.262  21.694  11.488 1.000 25.590 0  101 ASN A CA  1 
ATOM   807  C C   . ASN A 1 101 ? -6.849  23.096  11.445 1.000 26.370 0  101 ASN A C   1 
ATOM   808  O O   . ASN A 1 101 ? -7.525  23.504  12.396 1.000 27.680 0  101 ASN A O   1 
ATOM   809  C CB  . ASN A 1 101 ? -4.984  21.686  12.326 1.000 25.400 0  101 ASN A CB  1 
ATOM   810  C CG  . ASN A 1 101 ? -4.652  20.308  12.871 1.000 26.020 0  101 ASN A CG  1 
ATOM   811  O OD1 . ASN A 1 101 ? -5.525  19.593  13.365 1.000 28.010 0  101 ASN A OD1 1 
ATOM   812  N ND2 . ASN A 1 101 ? -3.382  19.929  12.784 1.000 25.220 0  101 ASN A ND2 1 
ATOM   813  N N   . ALA A 1 102 ? -6.613  23.838  10.366 1.000 26.690 0  102 ALA A N   1 
ATOM   814  C CA  . ALA A 1 102 ? -7.148  25.182  10.200 1.000 26.970 0  102 ALA A CA  1 
ATOM   815  C C   . ALA A 1 102 ? -8.514  25.203  9.529  1.000 27.600 0  102 ALA A C   1 
ATOM   816  O O   . ALA A 1 102 ? -9.043  26.288  9.270  1.000 29.370 0  102 ALA A O   1 
ATOM   817  C CB  . ALA A 1 102 ? -6.173  26.041  9.391  1.000 26.220 0  102 ALA A CB  1 
ATOM   818  N N   . LEU A 1 103 ? -9.097  24.044  9.245  1.000 28.710 0  103 LEU A N   1 
ATOM   819  C CA  . LEU A 1 103 ? -10.390 24.001  8.580  1.000 29.830 0  103 LEU A CA  1 
ATOM   820  C C   . LEU A 1 103 ? -11.500 24.523  9.486  1.000 30.580 0  103 LEU A C   1 
ATOM   821  O O   . LEU A 1 103 ? -11.463 24.371  10.710 1.000 32.700 0  103 LEU A O   1 
ATOM   822  C CB  . LEU A 1 103 ? -10.702 22.574  8.132  1.000 29.640 0  103 LEU A CB  1 
ATOM   823  C CG  . LEU A 1 103 ? -9.985  22.131  6.854  1.000 28.320 0  103 LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 103 ? -10.536 20.809  6.344  1.000 27.320 0  103 LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 103 ? -10.097 23.209  5.787  1.000 27.010 0  103 LEU A CD2 1 
ATOM   826  N N   . ASP A 1 104 ? -12.497 25.155  8.862  1.000 30.440 0  104 ASP A N   1 
ATOM   827  C CA  . ASP A 1 104 ? -13.664 25.695  9.563  1.000 29.310 0  104 ASP A CA  1 
ATOM   828  C C   . ASP A 1 104 ? -14.827 24.738  9.319  1.000 30.500 0  104 ASP A C   1 
ATOM   829  O O   . ASP A 1 104 ? -15.658 24.930  8.432  1.000 33.110 0  104 ASP A O   1 
ATOM   830  C CB  . ASP A 1 104 ? -13.967 27.115  9.081  1.000 34.630 0  104 ASP A CB  1 
ATOM   831  C CG  . ASP A 1 104 ? -15.286 27.656  9.617  1.000 34.820 0  104 ASP A CG  1 
ATOM   832  O OD1 . ASP A 1 104 ? -15.704 27.249  10.723 1.000 35.460 0  104 ASP A OD1 1 
ATOM   833  O OD2 . ASP A 1 104 ? -15.902 28.499  8.930  1.000 34.090 -1 104 ASP A OD2 1 
ATOM   834  N N   . LEU A 1 105 ? -14.884 23.690  10.140 1.000 29.350 0  105 LEU A N   1 
ATOM   835  C CA  . LEU A 1 105 ? -15.890 22.647  9.974  1.000 28.370 0  105 LEU A CA  1 
ATOM   836  C C   . LEU A 1 105 ? -17.176 22.919  10.738 1.000 29.790 0  105 LEU A C   1 
ATOM   837  O O   . LEU A 1 105 ? -18.245 22.470  10.308 1.000 29.500 0  105 LEU A O   1 
ATOM   838  C CB  . LEU A 1 105 ? -15.320 21.293  10.401 1.000 26.730 0  105 LEU A CB  1 
ATOM   839  C CG  . LEU A 1 105 ? -14.344 20.692  9.393  1.000 29.550 0  105 LEU A CG  1 
ATOM   840  C CD1 . LEU A 1 105 ? -13.923 19.299  9.825  1.000 27.790 0  105 LEU A CD1 1 
ATOM   841  C CD2 . LEU A 1 105 ? -14.968 20.673  8.005  1.000 28.720 0  105 LEU A CD2 1 
ATOM   842  N N   . LYS A 1 106 ? -17.101 23.634  11.863 1.000 31.580 0  106 LYS A N   1 
ATOM   843  C CA  . LYS A 1 106 ? -18.288 23.860  12.679 1.000 30.160 0  106 LYS A CA  1 
ATOM   844  C C   . LYS A 1 106 ? -19.326 24.708  11.955 1.000 30.610 0  106 LYS A C   1 
ATOM   845  O O   . LYS A 1 106 ? -20.516 24.608  12.267 1.000 31.440 0  106 LYS A O   1 
ATOM   846  C CB  . LYS A 1 106 ? -17.898 24.527  13.999 1.000 31.600 0  106 LYS A CB  1 
ATOM   847  C CG  . LYS A 1 106 ? -17.253 25.898  13.834 1.000 34.020 0  106 LYS A CG  1 
ATOM   848  C CD  . LYS A 1 106 ? -16.529 26.353  15.096 1.000 32.400 0  106 LYS A CD  1 
ATOM   849  C CE  . LYS A 1 106 ? -16.202 27.845  15.038 1.000 35.350 0  106 LYS A CE  1 
ATOM   850  N NZ  . LYS A 1 106 ? -15.307 28.186  13.894 1.000 36.860 1  106 LYS A NZ  1 
ATOM   851  N N   . SER A 1 107 ? -18.904 25.529  10.991 1.000 31.630 0  107 SER A N   1 
ATOM   852  C CA  . SER A 1 107 ? -19.825 26.323  10.190 1.000 30.940 0  107 SER A CA  1 
ATOM   853  C C   . SER A 1 107 ? -20.559 25.509  9.133  1.000 29.670 0  107 SER A C   1 
ATOM   854  O O   . SER A 1 107 ? -21.521 26.017  8.546  1.000 33.600 0  107 SER A O   1 
ATOM   855  C CB  . SER A 1 107 ? -19.071 27.473  9.518  1.000 31.310 0  107 SER A CB  1 
ATOM   856  O OG  . SER A 1 107 ? -19.109 28.638  10.322 1.000 29.400 0  107 SER A OG  1 
ATOM   857  N N   . LYS A 1 108 ? -20.141 24.281  8.871  1.000 27.710 0  108 LYS A N   1 
ATOM   858  C CA  . LYS A 1 108 ? -20.715 23.459  7.821  1.000 27.920 0  108 LYS A CA  1 
ATOM   859  C C   . LYS A 1 108 ? -21.343 22.210  8.429  1.000 31.290 0  108 LYS A C   1 
ATOM   860  O O   . LYS A 1 108 ? -21.064 21.870  9.587  1.000 31.330 0  108 LYS A O   1 
ATOM   861  C CB  . LYS A 1 108 ? -19.639 23.074  6.795  1.000 29.660 0  108 LYS A CB  1 
ATOM   862  C CG  . LYS A 1 108 ? -18.922 24.266  6.184  1.000 28.250 0  108 LYS A CG  1 
ATOM   863  C CD  . LYS A 1 108 ? -17.594 23.861  5.569  1.000 29.170 0  108 LYS A CD  1 
ATOM   864  C CE  . LYS A 1 108 ? -16.980 25.001  4.772  1.000 28.810 0  108 LYS A CE  1 
ATOM   865  N NZ  . LYS A 1 108 ? -16.500 26.101  5.652  1.000 31.330 1  108 LYS A NZ  1 
ATOM   866  N N   . PRO A 1 109 ? -22.203 21.506  7.687  1.000 29.100 0  109 PRO A N   1 
ATOM   867  C CA  . PRO A 1 109 ? -22.783 20.270  8.219  1.000 27.940 0  109 PRO A CA  1 
ATOM   868  C C   . PRO A 1 109 ? -21.715 19.225  8.496  1.000 28.000 0  109 PRO A C   1 
ATOM   869  O O   . PRO A 1 109 ? -20.587 19.300  8.006  1.000 30.430 0  109 PRO A O   1 
ATOM   870  C CB  . PRO A 1 109 ? -23.736 19.810  7.109  1.000 31.100 0  109 PRO A CB  1 
ATOM   871  C CG  . PRO A 1 109 ? -23.992 21.022  6.291  1.000 29.440 0  109 PRO A CG  1 
ATOM   872  C CD  . PRO A 1 109 ? -22.726 21.812  6.344  1.000 29.010 0  109 PRO A CD  1 
ATOM   873  N N   . VAL A 1 110 ? -22.092 18.231  9.303  1.000 28.210 0  110 VAL A N   1 
ATOM   874  C CA  . VAL A 1 110 ? -21.206 17.098  9.556  1.000 27.230 0  110 VAL A CA  1 
ATOM   875  C C   . VAL A 1 110 ? -20.942 16.335  8.265  1.000 28.350 0  110 VAL A C   1 
ATOM   876  O O   . VAL A 1 110 ? -19.874 15.728  8.094  1.000 30.340 0  110 VAL A O   1 
ATOM   877  C CB  . VAL A 1 110 ? -21.809 16.200  10.655 1.000 27.950 0  110 VAL A CB  1 
ATOM   878  C CG1 . VAL A 1 110 ? -21.426 14.741  10.454 1.000 27.010 0  110 VAL A CG1 1 
ATOM   879  C CG2 . VAL A 1 110 ? -21.371 16.686  12.034 1.000 29.330 0  110 VAL A CG2 1 
ATOM   880  N N   . ALA A 1 111 ? -21.884 16.386  7.319  1.000 27.780 0  111 ALA A N   1 
ATOM   881  C CA  . ALA A 1 111 ? -21.663 15.742  6.031  1.000 28.610 0  111 ALA A CA  1 
ATOM   882  C C   . ALA A 1 111 ? -20.440 16.314  5.327  1.000 28.810 0  111 ALA A C   1 
ATOM   883  O O   . ALA A 1 111 ? -19.793 15.612  4.546  1.000 31.620 0  111 ALA A O   1 
ATOM   884  C CB  . ALA A 1 111 ? -22.906 15.885  5.153  1.000 28.250 0  111 ALA A CB  1 
ATOM   885  N N   . HIS A 1 112 ? -20.070 17.560  5.635  1.000 27.810 0  112 HIS A N   1 
ATOM   886  C CA  . HIS A 1 112 ? -18.887 18.162  5.024  1.000 27.790 0  112 HIS A CA  1 
ATOM   887  C C   . HIS A 1 112 ? -17.605 17.506  5.534  1.000 27.930 0  112 HIS A C   1 
ATOM   888  O O   . HIS A 1 112 ? -16.730 17.118  4.744  1.000 27.520 0  112 HIS A O   1 
ATOM   889  C CB  . HIS A 1 112 ? -18.875 19.664  5.301  1.000 27.820 0  112 HIS A CB  1 
ATOM   890  C CG  . HIS A 1 112 ? -17.918 20.428  4.443  1.000 27.920 0  112 HIS A CG  1 
ATOM   891  N ND1 . HIS A 1 112 ? -16.600 20.625  4.792  1.000 29.930 0  112 HIS A ND1 1 
ATOM   892  C CD2 . HIS A 1 112 ? -18.091 21.052  3.253  1.000 28.250 0  112 HIS A CD2 1 
ATOM   893  C CE1 . HIS A 1 112 ? -15.998 21.332  3.852  1.000 27.870 0  112 HIS A CE1 1 
ATOM   894  N NE2 . HIS A 1 112 ? -16.881 21.605  2.908  1.000 28.780 0  112 HIS A NE2 1 
ATOM   895  N N   . ALA A 1 113 ? -17.469 17.392  6.859  1.000 27.300 0  113 ALA A N   1 
ATOM   896  C CA  . ALA A 1 113 ? -16.330 16.682  7.433  1.000 26.920 0  113 ALA A CA  1 
ATOM   897  C C   . ALA A 1 113 ? -16.294 15.235  6.962  1.000 28.020 0  113 ALA A C   1 
ATOM   898  O O   . ALA A 1 113 ? -15.218 14.682  6.687  1.000 28.330 0  113 ALA A O   1 
ATOM   899  C CB  . ALA A 1 113 ? -16.386 16.748  8.957  1.000 26.730 0  113 ALA A CB  1 
ATOM   900  N N   . GLU A 1 114 ? -17.468 14.601  6.874  1.000 28.860 0  114 GLU A N   1 
ATOM   901  C CA  . GLU A 1 114 ? -17.534 13.248  6.337  1.000 28.590 0  114 GLU A CA  1 
ATOM   902  C C   . GLU A 1 114 ? -17.004 13.202  4.911  1.000 29.350 0  114 GLU A C   1 
ATOM   903  O O   . GLU A 1 114 ? -16.273 12.277  4.548  1.000 30.250 0  114 GLU A O   1 
ATOM   904  C CB  . GLU A 1 114 ? -18.971 12.732  6.393  1.000 30.370 0  114 GLU A CB  1 
ATOM   905  C CG  . GLU A 1 114 ? -19.450 12.396  7.794  1.000 29.470 0  114 GLU A CG  1 
ATOM   906  C CD  . GLU A 1 114 ? -20.922 12.045  7.837  1.000 27.280 0  114 GLU A CD  1 
ATOM   907  O OE1 . GLU A 1 114 ? -21.604 12.212  6.804  1.000 27.570 0  114 GLU A OE1 1 
ATOM   908  O OE2 . GLU A 1 114 ? -21.395 11.601  8.903  1.000 27.160 -1 114 GLU A OE2 1 
ATOM   909  N N   . ALA A 1 115 ? -17.351 14.201  4.096  1.000 27.980 0  115 ALA A N   1 
ATOM   910  C CA  . ALA A 1 115 ? -16.855 14.256  2.725  1.000 27.870 0  115 ALA A CA  1 
ATOM   911  C C   . ALA A 1 115 ? -15.340 14.380  2.689  1.000 27.730 0  115 ALA A C   1 
ATOM   912  O O   . ALA A 1 115 ? -14.677 13.738  1.869  1.000 30.010 0  115 ALA A O   1 
ATOM   913  C CB  . ALA A 1 115 ? -17.499 15.424  1.980  1.000 28.150 0  115 ALA A CB  1 
ATOM   914  N N   . ILE A 1 116 ? -14.777 15.210  3.566  1.000 27.500 0  116 ILE A N   1 
ATOM   915  C CA  . ILE A 1 116 ? -13.322 15.372  3.591  1.000 27.540 0  116 ILE A CA  1 
ATOM   916  C C   . ILE A 1 116 ? -12.649 14.047  3.937  1.000 28.210 0  116 ILE A C   1 
ATOM   917  O O   . ILE A 1 116 ? -11.711 13.599  3.255  1.000 28.770 0  116 ILE A O   1 
ATOM   918  C CB  . ILE A 1 116 ? -12.922 16.481  4.578  1.000 27.240 0  116 ILE A CB  1 
ATOM   919  C CG1 . ILE A 1 116 ? -13.247 17.857  3.997  1.000 27.370 0  116 ILE A CG1 1 
ATOM   920  C CG2 . ILE A 1 116 ? -11.444 16.377  4.929  1.000 26.970 0  116 ILE A CG2 1 
ATOM   921  C CD1 . ILE A 1 116 ? -13.782 18.833  5.016  1.000 29.120 0  116 ILE A CD1 1 
ATOM   922  N N   . LEU A 1 117 ? -13.130 13.395  4.999  1.000 27.460 0  117 LEU A N   1 
ATOM   923  C CA  . LEU A 1 117 ? -12.520 12.138  5.423  1.000 26.860 0  117 LEU A CA  1 
ATOM   924  C C   . LEU A 1 117 ? -12.701 11.052  4.368  1.000 29.460 0  117 LEU A C   1 
ATOM   925  O O   . LEU A 1 117 ? -11.796 10.241  4.142  1.000 30.700 0  117 LEU A O   1 
ATOM   926  C CB  . LEU A 1 117 ? -13.112 11.691  6.760  1.000 26.630 0  117 LEU A CB  1 
ATOM   927  C CG  . LEU A 1 117 ? -12.722 12.526  7.980  1.000 26.370 0  117 LEU A CG  1 
ATOM   928  C CD1 . LEU A 1 117 ? -13.363 11.977  9.245  1.000 26.180 0  117 LEU A CD1 1 
ATOM   929  C CD2 . LEU A 1 117 ? -11.217 12.598  8.125  1.000 26.240 0  117 LEU A CD2 1 
ATOM   930  N N   . ARG A 1 118 ? -13.863 11.024  3.714  1.000 28.270 0  118 ARG A N   1 
ATOM   931  C CA  . ARG A 1 118 ? -14.090 10.076  2.631  1.000 29.100 0  118 ARG A CA  1 
ATOM   932  C C   . ARG A 1 118 ? -13.118 10.309  1.485  1.000 29.020 0  118 ARG A C   1 
ATOM   933  O O   . ARG A 1 118 ? -12.553 9.358   0.939  1.000 30.010 0  118 ARG A O   1 
ATOM   934  C CB  . ARG A 1 118 ? -15.531 10.167  2.136  1.000 30.750 0  118 ARG A CB  1 
ATOM   935  C CG  . ARG A 1 118 ? -15.804 9.304   0.911  1.000 29.800 0  118 ARG A CG  1 
ATOM   936  C CD  . ARG A 1 118 ? -17.226 9.485   0.426  1.000 32.980 0  118 ARG A CD  1 
ATOM   937  N NE  . ARG A 1 118 ? -18.182 9.039   1.431  1.000 34.490 0  118 ARG A NE  1 
ATOM   938  C CZ  . ARG A 1 118 ? -18.939 9.853   2.155  1.000 34.830 0  118 ARG A CZ  1 
ATOM   939  N NH1 . ARG A 1 118 ? -18.856 11.169  2.032  1.000 32.480 1  118 ARG A NH1 1 
ATOM   940  N NH2 . ARG A 1 118 ? -19.786 9.333   3.039  1.000 36.140 0  118 ARG A NH2 1 
ATOM   941  N N   . GLU A 1 119 ? -12.948 11.566  1.070  1.000 27.880 0  119 GLU A N   1 
ATOM   942  C CA  . GLU A 1 119 ? -11.979 11.874  0.022  1.000 30.110 0  119 GLU A CA  1 
ATOM   943  C C   . GLU A 1 119 ? -10.603 11.322  0.376  1.000 29.850 0  119 GLU A C   1 
ATOM   944  O O   . GLU A 1 119 ? -9.970  10.625  -0.433 1.000 29.990 0  119 GLU A O   1 
ATOM   945  C CB  . GLU A 1 119 ? -11.918 13.387  -0.209 1.000 29.410 0  119 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 119 ? -11.192 13.819  -1.483 1.000 32.260 0  119 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 119 ? -11.542 12.974  -2.701 1.000 37.040 0  119 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 119 ? -12.745 12.719  -2.937 1.000 34.150 0  119 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 119 ? -10.609 12.568  -3.425 1.000 34.020 -1 119 GLU A OE2 1 
ATOM   950  N N   . HIS A 1 120 ? -10.122 11.629  1.586  1.000 29.290 0  120 HIS A N   1 
ATOM   951  C CA  . HIS A 1 120 ? -8.805  11.140  1.999  1.000 29.200 0  120 HIS A CA  1 
ATOM   952  C C   . HIS A 1 120 ? -8.734  9.615   1.945  1.000 28.240 0  120 HIS A C   1 
ATOM   953  O O   . HIS A 1 120 ? -7.806  9.041   1.353  1.000 28.030 0  120 HIS A O   1 
ATOM   954  C CB  . HIS A 1 120 ? -8.462  11.642  3.402  1.000 27.810 0  120 HIS A CB  1 
ATOM   955  C CG  . HIS A 1 120 ? -7.108  11.211  3.878  1.000 26.990 0  120 HIS A CG  1 
ATOM   956  N ND1 . HIS A 1 120 ? -5.957  11.451  3.160  1.000 27.140 0  120 HIS A ND1 1 
ATOM   957  C CD2 . HIS A 1 120 ? -6.721  10.555  4.999  1.000 26.730 0  120 HIS A CD2 1 
ATOM   958  C CE1 . HIS A 1 120 ? -4.920  10.962  3.814  1.000 26.990 0  120 HIS A CE1 1 
ATOM   959  N NE2 . HIS A 1 120 ? -5.356  10.414  4.936  1.000 26.750 0  120 HIS A NE2 1 
ATOM   960  N N   . ALA A 1 121 ? -9.695  8.945   2.590  1.000 28.870 0  121 ALA A N   1 
ATOM   961  C CA  . ALA A 1 121 ? -9.678  7.487   2.668  1.000 27.870 0  121 ALA A CA  1 
ATOM   962  C C   . ALA A 1 121 ? -9.750  6.849   1.286  1.000 29.630 0  121 ALA A C   1 
ATOM   963  O O   . ALA A 1 121 ? -9.030  5.887   1.002  1.000 27.840 0  121 ALA A O   1 
ATOM   964  C CB  . ALA A 1 121 ? -10.829 7.002   3.547  1.000 27.240 0  121 ALA A CB  1 
ATOM   965  N N   . LYS A 1 122 ? -10.623 7.366   0.420  1.000 28.990 0  122 LYS A N   1 
ATOM   966  C CA  . LYS A 1 122 ? -10.775 6.816   -0.923 1.000 30.390 0  122 LYS A CA  1 
ATOM   967  C C   . LYS A 1 122 ? -9.487  6.963   -1.721 1.000 28.530 0  122 LYS A C   1 
ATOM   968  O O   . LYS A 1 122 ? -9.025  6.007   -2.357 1.000 28.740 0  122 LYS A O   1 
ATOM   969  C CB  . LYS A 1 122 ? -11.947 7.504   -1.627 1.000 28.560 0  122 LYS A CB  1 
ATOM   970  C CG  . LYS A 1 122 ? -12.002 7.333   -3.136 1.000 28.990 0  122 LYS A CG  1 
ATOM   971  C CD  . LYS A 1 122 ? -13.072 8.250   -3.719 1.000 31.740 0  122 LYS A CD  1 
ATOM   972  C CE  . LYS A 1 122 ? -12.819 8.578   -5.181 1.000 31.750 0  122 LYS A CE  1 
ATOM   973  N NZ  . LYS A 1 122 ? -13.953 9.352   -5.764 1.000 32.360 1  122 LYS A NZ  1 
ATOM   974  N N   . THR A 1 123 ? -8.893  8.160   -1.700 1.000 28.490 0  123 THR A N   1 
ATOM   975  C CA  . THR A 1 123 ? -7.620  8.368   -2.384 1.000 28.660 0  123 THR A CA  1 
ATOM   976  C C   . THR A 1 123 ? -6.573  7.366   -1.911 1.000 28.560 0  123 THR A C   1 
ATOM   977  O O   . THR A 1 123 ? -5.986  6.625   -2.714 1.000 28.830 0  123 THR A O   1 
ATOM   978  C CB  . THR A 1 123 ? -7.138  9.797   -2.139 1.000 29.120 0  123 THR A CB  1 
ATOM   979  O OG1 . THR A 1 123 ? -8.238  10.702  -2.301 1.000 33.510 0  123 THR A OG1 1 
ATOM   980  C CG2 . THR A 1 123 ? -6.027  10.168  -3.108 1.000 30.200 0  123 THR A CG2 1 
ATOM   981  N N   . VAL A 1 124 ? -6.363  7.305   -0.594 1.000 28.200 0  124 VAL A N   1 
ATOM   982  C CA  . VAL A 1 124 ? -5.292  6.480   -0.044 1.000 28.100 0  124 VAL A CA  1 
ATOM   983  C C   . VAL A 1 124 ? -5.538  5.004   -0.332 1.000 28.240 0  124 VAL A C   1 
ATOM   984  O O   . VAL A 1 124 ? -4.608  4.259   -0.665 1.000 28.400 0  124 VAL A O   1 
ATOM   985  C CB  . VAL A 1 124 ? -5.149  6.746   1.464  1.000 27.700 0  124 VAL A CB  1 
ATOM   986  C CG1 . VAL A 1 124 ? -4.280  5.682   2.116  1.000 27.600 0  124 VAL A CG1 1 
ATOM   987  C CG2 . VAL A 1 124 ? -4.588  8.140   1.697  1.000 27.590 0  124 VAL A CG2 1 
ATOM   988  N N   . CYS A 1 125 ? -6.792  4.557   -0.232 1.000 28.220 0  125 CYS A N   1 
ATOM   989  C CA  . CYS A 1 125 ? -7.063  3.130   -0.334 1.000 28.320 0  125 CYS A CA  1 
ATOM   990  C C   . CYS A 1 125 ? -7.099  2.649   -1.780 1.000 29.030 0  125 CYS A C   1 
ATOM   991  O O   . CYS A 1 125 ? -6.639  1.539   -2.071 1.000 29.510 0  125 CYS A O   1 
ATOM   992  C CB  . CYS A 1 125 ? -8.371  2.801   0.381  1.000 28.850 0  125 CYS A CB  1 
ATOM   993  S SG  . CYS A 1 125 ? -8.257  2.985   2.178  1.000 32.900 0  125 CYS A SG  1 
ATOM   994  N N   . THR A 1 126 ? -7.622  3.458   -2.709 1.000 28.950 0  126 THR A N   1 
ATOM   995  C CA  . THR A 1 126 ? -7.613  3.021   -4.098 1.000 29.380 0  126 THR A CA  1 
ATOM   996  C C   . THR A 1 126 ? -6.253  3.204   -4.749 1.000 29.590 0  126 THR A C   1 
ATOM   997  O O   . THR A 1 126 ? -5.960  2.514   -5.729 1.000 32.360 0  126 THR A O   1 
ATOM   998  C CB  . THR A 1 126 ? -8.677  3.752   -4.918 1.000 29.580 0  126 THR A CB  1 
ATOM   999  O OG1 . THR A 1 126 ? -8.300  5.121   -5.087 1.000 32.100 0  126 THR A OG1 1 
ATOM   1000 C CG2 . THR A 1 126 ? -10.032 3.672   -4.234 1.000 29.380 0  126 THR A CG2 1 
ATOM   1001 N N   . HIS A 1 127 ? -5.408  4.098   -4.228 1.000 29.410 0  127 HIS A N   1 
ATOM   1002 C CA  . HIS A 1 127 ? -4.039  4.129   -4.730 1.000 29.610 0  127 HIS A CA  1 
ATOM   1003 C C   . HIS A 1 127 ? -3.241  2.939   -4.211 1.000 29.560 0  127 HIS A C   1 
ATOM   1004 O O   . HIS A 1 127 ? -2.391  2.396   -4.925 1.000 29.870 0  127 HIS A O   1 
ATOM   1005 C CB  . HIS A 1 127 ? -3.357  5.441   -4.353 1.000 29.460 0  127 HIS A CB  1 
ATOM   1006 C CG  . HIS A 1 127 ? -1.960  5.554   -4.873 1.000 29.690 0  127 HIS A CG  1 
ATOM   1007 N ND1 . HIS A 1 127 ? -1.676  5.927   -6.168 1.000 30.100 0  127 HIS A ND1 1 
ATOM   1008 C CD2 . HIS A 1 127 ? -0.766  5.327   -4.277 1.000 29.580 0  127 HIS A CD2 1 
ATOM   1009 C CE1 . HIS A 1 127 ? -0.367  5.935   -6.346 1.000 30.250 0  127 HIS A CE1 1 
ATOM   1010 N NE2 . HIS A 1 127 ? 0.208   5.575   -5.214 1.000 29.940 0  127 HIS A NE2 1 
ATOM   1011 N N   . LEU A 1 128 ? -3.500  2.527   -2.976 1.000 29.350 0  128 LEU A N   1 
ATOM   1012 C CA  . LEU A 1 128 ? -2.798  1.403   -2.358 1.000 29.600 0  128 LEU A CA  1 
ATOM   1013 C C   . LEU A 1 128 ? -3.710  0.177   -2.316 1.000 29.950 0  128 LEU A C   1 
ATOM   1014 O O   . LEU A 1 128 ? -4.069  -0.335  -1.256 1.000 29.800 0  128 LEU A O   1 
ATOM   1015 C CB  . LEU A 1 128 ? -2.322  1.784   -0.960 1.000 28.750 0  128 LEU A CB  1 
ATOM   1016 C CG  . LEU A 1 128 ? -1.444  3.034   -0.842 1.000 28.670 0  128 LEU A CG  1 
ATOM   1017 C CD1 . LEU A 1 128 ? -1.088  3.309   0.609  1.000 28.280 0  128 LEU A CD1 1 
ATOM   1018 C CD2 . LEU A 1 128 ? -0.182  2.898   -1.680 1.000 29.010 0  128 LEU A CD2 1 
ATOM   1019 N N   . LYS A 1 129 ? -4.078  -0.311  -3.504 1.000 30.480 0  129 LYS A N   1 
ATOM   1020 C CA  . LYS A 1 129 ? -5.106  -1.343  -3.589 1.000 31.760 0  129 LYS A CA  1 
ATOM   1021 C C   . LYS A 1 129 ? -4.580  -2.743  -3.306 1.000 31.490 0  129 LYS A C   1 
ATOM   1022 O O   . LYS A 1 129 ? -5.384  -3.646  -3.048 1.000 31.160 0  129 LYS A O   1 
ATOM   1023 C CB  . LYS A 1 129 ? -5.764  -1.320  -4.971 1.000 31.630 0  129 LYS A CB  1 
ATOM   1024 C CG  . LYS A 1 129 ? -4.786  -1.298  -6.135 1.000 32.220 0  129 LYS A CG  1 
ATOM   1025 C CD  . LYS A 1 129 ? -5.515  -1.432  -7.468 1.000 37.600 0  129 LYS A CD  1 
ATOM   1026 C CE  . LYS A 1 129 ? -6.826  -0.646  -7.498 1.000 39.670 0  129 LYS A CE  1 
ATOM   1027 N NZ  . LYS A 1 129 ? -6.635  0.795   -7.848 1.000 33.770 1  129 LYS A NZ  1 
ATOM   1028 N N   . ASP A 1 130 ? -3.264  -2.947  -3.338 1.000 29.790 0  130 ASP A N   1 
ATOM   1029 C CA  . ASP A 1 130 ? -2.673  -4.239  -3.010 1.000 29.870 0  130 ASP A CA  1 
ATOM   1030 C C   . ASP A 1 130 ? -2.277  -4.363  -1.543 1.000 31.170 0  130 ASP A C   1 
ATOM   1031 O O   . ASP A 1 130 ? -1.778  -5.419  -1.139 1.000 30.700 0  130 ASP A O   1 
ATOM   1032 C CB  . ASP A 1 130 ? -1.453  -4.506  -3.904 1.000 32.880 0  130 ASP A CB  1 
ATOM   1033 C CG  . ASP A 1 130 ? -0.370  -3.450  -3.756 1.000 33.010 0  130 ASP A CG  1 
ATOM   1034 O OD1 . ASP A 1 130 ? -0.677  -2.330  -3.296 1.000 33.040 0  130 ASP A OD1 1 
ATOM   1035 O OD2 . ASP A 1 130 ? 0.793   -3.740  -4.114 1.000 33.410 -1 130 ASP A OD2 1 
ATOM   1036 N N   . VAL A 1 131 ? -2.502  -3.321  -0.738 1.000 31.990 0  131 VAL A N   1 
ATOM   1037 C CA  . VAL A 1 131 ? -2.097  -3.333  0.662  1.000 30.270 0  131 VAL A CA  1 
ATOM   1038 C C   . VAL A 1 131 ? -2.937  -4.341  1.438  1.000 31.600 0  131 VAL A C   1 
ATOM   1039 O O   . VAL A 1 131 ? -4.162  -4.424  1.265  1.000 31.970 0  131 VAL A O   1 
ATOM   1040 C CB  . VAL A 1 131 ? -2.216  -1.919  1.256  1.000 31.790 0  131 VAL A CB  1 
ATOM   1041 C CG1 . VAL A 1 131 ? -2.450  -1.974  2.758  1.000 29.760 0  131 VAL A CG1 1 
ATOM   1042 C CG2 . VAL A 1 131 ? -0.971  -1.104  0.933  1.000 30.070 0  131 VAL A CG2 1 
ATOM   1043 N N   . ILE A 1 132 ? -2.280  -5.109  2.305  1.000 30.730 0  132 ILE A N   1 
ATOM   1044 C CA  . ILE A 1 132 ? -2.965  -6.157  3.054  1.000 28.470 0  132 ILE A CA  1 
ATOM   1045 C C   . ILE A 1 132 ? -3.584  -5.652  4.356  1.000 29.090 0  132 ILE A C   1 
ATOM   1046 O O   . ILE A 1 132 ? -4.580  -6.215  4.819  1.000 31.310 0  132 ILE A O   1 
ATOM   1047 C CB  . ILE A 1 132 ? -1.995  -7.317  3.331  1.000 28.630 0  132 ILE A CB  1 
ATOM   1048 C CG1 . ILE A 1 132 ? -0.833  -6.841  4.208  1.000 28.450 0  132 ILE A CG1 1 
ATOM   1049 C CG2 . ILE A 1 132 ? -1.470  -7.895  2.028  1.000 30.530 0  132 ILE A CG2 1 
ATOM   1050 C CD1 . ILE A 1 132 ? -0.434  -7.822  5.289  1.000 28.380 0  132 ILE A CD1 1 
ATOM   1051 N N   . SER A 1 133 ? -3.028  -4.600  4.957  1.000 29.340 0  133 SER A N   1 
ATOM   1052 C CA  . SER A 1 133 ? -3.505  -4.132  6.253  1.000 27.500 0  133 SER A CA  1 
ATOM   1053 C C   . SER A 1 133 ? -3.297  -2.629  6.364  1.000 27.960 0  133 SER A C   1 
ATOM   1054 O O   . SER A 1 133 ? -2.215  -2.126  6.048  1.000 28.930 0  133 SER A O   1 
ATOM   1055 C CB  . SER A 1 133 ? -2.786  -4.854  7.397  1.000 27.380 0  133 SER A CB  1 
ATOM   1056 O OG  . SER A 1 133 ? -2.755  -4.057  8.569  1.000 27.050 0  133 SER A OG  1 
ATOM   1057 N N   . HIS A 1 134 ? -4.335  -1.925  6.810  1.000 27.330 0  134 HIS A N   1 
ATOM   1058 C CA  . HIS A 1 134 ? -4.300  -0.479  7.002  1.000 27.260 0  134 HIS A CA  1 
ATOM   1059 C C   . HIS A 1 134 ? -4.434  -0.146  8.482  1.000 27.530 0  134 HIS A C   1 
ATOM   1060 O O   . HIS A 1 134 ? -5.343  -0.648  9.155  1.000 28.780 0  134 HIS A O   1 
ATOM   1061 C CB  . HIS A 1 134 ? -5.432  0.208   6.235  1.000 27.130 0  134 HIS A CB  1 
ATOM   1062 C CG  . HIS A 1 134 ? -5.175  0.364   4.769  1.000 27.300 0  134 HIS A CG  1 
ATOM   1063 N ND1 . HIS A 1 134 ? -4.211  1.211   4.265  1.000 30.760 0  134 HIS A ND1 1 
ATOM   1064 C CD2 . HIS A 1 134 ? -5.778  -0.199  3.696  1.000 30.580 0  134 HIS A CD2 1 
ATOM   1065 C CE1 . HIS A 1 134 ? -4.224  1.153   2.945  1.000 30.800 0  134 HIS A CE1 1 
ATOM   1066 N NE2 . HIS A 1 134 ? -5.165  0.304   2.574  1.000 28.830 0  134 HIS A NE2 1 
ATOM   1067 N N   . ASP A 1 135 ? -3.568  0.745   8.968  1.000 27.980 0  135 ASP A N   1 
ATOM   1068 C CA  . ASP A 1 135 ? -3.761  1.425   10.249 1.000 26.400 0  135 ASP A CA  1 
ATOM   1069 C C   . ASP A 1 135 ? -4.740  2.565   10.008 1.000 28.470 0  135 ASP A C   1 
ATOM   1070 O O   . ASP A 1 135 ? -4.356  3.666   9.610  1.000 28.600 0  135 ASP A O   1 
ATOM   1071 C CB  . ASP A 1 135 ? -2.440  1.952   10.796 1.000 26.240 0  135 ASP A CB  1 
ATOM   1072 C CG  . ASP A 1 135 ? -1.591  0.868   11.423 1.000 27.990 0  135 ASP A CG  1 
ATOM   1073 O OD1 . ASP A 1 135 ? -2.164  -0.090  11.979 1.000 29.300 0  135 ASP A OD1 1 
ATOM   1074 O OD2 . ASP A 1 135 ? -0.349  0.983   11.364 1.000 26.160 -1 135 ASP A OD2 1 
ATOM   1075 N N   . VAL A 1 136 ? -6.024  2.302   10.261 1.000 27.290 0  136 VAL A N   1 
ATOM   1076 C CA  . VAL A 1 136 ? -7.050  3.287   9.926  1.000 26.050 0  136 VAL A CA  1 
ATOM   1077 C C   . VAL A 1 136 ? -6.935  4.513   10.824 1.000 26.850 0  136 VAL A C   1 
ATOM   1078 O O   . VAL A 1 136 ? -6.848  5.649   10.343 1.000 28.060 0  136 VAL A O   1 
ATOM   1079 C CB  . VAL A 1 136 ? -8.447  2.652   10.011 1.000 29.070 0  136 VAL A CB  1 
ATOM   1080 C CG1 . VAL A 1 136 ? -9.499  3.630   9.517  1.000 28.530 0  136 VAL A CG1 1 
ATOM   1081 C CG2 . VAL A 1 136 ? -8.486  1.369   9.194  1.000 31.640 0  136 VAL A CG2 1 
ATOM   1082 N N   . VAL A 1 137 ? -6.940  4.305   12.136 1.000 26.300 0  137 VAL A N   1 
ATOM   1083 C CA  . VAL A 1 137 ? -6.789  5.376   13.113 1.000 25.410 0  137 VAL A CA  1 
ATOM   1084 C C   . VAL A 1 137 ? -5.577  5.063   13.974 1.000 26.300 0  137 VAL A C   1 
ATOM   1085 O O   . VAL A 1 137 ? -5.433  3.936   14.460 1.000 27.110 0  137 VAL A O   1 
ATOM   1086 C CB  . VAL A 1 137 ? -8.048  5.543   13.982 1.000 25.300 0  137 VAL A CB  1 
ATOM   1087 C CG1 . VAL A 1 137 ? -7.814  6.598   15.050 1.000 25.100 0  137 VAL A CG1 1 
ATOM   1088 C CG2 . VAL A 1 137 ? -9.243  5.911   13.118 1.000 25.450 0  137 VAL A CG2 1 
ATOM   1089 N N   . ASN A 1 138 ? -4.715  6.056   14.167 1.000 25.210 0  138 ASN A N   1 
ATOM   1090 C CA  . ASN A 1 138 ? -3.494  5.888   14.939 1.000 25.120 0  138 ASN A CA  1 
ATOM   1091 C C   . ASN A 1 138 ? -3.545  6.764   16.183 1.000 25.770 0  138 ASN A C   1 
ATOM   1092 O O   . ASN A 1 138 ? -3.766  7.976   16.083 1.000 26.680 0  138 ASN A O   1 
ATOM   1093 C CB  . ASN A 1 138 ? -2.276  6.247   14.086 1.000 25.240 0  138 ASN A CB  1 
ATOM   1094 C CG  . ASN A 1 138 ? -0.991  5.678   14.638 1.000 25.230 0  138 ASN A CG  1 
ATOM   1095 O OD1 . ASN A 1 138 ? -0.917  4.499   14.978 1.000 25.630 0  138 ASN A OD1 1 
ATOM   1096 N ND2 . ASN A 1 138 ? 0.032   6.518   14.737 1.000 25.210 0  138 ASN A ND2 1 
ATOM   1097 N N   . GLU A 1 139 ? -3.331  6.144   17.350 1.000 24.810 0  139 GLU A N   1 
ATOM   1098 C CA  . GLU A 1 139 ? -3.179  6.845   18.623 1.000 24.620 0  139 GLU A CA  1 
ATOM   1099 C C   . GLU A 1 139 ? -4.316  7.822   18.882 1.000 24.550 0  139 GLU A C   1 
ATOM   1100 O O   . GLU A 1 139 ? -4.150  9.035   18.720 1.000 26.270 0  139 GLU A O   1 
ATOM   1101 C CB  . GLU A 1 139 ? -1.835  7.572   18.674 1.000 24.590 0  139 GLU A CB  1 
ATOM   1102 C CG  . GLU A 1 139 ? -0.720  6.823   17.970 1.000 24.740 0  139 GLU A CG  1 
ATOM   1103 C CD  . GLU A 1 139 ? 0.656   7.228   18.444 1.000 24.710 0  139 GLU A CD  1 
ATOM   1104 O OE1 . GLU A 1 139 ? 0.872   8.435   18.672 1.000 25.390 0  139 GLU A OE1 1 
ATOM   1105 O OE2 . GLU A 1 139 ? 1.527   6.342   18.567 1.000 24.790 -1 139 GLU A OE2 1 
ATOM   1106 N N   . ALA A 1 140 ? -5.478  7.303   19.267 1.000 24.970 0  140 ALA A N   1 
ATOM   1107 C CA  . ALA A 1 140 ? -6.660  8.117   19.508 1.000 24.510 0  140 ALA A CA  1 
ATOM   1108 C C   . ALA A 1 140 ? -7.042  8.165   20.982 1.000 26.810 0  140 ALA A C   1 
ATOM   1109 O O   . ALA A 1 140 ? -8.104  8.694   21.323 1.000 26.480 0  140 ALA A O   1 
ATOM   1110 C CB  . ALA A 1 140 ? -7.834  7.595   18.679 1.000 24.650 0  140 ALA A CB  1 
ATOM   1111 N N   . VAL A 1 141 ? -6.203  7.629   21.864 1.000 26.450 0  141 VAL A N   1 
ATOM   1112 C CA  . VAL A 1 141 ? -6.511  7.525   23.284 1.000 26.110 0  141 VAL A CA  1 
ATOM   1113 C C   . VAL A 1 141 ? -5.355  8.123   24.070 1.000 26.910 0  141 VAL A C   1 
ATOM   1114 O O   . VAL A 1 141 ? -4.194  7.758   23.849 1.000 25.500 0  141 VAL A O   1 
ATOM   1115 C CB  . VAL A 1 141 ? -6.761  6.064   23.703 1.000 26.910 0  141 VAL A CB  1 
ATOM   1116 C CG1 . VAL A 1 141 ? -6.961  5.959   25.208 1.000 27.000 0  141 VAL A CG1 1 
ATOM   1117 C CG2 . VAL A 1 141 ? -7.955  5.495   22.950 1.000 26.670 0  141 VAL A CG2 1 
ATOM   1118 N N   . SER A 1 142 ? -5.671  9.044   24.973 1.000 26.090 0  142 SER A N   1 
ATOM   1119 C CA  . SER A 1 142 ? -4.638  9.739   25.730 1.000 26.270 0  142 SER A CA  1 
ATOM   1120 C C   . SER A 1 142 ? -3.916  8.767   26.656 1.000 26.980 0  142 SER A C   1 
ATOM   1121 O O   . SER A 1 142 ? -4.565  8.073   27.449 1.000 26.180 0  142 SER A O   1 
ATOM   1122 C CB  . SER A 1 142 ? -5.243  10.883  26.540 1.000 29.180 0  142 SER A CB  1 
ATOM   1123 O OG  . SER A 1 142 ? -4.526  11.090  27.745 1.000 28.790 0  142 SER A OG  1 
ATOM   1124 N N   . PRO A 1 143 ? -2.584  8.683   26.585 1.000 26.720 0  143 PRO A N   1 
ATOM   1125 C CA  . PRO A 1 143 ? -1.836  7.846   27.535 1.000 24.720 0  143 PRO A CA  1 
ATOM   1126 C C   . PRO A 1 143 ? -1.833  8.378   28.958 1.000 31.250 0  143 PRO A C   1 
ATOM   1127 O O   . PRO A 1 143 ? -1.249  7.732   29.836 1.000 32.740 0  143 PRO A O   1 
ATOM   1128 C CB  . PRO A 1 143 ? -0.416  7.837   26.953 1.000 24.010 0  143 PRO A CB  1 
ATOM   1129 C CG  . PRO A 1 143 ? -0.335  9.066   26.116 1.000 23.970 0  143 PRO A CG  1 
ATOM   1130 C CD  . PRO A 1 143 ? -1.711  9.315   25.582 1.000 24.600 0  143 PRO A CD  1 
ATOM   1131 N N   . LYS A 1 144 ? -2.452  9.533   29.217 1.000 32.040 0  144 LYS A N   1 
ATOM   1132 C CA  . LYS A 1 144 ? -2.503  10.090  30.564 1.000 32.380 0  144 LYS A CA  1 
ATOM   1133 C C   . LYS A 1 144 ? -3.753  9.672   31.330 1.000 30.300 0  144 LYS A C   1 
ATOM   1134 O O   . LYS A 1 144 ? -3.659  9.318   32.509 1.000 35.300 0  144 LYS A O   1 
ATOM   1135 C CB  . LYS A 1 144 ? -2.419  11.618  30.508 1.000 34.500 0  144 LYS A CB  1 
ATOM   1136 C CG  . LYS A 1 144 ? -1.001  12.154  30.395 1.000 36.780 0  144 LYS A CG  1 
ATOM   1137 C CD  . LYS A 1 144 ? -0.934  13.645  30.703 1.000 40.290 0  144 LYS A CD  1 
ATOM   1138 C CE  . LYS A 1 144 ? -1.550  13.969  32.057 1.000 39.850 0  144 LYS A CE  1 
ATOM   1139 N NZ  . LYS A 1 144 ? -2.205  15.310  32.060 1.000 39.740 1  144 LYS A NZ  1 
ATOM   1140 N N   . ASP A 1 145 ? -4.926  9.705   30.694 1.000 28.730 0  145 ASP A N   1 
ATOM   1141 C CA  . ASP A 1 145 ? -6.159  9.391   31.409 1.000 29.010 0  145 ASP A CA  1 
ATOM   1142 C C   . ASP A 1 145 ? -7.121  8.533   30.594 1.000 29.150 0  145 ASP A C   1 
ATOM   1143 O O   . ASP A 1 145 ? -8.276  8.368   31.008 1.000 27.780 0  145 ASP A O   1 
ATOM   1144 C CB  . ASP A 1 145 ? -6.873  10.674  31.869 1.000 30.950 0  145 ASP A CB  1 
ATOM   1145 C CG  . ASP A 1 145 ? -7.291  11.576  30.713 1.000 32.200 0  145 ASP A CG  1 
ATOM   1146 O OD1 . ASP A 1 145 ? -7.030  11.237  29.539 1.000 30.850 0  145 ASP A OD1 1 
ATOM   1147 O OD2 . ASP A 1 145 ? -7.892  12.638  30.990 1.000 33.500 -1 145 ASP A OD2 1 
ATOM   1148 N N   . GLY A 1 146 ? -6.699  8.001   29.450 1.000 29.180 0  146 GLY A N   1 
ATOM   1149 C CA  . GLY A 1 146 ? -7.564  7.166   28.649 1.000 27.250 0  146 GLY A CA  1 
ATOM   1150 C C   . GLY A 1 146 ? -8.641  7.899   27.883 1.000 26.520 0  146 GLY A C   1 
ATOM   1151 O O   . GLY A 1 146 ? -9.435  7.247   27.195 1.000 28.080 0  146 GLY A O   1 
ATOM   1152 N N   . SER A 1 147 ? -8.705  9.224   27.984 1.000 26.140 0  147 SER A N   1 
ATOM   1153 C CA  . SER A 1 147 ? -9.658  9.985   27.191 1.000 26.650 0  147 SER A CA  1 
ATOM   1154 C C   . SER A 1 147 ? -9.259  9.962   25.718 1.000 26.830 0  147 SER A C   1 
ATOM   1155 O O   . SER A 1 147 ? -8.114  9.674   25.357 1.000 26.080 0  147 SER A O   1 
ATOM   1156 C CB  . SER A 1 147 ? -9.748  11.431  27.688 1.000 26.420 0  147 SER A CB  1 
ATOM   1157 O OG  . SER A 1 147 ? -8.612  12.186  27.300 1.000 24.050 0  147 SER A OG  1 
ATOM   1158 N N   . LEU A 1 148 ? -10.228 10.267  24.861 1.000 24.270 0  148 LEU A N   1 
ATOM   1159 C CA  . LEU A 1 148 ? -9.991  10.287  23.425 1.000 26.450 0  148 LEU A CA  1 
ATOM   1160 C C   . LEU A 1 148 ? -9.364  11.609  22.998 1.000 24.920 0  148 LEU A C   1 
ATOM   1161 O O   . LEU A 1 148 ? -9.842  12.684  23.370 1.000 26.620 0  148 LEU A O   1 
ATOM   1162 C CB  . LEU A 1 148 ? -11.297 10.037  22.674 1.000 27.280 0  148 LEU A CB  1 
ATOM   1163 C CG  . LEU A 1 148 ? -11.903 8.658   22.960 1.000 26.150 0  148 LEU A CG  1 
ATOM   1164 C CD1 . LEU A 1 148 ? -13.421 8.664   22.800 1.000 24.770 0  148 LEU A CD1 1 
ATOM   1165 C CD2 . LEU A 1 148 ? -11.262 7.590   22.079 1.000 24.560 0  148 LEU A CD2 1 
ATOM   1166 N N   . ILE A 1 149 ? -8.275  11.520  22.234 1.000 25.140 0  149 ILE A N   1 
ATOM   1167 C CA  . ILE A 1 149 ? -7.605  12.710  21.723 1.000 27.750 0  149 ILE A CA  1 
ATOM   1168 C C   . ILE A 1 149 ? -8.512  13.422  20.727 1.000 26.850 0  149 ILE A C   1 
ATOM   1169 O O   . ILE A 1 149 ? -9.134  12.791  19.862 1.000 27.110 0  149 ILE A O   1 
ATOM   1170 C CB  . ILE A 1 149 ? -6.256  12.327  21.091 1.000 27.120 0  149 ILE A CB  1 
ATOM   1171 C CG1 . ILE A 1 149 ? -5.374  11.622  22.122 1.000 26.540 0  149 ILE A CG1 1 
ATOM   1172 C CG2 . ILE A 1 149 ? -5.547  13.554  20.540 1.000 27.930 0  149 ILE A CG2 1 
ATOM   1173 C CD1 . ILE A 1 149 ? -4.434  10.602  21.528 1.000 26.310 0  149 ILE A CD1 1 
ATOM   1174 N N   . GLN A 1 150 ? -8.600  14.744  20.851 1.000 25.930 0  150 GLN A N   1 
ATOM   1175 C CA  . GLN A 1 150 ? -9.517  15.552  20.059 1.000 28.310 0  150 GLN A CA  1 
ATOM   1176 C C   . GLN A 1 150 ? -8.792  16.243  18.910 1.000 26.100 0  150 GLN A C   1 
ATOM   1177 O O   . GLN A 1 150 ? -7.611  16.584  19.007 1.000 25.510 0  150 GLN A O   1 
ATOM   1178 C CB  . GLN A 1 150 ? -10.205 16.610  20.928 1.000 28.690 0  150 GLN A CB  1 
ATOM   1179 C CG  . GLN A 1 150 ? -11.107 16.056  22.016 1.000 29.300 0  150 GLN A CG  1 
ATOM   1180 C CD  . GLN A 1 150 ? -12.406 15.492  21.473 1.000 28.550 0  150 GLN A CD  1 
ATOM   1181 O OE1 . GLN A 1 150 ? -13.270 16.233  21.000 1.000 29.910 0  150 GLN A OE1 1 
ATOM   1182 N NE2 . GLN A 1 150 ? -12.552 14.176  21.545 1.000 27.400 0  150 GLN A NE2 1 
ATOM   1183 N N   . ASN A 1 151 ? -9.520  16.443  17.813 1.000 25.070 0  151 ASN A N   1 
ATOM   1184 C CA  . ASN A 1 151 ? -9.037  17.233  16.690 1.000 24.840 0  151 ASN A CA  1 
ATOM   1185 C C   . ASN A 1 151 ? -10.231 17.916  16.033 1.000 28.420 0  151 ASN A C   1 
ATOM   1186 O O   . ASN A 1 151 ? -11.372 17.796  16.493 1.000 26.600 0  151 ASN A O   1 
ATOM   1187 C CB  . ASN A 1 151 ? -8.256  16.374  15.690 1.000 24.900 0  151 ASN A CB  1 
ATOM   1188 C CG  . ASN A 1 151 ? -9.065  15.205  15.167 1.000 25.000 0  151 ASN A CG  1 
ATOM   1189 O OD1 . ASN A 1 151 ? -10.205 15.362  14.731 1.000 26.950 0  151 ASN A OD1 1 
ATOM   1190 N ND2 . ASN A 1 151 ? -8.471  14.019  15.199 1.000 24.960 0  151 ASN A ND2 1 
ATOM   1191 N N   . VAL A 1 152 ? -9.956  18.637  14.942 1.000 25.430 0  152 VAL A N   1 
ATOM   1192 C CA  . VAL A 1 152 ? -10.989 19.416  14.272 1.000 25.760 0  152 VAL A CA  1 
ATOM   1193 C C   . VAL A 1 152 ? -12.105 18.532  13.720 1.000 28.100 0  152 VAL A C   1 
ATOM   1194 O O   . VAL A 1 152 ? -13.209 19.022  13.460 1.000 26.020 0  152 VAL A O   1 
ATOM   1195 C CB  . VAL A 1 152 ? -10.347 20.270  13.157 1.000 25.530 0  152 VAL A CB  1 
ATOM   1196 C CG1 . VAL A 1 152 ? -9.922  19.392  11.987 1.000 27.760 0  152 VAL A CG1 1 
ATOM   1197 C CG2 . VAL A 1 152 ? -11.285 21.378  12.708 1.000 27.960 0  152 VAL A CG2 1 
ATOM   1198 N N   . PHE A 1 153 ? -11.858 17.231  13.561 1.000 27.650 0  153 PHE A N   1 
ATOM   1199 C CA  . PHE A 1 153 ? -12.890 16.324  13.075 1.000 27.270 0  153 PHE A CA  1 
ATOM   1200 C C   . PHE A 1 153 ? -13.745 15.794  14.219 1.000 27.290 0  153 PHE A C   1 
ATOM   1201 O O   . PHE A 1 153 ? -14.975 15.758  14.113 1.000 26.670 0  153 PHE A O   1 
ATOM   1202 C CB  . PHE A 1 153 ? -12.268 15.146  12.316 1.000 29.010 0  153 PHE A CB  1 
ATOM   1203 C CG  . PHE A 1 153 ? -11.630 15.524  11.009 1.000 28.300 0  153 PHE A CG  1 
ATOM   1204 C CD1 . PHE A 1 153 ? -12.404 15.937  9.938  1.000 26.570 0  153 PHE A CD1 1 
ATOM   1205 C CD2 . PHE A 1 153 ? -10.255 15.449  10.849 1.000 26.890 0  153 PHE A CD2 1 
ATOM   1206 C CE1 . PHE A 1 153 ? -11.816 16.280  8.733  1.000 27.050 0  153 PHE A CE1 1 
ATOM   1207 C CE2 . PHE A 1 153 ? -9.662  15.788  9.649  1.000 26.030 0  153 PHE A CE2 1 
ATOM   1208 C CZ  . PHE A 1 153 ? -10.443 16.205  8.590  1.000 26.160 0  153 PHE A CZ  1 
ATOM   1209 N N   . THR A 1 154 ? -13.103 15.361  15.308 1.000 28.110 0  154 THR A N   1 
ATOM   1210 C CA  . THR A 1 154 ? -13.854 14.862  16.455 1.000 28.560 0  154 THR A CA  1 
ATOM   1211 C C   . THR A 1 154 ? -14.614 15.974  17.161 1.000 26.040 0  154 THR A C   1 
ATOM   1212 O O   . THR A 1 154 ? -15.698 15.731  17.700 1.000 29.070 0  154 THR A O   1 
ATOM   1213 C CB  . THR A 1 154 ? -12.916 14.160  17.436 1.000 27.850 0  154 THR A CB  1 
ATOM   1214 O OG1 . THR A 1 154 ? -12.256 15.134  18.254 1.000 26.550 0  154 THR A OG1 1 
ATOM   1215 C CG2 . THR A 1 154 ? -11.878 13.344  16.679 1.000 25.500 0  154 THR A CG2 1 
ATOM   1216 N N   . LYS A 1 155 ? -14.071 17.193  17.172 1.000 26.900 0  155 LYS A N   1 
ATOM   1217 C CA  . LYS A 1 155 ? -14.808 18.311  17.750 1.000 27.180 0  155 LYS A CA  1 
ATOM   1218 C C   . LYS A 1 155 ? -16.104 18.571  16.996 1.000 26.170 0  155 LYS A C   1 
ATOM   1219 O O   . LYS A 1 155 ? -17.064 19.095  17.571 1.000 25.770 0  155 LYS A O   1 
ATOM   1220 C CB  . LYS A 1 155 ? -13.936 19.566  17.786 1.000 25.250 0  155 LYS A CB  1 
ATOM   1221 C CG  . LYS A 1 155 ? -12.910 19.572  18.911 1.000 25.030 0  155 LYS A CG  1 
ATOM   1222 C CD  . LYS A 1 155 ? -11.914 20.707  18.743 1.000 27.170 0  155 LYS A CD  1 
ATOM   1223 C CE  . LYS A 1 155 ? -10.567 20.365  19.356 1.000 26.030 0  155 LYS A CE  1 
ATOM   1224 N NZ  . LYS A 1 155 ? -9.468  21.141  18.717 1.000 29.270 1  155 LYS A NZ  1 
ATOM   1225 N N   . ARG A 1 156 ? -16.155 18.205  15.717 1.000 26.440 0  156 ARG A N   1 
ATOM   1226 C CA  . ARG A 1 156 ? -17.330 18.456  14.893 1.000 27.470 0  156 ARG A CA  1 
ATOM   1227 C C   . ARG A 1 156 ? -18.292 17.274  14.879 1.000 28.840 0  156 ARG A C   1 
ATOM   1228 O O   . ARG A 1 156 ? -19.508 17.469  14.973 1.000 29.140 0  156 ARG A O   1 
ATOM   1229 C CB  . ARG A 1 156 ? -16.902 18.795  13.461 1.000 27.260 0  156 ARG A CB  1 
ATOM   1230 C CG  . ARG A 1 156 ? -18.044 19.195  12.536 1.000 27.910 0  156 ARG A CG  1 
ATOM   1231 C CD  . ARG A 1 156 ? -18.899 20.303  13.138 1.000 26.970 0  156 ARG A CD  1 
ATOM   1232 N NE  . ARG A 1 156 ? -20.007 20.673  12.265 1.000 29.140 0  156 ARG A NE  1 
ATOM   1233 C CZ  . ARG A 1 156 ? -21.282 20.397  12.509 1.000 28.960 0  156 ARG A CZ  1 
ATOM   1234 N NH1 . ARG A 1 156 ? -21.653 19.752  13.602 1.000 27.580 1  156 ARG A NH1 1 
ATOM   1235 N NH2 . ARG A 1 156 ? -22.207 20.782  11.634 1.000 27.330 0  156 ARG A NH2 1 
ATOM   1236 N N   . MET A 1 157 ? -17.779 16.048  14.767 1.000 30.350 0  157 MET A N   1 
ATOM   1237 C CA  . MET A 1 157 ? -18.626 14.870  14.645 1.000 29.280 0  157 MET A CA  1 
ATOM   1238 C C   . MET A 1 157 ? -18.779 14.094  15.944 1.000 31.190 0  157 MET A C   1 
ATOM   1239 O O   . MET A 1 157 ? -19.775 13.377  16.103 1.000 31.690 0  157 MET A O   1 
ATOM   1240 C CB  . MET A 1 157 ? -18.068 13.904  13.592 1.000 28.730 0  157 MET A CB  1 
ATOM   1241 C CG  . MET A 1 157 ? -17.664 14.532  12.278 1.000 31.000 0  157 MET A CG  1 
ATOM   1242 S SD  . MET A 1 157 ? -16.507 13.456  11.408 1.000 31.420 0  157 MET A SD  1 
ATOM   1243 C CE  . MET A 1 157 ? -17.442 11.931  11.372 1.000 26.910 0  157 MET A CE  1 
ATOM   1244 N N   . GLY A 1 158 ? -17.826 14.215  16.866 1.000 27.210 0  158 GLY A N   1 
ATOM   1245 C CA  . GLY A 1 158 ? -17.722 13.279  17.970 1.000 26.320 0  158 GLY A CA  1 
ATOM   1246 C C   . GLY A 1 158 ? -16.596 12.300  17.710 1.000 27.010 0  158 GLY A C   1 
ATOM   1247 O O   . GLY A 1 158 ? -16.393 11.886  16.565 1.000 29.440 0  158 GLY A O   1 
ATOM   1248 N N   . ALA A 1 159 ? -15.844 11.935  18.749 1.000 26.060 0  159 ALA A N   1 
ATOM   1249 C CA  . ALA A 1 159 ? -14.651 11.112  18.550 1.000 25.950 0  159 ALA A CA  1 
ATOM   1250 C C   . ALA A 1 159 ? -15.008 9.721   18.036 1.000 25.730 0  159 ALA A C   1 
ATOM   1251 O O   . ALA A 1 159 ? -14.457 9.259   17.027 1.000 25.370 0  159 ALA A O   1 
ATOM   1252 C CB  . ALA A 1 159 ? -13.858 11.016  19.853 1.000 25.270 0  159 ALA A CB  1 
ATOM   1253 N N   . VAL A 1 160 ? -15.911 9.028   18.735 1.000 27.180 0  160 VAL A N   1 
ATOM   1254 C CA  . VAL A 1 160 ? -16.284 7.676   18.327 1.000 25.360 0  160 VAL A CA  1 
ATOM   1255 C C   . VAL A 1 160 ? -16.970 7.702   16.968 1.000 25.580 0  160 VAL A C   1 
ATOM   1256 O O   . VAL A 1 160 ? -16.777 6.802   16.140 1.000 26.730 0  160 VAL A O   1 
ATOM   1257 C CB  . VAL A 1 160 ? -17.165 7.020   19.404 1.000 25.330 0  160 VAL A CB  1 
ATOM   1258 C CG1 . VAL A 1 160 ? -17.778 5.734   18.884 1.000 25.470 0  160 VAL A CG1 1 
ATOM   1259 C CG2 . VAL A 1 160 ? -16.347 6.756   20.652 1.000 25.150 0  160 VAL A CG2 1 
ATOM   1260 N N   . GLU A 1 161 ? -17.752 8.750   16.705 1.000 25.610 0  161 GLU A N   1 
ATOM   1261 C CA  . GLU A 1 161 ? -18.360 8.897   15.390 1.000 25.820 0  161 GLU A CA  1 
ATOM   1262 C C   . GLU A 1 161 ? -17.293 8.999   14.310 1.000 25.820 0  161 GLU A C   1 
ATOM   1263 O O   . GLU A 1 161 ? -17.380 8.328   13.273 1.000 26.110 0  161 GLU A O   1 
ATOM   1264 C CB  . GLU A 1 161 ? -19.261 10.132  15.360 1.000 27.690 0  161 GLU A CB  1 
ATOM   1265 C CG  . GLU A 1 161 ? -20.633 9.938   15.975 1.000 26.070 0  161 GLU A CG  1 
ATOM   1266 C CD  . GLU A 1 161 ? -20.577 9.775   17.480 1.000 28.570 0  161 GLU A CD  1 
ATOM   1267 O OE1 . GLU A 1 161 ? -19.796 10.503  18.128 1.000 25.780 0  161 GLU A OE1 1 
ATOM   1268 O OE2 . GLU A 1 161 ? -21.328 8.931   18.015 1.000 31.520 -1 161 GLU A OE2 1 
ATOM   1269 N N   . GLN A 1 162 ? -16.254 9.799   14.559 1.000 25.660 0  162 GLN A N   1 
ATOM   1270 C CA  . GLN A 1 162 ? -15.214 9.998   13.556 1.000 25.680 0  162 GLN A CA  1 
ATOM   1271 C C   . GLN A 1 162 ? -14.412 8.725   13.326 1.000 25.650 0  162 GLN A C   1 
ATOM   1272 O O   . GLN A 1 162 ? -14.080 8.394   12.182 1.000 26.190 0  162 GLN A O   1 
ATOM   1273 C CB  . GLN A 1 162 ? -14.300 11.147  13.981 1.000 26.290 0  162 GLN A CB  1 
ATOM   1274 C CG  . GLN A 1 162 ? -13.211 11.494  12.982 1.000 25.580 0  162 GLN A CG  1 
ATOM   1275 C CD  . GLN A 1 162 ? -11.825 11.339  13.569 1.000 26.680 0  162 GLN A CD  1 
ATOM   1276 O OE1 . GLN A 1 162 ? -11.557 10.395  14.310 1.000 28.700 0  162 GLN A OE1 1 
ATOM   1277 N NE2 . GLN A 1 162 ? -10.937 12.272  13.249 1.000 27.340 0  162 GLN A NE2 1 
ATOM   1278 N N   . ILE A 1 163 ? -14.125 7.975   14.392 1.000 25.500 0  163 ILE A N   1 
ATOM   1279 C CA  . ILE A 1 163 ? -13.321 6.765   14.238 1.000 25.760 0  163 ILE A CA  1 
ATOM   1280 C C   . ILE A 1 163 ? -14.119 5.676   13.526 1.000 26.530 0  163 ILE A C   1 
ATOM   1281 O O   . ILE A 1 163 ? -13.617 5.016   12.603 1.000 25.780 0  163 ILE A O   1 
ATOM   1282 C CB  . ILE A 1 163 ? -12.800 6.288   15.604 1.000 25.300 0  163 ILE A CB  1 
ATOM   1283 C CG1 . ILE A 1 163 ? -11.855 7.334   16.196 1.000 25.130 0  163 ILE A CG1 1 
ATOM   1284 C CG2 . ILE A 1 163 ? -12.095 4.951   15.467 1.000 25.320 0  163 ILE A CG2 1 
ATOM   1285 C CD1 . ILE A 1 163 ? -11.793 7.311   17.701 1.000 24.960 0  163 ILE A CD1 1 
ATOM   1286 N N   . GLU A 1 164 ? -15.367 5.459   13.959 1.000 25.770 0  164 GLU A N   1 
ATOM   1287 C CA  . GLU A 1 164 ? -16.263 4.545   13.261 1.000 25.930 0  164 GLU A CA  1 
ATOM   1288 C C   . GLU A 1 164 ? -16.373 4.890   11.781 1.000 26.130 0  164 GLU A C   1 
ATOM   1289 O O   . GLU A 1 164 ? -16.295 4.007   10.916 1.000 29.500 0  164 GLU A O   1 
ATOM   1290 C CB  . GLU A 1 164 ? -17.642 4.573   13.921 1.000 25.990 0  164 GLU A CB  1 
ATOM   1291 C CG  . GLU A 1 164 ? -18.720 3.844   13.142 1.000 26.220 0  164 GLU A CG  1 
ATOM   1292 C CD  . GLU A 1 164 ? -20.069 3.901   13.822 1.000 26.300 0  164 GLU A CD  1 
ATOM   1293 O OE1 . GLU A 1 164 ? -20.270 4.787   14.676 1.000 26.210 0  164 GLU A OE1 1 
ATOM   1294 O OE2 . GLU A 1 164 ? -20.936 3.063   13.501 1.000 27.530 -1 164 GLU A OE2 1 
ATOM   1295 N N   . PHE A 1 165 ? -16.572 6.175   11.470 1.000 26.160 0  165 PHE A N   1 
ATOM   1296 C CA  . PHE A 1 165 ? -16.719 6.584   10.078 1.000 26.860 0  165 PHE A CA  1 
ATOM   1297 C C   . PHE A 1 165 ? -15.445 6.322   9.283  1.000 27.660 0  165 PHE A C   1 
ATOM   1298 O O   . PHE A 1 165 ? -15.505 5.858   8.136  1.000 31.950 0  165 PHE A O   1 
ATOM   1299 C CB  . PHE A 1 165 ? -17.110 8.059   10.009 1.000 27.560 0  165 PHE A CB  1 
ATOM   1300 C CG  . PHE A 1 165 ? -17.262 8.580   8.612  1.000 27.890 0  165 PHE A CG  1 
ATOM   1301 C CD1 . PHE A 1 165 ? -18.457 8.430   7.929  1.000 28.250 0  165 PHE A CD1 1 
ATOM   1302 C CD2 . PHE A 1 165 ? -16.209 9.224   7.983  1.000 27.900 0  165 PHE A CD2 1 
ATOM   1303 C CE1 . PHE A 1 165 ? -18.601 8.913   6.642  1.000 28.690 0  165 PHE A CE1 1 
ATOM   1304 C CE2 . PHE A 1 165 ? -16.344 9.707   6.698  1.000 29.950 0  165 PHE A CE2 1 
ATOM   1305 C CZ  . PHE A 1 165 ? -17.541 9.550   6.025  1.000 31.900 0  165 PHE A CZ  1 
ATOM   1306 N N   . ALA A 1 166 ? -14.283 6.639   9.862  1.000 26.210 0  166 ALA A N   1 
ATOM   1307 C CA  . ALA A 1 166 ? -13.028 6.349   9.181  1.000 26.520 0  166 ALA A CA  1 
ATOM   1308 C C   . ALA A 1 166 ? -12.914 4.864   8.870  1.000 28.290 0  166 ALA A C   1 
ATOM   1309 O O   . ALA A 1 166 ? -12.524 4.482   7.759  1.000 31.470 0  166 ALA A O   1 
ATOM   1310 C CB  . ALA A 1 166 ? -11.841 6.810   10.026 1.000 26.010 0  166 ALA A CB  1 
ATOM   1311 N N   . PHE A 1 167 ? -13.274 4.013   9.835  1.000 27.570 0  167 PHE A N   1 
ATOM   1312 C CA  . PHE A 1 167 ? -13.181 2.576   9.601  1.000 28.470 0  167 PHE A CA  1 
ATOM   1313 C C   . PHE A 1 167 ? -14.140 2.135   8.501  1.000 32.680 0  167 PHE A C   1 
ATOM   1314 O O   . PHE A 1 167 ? -13.794 1.283   7.673  1.000 31.810 0  167 PHE A O   1 
ATOM   1315 C CB  . PHE A 1 167 ? -13.461 1.813   10.895 1.000 29.630 0  167 PHE A CB  1 
ATOM   1316 C CG  . PHE A 1 167 ? -12.221 1.401   11.630 1.000 31.830 0  167 PHE A CG  1 
ATOM   1317 C CD1 . PHE A 1 167 ? -11.511 0.275   11.244 1.000 30.280 0  167 PHE A CD1 1 
ATOM   1318 C CD2 . PHE A 1 167 ? -11.752 2.149   12.697 1.000 29.450 0  167 PHE A CD2 1 
ATOM   1319 C CE1 . PHE A 1 167 ? -10.367 -0.100  11.913 1.000 29.170 0  167 PHE A CE1 1 
ATOM   1320 C CE2 . PHE A 1 167 ? -10.604 1.778   13.369 1.000 28.950 0  167 PHE A CE2 1 
ATOM   1321 C CZ  . PHE A 1 167 ? -9.911  0.653   12.974 1.000 29.290 0  167 PHE A CZ  1 
ATOM   1322 N N   . ARG A 1 168 ? -15.333 2.731   8.451  1.000 28.280 0  168 ARG A N   1 
ATOM   1323 C CA  . ARG A 1 168 ? -16.287 2.340   7.419  1.000 28.990 0  168 ARG A CA  1 
ATOM   1324 C C   . ARG A 1 168 ? -15.799 2.750   6.035  1.000 32.120 0  168 ARG A C   1 
ATOM   1325 O O   . ARG A 1 168 ? -15.931 1.985   5.072  1.000 31.120 0  168 ARG A O   1 
ATOM   1326 C CB  . ARG A 1 168 ? -17.660 2.943   7.710  1.000 30.170 0  168 ARG A CB  1 
ATOM   1327 C CG  . ARG A 1 168 ? -18.415 2.203   8.796  1.000 28.260 0  168 ARG A CG  1 
ATOM   1328 C CD  . ARG A 1 168 ? -19.779 2.814   9.061  1.000 28.900 0  168 ARG A CD  1 
ATOM   1329 N NE  . ARG A 1 168 ? -20.241 2.521   10.411 1.000 28.750 0  168 ARG A NE  1 
ATOM   1330 C CZ  . ARG A 1 168 ? -20.604 1.319   10.839 1.000 31.960 0  168 ARG A CZ  1 
ATOM   1331 N NH1 . ARG A 1 168 ? -20.566 0.260   10.046 1.000 31.810 1  168 ARG A NH1 1 
ATOM   1332 N NH2 . ARG A 1 168 ? -21.007 1.173   12.099 1.000 31.560 0  168 ARG A NH2 1 
ATOM   1333 N N   . GLN A 1 169 ? -15.219 3.945   5.918  1.000 32.240 0  169 GLN A N   1 
ATOM   1334 C CA  . GLN A 1 169 ? -14.676 4.374   4.631  1.000 31.270 0  169 GLN A CA  1 
ATOM   1335 C C   . GLN A 1 169 ? -13.509 3.494   4.199  1.000 31.240 0  169 GLN A C   1 
ATOM   1336 O O   . GLN A 1 169 ? -13.410 3.111   3.022  1.000 32.970 0  169 GLN A O   1 
ATOM   1337 C CB  . GLN A 1 169 ? -14.255 5.839   4.702  1.000 29.610 0  169 GLN A CB  1 
ATOM   1338 C CG  . GLN A 1 169 ? -15.417 6.795   4.886  1.000 29.860 0  169 GLN A CG  1 
ATOM   1339 C CD  . GLN A 1 169 ? -16.378 6.773   3.713  1.000 30.690 0  169 GLN A CD  1 
ATOM   1340 O OE1 . GLN A 1 169 ? -15.991 6.473   2.584  1.000 31.470 0  169 GLN A OE1 1 
ATOM   1341 N NE2 . GLN A 1 169 ? -17.638 7.092   3.975  1.000 30.050 0  169 GLN A NE2 1 
ATOM   1342 N N   . ALA A 1 170 ? -12.603 3.179   5.129  1.000 28.820 0  170 ALA A N   1 
ATOM   1343 C CA  . ALA A 1 170 ? -11.494 2.289   4.804  1.000 29.450 0  170 ALA A CA  1 
ATOM   1344 C C   . ALA A 1 170 ? -12.001 0.928   4.343  1.000 31.660 0  170 ALA A C   1 
ATOM   1345 O O   . ALA A 1 170 ? -11.461 0.340   3.398  1.000 32.000 0  170 ALA A O   1 
ATOM   1346 C CB  . ALA A 1 170 ? -10.565 2.142   6.009  1.000 29.970 0  170 ALA A CB  1 
ATOM   1347 N N   . HIS A 1 171 ? -13.036 0.406   5.007  1.000 31.640 0  171 HIS A N   1 
ATOM   1348 C CA  . HIS A 1 171 ? -13.618 -0.866  4.591  1.000 32.360 0  171 HIS A CA  1 
ATOM   1349 C C   . HIS A 1 171 ? -14.259 -0.758  3.214  1.000 30.520 0  171 HIS A C   1 
ATOM   1350 O O   . HIS A 1 171 ? -14.212 -1.706  2.421  1.000 29.690 0  171 HIS A O   1 
ATOM   1351 C CB  . HIS A 1 171 ? -14.643 -1.328  5.627  1.000 30.420 0  171 HIS A CB  1 
ATOM   1352 C CG  . HIS A 1 171 ? -15.192 -2.697  5.372  1.000 31.260 0  171 HIS A CG  1 
ATOM   1353 N ND1 . HIS A 1 171 ? -14.390 -3.786  5.109  1.000 34.010 0  171 HIS A ND1 1 
ATOM   1354 C CD2 . HIS A 1 171 ? -16.467 -3.155  5.350  1.000 29.170 0  171 HIS A CD2 1 
ATOM   1355 C CE1 . HIS A 1 171 ? -15.146 -4.856  4.933  1.000 31.000 0  171 HIS A CE1 1 
ATOM   1356 N NE2 . HIS A 1 171 ? -16.410 -4.500  5.074  1.000 28.710 0  171 HIS A NE2 1 
ATOM   1357 N N   . GLU A 1 172 ? -14.864 0.391   2.913  1.000 30.290 0  172 GLU A N   1 
ATOM   1358 C CA  . GLU A 1 172 ? -15.539 0.547   1.632  1.000 31.290 0  172 GLU A CA  1 
ATOM   1359 C C   . GLU A 1 172 ? -14.548 0.613   0.477  1.000 31.910 0  172 GLU A C   1 
ATOM   1360 O O   . GLU A 1 172 ? -14.782 0.021   -0.582 1.000 31.690 0  172 GLU A O   1 
ATOM   1361 C CB  . GLU A 1 172 ? -16.411 1.801   1.649  1.000 31.830 0  172 GLU A CB  1 
ATOM   1362 C CG  . GLU A 1 172 ? -16.798 2.292   0.267  1.000 33.540 0  172 GLU A CG  1 
ATOM   1363 C CD  . GLU A 1 172 ? -18.149 2.967   0.250  1.000 35.720 0  172 GLU A CD  1 
ATOM   1364 O OE1 . GLU A 1 172 ? -18.207 4.188   0.508  1.000 36.390 0  172 GLU A OE1 1 
ATOM   1365 O OE2 . GLU A 1 172 ? -19.153 2.273   -0.015 1.000 39.990 -1 172 GLU A OE2 1 
ATOM   1366 N N   . HIS A 1 173 ? -13.428 1.309   0.665  1.000 31.960 0  173 HIS A N   1 
ATOM   1367 C CA  . HIS A 1 173 ? -12.477 1.511   -0.419 1.000 28.630 0  173 HIS A CA  1 
ATOM   1368 C C   . HIS A 1 173 ? -11.306 0.543   -0.372 1.000 29.340 0  173 HIS A C   1 
ATOM   1369 O O   . HIS A 1 173 ? -10.478 0.547   -1.287 1.000 29.790 0  173 HIS A O   1 
ATOM   1370 C CB  . HIS A 1 173 ? -11.970 2.955   -0.406 1.000 29.960 0  173 HIS A CB  1 
ATOM   1371 C CG  . HIS A 1 173 ? -13.066 3.970   -0.496 1.000 29.350 0  173 HIS A CG  1 
ATOM   1372 N ND1 . HIS A 1 173 ? -13.792 4.178   -1.648 1.000 31.320 0  173 HIS A ND1 1 
ATOM   1373 C CD2 . HIS A 1 173 ? -13.580 4.813   0.430  1.000 31.280 0  173 HIS A CD2 1 
ATOM   1374 C CE1 . HIS A 1 173 ? -14.697 5.116   -1.432 1.000 31.940 0  173 HIS A CE1 1 
ATOM   1375 N NE2 . HIS A 1 173 ? -14.590 5.518   -0.179 1.000 31.260 0  173 HIS A NE2 1 
ATOM   1376 N N   . ALA A 1 174 ? -11.220 -0.287  0.663  1.000 28.690 0  174 ALA A N   1 
ATOM   1377 C CA  . ALA A 1 174 ? -10.203 -1.334  0.756  1.000 30.310 0  174 ALA A CA  1 
ATOM   1378 C C   . ALA A 1 174 ? -10.860 -2.566  1.361  1.000 31.870 0  174 ALA A C   1 
ATOM   1379 O O   . ALA A 1 174 ? -10.566 -2.960  2.495  1.000 33.440 0  174 ALA A O   1 
ATOM   1380 C CB  . ALA A 1 174 ? -9.006  -0.869  1.586  1.000 29.040 0  174 ALA A CB  1 
ATOM   1381 N N   . PRO A 1 175 ? -11.760 -3.211  0.614  1.000 32.110 0  175 PRO A N   1 
ATOM   1382 C CA  . PRO A 1 175 ? -12.609 -4.246  1.222  1.000 30.600 0  175 PRO A CA  1 
ATOM   1383 C C   . PRO A 1 175 ? -11.862 -5.524  1.543  1.000 33.100 0  175 PRO A C   1 
ATOM   1384 O O   . PRO A 1 175 ? -12.364 -6.335  2.330  1.000 35.270 0  175 PRO A O   1 
ATOM   1385 C CB  . PRO A 1 175 ? -13.694 -4.485  0.160  1.000 33.240 0  175 PRO A CB  1 
ATOM   1386 C CG  . PRO A 1 175 ? -13.504 -3.387  -0.881 1.000 33.060 0  175 PRO A CG  1 
ATOM   1387 C CD  . PRO A 1 175 ? -12.061 -3.021  -0.814 1.000 31.490 0  175 PRO A CD  1 
ATOM   1388 N N   . LYS A 1 176 ? -10.680 -5.724  0.972  1.000 33.730 0  176 LYS A N   1 
ATOM   1389 C CA  . LYS A 1 176 ? -9.869  -6.899  1.248  1.000 30.640 0  176 LYS A CA  1 
ATOM   1390 C C   . LYS A 1 176 ? -8.832  -6.647  2.331  1.000 32.560 0  176 LYS A C   1 
ATOM   1391 O O   . LYS A 1 176 ? -8.049  -7.552  2.641  1.000 38.820 0  176 LYS A O   1 
ATOM   1392 C CB  . LYS A 1 176 ? -9.156  -7.363  -0.027 1.000 30.920 0  176 LYS A CB  1 
ATOM   1393 C CG  . LYS A 1 176 ? -10.075 -7.834  -1.139 1.000 34.440 0  176 LYS A CG  1 
ATOM   1394 C CD  . LYS A 1 176 ? -10.879 -9.054  -0.726 1.000 39.290 0  176 LYS A CD  1 
ATOM   1395 C CE  . LYS A 1 176 ? -12.373 -8.806  -0.862 1.000 36.620 0  176 LYS A CE  1 
ATOM   1396 N NZ  . LYS A 1 176 ? -13.154 -9.591  0.132  1.000 38.680 1  176 LYS A NZ  1 
ATOM   1397 N N   . ALA A 1 177 ? -8.814  -5.461  2.925  1.000 31.130 0  177 ALA A N   1 
ATOM   1398 C CA  . ALA A 1 177 ? -7.736  -5.073  3.818  1.000 29.600 0  177 ALA A CA  1 
ATOM   1399 C C   . ALA A 1 177 ? -8.130  -5.297  5.269  1.000 30.960 0  177 ALA A C   1 
ATOM   1400 O O   . ALA A 1 177 ? -9.269  -5.035  5.664  1.000 32.040 0  177 ALA A O   1 
ATOM   1401 C CB  . ALA A 1 177 ? -7.368  -3.601  3.608  1.000 28.290 0  177 ALA A CB  1 
ATOM   1402 N N   . GLN A 1 178 ? -7.175  -5.780  6.057  1.000 29.840 0  178 GLN A N   1 
ATOM   1403 C CA  . GLN A 1 178 ? -7.361  -5.864  7.497  1.000 28.970 0  178 GLN A CA  1 
ATOM   1404 C C   . GLN A 1 178 ? -7.271  -4.465  8.083  1.000 29.990 0  178 GLN A C   1 
ATOM   1405 O O   . GLN A 1 178 ? -6.247  -3.789  7.941  1.000 31.150 0  178 GLN A O   1 
ATOM   1406 C CB  . GLN A 1 178 ? -6.315  -6.784  8.120  1.000 28.250 0  178 GLN A CB  1 
ATOM   1407 C CG  . GLN A 1 178 ? -6.337  -6.818  9.642  1.000 27.050 0  178 GLN A CG  1 
ATOM   1408 C CD  . GLN A 1 178 ? -5.132  -7.538  10.222 1.000 29.180 0  178 GLN A CD  1 
ATOM   1409 O OE1 . GLN A 1 178 ? -3.991  -7.274  9.839  1.000 28.630 0  178 GLN A OE1 1 
ATOM   1410 N NE2 . GLN A 1 178 ? -5.380  -8.453  11.155 1.000 27.040 0  178 GLN A NE2 1 
ATOM   1411 N N   . LEU A 1 179 ? -8.333  -4.027  8.743  1.000 30.210 0  179 LEU A N   1 
ATOM   1412 C CA  . LEU A 1 179 ? -8.387  -2.694  9.319  1.000 29.390 0  179 LEU A CA  1 
ATOM   1413 C C   . LEU A 1 179 ? -7.983  -2.762  10.786 1.000 28.590 0  179 LEU A C   1 
ATOM   1414 O O   . LEU A 1 179 ? -8.519  -3.573  11.555 1.000 26.760 0  179 LEU A O   1 
ATOM   1415 C CB  . LEU A 1 179 ? -9.782  -2.091  9.151  1.000 32.940 0  179 LEU A CB  1 
ATOM   1416 C CG  . LEU A 1 179 ? -10.243 -1.997  7.691  1.000 31.820 0  179 LEU A CG  1 
ATOM   1417 C CD1 . LEU A 1 179 ? -11.445 -1.081  7.562  1.000 32.130 0  179 LEU A CD1 1 
ATOM   1418 C CD2 . LEU A 1 179 ? -9.112  -1.533  6.778  1.000 32.370 0  179 LEU A CD2 1 
ATOM   1419 N N   . VAL A 1 180 ? -7.022  -1.922  11.160 1.000 28.300 0  180 VAL A N   1 
ATOM   1420 C CA  . VAL A 1 180 ? -6.354  -2.005  12.448 1.000 27.530 0  180 VAL A CA  1 
ATOM   1421 C C   . VAL A 1 180 ? -6.451  -0.653  13.137 1.000 27.580 0  180 VAL A C   1 
ATOM   1422 O O   . VAL A 1 180 ? -6.321  0.396   12.493 1.000 28.310 0  180 VAL A O   1 
ATOM   1423 C CB  . VAL A 1 180 ? -4.878  -2.424  12.274 1.000 27.170 0  180 VAL A CB  1 
ATOM   1424 C CG1 . VAL A 1 180 ? -4.165  -2.477  13.614 1.000 26.520 0  180 VAL A CG1 1 
ATOM   1425 C CG2 . VAL A 1 180 ? -4.786  -3.761  11.553 1.000 27.700 0  180 VAL A CG2 1 
ATOM   1426 N N   . TYR A 1 181 ? -6.695  -0.681  14.444 1.000 26.210 0  181 TYR A N   1 
ATOM   1427 C CA  . TYR A 1 181 ? -6.477  0.482   15.295 1.000 25.440 0  181 TYR A CA  1 
ATOM   1428 C C   . TYR A 1 181 ? -5.121  0.327   15.967 1.000 25.380 0  181 TYR A C   1 
ATOM   1429 O O   . TYR A 1 181 ? -4.909  -0.629  16.714 1.000 25.980 0  181 TYR A O   1 
ATOM   1430 C CB  . TYR A 1 181 ? -7.573  0.636   16.345 1.000 25.310 0  181 TYR A CB  1 
ATOM   1431 C CG  . TYR A 1 181 ? -7.205  1.659   17.391 1.000 25.110 0  181 TYR A CG  1 
ATOM   1432 C CD1 . TYR A 1 181 ? -7.037  2.994   17.047 1.000 25.050 0  181 TYR A CD1 1 
ATOM   1433 C CD2 . TYR A 1 181 ? -6.990  1.290   18.713 1.000 25.000 0  181 TYR A CD2 1 
ATOM   1434 C CE1 . TYR A 1 181 ? -6.685  3.937   17.991 1.000 25.020 0  181 TYR A CE1 1 
ATOM   1435 C CE2 . TYR A 1 181 ? -6.637  2.227   19.667 1.000 24.840 0  181 TYR A CE2 1 
ATOM   1436 C CZ  . TYR A 1 181 ? -6.486  3.549   19.301 1.000 25.190 0  181 TYR A CZ  1 
ATOM   1437 O OH  . TYR A 1 181 ? -6.135  4.490   20.243 1.000 25.250 0  181 TYR A OH  1 
ATOM   1438 N N   . ASN A 1 182 ? -4.217  1.272   15.722 1.000 25.340 0  182 ASN A N   1 
ATOM   1439 C CA  . ASN A 1 182 ? -2.815  1.156   16.109 1.000 25.330 0  182 ASN A CA  1 
ATOM   1440 C C   . ASN A 1 182 ? -2.491  2.132   17.230 1.000 25.270 0  182 ASN A C   1 
ATOM   1441 O O   . ASN A 1 182 ? -2.774  3.330   17.114 1.000 25.030 0  182 ASN A O   1 
ATOM   1442 C CB  . ASN A 1 182 ? -1.908  1.428   14.904 1.000 25.490 0  182 ASN A CB  1 
ATOM   1443 C CG  . ASN A 1 182 ? -0.441  1.221   15.218 1.000 25.530 0  182 ASN A CG  1 
ATOM   1444 O OD1 . ASN A 1 182 ? -0.024  0.123   15.580 1.000 26.400 0  182 ASN A OD1 1 
ATOM   1445 N ND2 . ASN A 1 182 ? 0.355   2.280   15.073 1.000 25.500 0  182 ASN A ND2 1 
ATOM   1446 N N   . ASP A 1 183 ? -1.886  1.627   18.306 1.000 25.060 0  183 ASP A N   1 
ATOM   1447 C CA  . ASP A 1 183 ? -1.568  2.491   19.440 1.000 26.050 0  183 ASP A CA  1 
ATOM   1448 C C   . ASP A 1 183 ? -0.587  1.765   20.356 1.000 25.230 0  183 ASP A C   1 
ATOM   1449 O O   . ASP A 1 183 ? -0.423  0.545   20.271 1.000 25.020 0  183 ASP A O   1 
ATOM   1450 C CB  . ASP A 1 183 ? -2.844  2.909   20.185 1.000 24.740 0  183 ASP A CB  1 
ATOM   1451 C CG  . ASP A 1 183 ? -2.621  4.054   21.155 1.000 24.570 0  183 ASP A CG  1 
ATOM   1452 O OD1 . ASP A 1 183 ? -1.476  4.256   21.606 1.000 24.540 0  183 ASP A OD1 1 
ATOM   1453 O OD2 . ASP A 1 183 ? -3.606  4.751   21.472 1.000 24.490 -1 183 ASP A OD2 1 
ATOM   1454 N N   . PHE A 1 184 ? 0.071   2.535   21.228 1.000 24.770 0  184 PHE A N   1 
ATOM   1455 C CA  . PHE A 1 184 ? 1.210   2.038   21.994 1.000 24.800 0  184 PHE A CA  1 
ATOM   1456 C C   . PHE A 1 184 ? 0.868   1.695   23.445 1.000 25.020 0  184 PHE A C   1 
ATOM   1457 O O   . PHE A 1 184 ? 1.762   1.700   24.299 1.000 24.710 0  184 PHE A O   1 
ATOM   1458 C CB  . PHE A 1 184 ? 2.362   3.047   21.954 1.000 24.780 0  184 PHE A CB  1 
ATOM   1459 C CG  . PHE A 1 184 ? 1.998   4.424   22.445 1.000 24.590 0  184 PHE A CG  1 
ATOM   1460 C CD1 . PHE A 1 184 ? 2.014   4.722   23.799 1.000 24.470 0  184 PHE A CD1 1 
ATOM   1461 C CD2 . PHE A 1 184 ? 1.673   5.431   21.547 1.000 24.570 0  184 PHE A CD2 1 
ATOM   1462 C CE1 . PHE A 1 184 ? 1.690   5.986   24.249 1.000 24.330 0  184 PHE A CE1 1 
ATOM   1463 C CE2 . PHE A 1 184 ? 1.351   6.700   21.992 1.000 24.430 0  184 PHE A CE2 1 
ATOM   1464 C CZ  . PHE A 1 184 ? 1.359   6.977   23.344 1.000 24.300 0  184 PHE A CZ  1 
ATOM   1465 N N   . MET A 1 185 ? -0.393  1.388   23.748 1.000 25.000 0  185 MET A N   1 
ATOM   1466 C CA  . MET A 1 185 ? -0.727  0.932   25.091 1.000 26.010 0  185 MET A CA  1 
ATOM   1467 C C   . MET A 1 185 ? 0.013   -0.367  25.391 1.000 26.540 0  185 MET A C   1 
ATOM   1468 O O   . MET A 1 185 ? 0.354   -1.135  24.487 1.000 24.930 0  185 MET A O   1 
ATOM   1469 C CB  . MET A 1 185 ? -2.237  0.730   25.243 1.000 24.610 0  185 MET A CB  1 
ATOM   1470 C CG  . MET A 1 185 ? -2.733  -0.633  24.783 1.000 26.510 0  185 MET A CG  1 
ATOM   1471 S SD  . MET A 1 185 ? -2.861  -0.759  22.991 1.000 33.570 0  185 MET A SD  1 
ATOM   1472 C CE  . MET A 1 185 ? -3.500  0.851   22.646 1.000 26.470 0  185 MET A CE  1 
ATOM   1473 N N   . GLY A 1 186 ? 0.297   -0.592  26.673 1.000 27.470 0  186 GLY A N   1 
ATOM   1474 C CA  . GLY A 1 186 ? 1.035   -1.763  27.083 1.000 27.510 0  186 GLY A CA  1 
ATOM   1475 C C   . GLY A 1 186 ? 0.955   -2.050  28.568 1.000 29.310 0  186 GLY A C   1 
ATOM   1476 O O   . GLY A 1 186 ? 0.189   -1.428  29.311 1.000 30.500 0  186 GLY A O   1 
ATOM   1477 N N   . PRO A 1 187 ? 1.766   -3.001  29.030 1.000 29.120 0  187 PRO A N   1 
ATOM   1478 C CA  . PRO A 1 187 ? 1.731   -3.379  30.448 1.000 30.900 0  187 PRO A CA  1 
ATOM   1479 C C   . PRO A 1 187 ? 2.197   -2.246  31.350 1.000 33.000 0  187 PRO A C   1 
ATOM   1480 O O   . PRO A 1 187 ? 3.127   -1.505  31.020 1.000 33.630 0  187 PRO A O   1 
ATOM   1481 C CB  . PRO A 1 187 ? 2.687   -4.575  30.520 1.000 30.590 0  187 PRO A CB  1 
ATOM   1482 C CG  . PRO A 1 187 ? 2.786   -5.074  29.108 1.000 32.700 0  187 PRO A CG  1 
ATOM   1483 C CD  . PRO A 1 187 ? 2.676   -3.854  28.253 1.000 29.420 0  187 PRO A CD  1 
ATOM   1484 N N   . GLY A 1 188 ? 1.539   -2.120  32.493 1.000 32.200 0  188 GLY A N   1 
ATOM   1485 C CA  . GLY A 1 188 ? 1.849   -1.060  33.432 1.000 32.800 0  188 GLY A CA  1 
ATOM   1486 C C   . GLY A 1 188 ? 0.684   -0.793  34.354 1.000 30.100 0  188 GLY A C   1 
ATOM   1487 O O   . GLY A 1 188 ? -0.427  -1.279  34.156 1.000 30.760 0  188 GLY A O   1 
ATOM   1488 N N   . LEU A 1 189 ? 0.941   -0.082  35.460 1.000 32.110 0  189 LEU A N   1 
ATOM   1489 C CA  . LEU A 1 189 ? -0.077  0.045   36.537 1.000 31.430 0  189 LEU A CA  1 
ATOM   1490 C C   . LEU A 1 189 ? -0.773  1.408   36.611 1.000 34.660 0  189 LEU A C   1 
ATOM   1491 O O   . LEU A 1 189 ? -1.903  1.445   37.132 1.000 34.650 0  189 LEU A O   1 
ATOM   1492 C CB  . LEU A 1 189 ? 0.596   -0.251  37.877 1.000 28.430 0  189 LEU A CB  1 
ATOM   1493 C CG  . LEU A 1 189 ? 1.198   -1.643  38.062 1.000 32.010 0  189 LEU A CG  1 
ATOM   1494 C CD1 . LEU A 1 189 ? 2.678   -1.509  38.365 1.000 29.480 0  189 LEU A CD1 1 
ATOM   1495 C CD2 . LEU A 1 189 ? 0.485   -2.309  39.217 1.000 30.570 0  189 LEU A CD2 1 
ATOM   1496 N N   . GLY A 1 190 ? -0.140  2.482   36.162 1.000 32.490 0  190 GLY A N   1 
ATOM   1497 C CA  . GLY A 1 190 ? -0.776  3.790   36.363 1.000 31.830 0  190 GLY A CA  1 
ATOM   1498 C C   . GLY A 1 190 ? -1.470  4.296   35.135 1.000 29.200 0  190 GLY A C   1 
ATOM   1499 O O   . GLY A 1 190 ? -2.576  3.835   34.842 1.000 32.800 0  190 GLY A O   1 
ATOM   1500 N N   . ASP A 1 191 ? -0.869  5.269   34.485 1.000 30.380 0  191 ASP A N   1 
ATOM   1501 C CA  . ASP A 1 191 ? -1.446  5.844   33.248 1.000 31.660 0  191 ASP A CA  1 
ATOM   1502 C C   . ASP A 1 191 ? -1.375  4.775   32.156 1.000 31.330 0  191 ASP A C   1 
ATOM   1503 O O   . ASP A 1 191 ? -2.144  4.879   31.196 1.000 30.400 0  191 ASP A O   1 
ATOM   1504 C CB  . ASP A 1 191 ? -0.802  7.189   32.955 1.000 31.730 0  191 ASP A CB  1 
ATOM   1505 C CG  . ASP A 1 191 ? -0.853  8.204   34.082 1.000 33.940 0  191 ASP A CG  1 
ATOM   1506 O OD1 . ASP A 1 191 ? -1.589  7.960   35.054 1.000 35.160 0  191 ASP A OD1 1 
ATOM   1507 O OD2 . ASP A 1 191 ? -0.162  9.231   33.968 1.000 38.040 -1 191 ASP A OD2 1 
ATOM   1508 N N   . ARG A 1 192 ? -0.468  3.802   32.284 1.000 29.730 0  192 ARG A N   1 
ATOM   1509 C CA  . ARG A 1 192 ? -0.520  2.706   31.321 1.000 30.280 0  192 ARG A CA  1 
ATOM   1510 C C   . ARG A 1 192 ? -1.838  1.949   31.434 1.000 29.820 0  192 ARG A C   1 
ATOM   1511 O O   . ARG A 1 192 ? -2.446  1.581   30.419 1.000 32.870 0  192 ARG A O   1 
ATOM   1512 C CB  . ARG A 1 192 ? 0.664   1.761   31.528 1.000 30.750 0  192 ARG A CB  1 
ATOM   1513 C CG  . ARG A 1 192 ? 2.036   2.434   31.579 1.000 30.210 0  192 ARG A CG  1 
ATOM   1514 C CD  . ARG A 1 192 ? 2.563   2.782   30.187 1.000 32.360 0  192 ARG A CD  1 
ATOM   1515 N NE  . ARG A 1 192 ? 3.266   1.666   29.558 1.000 34.360 0  192 ARG A NE  1 
ATOM   1516 C CZ  . ARG A 1 192 ? 3.213   1.375   28.263 1.000 32.020 0  192 ARG A CZ  1 
ATOM   1517 N NH1 . ARG A 1 192 ? 2.518   2.115   27.414 1.000 29.500 1  192 ARG A NH1 1 
ATOM   1518 N NH2 . ARG A 1 192 ? 3.880   0.318   27.806 1.000 30.450 0  192 ARG A NH2 1 
ATOM   1519 N N   . ALA A 1 193 ? -2.309  1.733   32.666 1.000 27.440 0  193 ALA A N   1 
ATOM   1520 C CA  . ALA A 1 193 ? -3.584  1.051   32.869 1.000 27.980 0  193 ALA A CA  1 
ATOM   1521 C C   . ALA A 1 193 ? -4.753  1.897   32.379 1.000 26.710 0  193 ALA A C   1 
ATOM   1522 O O   . ALA A 1 193 ? -5.714  1.366   31.810 1.000 26.760 0  193 ALA A O   1 
ATOM   1523 C CB  . ALA A 1 193 ? -3.761  0.692   34.344 1.000 29.120 0  193 ALA A CB  1 
ATOM   1524 N N   . LYS A 1 194 ? -4.696  3.212   32.592 1.000 27.760 0  194 LYS A N   1 
ATOM   1525 C CA  . LYS A 1 194 ? -5.766  4.073   32.102 1.000 28.950 0  194 LYS A CA  1 
ATOM   1526 C C   . LYS A 1 194 ? -5.794  4.087   30.579 1.000 28.720 0  194 LYS A C   1 
ATOM   1527 O O   . LYS A 1 194 ? -6.870  4.106   29.970 1.000 29.510 0  194 LYS A O   1 
ATOM   1528 C CB  . LYS A 1 194 ? -5.598  5.489   32.652 1.000 29.250 0  194 LYS A CB  1 
ATOM   1529 C CG  . LYS A 1 194 ? -5.855  5.620   34.146 1.000 27.270 0  194 LYS A CG  1 
ATOM   1530 C CD  . LYS A 1 194 ? -5.595  7.045   34.603 1.000 30.050 0  194 LYS A CD  1 
ATOM   1531 C CE  . LYS A 1 194 ? -6.266  7.346   35.934 1.000 33.200 0  194 LYS A CE  1 
ATOM   1532 N NZ  . LYS A 1 194 ? -5.500  6.813   37.096 1.000 30.130 1  194 LYS A NZ  1 
ATOM   1533 N N   . HIS A 1 195 ? -4.617  4.070   29.952 1.000 27.590 0  195 HIS A N   1 
ATOM   1534 C CA  . HIS A 1 195 ? -4.541  3.964   28.501 1.000 28.120 0  195 HIS A CA  1 
ATOM   1535 C C   . HIS A 1 195 ? -5.174  2.664   28.017 1.000 28.550 0  195 HIS A C   1 
ATOM   1536 O O   . HIS A 1 195 ? -5.984  2.662   27.081 1.000 28.670 0  195 HIS A O   1 
ATOM   1537 C CB  . HIS A 1 195 ? -3.079  4.055   28.058 1.000 26.300 0  195 HIS A CB  1 
ATOM   1538 C CG  . HIS A 1 195 ? -2.904  4.329   26.598 1.000 24.710 0  195 HIS A CG  1 
ATOM   1539 N ND1 . HIS A 1 195 ? -1.672  4.568   26.030 1.000 24.840 0  195 HIS A ND1 1 
ATOM   1540 C CD2 . HIS A 1 195 ? -3.804  4.404   25.589 1.000 25.520 0  195 HIS A CD2 1 
ATOM   1541 C CE1 . HIS A 1 195 ? -1.820  4.778   24.734 1.000 24.290 0  195 HIS A CE1 1 
ATOM   1542 N NE2 . HIS A 1 195 ? -3.104  4.682   24.441 1.000 24.300 0  195 HIS A NE2 1 
ATOM   1543 N N   . ARG A 1 196 ? -4.815  1.544   28.654 1.000 26.480 0  196 ARG A N   1 
ATOM   1544 C CA  . ARG A 1 196 ? -5.396  0.258   28.277 1.000 26.990 0  196 ARG A CA  1 
ATOM   1545 C C   . ARG A 1 196 ? -6.910  0.260   28.434 1.000 27.440 0  196 ARG A C   1 
ATOM   1546 O O   . ARG A 1 196 ? -7.629  -0.274  27.583 1.000 29.500 0  196 ARG A O   1 
ATOM   1547 C CB  . ARG A 1 196 ? -4.794  -0.864  29.117 1.000 28.130 0  196 ARG A CB  1 
ATOM   1548 C CG  . ARG A 1 196 ? -3.346  -1.184  28.826 1.000 29.460 0  196 ARG A CG  1 
ATOM   1549 C CD  . ARG A 1 196 ? -3.040  -2.590  29.300 1.000 30.030 0  196 ARG A CD  1 
ATOM   1550 N NE  . ARG A 1 196 ? -3.431  -2.775  30.692 1.000 29.560 0  196 ARG A NE  1 
ATOM   1551 C CZ  . ARG A 1 196 ? -2.656  -2.492  31.729 1.000 29.880 0  196 ARG A CZ  1 
ATOM   1552 N NH1 . ARG A 1 196 ? -1.426  -2.037  31.566 1.000 33.760 1  196 ARG A NH1 1 
ATOM   1553 N NH2 . ARG A 1 196 ? -3.127  -2.672  32.961 1.000 29.640 0  196 ARG A NH2 1 
ATOM   1554 N N   . ALA A 1 197 ? -7.415  0.847   29.522 1.000 28.310 0  197 ALA A N   1 
ATOM   1555 C CA  . ALA A 1 197 ? -8.856  0.848   29.755 1.000 28.180 0  197 ALA A CA  1 
ATOM   1556 C C   . ALA A 1 197 ? -9.581  1.708   28.728 1.000 27.610 0  197 ALA A C   1 
ATOM   1557 O O   . ALA A 1 197 ? -10.631 1.309   28.210 1.000 29.840 0  197 ALA A O   1 
ATOM   1558 C CB  . ALA A 1 197 ? -9.167  1.321   31.173 1.000 24.600 0  197 ALA A CB  1 
ATOM   1559 N N   . GLY A 1 198 ? -9.046  2.893   28.423 1.000 27.160 0  198 GLY A N   1 
ATOM   1560 C CA  . GLY A 1 198 ? -9.674  3.727   27.409 1.000 28.880 0  198 GLY A CA  1 
ATOM   1561 C C   . GLY A 1 198 ? -9.670  3.071   26.042 1.000 28.680 0  198 GLY A C   1 
ATOM   1562 O O   . GLY A 1 198 ? -10.638 3.181   25.283 1.000 30.040 0  198 GLY A O   1 
ATOM   1563 N N   . VAL A 1 199 ? -8.593  2.350   25.723 1.000 28.540 0  199 VAL A N   1 
ATOM   1564 C CA  . VAL A 1 199 ? -8.524  1.657   24.441 1.000 29.390 0  199 VAL A CA  1 
ATOM   1565 C C   . VAL A 1 199 ? -9.514  0.500   24.402 1.000 32.090 0  199 VAL A C   1 
ATOM   1566 O O   . VAL A 1 199 ? -10.164 0.254   23.376 1.000 31.390 0  199 VAL A O   1 
ATOM   1567 C CB  . VAL A 1 199 ? -7.082  1.193   24.176 1.000 26.660 0  199 VAL A CB  1 
ATOM   1568 C CG1 . VAL A 1 199 ? -7.029  0.267   22.976 1.000 26.210 0  199 VAL A CG1 1 
ATOM   1569 C CG2 . VAL A 1 199 ? -6.202  2.410   23.962 1.000 25.720 0  199 VAL A CG2 1 
ATOM   1570 N N   . LEU A 1 200 ? -9.630  -0.243  25.509 1.000 30.900 0  200 LEU A N   1 
ATOM   1571 C CA  . LEU A 1 200 ? -10.660 -1.270  25.608 1.000 29.490 0  200 LEU A CA  1 
ATOM   1572 C C   . LEU A 1 200 ? -12.045 -0.680  25.395 1.000 30.560 0  200 LEU A C   1 
ATOM   1573 O O   . LEU A 1 200 ? -12.884 -1.280  24.716 1.000 32.980 0  200 LEU A O   1 
ATOM   1574 C CB  . LEU A 1 200 ? -10.581 -1.971  26.963 1.000 31.170 0  200 LEU A CB  1 
ATOM   1575 C CG  . LEU A 1 200 ? -9.685  -3.207  27.012 1.000 33.810 0  200 LEU A CG  1 
ATOM   1576 C CD1 . LEU A 1 200 ? -10.015 -4.067  28.220 1.000 34.110 0  200 LEU A CD1 1 
ATOM   1577 C CD2 . LEU A 1 200 ? -9.815  -4.007  25.723 1.000 35.820 0  200 LEU A CD2 1 
ATOM   1578 N N   . LYS A 1 201 ? -12.308 0.489   25.980 1.000 30.430 0  201 LYS A N   1 
ATOM   1579 C CA  . LYS A 1 201 ? -13.606 1.133   25.798 1.000 30.190 0  201 LYS A CA  1 
ATOM   1580 C C   . LYS A 1 201 ? -13.845 1.481   24.335 1.000 31.600 0  201 LYS A C   1 
ATOM   1581 O O   . LYS A 1 201 ? -14.940 1.260   23.800 1.000 33.060 0  201 LYS A O   1 
ATOM   1582 C CB  . LYS A 1 201 ? -13.700 2.386   26.663 1.000 29.170 0  201 LYS A CB  1 
ATOM   1583 C CG  . LYS A 1 201 ? -15.126 2.801   26.959 1.000 31.790 0  201 LYS A CG  1 
ATOM   1584 C CD  . LYS A 1 201 ? -15.217 4.300   27.169 1.000 33.310 0  201 LYS A CD  1 
ATOM   1585 C CE  . LYS A 1 201 ? -15.380 4.638   28.636 1.000 30.070 0  201 LYS A CE  1 
ATOM   1586 N NZ  . LYS A 1 201 ? -14.818 5.982   28.940 1.000 40.960 1  201 LYS A NZ  1 
ATOM   1587 N N   . LEU A 1 202 ? -12.834 2.051   23.675 1.000 29.720 0  202 LEU A N   1 
ATOM   1588 C CA  . LEU A 1 202 ? -12.992 2.407   22.269 1.000 28.180 0  202 LEU A CA  1 
ATOM   1589 C C   . LEU A 1 202 ? -13.281 1.171   21.427 1.000 27.960 0  202 LEU A C   1 
ATOM   1590 O O   . LEU A 1 202 ? -14.188 1.181   20.587 1.000 27.660 0  202 LEU A O   1 
ATOM   1591 C CB  . LEU A 1 202 ? -11.743 3.127   21.756 1.000 25.160 0  202 LEU A CB  1 
ATOM   1592 C CG  . LEU A 1 202 ? -11.809 3.613   20.303 1.000 25.910 0  202 LEU A CG  1 
ATOM   1593 C CD1 . LEU A 1 202 ? -12.822 4.732   20.165 1.000 24.920 0  202 LEU A CD1 1 
ATOM   1594 C CD2 . LEU A 1 202 ? -10.444 4.066   19.799 1.000 24.830 0  202 LEU A CD2 1 
ATOM   1595 N N   . LEU A 1 203 ? -12.538 0.086   21.661 1.000 29.820 0  203 LEU A N   1 
ATOM   1596 C CA  . LEU A 1 203 ? -12.742 -1.137  20.889 1.000 28.260 0  203 LEU A CA  1 
ATOM   1597 C C   . LEU A 1 203 ? -14.112 -1.744  21.161 1.000 31.640 0  203 LEU A C   1 
ATOM   1598 O O   . LEU A 1 203 ? -14.780 -2.229  20.237 1.000 33.130 0  203 LEU A O   1 
ATOM   1599 C CB  . LEU A 1 203 ? -11.635 -2.139  21.208 1.000 27.710 0  203 LEU A CB  1 
ATOM   1600 C CG  . LEU A 1 203 ? -10.247 -1.699  20.754 1.000 26.250 0  203 LEU A CG  1 
ATOM   1601 C CD1 . LEU A 1 203 ? -9.198  -2.706  21.184 1.000 27.770 0  203 LEU A CD1 1 
ATOM   1602 C CD2 . LEU A 1 203 ? -10.231 -1.510  19.251 1.000 27.500 0  203 LEU A CD2 1 
ATOM   1603 N N   . ALA A 1 204 ? -14.542 -1.735  22.425 1.000 32.910 0  204 ALA A N   1 
ATOM   1604 C CA  . ALA A 1 204 ? -15.849 -2.272  22.781 1.000 32.240 0  204 ALA A CA  1 
ATOM   1605 C C   . ALA A 1 204 ? -16.964 -1.504  22.087 1.000 29.890 0  204 ALA A C   1 
ATOM   1606 O O   . ALA A 1 204 ? -17.871 -2.104  21.499 1.000 32.980 0  204 ALA A O   1 
ATOM   1607 C CB  . ALA A 1 204 ? -16.030 -2.240  24.299 1.000 31.730 0  204 ALA A CB  1 
ATOM   1608 N N   . GLU A 1 205 ? -16.908 -0.171  22.134 1.000 28.530 0  205 GLU A N   1 
ATOM   1609 C CA  . GLU A 1 205 ? -17.943 0.629   21.483 1.000 30.520 0  205 GLU A CA  1 
ATOM   1610 C C   . GLU A 1 205 ? -17.902 0.459   19.966 1.000 29.900 0  205 GLU A C   1 
ATOM   1611 O O   . GLU A 1 205 ? -18.951 0.439   19.306 1.000 31.100 0  205 GLU A O   1 
ATOM   1612 C CB  . GLU A 1 205 ? -17.792 2.101   21.872 1.000 28.080 0  205 GLU A CB  1 
ATOM   1613 C CG  . GLU A 1 205 ? -18.748 3.042   21.156 1.000 29.310 0  205 GLU A CG  1 
ATOM   1614 C CD  . GLU A 1 205 ? -20.150 3.048   21.750 1.000 30.070 0  205 GLU A CD  1 
ATOM   1615 O OE1 . GLU A 1 205 ? -20.347 2.469   22.840 1.000 32.110 0  205 GLU A OE1 1 
ATOM   1616 O OE2 . GLU A 1 205 ? -21.057 3.634   21.122 1.000 27.660 -1 205 GLU A OE2 1 
ATOM   1617 N N   . LEU A 1 206 ? -16.701 0.314   19.398 1.000 29.120 0  206 LEU A N   1 
ATOM   1618 C CA  . LEU A 1 206 ? -16.586 0.145   17.954 1.000 29.980 0  206 LEU A CA  1 
ATOM   1619 C C   . LEU A 1 206 ? -17.201 -1.173  17.498 1.000 32.570 0  206 LEU A C   1 
ATOM   1620 O O   . LEU A 1 206 ? -17.923 -1.211  16.494 1.000 32.250 0  206 LEU A O   1 
ATOM   1621 C CB  . LEU A 1 206 ? -15.122 0.233   17.531 1.000 28.480 0  206 LEU A CB  1 
ATOM   1622 C CG  . LEU A 1 206 ? -14.560 1.651   17.417 1.000 25.520 0  206 LEU A CG  1 
ATOM   1623 C CD1 . LEU A 1 206 ? -13.100 1.615   17.007 1.000 26.120 0  206 LEU A CD1 1 
ATOM   1624 C CD2 . LEU A 1 206 ? -15.381 2.476   16.439 1.000 25.570 0  206 LEU A CD2 1 
ATOM   1625 N N   . LYS A 1 207 ? -16.928 -2.267  18.218 1.000 31.380 0  207 LYS A N   1 
ATOM   1626 C CA  . LYS A 1 207 ? -17.579 -3.530  17.879 1.000 31.550 0  207 LYS A CA  1 
ATOM   1627 C C   . LYS A 1 207 ? -19.077 -3.479  18.162 1.000 34.190 0  207 LYS A C   1 
ATOM   1628 O O   . LYS A 1 207 ? -19.861 -4.124  17.454 1.000 33.890 0  207 LYS A O   1 
ATOM   1629 C CB  . LYS A 1 207 ? -16.932 -4.696  18.631 1.000 32.420 0  207 LYS A CB  1 
ATOM   1630 C CG  . LYS A 1 207 ? -15.511 -5.022  18.180 1.000 34.040 0  207 LYS A CG  1 
ATOM   1631 C CD  . LYS A 1 207 ? -15.474 -5.666  16.796 1.000 35.820 0  207 LYS A CD  1 
ATOM   1632 C CE  . LYS A 1 207 ? -16.392 -6.874  16.691 1.000 37.840 0  207 LYS A CE  1 
ATOM   1633 N NZ  . LYS A 1 207 ? -16.038 -7.728  15.516 1.000 37.010 1  207 LYS A NZ  1 
ATOM   1634 N N   . LYS A 1 208 ? -19.492 -2.730  19.189 1.000 35.020 0  208 LYS A N   1 
ATOM   1635 C CA  . LYS A 1 208 ? -20.911 -2.636  19.515 1.000 33.360 0  208 LYS A CA  1 
ATOM   1636 C C   . LYS A 1 208 ? -21.689 -1.947  18.401 1.000 33.550 0  208 LYS A C   1 
ATOM   1637 O O   . LYS A 1 208 ? -22.817 -2.346  18.088 1.000 36.850 0  208 LYS A O   1 
ATOM   1638 C CB  . LYS A 1 208 ? -21.095 -1.892  20.837 1.000 31.330 0  208 LYS A CB  1 
ATOM   1639 C CG  . LYS A 1 208 ? -21.388 -2.798  22.025 1.000 36.670 0  208 LYS A CG  1 
ATOM   1640 C CD  . LYS A 1 208 ? -21.007 -2.144  23.354 1.000 33.170 0  208 LYS A CD  1 
ATOM   1641 C CE  . LYS A 1 208 ? -21.210 -0.634  23.326 1.000 34.080 0  208 LYS A CE  1 
ATOM   1642 N NZ  . LYS A 1 208 ? -20.759 0.017   24.588 1.000 35.280 1  208 LYS A NZ  1 
ATOM   1643 N N   . ARG A 1 209 ? -21.106 -0.919  17.787 1.000 31.900 0  209 ARG A N   1 
ATOM   1644 C CA  . ARG A 1 209 ? -21.816 -0.180  16.747 1.000 32.720 0  209 ARG A CA  1 
ATOM   1645 C C   . ARG A 1 209 ? -21.816 -0.883  15.395 1.000 32.970 0  209 ARG A C   1 
ATOM   1646 O O   . ARG A 1 209 ? -22.429 -0.371  14.454 1.000 33.140 0  209 ARG A O   1 
ATOM   1647 C CB  . ARG A 1 209 ? -21.216 1.219   16.589 1.000 32.960 0  209 ARG A CB  1 
ATOM   1648 C CG  . ARG A 1 209 ? -21.332 2.081   17.829 1.000 29.850 0  209 ARG A CG  1 
ATOM   1649 C CD  . ARG A 1 209 ? -20.572 3.379   17.663 1.000 27.260 0  209 ARG A CD  1 
ATOM   1650 N NE  . ARG A 1 209 ? -20.866 4.309   18.745 1.000 28.380 0  209 ARG A NE  1 
ATOM   1651 C CZ  . ARG A 1 209 ? -21.229 5.571   18.570 1.000 27.750 0  209 ARG A CZ  1 
ATOM   1652 N NH1 . ARG A 1 209 ? -21.339 6.097   17.361 1.000 28.620 1  209 ARG A NH1 1 
ATOM   1653 N NH2 . ARG A 1 209 ? -21.481 6.328   19.635 1.000 26.110 0  209 ARG A NH2 1 
ATOM   1654 N N   . GLY A 1 210 ? -21.153 -2.032  15.269 1.000 35.100 0  210 GLY A N   1 
ATOM   1655 C CA  . GLY A 1 210 ? -21.057 -2.692  13.981 1.000 34.910 0  210 GLY A CA  1 
ATOM   1656 C C   . GLY A 1 210 ? -19.952 -2.185  13.082 1.000 32.090 0  210 GLY A C   1 
ATOM   1657 O O   . GLY A 1 210 ? -19.974 -2.462  11.879 1.000 31.650 0  210 GLY A O   1 
ATOM   1658 N N   . ALA A 1 211 ? -18.988 -1.445  13.628 1.000 30.600 0  211 ALA A N   1 
ATOM   1659 C CA  . ALA A 1 211 ? -17.933 -0.862  12.811 1.000 30.910 0  211 ALA A CA  1 
ATOM   1660 C C   . ALA A 1 211 ? -16.965 -1.944  12.336 1.000 28.730 0  211 ALA A C   1 
ATOM   1661 O O   . ALA A 1 211 ? -16.620 -2.851  13.099 1.000 26.400 0  211 ALA A O   1 
ATOM   1662 C CB  . ALA A 1 211 ? -17.178 0.207   13.598 1.000 28.210 0  211 ALA A CB  1 
ATOM   1663 N N   . PRO A 1 212 ? -16.496 -1.867  11.087 1.000 28.890 0  212 PRO A N   1 
ATOM   1664 C CA  . PRO A 1 212 ? -15.602 -2.905  10.530 1.000 28.930 0  212 PRO A CA  1 
ATOM   1665 C C   . PRO A 1 212 ? -14.143 -2.727  10.934 1.000 28.750 0  212 PRO A C   1 
ATOM   1666 O O   . PRO A 1 212 ? -13.262 -2.411  10.127 1.000 28.440 0  212 PRO A O   1 
ATOM   1667 C CB  . PRO A 1 212 ? -15.810 -2.729  9.023  1.000 28.810 0  212 PRO A CB  1 
ATOM   1668 C CG  . PRO A 1 212 ? -16.049 -1.266  8.878  1.000 27.630 0  212 PRO A CG  1 
ATOM   1669 C CD  . PRO A 1 212 ? -16.884 -0.876  10.068 1.000 29.340 0  212 PRO A CD  1 
ATOM   1670 N N   . ILE A 1 213 ? -13.862 -2.935  12.219 1.000 27.810 0  213 ILE A N   1 
ATOM   1671 C CA  . ILE A 1 213 ? -12.494 -2.995  12.723 1.000 29.170 0  213 ILE A CA  1 
ATOM   1672 C C   . ILE A 1 213 ? -12.103 -4.457  12.864 1.000 28.310 0  213 ILE A C   1 
ATOM   1673 O O   . ILE A 1 213 ? -12.844 -5.252  13.455 1.000 29.500 0  213 ILE A O   1 
ATOM   1674 C CB  . ILE A 1 213 ? -12.348 -2.249  14.061 1.000 26.010 0  213 ILE A CB  1 
ATOM   1675 C CG1 . ILE A 1 213 ? -10.990 -2.563  14.694 1.000 26.430 0  213 ILE A CG1 1 
ATOM   1676 C CG2 . ILE A 1 213 ? -13.475 -2.605  15.011 1.000 26.140 0  213 ILE A CG2 1 
ATOM   1677 C CD1 . ILE A 1 213 ? -10.495 -1.498  15.638 1.000 26.670 0  213 ILE A CD1 1 
ATOM   1678 N N   . HIS A 1 214 ? -10.942 -4.821  12.323 1.000 27.980 0  214 HIS A N   1 
ATOM   1679 C CA  . HIS A 1 214 ? -10.528 -6.215  12.328 1.000 28.870 0  214 HIS A CA  1 
ATOM   1680 C C   . HIS A 1 214 ? -9.430  -6.532  13.328 1.000 27.780 0  214 HIS A C   1 
ATOM   1681 O O   . HIS A 1 214 ? -9.312  -7.696  13.724 1.000 27.160 0  214 HIS A O   1 
ATOM   1682 C CB  . HIS A 1 214 ? -10.044 -6.650  10.934 1.000 27.340 0  214 HIS A CB  1 
ATOM   1683 C CG  . HIS A 1 214 ? -11.030 -6.398  9.840  1.000 28.940 0  214 HIS A CG  1 
ATOM   1684 N ND1 . HIS A 1 214 ? -10.672 -5.839  8.632  1.000 30.630 0  214 HIS A ND1 1 
ATOM   1685 C CD2 . HIS A 1 214 ? -12.360 -6.642  9.762  1.000 30.460 0  214 HIS A CD2 1 
ATOM   1686 C CE1 . HIS A 1 214 ? -11.741 -5.742  7.860  1.000 30.420 0  214 HIS A CE1 1 
ATOM   1687 N NE2 . HIS A 1 214 ? -12.778 -6.222  8.522  1.000 30.610 0  214 HIS A NE2 1 
ATOM   1688 N N   . ALA A 1 215 ? -8.639  -5.549  13.759 1.000 28.920 0  215 ALA A N   1 
ATOM   1689 C CA  . ALA A 1 215 ? -7.523  -5.895  14.630 1.000 26.720 0  215 ALA A CA  1 
ATOM   1690 C C   . ALA A 1 215 ? -7.024  -4.692  15.420 1.000 25.930 0  215 ALA A C   1 
ATOM   1691 O O   . ALA A 1 215 ? -7.262  -3.530  15.068 1.000 26.420 0  215 ALA A O   1 
ATOM   1692 C CB  . ALA A 1 215 ? -6.373  -6.505  13.826 1.000 26.360 0  215 ALA A CB  1 
ATOM   1693 N N   . LEU A 1 216 ? -6.319  -5.009  16.502 1.000 25.850 0  216 LEU A N   1 
ATOM   1694 C CA  . LEU A 1 216 ? -5.599  -4.042  17.318 1.000 25.660 0  216 LEU A CA  1 
ATOM   1695 C C   . LEU A 1 216 ? -4.103  -4.171  17.046 1.000 26.310 0  216 LEU A C   1 
ATOM   1696 O O   . LEU A 1 216 ? -3.566  -5.285  17.009 1.000 26.650 0  216 LEU A O   1 
ATOM   1697 C CB  . LEU A 1 216 ? -5.899  -4.256  18.804 1.000 25.530 0  216 LEU A CB  1 
ATOM   1698 C CG  . LEU A 1 216 ? -4.969  -3.584  19.813 1.000 25.370 0  216 LEU A CG  1 
ATOM   1699 C CD1 . LEU A 1 216 ? -5.082  -2.074  19.721 1.000 25.220 0  216 LEU A CD1 1 
ATOM   1700 C CD2 . LEU A 1 216 ? -5.281  -4.062  21.221 1.000 25.310 0  216 LEU A CD2 1 
ATOM   1701 N N   . GLY A 1 217 ? -3.440  -3.033  16.859 1.000 25.640 0  217 GLY A N   1 
ATOM   1702 C CA  . GLY A 1 217 ? -2.008  -2.984  16.650 1.000 25.720 0  217 GLY A CA  1 
ATOM   1703 C C   . GLY A 1 217 ? -1.235  -2.496  17.857 1.000 25.560 0  217 GLY A C   1 
ATOM   1704 O O   . GLY A 1 217 ? -1.241  -1.300  18.185 1.000 25.390 0  217 GLY A O   1 
ATOM   1705 N N   . LEU A 1 218 ? -0.567  -3.436  18.523 1.000 25.630 0  218 LEU A N   1 
ATOM   1706 C CA  . LEU A 1 218 ? 0.333   -3.168  19.639 1.000 25.540 0  218 LEU A CA  1 
ATOM   1707 C C   . LEU A 1 218 ? 1.656   -2.667  19.079 1.000 25.620 0  218 LEU A C   1 
ATOM   1708 O O   . LEU A 1 218 ? 2.452   -3.447  18.553 1.000 25.840 0  218 LEU A O   1 
ATOM   1709 C CB  . LEU A 1 218 ? 0.550   -4.433  20.460 1.000 25.640 0  218 LEU A CB  1 
ATOM   1710 C CG  . LEU A 1 218 ? -0.634  -5.393  20.546 1.000 25.690 0  218 LEU A CG  1 
ATOM   1711 C CD1 . LEU A 1 218 ? -0.171  -6.778  20.954 1.000 25.880 0  218 LEU A CD1 1 
ATOM   1712 C CD2 . LEU A 1 218 ? -1.659  -4.860  21.524 1.000 25.490 0  218 LEU A CD2 1 
ATOM   1713 N N   . GLN A 1 219 ? 1.891   -1.358  19.178 1.000 25.470 0  219 GLN A N   1 
ATOM   1714 C CA  . GLN A 1 219 ? 3.155   -0.807  18.702 1.000 25.550 0  219 GLN A CA  1 
ATOM   1715 C C   . GLN A 1 219 ? 4.339   -1.496  19.371 1.000 26.220 0  219 GLN A C   1 
ATOM   1716 O O   . GLN A 1 219 ? 5.366   -1.735  18.730 1.000 25.860 0  219 GLN A O   1 
ATOM   1717 C CB  . GLN A 1 219 ? 3.186   0.702   18.930 1.000 25.360 0  219 GLN A CB  1 
ATOM   1718 C CG  . GLN A 1 219 ? 2.090   1.428   18.167 1.000 25.760 0  219 GLN A CG  1 
ATOM   1719 C CD  . GLN A 1 219 ? 2.236   2.932   18.203 1.000 25.360 0  219 GLN A CD  1 
ATOM   1720 O OE1 . GLN A 1 219 ? 3.258   3.462   18.637 1.000 25.120 0  219 GLN A OE1 1 
ATOM   1721 N NE2 . GLN A 1 219 ? 1.208   3.632   17.737 1.000 25.080 0  219 GLN A NE2 1 
ATOM   1722 N N   . SER A 1 220 ? 4.203   -1.838  20.653 1.000 25.560 0  220 SER A N   1 
ATOM   1723 C CA  . SER A 1 220 ? 5.194   -2.640  21.371 1.000 25.700 0  220 SER A CA  1 
ATOM   1724 C C   . SER A 1 220 ? 6.553   -1.945  21.416 1.000 26.080 0  220 SER A C   1 
ATOM   1725 O O   . SER A 1 220 ? 7.589   -2.524  21.077 1.000 26.060 0  220 SER A O   1 
ATOM   1726 C CB  . SER A 1 220 ? 5.310   -4.039  20.759 1.000 26.640 0  220 SER A CB  1 
ATOM   1727 O OG  . SER A 1 220 ? 4.051   -4.691  20.723 1.000 25.930 0  220 SER A OG  1 
ATOM   1728 N N   . HIS A 1 221 ? 6.543   -0.681  21.840 1.000 29.120 0  221 HIS A N   1 
ATOM   1729 C CA  . HIS A 1 221 ? 7.778   0.045   22.129 1.000 27.890 0  221 HIS A CA  1 
ATOM   1730 C C   . HIS A 1 221 ? 8.091   -0.180  23.603 1.000 26.290 0  221 HIS A C   1 
ATOM   1731 O O   . HIS A 1 221 ? 7.858   0.668   24.465 1.000 25.310 0  221 HIS A O   1 
ATOM   1732 C CB  . HIS A 1 221 ? 7.634   1.525   21.797 1.000 25.390 0  221 HIS A CB  1 
ATOM   1733 C CG  . HIS A 1 221 ? 7.459   1.813   20.337 1.000 26.220 0  221 HIS A CG  1 
ATOM   1734 N ND1 . HIS A 1 221 ? 8.489   1.706   19.426 1.000 27.260 0  221 HIS A ND1 1 
ATOM   1735 C CD2 . HIS A 1 221 ? 6.378   2.226   19.634 1.000 25.890 0  221 HIS A CD2 1 
ATOM   1736 C CE1 . HIS A 1 221 ? 8.047   2.033   18.225 1.000 28.750 0  221 HIS A CE1 1 
ATOM   1737 N NE2 . HIS A 1 221 ? 6.769   2.352   18.324 1.000 27.680 0  221 HIS A NE2 1 
ATOM   1738 N N   . ILE A 1 222 ? 8.631   -1.363  23.889 1.000 29.650 0  222 ILE A N   1 
ATOM   1739 C CA  . ILE A 1 222 ? 8.747   -1.820  25.266 1.000 31.640 0  222 ILE A CA  1 
ATOM   1740 C C   . ILE A 1 222 ? 10.017  -1.261  25.898 1.000 32.260 0  222 ILE A C   1 
ATOM   1741 O O   . ILE A 1 222 ? 10.968  -0.867  25.219 1.000 29.640 0  222 ILE A O   1 
ATOM   1742 C CB  . ILE A 1 222 ? 8.715   -3.358  25.348 1.000 29.640 0  222 ILE A CB  1 
ATOM   1743 C CG1 . ILE A 1 222 ? 9.929   -3.958  24.637 1.000 30.900 0  222 ILE A CG1 1 
ATOM   1744 C CG2 . ILE A 1 222 ? 7.421   -3.898  24.758 1.000 28.160 0  222 ILE A CG2 1 
ATOM   1745 C CD1 . ILE A 1 222 ? 9.894   -5.469  24.536 1.000 30.140 0  222 ILE A CD1 1 
ATOM   1746 N N   . SER A 1 223 ? 10.016  -1.225  27.228 1.000 33.740 0  223 SER A N   1 
ATOM   1747 C CA  . SER A 1 223 ? 11.157  -0.781  28.013 1.000 33.400 0  223 SER A CA  1 
ATOM   1748 C C   . SER A 1 223 ? 11.208  -1.627  29.280 1.000 37.990 0  223 SER A C   1 
ATOM   1749 O O   . SER A 1 223 ? 10.501  -2.632  29.406 1.000 36.350 0  223 SER A O   1 
ATOM   1750 C CB  . SER A 1 223 ? 11.055  0.717   28.320 1.000 31.710 0  223 SER A CB  1 
ATOM   1751 O OG  . SER A 1 223 ? 9.932   0.977   29.141 1.000 36.080 0  223 SER A OG  1 
ATOM   1752 N N   . ALA A 1 224 ? 12.025  -1.198  30.245 1.000 40.250 0  224 ALA A N   1 
ATOM   1753 C CA  . ALA A 1 224 ? 12.232  -1.999  31.444 1.000 37.510 0  224 ALA A CA  1 
ATOM   1754 C C   . ALA A 1 224 ? 10.997  -2.043  32.331 1.000 38.490 0  224 ALA A C   1 
ATOM   1755 O O   . ALA A 1 224 ? 10.872  -2.961  33.150 1.000 40.350 0  224 ALA A O   1 
ATOM   1756 C CB  . ALA A 1 224 ? 13.424  -1.467  32.237 1.000 36.550 0  224 ALA A CB  1 
ATOM   1757 N N   . GLY A 1 225 ? 10.085  -1.085  32.186 1.000 40.620 0  225 GLY A N   1 
ATOM   1758 C CA  . GLY A 1 225 ? 8.833   -1.117  32.914 1.000 37.380 0  225 GLY A CA  1 
ATOM   1759 C C   . GLY A 1 225 ? 7.782   -2.033  32.337 1.000 38.170 0  225 GLY A C   1 
ATOM   1760 O O   . GLY A 1 225 ? 6.670   -2.101  32.867 1.000 39.040 0  225 GLY A O   1 
ATOM   1761 N N   . ASP A 1 226 ? 8.104   -2.743  31.255 1.000 40.410 0  226 ASP A N   1 
ATOM   1762 C CA  . ASP A 1 226 ? 7.236   -3.764  30.688 1.000 38.040 0  226 ASP A CA  1 
ATOM   1763 C C   . ASP A 1 226 ? 7.679   -5.179  31.049 1.000 40.090 0  226 ASP A C   1 
ATOM   1764 O O   . ASP A 1 226 ? 7.193   -6.143  30.447 1.000 39.550 0  226 ASP A O   1 
ATOM   1765 C CB  . ASP A 1 226 ? 7.166   -3.602  29.167 1.000 36.560 0  226 ASP A CB  1 
ATOM   1766 C CG  . ASP A 1 226 ? 6.740   -2.204  28.748 1.000 36.860 0  226 ASP A CG  1 
ATOM   1767 O OD1 . ASP A 1 226 ? 5.519   -1.951  28.688 1.000 35.950 0  226 ASP A OD1 1 
ATOM   1768 O OD2 . ASP A 1 226 ? 7.620   -1.358  28.474 1.000 36.570 -1 226 ASP A OD2 1 
ATOM   1769 N N   . MET A 1 227 ? 8.596   -5.321  32.005 1.000 40.430 0  227 MET A N   1 
ATOM   1770 C CA  . MET A 1 227 ? 9.018   -6.642  32.452 1.000 39.230 0  227 MET A CA  1 
ATOM   1771 C C   . MET A 1 227 ? 7.849   -7.363  33.108 1.000 37.250 0  227 MET A C   1 
ATOM   1772 O O   . MET A 1 227 ? 7.110   -6.779  33.906 1.000 37.010 0  227 MET A O   1 
ATOM   1773 C CB  . MET A 1 227 ? 10.189  -6.522  33.429 1.000 37.690 0  227 MET A CB  1 
ATOM   1774 C CG  . MET A 1 227 ? 11.182  -7.675  33.378 1.000 38.300 0  227 MET A CG  1 
ATOM   1775 S SD  . MET A 1 227 ? 11.431  -8.370  31.732 1.000 44.260 0  227 MET A SD  1 
ATOM   1776 C CE  . MET A 1 227 ? 12.032  -10.005 32.143 1.000 35.250 0  227 MET A CE  1 
ATOM   1777 N N   . MET A 1 228 ? 7.671   -8.639  32.765 1.000 37.980 0  228 MET A N   1 
ATOM   1778 C CA  . MET A 1 228 ? 6.502   -9.375  33.218 1.000 39.880 0  228 MET A CA  1 
ATOM   1779 C C   . MET A 1 228 ? 6.795   -10.661 33.981 1.000 41.190 0  228 MET A C   1 
ATOM   1780 O O   . MET A 1 228 ? 5.917   -11.118 34.720 1.000 41.400 0  228 MET A O   1 
ATOM   1781 C CB  . MET A 1 228 ? 5.581   -9.700  32.032 1.000 36.950 0  228 MET A CB  1 
ATOM   1782 C CG  . MET A 1 228 ? 4.585   -8.593  31.754 1.000 35.750 0  228 MET A CG  1 
ATOM   1783 S SD  . MET A 1 228 ? 3.435   -8.989  30.432 1.000 42.720 0  228 MET A SD  1 
ATOM   1784 C CE  . MET A 1 228 ? 4.342   -8.352  29.023 1.000 35.090 0  228 MET A CE  1 
ATOM   1785 N N   . SER A 1 229 ? 7.972   -11.258 33.833 1.000 39.200 0  229 SER A N   1 
ATOM   1786 C CA  . SER A 1 229 ? 8.265   -12.482 34.564 1.000 40.150 0  229 SER A CA  1 
ATOM   1787 C C   . SER A 1 229 ? 8.869   -12.156 35.924 1.000 42.380 0  229 SER A C   1 
ATOM   1788 O O   . SER A 1 229 ? 9.518   -11.123 36.106 1.000 42.140 0  229 SER A O   1 
ATOM   1789 C CB  . SER A 1 229 ? 9.217   -13.379 33.773 1.000 41.180 0  229 SER A CB  1 
ATOM   1790 O OG  . SER A 1 229 ? 10.282  -12.629 33.218 1.000 41.890 0  229 SER A OG  1 
ATOM   1791 N N   . GLY A 1 230 ? 8.651   -13.055 36.883 1.000 42.590 0  230 GLY A N   1 
ATOM   1792 C CA  . GLY A 1 230 ? 9.085   -12.824 38.240 1.000 43.320 0  230 GLY A CA  1 
ATOM   1793 C C   . GLY A 1 230 ? 7.954   -12.408 39.160 1.000 44.110 0  230 GLY A C   1 
ATOM   1794 O O   . GLY A 1 230 ? 6.963   -11.805 38.732 1.000 43.950 0  230 GLY A O   1 
ATOM   1795 N N   . PRO A 1 231 ? 8.078   -12.743 40.449 1.000 41.470 0  231 PRO A N   1 
ATOM   1796 C CA  . PRO A 1 231 ? 7.029   -12.369 41.417 1.000 41.790 0  231 PRO A CA  1 
ATOM   1797 C C   . PRO A 1 231 ? 6.712   -10.882 41.442 1.000 42.610 0  231 PRO A C   1 
ATOM   1798 O O   . PRO A 1 231 ? 5.535   -10.511 41.546 1.000 43.280 0  231 PRO A O   1 
ATOM   1799 C CB  . PRO A 1 231 ? 7.612   -12.847 42.755 1.000 36.750 0  231 PRO A CB  1 
ATOM   1800 C CG  . PRO A 1 231 ? 8.524   -13.962 42.384 1.000 37.180 0  231 PRO A CG  1 
ATOM   1801 C CD  . PRO A 1 231 ? 9.126   -13.576 41.063 1.000 40.380 0  231 PRO A CD  1 
ATOM   1802 N N   . ALA A 1 232 ? 7.727   -10.017 41.359 1.000 40.350 0  232 ALA A N   1 
ATOM   1803 C CA  . ALA A 1 232 ? 7.483   -8.579  41.403 1.000 40.550 0  232 ALA A CA  1 
ATOM   1804 C C   . ALA A 1 232 ? 6.599   -8.107  40.258 1.000 42.990 0  232 ALA A C   1 
ATOM   1805 O O   . ALA A 1 232 ? 6.007   -7.026  40.349 1.000 42.910 0  232 ALA A O   1 
ATOM   1806 C CB  . ALA A 1 232 ? 8.809   -7.816  41.375 1.000 39.200 0  232 ALA A CB  1 
ATOM   1807 N N   . ASN A 1 233 ? 6.502   -8.888  39.182 1.000 43.260 0  233 ASN A N   1 
ATOM   1808 C CA  . ASN A 1 233 ? 5.758   -8.511  37.988 1.000 41.060 0  233 ASN A CA  1 
ATOM   1809 C C   . ASN A 1 233 ? 4.477   -9.323  37.816 1.000 40.150 0  233 ASN A C   1 
ATOM   1810 O O   . ASN A 1 233 ? 3.906   -9.339  36.721 1.000 40.010 0  233 ASN A O   1 
ATOM   1811 C CB  . ASN A 1 233 ? 6.650   -8.651  36.758 1.000 39.370 0  233 ASN A CB  1 
ATOM   1812 C CG  . ASN A 1 233 ? 7.996   -7.981  36.942 1.000 41.210 0  233 ASN A CG  1 
ATOM   1813 O OD1 . ASN A 1 233 ? 8.072   -6.839  37.393 1.000 42.280 0  233 ASN A OD1 1 
ATOM   1814 N ND2 . ASN A 1 233 ? 9.066   -8.690  36.601 1.000 41.060 0  233 ASN A ND2 1 
ATOM   1815 N N   . ALA A 1 234 ? 4.036   -10.022 38.864 1.000 39.870 0  234 ALA A N   1 
ATOM   1816 C CA  . ALA A 1 234 ? 2.851   -10.870 38.754 1.000 40.080 0  234 ALA A CA  1 
ATOM   1817 C C   . ALA A 1 234 ? 1.626   -10.079 38.304 1.000 39.820 0  234 ALA A C   1 
ATOM   1818 O O   . ALA A 1 234 ? 0.936   -10.468 37.355 1.000 37.840 0  234 ALA A O   1 
ATOM   1819 C CB  . ALA A 1 234 ? 2.580   -11.565 40.089 1.000 39.000 0  234 ALA A CB  1 
ATOM   1820 N N   . ALA A 1 235 ? 1.340   -8.962  38.978 1.000 40.320 0  235 ALA A N   1 
ATOM   1821 C CA  . ALA A 1 235 ? 0.138   -8.189  38.671 1.000 39.070 0  235 ALA A CA  1 
ATOM   1822 C C   . ALA A 1 235 ? 0.187   -7.591  37.268 1.000 37.060 0  235 ALA A C   1 
ATOM   1823 O O   . ALA A 1 235 ? -0.819  -7.601  36.549 1.000 37.860 0  235 ALA A O   1 
ATOM   1824 C CB  . ALA A 1 235 ? -0.060  -7.093  39.719 1.000 37.510 0  235 ALA A CB  1 
ATOM   1825 N N   . VAL A 1 236 ? 1.335   -7.030  36.882 1.000 34.720 0  236 VAL A N   1 
ATOM   1826 C CA  . VAL A 1 236 ? 1.485   -6.455  35.546 1.000 33.970 0  236 VAL A CA  1 
ATOM   1827 C C   . VAL A 1 236 ? 1.213   -7.501  34.470 1.000 34.980 0  236 VAL A C   1 
ATOM   1828 O O   . VAL A 1 236 ? 0.508   -7.235  33.486 1.000 33.250 0  236 VAL A O   1 
ATOM   1829 C CB  . VAL A 1 236 ? 2.887   -5.833  35.397 1.000 35.680 0  236 VAL A CB  1 
ATOM   1830 C CG1 . VAL A 1 236 ? 3.308   -5.782  33.937 1.000 34.380 0  236 VAL A CG1 1 
ATOM   1831 C CG2 . VAL A 1 236 ? 2.914   -4.442  36.015 1.000 32.020 0  236 VAL A CG2 1 
ATOM   1832 N N   . LEU A 1 237 ? 1.732   -8.718  34.659 1.000 36.070 0  237 LEU A N   1 
ATOM   1833 C CA  . LEU A 1 237 ? 1.531   -9.785  33.682 1.000 35.290 0  237 LEU A CA  1 
ATOM   1834 C C   . LEU A 1 237 ? 0.066   -10.193 33.615 1.000 33.880 0  237 LEU A C   1 
ATOM   1835 O O   . LEU A 1 237 ? -0.498  -10.351 32.525 1.000 34.640 0  237 LEU A O   1 
ATOM   1836 C CB  . LEU A 1 237 ? 2.418   -10.983 34.030 1.000 33.710 0  237 LEU A CB  1 
ATOM   1837 C CG  . LEU A 1 237 ? 1.985   -12.344 33.485 1.000 33.250 0  237 LEU A CG  1 
ATOM   1838 C CD1 . LEU A 1 237 ? 2.440   -12.498 32.050 1.000 31.370 0  237 LEU A CD1 1 
ATOM   1839 C CD2 . LEU A 1 237 ? 2.531   -13.475 34.343 1.000 31.390 0  237 LEU A CD2 1 
ATOM   1840 N N   . ARG A 1 238 ? -0.545  -10.427 34.779 1.000 35.740 0  238 ARG A N   1 
ATOM   1841 C CA  . ARG A 1 238 ? -1.959  -10.778 34.840 1.000 35.290 0  238 ARG A CA  1 
ATOM   1842 C C   . ARG A 1 238 ? -2.802  -9.751  34.097 1.000 34.360 0  238 ARG A C   1 
ATOM   1843 O O   . ARG A 1 238 ? -3.679  -10.107 33.302 1.000 34.390 0  238 ARG A O   1 
ATOM   1844 C CB  . ARG A 1 238 ? -2.405  -10.886 36.298 1.000 36.280 0  238 ARG A CB  1 
ATOM   1845 C CG  . ARG A 1 238 ? -3.464  -11.939 36.554 1.000 38.200 0  238 ARG A CG  1 
ATOM   1846 C CD  . ARG A 1 238 ? -3.494  -12.334 38.024 1.000 39.900 0  238 ARG A CD  1 
ATOM   1847 N NE  . ARG A 1 238 ? -3.108  -11.232 38.900 1.000 39.990 0  238 ARG A NE  1 
ATOM   1848 C CZ  . ARG A 1 238 ? -2.108  -11.277 39.769 1.000 39.880 0  238 ARG A CZ  1 
ATOM   1849 N NH1 . ARG A 1 238 ? -1.349  -12.355 39.897 1.000 39.700 1  238 ARG A NH1 1 
ATOM   1850 N NH2 . ARG A 1 238 ? -1.863  -10.214 40.532 1.000 38.840 0  238 ARG A NH2 1 
ATOM   1851 N N   . GLU A 1 239 ? -2.569  -8.465  34.377 1.000 32.010 0  239 GLU A N   1 
ATOM   1852 C CA  . GLU A 1 239 ? -3.375  -7.407  33.774 1.000 34.050 0  239 GLU A CA  1 
ATOM   1853 C C   . GLU A 1 239 ? -3.148  -7.308  32.266 1.000 34.020 0  239 GLU A C   1 
ATOM   1854 O O   . GLU A 1 239 ? -4.098  -7.084  31.506 1.000 36.050 0  239 GLU A O   1 
ATOM   1855 C CB  . GLU A 1 239 ? -3.078  -6.072  34.455 1.000 33.580 0  239 GLU A CB  1 
ATOM   1856 C CG  . GLU A 1 239 ? -3.929  -5.811  35.687 1.000 30.080 0  239 GLU A CG  1 
ATOM   1857 C CD  . GLU A 1 239 ? -5.395  -5.612  35.351 1.000 33.500 0  239 GLU A CD  1 
ATOM   1858 O OE1 . GLU A 1 239 ? -5.768  -4.495  34.929 1.000 32.570 0  239 GLU A OE1 1 
ATOM   1859 O OE2 . GLU A 1 239 ? -6.175  -6.577  35.503 1.000 33.180 -1 239 GLU A OE2 1 
ATOM   1860 N N   . TRP A 1 240 ? -1.898  -7.439  31.813 1.000 34.320 0  240 TRP A N   1 
ATOM   1861 C CA  . TRP A 1 240 ? -1.630  -7.439  30.375 1.000 33.080 0  240 TRP A CA  1 
ATOM   1862 C C   . TRP A 1 240 ? -2.364  -8.583  29.685 1.000 33.380 0  240 TRP A C   1 
ATOM   1863 O O   . TRP A 1 240 ? -2.981  -8.401  28.623 1.000 32.100 0  240 TRP A O   1 
ATOM   1864 C CB  . TRP A 1 240 ? -0.124  -7.527  30.121 1.000 31.480 0  240 TRP A CB  1 
ATOM   1865 C CG  . TRP A 1 240 ? 0.245   -7.519  28.664 1.000 32.950 0  240 TRP A CG  1 
ATOM   1866 C CD1 . TRP A 1 240 ? 0.976   -8.460  28.002 1.000 33.410 0  240 TRP A CD1 1 
ATOM   1867 C CD2 . TRP A 1 240 ? -0.086  -6.515  27.695 1.000 31.010 0  240 TRP A CD2 1 
ATOM   1868 N NE1 . TRP A 1 240 ? 1.114   -8.112  26.681 1.000 30.480 0  240 TRP A NE1 1 
ATOM   1869 C CE2 . TRP A 1 240 ? 0.474   -6.921  26.466 1.000 28.010 0  240 TRP A CE2 1 
ATOM   1870 C CE3 . TRP A 1 240 ? -0.800  -5.315  27.745 1.000 29.710 0  240 TRP A CE3 1 
ATOM   1871 C CZ2 . TRP A 1 240 ? 0.340   -6.172  25.301 1.000 27.150 0  240 TRP A CZ2 1 
ATOM   1872 C CZ3 . TRP A 1 240 ? -0.931  -4.574  26.587 1.000 27.920 0  240 TRP A CZ3 1 
ATOM   1873 C CH2 . TRP A 1 240 ? -0.365  -5.004  25.382 1.000 26.970 0  240 TRP A CH2 1 
ATOM   1874 N N   . ARG A 1 241 ? -2.272  -9.784  30.264 1.000 33.200 0  241 ARG A N   1 
ATOM   1875 C CA  . ARG A 1 241 ? -3.006  -10.923 29.727 1.000 34.400 0  241 ARG A CA  1 
ATOM   1876 C C   . ARG A 1 241 ? -4.504  -10.653 29.709 1.000 34.000 0  241 ARG A C   1 
ATOM   1877 O O   . ARG A 1 241 ? -5.190  -11.029 28.759 1.000 33.950 0  241 ARG A O   1 
ATOM   1878 C CB  . ARG A 1 241 ? -2.682  -12.190 30.521 1.000 33.800 0  241 ARG A CB  1 
ATOM   1879 C CG  . ARG A 1 241 ? -1.343  -12.825 30.140 1.000 34.090 0  241 ARG A CG  1 
ATOM   1880 C CD  . ARG A 1 241 ? -1.281  -14.306 30.507 1.000 34.010 0  241 ARG A CD  1 
ATOM   1881 N NE  . ARG A 1 241 ? -2.060  -15.132 29.592 1.000 38.120 0  241 ARG A NE  1 
ATOM   1882 C CZ  . ARG A 1 241 ? -1.657  -15.517 28.387 1.000 36.930 0  241 ARG A CZ  1 
ATOM   1883 N NH1 . ARG A 1 241 ? -0.458  -15.202 27.925 1.000 35.850 1  241 ARG A NH1 1 
ATOM   1884 N NH2 . ARG A 1 241 ? -2.477  -16.238 27.628 1.000 34.120 0  241 ARG A NH2 1 
ATOM   1885 N N   . LYS A 1 242 ? -5.035  -10.031 30.766 1.000 33.940 0  242 LYS A N   1 
ATOM   1886 C CA  . LYS A 1 242 ? -6.455  -9.689  30.793 1.000 33.680 0  242 LYS A CA  1 
ATOM   1887 C C   . LYS A 1 242 ? -6.822  -8.754  29.645 1.000 34.350 0  242 LYS A C   1 
ATOM   1888 O O   . LYS A 1 242 ? -7.870  -8.920  29.008 1.000 35.680 0  242 LYS A O   1 
ATOM   1889 C CB  . LYS A 1 242 ? -6.825  -9.056  32.134 1.000 35.570 0  242 LYS A CB  1 
ATOM   1890 C CG  . LYS A 1 242 ? -8.303  -8.701  32.254 1.000 36.810 0  242 LYS A CG  1 
ATOM   1891 C CD  . LYS A 1 242 ? -8.931  -9.315  33.493 1.000 39.250 0  242 LYS A CD  1 
ATOM   1892 C CE  . LYS A 1 242 ? -10.420 -9.566  33.288 1.000 39.620 0  242 LYS A CE  1 
ATOM   1893 N NZ  . LYS A 1 242 ? -10.863 -10.835 33.939 1.000 34.950 1  242 LYS A NZ  1 
ATOM   1894 N N   . PHE A 1 243 ? -5.995  -7.735  29.403 1.000 31.990 0  243 PHE A N   1 
ATOM   1895 C CA  . PHE A 1 243 ? -6.233  -6.828  28.281 1.000 32.120 0  243 PHE A CA  1 
ATOM   1896 C C   . PHE A 1 243 ? -6.307  -7.596  26.965 1.000 31.860 0  243 PHE A C   1 
ATOM   1897 O O   . PHE A 1 243 ? -7.273  -7.458  26.202 1.000 30.030 0  243 PHE A O   1 
ATOM   1898 C CB  . PHE A 1 243 ? -5.140  -5.757  28.225 1.000 30.840 0  243 PHE A CB  1 
ATOM   1899 C CG  . PHE A 1 243 ? -5.224  -4.861  27.017 1.000 30.720 0  243 PHE A CG  1 
ATOM   1900 C CD1 . PHE A 1 243 ? -6.303  -4.011  26.843 1.000 31.170 0  243 PHE A CD1 1 
ATOM   1901 C CD2 . PHE A 1 243 ? -4.225  -4.866  26.061 1.000 29.340 0  243 PHE A CD2 1 
ATOM   1902 C CE1 . PHE A 1 243 ? -6.383  -3.186  25.732 1.000 30.690 0  243 PHE A CE1 1 
ATOM   1903 C CE2 . PHE A 1 243 ? -4.299  -4.042  24.950 1.000 29.000 0  243 PHE A CE2 1 
ATOM   1904 C CZ  . PHE A 1 243 ? -5.379  -3.201  24.786 1.000 27.440 0  243 PHE A CZ  1 
ATOM   1905 N N   . LEU A 1 244 ? -5.278  -8.396  26.674 1.000 32.260 0  244 LEU A N   1 
ATOM   1906 C CA  . LEU A 1 244 ? -5.262  -9.153  25.422 1.000 29.740 0  244 LEU A CA  1 
ATOM   1907 C C   . LEU A 1 244 ? -6.434  -10.127 25.349 1.000 31.800 0  244 LEU A C   1 
ATOM   1908 O O   . LEU A 1 244 ? -7.002  -10.353 24.271 1.000 32.470 0  244 LEU A O   1 
ATOM   1909 C CB  . LEU A 1 244 ? -3.932  -9.885  25.266 1.000 28.420 0  244 LEU A CB  1 
ATOM   1910 C CG  . LEU A 1 244 ? -2.750  -8.934  25.079 1.000 29.270 0  244 LEU A CG  1 
ATOM   1911 C CD1 . LEU A 1 244 ? -1.450  -9.695  24.883 1.000 28.230 0  244 LEU A CD1 1 
ATOM   1912 C CD2 . LEU A 1 244 ? -3.015  -8.000  23.908 1.000 28.720 0  244 LEU A CD2 1 
ATOM   1913 N N   . ASP A 1 245 ? -6.787  -10.736 26.484 1.000 32.910 0  245 ASP A N   1 
ATOM   1914 C CA  . ASP A 1 245 ? -7.945  -11.618 26.556 1.000 33.090 0  245 ASP A CA  1 
ATOM   1915 C C   . ASP A 1 245 ? -9.204  -10.886 26.128 1.000 32.320 0  245 ASP A C   1 
ATOM   1916 O O   . ASP A 1 245 ? -9.984  -11.393 25.322 1.000 36.290 0  245 ASP A O   1 
ATOM   1917 C CB  . ASP A 1 245 ? -8.102  -12.170 27.975 1.000 32.300 0  245 ASP A CB  1 
ATOM   1918 C CG  . ASP A 1 245 ? -7.342  -13.459 28.186 1.000 29.390 0  245 ASP A CG  1 
ATOM   1919 O OD1 . ASP A 1 245 ? -6.768  -13.975 27.208 1.000 33.130 0  245 ASP A OD1 1 
ATOM   1920 O OD2 . ASP A 1 245 ? -7.328  -13.965 29.327 1.000 28.650 -1 245 ASP A OD2 1 
ATOM   1921 N N   . GLU A 1 246 ? -9.427  -9.697  26.686 1.000 34.030 0  246 GLU A N   1 
ATOM   1922 C CA  . GLU A 1 246 ? -10.610 -8.918  26.338 1.000 36.350 0  246 GLU A CA  1 
ATOM   1923 C C   . GLU A 1 246 ? -10.608 -8.552  24.858 1.000 33.550 0  246 GLU A C   1 
ATOM   1924 O O   . GLU A 1 246 ? -11.634 -8.679  24.169 1.000 34.600 0  246 GLU A O   1 
ATOM   1925 C CB  . GLU A 1 246 ? -10.644 -7.650  27.194 1.000 37.830 0  246 GLU A CB  1 
ATOM   1926 C CG  . GLU A 1 246 ? -11.527 -7.716  28.423 1.000 40.920 0  246 GLU A CG  1 
ATOM   1927 C CD  . GLU A 1 246 ? -12.932 -7.232  28.143 1.000 50.850 0  246 GLU A CD  1 
ATOM   1928 O OE1 . GLU A 1 246 ? -13.216 -6.048  28.438 1.000 52.340 0  246 GLU A OE1 1 
ATOM   1929 O OE2 . GLU A 1 246 ? -13.749 -8.029  27.633 1.000 49.580 -1 246 GLU A OE2 1 
ATOM   1930 N N   . VAL A 1 247 ? -9.444  -8.145  24.343 1.000 32.680 0  247 VAL A N   1 
ATOM   1931 C CA  . VAL A 1 247 ? -9.346  -7.737  22.943 1.000 33.930 0  247 VAL A CA  1 
ATOM   1932 C C   . VAL A 1 247 ? -9.717  -8.891  22.022 1.000 33.150 0  247 VAL A C   1 
ATOM   1933 O O   . VAL A 1 247 ? -10.565 -8.748  21.133 1.000 32.980 0  247 VAL A O   1 
ATOM   1934 C CB  . VAL A 1 247 ? -7.939  -7.198  22.632 1.000 32.840 0  247 VAL A CB  1 
ATOM   1935 C CG1 . VAL A 1 247 ? -7.793  -6.960  21.140 1.000 33.840 0  247 VAL A CG1 1 
ATOM   1936 C CG2 . VAL A 1 247 ? -7.683  -5.910  23.397 1.000 31.200 0  247 VAL A CG2 1 
ATOM   1937 N N   . THR A 1 248 ? -9.090  -10.052 22.221 1.000 33.060 0  248 THR A N   1 
ATOM   1938 C CA  . THR A 1 248 ? -9.401  -11.200 21.375 1.000 34.620 0  248 THR A CA  1 
ATOM   1939 C C   . THR A 1 248 ? -10.779 -11.782 21.667 1.000 34.530 0  248 THR A C   1 
ATOM   1940 O O   . THR A 1 248 ? -11.323 -12.503 20.822 1.000 34.860 0  248 THR A O   1 
ATOM   1941 C CB  . THR A 1 248 ? -8.334  -12.280 21.532 1.000 32.240 0  248 THR A CB  1 
ATOM   1942 O OG1 . THR A 1 248 ? -7.943  -12.365 22.908 1.000 34.220 0  248 THR A OG1 1 
ATOM   1943 C CG2 . THR A 1 248 ? -7.124  -11.941 20.685 1.000 33.310 0  248 THR A CG2 1 
ATOM   1944 N N   . GLY A 1 249 ? -11.349 -11.489 22.837 1.000 31.930 0  249 GLY A N   1 
ATOM   1945 C CA  . GLY A 1 249 ? -12.720 -11.871 23.107 1.000 31.480 0  249 GLY A CA  1 
ATOM   1946 C C   . GLY A 1 249 ? -13.722 -11.069 22.308 1.000 32.770 0  249 GLY A C   1 
ATOM   1947 O O   . GLY A 1 249 ? -14.801 -11.571 21.982 1.000 34.040 0  249 GLY A O   1 
ATOM   1948 N N   . MET A 1 250 ? -13.389 -9.819  21.978 1.000 32.790 0  250 MET A N   1 
ATOM   1949 C CA  . MET A 1 250 ? -14.279 -9.034  21.124 1.000 33.680 0  250 MET A CA  1 
ATOM   1950 C C   . MET A 1 250 ? -14.211 -9.444  19.654 1.000 32.930 0  250 MET A C   1 
ATOM   1951 O O   . MET A 1 250 ? -14.811 -8.767  18.812 1.000 34.460 0  250 MET A O   1 
ATOM   1952 C CB  . MET A 1 250 ? -13.965 -7.538  21.227 1.000 32.350 0  250 MET A CB  1 
ATOM   1953 C CG  . MET A 1 250 ? -13.801 -7.007  22.631 1.000 34.080 0  250 MET A CG  1 
ATOM   1954 S SD  . MET A 1 250 ? -13.226 -5.300  22.613 1.000 36.850 0  250 MET A SD  1 
ATOM   1955 C CE  . MET A 1 250 ? -13.264 -4.915  24.362 1.000 38.550 0  250 MET A CE  1 
ATOM   1956 N N   . GLY A 1 251 ? -13.497 -10.515 19.321 1.000 30.950 0  251 GLY A N   1 
ATOM   1957 C CA  . GLY A 1 251 ? -13.344 -10.890 17.931 1.000 31.190 0  251 GLY A CA  1 
ATOM   1958 C C   . GLY A 1 251 ? -12.353 -10.042 17.170 1.000 32.180 0  251 GLY A C   1 
ATOM   1959 O O   . GLY A 1 251 ? -12.506 -9.857  15.958 1.000 33.830 0  251 GLY A O   1 
ATOM   1960 N N   . LEU A 1 252 ? -11.344 -9.508  17.850 1.000 29.490 0  252 LEU A N   1 
ATOM   1961 C CA  . LEU A 1 252 ? -10.322 -8.679  17.230 1.000 29.200 0  252 LEU A CA  1 
ATOM   1962 C C   . LEU A 1 252 ? -9.024  -9.470  17.146 1.000 29.900 0  252 LEU A C   1 
ATOM   1963 O O   . LEU A 1 252 ? -8.617  -10.111 18.121 1.000 28.140 0  252 LEU A O   1 
ATOM   1964 C CB  . LEU A 1 252 ? -10.104 -7.391  18.026 1.000 31.850 0  252 LEU A CB  1 
ATOM   1965 C CG  . LEU A 1 252 ? -11.178 -6.304  17.954 1.000 28.690 0  252 LEU A CG  1 
ATOM   1966 C CD1 . LEU A 1 252 ? -10.826 -5.180  18.909 1.000 28.390 0  252 LEU A CD1 1 
ATOM   1967 C CD2 . LEU A 1 252 ? -11.332 -5.775  16.536 1.000 28.250 0  252 LEU A CD2 1 
ATOM   1968 N N   . ASP A 1 253 ? -8.385  -9.435  15.980 1.000 28.710 0  253 ASP A N   1 
ATOM   1969 C CA  . ASP A 1 253 ? -7.066  -10.026 15.839 1.000 28.530 0  253 ASP A CA  1 
ATOM   1970 C C   . ASP A 1 253 ? -6.008  -9.049  16.351 1.000 27.610 0  253 ASP A C   1 
ATOM   1971 O O   . ASP A 1 253 ? -6.300  -7.908  16.720 1.000 30.170 0  253 ASP A O   1 
ATOM   1972 C CB  . ASP A 1 253 ? -6.817  -10.435 14.389 1.000 29.650 0  253 ASP A CB  1 
ATOM   1973 C CG  . ASP A 1 253 ? -7.735  -11.558 13.937 1.000 30.640 0  253 ASP A CG  1 
ATOM   1974 O OD1 . ASP A 1 253 ? -8.245  -12.295 14.809 1.000 31.430 0  253 ASP A OD1 1 
ATOM   1975 O OD2 . ASP A 1 253 ? -7.933  -11.720 12.716 1.000 31.070 -1 253 ASP A OD2 1 
ATOM   1976 N N   . LEU A 1 254 ? -4.757  -9.492  16.374 1.000 26.500 0  254 LEU A N   1 
ATOM   1977 C CA  . LEU A 1 254 ? -3.685  -8.696  16.946 1.000 26.650 0  254 LEU A CA  1 
ATOM   1978 C C   . LEU A 1 254 ? -2.553  -8.533  15.944 1.000 27.630 0  254 LEU A C   1 
ATOM   1979 O O   . LEU A 1 254 ? -2.376  -9.350  15.037 1.000 28.950 0  254 LEU A O   1 
ATOM   1980 C CB  . LEU A 1 254 ? -3.150  -9.325  18.239 1.000 28.790 0  254 LEU A CB  1 
ATOM   1981 C CG  . LEU A 1 254 ? -4.194  -9.626  19.317 1.000 28.330 0  254 LEU A CG  1 
ATOM   1982 C CD1 . LEU A 1 254 ? -3.768  -10.808 20.170 1.000 27.330 0  254 LEU A CD1 1 
ATOM   1983 C CD2 . LEU A 1 254 ? -4.440  -8.399  20.179 1.000 25.970 0  254 LEU A CD2 1 
ATOM   1984 N N   . LEU A 1 255 ? -1.806  -7.444  16.108 1.000 27.620 0  255 LEU A N   1 
ATOM   1985 C CA  . LEU A 1 255 ? -0.547  -7.248  15.406 1.000 27.150 0  255 LEU A CA  1 
ATOM   1986 C C   . LEU A 1 255 ? 0.473   -6.683  16.378 1.000 26.380 0  255 LEU A C   1 
ATOM   1987 O O   . LEU A 1 255 ? 0.125   -5.930  17.288 1.000 26.140 0  255 LEU A O   1 
ATOM   1988 C CB  . LEU A 1 255 ? -0.661  -6.281  14.217 1.000 26.530 0  255 LEU A CB  1 
ATOM   1989 C CG  . LEU A 1 255 ? -1.522  -6.586  12.995 1.000 28.160 0  255 LEU A CG  1 
ATOM   1990 C CD1 . LEU A 1 255 ? -2.978  -6.367  13.311 1.000 26.530 0  255 LEU A CD1 1 
ATOM   1991 C CD2 . LEU A 1 255 ? -1.095  -5.699  11.839 1.000 26.780 0  255 LEU A CD2 1 
ATOM   1992 N N   . ILE A 1 256 ? 1.729   -7.073  16.190 1.000 28.650 0  256 ILE A N   1 
ATOM   1993 C CA  . ILE A 1 256 ? 2.872   -6.355  16.744 1.000 26.490 0  256 ILE A CA  1 
ATOM   1994 C C   . ILE A 1 256 ? 3.412   -5.482  15.619 1.000 26.560 0  256 ILE A C   1 
ATOM   1995 O O   . ILE A 1 256 ? 3.944   -5.993  14.627 1.000 27.040 0  256 ILE A O   1 
ATOM   1996 C CB  . ILE A 1 256 ? 3.944   -7.305  17.290 1.000 26.670 0  256 ILE A CB  1 
ATOM   1997 C CG1 . ILE A 1 256 ? 3.361   -8.181  18.398 1.000 28.970 0  256 ILE A CG1 1 
ATOM   1998 C CG2 . ILE A 1 256 ? 5.124   -6.510  17.817 1.000 28.740 0  256 ILE A CG2 1 
ATOM   1999 C CD1 . ILE A 1 256 ? 4.406   -8.866  19.252 1.000 28.440 0  256 ILE A CD1 1 
ATOM   2000 N N   . THR A 1 257 ? 3.268   -4.165  15.757 1.000 26.350 0  257 THR A N   1 
ATOM   2001 C CA  . THR A 1 257 ? 3.396   -3.271  14.615 1.000 26.400 0  257 THR A CA  1 
ATOM   2002 C C   . THR A 1 257 ? 4.674   -2.448  14.583 1.000 26.430 0  257 THR A C   1 
ATOM   2003 O O   . THR A 1 257 ? 5.112   -2.073  13.494 1.000 26.590 0  257 THR A O   1 
ATOM   2004 C CB  . THR A 1 257 ? 2.200   -2.312  14.559 1.000 26.180 0  257 THR A CB  1 
ATOM   2005 O OG1 . THR A 1 257 ? 1.863   -1.885  15.885 1.000 25.920 0  257 THR A OG1 1 
ATOM   2006 C CG2 . THR A 1 257 ? 0.999   -2.995  13.934 1.000 26.260 0  257 THR A CG2 1 
ATOM   2007 N N   . GLU A 1 258 ? 5.281   -2.141  15.727 1.000 26.290 0  258 GLU A N   1 
ATOM   2008 C CA  . GLU A 1 258 ? 6.404   -1.203  15.765 1.000 28.820 0  258 GLU A CA  1 
ATOM   2009 C C   . GLU A 1 258 ? 7.432   -1.628  16.813 1.000 28.780 0  258 GLU A C   1 
ATOM   2010 O O   . GLU A 1 258 ? 7.842   -0.837  17.662 1.000 30.120 0  258 GLU A O   1 
ATOM   2011 C CB  . GLU A 1 258 ? 5.926   0.223   16.057 1.000 28.610 0  258 GLU A CB  1 
ATOM   2012 C CG  . GLU A 1 258 ? 4.686   0.690   15.299 1.000 28.890 0  258 GLU A CG  1 
ATOM   2013 C CD  . GLU A 1 258 ? 4.399   2.169   15.500 1.000 30.020 0  258 GLU A CD  1 
ATOM   2014 O OE1 . GLU A 1 258 ? 5.316   2.908   15.926 1.000 28.900 0  258 GLU A OE1 1 
ATOM   2015 O OE2 . GLU A 1 258 ? 3.250   2.590   15.236 1.000 26.980 -1 258 GLU A OE2 1 
ATOM   2016 N N   . PHE A 1 259 ? 7.866   -2.886  16.770 1.000 27.610 0  259 PHE A N   1 
ATOM   2017 C CA  . PHE A 1 259 ? 8.679   -3.411  17.862 1.000 26.800 0  259 PHE A CA  1 
ATOM   2018 C C   . PHE A 1 259 ? 10.070  -2.782  17.896 1.000 28.250 0  259 PHE A C   1 
ATOM   2019 O O   . PHE A 1 259 ? 10.745  -2.667  16.867 1.000 26.920 0  259 PHE A O   1 
ATOM   2020 C CB  . PHE A 1 259 ? 8.806   -4.931  17.762 1.000 26.850 0  259 PHE A CB  1 
ATOM   2021 C CG  . PHE A 1 259 ? 9.612   -5.544  18.880 1.000 28.350 0  259 PHE A CG  1 
ATOM   2022 C CD1 . PHE A 1 259 ? 9.004   -5.905  20.072 1.000 27.750 0  259 PHE A CD1 1 
ATOM   2023 C CD2 . PHE A 1 259 ? 10.978  -5.752  18.742 1.000 28.890 0  259 PHE A CD2 1 
ATOM   2024 C CE1 . PHE A 1 259 ? 9.740   -6.466  21.104 1.000 26.860 0  259 PHE A CE1 1 
ATOM   2025 C CE2 . PHE A 1 259 ? 11.718  -6.311  19.772 1.000 28.240 0  259 PHE A CE2 1 
ATOM   2026 C CZ  . PHE A 1 259 ? 11.097  -6.668  20.953 1.000 27.120 0  259 PHE A CZ  1 
ATOM   2027 N N   . ASP A 1 260 ? 10.479  -2.375  19.095 1.000 29.840 0  260 ASP A N   1 
ATOM   2028 C CA  . ASP A 1 260 ? 11.857  -2.086  19.482 1.000 29.790 0  260 ASP A CA  1 
ATOM   2029 C C   . ASP A 1 260 ? 11.868  -2.005  21.005 1.000 29.940 0  260 ASP A C   1 
ATOM   2030 O O   . ASP A 1 260 ? 10.813  -1.979  21.645 1.000 29.550 0  260 ASP A O   1 
ATOM   2031 C CB  . ASP A 1 260 ? 12.407  -0.806  18.836 1.000 28.730 0  260 ASP A CB  1 
ATOM   2032 C CG  . ASP A 1 260 ? 11.451  0.372   18.935 1.000 30.120 0  260 ASP A CG  1 
ATOM   2033 O OD1 . ASP A 1 260 ? 10.874  0.597   20.020 1.000 28.570 0  260 ASP A OD1 1 
ATOM   2034 O OD2 . ASP A 1 260 ? 11.290  1.088   17.923 1.000 29.930 -1 260 ASP A OD2 1 
ATOM   2035 N N   . VAL A 1 261 ? 13.066  -1.968  21.583 1.000 28.270 0  261 VAL A N   1 
ATOM   2036 C CA  . VAL A 1 261 ? 13.240  -2.086  23.030 1.000 28.260 0  261 VAL A CA  1 
ATOM   2037 C C   . VAL A 1 261 ? 14.029  -0.884  23.533 1.000 29.120 0  261 VAL A C   1 
ATOM   2038 O O   . VAL A 1 261 ? 15.226  -0.754  23.248 1.000 32.540 0  261 VAL A O   1 
ATOM   2039 C CB  . VAL A 1 261 ? 13.938  -3.396  23.419 1.000 30.330 0  261 VAL A CB  1 
ATOM   2040 C CG1 . VAL A 1 261 ? 13.755  -3.664  24.900 1.000 31.960 0  261 VAL A CG1 1 
ATOM   2041 C CG2 . VAL A 1 261 ? 13.392  -4.554  22.600 1.000 27.720 0  261 VAL A CG2 1 
ATOM   2042 N N   . ASN A 1 262 ? 13.375  -0.041  24.326 1.000 31.940 0  262 ASN A N   1 
ATOM   2043 C CA  . ASN A 1 262 ? 14.010  1.145   24.889 1.000 31.700 0  262 ASN A CA  1 
ATOM   2044 C C   . ASN A 1 262 ? 15.023  0.733   25.955 1.000 30.670 0  262 ASN A C   1 
ATOM   2045 O O   . ASN A 1 262 ? 14.654  0.145   26.976 1.000 30.730 0  262 ASN A O   1 
ATOM   2046 C CB  . ASN A 1 262 ? 12.938  2.060   25.478 1.000 32.040 0  262 ASN A CB  1 
ATOM   2047 C CG  . ASN A 1 262 ? 13.398  3.494   25.617 1.000 32.360 0  262 ASN A CG  1 
ATOM   2048 O OD1 . ASN A 1 262 ? 14.502  3.763   26.087 1.000 35.230 0  262 ASN A OD1 1 
ATOM   2049 N ND2 . ASN A 1 262 ? 12.545  4.429   25.216 1.000 30.690 0  262 ASN A ND2 1 
ATOM   2050 N N   . ASP A 1 263 ? 16.299  1.046   25.716 1.000 31.740 0  263 ASP A N   1 
ATOM   2051 C CA  . ASP A 1 263 ? 17.407  0.548   26.523 1.000 32.760 0  263 ASP A CA  1 
ATOM   2052 C C   . ASP A 1 263 ? 17.913  1.554   27.556 1.000 34.010 0  263 ASP A C   1 
ATOM   2053 O O   . ASP A 1 263 ? 19.031  1.402   28.062 1.000 36.760 0  263 ASP A O   1 
ATOM   2054 C CB  . ASP A 1 263 ? 18.537  0.090   25.586 1.000 33.360 0  263 ASP A CB  1 
ATOM   2055 C CG  . ASP A 1 263 ? 19.457  1.232   25.129 1.000 35.480 0  263 ASP A CG  1 
ATOM   2056 O OD1 . ASP A 1 263 ? 19.071  2.415   25.206 1.000 37.770 0  263 ASP A OD1 1 
ATOM   2057 O OD2 . ASP A 1 263 ? 20.559  0.940   24.623 1.000 34.680 -1 263 ASP A OD2 1 
ATOM   2058 N N   . LYS A 1 264 ? 17.109  2.557   27.904 1.000 32.350 0  264 LYS A N   1 
ATOM   2059 C CA  . LYS A 1 264 ? 17.611  3.655   28.722 1.000 35.660 0  264 LYS A CA  1 
ATOM   2060 C C   . LYS A 1 264 ? 17.792  3.278   30.191 1.000 37.610 0  264 LYS A C   1 
ATOM   2061 O O   . LYS A 1 264 ? 18.470  4.007   30.922 1.000 38.790 0  264 LYS A O   1 
ATOM   2062 C CB  . LYS A 1 264 ? 16.703  4.880   28.569 1.000 34.270 0  264 LYS A CB  1 
ATOM   2063 C CG  . LYS A 1 264 ? 15.698  5.117   29.674 1.000 38.470 0  264 LYS A CG  1 
ATOM   2064 C CD  . LYS A 1 264 ? 14.835  6.330   29.337 1.000 40.980 0  264 LYS A CD  1 
ATOM   2065 C CE  . LYS A 1 264 ? 15.701  7.537   28.987 1.000 45.330 0  264 LYS A CE  1 
ATOM   2066 N NZ  . LYS A 1 264 ? 14.990  8.837   29.173 1.000 47.610 1  264 LYS A NZ  1 
ATOM   2067 N N   . ALA A 1 265 ? 17.209  2.167   30.643 1.000 33.100 0  265 ALA A N   1 
ATOM   2068 C CA  . ALA A 1 265 ? 17.360  1.713   32.021 1.000 33.980 0  265 ALA A CA  1 
ATOM   2069 C C   . ALA A 1 265 ? 18.447  0.655   32.181 1.000 36.130 0  265 ALA A C   1 
ATOM   2070 O O   . ALA A 1 265 ? 18.580  0.075   33.263 1.000 35.330 0  265 ALA A O   1 
ATOM   2071 C CB  . ALA A 1 265 ? 16.029  1.170   32.547 1.000 30.710 0  265 ALA A CB  1 
ATOM   2072 N N   . PHE A 1 266 ? 19.218  0.391   31.137 1.000 34.110 0  266 PHE A N   1 
ATOM   2073 C CA  . PHE A 1 266 ? 20.213  -0.666  31.119 1.000 35.100 0  266 PHE A CA  1 
ATOM   2074 C C   . PHE A 1 266 ? 21.631  -0.093  31.057 1.000 34.980 0  266 PHE A C   1 
ATOM   2075 O O   . PHE A 1 266 ? 21.832  1.041   30.611 1.000 36.700 0  266 PHE A O   1 
ATOM   2076 C CB  . PHE A 1 266 ? 19.946  -1.598  29.928 1.000 35.440 0  266 PHE A CB  1 
ATOM   2077 C CG  . PHE A 1 266 ? 18.591  -2.245  29.958 1.000 31.520 0  266 PHE A CG  1 
ATOM   2078 C CD1 . PHE A 1 266 ? 17.958  -2.504  31.164 1.000 32.910 0  266 PHE A CD1 1 
ATOM   2079 C CD2 . PHE A 1 266 ? 17.950  -2.594  28.783 1.000 34.270 0  266 PHE A CD2 1 
ATOM   2080 C CE1 . PHE A 1 266 ? 16.711  -3.097  31.195 1.000 33.590 0  266 PHE A CE1 1 
ATOM   2081 C CE2 . PHE A 1 266 ? 16.701  -3.188  28.805 1.000 33.140 0  266 PHE A CE2 1 
ATOM   2082 C CZ  . PHE A 1 266 ? 16.080  -3.440  30.013 1.000 34.840 0  266 PHE A CZ  1 
ATOM   2083 N N   . PRO A 1 267 ? 22.637  -0.843  31.520 1.000 38.070 0  267 PRO A N   1 
ATOM   2084 C CA  . PRO A 1 267 ? 23.989  -0.276  31.666 1.000 38.670 0  267 PRO A CA  1 
ATOM   2085 C C   . PRO A 1 267 ? 24.592  0.225   30.360 1.000 38.350 0  267 PRO A C   1 
ATOM   2086 O O   . PRO A 1 267 ? 24.124  -0.077  29.262 1.000 39.060 0  267 PRO A O   1 
ATOM   2087 C CB  . PRO A 1 267 ? 24.813  -1.443  32.232 1.000 37.240 0  267 PRO A CB  1 
ATOM   2088 C CG  . PRO A 1 267 ? 23.825  -2.459  32.690 1.000 38.180 0  267 PRO A CG  1 
ATOM   2089 C CD  . PRO A 1 267 ? 22.596  -2.273  31.875 1.000 36.750 0  267 PRO A CD  1 
ATOM   2090 N N   . ALA A 1 268 ? 25.656  1.021   30.502 1.000 41.640 0  268 ALA A N   1 
ATOM   2091 C CA  . ALA A 1 268 ? 26.377  1.530   29.339 1.000 40.880 0  268 ALA A CA  1 
ATOM   2092 C C   . ALA A 1 268 ? 27.087  0.420   28.572 1.000 39.180 0  268 ALA A C   1 
ATOM   2093 O O   . ALA A 1 268 ? 27.241  0.517   27.348 1.000 38.890 0  268 ALA A O   1 
ATOM   2094 C CB  . ALA A 1 268 ? 27.385  2.592   29.777 1.000 38.550 0  268 ALA A CB  1 
ATOM   2095 N N   . ASP A 1 269 ? 27.539  -0.621  29.268 1.000 34.970 0  269 ASP A N   1 
ATOM   2096 C CA  . ASP A 1 269 ? 28.258  -1.709  28.618 1.000 39.000 0  269 ASP A CA  1 
ATOM   2097 C C   . ASP A 1 269 ? 27.412  -2.328  27.513 1.000 39.060 0  269 ASP A C   1 
ATOM   2098 O O   . ASP A 1 269 ? 26.265  -2.722  27.743 1.000 39.930 0  269 ASP A O   1 
ATOM   2099 C CB  . ASP A 1 269 ? 28.651  -2.766  29.651 1.000 40.830 0  269 ASP A CB  1 
ATOM   2100 C CG  . ASP A 1 269 ? 29.213  -4.026  29.018 1.000 39.930 0  269 ASP A CG  1 
ATOM   2101 O OD1 . ASP A 1 269 ? 28.411  -4.879  28.583 1.000 39.360 0  269 ASP A OD1 1 
ATOM   2102 O OD2 . ASP A 1 269 ? 30.451  -4.168  28.963 1.000 36.330 -1 269 ASP A OD2 1 
ATOM   2103 N N   . PHE A 1 270 ? 27.985  -2.410  26.308 1.000 39.490 0  270 PHE A N   1 
ATOM   2104 C CA  . PHE A 1 270 ? 27.232  -2.905  25.158 1.000 39.680 0  270 PHE A CA  1 
ATOM   2105 C C   . PHE A 1 270 ? 26.746  -4.332  25.389 1.000 38.380 0  270 PHE A C   1 
ATOM   2106 O O   . PHE A 1 270 ? 25.613  -4.673  25.034 1.000 39.150 0  270 PHE A O   1 
ATOM   2107 C CB  . PHE A 1 270 ? 28.083  -2.830  23.886 1.000 39.120 0  270 PHE A CB  1 
ATOM   2108 C CG  . PHE A 1 270 ? 28.163  -1.450  23.270 1.000 38.620 0  270 PHE A CG  1 
ATOM   2109 C CD1 . PHE A 1 270 ? 27.594  -0.353  23.897 1.000 40.340 0  270 PHE A CD1 1 
ATOM   2110 C CD2 . PHE A 1 270 ? 28.823  -1.253  22.065 1.000 38.830 0  270 PHE A CD2 1 
ATOM   2111 C CE1 . PHE A 1 270 ? 27.677  0.913   23.331 1.000 39.980 0  270 PHE A CE1 1 
ATOM   2112 C CE2 . PHE A 1 270 ? 28.907  0.009   21.494 1.000 37.940 0  270 PHE A CE2 1 
ATOM   2113 C CZ  . PHE A 1 270 ? 28.333  1.092   22.130 1.000 38.190 0  270 PHE A CZ  1 
ATOM   2114 N N   . ALA A 1 271 ? 27.583  -5.175  25.998 1.000 38.790 0  271 ALA A N   1 
ATOM   2115 C CA  . ALA A 1 271 ? 27.224  -6.578  26.188 1.000 37.040 0  271 ALA A CA  1 
ATOM   2116 C C   . ALA A 1 271 ? 26.112  -6.734  27.219 1.000 37.200 0  271 ALA A C   1 
ATOM   2117 O O   . ALA A 1 271 ? 25.136  -7.460  26.987 1.000 37.330 0  271 ALA A O   1 
ATOM   2118 C CB  . ALA A 1 271 ? 28.457  -7.382  26.598 1.000 34.710 0  271 ALA A CB  1 
ATOM   2119 N N   . LYS A 1 272 ? 26.248  -6.071  28.374 1.000 39.130 0  272 LYS A N   1 
ATOM   2120 C CA  . LYS A 1 272 ? 25.195  -6.134  29.386 1.000 38.920 0  272 LYS A CA  1 
ATOM   2121 C C   . LYS A 1 272 ? 23.885  -5.578  28.844 1.000 36.880 0  272 LYS A C   1 
ATOM   2122 O O   . LYS A 1 272 ? 22.809  -6.129  29.106 1.000 36.900 0  272 LYS A O   1 
ATOM   2123 C CB  . LYS A 1 272 ? 25.610  -5.369  30.647 1.000 40.510 0  272 LYS A CB  1 
ATOM   2124 C CG  . LYS A 1 272 ? 26.988  -5.708  31.203 1.000 41.260 0  272 LYS A CG  1 
ATOM   2125 C CD  . LYS A 1 272 ? 26.956  -5.771  32.727 1.000 41.020 0  272 LYS A CD  1 
ATOM   2126 C CE  . LYS A 1 272 ? 28.269  -5.311  33.344 1.000 38.440 0  272 LYS A CE  1 
ATOM   2127 N NZ  . LYS A 1 272 ? 28.056  -4.297  34.419 1.000 39.450 1  272 LYS A NZ  1 
ATOM   2128 N N   . ARG A 1 273 ? 23.960  -4.489  28.078 1.000 37.780 0  273 ARG A N   1 
ATOM   2129 C CA  . ARG A 1 273 ? 22.752  -3.893  27.519 1.000 38.060 0  273 ARG A CA  1 
ATOM   2130 C C   . ARG A 1 273 ? 22.104  -4.814  26.497 1.000 37.230 0  273 ARG A C   1 
ATOM   2131 O O   . ARG A 1 273 ? 20.872  -4.932  26.450 1.000 37.900 0  273 ARG A O   1 
ATOM   2132 C CB  . ARG A 1 273 ? 23.074  -2.541  26.896 1.000 36.320 0  273 ARG A CB  1 
ATOM   2133 C CG  . ARG A 1 273 ? 22.200  -1.454  27.434 1.000 35.580 0  273 ARG A CG  1 
ATOM   2134 C CD  . ARG A 1 273 ? 22.343  -0.175  26.668 1.000 36.500 0  273 ARG A CD  1 
ATOM   2135 N NE  . ARG A 1 273 ? 23.728  0.243   26.509 1.000 36.730 0  273 ARG A NE  1 
ATOM   2136 C CZ  . ARG A 1 273 ? 24.133  1.123   25.606 1.000 37.380 0  273 ARG A CZ  1 
ATOM   2137 N NH1 . ARG A 1 273 ? 23.278  1.713   24.787 1.000 37.590 1  273 ARG A NH1 1 
ATOM   2138 N NH2 . ARG A 1 273 ? 25.424  1.431   25.531 1.000 39.300 0  273 ARG A NH2 1 
ATOM   2139 N N   . ASP A 1 274 ? 22.916  -5.457  25.655 1.000 35.170 0  274 ASP A N   1 
ATOM   2140 C CA  . ASP A 1 274 ? 22.369  -6.401  24.690 1.000 36.040 0  274 ASP A CA  1 
ATOM   2141 C C   . ASP A 1 274 ? 21.692  -7.563  25.399 1.000 36.050 0  274 ASP A C   1 
ATOM   2142 O O   . ASP A 1 274 ? 20.606  -7.997  24.999 1.000 37.700 0  274 ASP A O   1 
ATOM   2143 C CB  . ASP A 1 274 ? 23.475  -6.909  23.768 1.000 37.400 0  274 ASP A CB  1 
ATOM   2144 C CG  . ASP A 1 274 ? 23.924  -5.868  22.772 1.000 36.080 0  274 ASP A CG  1 
ATOM   2145 O OD1 . ASP A 1 274 ? 23.164  -4.902  22.550 1.000 36.140 0  274 ASP A OD1 1 
ATOM   2146 O OD2 . ASP A 1 274 ? 25.033  -6.013  22.215 1.000 34.970 -1 274 ASP A OD2 1 
ATOM   2147 N N   . ALA A 1 275 ? 22.303  -8.053  26.481 1.000 35.270 0  275 ALA A N   1 
ATOM   2148 C CA  . ALA A 1 275 ? 21.696  -9.143  27.240 1.000 35.060 0  275 ALA A CA  1 
ATOM   2149 C C   . ALA A 1 275 ? 20.382  -8.710  27.880 1.000 35.480 0  275 ALA A C   1 
ATOM   2150 O O   . ALA A 1 275 ? 19.407  -9.477  27.897 1.000 36.400 0  275 ALA A O   1 
ATOM   2151 C CB  . ALA A 1 275 ? 22.672  -9.645  28.302 1.000 36.260 0  275 ALA A CB  1 
ATOM   2152 N N   . ALA A 1 276 ? 20.323  -7.476  28.392 1.000 36.060 0  276 ALA A N   1 
ATOM   2153 C CA  . ALA A 1 276 ? 19.105  -7.016  29.051 1.000 33.990 0  276 ALA A CA  1 
ATOM   2154 C C   . ALA A 1 276 ? 17.978  -6.817  28.047 1.000 35.260 0  276 ALA A C   1 
ATOM   2155 O O   . ALA A 1 276 ? 16.833  -7.220  28.298 1.000 34.690 0  276 ALA A O   1 
ATOM   2156 C CB  . ALA A 1 276 ? 19.377  -5.724  29.820 1.000 32.830 0  276 ALA A CB  1 
ATOM   2157 N N   . THR A 1 277 ? 18.285  -6.216  26.892 1.000 36.180 0  277 THR A N   1 
ATOM   2158 C CA  . THR A 1 277 ? 17.276  -6.078  25.848 1.000 35.520 0  277 THR A CA  1 
ATOM   2159 C C   . THR A 1 277 ? 16.831  -7.435  25.325 1.000 35.530 0  277 THR A C   1 
ATOM   2160 O O   . THR A 1 277 ? 15.651  -7.620  25.009 1.000 36.510 0  277 THR A O   1 
ATOM   2161 C CB  . THR A 1 277 ? 17.806  -5.222  24.699 1.000 35.690 0  277 THR A CB  1 
ATOM   2162 O OG1 . THR A 1 277 ? 19.132  -5.649  24.358 1.000 36.850 0  277 THR A OG1 1 
ATOM   2163 C CG2 . THR A 1 277 ? 17.829  -3.752  25.095 1.000 33.310 0  277 THR A CG2 1 
ATOM   2164 N N   . ALA A 1 278 ? 17.742  -8.410  25.270 1.000 36.040 0  278 ALA A N   1 
ATOM   2165 C CA  . ALA A 1 278 ? 17.373  -9.735  24.785 1.000 34.990 0  278 ALA A CA  1 
ATOM   2166 C C   . ALA A 1 278 ? 16.420  -10.428 25.751 1.000 33.890 0  278 ALA A C   1 
ATOM   2167 O O   . ALA A 1 278 ? 15.396  -10.983 25.335 1.000 35.360 0  278 ALA A O   1 
ATOM   2168 C CB  . ALA A 1 278 ? 18.630  -10.577 24.560 1.000 34.960 0  278 ALA A CB  1 
ATOM   2169 N N   . ALA A 1 279 ? 16.739  -10.406 27.049 1.000 34.280 0  279 ALA A N   1 
ATOM   2170 C CA  . ALA A 1 279 ? 15.857  -11.033 28.032 1.000 32.400 0  279 ALA A CA  1 
ATOM   2171 C C   . ALA A 1 279 ? 14.500  -10.334 28.094 1.000 34.180 0  279 ALA A C   1 
ATOM   2172 O O   . ALA A 1 279 ? 13.456  -10.993 28.224 1.000 32.980 0  279 ALA A O   1 
ATOM   2173 C CB  . ALA A 1 279 ? 16.524  -11.041 29.405 1.000 28.980 0  279 ALA A CB  1 
ATOM   2174 N N   . LEU A 1 280 ? 14.491  -8.999  27.990 1.000 32.470 0  280 LEU A N   1 
ATOM   2175 C CA  . LEU A 1 280 ? 13.230  -8.266  28.014 1.000 32.690 0  280 LEU A CA  1 
ATOM   2176 C C   . LEU A 1 280 ? 12.378  -8.579  26.790 1.000 31.470 0  280 LEU A C   1 
ATOM   2177 O O   . LEU A 1 280 ? 11.158  -8.784  26.904 1.000 29.440 0  280 LEU A O   1 
ATOM   2178 C CB  . LEU A 1 280 ? 13.519  -6.771  28.106 1.000 31.490 0  280 LEU A CB  1 
ATOM   2179 C CG  . LEU A 1 280 ? 12.372  -5.778  27.971 1.000 34.230 0  280 LEU A CG  1 
ATOM   2180 C CD1 . LEU A 1 280 ? 11.204  -6.143  28.875 1.000 34.580 0  280 LEU A CD1 1 
ATOM   2181 C CD2 . LEU A 1 280 ? 12.905  -4.406  28.306 1.000 34.260 0  280 LEU A CD2 1 
ATOM   2182 N N   . ALA A 1 281 ? 13.002  -8.605  25.610 1.000 31.230 0  281 ALA A N   1 
ATOM   2183 C CA  . ALA A 1 281 ? 12.300  -9.009  24.398 1.000 30.530 0  281 ALA A CA  1 
ATOM   2184 C C   . ALA A 1 281 ? 11.728  -10.409 24.544 1.000 30.760 0  281 ALA A C   1 
ATOM   2185 O O   . ALA A 1 281 ? 10.572  -10.656 24.186 1.000 29.660 0  281 ALA A O   1 
ATOM   2186 C CB  . ALA A 1 281 ? 13.243  -8.931  23.197 1.000 30.340 0  281 ALA A CB  1 
ATOM   2187 N N   . ARG A 1 282 ? 12.529  -11.344 25.067 1.000 30.930 0  282 ARG A N   1 
ATOM   2188 C CA  . ARG A 1 282 ? 12.066  -12.718 25.233 1.000 31.030 0  282 ARG A CA  1 
ATOM   2189 C C   . ARG A 1 282 ? 10.837  -12.787 26.130 1.000 32.640 0  282 ARG A C   1 
ATOM   2190 O O   . ARG A 1 282 ? 9.838   -13.425 25.781 1.000 30.760 0  282 ARG A O   1 
ATOM   2191 C CB  . ARG A 1 282 ? 13.189  -13.582 25.806 1.000 31.230 0  282 ARG A CB  1 
ATOM   2192 C CG  . ARG A 1 282 ? 12.850  -15.062 25.908 1.000 30.500 0  282 ARG A CG  1 
ATOM   2193 C CD  . ARG A 1 282 ? 12.846  -15.714 24.539 1.000 32.670 0  282 ARG A CD  1 
ATOM   2194 N NE  . ARG A 1 282 ? 11.810  -16.731 24.408 1.000 32.480 0  282 ARG A NE  1 
ATOM   2195 C CZ  . ARG A 1 282 ? 12.038  -18.037 24.433 1.000 31.970 0  282 ARG A CZ  1 
ATOM   2196 N NH1 . ARG A 1 282 ? 13.260  -18.523 24.592 1.000 29.710 1  282 ARG A NH1 1 
ATOM   2197 N NH2 . ARG A 1 282 ? 11.018  -18.877 24.284 1.000 32.760 0  282 ARG A NH2 1 
ATOM   2198 N N   . ASP A 1 283 ? 10.898  -12.145 27.299 1.000 31.860 0  283 ASP A N   1 
ATOM   2199 C CA  . ASP A 1 283 ? 9.758   -12.145 28.217 1.000 30.270 0  283 ASP A CA  1 
ATOM   2200 C C   . ASP A 1 283 ? 8.506   -11.573 27.557 1.000 29.500 0  283 ASP A C   1 
ATOM   2201 O O   . ASP A 1 283 ? 7.446   -12.225 27.513 1.000 30.260 0  283 ASP A O   1 
ATOM   2202 C CB  . ASP A 1 283 ? 10.114  -11.354 29.475 1.000 34.410 0  283 ASP A CB  1 
ATOM   2203 C CG  . ASP A 1 283 ? 8.915   -11.097 30.359 1.000 35.890 0  283 ASP A CG  1 
ATOM   2204 O OD1 . ASP A 1 283 ? 8.462   -12.044 31.034 1.000 38.640 0  283 ASP A OD1 1 
ATOM   2205 O OD2 . ASP A 1 283 ? 8.426   -9.948  30.380 1.000 36.310 -1 283 ASP A OD2 1 
ATOM   2206 N N   . TYR A 1 284 ? 8.620   -10.351 27.020 1.000 31.640 0  284 TYR A N   1 
ATOM   2207 C CA  . TYR A 1 284 ? 7.449   -9.679  26.470 1.000 29.770 0  284 TYR A CA  1 
ATOM   2208 C C   . TYR A 1 284 ? 6.872   -10.458 25.298 1.000 30.240 0  284 TYR A C   1 
ATOM   2209 O O   . TYR A 1 284 ? 5.647   -10.588 25.168 1.000 30.220 0  284 TYR A O   1 
ATOM   2210 C CB  . TYR A 1 284 ? 7.803   -8.257  26.043 1.000 27.070 0  284 TYR A CB  1 
ATOM   2211 C CG  . TYR A 1 284 ? 6.740   -7.616  25.188 1.000 27.280 0  284 TYR A CG  1 
ATOM   2212 C CD1 . TYR A 1 284 ? 5.549   -7.173  25.745 1.000 28.760 0  284 TYR A CD1 1 
ATOM   2213 C CD2 . TYR A 1 284 ? 6.918   -7.464  23.820 1.000 29.110 0  284 TYR A CD2 1 
ATOM   2214 C CE1 . TYR A 1 284 ? 4.570   -6.592  24.969 1.000 27.130 0  284 TYR A CE1 1 
ATOM   2215 C CE2 . TYR A 1 284 ? 5.943   -6.883  23.034 1.000 27.480 0  284 TYR A CE2 1 
ATOM   2216 C CZ  . TYR A 1 284 ? 4.772   -6.449  23.614 1.000 26.570 0  284 TYR A CZ  1 
ATOM   2217 O OH  . TYR A 1 284 ? 3.799   -5.870  22.836 1.000 25.900 0  284 TYR A OH  1 
ATOM   2218 N N   . LEU A 1 285 ? 7.738   -10.983 24.430 1.000 28.120 0  285 LEU A N   1 
ATOM   2219 C CA  . LEU A 1 285 ? 7.254   -11.677 23.250 1.000 30.720 0  285 LEU A CA  1 
ATOM   2220 C C   . LEU A 1 285 ? 6.670   -13.030 23.618 1.000 31.130 0  285 LEU A C   1 
ATOM   2221 O O   . LEU A 1 285 ? 5.705   -13.471 22.989 1.000 30.280 0  285 LEU A O   1 
ATOM   2222 C CB  . LEU A 1 285 ? 8.377   -11.820 22.223 1.000 30.580 0  285 LEU A CB  1 
ATOM   2223 C CG  . LEU A 1 285 ? 8.765   -10.519 21.514 1.000 32.150 0  285 LEU A CG  1 
ATOM   2224 C CD1 . LEU A 1 285 ? 9.901   -10.751 20.532 1.000 27.710 0  285 LEU A CD1 1 
ATOM   2225 C CD2 . LEU A 1 285 ? 7.560   -9.904  20.816 1.000 29.450 0  285 LEU A CD2 1 
ATOM   2226 N N   . ASP A 1 286 ? 7.237   -13.708 24.622 1.000 32.070 0  286 ASP A N   1 
ATOM   2227 C CA  . ASP A 1 286 ? 6.647   -14.954 25.091 1.000 31.030 0  286 ASP A CA  1 
ATOM   2228 C C   . ASP A 1 286 ? 5.226   -14.726 25.573 1.000 31.900 0  286 ASP A C   1 
ATOM   2229 O O   . ASP A 1 286 ? 4.327   -15.527 25.289 1.000 33.070 0  286 ASP A O   1 
ATOM   2230 C CB  . ASP A 1 286 ? 7.484   -15.545 26.226 1.000 31.740 0  286 ASP A CB  1 
ATOM   2231 C CG  . ASP A 1 286 ? 8.738   -16.233 25.739 1.000 34.500 0  286 ASP A CG  1 
ATOM   2232 O OD1 . ASP A 1 286 ? 8.984   -16.259 24.515 1.000 35.630 0  286 ASP A OD1 1 
ATOM   2233 O OD2 . ASP A 1 286 ? 9.483   -16.751 26.598 1.000 36.760 -1 286 ASP A OD2 1 
ATOM   2234 N N   . VAL A 1 287 ? 4.995   -13.629 26.298 1.000 32.170 0  287 VAL A N   1 
ATOM   2235 C CA  . VAL A 1 287 ? 3.644   -13.379 26.795 1.000 31.210 0  287 VAL A CA  1 
ATOM   2236 C C   . VAL A 1 287 ? 2.710   -13.006 25.648 1.000 28.940 0  287 VAL A C   1 
ATOM   2237 O O   . VAL A 1 287 ? 1.636   -13.596 25.485 1.000 29.620 0  287 VAL A O   1 
ATOM   2238 C CB  . VAL A 1 287 ? 3.647   -12.297 27.887 1.000 30.780 0  287 VAL A CB  1 
ATOM   2239 C CG1 . VAL A 1 287 ? 2.256   -12.162 28.478 1.000 28.700 0  287 VAL A CG1 1 
ATOM   2240 C CG2 . VAL A 1 287 ? 4.647   -12.645 28.973 1.000 32.730 0  287 VAL A CG2 1 
ATOM   2241 N N   . THR A 1 288 ? 3.111   -12.034 24.827 1.000 29.210 0  288 THR A N   1 
ATOM   2242 C CA  . THR A 1 288 ? 2.193   -11.492 23.831 1.000 29.620 0  288 THR A CA  1 
ATOM   2243 C C   . THR A 1 288 ? 1.964   -12.443 22.659 1.000 30.990 0  288 THR A C   1 
ATOM   2244 O O   . THR A 1 288 ? 0.869   -12.457 22.085 1.000 33.090 0  288 THR A O   1 
ATOM   2245 C CB  . THR A 1 288 ? 2.719   -10.153 23.320 1.000 30.380 0  288 THR A CB  1 
ATOM   2246 O OG1 . THR A 1 288 ? 3.235   -9.396  24.422 1.000 31.470 0  288 THR A OG1 1 
ATOM   2247 C CG2 . THR A 1 288 ? 1.605   -9.368  22.658 1.000 29.100 0  288 THR A CG2 1 
ATOM   2248 N N   . LEU A 1 289 ? 2.961   -13.240 22.287 1.000 29.650 0  289 LEU A N   1 
ATOM   2249 C CA  . LEU A 1 289 ? 2.852   -14.097 21.114 1.000 30.550 0  289 LEU A CA  1 
ATOM   2250 C C   . LEU A 1 289 ? 2.107   -15.402 21.370 1.000 30.120 0  289 LEU A C   1 
ATOM   2251 O O   . LEU A 1 289 ? 1.824   -16.124 20.409 1.000 30.100 0  289 LEU A O   1 
ATOM   2252 C CB  . LEU A 1 289 ? 4.244   -14.417 20.565 1.000 31.560 0  289 LEU A CB  1 
ATOM   2253 C CG  . LEU A 1 289 ? 4.984   -13.319 19.800 1.000 29.050 0  289 LEU A CG  1 
ATOM   2254 C CD1 . LEU A 1 289 ? 6.289   -13.875 19.274 1.000 27.920 0  289 LEU A CD1 1 
ATOM   2255 C CD2 . LEU A 1 289 ? 4.131   -12.778 18.661 1.000 27.490 0  289 LEU A CD2 1 
ATOM   2256 N N   . SER A 1 290 ? 1.763   -15.716 22.618 1.000 30.270 0  290 SER A N   1 
ATOM   2257 C CA  . SER A 1 290 ? 0.972   -16.904 22.903 1.000 31.360 0  290 SER A CA  1 
ATOM   2258 C C   . SER A 1 290 ? -0.500  -16.738 22.533 1.000 32.960 0  290 SER A C   1 
ATOM   2259 O O   . SER A 1 290 ? -1.316  -17.595 22.892 1.000 34.690 0  290 SER A O   1 
ATOM   2260 C CB  . SER A 1 290 ? 1.092   -17.278 24.382 1.000 30.960 0  290 SER A CB  1 
ATOM   2261 O OG  . SER A 1 290 ? 0.342   -16.390 25.193 1.000 32.090 0  290 SER A OG  1 
ATOM   2262 N N   . TYR A 1 291 ? -0.847  -15.670 21.822 1.000 30.440 0  291 TYR A N   1 
ATOM   2263 C CA  . TYR A 1 291 ? -2.193  -15.487 21.315 1.000 28.740 0  291 TYR A CA  1 
ATOM   2264 C C   . TYR A 1 291 ? -2.205  -15.832 19.836 1.000 29.780 0  291 TYR A C   1 
ATOM   2265 O O   . TYR A 1 291 ? -1.651  -15.072 19.030 1.000 31.590 0  291 TYR A O   1 
ATOM   2266 C CB  . TYR A 1 291 ? -2.662  -14.052 21.542 1.000 29.340 0  291 TYR A CB  1 
ATOM   2267 C CG  . TYR A 1 291 ? -2.914  -13.756 23.000 1.000 30.590 0  291 TYR A CG  1 
ATOM   2268 C CD1 . TYR A 1 291 ? -1.877  -13.382 23.842 1.000 30.960 0  291 TYR A CD1 1 
ATOM   2269 C CD2 . TYR A 1 291 ? -4.185  -13.886 23.543 1.000 29.500 0  291 TYR A CD2 1 
ATOM   2270 C CE1 . TYR A 1 291 ? -2.102  -13.128 25.181 1.000 31.760 0  291 TYR A CE1 1 
ATOM   2271 C CE2 . TYR A 1 291 ? -4.419  -13.633 24.878 1.000 29.970 0  291 TYR A CE2 1 
ATOM   2272 C CZ  . TYR A 1 291 ? -3.375  -13.255 25.694 1.000 31.710 0  291 TYR A CZ  1 
ATOM   2273 O OH  . TYR A 1 291 ? -3.610  -13.003 27.027 1.000 31.290 0  291 TYR A OH  1 
ATOM   2274 N N   . PRO A 1 292 ? -2.804  -16.955 19.429 1.000 30.140 0  292 PRO A N   1 
ATOM   2275 C CA  . PRO A 1 292 ? -2.694  -17.389 18.028 1.000 29.640 0  292 PRO A CA  1 
ATOM   2276 C C   . PRO A 1 292 ? -3.371  -16.462 17.036 1.000 29.150 0  292 PRO A C   1 
ATOM   2277 O O   . PRO A 1 292 ? -3.264  -16.695 15.828 1.000 30.510 0  292 PRO A O   1 
ATOM   2278 C CB  . PRO A 1 292 ? -3.370  -18.770 18.037 1.000 28.890 0  292 PRO A CB  1 
ATOM   2279 C CG  . PRO A 1 292 ? -3.326  -19.208 19.466 1.000 28.010 0  292 PRO A CG  1 
ATOM   2280 C CD  . PRO A 1 292 ? -3.497  -17.953 20.259 1.000 29.370 0  292 PRO A CD  1 
ATOM   2281 N N   . THR A 1 293 ? -4.063  -15.426 17.499 1.000 31.330 0  293 THR A N   1 
ATOM   2282 C CA  . THR A 1 293 ? -4.695  -14.454 16.618 1.000 32.690 0  293 THR A CA  1 
ATOM   2283 C C   . THR A 1 293 ? -3.775  -13.296 16.266 1.000 31.990 0  293 THR A C   1 
ATOM   2284 O O   . THR A 1 293 ? -4.192  -12.391 15.536 1.000 34.300 0  293 THR A O   1 
ATOM   2285 C CB  . THR A 1 293 ? -5.975  -13.920 17.263 1.000 29.550 0  293 THR A CB  1 
ATOM   2286 O OG1 . THR A 1 293 ? -5.894  -14.094 18.682 1.000 32.270 0  293 THR A OG1 1 
ATOM   2287 C CG2 . THR A 1 293 ? -7.177  -14.678 16.739 1.000 31.160 0  293 THR A CG2 1 
ATOM   2288 N N   . CYS A 1 294 ? -2.547  -13.295 16.781 1.000 30.970 0  294 CYS A N   1 
ATOM   2289 C CA  . CYS A 1 294 ? -1.537  -12.296 16.435 1.000 30.270 0  294 CYS A CA  1 
ATOM   2290 C C   . CYS A 1 294 ? -0.764  -12.820 15.234 1.000 29.910 0  294 CYS A C   1 
ATOM   2291 O O   . CYS A 1 294 ? 0.226   -13.534 15.375 1.000 29.640 0  294 CYS A O   1 
ATOM   2292 C CB  . CYS A 1 294 ? -0.619  -12.017 17.618 1.000 30.110 0  294 CYS A CB  1 
ATOM   2293 S SG  . CYS A 1 294 ? 0.674   -10.795 17.277 1.000 34.740 0  294 CYS A SG  1 
ATOM   2294 N N   . ARG A 1 295 ? -1.234  -12.483 14.037 1.000 30.150 0  295 ARG A N   1 
ATOM   2295 C CA  . ARG A 1 295 ? -0.667  -13.016 12.805 1.000 30.240 0  295 ARG A CA  1 
ATOM   2296 C C   . ARG A 1 295 ? 0.395   -12.122 12.174 1.000 29.430 0  295 ARG A C   1 
ATOM   2297 O O   . ARG A 1 295 ? 0.915   -12.472 11.109 1.000 29.960 0  295 ARG A O   1 
ATOM   2298 C CB  . ARG A 1 295 ? -1.784  -13.279 11.790 1.000 30.930 0  295 ARG A CB  1 
ATOM   2299 C CG  . ARG A 1 295 ? -2.806  -14.291 12.277 1.000 32.610 0  295 ARG A CG  1 
ATOM   2300 C CD  . ARG A 1 295 ? -3.703  -14.783 11.151 1.000 32.270 0  295 ARG A CD  1 
ATOM   2301 N NE  . ARG A 1 295 ? -4.833  -15.551 11.660 1.000 32.700 0  295 ARG A NE  1 
ATOM   2302 C CZ  . ARG A 1 295 ? -5.834  -15.044 12.369 1.000 34.130 0  295 ARG A CZ  1 
ATOM   2303 N NH1 . ARG A 1 295 ? -5.900  -13.752 12.648 1.000 33.050 1  295 ARG A NH1 1 
ATOM   2304 N NH2 . ARG A 1 295 ? -6.795  -15.853 12.804 1.000 34.550 0  295 ARG A NH2 1 
ATOM   2305 N N   . ASP A 1 296 ? 0.730   -10.984 12.781 1.000 28.320 0  296 ASP A N   1 
ATOM   2306 C CA  . ASP A 1 296 ? 1.699   -10.075 12.184 1.000 28.000 0  296 ASP A CA  1 
ATOM   2307 C C   . ASP A 1 296 ? 2.669   -9.552  13.234 1.000 28.120 0  296 ASP A C   1 
ATOM   2308 O O   . ASP A 1 296 ? 2.282   -9.289  14.377 1.000 27.200 0  296 ASP A O   1 
ATOM   2309 C CB  . ASP A 1 296 ? 1.002   -8.903  11.479 1.000 29.690 0  296 ASP A CB  1 
ATOM   2310 C CG  . ASP A 1 296 ? 0.467   -9.286  10.108 1.000 31.880 0  296 ASP A CG  1 
ATOM   2311 O OD1 . ASP A 1 296 ? 1.250   -9.282  9.134  1.000 29.630 0  296 ASP A OD1 1 
ATOM   2312 O OD2 . ASP A 1 296 ? -0.740  -9.595  10.008 1.000 32.930 -1 296 ASP A OD2 1 
ATOM   2313 N N   . PHE A 1 297 ? 3.929   -9.399  12.826 1.000 29.110 0  297 PHE A N   1 
ATOM   2314 C CA  . PHE A 1 297 ? 5.013   -8.937  13.687 1.000 28.500 0  297 PHE A CA  1 
ATOM   2315 C C   . PHE A 1 297 ? 5.931   -8.069  12.838 1.000 29.830 0  297 PHE A C   1 
ATOM   2316 O O   . PHE A 1 297 ? 6.462   -8.536  11.826 1.000 31.660 0  297 PHE A O   1 
ATOM   2317 C CB  . PHE A 1 297 ? 5.769   -10.136 14.279 1.000 29.630 0  297 PHE A CB  1 
ATOM   2318 C CG  . PHE A 1 297 ? 6.873   -9.780  15.250 1.000 31.280 0  297 PHE A CG  1 
ATOM   2319 C CD1 . PHE A 1 297 ? 7.073   -8.481  15.688 1.000 30.340 0  297 PHE A CD1 1 
ATOM   2320 C CD2 . PHE A 1 297 ? 7.707   -10.774 15.739 1.000 35.440 0  297 PHE A CD2 1 
ATOM   2321 C CE1 . PHE A 1 297 ? 8.089   -8.180  16.576 1.000 31.590 0  297 PHE A CE1 1 
ATOM   2322 C CE2 . PHE A 1 297 ? 8.723   -10.479 16.630 1.000 33.230 0  297 PHE A CE2 1 
ATOM   2323 C CZ  . PHE A 1 297 ? 8.914   -9.182  17.050 1.000 31.850 0  297 PHE A CZ  1 
ATOM   2324 N N   . LEU A 1 298 ? 6.124   -6.814  13.247 1.000 27.420 0  298 LEU A N   1 
ATOM   2325 C CA  . LEU A 1 298 ? 6.974   -5.884  12.519 1.000 27.680 0  298 LEU A CA  1 
ATOM   2326 C C   . LEU A 1 298 ? 7.919   -5.164  13.468 1.000 27.760 0  298 LEU A C   1 
ATOM   2327 O O   . LEU A 1 298 ? 7.552   -4.842  14.603 1.000 27.670 0  298 LEU A O   1 
ATOM   2328 C CB  . LEU A 1 298 ? 6.134   -4.861  11.746 1.000 27.380 0  298 LEU A CB  1 
ATOM   2329 C CG  . LEU A 1 298 ? 5.297   -5.453  10.611 1.000 27.720 0  298 LEU A CG  1 
ATOM   2330 C CD1 . LEU A 1 298 ? 3.820   -5.472  10.985 1.000 27.330 0  298 LEU A CD1 1 
ATOM   2331 C CD2 . LEU A 1 298 ? 5.522   -4.685  9.323  1.000 27.730 0  298 LEU A CD2 1 
ATOM   2332 N N   . LEU A 1 299 ? 9.141   -4.923  12.999 1.000 27.600 0  299 LEU A N   1 
ATOM   2333 C CA  . LEU A 1 299 ? 10.129  -4.128  13.718 1.000 27.710 0  299 LEU A CA  1 
ATOM   2334 C C   . LEU A 1 299 ? 10.107  -2.696  13.204 1.000 27.670 0  299 LEU A C   1 
ATOM   2335 O O   . LEU A 1 299 ? 10.057  -2.469  11.992 1.000 27.920 0  299 LEU A O   1 
ATOM   2336 C CB  . LEU A 1 299 ? 11.531  -4.710  13.550 1.000 27.860 0  299 LEU A CB  1 
ATOM   2337 C CG  . LEU A 1 299 ? 11.681  -6.207  13.794 1.000 28.540 0  299 LEU A CG  1 
ATOM   2338 C CD1 . LEU A 1 299 ? 12.864  -6.753  13.008 1.000 29.000 0  299 LEU A CD1 1 
ATOM   2339 C CD2 . LEU A 1 299 ? 11.846  -6.472  15.279 1.000 28.350 0  299 LEU A CD2 1 
ATOM   2340 N N   . TRP A 1 300 ? 10.132  -1.730  14.122 1.000 27.100 0  300 TRP A N   1 
ATOM   2341 C CA  . TRP A 1 300 ? 10.225  -0.323  13.731 1.000 27.000 0  300 TRP A CA  1 
ATOM   2342 C C   . TRP A 1 300 ? 11.678  0.008   13.389 1.000 30.490 0  300 TRP A C   1 
ATOM   2343 O O   . TRP A 1 300 ? 12.377  0.740   14.093 1.000 29.650 0  300 TRP A O   1 
ATOM   2344 C CB  . TRP A 1 300 ? 9.680   0.588   14.817 1.000 29.700 0  300 TRP A CB  1 
ATOM   2345 C CG  . TRP A 1 300 ? 9.085   1.832   14.244 1.000 31.690 0  300 TRP A CG  1 
ATOM   2346 C CD1 . TRP A 1 300 ? 9.511   3.113   14.442 1.000 29.810 0  300 TRP A CD1 1 
ATOM   2347 C CD2 . TRP A 1 300 ? 7.972   1.910   13.349 1.000 28.900 0  300 TRP A CD2 1 
ATOM   2348 N NE1 . TRP A 1 300 ? 8.718   3.987   13.737 1.000 30.580 0  300 TRP A NE1 1 
ATOM   2349 C CE2 . TRP A 1 300 ? 7.765   3.272   13.058 1.000 30.340 0  300 TRP A CE2 1 
ATOM   2350 C CE3 . TRP A 1 300 ? 7.123   0.959   12.773 1.000 28.870 0  300 TRP A CE3 1 
ATOM   2351 C CZ2 . TRP A 1 300 ? 6.746   3.708   12.214 1.000 31.120 0  300 TRP A CZ2 1 
ATOM   2352 C CZ3 . TRP A 1 300 ? 6.113   1.392   11.937 1.000 29.250 0  300 TRP A CZ3 1 
ATOM   2353 C CH2 . TRP A 1 300 ? 5.933   2.755   11.664 1.000 31.700 0  300 TRP A CH2 1 
ATOM   2354 N N   . GLY A 1 301 ? 12.128  -0.556  12.270 1.000 30.390 0  301 GLY A N   1 
ATOM   2355 C CA  . GLY A 1 301 ? 13.531  -0.539  11.921 1.000 32.300 0  301 GLY A CA  1 
ATOM   2356 C C   . GLY A 1 301 ? 14.258  -1.698  12.566 1.000 34.450 0  301 GLY A C   1 
ATOM   2357 O O   . GLY A 1 301 ? 13.958  -2.064  13.706 1.000 34.690 0  301 GLY A O   1 
ATOM   2358 N N   . MET A 1 302 ? 15.206  -2.300  11.848 1.000 33.310 0  302 MET A N   1 
ATOM   2359 C CA  . MET A 1 302 ? 15.901  -3.483  12.336 1.000 33.620 0  302 MET A CA  1 
ATOM   2360 C C   . MET A 1 302 ? 17.385  -3.244  12.575 1.000 33.440 0  302 MET A C   1 
ATOM   2361 O O   . MET A 1 302 ? 18.109  -4.198  12.874 1.000 32.830 0  302 MET A O   1 
ATOM   2362 C CB  . MET A 1 302 ? 15.709  -4.653  11.371 1.000 32.880 0  302 MET A CB  1 
ATOM   2363 C CG  . MET A 1 302 ? 15.654  -4.253  9.915  1.000 33.730 0  302 MET A CG  1 
ATOM   2364 S SD  . MET A 1 302 ? 15.127  -5.644  8.907  1.000 35.180 0  302 MET A SD  1 
ATOM   2365 C CE  . MET A 1 302 ? 16.255  -6.909  9.476  1.000 34.470 0  302 MET A CE  1 
ATOM   2366 N N   . ALA A 1 303 ? 17.858  -2.007  12.441 1.000 33.790 0  303 ALA A N   1 
ATOM   2367 C CA  . ALA A 1 303 ? 19.237  -1.654  12.745 1.000 32.220 0  303 ALA A CA  1 
ATOM   2368 C C   . ALA A 1 303 ? 19.235  -0.477  13.710 1.000 32.880 0  303 ALA A C   1 
ATOM   2369 O O   . ALA A 1 303 ? 18.406  0.428   13.591 1.000 34.890 0  303 ALA A O   1 
ATOM   2370 C CB  . ALA A 1 303 ? 20.026  -1.305  11.483 1.000 34.410 0  303 ALA A CB  1 
ATOM   2371 N N   . ASP A 1 304 ? 20.152  -0.509  14.680 1.000 33.590 0  304 ASP A N   1 
ATOM   2372 C CA  . ASP A 1 304 ? 20.111  0.456   15.776 1.000 32.800 0  304 ASP A CA  1 
ATOM   2373 C C   . ASP A 1 304 ? 20.192  1.893   15.278 1.000 32.890 0  304 ASP A C   1 
ATOM   2374 O O   . ASP A 1 304 ? 19.455  2.762   15.755 1.000 33.860 0  304 ASP A O   1 
ATOM   2375 C CB  . ASP A 1 304 ? 21.237  0.171   16.764 1.000 32.620 0  304 ASP A CB  1 
ATOM   2376 C CG  . ASP A 1 304 ? 21.011  -1.104  17.545 1.000 33.070 0  304 ASP A CG  1 
ATOM   2377 O OD1 . ASP A 1 304 ? 19.873  -1.615  17.532 1.000 31.160 0  304 ASP A OD1 1 
ATOM   2378 O OD2 . ASP A 1 304 ? 21.973  -1.596  18.171 1.000 35.640 -1 304 ASP A OD2 1 
ATOM   2379 N N   . HIS A 1 305 ? 21.075  2.165   14.318 1.000 36.340 0  305 HIS A N   1 
ATOM   2380 C CA  . HIS A 1 305 ? 21.341  3.550   13.943 1.000 35.960 0  305 HIS A CA  1 
ATOM   2381 C C   . HIS A 1 305 ? 20.188  4.193   13.179 1.000 34.910 0  305 HIS A C   1 
ATOM   2382 O O   . HIS A 1 305 ? 20.137  5.424   13.091 1.000 39.080 0  305 HIS A O   1 
ATOM   2383 C CB  . HIS A 1 305 ? 22.627  3.640   13.124 1.000 33.300 0  305 HIS A CB  1 
ATOM   2384 C CG  . HIS A 1 305 ? 22.505  3.086   11.740 1.000 37.010 0  305 HIS A CG  1 
ATOM   2385 N ND1 . HIS A 1 305 ? 22.554  1.734   11.472 1.000 37.150 0  305 HIS A ND1 1 
ATOM   2386 C CD2 . HIS A 1 305 ? 22.350  3.701   10.543 1.000 36.330 0  305 HIS A CD2 1 
ATOM   2387 C CE1 . HIS A 1 305 ? 22.428  1.540   10.171 1.000 36.280 0  305 HIS A CE1 1 
ATOM   2388 N NE2 . HIS A 1 305 ? 22.304  2.718   9.585  1.000 36.060 0  305 HIS A NE2 1 
ATOM   2389 N N   . VAL A 1 306 ? 19.268  3.404   12.616 1.000 32.000 0  306 VAL A N   1 
ATOM   2390 C CA  . VAL A 1 306 ? 18.132  3.963   11.892 1.000 34.230 0  306 VAL A CA  1 
ATOM   2391 C C   . VAL A 1 306 ? 16.879  4.048   12.746 1.000 35.330 0  306 VAL A C   1 
ATOM   2392 O O   . VAL A 1 306 ? 15.839  4.514   12.261 1.000 34.460 0  306 VAL A O   1 
ATOM   2393 C CB  . VAL A 1 306 ? 17.836  3.168   10.603 1.000 35.610 0  306 VAL A CB  1 
ATOM   2394 C CG1 . VAL A 1 306 ? 19.028  3.208   9.666  1.000 34.080 0  306 VAL A CG1 1 
ATOM   2395 C CG2 . VAL A 1 306 ? 17.440  1.738   10.925 1.000 35.750 0  306 VAL A CG2 1 
ATOM   2396 N N   . ASN A 1 307 ? 16.942  3.619   14.002 1.000 35.650 0  307 ASN A N   1 
ATOM   2397 C CA  . ASN A 1 307 ? 15.755  3.592   14.842 1.000 33.600 0  307 ASN A CA  1 
ATOM   2398 C C   . ASN A 1 307 ? 15.443  4.977   15.393 1.000 34.790 0  307 ASN A C   1 
ATOM   2399 O O   . ASN A 1 307 ? 16.343  5.738   15.758 1.000 32.970 0  307 ASN A O   1 
ATOM   2400 C CB  . ASN A 1 307 ? 15.936  2.601   15.988 1.000 34.150 0  307 ASN A CB  1 
ATOM   2401 C CG  . ASN A 1 307 ? 14.678  2.436   16.806 1.000 32.690 0  307 ASN A CG  1 
ATOM   2402 O OD1 . ASN A 1 307 ? 14.583  2.943   17.917 1.000 31.440 0  307 ASN A OD1 1 
ATOM   2403 N ND2 . ASN A 1 307 ? 13.698  1.732   16.253 1.000 31.840 0  307 ASN A ND2 1 
ATOM   2404 N N   . TRP A 1 308 ? 14.147  5.293   15.456 1.000 35.990 0  308 TRP A N   1 
ATOM   2405 C CA  . TRP A 1 308 ? 13.693  6.608   15.894 1.000 34.450 0  308 TRP A CA  1 
ATOM   2406 C C   . TRP A 1 308 ? 14.101  6.926   17.327 1.000 36.190 0  308 TRP A C   1 
ATOM   2407 O O   . TRP A 1 308 ? 14.191  8.107   17.682 1.000 37.450 0  308 TRP A O   1 
ATOM   2408 C CB  . TRP A 1 308 ? 12.171  6.702   15.750 1.000 33.760 0  308 TRP A CB  1 
ATOM   2409 C CG  . TRP A 1 308 ? 11.428  5.839   16.723 1.000 33.700 0  308 TRP A CG  1 
ATOM   2410 C CD1 . TRP A 1 308 ? 11.433  4.476   16.773 1.000 34.000 0  308 TRP A CD1 1 
ATOM   2411 C CD2 . TRP A 1 308 ? 10.554  6.275   17.772 1.000 36.810 0  308 TRP A CD2 1 
ATOM   2412 N NE1 . TRP A 1 308 ? 10.629  4.036   17.796 1.000 34.170 0  308 TRP A NE1 1 
ATOM   2413 C CE2 . TRP A 1 308 ? 10.076  5.121   18.424 1.000 35.310 0  308 TRP A CE2 1 
ATOM   2414 C CE3 . TRP A 1 308 ? 10.134  7.529   18.229 1.000 37.640 0  308 TRP A CE3 1 
ATOM   2415 C CZ2 . TRP A 1 308 ? 9.198   5.183   19.505 1.000 35.240 0  308 TRP A CZ2 1 
ATOM   2416 C CZ3 . TRP A 1 308 ? 9.263   7.589   19.302 1.000 37.760 0  308 TRP A CZ3 1 
ATOM   2417 C CH2 . TRP A 1 308 ? 8.803   6.423   19.927 1.000 36.610 0  308 TRP A CH2 1 
ATOM   2418 N N   . LEU A 1 309 ? 14.353  5.913   18.158 1.000 35.560 0  309 LEU A N   1 
ATOM   2419 C CA  . LEU A 1 309 ? 14.708  6.178   19.548 1.000 35.950 0  309 LEU A CA  1 
ATOM   2420 C C   . LEU A 1 309 ? 16.052  6.879   19.686 1.000 38.370 0  309 LEU A C   1 
ATOM   2421 O O   . LEU A 1 309 ? 16.361  7.372   20.777 1.000 40.840 0  309 LEU A O   1 
ATOM   2422 C CB  . LEU A 1 309 ? 14.724  4.880   20.358 1.000 34.560 0  309 LEU A CB  1 
ATOM   2423 C CG  . LEU A 1 309 ? 13.393  4.136   20.509 1.000 35.020 0  309 LEU A CG  1 
ATOM   2424 C CD1 . LEU A 1 309 ? 13.626  2.742   21.065 1.000 32.450 0  309 LEU A CD1 1 
ATOM   2425 C CD2 . LEU A 1 309 ? 12.416  4.912   21.382 1.000 36.340 0  309 LEU A CD2 1 
ATOM   2426 N N   . GLN A 1 310 ? 16.849  6.944   18.616 1.000 35.110 0  310 GLN A N   1 
ATOM   2427 C CA  . GLN A 1 310 ? 18.138  7.617   18.686 1.000 36.430 0  310 GLN A CA  1 
ATOM   2428 C C   . GLN A 1 310 ? 18.001  9.132   18.780 1.000 39.960 0  310 GLN A C   1 
ATOM   2429 O O   . GLN A 1 310 ? 18.913  9.791   19.291 1.000 39.620 0  310 GLN A O   1 
ATOM   2430 C CB  . GLN A 1 310 ? 18.984  7.264   17.458 1.000 34.000 0  310 GLN A CB  1 
ATOM   2431 C CG  . GLN A 1 310 ? 19.299  5.777   17.282 1.000 34.670 0  310 GLN A CG  1 
ATOM   2432 C CD  . GLN A 1 310 ? 20.414  5.291   18.190 1.000 33.550 0  310 GLN A CD  1 
ATOM   2433 O OE1 . GLN A 1 310 ? 20.972  6.057   18.971 1.000 34.710 0  310 GLN A OE1 1 
ATOM   2434 N NE2 . GLN A 1 310 ? 20.751  4.009   18.081 1.000 30.170 0  310 GLN A NE2 1 
ATOM   2435 N N   . VAL A 1 311 ? 16.889  9.702   18.306 1.000 39.060 0  311 VAL A N   1 
ATOM   2436 C CA  . VAL A 1 311 ? 16.758  11.154  18.212 1.000 41.480 0  311 VAL A CA  1 
ATOM   2437 C C   . VAL A 1 311 ? 15.534  11.668  18.962 1.000 45.150 0  311 VAL A C   1 
ATOM   2438 O O   . VAL A 1 311 ? 15.502  12.834  19.373 1.000 46.960 0  311 VAL A O   1 
ATOM   2439 C CB  . VAL A 1 311 ? 16.713  11.604  16.739 1.000 42.560 0  311 VAL A CB  1 
ATOM   2440 C CG1 . VAL A 1 311 ? 18.059  11.367  16.074 1.000 40.230 0  311 VAL A CG1 1 
ATOM   2441 C CG2 . VAL A 1 311 ? 15.603  10.882  15.990 1.000 39.280 0  311 VAL A CG2 1 
ATOM   2442 N N   . TRP A 1 312 ? 14.516  10.826  19.121 1.000 43.800 0  312 TRP A N   1 
ATOM   2443 C CA  . TRP A 1 312 ? 13.330  11.206  19.883 1.000 44.220 0  312 TRP A CA  1 
ATOM   2444 C C   . TRP A 1 312 ? 13.754  11.623  21.287 1.000 45.790 0  312 TRP A C   1 
ATOM   2445 O O   . TRP A 1 312 ? 14.329  10.803  22.019 1.000 47.530 0  312 TRP A O   1 
ATOM   2446 C CB  . TRP A 1 312 ? 12.332  10.052  19.932 1.000 44.900 0  312 TRP A CB  1 
ATOM   2447 C CG  . TRP A 1 312 ? 10.973  10.427  20.455 1.000 44.330 0  312 TRP A CG  1 
ATOM   2448 C CD1 . TRP A 1 312 ? 10.103  11.330  19.914 1.000 44.850 0  312 TRP A CD1 1 
ATOM   2449 C CD2 . TRP A 1 312 ? 10.318  9.879   21.606 1.000 42.750 0  312 TRP A CD2 1 
ATOM   2450 N NE1 . TRP A 1 312 ? 8.954   11.390  20.667 1.000 46.210 0  312 TRP A NE1 1 
ATOM   2451 C CE2 . TRP A 1 312 ? 9.061   10.508  21.710 1.000 43.790 0  312 TRP A CE2 1 
ATOM   2452 C CE3 . TRP A 1 312 ? 10.677  8.924   22.562 1.000 46.950 0  312 TRP A CE3 1 
ATOM   2453 C CZ2 . TRP A 1 312 ? 8.162   10.212  22.732 1.000 47.230 0  312 TRP A CZ2 1 
ATOM   2454 C CZ3 . TRP A 1 312 ? 9.781   8.630   23.576 1.000 46.260 0  312 TRP A CZ3 1 
ATOM   2455 C CH2 . TRP A 1 312 ? 8.540   9.273   23.653 1.000 48.600 0  312 TRP A CH2 1 
ATOM   2456 N N   . PRO A 1 313 ? 13.478  12.861  21.708 1.000 45.030 0  313 PRO A N   1 
ATOM   2457 C CA  . PRO A 1 313 ? 14.172  13.401  22.890 1.000 46.320 0  313 PRO A CA  1 
ATOM   2458 C C   . PRO A 1 313 ? 13.810  12.721  24.197 1.000 46.490 0  313 PRO A C   1 
ATOM   2459 O O   . PRO A 1 313 ? 14.672  12.611  25.077 1.000 47.220 0  313 PRO A O   1 
ATOM   2460 C CB  . PRO A 1 313 ? 13.756  14.879  22.889 1.000 45.520 0  313 PRO A CB  1 
ATOM   2461 C CG  . PRO A 1 313 ? 12.434  14.892  22.209 1.000 47.340 0  313 PRO A CG  1 
ATOM   2462 C CD  . PRO A 1 313 ? 12.465  13.792  21.181 1.000 46.180 0  313 PRO A CD  1 
ATOM   2463 N N   . ASP A 1 314 ? 12.577  12.242  24.356 1.000 46.300 0  314 ASP A N   1 
ATOM   2464 C CA  . ASP A 1 314 ? 12.188  11.647  25.627 1.000 45.680 0  314 ASP A CA  1 
ATOM   2465 C C   . ASP A 1 314 ? 12.949  10.365  25.934 1.000 46.660 0  314 ASP A C   1 
ATOM   2466 O O   . ASP A 1 314 ? 12.799  9.825   27.035 1.000 48.730 0  314 ASP A O   1 
ATOM   2467 C CB  . ASP A 1 314 ? 10.685  11.373  25.634 1.000 46.360 0  314 ASP A CB  1 
ATOM   2468 C CG  . ASP A 1 314 ? 9.873   12.597  25.267 1.000 48.990 0  314 ASP A CG  1 
ATOM   2469 O OD1 . ASP A 1 314 ? 10.434  13.715  25.293 1.000 47.210 0  314 ASP A OD1 1 
ATOM   2470 O OD2 . ASP A 1 314 ? 8.674   12.442  24.951 1.000 53.150 -1 314 ASP A OD2 1 
ATOM   2471 N N   . ALA A 1 315 ? 13.766  9.877   25.000 1.000 47.100 0  315 ALA A N   1 
ATOM   2472 C CA  . ALA A 1 315 ? 14.450  8.601   25.148 1.000 45.480 0  315 ALA A CA  1 
ATOM   2473 C C   . ALA A 1 315 ? 15.967  8.733   25.132 1.000 45.760 0  315 ALA A C   1 
ATOM   2474 O O   . ALA A 1 315 ? 16.664  7.712   25.085 1.000 44.920 0  315 ALA A O   1 
ATOM   2475 C CB  . ALA A 1 315 ? 14.002  7.628   24.052 1.000 44.240 0  315 ALA A CB  1 
ATOM   2476 N N   . LYS A 1 316 ? 16.502  9.954   25.160 1.000 47.160 0  316 LYS A N   1 
ATOM   2477 C CA  . LYS A 1 316 ? 17.948  10.117  25.243 1.000 43.920 0  316 LYS A CA  1 
ATOM   2478 C C   . LYS A 1 316 ? 18.466  9.555   26.561 1.000 46.280 0  316 LYS A C   1 
ATOM   2479 O O   . LYS A 1 316 ? 17.812  9.664   27.604 1.000 47.730 0  316 LYS A O   1 
ATOM   2480 C CB  . LYS A 1 316 ? 18.342  11.590  25.109 1.000 42.680 0  316 LYS A CB  1 
ATOM   2481 C CG  . LYS A 1 316 ? 19.854  11.802  25.036 1.000 44.870 0  316 LYS A CG  1 
ATOM   2482 C CD  . LYS A 1 316 ? 20.235  13.095  24.335 1.000 44.640 0  316 LYS A CD  1 
ATOM   2483 C CE  . LYS A 1 316 ? 20.536  14.189  25.346 1.000 45.350 0  316 LYS A CE  1 
ATOM   2484 N NZ  . LYS A 1 316 ? 21.224  13.645  26.551 1.000 49.030 1  316 LYS A NZ  1 
ATOM   2485 N N   . ARG A 1 317 ? 19.653  8.952   26.511 1.000 43.920 0  317 ARG A N   1 
ATOM   2486 C CA  . ARG A 1 317 ? 20.230  8.308   27.680 1.000 43.730 0  317 ARG A CA  1 
ATOM   2487 C C   . ARG A 1 317 ? 21.027  9.311   28.508 1.000 45.720 0  317 ARG A C   1 
ATOM   2488 O O   . ARG A 1 317 ? 21.581  10.273  27.966 1.000 46.340 0  317 ARG A O   1 
ATOM   2489 C CB  . ARG A 1 317 ? 21.134  7.161   27.250 1.000 41.860 0  317 ARG A CB  1 
ATOM   2490 C CG  . ARG A 1 317 ? 20.374  5.960   26.739 1.000 39.190 0  317 ARG A CG  1 
ATOM   2491 C CD  . ARG A 1 317 ? 21.320  4.912   26.199 1.000 38.480 0  317 ARG A CD  1 
ATOM   2492 N NE  . ARG A 1 317 ? 22.383  4.605   27.145 1.000 38.350 0  317 ARG A NE  1 
ATOM   2493 C CZ  . ARG A 1 317 ? 22.369  3.564   27.966 1.000 40.830 0  317 ARG A CZ  1 
ATOM   2494 N NH1 . ARG A 1 317 ? 21.340  2.733   28.010 1.000 36.930 1  317 ARG A NH1 1 
ATOM   2495 N NH2 . ARG A 1 317 ? 23.412  3.353   28.763 1.000 41.330 0  317 ARG A NH2 1 
ATOM   2496 N N   . PRO A 1 318 ? 21.087  9.114   29.830 1.000 45.960 0  318 PRO A N   1 
ATOM   2497 C CA  . PRO A 1 318 ? 21.860  10.049  30.667 1.000 45.790 0  318 PRO A CA  1 
ATOM   2498 C C   . PRO A 1 318 ? 23.325  10.141  30.270 1.000 44.230 0  318 PRO A C   1 
ATOM   2499 O O   . PRO A 1 318 ? 23.886  11.243  30.240 1.000 44.290 0  318 PRO A O   1 
ATOM   2500 C CB  . PRO A 1 318 ? 21.677  9.477   32.080 1.000 44.930 0  318 PRO A CB  1 
ATOM   2501 C CG  . PRO A 1 318 ? 20.394  8.709   32.012 1.000 41.380 0  318 PRO A CG  1 
ATOM   2502 C CD  . PRO A 1 318 ? 20.363  8.115   30.636 1.000 44.100 0  318 PRO A CD  1 
ATOM   2503 N N   . ASP A 1 319 ? 23.963  9.016   29.957 1.000 43.380 0  319 ASP A N   1 
ATOM   2504 C CA  . ASP A 1 319 ? 25.238  9.075   29.266 1.000 43.920 0  319 ASP A CA  1 
ATOM   2505 C C   . ASP A 1 319 ? 24.999  9.371   27.790 1.000 43.520 0  319 ASP A C   1 
ATOM   2506 O O   . ASP A 1 319 ? 23.909  9.155   27.257 1.000 45.340 0  319 ASP A O   1 
ATOM   2507 C CB  . ASP A 1 319 ? 26.022  7.769   29.431 1.000 41.530 0  319 ASP A CB  1 
ATOM   2508 C CG  . ASP A 1 319 ? 25.211  6.539   29.049 1.000 43.030 0  319 ASP A CG  1 
ATOM   2509 O OD1 . ASP A 1 319 ? 24.006  6.672   28.755 1.000 45.690 0  319 ASP A OD1 1 
ATOM   2510 O OD2 . ASP A 1 319 ? 25.788  5.430   29.040 1.000 41.110 -1 319 ASP A OD2 1 
ATOM   2511 N N   . GLY A 1 320 ? 26.032  9.868   27.123 1.000 42.000 0  320 GLY A N   1 
ATOM   2512 C CA  . GLY A 1 320 ? 25.852  10.312  25.754 1.000 44.510 0  320 GLY A CA  1 
ATOM   2513 C C   . GLY A 1 320 ? 25.652  9.184   24.762 1.000 43.240 0  320 GLY A C   1 
ATOM   2514 O O   . GLY A 1 320 ? 25.586  9.419   23.552 1.000 43.270 0  320 GLY A O   1 
ATOM   2515 N N   . LEU A 1 321 ? 25.529  7.957   25.262 1.000 44.330 0  321 LEU A N   1 
ATOM   2516 C CA  . LEU A 1 321 ? 25.608  6.787   24.402 1.000 43.520 0  321 LEU A CA  1 
ATOM   2517 C C   . LEU A 1 321 ? 24.338  6.612   23.577 1.000 40.370 0  321 LEU A C   1 
ATOM   2518 O O   . LEU A 1 321 ? 23.235  6.971   24.001 1.000 39.050 0  321 LEU A O   1 
ATOM   2519 C CB  . LEU A 1 321 ? 25.862  5.530   25.233 1.000 40.450 0  321 LEU A CB  1 
ATOM   2520 C CG  . LEU A 1 321 ? 27.151  5.499   26.055 1.000 43.480 0  321 LEU A CG  1 
ATOM   2521 C CD1 . LEU A 1 321 ? 27.477  4.071   26.463 1.000 42.960 0  321 LEU A CD1 1 
ATOM   2522 C CD2 . LEU A 1 321 ? 28.310  6.121   25.288 1.000 39.400 0  321 LEU A CD2 1 
ATOM   2523 N N   . ALA A 1 322 ? 24.514  6.060   22.380 1.000 38.410 0  322 ALA A N   1 
ATOM   2524 C CA  . ALA A 1 322 ? 23.404  5.761   21.492 1.000 34.580 0  322 ALA A CA  1 
ATOM   2525 C C   . ALA A 1 322 ? 22.656  4.517   21.960 1.000 34.590 0  322 ALA A C   1 
ATOM   2526 O O   . ALA A 1 322 ? 23.244  3.577   22.499 1.000 32.990 0  322 ALA A O   1 
ATOM   2527 C CB  . ALA A 1 322 ? 23.909  5.560   20.061 1.000 29.240 0  322 ALA A CB  1 
ATOM   2528 N N   . GLN A 1 323 ? 21.343  4.520   21.740 1.000 33.380 0  323 GLN A N   1 
ATOM   2529 C CA  . GLN A 1 323 ? 20.529  3.358   22.061 1.000 33.370 0  323 GLN A CA  1 
ATOM   2530 C C   . GLN A 1 323 ? 20.884  2.178   21.162 1.000 33.700 0  323 GLN A C   1 
ATOM   2531 O O   . GLN A 1 323 ? 21.332  2.346   20.023 1.000 33.350 0  323 GLN A O   1 
ATOM   2532 C CB  . GLN A 1 323 ? 19.042  3.689   21.916 1.000 33.280 0  323 GLN A CB  1 
ATOM   2533 C CG  . GLN A 1 323 ? 18.499  4.630   22.983 1.000 35.850 0  323 GLN A CG  1 
ATOM   2534 C CD  . GLN A 1 323 ? 17.219  4.116   23.629 1.000 36.780 0  323 GLN A CD  1 
ATOM   2535 O OE1 . GLN A 1 323 ? 16.909  2.924   23.565 1.000 33.240 0  323 GLN A OE1 1 
ATOM   2536 N NE2 . GLN A 1 323 ? 16.467  5.017   24.253 1.000 37.150 0  323 GLN A NE2 1 
ATOM   2537 N N   . ARG A 1 324 ? 20.681  0.971   21.689 1.000 34.060 0  324 ARG A N   1 
ATOM   2538 C CA  . ARG A 1 324 ? 20.856  -0.275  20.944 1.000 31.750 0  324 ARG A CA  1 
ATOM   2539 C C   . ARG A 1 324 ? 19.546  -1.061  20.972 1.000 32.470 0  324 ARG A C   1 
ATOM   2540 O O   . ARG A 1 324 ? 19.478  -2.156  21.547 1.000 34.610 0  324 ARG A O   1 
ATOM   2541 C CB  . ARG A 1 324 ? 22.006  -1.103  21.513 1.000 31.060 0  324 ARG A CB  1 
ATOM   2542 C CG  . ARG A 1 324 ? 23.372  -0.447  21.365 1.000 33.460 0  324 ARG A CG  1 
ATOM   2543 C CD  . ARG A 1 324 ? 24.441  -1.211  22.128 1.000 34.100 0  324 ARG A CD  1 
ATOM   2544 N NE  . ARG A 1 324 ? 24.622  -2.566  21.618 1.000 37.160 0  324 ARG A NE  1 
ATOM   2545 C CZ  . ARG A 1 324 ? 25.333  -2.876  20.542 1.000 36.210 0  324 ARG A CZ  1 
ATOM   2546 N NH1 . ARG A 1 324 ? 25.970  -1.951  19.844 1.000 33.950 1  324 ARG A NH1 1 
ATOM   2547 N NH2 . ARG A 1 324 ? 25.412  -4.148  20.163 1.000 34.020 0  324 ARG A NH2 1 
ATOM   2548 N N   . PRO A 1 325 ? 18.494  -0.543  20.338 1.000 31.830 0  325 PRO A N   1 
ATOM   2549 C CA  . PRO A 1 325 ? 17.134  -1.064  20.563 1.000 29.770 0  325 PRO A CA  1 
ATOM   2550 C C   . PRO A 1 325 ? 16.601  -2.058  19.535 1.000 31.250 0  325 PRO A C   1 
ATOM   2551 O O   . PRO A 1 325 ? 15.444  -2.468  19.673 1.000 31.600 0  325 PRO A O   1 
ATOM   2552 C CB  . PRO A 1 325 ? 16.301  0.224   20.523 1.000 30.420 0  325 PRO A CB  1 
ATOM   2553 C CG  . PRO A 1 325 ? 17.098  1.193   19.659 1.000 31.020 0  325 PRO A CG  1 
ATOM   2554 C CD  . PRO A 1 325 ? 18.474  0.618   19.436 1.000 31.660 0  325 PRO A CD  1 
ATOM   2555 N N   . THR A 1 326 ? 17.379  -2.447  18.521 1.000 32.080 0  326 THR A N   1 
ATOM   2556 C CA  . THR A 1 326 ? 16.883  -3.348  17.482 1.000 33.000 0  326 THR A CA  1 
ATOM   2557 C C   . THR A 1 326 ? 17.718  -4.628  17.439 1.000 32.320 0  326 THR A C   1 
ATOM   2558 O O   . THR A 1 326 ? 18.756  -4.706  18.106 1.000 32.310 0  326 THR A O   1 
ATOM   2559 C CB  . THR A 1 326 ? 16.894  -2.650  16.118 1.000 33.320 0  326 THR A CB  1 
ATOM   2560 O OG1 . THR A 1 326 ? 18.218  -2.684  15.577 1.000 30.480 0  326 THR A OG1 1 
ATOM   2561 C CG2 . THR A 1 326 ? 16.423  -1.209  16.242 1.000 31.970 0  326 THR A CG2 1 
ATOM   2562 N N   . PRO A 1 327 ? 17.302  -5.656  16.688 1.000 31.790 0  327 PRO A N   1 
ATOM   2563 C CA  . PRO A 1 327 ? 18.073  -6.913  16.665 1.000 31.590 0  327 PRO A CA  1 
ATOM   2564 C C   . PRO A 1 327 ? 19.383  -6.863  15.884 1.000 30.850 0  327 PRO A C   1 
ATOM   2565 O O   . PRO A 1 327 ? 20.118  -7.858  15.902 1.000 30.530 0  327 PRO A O   1 
ATOM   2566 C CB  . PRO A 1 327 ? 17.093  -7.907  16.018 1.000 33.050 0  327 PRO A CB  1 
ATOM   2567 C CG  . PRO A 1 327 ? 15.743  -7.324  16.252 1.000 31.770 0  327 PRO A CG  1 
ATOM   2568 C CD  . PRO A 1 327 ? 15.940  -5.849  16.154 1.000 30.350 0  327 PRO A CD  1 
ATOM   2569 N N   . TYR A 1 328 ? 19.720  -5.763  15.212 1.000 33.240 0  328 TYR A N   1 
ATOM   2570 C CA  . TYR A 1 328 ? 20.988  -5.641  14.505 1.000 30.240 0  328 TYR A CA  1 
ATOM   2571 C C   . TYR A 1 328 ? 21.672  -4.342  14.900 1.000 31.660 0  328 TYR A C   1 
ATOM   2572 O O   . TYR A 1 328 ? 21.016  -3.324  15.135 1.000 30.990 0  328 TYR A O   1 
ATOM   2573 C CB  . TYR A 1 328 ? 20.808  -5.676  12.982 1.000 30.120 0  328 TYR A CB  1 
ATOM   2574 C CG  . TYR A 1 328 ? 20.244  -6.974  12.462 1.000 30.810 0  328 TYR A CG  1 
ATOM   2575 C CD1 . TYR A 1 328 ? 18.887  -7.249  12.543 1.000 34.130 0  328 TYR A CD1 1 
ATOM   2576 C CD2 . TYR A 1 328 ? 21.072  -7.927  11.888 1.000 31.470 0  328 TYR A CD2 1 
ATOM   2577 C CE1 . TYR A 1 328 ? 18.371  -8.436  12.070 1.000 32.940 0  328 TYR A CE1 1 
ATOM   2578 C CE2 . TYR A 1 328 ? 20.566  -9.114  11.412 1.000 32.010 0  328 TYR A CE2 1 
ATOM   2579 C CZ  . TYR A 1 328 ? 19.217  -9.364  11.505 1.000 34.330 0  328 TYR A CZ  1 
ATOM   2580 O OH  . TYR A 1 328 ? 18.718  -10.556 11.033 1.000 37.590 0  328 TYR A OH  1 
ATOM   2581 N N   . ASP A 1 329 ? 23.001  -4.383  14.969 1.000 32.980 0  329 ASP A N   1 
ATOM   2582 C CA  . ASP A 1 329 ? 23.760  -3.212  15.373 1.000 30.700 0  329 ASP A CA  1 
ATOM   2583 C C   . ASP A 1 329 ? 24.019  -2.300  14.175 1.000 33.470 0  329 ASP A C   1 
ATOM   2584 O O   . ASP A 1 329 ? 23.591  -2.565  13.046 1.000 31.950 0  329 ASP A O   1 
ATOM   2585 C CB  . ASP A 1 329 ? 25.053  -3.630  16.071 1.000 30.940 0  329 ASP A CB  1 
ATOM   2586 C CG  . ASP A 1 329 ? 26.029  -4.333  15.150 1.000 35.170 0  329 ASP A CG  1 
ATOM   2587 O OD1 . ASP A 1 329 ? 25.742  -4.508  13.948 1.000 36.530 0  329 ASP A OD1 1 
ATOM   2588 O OD2 . ASP A 1 329 ? 27.098  -4.732  15.647 1.000 35.350 -1 329 ASP A OD2 1 
ATOM   2589 N N   . SER A 1 330 ? 24.737  -1.201  14.428 1.000 35.500 0  330 SER A N   1 
ATOM   2590 C CA  . SER A 1 330 ? 24.997  -0.223  13.378 1.000 35.190 0  330 SER A CA  1 
ATOM   2591 C C   . SER A 1 330 ? 25.828  -0.792  12.236 1.000 34.830 0  330 SER A C   1 
ATOM   2592 O O   . SER A 1 330 ? 25.812  -0.227  11.138 1.000 36.560 0  330 SER A O   1 
ATOM   2593 C CB  . SER A 1 330 ? 25.702  1.002   13.969 1.000 34.760 0  330 SER A CB  1 
ATOM   2594 O OG  . SER A 1 330 ? 27.030  0.691   14.356 1.000 36.760 0  330 SER A OG  1 
ATOM   2595 N N   . GLN A 1 331 ? 26.541  -1.895  12.456 1.000 35.200 0  331 GLN A N   1 
ATOM   2596 C CA  . GLN A 1 331 ? 27.287  -2.562  11.397 1.000 35.150 0  331 GLN A CA  1 
ATOM   2597 C C   . GLN A 1 331 ? 26.489  -3.678  10.734 1.000 34.850 0  331 GLN A C   1 
ATOM   2598 O O   . GLN A 1 331 ? 27.071  -4.490  10.007 1.000 33.250 0  331 GLN A O   1 
ATOM   2599 C CB  . GLN A 1 331 ? 28.610  -3.112  11.936 1.000 34.800 0  331 GLN A CB  1 
ATOM   2600 C CG  . GLN A 1 331 ? 29.806  -2.755  11.072 1.000 36.960 0  331 GLN A CG  1 
ATOM   2601 C CD  . GLN A 1 331 ? 29.905  -1.263  10.814 1.000 38.550 0  331 GLN A CD  1 
ATOM   2602 O OE1 . GLN A 1 331 ? 29.934  -0.460  11.748 1.000 36.960 0  331 GLN A OE1 1 
ATOM   2603 N NE2 . GLN A 1 331 ? 29.950  -0.885  9.540  1.000 37.810 0  331 GLN A NE2 1 
ATOM   2604 N N   . LEU A 1 332 ? 25.178  -3.736  10.983 1.000 33.810 0  332 LEU A N   1 
ATOM   2605 C CA  . LEU A 1 332 ? 24.290  -4.746  10.404 1.000 32.880 0  332 LEU A CA  1 
ATOM   2606 C C   . LEU A 1 332 ? 24.688  -6.161  10.813 1.000 33.240 0  332 LEU A C   1 
ATOM   2607 O O   . LEU A 1 332 ? 24.533  -7.111  10.041 1.000 33.300 0  332 LEU A O   1 
ATOM   2608 C CB  . LEU A 1 332 ? 24.223  -4.622  8.879  1.000 31.720 0  332 LEU A CB  1 
ATOM   2609 C CG  . LEU A 1 332 ? 23.704  -3.280  8.355  1.000 31.920 0  332 LEU A CG  1 
ATOM   2610 C CD1 . LEU A 1 332 ? 23.328  -3.379  6.886  1.000 33.570 0  332 LEU A CD1 1 
ATOM   2611 C CD2 . LEU A 1 332 ? 22.524  -2.797  9.183  1.000 31.330 0  332 LEU A CD2 1 
ATOM   2612 N N   . ARG A 1 333 ? 25.205  -6.309  12.032 1.000 32.240 0  333 ARG A N   1 
ATOM   2613 C CA  . ARG A 1 333 ? 25.523  -7.588  12.647 1.000 31.890 0  333 ARG A CA  1 
ATOM   2614 C C   . ARG A 1 333 ? 24.417  -8.002  13.608 1.000 33.560 0  333 ARG A C   1 
ATOM   2615 O O   . ARG A 1 333 ? 23.893  -7.163  14.348 1.000 33.160 0  333 ARG A O   1 
ATOM   2616 C CB  . ARG A 1 333 ? 26.845  -7.514  13.413 1.000 34.020 0  333 ARG A CB  1 
ATOM   2617 C CG  . ARG A 1 333 ? 28.091  -7.723  12.565 1.000 35.120 0  333 ARG A CG  1 
ATOM   2618 C CD  . ARG A 1 333 ? 29.319  -7.082  13.209 1.000 39.080 0  333 ARG A CD  1 
ATOM   2619 N NE  . ARG A 1 333 ? 28.971  -5.973  14.093 1.000 39.970 0  333 ARG A NE  1 
ATOM   2620 C CZ  . ARG A 1 333 ? 29.802  -5.421  14.969 1.000 40.320 0  333 ARG A CZ  1 
ATOM   2621 N NH1 . ARG A 1 333 ? 31.045  -5.853  15.115 1.000 40.740 1  333 ARG A NH1 1 
ATOM   2622 N NH2 . ARG A 1 333 ? 29.373  -4.409  15.719 1.000 38.140 0  333 ARG A NH2 1 
ATOM   2623 N N   . PRO A 1 334 ? 24.037  -9.279  13.613 1.000 32.510 0  334 PRO A N   1 
ATOM   2624 C CA  . PRO A 1 334 ? 22.967  -9.721  14.518 1.000 33.590 0  334 PRO A CA  1 
ATOM   2625 C C   . PRO A 1 334 ? 23.403  -9.631  15.971 1.000 33.680 0  334 PRO A C   1 
ATOM   2626 O O   . PRO A 1 334 ? 24.538  -9.965  16.319 1.000 34.270 0  334 PRO A O   1 
ATOM   2627 C CB  . PRO A 1 334 ? 22.722  -11.173 14.093 1.000 31.690 0  334 PRO A CB  1 
ATOM   2628 C CG  . PRO A 1 334 ? 24.016  -11.596 13.467 1.000 32.150 0  334 PRO A CG  1 
ATOM   2629 C CD  . PRO A 1 334 ? 24.538  -10.375 12.770 1.000 32.160 0  334 PRO A CD  1 
ATOM   2630 N N   . LYS A 1 335 ? 22.491  -9.172  16.816 1.000 33.630 0  335 LYS A N   1 
ATOM   2631 C CA  . LYS A 1 335 ? 22.688  -9.045  18.252 1.000 33.470 0  335 LYS A CA  1 
ATOM   2632 C C   . LYS A 1 335 ? 21.960  -10.156 18.995 1.000 35.620 0  335 LYS A C   1 
ATOM   2633 O O   . LYS A 1 335 ? 21.136  -10.873 18.420 1.000 37.040 0  335 LYS A O   1 
ATOM   2634 C CB  . LYS A 1 335 ? 22.197  -7.677  18.728 1.000 33.690 0  335 LYS A CB  1 
ATOM   2635 C CG  . LYS A 1 335 ? 22.784  -6.502  17.979 1.000 34.350 0  335 LYS A CG  1 
ATOM   2636 C CD  . LYS A 1 335 ? 21.883  -5.291  18.103 1.000 32.700 0  335 LYS A CD  1 
ATOM   2637 C CE  . LYS A 1 335 ? 21.841  -4.784  19.528 1.000 30.410 0  335 LYS A CE  1 
ATOM   2638 N NZ  . LYS A 1 335 ? 20.967  -3.591  19.641 1.000 30.160 1  335 LYS A NZ  1 
ATOM   2639 N N   . PRO A 1 336 ? 22.256  -10.344 20.287 1.000 35.850 0  336 PRO A N   1 
ATOM   2640 C CA  . PRO A 1 336 ? 21.527  -11.366 21.062 1.000 33.690 0  336 PRO A CA  1 
ATOM   2641 C C   . PRO A 1 336 ? 20.017  -11.179 21.082 1.000 34.460 0  336 PRO A C   1 
ATOM   2642 O O   . PRO A 1 336 ? 19.290  -12.161 21.302 1.000 34.620 0  336 PRO A O   1 
ATOM   2643 C CB  . PRO A 1 336 ? 22.125  -11.225 22.468 1.000 34.040 0  336 PRO A CB  1 
ATOM   2644 C CG  . PRO A 1 336 ? 23.506  -10.716 22.227 1.000 34.710 0  336 PRO A CG  1 
ATOM   2645 C CD  . PRO A 1 336 ? 23.404  -9.801  21.039 1.000 34.590 0  336 PRO A CD  1 
ATOM   2646 N N   . MET A 1 337 ? 19.511  -9.962  20.859 1.000 33.640 0  337 MET A N   1 
ATOM   2647 C CA  . MET A 1 337 ? 18.063  -9.784  20.836 1.000 33.450 0  337 MET A CA  1 
ATOM   2648 C C   . MET A 1 337 ? 17.437  -10.469 19.627 1.000 34.190 0  337 MET A C   1 
ATOM   2649 O O   . MET A 1 337 ? 16.309  -10.970 19.715 1.000 35.170 0  337 MET A O   1 
ATOM   2650 C CB  . MET A 1 337 ? 17.706  -8.296  20.853 1.000 34.900 0  337 MET A CB  1 
ATOM   2651 C CG  . MET A 1 337 ? 16.215  -8.013  20.692 1.000 32.440 0  337 MET A CG  1 
ATOM   2652 S SD  . MET A 1 337 ? 15.831  -6.468  19.847 1.000 32.470 0  337 MET A SD  1 
ATOM   2653 C CE  . MET A 1 337 ? 16.603  -5.286  20.949 1.000 30.700 0  337 MET A CE  1 
ATOM   2654 N N   . ARG A 1 338 ? 18.154  -10.522 18.500 1.000 31.660 0  338 ARG A N   1 
ATOM   2655 C CA  . ARG A 1 338 ? 17.676  -11.303 17.364 1.000 32.860 0  338 ARG A CA  1 
ATOM   2656 C C   . ARG A 1 338 ? 17.547  -12.770 17.742 1.000 34.090 0  338 ARG A C   1 
ATOM   2657 O O   . ARG A 1 338 ? 16.596  -13.447 17.338 1.000 31.490 0  338 ARG A O   1 
ATOM   2658 C CB  . ARG A 1 338 ? 18.610  -11.146 16.164 1.000 33.790 0  338 ARG A CB  1 
ATOM   2659 C CG  . ARG A 1 338 ? 17.990  -11.636 14.865 1.000 33.400 0  338 ARG A CG  1 
ATOM   2660 C CD  . ARG A 1 338 ? 18.995  -12.352 13.984 1.000 34.700 0  338 ARG A CD  1 
ATOM   2661 N NE  . ARG A 1 338 ? 18.394  -12.800 12.732 1.000 36.560 0  338 ARG A NE  1 
ATOM   2662 C CZ  . ARG A 1 338 ? 18.140  -14.067 12.435 1.000 36.310 0  338 ARG A CZ  1 
ATOM   2663 N NH1 . ARG A 1 338 ? 18.442  -15.047 13.270 1.000 36.390 1  338 ARG A NH1 1 
ATOM   2664 N NH2 . ARG A 1 338 ? 17.579  -14.358 11.265 1.000 35.200 0  338 ARG A NH2 1 
ATOM   2665 N N   . GLU A 1 339 ? 18.515  -13.282 18.500 1.000 34.380 0  339 GLU A N   1 
ATOM   2666 C CA  . GLU A 1 339 ? 18.446  -14.653 18.987 1.000 33.280 0  339 GLU A CA  1 
ATOM   2667 C C   . GLU A 1 339 ? 17.236  -14.863 19.892 1.000 32.000 0  339 GLU A C   1 
ATOM   2668 O O   . GLU A 1 339 ? 16.541  -15.883 19.789 1.000 32.680 0  339 GLU A O   1 
ATOM   2669 C CB  . GLU A 1 339 ? 19.734  -14.975 19.733 1.000 33.280 0  339 GLU A CB  1 
ATOM   2670 C CG  . GLU A 1 339 ? 19.825  -16.372 20.245 1.000 35.220 0  339 GLU A CG  1 
ATOM   2671 C CD  . GLU A 1 339 ? 21.251  -16.846 20.279 1.000 37.040 0  339 GLU A CD  1 
ATOM   2672 O OE1 . GLU A 1 339 ? 22.166  -15.994 20.284 1.000 37.690 0  339 GLU A OE1 1 
ATOM   2673 O OE2 . GLU A 1 339 ? 21.459  -18.066 20.295 1.000 36.180 -1 339 GLU A OE2 1 
ATOM   2674 N N   . ALA A 1 340 ? 16.970  -13.906 20.786 1.000 31.600 0  340 ALA A N   1 
ATOM   2675 C CA  . ALA A 1 340 ? 15.793  -14.001 21.647 1.000 32.260 0  340 ALA A CA  1 
ATOM   2676 C C   . ALA A 1 340 ? 14.509  -14.035 20.825 1.000 31.740 0  340 ALA A C   1 
ATOM   2677 O O   . ALA A 1 340 ? 13.590  -14.812 21.118 1.000 30.050 0  340 ALA A O   1 
ATOM   2678 C CB  . ALA A 1 340 ? 15.770  -12.831 22.632 1.000 31.200 0  340 ALA A CB  1 
ATOM   2679 N N   . ILE A 1 341 ? 14.425  -13.184 19.801 1.000 32.600 0  341 ILE A N   1 
ATOM   2680 C CA  . ILE A 1 341 ? 13.247  -13.149 18.938 1.000 31.540 0  341 ILE A CA  1 
ATOM   2681 C C   . ILE A 1 341 ? 13.099  -14.463 18.176 1.000 32.140 0  341 ILE A C   1 
ATOM   2682 O O   . ILE A 1 341 ? 11.989  -14.985 18.022 1.000 32.050 0  341 ILE A O   1 
ATOM   2683 C CB  . ILE A 1 341 ? 13.325  -11.939 17.990 1.000 31.090 0  341 ILE A CB  1 
ATOM   2684 C CG1 . ILE A 1 341 ? 13.215  -10.642 18.794 1.000 29.640 0  341 ILE A CG1 1 
ATOM   2685 C CG2 . ILE A 1 341 ? 12.240  -12.015 16.928 1.000 28.800 0  341 ILE A CG2 1 
ATOM   2686 C CD1 . ILE A 1 341 ? 13.059  -9.401  17.948 1.000 30.090 0  341 ILE A CD1 1 
ATOM   2687 N N   . ALA A 1 342 ? 14.209  -15.000 17.661 1.000 32.420 0  342 ALA A N   1 
ATOM   2688 C CA  . ALA A 1 342 ? 14.159  -16.285 16.970 1.000 33.040 0  342 ALA A CA  1 
ATOM   2689 C C   . ALA A 1 342 ? 13.659  -17.386 17.895 1.000 32.960 0  342 ALA A C   1 
ATOM   2690 O O   . ALA A 1 342 ? 12.856  -18.237 17.493 1.000 33.790 0  342 ALA A O   1 
ATOM   2691 C CB  . ALA A 1 342 ? 15.541  -16.637 16.422 1.000 33.510 0  342 ALA A CB  1 
ATOM   2692 N N   . ALA A 1 343 ? 14.103  -17.368 19.153 1.000 32.790 0  343 ALA A N   1 
ATOM   2693 C CA  . ALA A 1 343 ? 13.630  -18.354 20.118 1.000 31.570 0  343 ALA A CA  1 
ATOM   2694 C C   . ALA A 1 343 ? 12.134  -18.197 20.363 1.000 33.370 0  343 ALA A C   1 
ATOM   2695 O O   . ALA A 1 343 ? 11.385  -19.183 20.374 1.000 34.140 0  343 ALA A O   1 
ATOM   2696 C CB  . ALA A 1 343 ? 14.409  -18.225 21.426 1.000 32.120 0  343 ALA A CB  1 
ATOM   2697 N N   . SER A 1 344 ? 11.681  -16.958 20.572 1.000 32.020 0  344 SER A N   1 
ATOM   2698 C CA  . SER A 1 344 ? 10.259  -16.723 20.798 1.000 31.680 0  344 SER A CA  1 
ATOM   2699 C C   . SER A 1 344 ? 9.427   -17.155 19.599 1.000 31.110 0  344 SER A C   1 
ATOM   2700 O O   . SER A 1 344 ? 8.305   -17.642 19.765 1.000 32.320 0  344 SER A O   1 
ATOM   2701 C CB  . SER A 1 344 ? 10.017  -15.245 21.107 1.000 31.200 0  344 SER A CB  1 
ATOM   2702 O OG  . SER A 1 344 ? 10.253  -14.964 22.476 1.000 33.820 0  344 SER A OG  1 
ATOM   2703 N N   . LEU A 1 345 ? 9.964   -17.004 18.388 1.000 32.320 0  345 LEU A N   1 
ATOM   2704 C CA  . LEU A 1 345 ? 9.248   -17.470 17.206 1.000 32.280 0  345 LEU A CA  1 
ATOM   2705 C C   . LEU A 1 345 ? 9.219   -18.990 17.149 1.000 33.910 0  345 LEU A C   1 
ATOM   2706 O O   . LEU A 1 345 ? 8.237   -19.576 16.676 1.000 33.730 0  345 LEU A O   1 
ATOM   2707 C CB  . LEU A 1 345 ? 9.880   -16.893 15.940 1.000 31.280 0  345 LEU A CB  1 
ATOM   2708 C CG  . LEU A 1 345 ? 9.549   -15.422 15.670 1.000 32.970 0  345 LEU A CG  1 
ATOM   2709 C CD1 . LEU A 1 345 ? 10.574  -14.793 14.739 1.000 30.250 0  345 LEU A CD1 1 
ATOM   2710 C CD2 . LEU A 1 345 ? 8.143   -15.271 15.106 1.000 29.320 0  345 LEU A CD2 1 
ATOM   2711 N N   . ARG A 1 346 ? 10.283  -19.643 17.625 1.000 32.520 0  346 ARG A N   1 
ATOM   2712 C CA  . ARG A 1 346 ? 10.313  -21.102 17.628 1.000 31.450 0  346 ARG A CA  1 
ATOM   2713 C C   . ARG A 1 346 ? 9.336   -21.682 18.644 1.000 33.740 0  346 ARG A C   1 
ATOM   2714 O O   . ARG A 1 346 ? 8.666   -22.683 18.364 1.000 37.620 0  346 ARG A O   1 
ATOM   2715 C CB  . ARG A 1 346 ? 11.724  -21.599 17.935 1.000 33.360 0  346 ARG A CB  1 
ATOM   2716 C CG  . ARG A 1 346 ? 12.600  -21.827 16.728 1.000 32.660 0  346 ARG A CG  1 
ATOM   2717 C CD  . ARG A 1 346 ? 13.889  -22.510 17.135 1.000 32.030 0  346 ARG A CD  1 
ATOM   2718 N NE  . ARG A 1 346 ? 15.040  -21.656 16.885 1.000 33.500 0  346 ARG A NE  1 
ATOM   2719 C CZ  . ARG A 1 346 ? 15.652  -21.559 15.713 1.000 33.820 0  346 ARG A CZ  1 
ATOM   2720 N NH1 . ARG A 1 346 ? 15.267  -22.278 14.672 1.000 32.230 1  346 ARG A NH1 1 
ATOM   2721 N NH2 . ARG A 1 346 ? 16.677  -20.722 15.582 1.000 34.220 0  346 ARG A NH2 1 
ATOM   2722 N N   . ALA A 1 347 ? 9.236   -21.071 19.823 1.000 30.780 0  347 ALA A N   1 
ATOM   2723 C CA  . ALA A 1 347 ? 8.489   -21.663 20.927 1.000 31.670 0  347 ALA A CA  1 
ATOM   2724 C C   . ALA A 1 347 ? 7.026   -21.240 20.979 1.000 32.090 0  347 ALA A C   1 
ATOM   2725 O O   . ALA A 1 347 ? 6.277   -21.759 21.813 1.000 31.620 0  347 ALA A O   1 
ATOM   2726 C CB  . ALA A 1 347 ? 9.163   -21.319 22.260 1.000 29.810 0  347 ALA A CB  1 
ATOM   2727 N N   . MET A 1 348 ? 6.595   -20.344 20.103 1.000 30.450 0  348 MET A N   1 
ATOM   2728 C CA  . MET A 1 348 ? 5.241   -19.819 20.171 1.000 29.320 0  348 MET A CA  1 
ATOM   2729 C C   . MET A 1 348 ? 4.250   -20.781 19.516 1.000 31.740 0  348 MET A C   1 
ATOM   2730 O O   . MET A 1 348 ? 4.623   -21.576 18.647 1.000 30.560 0  348 MET A O   1 
ATOM   2731 C CB  . MET A 1 348 ? 5.179   -18.451 19.499 1.000 28.720 0  348 MET A CB  1 
ATOM   2732 C CG  . MET A 1 348 ? 4.734   -18.462 18.048 1.000 28.810 0  348 MET A CG  1 
ATOM   2733 S SD  . MET A 1 348 ? 4.791   -16.796 17.366 1.000 28.530 0  348 MET A SD  1 
ATOM   2734 C CE  . MET A 1 348 ? 4.840   -17.127 15.611 1.000 29.120 0  348 MET A CE  1 
ATOM   2735 N N   . PRO A 1 349 ? 2.986   -20.753 19.945 1.000 30.120 0  349 PRO A N   1 
ATOM   2736 C CA  . PRO A 1 349 ? 1.981   -21.629 19.330 1.000 29.060 0  349 PRO A CA  1 
ATOM   2737 C C   . PRO A 1 349 ? 1.740   -21.276 17.870 1.000 29.090 0  349 PRO A C   1 
ATOM   2738 O O   . PRO A 1 349 ? 1.938   -20.138 17.439 1.000 31.250 0  349 PRO A O   1 
ATOM   2739 C CB  . PRO A 1 349 ? 0.724   -21.385 20.174 1.000 28.790 0  349 PRO A CB  1 
ATOM   2740 C CG  . PRO A 1 349 ? 1.203   -20.743 21.427 1.000 29.500 0  349 PRO A CG  1 
ATOM   2741 C CD  . PRO A 1 349 ? 2.429   -19.973 21.063 1.000 28.580 0  349 PRO A CD  1 
ATOM   2742 N N   . MET A 1 350 ? 1.327   -22.285 17.107 1.000 29.370 0  350 MET A N   1 
ATOM   2743 C CA  . MET A 1 350 ? 0.888   -22.073 15.734 1.000 29.580 0  350 MET A CA  1 
ATOM   2744 C C   . MET A 1 350 ? -0.256  -21.067 15.697 1.000 31.700 0  350 MET A C   1 
ATOM   2745 O O   . MET A 1 350 ? -1.177  -21.124 16.516 1.000 29.560 0  350 MET A O   1 
ATOM   2746 C CB  . MET A 1 350 ? 0.442   -23.402 15.121 1.000 30.240 0  350 MET A CB  1 
ATOM   2747 C CG  . MET A 1 350 ? 0.010   -23.326 13.667 1.000 32.150 0  350 MET A CG  1 
ATOM   2748 S SD  . MET A 1 350 ? 1.395   -23.110 12.539 1.000 32.550 0  350 MET A SD  1 
ATOM   2749 C CE  . MET A 1 350 ? 0.559   -22.460 11.094 1.000 31.720 0  350 MET A CE  1 
ATOM   2750 N N   . ARG A 1 351 ? -0.191  -20.133 14.747 1.000 31.620 0  351 ARG A N   1 
ATOM   2751 C CA  . ARG A 1 351 ? -1.270  -19.167 14.604 1.000 29.930 0  351 ARG A CA  1 
ATOM   2752 C C   . ARG A 1 351 ? -2.562  -19.869 14.208 1.000 31.680 0  351 ARG A C   1 
ATOM   2753 O O   . ARG A 1 351 ? -2.554  -20.892 13.518 1.000 34.110 0  351 ARG A O   1 
ATOM   2754 C CB  . ARG A 1 351 ? -0.921  -18.113 13.552 1.000 31.700 0  351 ARG A CB  1 
ATOM   2755 C CG  . ARG A 1 351 ? 0.460   -17.489 13.678 1.000 32.230 0  351 ARG A CG  1 
ATOM   2756 C CD  . ARG A 1 351 ? 0.561   -16.566 14.870 1.000 29.850 0  351 ARG A CD  1 
ATOM   2757 N NE  . ARG A 1 351 ? 0.845   -17.289 16.102 1.000 28.940 0  351 ARG A NE  1 
ATOM   2758 C CZ  . ARG A 1 351 ? 1.146   -16.710 17.254 1.000 30.250 0  351 ARG A CZ  1 
ATOM   2759 N NH1 . ARG A 1 351 ? 1.229   -15.394 17.363 1.000 29.830 1  351 ARG A NH1 1 
ATOM   2760 N NH2 . ARG A 1 351 ? 1.371   -17.468 18.323 1.000 29.430 0  351 ARG A NH2 1 
ATOM   2761 N N   . LYS A 1 352 ? -3.682  -19.305 14.647 1.000 31.110 0  352 LYS A N   1 
ATOM   2762 C CA  . LYS A 1 352 ? -4.979  -19.818 14.239 1.000 32.910 0  352 LYS A CA  1 
ATOM   2763 C C   . LYS A 1 352 ? -5.212  -19.522 12.762 1.000 35.340 0  352 LYS A C   1 
ATOM   2764 O O   . LYS A 1 352 ? -4.784  -18.490 12.236 1.000 35.210 0  352 LYS A O   1 
ATOM   2765 C CB  . LYS A 1 352 ? -6.080  -19.214 15.115 1.000 35.740 0  352 LYS A CB  1 
ATOM   2766 C CG  . LYS A 1 352 ? -7.471  -19.179 14.505 1.000 39.690 0  352 LYS A CG  1 
ATOM   2767 C CD  . LYS A 1 352 ? -8.424  -18.365 15.374 1.000 40.350 0  352 LYS A CD  1 
ATOM   2768 C CE  . LYS A 1 352 ? -8.235  -18.704 16.848 1.000 38.620 0  352 LYS A CE  1 
ATOM   2769 N NZ  . LYS A 1 352 ? -9.502  -18.624 17.620 1.000 40.830 1  352 LYS A NZ  1 
ATOM   2770 N N   . ALA A 1 353 ? -5.892  -20.444 12.086 1.000 39.180 0  353 ALA A N   1 
ATOM   2771 C CA  . ALA A 1 353 ? -6.084  -20.331 10.641 1.000 38.810 0  353 ALA A CA  1 
ATOM   2772 C C   . ALA A 1 353 ? -7.260  -19.418 10.303 1.000 37.210 0  353 ALA A C   1 
ATOM   2773 O O   . ALA A 1 353 ? -7.502  -18.421 10.987 1.000 38.040 0  353 ALA A O   1 
ATOM   2774 C CB  . ALA A 1 353 ? -6.286  -21.706 10.026 1.000 31.550 0  353 ALA A CB  1 
ATOM   2775 N N   . PRO B 1 1   ? 32.710  49.651  25.436 1.000 28.810 0  1   PRO B N   1 
ATOM   2776 C CA  . PRO B 1 1   ? 32.117  49.474  26.764 1.000 28.510 0  1   PRO B CA  1 
ATOM   2777 C C   . PRO B 1 1   ? 31.648  48.041  26.975 1.000 28.240 0  1   PRO B C   1 
ATOM   2778 O O   . PRO B 1 1   ? 31.224  47.399  26.015 1.000 29.250 0  1   PRO B O   1 
ATOM   2779 C CB  . PRO B 1 1   ? 30.929  50.447  26.758 1.000 28.390 0  1   PRO B CB  1 
ATOM   2780 C CG  . PRO B 1 1   ? 30.832  50.994  25.336 1.000 28.600 0  1   PRO B CG  1 
ATOM   2781 C CD  . PRO B 1 1   ? 31.735  50.177  24.471 1.000 29.140 0  1   PRO B CD  1 
ATOM   2782 N N   . ALA B 1 2   ? 31.732  47.544  28.206 1.000 28.080 0  2   ALA B N   1 
ATOM   2783 C CA  . ALA B 1 2   ? 31.333  46.172  28.486 1.000 28.300 0  2   ALA B CA  1 
ATOM   2784 C C   . ALA B 1 2   ? 29.827  46.086  28.700 1.000 31.320 0  2   ALA B C   1 
ATOM   2785 O O   . ALA B 1 2   ? 29.194  47.023  29.197 1.000 34.570 0  2   ALA B O   1 
ATOM   2786 C CB  . ALA B 1 2   ? 32.066  45.643  29.717 1.000 29.440 0  2   ALA B CB  1 
ATOM   2787 N N   . LEU B 1 3   ? 29.252  44.942  28.316 1.000 29.750 0  3   LEU B N   1 
ATOM   2788 C CA  . LEU B 1 3   ? 27.813  44.750  28.468 1.000 27.940 0  3   LEU B CA  1 
ATOM   2789 C C   . LEU B 1 3   ? 27.374  44.970  29.909 1.000 31.880 0  3   LEU B C   1 
ATOM   2790 O O   . LEU B 1 3   ? 26.325  45.577  30.164 1.000 33.080 0  3   LEU B O   1 
ATOM   2791 C CB  . LEU B 1 3   ? 27.416  43.352  27.997 1.000 26.920 0  3   LEU B CB  1 
ATOM   2792 C CG  . LEU B 1 3   ? 27.553  43.078  26.499 1.000 27.740 0  3   LEU B CG  1 
ATOM   2793 C CD1 . LEU B 1 3   ? 27.108  41.665  26.180 1.000 26.920 0  3   LEU B CD1 1 
ATOM   2794 C CD2 . LEU B 1 3   ? 26.754  44.085  25.689 1.000 28.440 0  3   LEU B CD2 1 
ATOM   2795 N N   . LYS B 1 4   ? 28.179  44.511  30.868 1.000 31.260 0  4   LYS B N   1 
ATOM   2796 C CA  . LYS B 1 4   ? 27.828  44.709  32.267 1.000 33.180 0  4   LYS B CA  1 
ATOM   2797 C C   . LYS B 1 4   ? 27.809  46.187  32.629 1.000 33.160 0  4   LYS B C   1 
ATOM   2798 O O   . LYS B 1 4   ? 27.028  46.597  33.490 1.000 33.990 0  4   LYS B O   1 
ATOM   2799 C CB  . LYS B 1 4   ? 28.786  43.935  33.174 1.000 30.520 0  4   LYS B CB  1 
ATOM   2800 C CG  . LYS B 1 4   ? 30.025  44.693  33.593 1.000 31.010 0  4   LYS B CG  1 
ATOM   2801 C CD  . LYS B 1 4   ? 30.966  43.791  34.367 1.000 31.700 0  4   LYS B CD  1 
ATOM   2802 C CE  . LYS B 1 4   ? 32.408  44.211  34.175 1.000 27.890 0  4   LYS B CE  1 
ATOM   2803 N NZ  . LYS B 1 4   ? 33.343  43.105  34.494 1.000 28.100 1  4   LYS B NZ  1 
ATOM   2804 N N   . ASP B 1 5   ? 28.599  47.014  31.940 1.000 31.200 0  5   ASP B N   1 
ATOM   2805 C CA  . ASP B 1 5   ? 28.629  48.436  32.268 1.000 33.000 0  5   ASP B CA  1 
ATOM   2806 C C   . ASP B 1 5   ? 27.370  49.144  31.785 1.000 31.210 0  5   ASP B C   1 
ATOM   2807 O O   . ASP B 1 5   ? 26.786  49.951  32.516 1.000 30.190 0  5   ASP B O   1 
ATOM   2808 C CB  . ASP B 1 5   ? 29.882  49.080  31.679 1.000 32.170 0  5   ASP B CB  1 
ATOM   2809 C CG  . ASP B 1 5   ? 31.147  48.517  32.279 1.000 32.920 0  5   ASP B CG  1 
ATOM   2810 O OD1 . ASP B 1 5   ? 31.119  48.171  33.479 1.000 33.980 0  5   ASP B OD1 1 
ATOM   2811 O OD2 . ASP B 1 5   ? 32.162  48.415  31.559 1.000 33.460 -1 5   ASP B OD2 1 
ATOM   2812 N N   . LEU B 1 6   ? 26.942  48.869  30.552 1.000 28.570 0  6   LEU B N   1 
ATOM   2813 C CA  . LEU B 1 6   ? 25.660  49.389  30.084 1.000 30.410 0  6   LEU B CA  1 
ATOM   2814 C C   . LEU B 1 6   ? 24.519  48.904  30.972 1.000 30.060 0  6   LEU B C   1 
ATOM   2815 O O   . LEU B 1 6   ? 23.662  49.691  31.404 1.000 27.090 0  6   LEU B O   1 
ATOM   2816 C CB  . LEU B 1 6   ? 25.425  48.971  28.631 1.000 31.850 0  6   LEU B CB  1 
ATOM   2817 C CG  . LEU B 1 6   ? 26.590  49.080  27.649 1.000 27.400 0  6   LEU B CG  1 
ATOM   2818 C CD1 . LEU B 1 6   ? 26.271  48.297  26.395 1.000 29.290 0  6   LEU B CD1 1 
ATOM   2819 C CD2 . LEU B 1 6   ? 26.873  50.530  27.309 1.000 27.650 0  6   LEU B CD2 1 
ATOM   2820 N N   . ALA B 1 7   ? 24.511  47.604  31.279 1.000 32.310 0  7   ALA B N   1 
ATOM   2821 C CA  . ALA B 1 7   ? 23.449  47.039  32.102 1.000 31.270 0  7   ALA B CA  1 
ATOM   2822 C C   . ALA B 1 7   ? 23.433  47.671  33.486 1.000 31.500 0  7   ALA B C   1 
ATOM   2823 O O   . ALA B 1 7   ? 22.365  47.882  34.074 1.000 32.190 0  7   ALA B O   1 
ATOM   2824 C CB  . ALA B 1 7   ? 23.631  45.526  32.208 1.000 28.540 0  7   ALA B CB  1 
ATOM   2825 N N   . LYS B 1 8   ? 24.608  47.979  34.021 1.000 30.250 0  8   LYS B N   1 
ATOM   2826 C CA  . LYS B 1 8   ? 24.696  48.539  35.357 1.000 29.540 0  8   LYS B CA  1 
ATOM   2827 C C   . LYS B 1 8   ? 24.307  50.009  35.357 1.000 30.570 0  8   LYS B C   1 
ATOM   2828 O O   . LYS B 1 8   ? 23.689  50.489  36.313 1.000 32.670 0  8   LYS B O   1 
ATOM   2829 C CB  . LYS B 1 8   ? 26.107  48.324  35.892 1.000 31.300 0  8   LYS B CB  1 
ATOM   2830 C CG  . LYS B 1 8   ? 26.472  49.152  37.084 1.000 33.960 0  8   LYS B CG  1 
ATOM   2831 C CD  . LYS B 1 8   ? 27.975  49.116  37.273 1.000 33.080 0  8   LYS B CD  1 
ATOM   2832 C CE  . LYS B 1 8   ? 28.394  49.929  38.472 1.000 35.510 0  8   LYS B CE  1 
ATOM   2833 N NZ  . LYS B 1 8   ? 29.879  49.977  38.597 1.000 41.650 1  8   LYS B NZ  1 
ATOM   2834 N N   . ALA B 1 9   ? 24.660  50.732  34.291 1.000 30.850 0  9   ALA B N   1 
ATOM   2835 C CA  . ALA B 1 9   ? 24.165  52.088  34.104 1.000 30.520 0  9   ALA B CA  1 
ATOM   2836 C C   . ALA B 1 9   ? 22.651  52.116  33.981 1.000 29.900 0  9   ALA B C   1 
ATOM   2837 O O   . ALA B 1 9   ? 22.031  53.139  34.287 1.000 30.520 0  9   ALA B O   1 
ATOM   2838 C CB  . ALA B 1 9   ? 24.804  52.720  32.866 1.000 28.170 0  9   ALA B CB  1 
ATOM   2839 N N   . LYS B 1 10  ? 22.040  51.016  33.550 1.000 31.410 0  10  LYS B N   1 
ATOM   2840 C CA  . LYS B 1 10  ? 20.588  50.945  33.490 1.000 26.900 0  10  LYS B CA  1 
ATOM   2841 C C   . LYS B 1 10  ? 19.978  50.304  34.727 1.000 29.220 0  10  LYS B C   1 
ATOM   2842 O O   . LYS B 1 10  ? 18.751  50.223  34.820 1.000 30.060 0  10  LYS B O   1 
ATOM   2843 C CB  . LYS B 1 10  ? 20.144  50.172  32.246 1.000 28.060 0  10  LYS B CB  1 
ATOM   2844 C CG  . LYS B 1 10  ? 20.468  50.877  30.948 1.000 27.550 0  10  LYS B CG  1 
ATOM   2845 C CD  . LYS B 1 10  ? 19.631  52.131  30.800 1.000 27.460 0  10  LYS B CD  1 
ATOM   2846 C CE  . LYS B 1 10  ? 19.932  52.832  29.493 1.000 29.620 0  10  LYS B CE  1 
ATOM   2847 N NZ  . LYS B 1 10  ? 18.715  53.439  28.892 1.000 28.990 1  10  LYS B NZ  1 
ATOM   2848 N N   . GLY B 1 11  ? 20.795  49.884  35.689 1.000 31.610 0  11  GLY B N   1 
ATOM   2849 C CA  . GLY B 1 11  ? 20.281  49.251  36.888 1.000 28.350 0  11  GLY B CA  1 
ATOM   2850 C C   . GLY B 1 11  ? 20.020  47.768  36.741 1.000 30.820 0  11  GLY B C   1 
ATOM   2851 O O   . GLY B 1 11  ? 19.145  47.230  37.423 1.000 31.990 0  11  GLY B O   1 
ATOM   2852 N N   . MET B 1 12  ? 20.768  47.089  35.875 1.000 31.290 0  12  MET B N   1 
ATOM   2853 C CA  . MET B 1 12  ? 20.533  45.692  35.540 1.000 30.120 0  12  MET B CA  1 
ATOM   2854 C C   . MET B 1 12  ? 21.827  44.904  35.687 1.000 30.510 0  12  MET B C   1 
ATOM   2855 O O   . MET B 1 12  ? 22.905  45.392  35.333 1.000 26.060 0  12  MET B O   1 
ATOM   2856 C CB  . MET B 1 12  ? 19.990  45.565  34.106 1.000 30.000 0  12  MET B CB  1 
ATOM   2857 C CG  . MET B 1 12  ? 19.058  44.384  33.864 1.000 30.580 0  12  MET B CG  1 
ATOM   2858 S SD  . MET B 1 12  ? 18.837  43.958  32.121 1.000 30.510 0  12  MET B SD  1 
ATOM   2859 C CE  . MET B 1 12  ? 20.513  44.120  31.540 1.000 27.480 0  12  MET B CE  1 
ATOM   2860 N N   . ARG B 1 13  ? 21.723  43.694  36.233 1.000 31.120 0  13  ARG B N   1 
ATOM   2861 C CA  . ARG B 1 13  ? 22.866  42.795  36.291 1.000 28.740 0  13  ARG B CA  1 
ATOM   2862 C C   . ARG B 1 13  ? 22.989  42.014  34.988 1.000 28.940 0  13  ARG B C   1 
ATOM   2863 O O   . ARG B 1 13  ? 21.988  41.651  34.358 1.000 29.250 0  13  ARG B O   1 
ATOM   2864 C CB  . ARG B 1 13  ? 22.748  41.824  37.467 1.000 29.180 0  13  ARG B CB  1 
ATOM   2865 C CG  . ARG B 1 13  ? 23.079  42.422  38.824 1.000 27.720 0  13  ARG B CG  1 
ATOM   2866 C CD  . ARG B 1 13  ? 22.560  41.534  39.944 1.000 25.700 0  13  ARG B CD  1 
ATOM   2867 N NE  . ARG B 1 13  ? 21.108  41.412  39.898 1.000 25.510 0  13  ARG B NE  1 
ATOM   2868 C CZ  . ARG B 1 13  ? 20.260  42.285  40.423 1.000 27.100 0  13  ARG B CZ  1 
ATOM   2869 N NH1 . ARG B 1 13  ? 20.686  43.341  41.098 1.000 27.540 1  13  ARG B NH1 1 
ATOM   2870 N NH2 . ARG B 1 13  ? 18.953  42.096  40.267 1.000 25.390 0  13  ARG B NH2 1 
ATOM   2871 N N   . PHE B 1 14  ? 24.233  41.757  34.590 1.000 28.060 0  14  PHE B N   1 
ATOM   2872 C CA  . PHE B 1 14  ? 24.529  41.006  33.379 1.000 28.790 0  14  PHE B CA  1 
ATOM   2873 C C   . PHE B 1 14  ? 25.440  39.840  33.727 1.000 28.370 0  14  PHE B C   1 
ATOM   2874 O O   . PHE B 1 14  ? 26.457  40.012  34.412 1.000 30.570 0  14  PHE B O   1 
ATOM   2875 C CB  . PHE B 1 14  ? 25.173  41.885  32.304 1.000 28.160 0  14  PHE B CB  1 
ATOM   2876 C CG  . PHE B 1 14  ? 24.933  41.391  30.910 1.000 26.810 0  14  PHE B CG  1 
ATOM   2877 C CD1 . PHE B 1 14  ? 23.787  41.753  30.224 1.000 26.050 0  14  PHE B CD1 1 
ATOM   2878 C CD2 . PHE B 1 14  ? 25.838  40.543  30.297 1.000 28.300 0  14  PHE B CD2 1 
ATOM   2879 C CE1 . PHE B 1 14  ? 23.556  41.290  28.943 1.000 27.920 0  14  PHE B CE1 1 
ATOM   2880 C CE2 . PHE B 1 14  ? 25.613  40.076  29.017 1.000 29.310 0  14  PHE B CE2 1 
ATOM   2881 C CZ  . PHE B 1 14  ? 24.471  40.451  28.338 1.000 27.000 0  14  PHE B CZ  1 
ATOM   2882 N N   . GLY B 1 15  ? 25.066  38.658  33.262 1.000 25.870 0  15  GLY B N   1 
ATOM   2883 C CA  . GLY B 1 15  ? 25.803  37.466  33.606 1.000 28.330 0  15  GLY B CA  1 
ATOM   2884 C C   . GLY B 1 15  ? 25.770  36.390  32.548 1.000 30.990 0  15  GLY B C   1 
ATOM   2885 O O   . GLY B 1 15  ? 25.312  36.599  31.420 1.000 28.910 0  15  GLY B O   1 
ATOM   2886 N N   . SER B 1 16  ? 26.249  35.213  32.927 1.000 28.710 0  16  SER B N   1 
ATOM   2887 C CA  . SER B 1 16  ? 26.359  34.115  31.983 1.000 29.270 0  16  SER B CA  1 
ATOM   2888 C C   . SER B 1 16  ? 26.381  32.792  32.727 1.000 32.230 0  16  SER B C   1 
ATOM   2889 O O   . SER B 1 16  ? 26.661  32.726  33.928 1.000 32.650 0  16  SER B O   1 
ATOM   2890 C CB  . SER B 1 16  ? 27.612  34.242  31.110 1.000 32.290 0  16  SER B CB  1 
ATOM   2891 O OG  . SER B 1 16  ? 27.663  33.193  30.158 1.000 30.460 0  16  SER B OG  1 
ATOM   2892 N N   . ALA B 1 17  ? 26.035  31.745  31.991 1.000 30.860 0  17  ALA B N   1 
ATOM   2893 C CA  . ALA B 1 17  ? 26.246  30.387  32.448 1.000 27.310 0  17  ALA B CA  1 
ATOM   2894 C C   . ALA B 1 17  ? 27.708  30.013  32.266 1.000 28.000 0  17  ALA B C   1 
ATOM   2895 O O   . ALA B 1 17  ? 28.399  30.526  31.382 1.000 31.910 0  17  ALA B O   1 
ATOM   2896 C CB  . ALA B 1 17  ? 25.359  29.410  31.679 1.000 26.760 0  17  ALA B CB  1 
ATOM   2897 N N   . ILE B 1 18  ? 28.180  29.126  33.128 1.000 26.910 0  18  ILE B N   1 
ATOM   2898 C CA  . ILE B 1 18  ? 29.528  28.589  33.011 1.000 26.490 0  18  ILE B CA  1 
ATOM   2899 C C   . ILE B 1 18  ? 29.524  27.207  33.642 1.000 28.210 0  18  ILE B C   1 
ATOM   2900 O O   . ILE B 1 18  ? 28.835  26.968  34.638 1.000 29.140 0  18  ILE B O   1 
ATOM   2901 C CB  . ILE B 1 18  ? 30.567  29.531  33.658 1.000 28.540 0  18  ILE B CB  1 
ATOM   2902 C CG1 . ILE B 1 18  ? 31.996  29.093  33.314 1.000 29.240 0  18  ILE B CG1 1 
ATOM   2903 C CG2 . ILE B 1 18  ? 30.365  29.600  35.157 1.000 27.890 0  18  ILE B CG2 1 
ATOM   2904 C CD1 . ILE B 1 18  ? 32.985  30.242  33.202 1.000 27.260 0  18  ILE B CD1 1 
ATOM   2905 N N   . GLY B 1 19  ? 30.265  26.279  33.039 1.000 27.970 0  19  GLY B N   1 
ATOM   2906 C CA  . GLY B 1 19  ? 30.169  24.889  33.422 1.000 27.980 0  19  GLY B CA  1 
ATOM   2907 C C   . GLY B 1 19  ? 31.529  24.228  33.497 1.000 29.230 0  19  GLY B C   1 
ATOM   2908 O O   . GLY B 1 19  ? 32.544  24.775  33.063 1.000 32.400 0  19  GLY B O   1 
ATOM   2909 N N   . LEU B 1 20  ? 31.521  23.034  34.073 1.000 31.320 0  20  LEU B N   1 
ATOM   2910 C CA  . LEU B 1 20  ? 32.723  22.226  34.234 1.000 31.970 0  20  LEU B CA  1 
ATOM   2911 C C   . LEU B 1 20  ? 32.514  20.745  33.954 1.000 34.190 0  20  LEU B C   1 
ATOM   2912 O O   . LEU B 1 20  ? 33.470  20.080  33.545 1.000 35.580 0  20  LEU B O   1 
ATOM   2913 C CB  . LEU B 1 20  ? 33.293  22.387  35.650 1.000 32.130 0  20  LEU B CB  1 
ATOM   2914 C CG  . LEU B 1 20  ? 34.809  22.230  35.790 1.000 32.050 0  20  LEU B CG  1 
ATOM   2915 C CD1 . LEU B 1 20  ? 35.531  22.752  34.558 1.000 32.090 0  20  LEU B CD1 1 
ATOM   2916 C CD2 . LEU B 1 20  ? 35.306  22.936  37.038 1.000 32.570 0  20  LEU B CD2 1 
ATOM   2917 N N   . LEU B 1 21  ? 31.314  20.200  34.162 1.000 37.400 0  21  LEU B N   1 
ATOM   2918 C CA  . LEU B 1 21  ? 31.097  18.758  34.175 1.000 40.230 0  21  LEU B CA  1 
ATOM   2919 C C   . LEU B 1 21  ? 30.795  18.168  32.798 1.000 39.660 0  21  LEU B C   1 
ATOM   2920 O O   . LEU B 1 21  ? 31.416  17.176  32.403 1.000 39.720 0  21  LEU B O   1 
ATOM   2921 C CB  . LEU B 1 21  ? 29.965  18.423  35.154 1.000 36.990 0  21  LEU B CB  1 
ATOM   2922 C CG  . LEU B 1 21  ? 30.341  18.530  36.636 1.000 35.660 0  21  LEU B CG  1 
ATOM   2923 C CD1 . LEU B 1 21  ? 29.364  17.748  37.501 1.000 31.310 0  21  LEU B CD1 1 
ATOM   2924 C CD2 . LEU B 1 21  ? 31.771  18.054  36.866 1.000 31.820 0  21  LEU B CD2 1 
ATOM   2925 N N   . GLU B 1 22  ? 29.855  18.751  32.058 1.000 41.040 0  22  GLU B N   1 
ATOM   2926 C CA  . GLU B 1 22  ? 29.292  18.104  30.878 1.000 43.640 0  22  GLU B CA  1 
ATOM   2927 C C   . GLU B 1 22  ? 29.969  18.560  29.592 1.000 43.420 0  22  GLU B C   1 
ATOM   2928 O O   . GLU B 1 22  ? 30.343  19.730  29.453 1.000 42.270 0  22  GLU B O   1 
ATOM   2929 C CB  . GLU B 1 22  ? 27.788  18.378  30.782 1.000 41.570 0  22  GLU B CB  1 
ATOM   2930 C CG  . GLU B 1 22  ? 26.995  17.960  32.010 1.000 43.780 0  22  GLU B CG  1 
ATOM   2931 C CD  . GLU B 1 22  ? 25.575  17.536  31.672 1.000 43.510 0  22  GLU B CD  1 
ATOM   2932 O OE1 . GLU B 1 22  ? 25.038  18.001  30.644 1.000 41.210 0  22  GLU B OE1 1 
ATOM   2933 O OE2 . GLU B 1 22  ? 24.996  16.731  32.436 1.000 44.290 -1 22  GLU B OE2 1 
ATOM   2934 N N   . ASP B 1 23  ? 30.118  17.619  28.656 1.000 44.860 0  23  ASP B N   1 
ATOM   2935 C CA  . ASP B 1 23  ? 30.588  17.869  27.292 1.000 45.380 0  23  ASP B CA  1 
ATOM   2936 C C   . ASP B 1 23  ? 31.896  18.662  27.289 1.000 47.680 0  23  ASP B C   1 
ATOM   2937 O O   . ASP B 1 23  ? 32.006  19.742  26.705 1.000 48.760 0  23  ASP B O   1 
ATOM   2938 C CB  . ASP B 1 23  ? 29.503  18.576  26.472 1.000 44.520 0  23  ASP B CB  1 
ATOM   2939 C CG  . ASP B 1 23  ? 28.292  17.687  26.209 1.000 46.150 0  23  ASP B CG  1 
ATOM   2940 O OD1 . ASP B 1 23  ? 28.482  16.516  25.808 1.000 47.550 0  23  ASP B OD1 1 
ATOM   2941 O OD2 . ASP B 1 23  ? 27.150  18.158  26.404 1.000 42.860 -1 23  ASP B OD2 1 
ATOM   2942 N N   . GLN B 1 24  ? 32.906  18.087  27.943 1.000 47.220 0  24  GLN B N   1 
ATOM   2943 C CA  . GLN B 1 24  ? 34.116  18.844  28.240 1.000 47.960 0  24  GLN B CA  1 
ATOM   2944 C C   . GLN B 1 24  ? 35.095  18.863  27.071 1.000 48.780 0  24  GLN B C   1 
ATOM   2945 O O   . GLN B 1 24  ? 35.742  19.887  26.823 1.000 50.170 0  24  GLN B O   1 
ATOM   2946 C CB  . GLN B 1 24  ? 34.788  18.284  29.493 1.000 48.700 0  24  GLN B CB  1 
ATOM   2947 C CG  . GLN B 1 24  ? 34.281  18.923  30.771 1.000 42.860 0  24  GLN B CG  1 
ATOM   2948 C CD  . GLN B 1 24  ? 34.063  20.418  30.617 1.000 42.670 0  24  GLN B CD  1 
ATOM   2949 O OE1 . GLN B 1 24  ? 32.941  20.878  30.395 1.000 39.810 0  24  GLN B OE1 1 
ATOM   2950 N NE2 . GLN B 1 24  ? 35.141  21.186  30.728 1.000 43.530 0  24  GLN B NE2 1 
ATOM   2951 N N   . ASP B 1 25  ? 35.212  17.754  26.339 1.000 48.510 0  25  ASP B N   1 
ATOM   2952 C CA  . ASP B 1 25  ? 36.179  17.692  25.246 1.000 49.610 0  25  ASP B CA  1 
ATOM   2953 C C   . ASP B 1 25  ? 35.900  18.740  24.176 1.000 51.270 0  25  ASP B C   1 
ATOM   2954 O O   . ASP B 1 25  ? 36.826  19.179  23.482 1.000 52.670 0  25  ASP B O   1 
ATOM   2955 C CB  . ASP B 1 25  ? 36.160  16.300  24.621 1.000 50.250 0  25  ASP B CB  1 
ATOM   2956 C CG  . ASP B 1 25  ? 34.749  15.815  24.339 1.000 54.230 0  25  ASP B CG  1 
ATOM   2957 O OD1 . ASP B 1 25  ? 33.791  16.552  24.665 1.000 50.860 0  25  ASP B OD1 1 
ATOM   2958 O OD2 . ASP B 1 25  ? 34.597  14.702  23.790 1.000 59.870 -1 25  ASP B OD2 1 
ATOM   2959 N N   . THR B 1 26  ? 34.645  19.163  24.037 1.000 48.650 0  26  THR B N   1 
ATOM   2960 C CA  . THR B 1 26  ? 34.240  20.102  22.999 1.000 48.530 0  26  THR B CA  1 
ATOM   2961 C C   . THR B 1 26  ? 33.823  21.456  23.552 1.000 46.890 0  26  THR B C   1 
ATOM   2962 O O   . THR B 1 26  ? 34.267  22.492  23.047 1.000 48.420 0  26  THR B O   1 
ATOM   2963 C CB  . THR B 1 26  ? 33.096  19.504  22.163 1.000 49.370 0  26  THR B CB  1 
ATOM   2964 O OG1 . THR B 1 26  ? 31.910  19.405  22.962 1.000 48.320 0  26  THR B OG1 1 
ATOM   2965 C CG2 . THR B 1 26  ? 33.480  18.121  21.651 1.000 46.200 0  26  THR B CG2 1 
ATOM   2966 N N   . ARG B 1 27  ? 32.988  21.479  24.585 1.000 45.280 0  27  ARG B N   1 
ATOM   2967 C CA  . ARG B 1 27  ? 32.448  22.724  25.137 1.000 43.690 0  27  ARG B CA  1 
ATOM   2968 C C   . ARG B 1 27  ? 33.241  23.186  26.355 1.000 42.830 0  27  ARG B C   1 
ATOM   2969 O O   . ARG B 1 27  ? 32.676  23.486  27.408 1.000 41.500 0  27  ARG B O   1 
ATOM   2970 C CB  . ARG B 1 27  ? 30.974  22.540  25.488 1.000 40.080 0  27  ARG B CB  1 
ATOM   2971 C CG  . ARG B 1 27  ? 30.146  21.844  24.417 1.000 41.270 0  27  ARG B CG  1 
ATOM   2972 C CD  . ARG B 1 27  ? 28.716  22.382  24.369 1.000 39.240 0  27  ARG B CD  1 
ATOM   2973 N NE  . ARG B 1 27  ? 27.867  21.803  25.405 1.000 40.150 0  27  ARG B NE  1 
ATOM   2974 C CZ  . ARG B 1 27  ? 27.617  22.373  26.577 1.000 39.990 0  27  ARG B CZ  1 
ATOM   2975 N NH1 . ARG B 1 27  ? 28.121  23.555  26.894 1.000 34.480 1  27  ARG B NH1 1 
ATOM   2976 N NH2 . ARG B 1 27  ? 26.833  21.744  27.451 1.000 40.140 0  27  ARG B NH2 1 
ATOM   2977 N N   . LYS B 1 28  ? 34.566  23.253  26.222 1.000 43.810 0  28  LYS B N   1 
ATOM   2978 C CA  . LYS B 1 28  ? 35.438  23.628  27.332 1.000 41.370 0  28  LYS B CA  1 
ATOM   2979 C C   . LYS B 1 28  ? 35.231  25.099  27.674 1.000 37.850 0  28  LYS B C   1 
ATOM   2980 O O   . LYS B 1 28  ? 35.539  25.983  26.868 1.000 39.470 0  28  LYS B O   1 
ATOM   2981 C CB  . LYS B 1 28  ? 36.894  23.348  26.969 1.000 38.970 0  28  LYS B CB  1 
ATOM   2982 C CG  . LYS B 1 28  ? 37.883  23.616  28.092 1.000 36.250 0  28  LYS B CG  1 
ATOM   2983 C CD  . LYS B 1 28  ? 38.987  22.567  28.116 1.000 37.600 0  28  LYS B CD  1 
ATOM   2984 C CE  . LYS B 1 28  ? 38.418  21.167  27.927 1.000 42.300 0  28  LYS B CE  1 
ATOM   2985 N NZ  . LYS B 1 28  ? 39.302  20.096  28.469 1.000 44.760 1  28  LYS B NZ  1 
ATOM   2986 N N   . SER B 1 29  ? 34.698  25.369  28.869 1.000 34.860 0  29  SER B N   1 
ATOM   2987 C CA  . SER B 1 29  ? 34.345  26.731  29.260 1.000 35.260 0  29  SER B CA  1 
ATOM   2988 C C   . SER B 1 29  ? 35.183  27.205  30.442 1.000 33.110 0  29  SER B C   1 
ATOM   2989 O O   . SER B 1 29  ? 36.083  28.027  30.253 1.000 31.610 0  29  SER B O   1 
ATOM   2990 C CB  . SER B 1 29  ? 32.843  26.812  29.556 1.000 33.720 0  29  SER B CB  1 
ATOM   2991 O OG  . SER B 1 29  ? 32.565  26.608  30.931 1.000 32.130 0  29  SER B OG  1 
ATOM   2992 N N   . PHE B 1 30  ? 34.927  26.704  31.653 1.000 32.890 0  30  PHE B N   1 
ATOM   2993 C CA  . PHE B 1 30  ? 35.628  27.209  32.828 1.000 30.100 0  30  PHE B CA  1 
ATOM   2994 C C   . PHE B 1 30  ? 37.115  26.889  32.781 1.000 31.900 0  30  PHE B C   1 
ATOM   2995 O O   . PHE B 1 30  ? 37.929  27.656  33.306 1.000 32.120 0  30  PHE B O   1 
ATOM   2996 C CB  . PHE B 1 30  ? 34.997  26.638  34.095 1.000 31.760 0  30  PHE B CB  1 
ATOM   2997 C CG  . PHE B 1 30  ? 35.684  27.061  35.358 1.000 30.790 0  30  PHE B CG  1 
ATOM   2998 C CD1 . PHE B 1 30  ? 35.419  28.295  35.923 1.000 29.600 0  30  PHE B CD1 1 
ATOM   2999 C CD2 . PHE B 1 30  ? 36.581  26.218  35.992 1.000 31.800 0  30  PHE B CD2 1 
ATOM   3000 C CE1 . PHE B 1 30  ? 36.043  28.687  37.088 1.000 30.190 0  30  PHE B CE1 1 
ATOM   3001 C CE2 . PHE B 1 30  ? 37.207  26.604  37.160 1.000 31.990 0  30  PHE B CE2 1 
ATOM   3002 C CZ  . PHE B 1 30  ? 36.937  27.840  37.707 1.000 30.930 0  30  PHE B CZ  1 
ATOM   3003 N N   . ARG B 1 31  ? 37.490  25.766  32.167 1.000 31.050 0  31  ARG B N   1 
ATOM   3004 C CA  . ARG B 1 31  ? 38.895  25.389  32.109 1.000 29.840 0  31  ARG B CA  1 
ATOM   3005 C C   . ARG B 1 31  ? 39.693  26.256  31.144 1.000 30.750 0  31  ARG B C   1 
ATOM   3006 O O   . ARG B 1 31  ? 40.924  26.148  31.111 1.000 30.570 0  31  ARG B O   1 
ATOM   3007 C CB  . ARG B 1 31  ? 39.030  23.921  31.698 1.000 29.330 0  31  ARG B CB  1 
ATOM   3008 C CG  . ARG B 1 31  ? 38.672  22.927  32.784 1.000 29.160 0  31  ARG B CG  1 
ATOM   3009 C CD  . ARG B 1 31  ? 39.590  23.062  33.980 1.000 29.380 0  31  ARG B CD  1 
ATOM   3010 N NE  . ARG B 1 31  ? 39.165  22.210  35.084 1.000 29.260 0  31  ARG B NE  1 
ATOM   3011 C CZ  . ARG B 1 31  ? 39.083  22.605  36.347 1.000 29.160 0  31  ARG B CZ  1 
ATOM   3012 N NH1 . ARG B 1 31  ? 39.399  23.838  36.708 1.000 29.170 1  31  ARG B NH1 1 
ATOM   3013 N NH2 . ARG B 1 31  ? 38.679  21.740  37.273 1.000 29.090 0  31  ARG B NH2 1 
ATOM   3014 N N   . ASP B 1 32  ? 39.030  27.112  30.371 1.000 29.610 0  32  ASP B N   1 
ATOM   3015 C CA  . ASP B 1 32  ? 39.716  27.976  29.427 1.000 29.460 0  32  ASP B CA  1 
ATOM   3016 C C   . ASP B 1 32  ? 39.957  29.331  30.069 1.000 29.420 0  32  ASP B C   1 
ATOM   3017 O O   . ASP B 1 32  ? 38.993  30.084  30.279 1.000 29.370 0  32  ASP B O   1 
ATOM   3018 C CB  . ASP B 1 32  ? 38.895  28.130  28.150 1.000 29.940 0  32  ASP B CB  1 
ATOM   3019 C CG  . ASP B 1 32  ? 39.649  28.857  27.052 1.000 30.320 0  32  ASP B CG  1 
ATOM   3020 O OD1 . ASP B 1 32  ? 40.814  29.248  27.276 1.000 33.570 0  32  ASP B OD1 1 
ATOM   3021 O OD2 . ASP B 1 32  ? 39.069  29.044  25.963 1.000 29.580 -1 32  ASP B OD2 1 
ATOM   3022 N N   . PRO B 1 33  ? 41.199  29.686  30.405 1.000 29.780 0  33  PRO B N   1 
ATOM   3023 C CA  . PRO B 1 33  ? 41.438  30.999  31.028 1.000 29.760 0  33  PRO B CA  1 
ATOM   3024 C C   . PRO B 1 33  ? 40.972  32.157  30.164 1.000 29.660 0  33  PRO B C   1 
ATOM   3025 O O   . PRO B 1 33  ? 40.556  33.191  30.700 1.000 29.470 0  33  PRO B O   1 
ATOM   3026 C CB  . PRO B 1 33  ? 42.960  31.021  31.243 1.000 30.250 0  33  PRO B CB  1 
ATOM   3027 C CG  . PRO B 1 33  ? 43.504  29.925  30.368 1.000 30.540 0  33  PRO B CG  1 
ATOM   3028 C CD  . PRO B 1 33  ? 42.431  28.890  30.287 1.000 30.220 0  33  PRO B CD  1 
ATOM   3029 N N   . ALA B 1 34  ? 41.047  32.017  28.837 1.000 29.810 0  34  ALA B N   1 
ATOM   3030 C CA  . ALA B 1 34  ? 40.554  33.068  27.952 1.000 29.740 0  34  ALA B CA  1 
ATOM   3031 C C   . ALA B 1 34  ? 39.045  33.234  28.084 1.000 29.400 0  34  ALA B C   1 
ATOM   3032 O O   . ALA B 1 34  ? 38.530  34.359  28.071 1.000 30.440 0  34  ALA B O   1 
ATOM   3033 C CB  . ALA B 1 34  ? 40.934  32.754  26.507 1.000 30.020 0  34  ALA B CB  1 
ATOM   3034 N N   . TYR B 1 35  ? 38.318  32.124  28.221 1.000 29.040 0  35  TYR B N   1 
ATOM   3035 C CA  . TYR B 1 35  ? 36.877  32.225  28.402 1.000 28.610 0  35  TYR B CA  1 
ATOM   3036 C C   . TYR B 1 35  ? 36.534  32.875  29.736 1.000 28.790 0  35  TYR B C   1 
ATOM   3037 O O   . TYR B 1 35  ? 35.645  33.732  29.804 1.000 32.420 0  35  TYR B O   1 
ATOM   3038 C CB  . TYR B 1 35  ? 36.232  30.845  28.299 1.000 28.450 0  35  TYR B CB  1 
ATOM   3039 C CG  . TYR B 1 35  ? 34.726  30.898  28.216 1.000 29.200 0  35  TYR B CG  1 
ATOM   3040 C CD1 . TYR B 1 35  ? 34.096  31.356  27.069 1.000 28.380 0  35  TYR B CD1 1 
ATOM   3041 C CD2 . TYR B 1 35  ? 33.935  30.502  29.285 1.000 28.310 0  35  TYR B CD2 1 
ATOM   3042 C CE1 . TYR B 1 35  ? 32.722  31.412  26.986 1.000 28.830 0  35  TYR B CE1 1 
ATOM   3043 C CE2 . TYR B 1 35  ? 32.561  30.554  29.210 1.000 29.220 0  35  TYR B CE2 1 
ATOM   3044 C CZ  . TYR B 1 35  ? 31.957  31.011  28.058 1.000 29.560 0  35  TYR B CZ  1 
ATOM   3045 O OH  . TYR B 1 35  ? 30.583  31.069  27.976 1.000 28.910 0  35  TYR B OH  1 
ATOM   3046 N N   . ARG B 1 36  ? 37.226  32.478  30.809 1.000 28.490 0  36  ARG B N   1 
ATOM   3047 C CA  . ARG B 1 36  ? 37.012  33.130  32.097 1.000 29.610 0  36  ARG B CA  1 
ATOM   3048 C C   . ARG B 1 36  ? 37.299  34.622  32.013 1.000 31.570 0  36  ARG B C   1 
ATOM   3049 O O   . ARG B 1 36  ? 36.554  35.435  32.571 1.000 30.980 0  36  ARG B O   1 
ATOM   3050 C CB  . ARG B 1 36  ? 37.871  32.474  33.177 1.000 28.520 0  36  ARG B CB  1 
ATOM   3051 C CG  . ARG B 1 36  ? 37.641  30.986  33.327 1.000 28.470 0  36  ARG B CG  1 
ATOM   3052 C CD  . ARG B 1 36  ? 38.203  30.471  34.638 1.000 28.570 0  36  ARG B CD  1 
ATOM   3053 N NE  . ARG B 1 36  ? 39.644  30.663  34.731 1.000 28.990 0  36  ARG B NE  1 
ATOM   3054 C CZ  . ARG B 1 36  ? 40.540  29.735  34.427 1.000 29.300 0  36  ARG B CZ  1 
ATOM   3055 N NH1 . ARG B 1 36  ? 40.176  28.535  34.005 1.000 29.250 1  36  ARG B NH1 1 
ATOM   3056 N NH2 . ARG B 1 36  ? 41.834  30.014  34.558 1.000 29.690 0  36  ARG B NH2 1 
ATOM   3057 N N   . ALA B 1 37  ? 38.372  35.003  31.313 1.000 29.150 0  37  ALA B N   1 
ATOM   3058 C CA  . ALA B 1 37  ? 38.711  36.417  31.204 1.000 31.660 0  37  ALA B CA  1 
ATOM   3059 C C   . ALA B 1 37  ? 37.652  37.179  30.414 1.000 31.740 0  37  ALA B C   1 
ATOM   3060 O O   . ALA B 1 37  ? 37.289  38.303  30.779 1.000 34.100 0  37  ALA B O   1 
ATOM   3061 C CB  . ALA B 1 37  ? 40.086  36.579  30.557 1.000 30.600 0  37  ALA B CB  1 
ATOM   3062 N N   . LEU B 1 38  ? 37.129  36.577  29.343 1.000 31.260 0  38  LEU B N   1 
ATOM   3063 C CA  . LEU B 1 38  ? 36.060  37.218  28.581 1.000 33.090 0  38  LEU B CA  1 
ATOM   3064 C C   . LEU B 1 38  ? 34.807  37.399  29.434 1.000 30.860 0  38  LEU B C   1 
ATOM   3065 O O   . LEU B 1 38  ? 34.189  38.473  29.439 1.000 30.620 0  38  LEU B O   1 
ATOM   3066 C CB  . LEU B 1 38  ? 35.746  36.399  27.328 1.000 34.140 0  38  LEU B CB  1 
ATOM   3067 C CG  . LEU B 1 38  ? 34.458  36.777  26.593 1.000 33.480 0  38  LEU B CG  1 
ATOM   3068 C CD1 . LEU B 1 38  ? 34.564  38.175  26.000 1.000 31.390 0  38  LEU B CD1 1 
ATOM   3069 C CD2 . LEU B 1 38  ? 34.136  35.758  25.516 1.000 32.650 0  38  LEU B CD2 1 
ATOM   3070 N N   . MET B 1 39  ? 34.406  36.346  30.151 1.000 32.240 0  39  MET B N   1 
ATOM   3071 C CA  . MET B 1 39  ? 33.231  36.441  31.013 1.000 33.030 0  39  MET B CA  1 
ATOM   3072 C C   . MET B 1 39  ? 33.412  37.505  32.089 1.000 33.450 0  39  MET B C   1 
ATOM   3073 O O   . MET B 1 39  ? 32.493  38.289  32.357 1.000 33.570 0  39  MET B O   1 
ATOM   3074 C CB  . MET B 1 39  ? 32.931  35.089  31.652 1.000 31.590 0  39  MET B CB  1 
ATOM   3075 C CG  . MET B 1 39  ? 31.510  34.992  32.161 1.000 35.490 0  39  MET B CG  1 
ATOM   3076 S SD  . MET B 1 39  ? 30.977  33.296  32.409 1.000 37.550 0  39  MET B SD  1 
ATOM   3077 C CE  . MET B 1 39  ? 29.951  33.492  33.863 1.000 33.150 0  39  MET B CE  1 
ATOM   3078 N N   . ALA B 1 40  ? 34.585  37.536  32.727 1.000 31.440 0  40  ALA B N   1 
ATOM   3079 C CA  . ALA B 1 40  ? 34.843  38.536  33.755 1.000 31.220 0  40  ALA B CA  1 
ATOM   3080 C C   . ALA B 1 40  ? 34.877  39.938  33.170 1.000 30.220 0  40  ALA B C   1 
ATOM   3081 O O   . ALA B 1 40  ? 34.569  40.908  33.872 1.000 31.420 0  40  ALA B O   1 
ATOM   3082 C CB  . ALA B 1 40  ? 36.159  38.231  34.469 1.000 32.860 0  40  ALA B CB  1 
ATOM   3083 N N   . ARG B 1 41  ? 35.256  40.067  31.897 1.000 29.810 0  41  ARG B N   1 
ATOM   3084 C CA  . ARG B 1 41  ? 35.207  41.368  31.244 1.000 28.320 0  41  ARG B CA  1 
ATOM   3085 C C   . ARG B 1 41  ? 33.766  41.816  31.033 1.000 29.930 0  41  ARG B C   1 
ATOM   3086 O O   . ARG B 1 41  ? 33.398  42.946  31.376 1.000 30.560 0  41  ARG B O   1 
ATOM   3087 C CB  . ARG B 1 41  ? 35.958  41.321  29.914 1.000 32.650 0  41  ARG B CB  1 
ATOM   3088 C CG  . ARG B 1 41  ? 37.364  41.906  29.968 1.000 33.910 0  41  ARG B CG  1 
ATOM   3089 C CD  . ARG B 1 41  ? 38.011  41.926  28.588 1.000 36.070 0  41  ARG B CD  1 
ATOM   3090 N NE  . ARG B 1 41  ? 37.914  40.639  27.909 1.000 38.620 0  41  ARG B NE  1 
ATOM   3091 C CZ  . ARG B 1 41  ? 38.938  39.821  27.702 1.000 40.100 0  41  ARG B CZ  1 
ATOM   3092 N NH1 . ARG B 1 41  ? 40.160  40.127  28.105 1.000 37.340 1  41  ARG B NH1 1 
ATOM   3093 N NH2 . ARG B 1 41  ? 38.730  38.669  27.069 1.000 38.650 0  41  ARG B NH2 1 
ATOM   3094 N N   . GLU B 1 42  ? 32.935  40.945  30.459 1.000 29.930 0  42  GLU B N   1 
ATOM   3095 C CA  . GLU B 1 42  ? 31.600  41.351  30.038 1.000 29.740 0  42  GLU B CA  1 
ATOM   3096 C C   . GLU B 1 42  ? 30.521  41.161  31.099 1.000 30.680 0  42  GLU B C   1 
ATOM   3097 O O   . GLU B 1 42  ? 29.431  41.723  30.945 1.000 29.870 0  42  GLU B O   1 
ATOM   3098 C CB  . GLU B 1 42  ? 31.186  40.576  28.783 1.000 30.160 0  42  GLU B CB  1 
ATOM   3099 C CG  . GLU B 1 42  ? 32.069  40.821  27.576 1.000 28.640 0  42  GLU B CG  1 
ATOM   3100 C CD  . GLU B 1 42  ? 32.116  42.279  27.187 1.000 27.830 0  42  GLU B CD  1 
ATOM   3101 O OE1 . GLU B 1 42  ? 31.037  42.881  26.996 1.000 27.670 0  42  GLU B OE1 1 
ATOM   3102 O OE2 . GLU B 1 42  ? 33.234  42.821  27.069 1.000 28.130 -1 42  GLU B OE2 1 
ATOM   3103 N N   . CYS B 1 43  ? 30.775  40.403  32.163 1.000 31.640 0  43  CYS B N   1 
ATOM   3104 C CA  . CYS B 1 43  ? 29.713  40.028  33.088 1.000 32.160 0  43  CYS B CA  1 
ATOM   3105 C C   . CYS B 1 43  ? 30.084  40.330  34.531 1.000 31.920 0  43  CYS B C   1 
ATOM   3106 O O   . CYS B 1 43  ? 31.260  40.349  34.903 1.000 32.050 0  43  CYS B O   1 
ATOM   3107 C CB  . CYS B 1 43  ? 29.366  38.542  32.964 1.000 32.610 0  43  CYS B CB  1 
ATOM   3108 S SG  . CYS B 1 43  ? 28.669  38.080  31.374 1.000 34.310 0  43  CYS B SG  1 
ATOM   3109 N N   . ASN B 1 44  ? 29.050  40.568  35.341 1.000 29.160 0  44  ASN B N   1 
ATOM   3110 C CA  . ASN B 1 44  ? 29.183  40.601  36.791 1.000 31.900 0  44  ASN B CA  1 
ATOM   3111 C C   . ASN B 1 44  ? 28.241  39.608  37.469 1.000 31.970 0  44  ASN B C   1 
ATOM   3112 O O   . ASN B 1 44  ? 28.002  39.714  38.678 1.000 30.280 0  44  ASN B O   1 
ATOM   3113 C CB  . ASN B 1 44  ? 28.962  42.018  37.332 1.000 29.710 0  44  ASN B CB  1 
ATOM   3114 C CG  . ASN B 1 44  ? 27.609  42.597  36.951 1.000 29.740 0  44  ASN B CG  1 
ATOM   3115 O OD1 . ASN B 1 44  ? 26.765  41.916  36.372 1.000 29.510 0  44  ASN B OD1 1 
ATOM   3116 N ND2 . ASN B 1 44  ? 27.398  43.867  37.282 1.000 28.150 0  44  ASN B ND2 1 
ATOM   3117 N N   . MET B 1 45  ? 27.698  38.641  36.721 1.000 30.570 0  45  MET B N   1 
ATOM   3118 C CA  . MET B 1 45  ? 26.818  37.637  37.308 1.000 28.020 0  45  MET B CA  1 
ATOM   3119 C C   . MET B 1 45  ? 27.074  36.265  36.697 1.000 29.630 0  45  MET B C   1 
ATOM   3120 O O   . MET B 1 45  ? 27.252  36.131  35.483 1.000 28.280 0  45  MET B O   1 
ATOM   3121 C CB  . MET B 1 45  ? 25.350  38.023  37.129 1.000 25.800 0  45  MET B CB  1 
ATOM   3122 C CG  . MET B 1 45  ? 24.409  37.230  38.004 1.000 26.970 0  45  MET B CG  1 
ATOM   3123 S SD  . MET B 1 45  ? 22.726  37.858  37.954 1.000 25.420 0  45  MET B SD  1 
ATOM   3124 C CE  . MET B 1 45  ? 22.652  38.502  36.282 1.000 25.450 0  45  MET B CE  1 
ATOM   3125 N N   . ILE B 1 46  ? 27.055  35.241  37.547 1.000 28.430 0  46  ILE B N   1 
ATOM   3126 C CA  . ILE B 1 46  ? 27.402  33.877  37.167 1.000 28.210 0  46  ILE B CA  1 
ATOM   3127 C C   . ILE B 1 46  ? 26.240  32.955  37.509 1.000 27.790 0  46  ILE B C   1 
ATOM   3128 O O   . ILE B 1 46  ? 25.545  33.158  38.509 1.000 25.660 0  46  ILE B O   1 
ATOM   3129 C CB  . ILE B 1 46  ? 28.693  33.423  37.884 1.000 29.110 0  46  ILE B CB  1 
ATOM   3130 C CG1 . ILE B 1 46  ? 28.916  31.915  37.788 1.000 28.840 0  46  ILE B CG1 1 
ATOM   3131 C CG2 . ILE B 1 46  ? 28.644  33.786  39.338 1.000 30.260 0  46  ILE B CG2 1 
ATOM   3132 C CD1 . ILE B 1 46  ? 30.357  31.521  38.039 1.000 27.050 0  46  ILE B CD1 1 
ATOM   3133 N N   . VAL B 1 47  ? 26.025  31.948  36.666 1.000 28.610 0  47  VAL B N   1 
ATOM   3134 C CA  . VAL B 1 47  ? 25.144  30.835  36.987 1.000 27.980 0  47  VAL B CA  1 
ATOM   3135 C C   . VAL B 1 47  ? 25.829  29.558  36.521 1.000 26.360 0  47  VAL B C   1 
ATOM   3136 O O   . VAL B 1 47  ? 26.572  29.556  35.534 1.000 28.080 0  47  VAL B O   1 
ATOM   3137 C CB  . VAL B 1 47  ? 23.741  31.001  36.353 1.000 27.840 0  47  VAL B CB  1 
ATOM   3138 C CG1 . VAL B 1 47  ? 23.840  31.156  34.853 1.000 28.620 0  47  VAL B CG1 1 
ATOM   3139 C CG2 . VAL B 1 47  ? 22.841  29.841  36.711 1.000 25.970 0  47  VAL B CG2 1 
ATOM   3140 N N   . ALA B 1 48  ? 25.620  28.479  37.273 1.000 25.630 0  48  ALA B N   1 
ATOM   3141 C CA  . ALA B 1 48  ? 26.223  27.187  36.973 1.000 25.760 0  48  ALA B CA  1 
ATOM   3142 C C   . ALA B 1 48  ? 25.337  26.444  35.981 1.000 25.610 0  48  ALA B C   1 
ATOM   3143 O O   . ALA B 1 48  ? 24.150  26.222  36.250 1.000 26.550 0  48  ALA B O   1 
ATOM   3144 C CB  . ALA B 1 48  ? 26.414  26.367  38.247 1.000 25.810 0  48  ALA B CB  1 
ATOM   3145 N N   . GLU B 1 49  ? 25.911  26.063  34.838 1.000 25.740 0  49  GLU B N   1 
ATOM   3146 C CA  . GLU B 1 49  ? 25.128  25.402  33.799 1.000 25.630 0  49  GLU B CA  1 
ATOM   3147 C C   . GLU B 1 49  ? 24.569  24.071  34.286 1.000 25.550 0  49  GLU B C   1 
ATOM   3148 O O   . GLU B 1 49  ? 23.424  23.721  33.978 1.000 25.710 0  49  GLU B O   1 
ATOM   3149 C CB  . GLU B 1 49  ? 25.974  25.206  32.542 1.000 25.830 0  49  GLU B CB  1 
ATOM   3150 C CG  . GLU B 1 49  ? 25.262  24.455  31.419 1.000 26.560 0  49  GLU B CG  1 
ATOM   3151 C CD  . GLU B 1 49  ? 25.676  24.930  30.037 1.000 28.740 0  49  GLU B CD  1 
ATOM   3152 O OE1 . GLU B 1 49  ? 26.078  26.105  29.909 1.000 28.530 0  49  GLU B OE1 1 
ATOM   3153 O OE2 . GLU B 1 49  ? 25.594  24.131  29.077 1.000 29.420 -1 49  GLU B OE2 1 
ATOM   3154 N N   . ASN B 1 50  ? 25.348  23.326  35.069 1.000 25.710 0  50  ASN B N   1 
ATOM   3155 C CA  . ASN B 1 50  ? 24.930  21.996  35.492 1.000 25.670 0  50  ASN B CA  1 
ATOM   3156 C C   . ASN B 1 50  ? 25.349  21.635  36.907 1.000 25.760 0  50  ASN B C   1 
ATOM   3157 O O   . ASN B 1 50  ? 24.852  20.637  37.436 1.000 25.720 0  50  ASN B O   1 
ATOM   3158 C CB  . ASN B 1 50  ? 25.505  20.936  34.538 1.000 27.870 0  50  ASN B CB  1 
ATOM   3159 C CG  . ASN B 1 50  ? 24.866  20.968  33.167 1.000 27.380 0  50  ASN B CG  1 
ATOM   3160 O OD1 . ASN B 1 50  ? 23.644  20.961  33.040 1.000 27.290 0  50  ASN B OD1 1 
ATOM   3161 N ND2 . ASN B 1 50  ? 25.694  21.007  32.128 1.000 28.600 0  50  ASN B ND2 1 
ATOM   3162 N N   . GLU B 1 51  ? 26.232  22.404  37.539 1.000 26.350 0  51  GLU B N   1 
ATOM   3163 C CA  . GLU B 1 51  ? 26.936  21.971  38.738 1.000 26.080 0  51  GLU B CA  1 
ATOM   3164 C C   . GLU B 1 51  ? 26.141  22.152  40.027 1.000 25.940 0  51  GLU B C   1 
ATOM   3165 O O   . GLU B 1 51  ? 26.548  21.614  41.063 1.000 26.450 0  51  GLU B O   1 
ATOM   3166 C CB  . GLU B 1 51  ? 28.275  22.708  38.828 1.000 26.320 0  51  GLU B CB  1 
ATOM   3167 C CG  . GLU B 1 51  ? 29.314  22.224  37.809 1.000 27.280 0  51  GLU B CG  1 
ATOM   3168 C CD  . GLU B 1 51  ? 28.892  22.444  36.358 1.000 28.430 0  51  GLU B CD  1 
ATOM   3169 O OE1 . GLU B 1 51  ? 28.200  23.444  36.077 1.000 26.400 0  51  GLU B OE1 1 
ATOM   3170 O OE2 . GLU B 1 51  ? 29.251  21.611  35.498 1.000 31.000 -1 51  GLU B OE2 1 
ATOM   3171 N N   . THR B 1 52  ? 25.027  22.884  40.003 1.000 25.700 0  52  THR B N   1 
ATOM   3172 C CA  . THR B 1 52  ? 24.192  23.026  41.191 1.000 25.600 0  52  THR B CA  1 
ATOM   3173 C C   . THR B 1 52  ? 22.789  22.475  40.964 1.000 25.370 0  52  THR B C   1 
ATOM   3174 O O   . THR B 1 52  ? 21.862  22.809  41.709 1.000 25.250 0  52  THR B O   1 
ATOM   3175 C CB  . THR B 1 52  ? 24.129  24.485  41.647 1.000 25.550 0  52  THR B CB  1 
ATOM   3176 O OG1 . THR B 1 52  ? 24.114  25.349  40.502 1.000 26.560 0  52  THR B OG1 1 
ATOM   3177 C CG2 . THR B 1 52  ? 25.333  24.819  42.514 1.000 25.790 0  52  THR B CG2 1 
ATOM   3178 N N   . LYS B 1 53  ? 22.618  21.638  39.945 1.000 25.340 0  53  LYS B N   1 
ATOM   3179 C CA  . LYS B 1 53  ? 21.405  20.853  39.794 1.000 25.170 0  53  LYS B CA  1 
ATOM   3180 C C   . LYS B 1 53  ? 21.456  19.626  40.701 1.000 25.270 0  53  LYS B C   1 
ATOM   3181 O O   . LYS B 1 53  ? 22.526  19.159  41.103 1.000 26.220 0  53  LYS B O   1 
ATOM   3182 C CB  . LYS B 1 53  ? 21.210  20.427  38.337 1.000 25.120 0  53  LYS B CB  1 
ATOM   3183 C CG  . LYS B 1 53  ? 21.034  21.580  37.365 1.000 25.030 0  53  LYS B CG  1 
ATOM   3184 C CD  . LYS B 1 53  ? 20.712  21.072  35.969 1.000 24.980 0  53  LYS B CD  1 
ATOM   3185 C CE  . LYS B 1 53  ? 20.754  22.192  34.943 1.000 24.950 0  53  LYS B CE  1 
ATOM   3186 N NZ  . LYS B 1 53  ? 20.871  21.667  33.556 1.000 25.010 1  53  LYS B NZ  1 
ATOM   3187 N N   . TRP B 1 54  ? 20.271  19.112  41.033 1.000 25.140 0  54  TRP B N   1 
ATOM   3188 C CA  . TRP B 1 54  ? 20.183  17.978  41.948 1.000 25.240 0  54  TRP B CA  1 
ATOM   3189 C C   . TRP B 1 54  ? 20.935  16.764  41.413 1.000 27.680 0  54  TRP B C   1 
ATOM   3190 O O   . TRP B 1 54  ? 21.604  16.058  42.176 1.000 27.400 0  54  TRP B O   1 
ATOM   3191 C CB  . TRP B 1 54  ? 18.716  17.636  42.199 1.000 25.070 0  54  TRP B CB  1 
ATOM   3192 C CG  . TRP B 1 54  ? 18.465  16.897  43.473 1.000 28.330 0  54  TRP B CG  1 
ATOM   3193 C CD1 . TRP B 1 54  ? 19.395  16.315  44.290 1.000 29.010 0  54  TRP B CD1 1 
ATOM   3194 C CD2 . TRP B 1 54  ? 17.191  16.644  44.073 1.000 27.520 0  54  TRP B CD2 1 
ATOM   3195 N NE1 . TRP B 1 54  ? 18.777  15.720  45.363 1.000 27.720 0  54  TRP B NE1 1 
ATOM   3196 C CE2 . TRP B 1 54  ? 17.424  15.909  45.253 1.000 26.640 0  54  TRP B CE2 1 
ATOM   3197 C CE3 . TRP B 1 54  ? 15.875  16.969  43.728 1.000 27.840 0  54  TRP B CE3 1 
ATOM   3198 C CZ2 . TRP B 1 54  ? 16.390  15.495  46.088 1.000 27.830 0  54  TRP B CZ2 1 
ATOM   3199 C CZ3 . TRP B 1 54  ? 14.851  16.557  44.555 1.000 27.850 0  54  TRP B CZ3 1 
ATOM   3200 C CH2 . TRP B 1 54  ? 15.113  15.827  45.724 1.000 30.250 0  54  TRP B CH2 1 
ATOM   3201 N N   . GLN B 1 55  ? 20.849  16.515  40.101 1.000 28.300 0  55  GLN B N   1 
ATOM   3202 C CA  . GLN B 1 55  ? 21.492  15.341  39.515 1.000 26.510 0  55  GLN B CA  1 
ATOM   3203 C C   . GLN B 1 55  ? 23.009  15.400  39.636 1.000 27.540 0  55  GLN B C   1 
ATOM   3204 O O   . GLN B 1 55  ? 23.671  14.355  39.653 1.000 26.920 0  55  GLN B O   1 
ATOM   3205 C CB  . GLN B 1 55  ? 21.098  15.202  38.045 1.000 26.720 0  55  GLN B CB  1 
ATOM   3206 C CG  . GLN B 1 55  ? 19.812  14.430  37.805 1.000 27.110 0  55  GLN B CG  1 
ATOM   3207 C CD  . GLN B 1 55  ? 19.420  14.385  36.338 1.000 28.000 0  55  GLN B CD  1 
ATOM   3208 O OE1 . GLN B 1 55  ? 19.976  15.109  35.510 1.000 25.190 0  55  GLN B OE1 1 
ATOM   3209 N NE2 . GLN B 1 55  ? 18.457  13.533  36.009 1.000 30.360 0  55  GLN B NE2 1 
ATOM   3210 N N   . ALA B 1 56  ? 23.576  16.601  39.714 1.000 26.620 0  56  ALA B N   1 
ATOM   3211 C CA  . ALA B 1 56  ? 25.016  16.755  39.858 1.000 26.060 0  56  ALA B CA  1 
ATOM   3212 C C   . ALA B 1 56  ? 25.451  16.771  41.312 1.000 28.900 0  56  ALA B C   1 
ATOM   3213 O O   . ALA B 1 56  ? 26.568  16.341  41.624 1.000 30.660 0  56  ALA B O   1 
ATOM   3214 C CB  . ALA B 1 56  ? 25.485  18.037  39.168 1.000 26.030 0  56  ALA B CB  1 
ATOM   3215 N N   . LEU B 1 57  ? 24.592  17.255  42.209 1.000 27.620 0  57  LEU B N   1 
ATOM   3216 C CA  . LEU B 1 57  ? 24.970  17.385  43.610 1.000 28.520 0  57  LEU B CA  1 
ATOM   3217 C C   . LEU B 1 57  ? 24.824  16.069  44.358 1.000 29.480 0  57  LEU B C   1 
ATOM   3218 O O   . LEU B 1 57  ? 25.683  15.718  45.176 1.000 29.200 0  57  LEU B O   1 
ATOM   3219 C CB  . LEU B 1 57  ? 24.123  18.459  44.286 1.000 28.960 0  57  LEU B CB  1 
ATOM   3220 C CG  . LEU B 1 57  ? 24.375  19.893  43.833 1.000 29.470 0  57  LEU B CG  1 
ATOM   3221 C CD1 . LEU B 1 57  ? 23.412  20.827  44.541 1.000 25.760 0  57  LEU B CD1 1 
ATOM   3222 C CD2 . LEU B 1 57  ? 25.825  20.282  44.091 1.000 26.180 0  57  LEU B CD2 1 
ATOM   3223 N N   . GLN B 1 58  ? 23.753  15.329  44.088 1.000 30.170 0  58  GLN B N   1 
ATOM   3224 C CA  . GLN B 1 58  ? 23.427  14.099  44.808 1.000 29.040 0  58  GLN B CA  1 
ATOM   3225 C C   . GLN B 1 58  ? 23.099  12.996  43.811 1.000 28.890 0  58  GLN B C   1 
ATOM   3226 O O   . GLN B 1 58  ? 21.946  12.563  43.699 1.000 28.880 0  58  GLN B O   1 
ATOM   3227 C CB  . GLN B 1 58  ? 22.267  14.332  45.776 1.000 28.120 0  58  GLN B CB  1 
ATOM   3228 C CG  . GLN B 1 58  ? 22.449  13.671  47.131 1.000 29.000 0  58  GLN B CG  1 
ATOM   3229 C CD  . GLN B 1 58  ? 21.234  13.829  48.021 1.000 30.610 0  58  GLN B CD  1 
ATOM   3230 O OE1 . GLN B 1 58  ? 20.195  14.328  47.591 1.000 28.900 0  58  GLN B OE1 1 
ATOM   3231 N NE2 . GLN B 1 58  ? 21.359  13.402  49.273 1.000 31.000 0  58  GLN B NE2 1 
ATOM   3232 N N   . PRO B 1 59  ? 24.094  12.528  43.050 1.000 28.010 0  59  PRO B N   1 
ATOM   3233 C CA  . PRO B 1 59  ? 23.833  11.443  42.090 1.000 26.410 0  59  PRO B CA  1 
ATOM   3234 C C   . PRO B 1 59  ? 23.561  10.104  42.750 1.000 28.340 0  59  PRO B C   1 
ATOM   3235 O O   . PRO B 1 59  ? 22.998  9.215   42.098 1.000 29.180 0  59  PRO B O   1 
ATOM   3236 C CB  . PRO B 1 59  ? 25.109  11.400  41.241 1.000 26.630 0  59  PRO B CB  1 
ATOM   3237 C CG  . PRO B 1 59  ? 26.172  12.008  42.092 1.000 28.600 0  59  PRO B CG  1 
ATOM   3238 C CD  . PRO B 1 59  ? 25.531  12.822  43.187 1.000 27.640 0  59  PRO B CD  1 
ATOM   3239 N N   . LYS B 1 60  ? 23.961  9.925   44.001 1.000 28.180 0  60  LYS B N   1 
ATOM   3240 C CA  . LYS B 1 60  ? 23.660  8.743   44.792 1.000 27.420 0  60  LYS B CA  1 
ATOM   3241 C C   . LYS B 1 60  ? 23.393  9.188   46.223 1.000 29.450 0  60  LYS B C   1 
ATOM   3242 O O   . LYS B 1 60  ? 23.780  10.294  46.611 1.000 26.880 0  60  LYS B O   1 
ATOM   3243 C CB  . LYS B 1 60  ? 24.815  7.731   44.730 1.000 28.590 0  60  LYS B CB  1 
ATOM   3244 C CG  . LYS B 1 60  ? 25.758  7.732   45.929 1.000 31.480 0  60  LYS B CG  1 
ATOM   3245 C CD  . LYS B 1 60  ? 27.208  7.476   45.502 1.000 34.060 0  60  LYS B CD  1 
ATOM   3246 C CE  . LYS B 1 60  ? 28.188  7.701   46.654 1.000 33.850 0  60  LYS B CE  1 
ATOM   3247 N NZ  . LYS B 1 60  ? 29.623  7.683   46.235 1.000 31.110 1  60  LYS B NZ  1 
ATOM   3248 N N   . PRO B 1 61  ? 22.712  8.358   47.021 1.000 33.180 0  61  PRO B N   1 
ATOM   3249 C CA  . PRO B 1 61  ? 22.399  8.758   48.402 1.000 29.610 0  61  PRO B CA  1 
ATOM   3250 C C   . PRO B 1 61  ? 23.647  9.171   49.168 1.000 27.270 0  61  PRO B C   1 
ATOM   3251 O O   . PRO B 1 61  ? 24.774  8.804   48.828 1.000 28.110 0  61  PRO B O   1 
ATOM   3252 C CB  . PRO B 1 61  ? 21.771  7.498   49.018 1.000 27.120 0  61  PRO B CB  1 
ATOM   3253 C CG  . PRO B 1 61  ? 21.609  6.506   47.914 1.000 28.190 0  61  PRO B CG  1 
ATOM   3254 C CD  . PRO B 1 61  ? 22.004  7.131   46.616 1.000 27.970 0  61  PRO B CD  1 
ATOM   3255 N N   . GLY B 1 62  ? 23.433  9.949   50.222 1.000 27.270 0  62  GLY B N   1 
ATOM   3256 C CA  . GLY B 1 62  ? 24.539  10.463  50.988 1.000 27.520 0  62  GLY B CA  1 
ATOM   3257 C C   . GLY B 1 62  ? 24.814  11.928  50.721 1.000 29.120 0  62  GLY B C   1 
ATOM   3258 O O   . GLY B 1 62  ? 23.957  12.677  50.241 1.000 29.500 0  62  GLY B O   1 
ATOM   3259 N N   . PRO B 1 63  ? 26.035  12.360  51.027 1.000 29.350 0  63  PRO B N   1 
ATOM   3260 C CA  . PRO B 1 63  ? 26.351  13.792  51.007 1.000 27.500 0  63  PRO B CA  1 
ATOM   3261 C C   . PRO B 1 63  ? 26.411  14.347  49.593 1.000 28.190 0  63  PRO B C   1 
ATOM   3262 O O   . PRO B 1 63  ? 26.460  13.622  48.598 1.000 29.480 0  63  PRO B O   1 
ATOM   3263 C CB  . PRO B 1 63  ? 27.721  13.850  51.679 1.000 29.200 0  63  PRO B CB  1 
ATOM   3264 C CG  . PRO B 1 63  ? 28.327  12.516  51.370 1.000 28.990 0  63  PRO B CG  1 
ATOM   3265 C CD  . PRO B 1 63  ? 27.191  11.544  51.436 1.000 27.980 0  63  PRO B CD  1 
ATOM   3266 N N   . TYR B 1 64  ? 26.412  15.676  49.527 1.000 29.090 0  64  TYR B N   1 
ATOM   3267 C CA  . TYR B 1 64  ? 26.381  16.412  48.274 1.000 29.930 0  64  TYR B CA  1 
ATOM   3268 C C   . TYR B 1 64  ? 27.784  16.539  47.675 1.000 32.770 0  64  TYR B C   1 
ATOM   3269 O O   . TYR B 1 64  ? 28.801  16.403  48.362 1.000 30.070 0  64  TYR B O   1 
ATOM   3270 C CB  . TYR B 1 64  ? 25.775  17.801  48.490 1.000 29.300 0  64  TYR B CB  1 
ATOM   3271 C CG  . TYR B 1 64  ? 24.260  17.836  48.475 1.000 29.680 0  64  TYR B CG  1 
ATOM   3272 C CD1 . TYR B 1 64  ? 23.512  16.832  49.075 1.000 29.060 0  64  TYR B CD1 1 
ATOM   3273 C CD2 . TYR B 1 64  ? 23.578  18.881  47.862 1.000 30.740 0  64  TYR B CD2 1 
ATOM   3274 C CE1 . TYR B 1 64  ? 22.128  16.866  49.062 1.000 29.750 0  64  TYR B CE1 1 
ATOM   3275 C CE2 . TYR B 1 64  ? 22.193  18.922  47.844 1.000 28.480 0  64  TYR B CE2 1 
ATOM   3276 C CZ  . TYR B 1 64  ? 21.474  17.912  48.445 1.000 28.950 0  64  TYR B CZ  1 
ATOM   3277 O OH  . TYR B 1 64  ? 20.099  17.945  48.432 1.000 27.780 0  64  TYR B OH  1 
ATOM   3278 N N   . GLN B 1 65  ? 27.824  16.802  46.369 1.000 32.460 0  65  GLN B N   1 
ATOM   3279 C CA  . GLN B 1 65  ? 29.060  16.923  45.592 1.000 30.590 0  65  GLN B CA  1 
ATOM   3280 C C   . GLN B 1 65  ? 29.237  18.384  45.177 1.000 29.320 0  65  GLN B C   1 
ATOM   3281 O O   . GLN B 1 65  ? 28.884  18.786  44.067 1.000 27.210 0  65  GLN B O   1 
ATOM   3282 C CB  . GLN B 1 65  ? 29.029  15.992  44.381 1.000 30.790 0  65  GLN B CB  1 
ATOM   3283 C CG  . GLN B 1 65  ? 28.745  14.543  44.724 1.000 32.910 0  65  GLN B CG  1 
ATOM   3284 C CD  . GLN B 1 65  ? 29.913  13.866  45.411 1.000 36.290 0  65  GLN B CD  1 
ATOM   3285 O OE1 . GLN B 1 65  ? 29.886  13.628  46.619 1.000 36.570 0  65  GLN B OE1 1 
ATOM   3286 N NE2 . GLN B 1 65  ? 30.948  13.546  44.641 1.000 39.280 0  65  GLN B NE2 1 
ATOM   3287 N N   . TRP B 1 66  ? 29.794  19.182  46.084 1.000 29.170 0  66  TRP B N   1 
ATOM   3288 C CA  . TRP B 1 66  ? 29.941  20.618  45.885 1.000 27.130 0  66  TRP B CA  1 
ATOM   3289 C C   . TRP B 1 66  ? 31.223  21.010  45.155 1.000 30.110 0  66  TRP B C   1 
ATOM   3290 O O   . TRP B 1 66  ? 31.404  22.197  44.863 1.000 31.450 0  66  TRP B O   1 
ATOM   3291 C CB  . TRP B 1 66  ? 29.889  21.338  47.237 1.000 27.180 0  66  TRP B CB  1 
ATOM   3292 C CG  . TRP B 1 66  ? 28.541  21.302  47.892 1.000 27.010 0  66  TRP B CG  1 
ATOM   3293 C CD1 . TRP B 1 66  ? 28.208  20.666  49.053 1.000 27.050 0  66  TRP B CD1 1 
ATOM   3294 C CD2 . TRP B 1 66  ? 27.342  21.924  47.419 1.000 26.640 0  66  TRP B CD2 1 
ATOM   3295 N NE1 . TRP B 1 66  ? 26.876  20.859  49.335 1.000 28.420 0  66  TRP B NE1 1 
ATOM   3296 C CE2 . TRP B 1 66  ? 26.323  21.630  48.347 1.000 26.560 0  66  TRP B CE2 1 
ATOM   3297 C CE3 . TRP B 1 66  ? 27.032  22.708  46.305 1.000 26.450 0  66  TRP B CE3 1 
ATOM   3298 C CZ2 . TRP B 1 66  ? 25.018  22.088  48.189 1.000 28.370 0  66  TRP B CZ2 1 
ATOM   3299 C CZ3 . TRP B 1 66  ? 25.739  23.163  46.151 1.000 26.170 0  66  TRP B CZ3 1 
ATOM   3300 C CH2 . TRP B 1 66  ? 24.747  22.853  47.089 1.000 27.980 0  66  TRP B CH2 1 
ATOM   3301 N N   . GLY B 1 67  ? 32.104  20.055  44.852 1.000 28.940 0  67  GLY B N   1 
ATOM   3302 C CA  . GLY B 1 67  ? 33.412  20.332  44.300 1.000 27.860 0  67  GLY B CA  1 
ATOM   3303 C C   . GLY B 1 67  ? 33.464  21.297  43.126 1.000 28.300 0  67  GLY B C   1 
ATOM   3304 O O   . GLY B 1 67  ? 34.053  22.382  43.216 1.000 31.060 0  67  GLY B O   1 
ATOM   3305 N N   . PRO B 1 68  ? 32.859  20.918  41.995 1.000 28.110 0  68  PRO B N   1 
ATOM   3306 C CA  . PRO B 1 68  ? 32.928  21.795  40.808 1.000 28.880 0  68  PRO B CA  1 
ATOM   3307 C C   . PRO B 1 68  ? 32.245  23.138  41.012 1.000 28.300 0  68  PRO B C   1 
ATOM   3308 O O   . PRO B 1 68  ? 32.767  24.182  40.587 1.000 30.560 0  68  PRO B O   1 
ATOM   3309 C CB  . PRO B 1 68  ? 32.238  20.959  39.719 1.000 27.880 0  68  PRO B CB  1 
ATOM   3310 C CG  . PRO B 1 68  ? 32.348  19.543  40.194 1.000 27.490 0  68  PRO B CG  1 
ATOM   3311 C CD  . PRO B 1 68  ? 32.265  19.607  41.684 1.000 27.510 0  68  PRO B CD  1 
ATOM   3312 N N   . ALA B 1 69  ? 31.074  23.132  41.653 1.000 29.540 0  69  ALA B N   1 
ATOM   3313 C CA  . ALA B 1 69  ? 30.403  24.387  41.967 1.000 29.840 0  69  ALA B CA  1 
ATOM   3314 C C   . ALA B 1 69  ? 31.268  25.252  42.872 1.000 30.900 0  69  ALA B C   1 
ATOM   3315 O O   . ALA B 1 69  ? 31.336  26.472  42.694 1.000 31.440 0  69  ALA B O   1 
ATOM   3316 C CB  . ALA B 1 69  ? 29.045  24.113  42.612 1.000 26.720 0  69  ALA B CB  1 
ATOM   3317 N N   . ASP B 1 70  ? 31.928  24.638  43.856 1.000 28.820 0  70  ASP B N   1 
ATOM   3318 C CA  . ASP B 1 70  ? 32.810  25.394  44.742 1.000 29.750 0  70  ASP B CA  1 
ATOM   3319 C C   . ASP B 1 70  ? 33.975  26.015  43.981 1.000 30.360 0  70  ASP B C   1 
ATOM   3320 O O   . ASP B 1 70  ? 34.347  27.165  44.239 1.000 32.630 0  70  ASP B O   1 
ATOM   3321 C CB  . ASP B 1 70  ? 33.313  24.498  45.872 1.000 28.670 0  70  ASP B CB  1 
ATOM   3322 C CG  . ASP B 1 70  ? 32.340  24.435  47.028 1.000 27.520 0  70  ASP B CG  1 
ATOM   3323 O OD1 . ASP B 1 70  ? 31.401  25.255  47.044 1.000 28.080 0  70  ASP B OD1 1 
ATOM   3324 O OD2 . ASP B 1 70  ? 32.506  23.573  47.915 1.000 27.800 -1 70  ASP B OD2 1 
ATOM   3325 N N   . GLU B 1 71  ? 34.575  25.271  43.048 1.000 31.470 0  71  GLU B N   1 
ATOM   3326 C CA  . GLU B 1 71  ? 35.661  25.833  42.246 1.000 30.360 0  71  GLU B CA  1 
ATOM   3327 C C   . GLU B 1 71  ? 35.173  27.050  41.466 1.000 33.100 0  71  GLU B C   1 
ATOM   3328 O O   . GLU B 1 71  ? 35.761  28.146  41.545 1.000 31.480 0  71  GLU B O   1 
ATOM   3329 C CB  . GLU B 1 71  ? 36.217  24.766  41.299 1.000 29.080 0  71  GLU B CB  1 
ATOM   3330 C CG  . GLU B 1 71  ? 37.545  25.124  40.643 1.000 31.090 0  71  GLU B CG  1 
ATOM   3331 C CD  . GLU B 1 71  ? 38.275  23.912  40.075 1.000 35.540 0  71  GLU B CD  1 
ATOM   3332 O OE1 . GLU B 1 71  ? 37.846  22.765  40.339 1.000 33.400 0  71  GLU B OE1 1 
ATOM   3333 O OE2 . GLU B 1 71  ? 39.284  24.109  39.363 1.000 33.850 -1 71  GLU B OE2 1 
ATOM   3334 N N   . MET B 1 72  ? 34.071  26.879  40.728 1.000 30.490 0  72  MET B N   1 
ATOM   3335 C CA  . MET B 1 72  ? 33.566  27.972  39.906 1.000 30.410 0  72  MET B CA  1 
ATOM   3336 C C   . MET B 1 72  ? 33.143  29.159  40.764 1.000 30.540 0  72  MET B C   1 
ATOM   3337 O O   . MET B 1 72  ? 33.285  30.310  40.343 1.000 32.200 0  72  MET B O   1 
ATOM   3338 C CB  . MET B 1 72  ? 32.395  27.493  39.042 1.000 30.670 0  72  MET B CB  1 
ATOM   3339 C CG  . MET B 1 72  ? 32.773  26.544  37.897 1.000 31.460 0  72  MET B CG  1 
ATOM   3340 S SD  . MET B 1 72  ? 31.408  26.225  36.750 1.000 34.200 0  72  MET B SD  1 
ATOM   3341 C CE  . MET B 1 72  ? 30.124  25.718  37.888 1.000 26.590 0  72  MET B CE  1 
ATOM   3342 N N   . PHE B 1 73  ? 32.663  28.912  41.987 1.000 30.550 0  73  PHE B N   1 
ATOM   3343 C CA  . PHE B 1 73  ? 32.155  30.012  42.799 1.000 31.720 0  73  PHE B CA  1 
ATOM   3344 C C   . PHE B 1 73  ? 33.260  30.734  43.555 1.000 29.250 0  73  PHE B C   1 
ATOM   3345 O O   . PHE B 1 73  ? 33.151  31.942  43.787 1.000 31.020 0  73  PHE B O   1 
ATOM   3346 C CB  . PHE B 1 73  ? 31.089  29.500  43.767 1.000 31.720 0  73  PHE B CB  1 
ATOM   3347 C CG  . PHE B 1 73  ? 29.803  29.123  43.093 1.000 30.550 0  73  PHE B CG  1 
ATOM   3348 C CD1 . PHE B 1 73  ? 29.610  29.393  41.746 1.000 28.930 0  73  PHE B CD1 1 
ATOM   3349 C CD2 . PHE B 1 73  ? 28.792  28.491  43.796 1.000 29.780 0  73  PHE B CD2 1 
ATOM   3350 C CE1 . PHE B 1 73  ? 28.432  29.044  41.115 1.000 29.540 0  73  PHE B CE1 1 
ATOM   3351 C CE2 . PHE B 1 73  ? 27.608  28.139  43.169 1.000 29.620 0  73  PHE B CE2 1 
ATOM   3352 C CZ  . PHE B 1 73  ? 27.430  28.416  41.826 1.000 29.050 0  73  PHE B CZ  1 
ATOM   3353 N N   . ALA B 1 74  ? 34.332  30.035  43.930 1.000 31.360 0  74  ALA B N   1 
ATOM   3354 C CA  . ALA B 1 74  ? 35.521  30.736  44.396 1.000 29.930 0  74  ALA B CA  1 
ATOM   3355 C C   . ALA B 1 74  ? 36.055  31.653  43.306 1.000 28.890 0  74  ALA B C   1 
ATOM   3356 O O   . ALA B 1 74  ? 36.406  32.813  43.569 1.000 30.560 0  74  ALA B O   1 
ATOM   3357 C CB  . ALA B 1 74  ? 36.588  29.736  44.833 1.000 28.200 0  74  ALA B CB  1 
ATOM   3358 N N   . TRP B 1 75  ? 36.090  31.159  42.063 1.000 28.290 0  75  TRP B N   1 
ATOM   3359 C CA  . TRP B 1 75  ? 36.480  32.030  40.958 1.000 28.140 0  75  TRP B CA  1 
ATOM   3360 C C   . TRP B 1 75  ? 35.536  33.218  40.831 1.000 28.250 0  75  TRP B C   1 
ATOM   3361 O O   . TRP B 1 75  ? 35.980  34.359  40.658 1.000 29.710 0  75  TRP B O   1 
ATOM   3362 C CB  . TRP B 1 75  ? 36.514  31.252  39.645 1.000 29.230 0  75  TRP B CB  1 
ATOM   3363 C CG  . TRP B 1 75  ? 36.662  32.145  38.450 1.000 28.030 0  75  TRP B CG  1 
ATOM   3364 C CD1 . TRP B 1 75  ? 37.813  32.722  38.000 1.000 29.080 0  75  TRP B CD1 1 
ATOM   3365 C CD2 . TRP B 1 75  ? 35.626  32.568  37.556 1.000 27.760 0  75  TRP B CD2 1 
ATOM   3366 N NE1 . TRP B 1 75  ? 37.560  33.476  36.881 1.000 29.010 0  75  TRP B NE1 1 
ATOM   3367 C CE2 . TRP B 1 75  ? 36.224  33.399  36.587 1.000 27.930 0  75  TRP B CE2 1 
ATOM   3368 C CE3 . TRP B 1 75  ? 34.250  32.325  37.480 1.000 30.610 0  75  TRP B CE3 1 
ATOM   3369 C CZ2 . TRP B 1 75  ? 35.496  33.986  35.554 1.000 28.660 0  75  TRP B CZ2 1 
ATOM   3370 C CZ3 . TRP B 1 75  ? 33.528  32.910  36.453 1.000 31.220 0  75  TRP B CZ3 1 
ATOM   3371 C CH2 . TRP B 1 75  ? 34.152  33.730  35.504 1.000 31.700 0  75  TRP B CH2 1 
ATOM   3372 N N   . ALA B 1 76  ? 34.227  32.968  40.919 1.000 27.750 0  76  ALA B N   1 
ATOM   3373 C CA  . ALA B 1 76  ? 33.244  34.036  40.769 1.000 28.060 0  76  ALA B CA  1 
ATOM   3374 C C   . ALA B 1 76  ? 33.403  35.104  41.844 1.000 29.760 0  76  ALA B C   1 
ATOM   3375 O O   . ALA B 1 76  ? 33.258  36.300  41.565 1.000 31.930 0  76  ALA B O   1 
ATOM   3376 C CB  . ALA B 1 76  ? 31.835  33.447  40.806 1.000 28.700 0  76  ALA B CB  1 
ATOM   3377 N N   . ARG B 1 77  ? 33.687  34.695  43.081 1.000 29.250 0  77  ARG B N   1 
ATOM   3378 C CA  . ARG B 1 77  ? 33.857  35.673  44.149 1.000 29.100 0  77  ARG B CA  1 
ATOM   3379 C C   . ARG B 1 77  ? 35.154  36.452  43.986 1.000 32.550 0  77  ARG B C   1 
ATOM   3380 O O   . ARG B 1 77  ? 35.202  37.651  44.289 1.000 31.200 0  77  ARG B O   1 
ATOM   3381 C CB  . ARG B 1 77  ? 33.828  34.990  45.512 1.000 27.510 0  77  ARG B CB  1 
ATOM   3382 C CG  . ARG B 1 77  ? 32.534  34.292  45.831 1.000 30.650 0  77  ARG B CG  1 
ATOM   3383 C CD  . ARG B 1 77  ? 32.756  33.244  46.902 1.000 34.560 0  77  ARG B CD  1 
ATOM   3384 N NE  . ARG B 1 77  ? 31.582  32.400  47.085 1.000 36.630 0  77  ARG B NE  1 
ATOM   3385 C CZ  . ARG B 1 77  ? 31.608  31.075  47.075 1.000 37.780 0  77  ARG B CZ  1 
ATOM   3386 N NH1 . ARG B 1 77  ? 32.738  30.407  46.901 1.000 35.850 1  77  ARG B NH1 1 
ATOM   3387 N NH2 . ARG B 1 77  ? 30.473  30.403  47.249 1.000 36.470 0  77  ARG B NH2 1 
ATOM   3388 N N   . LYS B 1 78  ? 36.218  35.801  43.504 1.000 31.110 0  78  LYS B N   1 
ATOM   3389 C CA  . LYS B 1 78  ? 37.471  36.530  43.357 1.000 30.330 0  78  LYS B CA  1 
ATOM   3390 C C   . LYS B 1 78  ? 37.481  37.437  42.129 1.000 31.470 0  78  LYS B C   1 
ATOM   3391 O O   . LYS B 1 78  ? 38.360  38.301  42.022 1.000 32.910 0  78  LYS B O   1 
ATOM   3392 C CB  . LYS B 1 78  ? 38.659  35.554  43.353 1.000 31.950 0  78  LYS B CB  1 
ATOM   3393 C CG  . LYS B 1 78  ? 39.130  35.022  42.013 1.000 34.250 0  78  LYS B CG  1 
ATOM   3394 C CD  . LYS B 1 78  ? 40.437  34.248  42.211 1.000 39.220 0  78  LYS B CD  1 
ATOM   3395 C CE  . LYS B 1 78  ? 41.112  33.872  40.896 1.000 41.240 0  78  LYS B CE  1 
ATOM   3396 N NZ  . LYS B 1 78  ? 41.297  35.036  39.985 1.000 39.000 1  78  LYS B NZ  1 
ATOM   3397 N N   . GLU B 1 79  ? 36.527  37.276  41.213 1.000 31.210 0  79  GLU B N   1 
ATOM   3398 C CA  . GLU B 1 79  ? 36.293  38.245  40.151 1.000 33.140 0  79  GLU B CA  1 
ATOM   3399 C C   . GLU B 1 79  ? 35.115  39.153  40.471 1.000 31.390 0  79  GLU B C   1 
ATOM   3400 O O   . GLU B 1 79  ? 34.651  39.887  39.592 1.000 32.390 0  79  GLU B O   1 
ATOM   3401 C CB  . GLU B 1 79  ? 36.048  37.539  38.815 1.000 31.920 0  79  GLU B CB  1 
ATOM   3402 C CG  . GLU B 1 79  ? 37.202  36.696  38.314 1.000 31.500 0  79  GLU B CG  1 
ATOM   3403 C CD  . GLU B 1 79  ? 38.444  37.515  38.030 1.000 35.200 0  79  GLU B CD  1 
ATOM   3404 O OE1 . GLU B 1 79  ? 38.459  38.236  37.011 1.000 40.010 0  79  GLU B OE1 1 
ATOM   3405 O OE2 . GLU B 1 79  ? 39.410  37.422  38.817 1.000 36.010 -1 79  GLU B OE2 1 
ATOM   3406 N N   . GLY B 1 80  ? 34.626  39.119  41.710 1.000 30.050 0  80  GLY B N   1 
ATOM   3407 C CA  . GLY B 1 80  ? 33.553  39.991  42.150 1.000 31.300 0  80  GLY B CA  1 
ATOM   3408 C C   . GLY B 1 80  ? 32.264  39.830  41.373 1.000 29.290 0  80  GLY B C   1 
ATOM   3409 O O   . GLY B 1 80  ? 31.747  40.808  40.827 1.000 31.770 0  80  GLY B O   1 
ATOM   3410 N N   . MET B 1 81  ? 31.725  38.614  41.316 1.000 27.360 0  81  MET B N   1 
ATOM   3411 C CA  . MET B 1 81  ? 30.522  38.331  40.545 1.000 31.690 0  81  MET B CA  1 
ATOM   3412 C C   . MET B 1 81  ? 29.443  37.738  41.438 1.000 29.470 0  81  MET B C   1 
ATOM   3413 O O   . MET B 1 81  ? 29.703  36.797  42.196 1.000 32.250 0  81  MET B O   1 
ATOM   3414 C CB  . MET B 1 81  ? 30.822  37.373  39.391 1.000 31.770 0  81  MET B CB  1 
ATOM   3415 C CG  . MET B 1 81  ? 31.819  37.907  38.386 1.000 30.420 0  81  MET B CG  1 
ATOM   3416 S SD  . MET B 1 81  ? 32.429  36.593  37.323 1.000 37.850 0  81  MET B SD  1 
ATOM   3417 C CE  . MET B 1 81  ? 31.968  37.238  35.716 1.000 36.820 0  81  MET B CE  1 
ATOM   3418 N N   . ALA B 1 82  ? 28.233  38.283  41.338 1.000 26.330 0  82  ALA B N   1 
ATOM   3419 C CA  . ALA B 1 82  ? 27.096  37.718  42.050 1.000 29.060 0  82  ALA B CA  1 
ATOM   3420 C C   . ALA B 1 82  ? 26.728  36.363  41.459 1.000 28.620 0  82  ALA B C   1 
ATOM   3421 O O   . ALA B 1 82  ? 26.929  36.103  40.271 1.000 29.300 0  82  ALA B O   1 
ATOM   3422 C CB  . ALA B 1 82  ? 25.902  38.667  41.985 1.000 28.230 0  82  ALA B CB  1 
ATOM   3423 N N   . ILE B 1 83  ? 26.141  35.509  42.292 1.000 27.840 0  83  ILE B N   1 
ATOM   3424 C CA  . ILE B 1 83  ? 25.959  34.098  41.973 1.000 26.000 0  83  ILE B CA  1 
ATOM   3425 C C   . ILE B 1 83  ? 24.482  33.746  42.065 1.000 28.640 0  83  ILE B C   1 
ATOM   3426 O O   . ILE B 1 83  ? 23.810  34.104  43.039 1.000 27.330 0  83  ILE B O   1 
ATOM   3427 C CB  . ILE B 1 83  ? 26.788  33.203  42.912 1.000 28.310 0  83  ILE B CB  1 
ATOM   3428 C CG1 . ILE B 1 83  ? 28.264  33.601  42.858 1.000 26.260 0  83  ILE B CG1 1 
ATOM   3429 C CG2 . ILE B 1 83  ? 26.607  31.741  42.547 1.000 29.570 0  83  ILE B CG2 1 
ATOM   3430 C CD1 . ILE B 1 83  ? 29.150  32.768  43.741 1.000 29.540 0  83  ILE B CD1 1 
ATOM   3431 N N   . ARG B 1 84  ? 23.984  33.046  41.052 1.000 30.330 0  84  ARG B N   1 
ATOM   3432 C CA  . ARG B 1 84  ? 22.648  32.474  41.063 1.000 25.800 0  84  ARG B CA  1 
ATOM   3433 C C   . ARG B 1 84  ? 22.707  30.994  41.421 1.000 27.070 0  84  ARG B C   1 
ATOM   3434 O O   . ARG B 1 84  ? 23.743  30.336  41.295 1.000 26.770 0  84  ARG B O   1 
ATOM   3435 C CB  . ARG B 1 84  ? 21.969  32.638  39.702 1.000 26.740 0  84  ARG B CB  1 
ATOM   3436 C CG  . ARG B 1 84  ? 22.204  33.967  39.016 1.000 26.820 0  84  ARG B CG  1 
ATOM   3437 C CD  . ARG B 1 84  ? 21.120  34.224  37.979 1.000 25.510 0  84  ARG B CD  1 
ATOM   3438 N NE  . ARG B 1 84  ? 19.787  34.261  38.572 1.000 26.080 0  84  ARG B NE  1 
ATOM   3439 C CZ  . ARG B 1 84  ? 18.834  33.370  38.335 1.000 24.770 0  84  ARG B CZ  1 
ATOM   3440 N NH1 . ARG B 1 84  ? 19.023  32.360  37.502 1.000 24.740 1  84  ARG B NH1 1 
ATOM   3441 N NH2 . ARG B 1 84  ? 17.660  33.499  38.943 1.000 24.670 0  84  ARG B NH2 1 
ATOM   3442 N N   . GLY B 1 85  ? 21.569  30.473  41.869 1.000 31.020 0  85  GLY B N   1 
ATOM   3443 C CA  . GLY B 1 85  ? 21.449  29.054  42.128 1.000 28.360 0  85  GLY B CA  1 
ATOM   3444 C C   . GLY B 1 85  ? 20.496  28.387  41.162 1.000 28.170 0  85  GLY B C   1 
ATOM   3445 O O   . GLY B 1 85  ? 19.279  28.565  41.261 1.000 29.450 0  85  GLY B O   1 
ATOM   3446 N N   . HIS B 1 86  ? 21.035  27.616  40.221 1.000 27.910 0  86  HIS B N   1 
ATOM   3447 C CA  . HIS B 1 86  ? 20.237  26.945  39.202 1.000 26.990 0  86  HIS B CA  1 
ATOM   3448 C C   . HIS B 1 86  ? 20.573  25.465  39.217 1.000 24.900 0  86  HIS B C   1 
ATOM   3449 O O   . HIS B 1 86  ? 21.719  25.088  38.958 1.000 27.370 0  86  HIS B O   1 
ATOM   3450 C CB  . HIS B 1 86  ? 20.495  27.538  37.815 1.000 25.880 0  86  HIS B CB  1 
ATOM   3451 C CG  . HIS B 1 86  ? 19.910  26.735  36.696 1.000 24.760 0  86  HIS B CG  1 
ATOM   3452 N ND1 . HIS B 1 86  ? 18.568  26.763  36.379 1.000 24.700 0  86  HIS B ND1 1 
ATOM   3453 C CD2 . HIS B 1 86  ? 20.484  25.881  35.817 1.000 24.830 0  86  HIS B CD2 1 
ATOM   3454 C CE1 . HIS B 1 86  ? 18.342  25.961  35.354 1.000 26.010 0  86  HIS B CE1 1 
ATOM   3455 N NE2 . HIS B 1 86  ? 19.488  25.413  34.994 1.000 24.710 0  86  HIS B NE2 1 
ATOM   3456 N N   . ALA B 1 87  ? 19.590  24.634  39.539 1.000 26.080 0  87  ALA B N   1 
ATOM   3457 C CA  . ALA B 1 87  ? 18.254  24.993  39.994 1.000 28.070 0  87  ALA B CA  1 
ATOM   3458 C C   . ALA B 1 87  ? 17.899  24.038  41.123 1.000 30.180 0  87  ALA B C   1 
ATOM   3459 O O   . ALA B 1 87  ? 18.457  22.942  41.197 1.000 31.980 0  87  ALA B O   1 
ATOM   3460 C CB  . ALA B 1 87  ? 17.244  24.904  38.863 1.000 25.260 0  87  ALA B CB  1 
ATOM   3461 N N   . LEU B 1 88  ? 16.985  24.435  42.009 1.000 27.360 0  88  LEU B N   1 
ATOM   3462 C CA  . LEU B 1 88  ? 16.716  23.603  43.177 1.000 27.780 0  88  LEU B CA  1 
ATOM   3463 C C   . LEU B 1 88  ? 16.024  22.307  42.774 1.000 29.380 0  88  LEU B C   1 
ATOM   3464 O O   . LEU B 1 88  ? 16.514  21.209  43.066 1.000 28.950 0  88  LEU B O   1 
ATOM   3465 C CB  . LEU B 1 88  ? 15.875  24.371  44.196 1.000 27.830 0  88  LEU B CB  1 
ATOM   3466 C CG  . LEU B 1 88  ? 15.658  23.591  45.491 1.000 27.770 0  88  LEU B CG  1 
ATOM   3467 C CD1 . LEU B 1 88  ? 16.944  23.553  46.304 1.000 25.470 0  88  LEU B CD1 1 
ATOM   3468 C CD2 . LEU B 1 88  ? 14.518  24.190  46.295 1.000 26.340 0  88  LEU B CD2 1 
ATOM   3469 N N   . ILE B 1 89  ? 14.885  22.411  42.092 1.000 26.480 0  89  ILE B N   1 
ATOM   3470 C CA  . ILE B 1 89  ? 14.159  21.247  41.604 1.000 27.730 0  89  ILE B CA  1 
ATOM   3471 C C   . ILE B 1 89  ? 13.807  21.466  40.140 1.000 28.650 0  89  ILE B C   1 
ATOM   3472 O O   . ILE B 1 89  ? 13.301  22.531  39.767 1.000 30.120 0  89  ILE B O   1 
ATOM   3473 C CB  . ILE B 1 89  ? 12.891  20.962  42.432 1.000 28.420 0  89  ILE B CB  1 
ATOM   3474 C CG1 . ILE B 1 89  ? 13.163  21.176  43.920 1.000 27.910 0  89  ILE B CG1 1 
ATOM   3475 C CG2 . ILE B 1 89  ? 12.402  19.542  42.186 1.000 28.110 0  89  ILE B CG2 1 
ATOM   3476 C CD1 . ILE B 1 89  ? 11.923  21.166  44.759 1.000 30.620 0  89  ILE B CD1 1 
ATOM   3477 N N   . TRP B 1 90  ? 14.068  20.455  39.321 1.000 27.590 0  90  TRP B N   1 
ATOM   3478 C CA  . TRP B 1 90  ? 13.709  20.434  37.908 1.000 26.980 0  90  TRP B CA  1 
ATOM   3479 C C   . TRP B 1 90  ? 12.629  19.366  37.754 1.000 27.900 0  90  TRP B C   1 
ATOM   3480 O O   . TRP B 1 90  ? 12.898  18.175  37.941 1.000 30.700 0  90  TRP B O   1 
ATOM   3481 C CB  . TRP B 1 90  ? 14.943  20.144  37.059 1.000 27.430 0  90  TRP B CB  1 
ATOM   3482 C CG  . TRP B 1 90  ? 14.838  20.506  35.612 1.000 26.310 0  90  TRP B CG  1 
ATOM   3483 C CD1 . TRP B 1 90  ? 13.729  20.939  34.946 1.000 26.160 0  90  TRP B CD1 1 
ATOM   3484 C CD2 . TRP B 1 90  ? 15.888  20.439  34.640 1.000 24.820 0  90  TRP B CD2 1 
ATOM   3485 N NE1 . TRP B 1 90  ? 14.027  21.153  33.621 1.000 24.610 0  90  TRP B NE1 1 
ATOM   3486 C CE2 . TRP B 1 90  ? 15.347  20.851  33.409 1.000 24.290 0  90  TRP B CE2 1 
ATOM   3487 C CE3 . TRP B 1 90  ? 17.236  20.070  34.694 1.000 24.660 0  90  TRP B CE3 1 
ATOM   3488 C CZ2 . TRP B 1 90  ? 16.107  20.908  32.243 1.000 24.400 0  90  TRP B CZ2 1 
ATOM   3489 C CZ3 . TRP B 1 90  ? 17.987  20.125  33.537 1.000 24.640 0  90  TRP B CZ3 1 
ATOM   3490 C CH2 . TRP B 1 90  ? 17.422  20.541  32.328 1.000 24.570 0  90  TRP B CH2 1 
ATOM   3491 N N   . GLN B 1 91  ? 11.409  19.797  37.418 1.000 26.320 0  91  GLN B N   1 
ATOM   3492 C CA  . GLN B 1 91  ? 10.220  19.016  37.754 1.000 26.920 0  91  GLN B CA  1 
ATOM   3493 C C   . GLN B 1 91  ? 10.162  17.679  37.025 1.000 29.150 0  91  GLN B C   1 
ATOM   3494 O O   . GLN B 1 91  ? 9.766   16.670  37.620 1.000 31.710 0  91  GLN B O   1 
ATOM   3495 C CB  . GLN B 1 91  ? 8.960   19.830  37.464 1.000 27.580 0  91  GLN B CB  1 
ATOM   3496 C CG  . GLN B 1 91  ? 8.597   20.790  38.573 1.000 27.210 0  91  GLN B CG  1 
ATOM   3497 C CD  . GLN B 1 91  ? 7.904   20.105  39.730 1.000 25.330 0  91  GLN B CD  1 
ATOM   3498 O OE1 . GLN B 1 91  ? 8.552   19.483  40.571 1.000 26.180 0  91  GLN B OE1 1 
ATOM   3499 N NE2 . GLN B 1 91  ? 6.583   20.222  39.785 1.000 26.940 0  91  GLN B NE2 1 
ATOM   3500 N N   . ASP B 1 92  ? 10.532  17.640  35.748 1.000 28.690 0  92  ASP B N   1 
ATOM   3501 C CA  . ASP B 1 92  ? 10.380  16.402  34.995 1.000 28.910 0  92  ASP B CA  1 
ATOM   3502 C C   . ASP B 1 92  ? 11.209  15.297  35.646 1.000 30.270 0  92  ASP B C   1 
ATOM   3503 O O   . ASP B 1 92  ? 12.352  15.538  36.055 1.000 31.310 0  92  ASP B O   1 
ATOM   3504 C CB  . ASP B 1 92  ? 10.794  16.592  33.535 1.000 29.550 0  92  ASP B CB  1 
ATOM   3505 C CG  . ASP B 1 92  ? 10.348  15.436  32.649 1.000 32.500 0  92  ASP B CG  1 
ATOM   3506 O OD1 . ASP B 1 92  ? 10.901  14.324  32.788 1.000 30.950 0  92  ASP B OD1 1 
ATOM   3507 O OD2 . ASP B 1 92  ? 9.434   15.637  31.822 1.000 38.010 -1 92  ASP B OD2 1 
ATOM   3508 N N   . PRO B 1 93  ? 10.661  14.086  35.778 1.000 30.620 0  93  PRO B N   1 
ATOM   3509 C CA  . PRO B 1 93  ? 11.406  13.005  36.446 1.000 30.140 0  93  PRO B CA  1 
ATOM   3510 C C   . PRO B 1 93  ? 12.756  12.693  35.826 1.000 29.590 0  93  PRO B C   1 
ATOM   3511 O O   . PRO B 1 93  ? 13.621  12.145  36.519 1.000 31.550 0  93  PRO B O   1 
ATOM   3512 C CB  . PRO B 1 93  ? 10.455  11.806  36.330 1.000 30.350 0  93  PRO B CB  1 
ATOM   3513 C CG  . PRO B 1 93  ? 9.100   12.419  36.245 1.000 29.690 0  93  PRO B CG  1 
ATOM   3514 C CD  . PRO B 1 93  ? 9.286   13.677  35.440 1.000 31.110 0  93  PRO B CD  1 
ATOM   3515 N N   . LYS B 1 94  ? 12.969  13.017  34.550 1.000 27.700 0  94  LYS B N   1 
ATOM   3516 C CA  . LYS B 1 94  ? 14.261  12.772  33.922 1.000 29.630 0  94  LYS B CA  1 
ATOM   3517 C C   . LYS B 1 94  ? 15.357  13.704  34.426 1.000 29.820 0  94  LYS B C   1 
ATOM   3518 O O   . LYS B 1 94  ? 16.530  13.486  34.098 1.000 29.720 0  94  LYS B O   1 
ATOM   3519 C CB  . LYS B 1 94  ? 14.134  12.898  32.402 1.000 31.010 0  94  LYS B CB  1 
ATOM   3520 C CG  . LYS B 1 94  ? 14.340  14.313  31.882 1.000 32.690 0  94  LYS B CG  1 
ATOM   3521 C CD  . LYS B 1 94  ? 13.806  14.488  30.466 1.000 33.230 0  94  LYS B CD  1 
ATOM   3522 C CE  . LYS B 1 94  ? 13.982  13.225  29.638 1.000 38.010 0  94  LYS B CE  1 
ATOM   3523 N NZ  . LYS B 1 94  ? 13.849  13.511  28.183 1.000 43.350 1  94  LYS B NZ  1 
ATOM   3524 N N   . TRP B 1 95  ? 15.013  14.714  35.224 1.000 29.610 0  95  TRP B N   1 
ATOM   3525 C CA  . TRP B 1 95  ? 15.978  15.677  35.732 1.000 28.810 0  95  TRP B CA  1 
ATOM   3526 C C   . TRP B 1 95  ? 16.164  15.582  37.238 1.000 30.390 0  95  TRP B C   1 
ATOM   3527 O O   . TRP B 1 95  ? 16.948  16.350  37.808 1.000 28.850 0  95  TRP B O   1 
ATOM   3528 C CB  . TRP B 1 95  ? 15.559  17.094  35.334 1.000 27.420 0  95  TRP B CB  1 
ATOM   3529 C CG  . TRP B 1 95  ? 15.424  17.258  33.851 1.000 27.580 0  95  TRP B CG  1 
ATOM   3530 C CD1 . TRP B 1 95  ? 14.303  17.621  33.163 1.000 27.840 0  95  TRP B CD1 1 
ATOM   3531 C CD2 . TRP B 1 95  ? 16.446  17.043  32.867 1.000 26.330 0  95  TRP B CD2 1 
ATOM   3532 N NE1 . TRP B 1 95  ? 14.565  17.656  31.813 1.000 28.940 0  95  TRP B NE1 1 
ATOM   3533 C CE2 . TRP B 1 95  ? 15.875  17.305  31.607 1.000 27.680 0  95  TRP B CE2 1 
ATOM   3534 C CE3 . TRP B 1 95  ? 17.791  16.663  32.932 1.000 26.330 0  95  TRP B CE3 1 
ATOM   3535 C CZ2 . TRP B 1 95  ? 16.598  17.194  30.421 1.000 26.780 0  95  TRP B CZ2 1 
ATOM   3536 C CZ3 . TRP B 1 95  ? 18.509  16.554  31.755 1.000 24.920 0  95  TRP B CZ3 1 
ATOM   3537 C CH2 . TRP B 1 95  ? 17.912  16.818  30.516 1.000 27.120 0  95  TRP B CH2 1 
ATOM   3538 N N   . LEU B 1 96  ? 15.470  14.679  37.882 1.000 29.700 0  96  LEU B N   1 
ATOM   3539 C CA  . LEU B 1 96  ? 15.710  14.317  39.264 1.000 29.870 0  96  LEU B CA  1 
ATOM   3540 C C   . LEU B 1 96  ? 16.747  13.206  39.303 1.000 31.680 0  96  LEU B C   1 
ATOM   3541 O O   . LEU B 1 96  ? 16.992  12.540  38.291 1.000 29.850 0  96  LEU B O   1 
ATOM   3542 C CB  . LEU B 1 96  ? 14.412  13.851  39.919 1.000 29.710 0  96  LEU B CB  1 
ATOM   3543 C CG  . LEU B 1 96  ? 13.240  14.831  39.952 1.000 29.020 0  96  LEU B CG  1 
ATOM   3544 C CD1 . LEU B 1 96  ? 11.924  14.073  40.029 1.000 29.820 0  96  LEU B CD1 1 
ATOM   3545 C CD2 . LEU B 1 96  ? 13.378  15.784  41.121 1.000 27.760 0  96  LEU B CD2 1 
ATOM   3546 N N   . PRO B 1 97  ? 17.419  13.008  40.434 1.000 31.750 0  97  PRO B N   1 
ATOM   3547 C CA  . PRO B 1 97  ? 18.349  11.879  40.526 1.000 28.410 0  97  PRO B CA  1 
ATOM   3548 C C   . PRO B 1 97  ? 17.614  10.567  40.300 1.000 29.940 0  97  PRO B C   1 
ATOM   3549 O O   . PRO B 1 97  ? 16.448  10.418  40.671 1.000 31.590 0  97  PRO B O   1 
ATOM   3550 C CB  . PRO B 1 97  ? 18.896  11.985  41.954 1.000 28.890 0  97  PRO B CB  1 
ATOM   3551 C CG  . PRO B 1 97  ? 18.696  13.412  42.332 1.000 29.770 0  97  PRO B CG  1 
ATOM   3552 C CD  . PRO B 1 97  ? 17.434  13.838  41.650 1.000 29.460 0  97  PRO B CD  1 
ATOM   3553 N N   . ALA B 1 98  ? 18.304  9.621   39.656 1.000 29.440 0  98  ALA B N   1 
ATOM   3554 C CA  . ALA B 1 98  ? 17.685  8.337   39.343 1.000 27.640 0  98  ALA B CA  1 
ATOM   3555 C C   . ALA B 1 98  ? 17.201  7.635   40.603 1.000 31.540 0  98  ALA B C   1 
ATOM   3556 O O   . ALA B 1 98  ? 16.116  7.039   40.616 1.000 32.050 0  98  ALA B O   1 
ATOM   3557 C CB  . ALA B 1 98  ? 18.666  7.449   38.579 1.000 26.300 0  98  ALA B CB  1 
ATOM   3558 N N   . TRP B 1 99  ? 17.988  7.702   41.677 1.000 28.710 0  99  TRP B N   1 
ATOM   3559 C CA  . TRP B 1 99  ? 17.596  7.039   42.916 1.000 31.010 0  99  TRP B CA  1 
ATOM   3560 C C   . TRP B 1 99  ? 16.367  7.688   43.539 1.000 30.990 0  99  TRP B C   1 
ATOM   3561 O O   . TRP B 1 99  ? 15.620  7.023   44.265 1.000 31.840 0  99  TRP B O   1 
ATOM   3562 C CB  . TRP B 1 99  ? 18.760  7.049   43.907 1.000 31.340 0  99  TRP B CB  1 
ATOM   3563 C CG  . TRP B 1 99  ? 19.095  8.412   44.426 1.000 32.070 0  99  TRP B CG  1 
ATOM   3564 C CD1 . TRP B 1 99  ? 19.874  9.353   43.821 1.000 31.110 0  99  TRP B CD1 1 
ATOM   3565 C CD2 . TRP B 1 99  ? 18.657  8.989   45.661 1.000 31.470 0  99  TRP B CD2 1 
ATOM   3566 N NE1 . TRP B 1 99  ? 19.951  10.480  44.604 1.000 30.540 0  99  TRP B NE1 1 
ATOM   3567 C CE2 . TRP B 1 99  ? 19.212  10.281  45.739 1.000 30.890 0  99  TRP B CE2 1 
ATOM   3568 C CE3 . TRP B 1 99  ? 17.852  8.535   46.709 1.000 32.650 0  99  TRP B CE3 1 
ATOM   3569 C CZ2 . TRP B 1 99  ? 18.986  11.127  46.822 1.000 32.780 0  99  TRP B CZ2 1 
ATOM   3570 C CZ3 . TRP B 1 99  ? 17.628  9.376   47.783 1.000 34.650 0  99  TRP B CZ3 1 
ATOM   3571 C CH2 . TRP B 1 99  ? 18.193  10.657  47.832 1.000 34.790 0  99  TRP B CH2 1 
ATOM   3572 N N   . VAL B 1 100 ? 16.142  8.975   43.269 1.000 31.250 0  100 VAL B N   1 
ATOM   3573 C CA  . VAL B 1 100 ? 14.965  9.656   43.803 1.000 31.750 0  100 VAL B CA  1 
ATOM   3574 C C   . VAL B 1 100 ? 13.692  9.127   43.150 1.000 28.150 0  100 VAL B C   1 
ATOM   3575 O O   . VAL B 1 100 ? 12.676  8.916   43.822 1.000 27.800 0  100 VAL B O   1 
ATOM   3576 C CB  . VAL B 1 100 ? 15.111  11.181  43.627 1.000 32.510 0  100 VAL B CB  1 
ATOM   3577 C CG1 . VAL B 1 100 ? 13.747  11.851  43.525 1.000 30.980 0  100 VAL B CG1 1 
ATOM   3578 C CG2 . VAL B 1 100 ? 15.919  11.772  44.773 1.000 30.040 0  100 VAL B CG2 1 
ATOM   3579 N N   . ASN B 1 101 ? 13.726  8.884   41.840 1.000 29.130 0  101 ASN B N   1 
ATOM   3580 C CA  . ASN B 1 101 ? 12.540  8.402   41.144 1.000 28.780 0  101 ASN B CA  1 
ATOM   3581 C C   . ASN B 1 101 ? 12.134  6.999   41.582 1.000 31.450 0  101 ASN B C   1 
ATOM   3582 O O   . ASN B 1 101 ? 10.970  6.624   41.408 1.000 31.980 0  101 ASN B O   1 
ATOM   3583 C CB  . ASN B 1 101 ? 12.773  8.428   39.634 1.000 28.500 0  101 ASN B CB  1 
ATOM   3584 C CG  . ASN B 1 101 ? 12.977  9.833   39.105 1.000 29.900 0  101 ASN B CG  1 
ATOM   3585 O OD1 . ASN B 1 101 ? 12.175  10.730  39.366 1.000 30.170 0  101 ASN B OD1 1 
ATOM   3586 N ND2 . ASN B 1 101 ? 14.057  10.033  38.358 1.000 28.990 0  101 ASN B ND2 1 
ATOM   3587 N N   . ALA B 1 102 ? 13.058  6.224   42.145 1.000 33.910 0  102 ALA B N   1 
ATOM   3588 C CA  . ALA B 1 102 ? 12.765  4.884   42.632 1.000 28.300 0  102 ALA B CA  1 
ATOM   3589 C C   . ALA B 1 102 ? 12.305  4.870   44.082 1.000 28.220 0  102 ALA B C   1 
ATOM   3590 O O   . ALA B 1 102 ? 12.108  3.789   44.645 1.000 29.750 0  102 ALA B O   1 
ATOM   3591 C CB  . ALA B 1 102 ? 13.995  3.984   42.474 1.000 32.660 0  102 ALA B CB  1 
ATOM   3592 N N   . LEU B 1 103 ? 12.145  6.038   44.700 1.000 31.720 0  103 LEU B N   1 
ATOM   3593 C CA  . LEU B 1 103 ? 11.687  6.113   46.081 1.000 31.620 0  103 LEU B CA  1 
ATOM   3594 C C   . LEU B 1 103 ? 10.230  5.673   46.191 1.000 31.990 0  103 LEU B C   1 
ATOM   3595 O O   . LEU B 1 103 ? 9.428   5.855   45.272 1.000 31.020 0  103 LEU B O   1 
ATOM   3596 C CB  . LEU B 1 103 ? 11.841  7.536   46.619 1.000 32.090 0  103 LEU B CB  1 
ATOM   3597 C CG  . LEU B 1 103 ? 13.264  8.048   46.849 1.000 29.060 0  103 LEU B CG  1 
ATOM   3598 C CD1 . LEU B 1 103 ? 13.258  9.554   47.061 1.000 27.850 0  103 LEU B CD1 1 
ATOM   3599 C CD2 . LEU B 1 103 ? 13.891  7.342   48.032 1.000 29.970 0  103 LEU B CD2 1 
ATOM   3600 N N   . ASP B 1 104 ? 9.891   5.093   47.342 1.000 34.630 0  104 ASP B N   1 
ATOM   3601 C CA  . ASP B 1 104 ? 8.538   4.609   47.624 1.000 32.620 0  104 ASP B CA  1 
ATOM   3602 C C   . ASP B 1 104 ? 7.843   5.636   48.515 1.000 34.140 0  104 ASP B C   1 
ATOM   3603 O O   . ASP B 1 104 ? 7.858   5.535   49.743 1.000 33.500 0  104 ASP B O   1 
ATOM   3604 C CB  . ASP B 1 104 ? 8.580   3.231   48.277 1.000 35.430 0  104 ASP B CB  1 
ATOM   3605 C CG  . ASP B 1 104 ? 7.197   2.719   48.658 1.000 38.530 0  104 ASP B CG  1 
ATOM   3606 O OD1 . ASP B 1 104 ? 6.205   3.129   48.016 1.000 35.300 0  104 ASP B OD1 1 
ATOM   3607 O OD2 . ASP B 1 104 ? 7.105   1.908   49.608 1.000 39.320 -1 104 ASP B OD2 1 
ATOM   3608 N N   . LEU B 1 105 ? 7.245   6.645   47.884 1.000 33.670 0  105 LEU B N   1 
ATOM   3609 C CA  . LEU B 1 105 ? 6.588   7.712   48.626 1.000 32.170 0  105 LEU B CA  1 
ATOM   3610 C C   . LEU B 1 105 ? 5.114   7.441   48.891 1.000 34.770 0  105 LEU B C   1 
ATOM   3611 O O   . LEU B 1 105 ? 4.590   7.890   49.918 1.000 36.150 0  105 LEU B O   1 
ATOM   3612 C CB  . LEU B 1 105 ? 6.741   9.037   47.878 1.000 32.060 0  105 LEU B CB  1 
ATOM   3613 C CG  . LEU B 1 105 ? 8.202   9.432   47.661 1.000 34.660 0  105 LEU B CG  1 
ATOM   3614 C CD1 . LEU B 1 105 ? 8.297   10.705  46.845 1.000 34.120 0  105 LEU B CD1 1 
ATOM   3615 C CD2 . LEU B 1 105 ? 8.923   9.583   48.995 1.000 31.510 0  105 LEU B CD2 1 
ATOM   3616 N N   . LYS B 1 106 ? 4.427   6.717   48.000 1.000 33.180 0  106 LYS B N   1 
ATOM   3617 C CA  . LYS B 1 106 ? 2.994   6.503   48.181 1.000 34.290 0  106 LYS B CA  1 
ATOM   3618 C C   . LYS B 1 106 ? 2.686   5.645   49.400 1.000 36.020 0  106 LYS B C   1 
ATOM   3619 O O   . LYS B 1 106 ? 1.581   5.737   49.945 1.000 38.980 0  106 LYS B O   1 
ATOM   3620 C CB  . LYS B 1 106 ? 2.378   5.880   46.927 1.000 33.950 0  106 LYS B CB  1 
ATOM   3621 C CG  . LYS B 1 106 ? 3.248   4.874   46.204 1.000 36.830 0  106 LYS B CG  1 
ATOM   3622 C CD  . LYS B 1 106 ? 2.523   4.332   44.979 1.000 39.510 0  106 LYS B CD  1 
ATOM   3623 C CE  . LYS B 1 106 ? 2.582   2.812   44.908 1.000 42.490 0  106 LYS B CE  1 
ATOM   3624 N NZ  . LYS B 1 106 ? 1.918   2.290   43.678 1.000 38.420 1  106 LYS B NZ  1 
ATOM   3625 N N   . SER B 1 107 ? 3.634   4.819   49.841 1.000 36.110 0  107 SER B N   1 
ATOM   3626 C CA  . SER B 1 107 ? 3.457   4.033   51.055 1.000 34.360 0  107 SER B CA  1 
ATOM   3627 C C   . SER B 1 107 ? 3.595   4.862   52.324 1.000 33.950 0  107 SER B C   1 
ATOM   3628 O O   . SER B 1 107 ? 3.288   4.356   53.407 1.000 36.380 0  107 SER B O   1 
ATOM   3629 C CB  . SER B 1 107 ? 4.471   2.889   51.087 1.000 36.050 0  107 SER B CB  1 
ATOM   3630 O OG  . SER B 1 107 ? 3.993   1.768   50.369 1.000 41.240 0  107 SER B OG  1 
ATOM   3631 N N   . LYS B 1 108 ? 4.062   6.105   52.224 1.000 34.280 0  108 LYS B N   1 
ATOM   3632 C CA  . LYS B 1 108 ? 4.368   6.907   53.403 1.000 33.980 0  108 LYS B CA  1 
ATOM   3633 C C   . LYS B 1 108 ? 3.502   8.161   53.484 1.000 33.940 0  108 LYS B C   1 
ATOM   3634 O O   . LYS B 1 108 ? 2.863   8.541   52.494 1.000 33.060 0  108 LYS B O   1 
ATOM   3635 C CB  . LYS B 1 108 ? 5.851   7.278   53.392 1.000 32.990 0  108 LYS B CB  1 
ATOM   3636 C CG  . LYS B 1 108 ? 6.754   6.129   52.985 1.000 33.080 0  108 LYS B CG  1 
ATOM   3637 C CD  . LYS B 1 108 ? 8.135   6.269   53.589 1.000 36.350 0  108 LYS B CD  1 
ATOM   3638 C CE  . LYS B 1 108 ? 9.012   5.094   53.207 1.000 34.660 0  108 LYS B CE  1 
ATOM   3639 N NZ  . LYS B 1 108 ? 8.964   4.835   51.742 1.000 31.890 1  108 LYS B NZ  1 
ATOM   3640 N N   . PRO B 1 109 ? 3.451   8.823   54.643 1.000 34.560 0  109 PRO B N   1 
ATOM   3641 C CA  . PRO B 1 109 ? 2.692   10.074  54.747 1.000 33.510 0  109 PRO B CA  1 
ATOM   3642 C C   . PRO B 1 109 ? 3.217   11.137  53.792 1.000 34.590 0  109 PRO B C   1 
ATOM   3643 O O   . PRO B 1 109 ? 4.324   11.047  53.258 1.000 36.620 0  109 PRO B O   1 
ATOM   3644 C CB  . PRO B 1 109 ? 2.899   10.503  56.205 1.000 31.430 0  109 PRO B CB  1 
ATOM   3645 C CG  . PRO B 1 109 ? 3.250   9.265   56.929 1.000 30.600 0  109 PRO B CG  1 
ATOM   3646 C CD  . PRO B 1 109 ? 3.920   8.347   55.957 1.000 32.420 0  109 PRO B CD  1 
ATOM   3647 N N   . VAL B 1 110 ? 2.384   12.159  53.579 1.000 34.700 0  110 VAL B N   1 
ATOM   3648 C CA  . VAL B 1 110 ? 2.797   13.305  52.775 1.000 35.990 0  110 VAL B CA  1 
ATOM   3649 C C   . VAL B 1 110 ? 3.969   14.019  53.434 1.000 36.110 0  110 VAL B C   1 
ATOM   3650 O O   . VAL B 1 110 ? 4.813   14.617  52.751 1.000 35.660 0  110 VAL B O   1 
ATOM   3651 C CB  . VAL B 1 110 ? 1.586   14.242  52.562 1.000 36.500 0  110 VAL B CB  1 
ATOM   3652 C CG1 . VAL B 1 110 ? 2.019   15.622  52.078 1.000 34.590 0  110 VAL B CG1 1 
ATOM   3653 C CG2 . VAL B 1 110 ? 0.596   13.612  51.593 1.000 32.360 0  110 VAL B CG2 1 
ATOM   3654 N N   . ALA B 1 111 ? 4.061   13.938  54.763 1.000 35.380 0  111 ALA B N   1 
ATOM   3655 C CA  . ALA B 1 111 ? 5.175   14.530  55.495 1.000 35.450 0  111 ALA B CA  1 
ATOM   3656 C C   . ALA B 1 111 ? 6.524   13.934  55.107 1.000 35.940 0  111 ALA B C   1 
ATOM   3657 O O   . ALA B 1 111 ? 7.552   14.592  55.289 1.000 35.040 0  111 ALA B O   1 
ATOM   3658 C CB  . ALA B 1 111 ? 4.946   14.367  57.000 1.000 33.580 0  111 ALA B CB  1 
ATOM   3659 N N   . HIS B 1 112 ? 6.547   12.705  54.586 1.000 35.530 0  112 HIS B N   1 
ATOM   3660 C CA  . HIS B 1 112 ? 7.807   12.071  54.203 1.000 35.080 0  112 HIS B CA  1 
ATOM   3661 C C   . HIS B 1 112 ? 8.421   12.746  52.977 1.000 36.710 0  112 HIS B C   1 
ATOM   3662 O O   . HIS B 1 112 ? 9.609   13.113  52.974 1.000 39.540 0  112 HIS B O   1 
ATOM   3663 C CB  . HIS B 1 112 ? 7.558   10.585  53.941 1.000 37.780 0  112 HIS B CB  1 
ATOM   3664 C CG  . HIS B 1 112 ? 8.804   9.770   53.801 1.000 38.460 0  112 HIS B CG  1 
ATOM   3665 N ND1 . HIS B 1 112 ? 9.268   9.326   52.581 1.000 37.120 0  112 HIS B ND1 1 
ATOM   3666 C CD2 . HIS B 1 112 ? 9.673   9.305   54.728 1.000 38.360 0  112 HIS B CD2 1 
ATOM   3667 C CE1 . HIS B 1 112 ? 10.377  8.630   52.762 1.000 37.990 0  112 HIS B CE1 1 
ATOM   3668 N NE2 . HIS B 1 112 ? 10.644  8.603   54.056 1.000 42.090 0  112 HIS B NE2 1 
ATOM   3669 N N   . ALA B 1 113 ? 7.625   12.906  51.917 1.000 35.020 0  113 ALA B N   1 
ATOM   3670 C CA  . ALA B 1 113 ? 8.092   13.639  50.746 1.000 35.450 0  113 ALA B CA  1 
ATOM   3671 C C   . ALA B 1 113 ? 8.462   15.069  51.116 1.000 34.290 0  113 ALA B C   1 
ATOM   3672 O O   . ALA B 1 113 ? 9.455   15.617  50.614 1.000 34.300 0  113 ALA B O   1 
ATOM   3673 C CB  . ALA B 1 113 ? 7.020   13.620  49.657 1.000 32.560 0  113 ALA B CB  1 
ATOM   3674 N N   . GLU B 1 114 ? 7.667   15.686  51.996 1.000 36.730 0  114 GLU B N   1 
ATOM   3675 C CA  . GLU B 1 114 ? 7.986   17.023  52.486 1.000 35.100 0  114 GLU B CA  1 
ATOM   3676 C C   . GLU B 1 114 ? 9.338   17.051  53.182 1.000 32.980 0  114 GLU B C   1 
ATOM   3677 O O   . GLU B 1 114 ? 10.105  18.002  53.015 1.000 33.060 0  114 GLU B O   1 
ATOM   3678 C CB  . GLU B 1 114 ? 6.892   17.514  53.431 1.000 34.140 0  114 GLU B CB  1 
ATOM   3679 C CG  . GLU B 1 114 ? 5.649   18.017  52.722 1.000 36.420 0  114 GLU B CG  1 
ATOM   3680 C CD  . GLU B 1 114 ? 4.516   18.317  53.681 1.000 38.540 0  114 GLU B CD  1 
ATOM   3681 O OE1 . GLU B 1 114 ? 4.682   18.077  54.897 1.000 40.550 0  114 GLU B OE1 1 
ATOM   3682 O OE2 . GLU B 1 114 ? 3.460   18.797  53.218 1.000 39.860 -1 114 GLU B OE2 1 
ATOM   3683 N N   . ALA B 1 115 ? 9.640   16.022  53.977 1.000 32.660 0  115 ALA B N   1 
ATOM   3684 C CA  . ALA B 1 115 ? 10.929  15.955  54.658 1.000 33.180 0  115 ALA B CA  1 
ATOM   3685 C C   . ALA B 1 115 ? 12.074  15.858  53.662 1.000 32.370 0  115 ALA B C   1 
ATOM   3686 O O   . ALA B 1 115 ? 13.116  16.507  53.832 1.000 31.930 0  115 ALA B O   1 
ATOM   3687 C CB  . ALA B 1 115 ? 10.956  14.765  55.617 1.000 32.190 0  115 ALA B CB  1 
ATOM   3688 N N   . ILE B 1 116 ? 11.903  15.045  52.618 1.000 33.520 0  116 ILE B N   1 
ATOM   3689 C CA  . ILE B 1 116 ? 12.956  14.913  51.610 1.000 31.230 0  116 ILE B CA  1 
ATOM   3690 C C   . ILE B 1 116 ? 13.210  16.257  50.932 1.000 31.630 0  116 ILE B C   1 
ATOM   3691 O O   . ILE B 1 116 ? 14.359  16.711  50.803 1.000 33.330 0  116 ILE B O   1 
ATOM   3692 C CB  . ILE B 1 116 ? 12.584  13.826  50.587 1.000 31.550 0  116 ILE B CB  1 
ATOM   3693 C CG1 . ILE B 1 116 ? 12.713  12.437  51.206 1.000 32.320 0  116 ILE B CG1 1 
ATOM   3694 C CG2 . ILE B 1 116 ? 13.450  13.931  49.347 1.000 31.900 0  116 ILE B CG2 1 
ATOM   3695 C CD1 . ILE B 1 116 ? 12.065  11.346  50.378 1.000 33.910 0  116 ILE B CD1 1 
ATOM   3696 N N   . LEU B 1 117 ? 12.133  16.923  50.506 1.000 31.130 0  117 LEU B N   1 
ATOM   3697 C CA  . LEU B 1 117 ? 12.289  18.218  49.847 1.000 30.750 0  117 LEU B CA  1 
ATOM   3698 C C   . LEU B 1 117 ? 12.884  19.254  50.799 1.000 31.200 0  117 LEU B C   1 
ATOM   3699 O O   . LEU B 1 117 ? 13.663  20.124  50.375 1.000 29.060 0  117 LEU B O   1 
ATOM   3700 C CB  . LEU B 1 117 ? 10.946  18.695  49.295 1.000 29.090 0  117 LEU B CB  1 
ATOM   3701 C CG  . LEU B 1 117 ? 10.296  17.763  48.267 1.000 32.100 0  117 LEU B CG  1 
ATOM   3702 C CD1 . LEU B 1 117 ? 8.807   17.995  48.246 1.000 31.810 0  117 LEU B CD1 1 
ATOM   3703 C CD2 . LEU B 1 117 ? 10.894  17.967  46.882 1.000 30.500 0  117 LEU B CD2 1 
ATOM   3704 N N   . ARG B 1 118 ? 12.524  19.171  52.087 1.000 28.890 0  118 ARG B N   1 
ATOM   3705 C CA  . ARG B 1 118 ? 13.093  20.055  53.097 1.000 29.640 0  118 ARG B CA  1 
ATOM   3706 C C   . ARG B 1 118 ? 14.605  19.867  53.192 1.000 29.970 0  118 ARG B C   1 
ATOM   3707 O O   . ARG B 1 118 ? 15.357  20.839  53.246 1.000 28.410 0  118 ARG B O   1 
ATOM   3708 C CB  . ARG B 1 118 ? 12.385  19.822  54.433 1.000 32.030 0  118 ARG B CB  1 
ATOM   3709 C CG  . ARG B 1 118 ? 12.961  20.583  55.599 1.000 30.040 0  118 ARG B CG  1 
ATOM   3710 C CD  . ARG B 1 118 ? 12.202  20.202  56.883 1.000 32.450 0  118 ARG B CD  1 
ATOM   3711 N NE  . ARG B 1 118 ? 10.833  20.714  56.895 1.000 36.350 0  118 ARG B NE  1 
ATOM   3712 C CZ  . ARG B 1 118 ? 9.746   19.959  56.774 1.000 32.300 0  118 ARG B CZ  1 
ATOM   3713 N NH1 . ARG B 1 118 ? 9.830   18.651  56.593 1.000 28.340 1  118 ARG B NH1 1 
ATOM   3714 N NH2 . ARG B 1 118 ? 8.545   20.531  56.838 1.000 31.710 0  118 ARG B NH2 1 
ATOM   3715 N N   . GLU B 1 119 ? 15.070  18.623  53.247 1.000 30.590 0  119 GLU B N   1 
ATOM   3716 C CA  . GLU B 1 119 ? 16.506  18.377  53.184 1.000 31.720 0  119 GLU B CA  1 
ATOM   3717 C C   . GLU B 1 119 ? 17.141  18.971  51.954 1.000 31.640 0  119 GLU B C   1 
ATOM   3718 O O   . GLU B 1 119 ? 18.122  19.692  52.081 1.000 31.490 0  119 GLU B O   1 
ATOM   3719 C CB  . GLU B 1 119 ? 16.791  16.887  53.299 1.000 38.240 0  119 GLU B CB  1 
ATOM   3720 C CG  . GLU B 1 119 ? 17.639  16.443  54.467 1.000 40.400 0  119 GLU B CG  1 
ATOM   3721 C CD  . GLU B 1 119 ? 18.807  17.415  54.659 1.000 46.810 0  119 GLU B CD  1 
ATOM   3722 O OE1 . GLU B 1 119 ? 18.872  18.138  55.646 1.000 53.200 0  119 GLU B OE1 1 
ATOM   3723 O OE2 . GLU B 1 119 ? 19.579  17.549  53.657 1.000 45.640 -1 119 GLU B OE2 1 
ATOM   3724 N N   . HIS B 1 120 ? 16.605  18.702  50.762 1.000 30.970 0  120 HIS B N   1 
ATOM   3725 C CA  . HIS B 1 120 ? 17.234  19.254  49.554 1.000 29.020 0  120 HIS B CA  1 
ATOM   3726 C C   . HIS B 1 120 ? 17.344  20.792  49.606 1.000 28.200 0  120 HIS B C   1 
ATOM   3727 O O   . HIS B 1 120 ? 18.437  21.367  49.437 1.000 29.970 0  120 HIS B O   1 
ATOM   3728 C CB  . HIS B 1 120 ? 16.467  18.814  48.307 1.000 27.990 0  120 HIS B CB  1 
ATOM   3729 C CG  . HIS B 1 120 ? 17.142  19.220  47.049 1.000 27.780 0  120 HIS B CG  1 
ATOM   3730 N ND1 . HIS B 1 120 ? 18.486  19.001  46.853 1.000 29.150 0  120 HIS B ND1 1 
ATOM   3731 C CD2 . HIS B 1 120 ? 16.681  19.832  45.934 1.000 26.250 0  120 HIS B CD2 1 
ATOM   3732 C CE1 . HIS B 1 120 ? 18.827  19.461  45.666 1.000 27.460 0  120 HIS B CE1 1 
ATOM   3733 N NE2 . HIS B 1 120 ? 17.752  19.967  45.087 1.000 26.420 0  120 HIS B NE2 1 
ATOM   3734 N N   . ALA B 1 121 ? 16.216  21.475  49.843 1.000 30.160 0  121 ALA B N   1 
ATOM   3735 C CA  . ALA B 1 121 ? 16.230  22.937  49.862 1.000 29.640 0  121 ALA B CA  1 
ATOM   3736 C C   . ALA B 1 121 ? 17.170  23.467  50.938 1.000 29.830 0  121 ALA B C   1 
ATOM   3737 O O   . ALA B 1 121 ? 17.961  24.384  50.679 1.000 30.240 0  121 ALA B O   1 
ATOM   3738 C CB  . ALA B 1 121 ? 14.815  23.492  50.073 1.000 25.230 0  121 ALA B CB  1 
ATOM   3739 N N   . LYS B 1 122 ? 17.120  22.890  52.145 1.000 28.030 0  122 LYS B N   1 
ATOM   3740 C CA  . LYS B 1 122 ? 17.960  23.369  53.235 1.000 29.450 0  122 LYS B CA  1 
ATOM   3741 C C   . LYS B 1 122 ? 19.442  23.197  52.918 1.000 32.130 0  122 LYS B C   1 
ATOM   3742 O O   . LYS B 1 122 ? 20.231  24.135  53.073 1.000 31.370 0  122 LYS B O   1 
ATOM   3743 C CB  . LYS B 1 122 ? 17.593  22.623  54.515 1.000 30.030 0  122 LYS B CB  1 
ATOM   3744 C CG  . LYS B 1 122 ? 17.928  23.360  55.796 1.000 30.610 0  122 LYS B CG  1 
ATOM   3745 C CD  . LYS B 1 122 ? 18.163  22.383  56.934 1.000 30.880 0  122 LYS B CD  1 
ATOM   3746 C CE  . LYS B 1 122 ? 19.385  22.775  57.740 1.000 36.060 0  122 LYS B CE  1 
ATOM   3747 N NZ  . LYS B 1 122 ? 20.624  22.635  56.925 1.000 37.590 1  122 LYS B NZ  1 
ATOM   3748 N N   . THR B 1 123 ? 19.834  21.997  52.478 1.000 31.950 0  123 THR B N   1 
ATOM   3749 C CA  . THR B 1 123 ? 21.227  21.751  52.121 1.000 31.660 0  123 THR B CA  1 
ATOM   3750 C C   . THR B 1 123 ? 21.710  22.762  51.089 1.000 31.710 0  123 THR B C   1 
ATOM   3751 O O   . THR B 1 123 ? 22.725  23.448  51.293 1.000 32.760 0  123 THR B O   1 
ATOM   3752 C CB  . THR B 1 123 ? 21.377  20.327  51.589 1.000 32.240 0  123 THR B CB  1 
ATOM   3753 O OG1 . THR B 1 123 ? 20.889  19.396  52.563 1.000 34.790 0  123 THR B OG1 1 
ATOM   3754 C CG2 . THR B 1 123 ? 22.834  20.010  51.280 1.000 28.690 0  123 THR B CG2 1 
ATOM   3755 N N   . VAL B 1 124 ? 20.975  22.884  49.981 1.000 29.770 0  124 VAL B N   1 
ATOM   3756 C CA  . VAL B 1 124 ? 21.429  23.750  48.897 1.000 30.300 0  124 VAL B CA  1 
ATOM   3757 C C   . VAL B 1 124 ? 21.489  25.201  49.362 1.000 30.770 0  124 VAL B C   1 
ATOM   3758 O O   . VAL B 1 124 ? 22.420  25.939  49.018 1.000 32.380 0  124 VAL B O   1 
ATOM   3759 C CB  . VAL B 1 124 ? 20.529  23.577  47.660 1.000 28.330 0  124 VAL B CB  1 
ATOM   3760 C CG1 . VAL B 1 124 ? 20.961  24.525  46.554 1.000 25.430 0  124 VAL B CG1 1 
ATOM   3761 C CG2 . VAL B 1 124 ? 20.571  22.136  47.170 1.000 25.510 0  124 VAL B CG2 1 
ATOM   3762 N N   . CYS B 1 125 ? 20.525  25.624  50.183 1.000 31.610 0  125 CYS B N   1 
ATOM   3763 C CA  . CYS B 1 125 ? 20.437  27.037  50.535 1.000 33.400 0  125 CYS B CA  1 
ATOM   3764 C C   . CYS B 1 125 ? 21.452  27.427  51.601 1.000 33.350 0  125 CYS B C   1 
ATOM   3765 O O   . CYS B 1 125 ? 21.976  28.546  51.573 1.000 37.050 0  125 CYS B O   1 
ATOM   3766 C CB  . CYS B 1 125 ? 19.020  27.373  50.999 1.000 31.930 0  125 CYS B CB  1 
ATOM   3767 S SG  . CYS B 1 125 ? 17.853  27.592  49.637 1.000 37.660 0  125 CYS B SG  1 
ATOM   3768 N N   . THR B 1 126 ? 21.738  26.542  52.557 1.000 31.410 0  126 THR B N   1 
ATOM   3769 C CA  . THR B 1 126 ? 22.760  26.868  53.542 1.000 32.260 0  126 THR B CA  1 
ATOM   3770 C C   . THR B 1 126 ? 24.169  26.669  53.008 1.000 34.310 0  126 THR B C   1 
ATOM   3771 O O   . THR B 1 126 ? 25.100  27.300  53.520 1.000 36.740 0  126 THR B O   1 
ATOM   3772 C CB  . THR B 1 126 ? 22.586  26.055  54.833 1.000 35.730 0  126 THR B CB  1 
ATOM   3773 O OG1 . THR B 1 126 ? 23.190  24.761  54.687 1.000 36.520 0  126 THR B OG1 1 
ATOM   3774 C CG2 . THR B 1 126 ? 21.123  25.950  55.256 1.000 32.380 0  126 THR B CG2 1 
ATOM   3775 N N   . HIS B 1 127 ? 24.365  25.829  51.990 1.000 32.930 0  127 HIS B N   1 
ATOM   3776 C CA  . HIS B 1 127 ? 25.695  25.802  51.397 1.000 30.890 0  127 HIS B CA  1 
ATOM   3777 C C   . HIS B 1 127 ? 25.941  27.018  50.513 1.000 31.210 0  127 HIS B C   1 
ATOM   3778 O O   . HIS B 1 127 ? 27.057  27.549  50.486 1.000 32.980 0  127 HIS B O   1 
ATOM   3779 C CB  . HIS B 1 127 ? 25.917  24.525  50.595 1.000 29.600 0  127 HIS B CB  1 
ATOM   3780 C CG  . HIS B 1 127 ? 27.274  24.459  49.971 1.000 29.020 0  127 HIS B CG  1 
ATOM   3781 N ND1 . HIS B 1 127 ? 28.381  23.984  50.640 1.000 27.720 0  127 HIS B ND1 1 
ATOM   3782 C CD2 . HIS B 1 127 ? 27.712  24.849  48.750 1.000 28.490 0  127 HIS B CD2 1 
ATOM   3783 C CE1 . HIS B 1 127 ? 29.436  24.059  49.848 1.000 27.250 0  127 HIS B CE1 1 
ATOM   3784 N NE2 . HIS B 1 127 ? 29.057  24.581  48.696 1.000 27.160 0  127 HIS B NE2 1 
ATOM   3785 N N   . LEU B 1 128 ? 24.920  27.476  49.795 1.000 29.220 0  128 LEU B N   1 
ATOM   3786 C CA  . LEU B 1 128 ? 25.064  28.599  48.868 1.000 32.340 0  128 LEU B CA  1 
ATOM   3787 C C   . LEU B 1 128 ? 24.454  29.867  49.460 1.000 34.200 0  128 LEU B C   1 
ATOM   3788 O O   . LEU B 1 128 ? 23.499  30.439  48.935 1.000 33.750 0  128 LEU B O   1 
ATOM   3789 C CB  . LEU B 1 128 ? 24.430  28.257  47.523 1.000 30.550 0  128 LEU B CB  1 
ATOM   3790 C CG  . LEU B 1 128 ? 24.999  27.044  46.783 1.000 28.930 0  128 LEU B CG  1 
ATOM   3791 C CD1 . LEU B 1 128 ? 24.196  26.764  45.529 1.000 26.300 0  128 LEU B CD1 1 
ATOM   3792 C CD2 . LEU B 1 128 ? 26.470  27.256  46.447 1.000 27.380 0  128 LEU B CD2 1 
ATOM   3793 N N   . LYS B 1 129 ? 25.043  30.322  50.565 1.000 35.610 0  129 LYS B N   1 
ATOM   3794 C CA  . LYS B 1 129 ? 24.464  31.420  51.328 1.000 36.670 0  129 LYS B CA  1 
ATOM   3795 C C   . LYS B 1 129 ? 24.764  32.785  50.726 1.000 35.880 0  129 LYS B C   1 
ATOM   3796 O O   . LYS B 1 129 ? 24.140  33.771  51.131 1.000 40.240 0  129 LYS B O   1 
ATOM   3797 C CB  . LYS B 1 129 ? 24.948  31.370  52.781 1.000 37.900 0  129 LYS B CB  1 
ATOM   3798 C CG  . LYS B 1 129 ? 26.451  31.502  52.967 1.000 37.520 0  129 LYS B CG  1 
ATOM   3799 C CD  . LYS B 1 129 ? 26.859  31.171  54.401 1.000 41.190 0  129 LYS B CD  1 
ATOM   3800 C CE  . LYS B 1 129 ? 25.892  30.179  55.048 1.000 40.100 0  129 LYS B CE  1 
ATOM   3801 N NZ  . LYS B 1 129 ? 26.455  29.514  56.263 1.000 36.370 1  129 LYS B NZ  1 
ATOM   3802 N N   . ASP B 1 130 ? 25.703  32.872  49.789 1.000 37.770 0  130 ASP B N   1 
ATOM   3803 C CA  . ASP B 1 130 ? 25.996  34.122  49.100 1.000 37.370 0  130 ASP B CA  1 
ATOM   3804 C C   . ASP B 1 130 ? 25.197  34.288  47.812 1.000 35.950 0  130 ASP B C   1 
ATOM   3805 O O   . ASP B 1 130 ? 25.347  35.309  47.132 1.000 35.430 0  130 ASP B O   1 
ATOM   3806 C CB  . ASP B 1 130 ? 27.498  34.215  48.789 1.000 37.800 0  130 ASP B CB  1 
ATOM   3807 C CG  . ASP B 1 130 ? 28.090  32.888  48.329 1.000 40.220 0  130 ASP B CG  1 
ATOM   3808 O OD1 . ASP B 1 130 ? 27.395  31.852  48.422 1.000 39.450 0  130 ASP B OD1 1 
ATOM   3809 O OD2 . ASP B 1 130 ? 29.253  32.885  47.870 1.000 40.120 -1 130 ASP B OD2 1 
ATOM   3810 N N   . VAL B 1 131 ? 24.360  33.311  47.461 1.000 34.100 0  131 VAL B N   1 
ATOM   3811 C CA  . VAL B 1 131 ? 23.596  33.372  46.221 1.000 31.300 0  131 VAL B CA  1 
ATOM   3812 C C   . VAL B 1 131 ? 22.532  34.457  46.330 1.000 32.660 0  131 VAL B C   1 
ATOM   3813 O O   . VAL B 1 131 ? 21.831  34.563  47.344 1.000 33.280 0  131 VAL B O   1 
ATOM   3814 C CB  . VAL B 1 131 ? 22.973  32.001  45.914 1.000 31.300 0  131 VAL B CB  1 
ATOM   3815 C CG1 . VAL B 1 131 ? 21.690  32.149  45.105 1.000 32.560 0  131 VAL B CG1 1 
ATOM   3816 C CG2 . VAL B 1 131 ? 23.966  31.119  45.180 1.000 28.920 0  131 VAL B CG2 1 
ATOM   3817 N N   . ILE B 1 132 ? 22.405  35.268  45.279 1.000 32.450 0  132 ILE B N   1 
ATOM   3818 C CA  . ILE B 1 132 ? 21.429  36.353  45.278 1.000 29.070 0  132 ILE B CA  1 
ATOM   3819 C C   . ILE B 1 132 ? 20.069  35.914  44.736 1.000 28.860 0  132 ILE B C   1 
ATOM   3820 O O   . ILE B 1 132 ? 19.047  36.513  45.088 1.000 27.760 0  132 ILE B O   1 
ATOM   3821 C CB  . ILE B 1 132 ? 21.962  37.563  44.491 1.000 27.270 0  132 ILE B CB  1 
ATOM   3822 C CG1 . ILE B 1 132 ? 22.086  37.222  43.004 1.000 27.320 0  132 ILE B CG1 1 
ATOM   3823 C CG2 . ILE B 1 132 ? 23.291  38.028  45.067 1.000 30.080 0  132 ILE B CG2 1 
ATOM   3824 C CD1 . ILE B 1 132 ? 22.355  38.421  42.122 1.000 26.110 0  132 ILE B CD1 1 
ATOM   3825 N N   . SER B 1 133 ? 20.024  34.893  43.880 1.000 29.720 0  133 SER B N   1 
ATOM   3826 C CA  . SER B 1 133 ? 18.778  34.508  43.227 1.000 27.350 0  133 SER B CA  1 
ATOM   3827 C C   . SER B 1 133 ? 18.760  33.012  42.952 1.000 27.650 0  133 SER B C   1 
ATOM   3828 O O   . SER B 1 133 ? 19.728  32.462  42.421 1.000 30.460 0  133 SER B O   1 
ATOM   3829 C CB  . SER B 1 133 ? 18.591  35.290  41.923 1.000 28.570 0  133 SER B CB  1 
ATOM   3830 O OG  . SER B 1 133 ? 17.482  34.812  41.183 1.000 28.540 0  133 SER B OG  1 
ATOM   3831 N N   . HIS B 1 134 ? 17.648  32.368  43.302 1.000 25.420 0  134 HIS B N   1 
ATOM   3832 C CA  . HIS B 1 134 ? 17.442  30.938  43.107 1.000 27.070 0  134 HIS B CA  1 
ATOM   3833 C C   . HIS B 1 134 ? 16.331  30.696  42.097 1.000 25.980 0  134 HIS B C   1 
ATOM   3834 O O   . HIS B 1 134 ? 15.290  31.361  42.146 1.000 27.640 0  134 HIS B O   1 
ATOM   3835 C CB  . HIS B 1 134 ? 17.071  30.253  44.424 1.000 27.530 0  134 HIS B CB  1 
ATOM   3836 C CG  . HIS B 1 134 ? 18.236  29.993  45.322 1.000 34.130 0  134 HIS B CG  1 
ATOM   3837 N ND1 . HIS B 1 134 ? 18.318  30.504  46.599 1.000 34.510 0  134 HIS B ND1 1 
ATOM   3838 C CD2 . HIS B 1 134 ? 19.369  29.277  45.128 1.000 33.200 0  134 HIS B CD2 1 
ATOM   3839 C CE1 . HIS B 1 134 ? 19.452  30.115  47.154 1.000 35.450 0  134 HIS B CE1 1 
ATOM   3840 N NE2 . HIS B 1 134 ? 20.108  29.369  46.282 1.000 32.860 0  134 HIS B NE2 1 
ATOM   3841 N N   . ASP B 1 135 ? 16.571  29.772  41.166 1.000 24.550 0  135 ASP B N   1 
ATOM   3842 C CA  . ASP B 1 135 ? 15.490  29.144  40.407 1.000 27.220 0  135 ASP B CA  1 
ATOM   3843 C C   . ASP B 1 135 ? 14.943  28.024  41.283 1.000 28.770 0  135 ASP B C   1 
ATOM   3844 O O   . ASP B 1 135 ? 15.472  26.910  41.302 1.000 30.830 0  135 ASP B O   1 
ATOM   3845 C CB  . ASP B 1 135 ? 15.979  28.605  39.067 1.000 27.540 0  135 ASP B CB  1 
ATOM   3846 C CG  . ASP B 1 135 ? 16.497  29.691  38.150 1.000 27.280 0  135 ASP B CG  1 
ATOM   3847 O OD1 . ASP B 1 135 ? 15.790  30.706  37.967 1.000 28.270 0  135 ASP B OD1 1 
ATOM   3848 O OD2 . ASP B 1 135 ? 17.602  29.519  37.596 1.000 26.920 -1 135 ASP B OD2 1 
ATOM   3849 N N   . VAL B 1 136 ? 13.879  28.316  42.035 1.000 27.240 0  136 VAL B N   1 
ATOM   3850 C CA  . VAL B 1 136 ? 13.375  27.326  42.983 1.000 28.320 0  136 VAL B CA  1 
ATOM   3851 C C   . VAL B 1 136 ? 12.781  26.137  42.240 1.000 26.330 0  136 VAL B C   1 
ATOM   3852 O O   . VAL B 1 136 ? 13.171  24.985  42.465 1.000 27.130 0  136 VAL B O   1 
ATOM   3853 C CB  . VAL B 1 136 ? 12.358  27.965  43.942 1.000 25.820 0  136 VAL B CB  1 
ATOM   3854 C CG1 . VAL B 1 136 ? 11.707  26.897  44.802 1.000 25.500 0  136 VAL B CG1 1 
ATOM   3855 C CG2 . VAL B 1 136 ? 13.040  29.002  44.812 1.000 25.120 0  136 VAL B CG2 1 
ATOM   3856 N N   . VAL B 1 137 ? 11.851  26.400  41.329 1.000 24.900 0  137 VAL B N   1 
ATOM   3857 C CA  . VAL B 1 137 ? 11.232  25.375  40.500 1.000 25.490 0  137 VAL B CA  1 
ATOM   3858 C C   . VAL B 1 137 ? 11.513  25.724  39.045 1.000 24.600 0  137 VAL B C   1 
ATOM   3859 O O   . VAL B 1 137 ? 11.325  26.874  38.632 1.000 24.610 0  137 VAL B O   1 
ATOM   3860 C CB  . VAL B 1 137 ? 9.719   25.273  40.766 1.000 25.570 0  137 VAL B CB  1 
ATOM   3861 C CG1 . VAL B 1 137 ? 9.085   24.214  39.875 1.000 25.950 0  137 VAL B CG1 1 
ATOM   3862 C CG2 . VAL B 1 137 ? 9.460   24.979  42.237 1.000 24.100 0  137 VAL B CG2 1 
ATOM   3863 N N   . ASN B 1 138 ? 11.987  24.746  38.281 1.000 24.010 0  138 ASN B N   1 
ATOM   3864 C CA  . ASN B 1 138 ? 12.329  24.940  36.879 1.000 25.290 0  138 ASN B CA  1 
ATOM   3865 C C   . ASN B 1 138 ? 11.473  24.040  36.001 1.000 24.730 0  138 ASN B C   1 
ATOM   3866 O O   . ASN B 1 138 ? 11.404  22.829  36.234 1.000 23.990 0  138 ASN B O   1 
ATOM   3867 C CB  . ASN B 1 138 ? 13.814  24.663  36.630 1.000 24.670 0  138 ASN B CB  1 
ATOM   3868 C CG  . ASN B 1 138 ? 14.302  25.253  35.323 1.000 24.130 0  138 ASN B CG  1 
ATOM   3869 O OD1 . ASN B 1 138 ? 14.411  26.470  35.180 1.000 24.150 0  138 ASN B OD1 1 
ATOM   3870 N ND2 . ASN B 1 138 ? 14.593  24.392  34.357 1.000 24.230 0  138 ASN B ND2 1 
ATOM   3871 N N   . GLU B 1 139 ? 10.839  24.633  34.989 1.000 25.980 0  139 GLU B N   1 
ATOM   3872 C CA  . GLU B 1 139 ? 10.107  23.900  33.956 1.000 26.860 0  139 GLU B CA  1 
ATOM   3873 C C   . GLU B 1 139 ? 9.073   22.950  34.573 1.000 27.520 0  139 GLU B C   1 
ATOM   3874 O O   . GLU B 1 139 ? 9.242   21.732  34.604 1.000 28.190 0  139 GLU B O   1 
ATOM   3875 C CB  . GLU B 1 139 ? 11.081  23.130  33.059 1.000 24.320 0  139 GLU B CB  1 
ATOM   3876 C CG  . GLU B 1 139 ? 11.634  23.909  31.872 1.000 26.170 0  139 GLU B CG  1 
ATOM   3877 C CD  . GLU B 1 139 ? 13.003  23.407  31.418 1.000 24.060 0  139 GLU B CD  1 
ATOM   3878 O OE1 . GLU B 1 139 ? 13.169  22.180  31.262 1.000 24.080 0  139 GLU B OE1 1 
ATOM   3879 O OE2 . GLU B 1 139 ? 13.912  24.238  31.204 1.000 24.150 -1 139 GLU B OE2 1 
ATOM   3880 N N   . ALA B 1 140 ? 7.983   23.547  35.061 1.000 27.150 0  140 ALA B N   1 
ATOM   3881 C CA  . ALA B 1 140 ? 6.918   22.806  35.733 1.000 27.510 0  140 ALA B CA  1 
ATOM   3882 C C   . ALA B 1 140 ? 5.614   22.782  34.947 1.000 29.750 0  140 ALA B C   1 
ATOM   3883 O O   . ALA B 1 140 ? 4.606   22.281  35.457 1.000 29.620 0  140 ALA B O   1 
ATOM   3884 C CB  . ALA B 1 140 ? 6.667   23.390  37.123 1.000 28.520 0  140 ALA B CB  1 
ATOM   3885 N N   . VAL B 1 141 ? 5.600   23.302  33.724 1.000 29.750 0  141 VAL B N   1 
ATOM   3886 C CA  . VAL B 1 141 ? 4.378   23.401  32.937 1.000 29.660 0  141 VAL B CA  1 
ATOM   3887 C C   . VAL B 1 141 ? 4.646   22.804  31.565 1.000 28.670 0  141 VAL B C   1 
ATOM   3888 O O   . VAL B 1 141 ? 5.628   23.167  30.906 1.000 29.240 0  141 VAL B O   1 
ATOM   3889 C CB  . VAL B 1 141 ? 3.887   24.856  32.815 1.000 30.900 0  141 VAL B CB  1 
ATOM   3890 C CG1 . VAL B 1 141 ? 2.765   24.947  31.798 1.000 31.150 0  141 VAL B CG1 1 
ATOM   3891 C CG2 . VAL B 1 141 ? 3.429   25.380  34.170 1.000 28.510 0  141 VAL B CG2 1 
ATOM   3892 N N   . SER B 1 142 ? 3.776   21.898  31.138 1.000 28.770 0  142 SER B N   1 
ATOM   3893 C CA  . SER B 1 142 ? 3.991   21.193  29.885 1.000 30.320 0  142 SER B CA  1 
ATOM   3894 C C   . SER B 1 142 ? 3.936   22.166  28.712 1.000 30.050 0  142 SER B C   1 
ATOM   3895 O O   . SER B 1 142 ? 2.937   22.881  28.548 1.000 30.110 0  142 SER B O   1 
ATOM   3896 C CB  . SER B 1 142 ? 2.941   20.101  29.700 1.000 29.320 0  142 SER B CB  1 
ATOM   3897 O OG  . SER B 1 142 ? 2.932   19.637  28.362 1.000 30.090 0  142 SER B OG  1 
ATOM   3898 N N   . PRO B 1 143 ? 4.972   22.219  27.869 1.000 30.550 0  143 PRO B N   1 
ATOM   3899 C CA  . PRO B 1 143 ? 4.911   23.070  26.672 1.000 29.640 0  143 PRO B CA  1 
ATOM   3900 C C   . PRO B 1 143 ? 3.937   22.573  25.620 1.000 30.790 0  143 PRO B C   1 
ATOM   3901 O O   . PRO B 1 143 ? 3.763   23.245  24.597 1.000 32.420 0  143 PRO B O   1 
ATOM   3902 C CB  . PRO B 1 143 ? 6.354   23.040  26.141 1.000 25.520 0  143 PRO B CB  1 
ATOM   3903 C CG  . PRO B 1 143 ? 6.967   21.818  26.716 1.000 29.220 0  143 PRO B CG  1 
ATOM   3904 C CD  . PRO B 1 143 ? 6.248   21.494  27.994 1.000 29.650 0  143 PRO B CD  1 
ATOM   3905 N N   . LYS B 1 144 ? 3.295   21.424  25.835 1.000 31.170 0  144 LYS B N   1 
ATOM   3906 C CA  . LYS B 1 144 ? 2.318   20.886  24.898 1.000 31.480 0  144 LYS B CA  1 
ATOM   3907 C C   . LYS B 1 144 ? 0.889   21.295  25.244 1.000 33.200 0  144 LYS B C   1 
ATOM   3908 O O   . LYS B 1 144 ? 0.121   21.673  24.352 1.000 34.280 0  144 LYS B O   1 
ATOM   3909 C CB  . LYS B 1 144 ? 2.430   19.361  24.855 1.000 34.800 0  144 LYS B CB  1 
ATOM   3910 C CG  . LYS B 1 144 ? 3.233   18.827  23.677 1.000 39.870 0  144 LYS B CG  1 
ATOM   3911 C CD  . LYS B 1 144 ? 3.267   17.305  23.680 1.000 45.300 0  144 LYS B CD  1 
ATOM   3912 C CE  . LYS B 1 144 ? 4.555   16.782  24.305 1.000 42.760 0  144 LYS B CE  1 
ATOM   3913 N NZ  . LYS B 1 144 ? 5.127   15.649  23.525 1.000 40.820 1  144 LYS B NZ  1 
ATOM   3914 N N   . ASP B 1 145 ? 0.512   21.237  26.527 1.000 30.110 0  145 ASP B N   1 
ATOM   3915 C CA  . ASP B 1 145 ? -0.870  21.510  26.898 1.000 30.570 0  145 ASP B CA  1 
ATOM   3916 C C   . ASP B 1 145 ? -1.020  22.352  28.161 1.000 31.480 0  145 ASP B C   1 
ATOM   3917 O O   . ASP B 1 145 ? -2.150  22.532  28.633 1.000 32.990 0  145 ASP B O   1 
ATOM   3918 C CB  . ASP B 1 145 ? -1.632  20.186  27.074 1.000 30.880 0  145 ASP B CB  1 
ATOM   3919 C CG  . ASP B 1 145 ? -0.997  19.271  28.115 1.000 31.540 0  145 ASP B CG  1 
ATOM   3920 O OD1 . ASP B 1 145 ? -0.195  19.750  28.947 1.000 30.970 0  145 ASP B OD1 1 
ATOM   3921 O OD2 . ASP B 1 145 ? -1.296  18.059  28.099 1.000 31.820 -1 145 ASP B OD2 1 
ATOM   3922 N N   . GLY B 1 146 ? 0.065   22.877  28.725 1.000 29.270 0  146 GLY B N   1 
ATOM   3923 C CA  . GLY B 1 146 ? -0.048  23.709  29.903 1.000 30.250 0  146 GLY B CA  1 
ATOM   3924 C C   . GLY B 1 146 ? -0.357  22.983  31.194 1.000 30.760 0  146 GLY B C   1 
ATOM   3925 O O   . GLY B 1 146 ? -0.486  23.639  32.235 1.000 29.830 0  146 GLY B O   1 
ATOM   3926 N N   . SER B 1 147 ? -0.491  21.660  31.169 1.000 30.010 0  147 SER B N   1 
ATOM   3927 C CA  . SER B 1 147 ? -0.686  20.918  32.403 1.000 27.520 0  147 SER B CA  1 
ATOM   3928 C C   . SER B 1 147 ? 0.594   20.939  33.232 1.000 26.820 0  147 SER B C   1 
ATOM   3929 O O   . SER B 1 147 ? 1.685   21.215  32.729 1.000 32.110 0  147 SER B O   1 
ATOM   3930 C CB  . SER B 1 147 ? -1.096  19.475  32.110 1.000 29.840 0  147 SER B CB  1 
ATOM   3931 O OG  . SER B 1 147 ? -0.117  18.817  31.324 1.000 30.590 0  147 SER B OG  1 
ATOM   3932 N N   . LEU B 1 148 ? 0.454   20.640  34.517 1.000 26.600 0  148 LEU B N   1 
ATOM   3933 C CA  . LEU B 1 148 ? 1.613   20.613  35.394 1.000 27.980 0  148 LEU B CA  1 
ATOM   3934 C C   . LEU B 1 148 ? 2.348   19.287  35.236 1.000 29.860 0  148 LEU B C   1 
ATOM   3935 O O   . LEU B 1 148 ? 1.742   18.214  35.329 1.000 27.040 0  148 LEU B O   1 
ATOM   3936 C CB  . LEU B 1 148 ? 1.182   20.837  36.842 1.000 23.920 0  148 LEU B CB  1 
ATOM   3937 C CG  . LEU B 1 148 ? 0.695   22.270  37.072 1.000 23.910 0  148 LEU B CG  1 
ATOM   3938 C CD1 . LEU B 1 148 ? 0.114   22.440  38.459 1.000 24.950 0  148 LEU B CD1 1 
ATOM   3939 C CD2 . LEU B 1 148 ? 1.826   23.262  36.837 1.000 25.110 0  148 LEU B CD2 1 
ATOM   3940 N N   . ILE B 1 149 ? 3.658   19.368  34.989 1.000 29.290 0  149 ILE B N   1 
ATOM   3941 C CA  . ILE B 1 149 ? 4.477   18.174  34.820 1.000 28.690 0  149 ILE B CA  1 
ATOM   3942 C C   . ILE B 1 149 ? 4.544   17.414  36.137 1.000 30.040 0  149 ILE B C   1 
ATOM   3943 O O   . ILE B 1 149 ? 4.785   18.002  37.201 1.000 30.410 0  149 ILE B O   1 
ATOM   3944 C CB  . ILE B 1 149 ? 5.879   18.555  34.319 1.000 28.590 0  149 ILE B CB  1 
ATOM   3945 C CG1 . ILE B 1 149 ? 5.847   18.872  32.821 1.000 29.230 0  149 ILE B CG1 1 
ATOM   3946 C CG2 . ILE B 1 149 ? 6.876   17.443  34.601 1.000 28.300 0  149 ILE B CG2 1 
ATOM   3947 C CD1 . ILE B 1 149 ? 6.853   19.919  32.396 1.000 26.470 0  149 ILE B CD1 1 
ATOM   3948 N N   . GLN B 1 150 ? 4.338   16.102  36.071 1.000 29.800 0  150 GLN B N   1 
ATOM   3949 C CA  . GLN B 1 150 ? 4.247   15.266  37.256 1.000 31.790 0  150 GLN B CA  1 
ATOM   3950 C C   . GLN B 1 150 ? 5.545   14.503  37.489 1.000 31.530 0  150 GLN B C   1 
ATOM   3951 O O   . GLN B 1 150 ? 6.241   14.113  36.547 1.000 30.150 0  150 GLN B O   1 
ATOM   3952 C CB  . GLN B 1 150 ? 3.086   14.278  37.134 1.000 32.520 0  150 GLN B CB  1 
ATOM   3953 C CG  . GLN B 1 150 ? 1.717   14.929  37.083 1.000 33.610 0  150 GLN B CG  1 
ATOM   3954 C CD  . GLN B 1 150 ? 1.018   14.931  38.427 1.000 37.330 0  150 GLN B CD  1 
ATOM   3955 O OE1 . GLN B 1 150 ? 1.639   15.161  39.464 1.000 32.500 0  150 GLN B OE1 1 
ATOM   3956 N NE2 . GLN B 1 150 ? -0.286  14.675  38.413 1.000 41.130 0  150 GLN B NE2 1 
ATOM   3957 N N   . ASN B 1 151 ? 5.857   14.287  38.763 1.000 30.840 0  151 ASN B N   1 
ATOM   3958 C CA  . ASN B 1 151 ? 6.968   13.441  39.165 1.000 30.390 0  151 ASN B CA  1 
ATOM   3959 C C   . ASN B 1 151 ? 6.603   12.789  40.491 1.000 31.370 0  151 ASN B C   1 
ATOM   3960 O O   . ASN B 1 151 ? 5.503   12.979  41.015 1.000 33.630 0  151 ASN B O   1 
ATOM   3961 C CB  . ASN B 1 151 ? 8.279   14.232  39.243 1.000 32.020 0  151 ASN B CB  1 
ATOM   3962 C CG  . ASN B 1 151 ? 8.261   15.311  40.312 1.000 32.350 0  151 ASN B CG  1 
ATOM   3963 O OD1 . ASN B 1 151 ? 7.291   15.462  41.053 1.000 31.840 0  151 ASN B OD1 1 
ATOM   3964 N ND2 . ASN B 1 151 ? 9.348   16.070  40.395 1.000 31.010 0  151 ASN B ND2 1 
ATOM   3965 N N   . VAL B 1 152 ? 7.549   12.031  41.047 1.000 31.600 0  152 VAL B N   1 
ATOM   3966 C CA  . VAL B 1 152 ? 7.272   11.248  42.245 1.000 30.700 0  152 VAL B CA  1 
ATOM   3967 C C   . VAL B 1 152 ? 6.870   12.116  43.434 1.000 31.140 0  152 VAL B C   1 
ATOM   3968 O O   . VAL B 1 152 ? 6.291   11.606  44.396 1.000 33.800 0  152 VAL B O   1 
ATOM   3969 C CB  . VAL B 1 152 ? 8.494   10.363  42.576 1.000 30.700 0  152 VAL B CB  1 
ATOM   3970 C CG1 . VAL B 1 152 ? 9.515   11.136  43.396 1.000 30.330 0  152 VAL B CG1 1 
ATOM   3971 C CG2 . VAL B 1 152 ? 8.054   9.095   43.290 1.000 30.930 0  152 VAL B CG2 1 
ATOM   3972 N N   . PHE B 1 153 ? 7.148   13.420  43.393 1.000 32.320 0  153 PHE B N   1 
ATOM   3973 C CA  . PHE B 1 153 ? 6.747   14.304  44.482 1.000 30.460 0  153 PHE B CA  1 
ATOM   3974 C C   . PHE B 1 153 ? 5.339   14.851  44.276 1.000 32.120 0  153 PHE B C   1 
ATOM   3975 O O   . PHE B 1 153 ? 4.525   14.857  45.207 1.000 32.020 0  153 PHE B O   1 
ATOM   3976 C CB  . PHE B 1 153 ? 7.745   15.452  44.625 1.000 29.120 0  153 PHE B CB  1 
ATOM   3977 C CG  . PHE B 1 153 ? 9.095   15.017  45.104 1.000 30.310 0  153 PHE B CG  1 
ATOM   3978 C CD1 . PHE B 1 153 ? 9.300   14.691  46.434 1.000 31.170 0  153 PHE B CD1 1 
ATOM   3979 C CD2 . PHE B 1 153 ? 10.164  14.936  44.227 1.000 29.630 0  153 PHE B CD2 1 
ATOM   3980 C CE1 . PHE B 1 153 ? 10.546  14.288  46.879 1.000 33.530 0  153 PHE B CE1 1 
ATOM   3981 C CE2 . PHE B 1 153 ? 11.411  14.537  44.665 1.000 27.570 0  153 PHE B CE2 1 
ATOM   3982 C CZ  . PHE B 1 153 ? 11.603  14.212  45.992 1.000 29.820 0  153 PHE B CZ  1 
ATOM   3983 N N   . THR B 1 154 ? 5.042   15.316  43.064 1.000 32.580 0  154 THR B N   1 
ATOM   3984 C CA  . THR B 1 154 ? 3.701   15.805  42.774 1.000 31.440 0  154 THR B CA  1 
ATOM   3985 C C   . THR B 1 154 ? 2.683   14.670  42.800 1.000 33.400 0  154 THR B C   1 
ATOM   3986 O O   . THR B 1 154 ? 1.513   14.898  43.129 1.000 32.740 0  154 THR B O   1 
ATOM   3987 C CB  . THR B 1 154 ? 3.690   16.527  41.428 1.000 32.060 0  154 THR B CB  1 
ATOM   3988 O OG1 . THR B 1 154 ? 3.935   15.586  40.379 1.000 33.510 0  154 THR B OG1 1 
ATOM   3989 C CG2 . THR B 1 154 ? 4.772   17.601  41.398 1.000 29.940 0  154 THR B CG2 1 
ATOM   3990 N N   . LYS B 1 155 ? 3.107   13.444  42.465 1.000 32.820 0  155 LYS B N   1 
ATOM   3991 C CA  . LYS B 1 155 ? 2.207   12.301  42.574 1.000 30.950 0  155 LYS B CA  1 
ATOM   3992 C C   . LYS B 1 155 ? 1.729   12.106  44.007 1.000 32.280 0  155 LYS B C   1 
ATOM   3993 O O   . LYS B 1 155 ? 0.602   11.650  44.231 1.000 35.690 0  155 LYS B O   1 
ATOM   3994 C CB  . LYS B 1 155 ? 2.912   11.015  42.129 1.000 33.580 0  155 LYS B CB  1 
ATOM   3995 C CG  . LYS B 1 155 ? 2.645   10.485  40.722 1.000 32.090 0  155 LYS B CG  1 
ATOM   3996 C CD  . LYS B 1 155 ? 2.811   11.513  39.632 1.000 34.230 0  155 LYS B CD  1 
ATOM   3997 C CE  . LYS B 1 155 ? 2.968   10.806  38.288 1.000 37.880 0  155 LYS B CE  1 
ATOM   3998 N NZ  . LYS B 1 155 ? 4.337   10.221  38.121 1.000 37.220 1  155 LYS B NZ  1 
ATOM   3999 N N   . ARG B 1 156 ? 2.554   12.476  44.985 1.000 30.550 0  156 ARG B N   1 
ATOM   4000 C CA  . ARG B 1 156 ? 2.265   12.245  46.396 1.000 32.240 0  156 ARG B CA  1 
ATOM   4001 C C   . ARG B 1 156 ? 1.626   13.436  47.098 1.000 33.340 0  156 ARG B C   1 
ATOM   4002 O O   . ARG B 1 156 ? 0.700   13.249  47.892 1.000 32.200 0  156 ARG B O   1 
ATOM   4003 C CB  . ARG B 1 156 ? 3.553   11.863  47.131 1.000 31.790 0  156 ARG B CB  1 
ATOM   4004 C CG  . ARG B 1 156 ? 3.343   11.453  48.573 1.000 31.750 0  156 ARG B CG  1 
ATOM   4005 C CD  . ARG B 1 156 ? 2.630   10.119  48.652 1.000 33.800 0  156 ARG B CD  1 
ATOM   4006 N NE  . ARG B 1 156 ? 2.018   9.911   49.958 1.000 35.590 0  156 ARG B NE  1 
ATOM   4007 C CZ  . ARG B 1 156 ? 0.717   10.012  50.198 1.000 37.740 0  156 ARG B CZ  1 
ATOM   4008 N NH1 . ARG B 1 156 ? -0.140  10.312  49.234 1.000 33.840 1  156 ARG B NH1 1 
ATOM   4009 N NH2 . ARG B 1 156 ? 0.267   9.807   51.433 1.000 36.680 0  156 ARG B NH2 1 
ATOM   4010 N N   . MET B 1 157 ? 2.105   14.654  46.835 1.000 33.610 0  157 MET B N   1 
ATOM   4011 C CA  . MET B 1 157 ? 1.646   15.844  47.543 1.000 30.560 0  157 MET B CA  1 
ATOM   4012 C C   . MET B 1 157 ? 0.630   16.664  46.765 1.000 33.090 0  157 MET B C   1 
ATOM   4013 O O   . MET B 1 157 ? -0.125  17.428  47.376 1.000 31.590 0  157 MET B O   1 
ATOM   4014 C CB  . MET B 1 157 ? 2.831   16.756  47.871 1.000 30.240 0  157 MET B CB  1 
ATOM   4015 C CG  . MET B 1 157 ? 4.123   16.032  48.171 1.000 31.980 0  157 MET B CG  1 
ATOM   4016 S SD  . MET B 1 157 ? 5.458   17.181  48.552 1.000 32.390 0  157 MET B SD  1 
ATOM   4017 C CE  . MET B 1 157 ? 4.554   18.549  49.274 1.000 31.950 0  157 MET B CE  1 
ATOM   4018 N N   . GLY B 1 158 ? 0.607   16.540  45.442 1.000 31.220 0  158 GLY B N   1 
ATOM   4019 C CA  . GLY B 1 158 ? -0.093  17.485  44.600 1.000 30.140 0  158 GLY B CA  1 
ATOM   4020 C C   . GLY B 1 158 ? 0.896   18.435  43.960 1.000 30.590 0  158 GLY B C   1 
ATOM   4021 O O   . GLY B 1 158 ? 1.838   18.890  44.617 1.000 29.490 0  158 GLY B O   1 
ATOM   4022 N N   . ALA B 1 159 ? 0.690   18.754  42.681 1.000 31.270 0  159 ALA B N   1 
ATOM   4023 C CA  . ALA B 1 159 ? 1.684   19.532  41.950 1.000 28.230 0  159 ALA B CA  1 
ATOM   4024 C C   . ALA B 1 159 ? 1.812   20.938  42.521 1.000 29.650 0  159 ALA B C   1 
ATOM   4025 O O   . ALA B 1 159 ? 2.908   21.358  42.921 1.000 30.720 0  159 ALA B O   1 
ATOM   4026 C CB  . ALA B 1 159 ? 1.321   19.576  40.466 1.000 27.520 0  159 ALA B CB  1 
ATOM   4027 N N   . VAL B 1 160 ? 0.695   21.668  42.601 1.000 29.190 0  160 VAL B N   1 
ATOM   4028 C CA  . VAL B 1 160 ? 0.741   23.029  43.128 1.000 30.370 0  160 VAL B CA  1 
ATOM   4029 C C   . VAL B 1 160 ? 1.171   23.006  44.585 1.000 29.870 0  160 VAL B C   1 
ATOM   4030 O O   . VAL B 1 160 ? 1.895   23.898  45.044 1.000 31.370 0  160 VAL B O   1 
ATOM   4031 C CB  . VAL B 1 160 ? -0.626  23.723  42.945 1.000 30.810 0  160 VAL B CB  1 
ATOM   4032 C CG1 . VAL B 1 160 ? -0.789  24.875  43.928 1.000 29.450 0  160 VAL B CG1 1 
ATOM   4033 C CG2 . VAL B 1 160 ? -0.792  24.217  41.518 1.000 29.100 0  160 VAL B CG2 1 
ATOM   4034 N N   . GLU B 1 161 ? 0.764   21.973  45.326 1.000 29.440 0  161 GLU B N   1 
ATOM   4035 C CA  . GLU B 1 161 ? 1.219   21.828  46.703 1.000 30.690 0  161 GLU B CA  1 
ATOM   4036 C C   . GLU B 1 161 ? 2.735   21.693  46.766 1.000 29.920 0  161 GLU B C   1 
ATOM   4037 O O   . GLU B 1 161 ? 3.387   22.340  47.591 1.000 32.920 0  161 GLU B O   1 
ATOM   4038 C CB  . GLU B 1 161 ? 0.540   20.624  47.357 1.000 31.250 0  161 GLU B CB  1 
ATOM   4039 C CG  . GLU B 1 161 ? -0.870  20.902  47.867 1.000 30.390 0  161 GLU B CG  1 
ATOM   4040 C CD  . GLU B 1 161 ? -1.904  20.942  46.756 1.000 31.130 0  161 GLU B CD  1 
ATOM   4041 O OE1 . GLU B 1 161 ? -1.566  20.573  45.611 1.000 30.490 0  161 GLU B OE1 1 
ATOM   4042 O OE2 . GLU B 1 161 ? -3.056  21.341  47.026 1.000 33.130 -1 161 GLU B OE2 1 
ATOM   4043 N N   . GLN B 1 162 ? 3.316   20.884  45.878 1.000 26.930 0  162 GLN B N   1 
ATOM   4044 C CA  . GLN B 1 162 ? 4.761   20.684  45.909 1.000 30.640 0  162 GLN B CA  1 
ATOM   4045 C C   . GLN B 1 162 ? 5.503   21.960  45.529 1.000 29.980 0  162 GLN B C   1 
ATOM   4046 O O   . GLN B 1 162 ? 6.559   22.265  46.097 1.000 27.530 0  162 GLN B O   1 
ATOM   4047 C CB  . GLN B 1 162 ? 5.158   19.532  44.985 1.000 30.580 0  162 GLN B CB  1 
ATOM   4048 C CG  . GLN B 1 162 ? 6.660   19.282  44.926 1.000 29.500 0  162 GLN B CG  1 
ATOM   4049 C CD  . GLN B 1 162 ? 7.241   19.560  43.556 1.000 27.810 0  162 GLN B CD  1 
ATOM   4050 O OE1 . GLN B 1 162 ? 6.587   20.160  42.706 1.000 29.630 0  162 GLN B OE1 1 
ATOM   4051 N NE2 . GLN B 1 162 ? 8.479   19.130  43.336 1.000 26.450 0  162 GLN B NE2 1 
ATOM   4052 N N   . ILE B 1 163 ? 4.961   22.728  44.583 1.000 29.630 0  163 ILE B N   1 
ATOM   4053 C CA  . ILE B 1 163 ? 5.635   23.951  44.153 1.000 26.660 0  163 ILE B CA  1 
ATOM   4054 C C   . ILE B 1 163 ? 5.571   25.010  45.251 1.000 25.720 0  163 ILE B C   1 
ATOM   4055 O O   . ILE B 1 163 ? 6.576   25.664  45.575 1.000 27.670 0  163 ILE B O   1 
ATOM   4056 C CB  . ILE B 1 163 ? 5.026   24.453  42.833 1.000 25.530 0  163 ILE B CB  1 
ATOM   4057 C CG1 . ILE B 1 163 ? 5.101   23.344  41.779 1.000 25.340 0  163 ILE B CG1 1 
ATOM   4058 C CG2 . ILE B 1 163 ? 5.738   25.706  42.358 1.000 26.870 0  163 ILE B CG2 1 
ATOM   4059 C CD1 . ILE B 1 163 ? 4.956   23.818  40.360 1.000 25.190 0  163 ILE B CD1 1 
ATOM   4060 N N   . GLU B 1 164 ? 4.384   25.200  45.832 1.000 27.570 0  164 GLU B N   1 
ATOM   4061 C CA  . GLU B 1 164 ? 4.241   26.073  46.992 1.000 27.660 0  164 GLU B CA  1 
ATOM   4062 C C   . GLU B 1 164 ? 5.224   25.685  48.088 1.000 28.090 0  164 GLU B C   1 
ATOM   4063 O O   . GLU B 1 164 ? 5.898   26.544  48.669 1.000 28.790 0  164 GLU B O   1 
ATOM   4064 C CB  . GLU B 1 164 ? 2.800   26.016  47.510 1.000 26.460 0  164 GLU B CB  1 
ATOM   4065 C CG  . GLU B 1 164 ? 2.589   26.699  48.853 1.000 29.830 0  164 GLU B CG  1 
ATOM   4066 C CD  . GLU B 1 164 ? 1.143   26.644  49.319 1.000 31.840 0  164 GLU B CD  1 
ATOM   4067 O OE1 . GLU B 1 164 ? 0.319   26.002  48.637 1.000 33.410 0  164 GLU B OE1 1 
ATOM   4068 O OE2 . GLU B 1 164 ? 0.831   27.241  50.370 1.000 33.430 -1 164 GLU B OE2 1 
ATOM   4069 N N   . PHE B 1 165 ? 5.317   24.385  48.381 1.000 25.770 0  165 PHE B N   1 
ATOM   4070 C CA  . PHE B 1 165 ? 6.206   23.919  49.437 1.000 26.900 0  165 PHE B CA  1 
ATOM   4071 C C   . PHE B 1 165 ? 7.666   24.224  49.121 1.000 28.670 0  165 PHE B C   1 
ATOM   4072 O O   . PHE B 1 165 ? 8.423   24.654  50.001 1.000 28.250 0  165 PHE B O   1 
ATOM   4073 C CB  . PHE B 1 165 ? 6.003   22.419  49.646 1.000 29.950 0  165 PHE B CB  1 
ATOM   4074 C CG  . PHE B 1 165 ? 6.750   21.859  50.821 1.000 30.420 0  165 PHE B CG  1 
ATOM   4075 C CD1 . PHE B 1 165 ? 6.230   21.954  52.098 1.000 27.820 0  165 PHE B CD1 1 
ATOM   4076 C CD2 . PHE B 1 165 ? 7.971   21.228  50.644 1.000 30.100 0  165 PHE B CD2 1 
ATOM   4077 C CE1 . PHE B 1 165 ? 6.913   21.436  53.179 1.000 29.970 0  165 PHE B CE1 1 
ATOM   4078 C CE2 . PHE B 1 165 ? 8.660   20.708  51.721 1.000 32.690 0  165 PHE B CE2 1 
ATOM   4079 C CZ  . PHE B 1 165 ? 8.130   20.813  52.992 1.000 33.780 0  165 PHE B CZ  1 
ATOM   4080 N N   . ALA B 1 166 ? 8.086   23.985  47.875 1.000 26.930 0  166 ALA B N   1 
ATOM   4081 C CA  . ALA B 1 166 ? 9.462   24.282  47.487 1.000 26.350 0  166 ALA B CA  1 
ATOM   4082 C C   . ALA B 1 166 ? 9.779   25.755  47.696 1.000 26.900 0  166 ALA B C   1 
ATOM   4083 O O   . ALA B 1 166 ? 10.834  26.109  48.240 1.000 26.120 0  166 ALA B O   1 
ATOM   4084 C CB  . ALA B 1 166 ? 9.697   23.881  46.032 1.000 25.050 0  166 ALA B CB  1 
ATOM   4085 N N   . PHE B 1 167 ? 8.863   26.634  47.280 1.000 27.000 0  167 PHE B N   1 
ATOM   4086 C CA  . PHE B 1 167 ? 9.108   28.064  47.446 1.000 24.910 0  167 PHE B CA  1 
ATOM   4087 C C   . PHE B 1 167 ? 9.120   28.465  48.918 1.000 24.990 0  167 PHE B C   1 
ATOM   4088 O O   . PHE B 1 167 ? 9.910   29.326  49.325 1.000 24.990 0  167 PHE B O   1 
ATOM   4089 C CB  . PHE B 1 167 ? 8.074   28.868  46.665 1.000 24.570 0  167 PHE B CB  1 
ATOM   4090 C CG  . PHE B 1 167 ? 8.460   29.108  45.236 1.000 24.430 0  167 PHE B CG  1 
ATOM   4091 C CD1 . PHE B 1 167 ? 9.310   30.147  44.902 1.000 24.450 0  167 PHE B CD1 1 
ATOM   4092 C CD2 . PHE B 1 167 ? 7.978   28.293  44.227 1.000 24.300 0  167 PHE B CD2 1 
ATOM   4093 C CE1 . PHE B 1 167 ? 9.671   30.370  43.590 1.000 24.550 0  167 PHE B CE1 1 
ATOM   4094 C CE2 . PHE B 1 167 ? 8.333   28.512  42.910 1.000 24.200 0  167 PHE B CE2 1 
ATOM   4095 C CZ  . PHE B 1 167 ? 9.180   29.551  42.591 1.000 24.370 0  167 PHE B CZ  1 
ATOM   4096 N N   . ARG B 1 168 ? 8.262   27.852  49.735 1.000 27.260 0  168 ARG B N   1 
ATOM   4097 C CA  . ARG B 1 168 ? 8.237   28.208  51.150 1.000 26.310 0  168 ARG B CA  1 
ATOM   4098 C C   . ARG B 1 168 ? 9.516   27.766  51.849 1.000 27.700 0  168 ARG B C   1 
ATOM   4099 O O   . ARG B 1 168 ? 10.086  28.519  52.650 1.000 29.110 0  168 ARG B O   1 
ATOM   4100 C CB  . ARG B 1 168 ? 7.003   27.607  51.825 1.000 25.880 0  168 ARG B CB  1 
ATOM   4101 C CG  . ARG B 1 168 ? 5.703   28.340  51.496 1.000 25.550 0  168 ARG B CG  1 
ATOM   4102 C CD  . ARG B 1 168 ? 4.548   27.828  52.342 1.000 29.280 0  168 ARG B CD  1 
ATOM   4103 N NE  . ARG B 1 168 ? 3.243   28.241  51.832 1.000 29.990 0  168 ARG B NE  1 
ATOM   4104 C CZ  . ARG B 1 168 ? 2.709   29.443  52.003 1.000 29.060 0  168 ARG B CZ  1 
ATOM   4105 N NH1 . ARG B 1 168 ? 3.349   30.399  52.656 1.000 27.070 1  168 ARG B NH1 1 
ATOM   4106 N NH2 . ARG B 1 168 ? 1.500   29.691  51.507 1.000 28.540 0  168 ARG B NH2 1 
ATOM   4107 N N   . GLN B 1 169 ? 10.010  26.567  51.525 1.000 27.160 0  169 GLN B N   1 
ATOM   4108 C CA  . GLN B 1 169 ? 11.268  26.110  52.104 1.000 26.760 0  169 GLN B CA  1 
ATOM   4109 C C   . GLN B 1 169 ? 12.419  27.007  51.668 1.000 28.110 0  169 GLN B C   1 
ATOM   4110 O O   . GLN B 1 169 ? 13.261  27.400  52.490 1.000 25.830 0  169 GLN B O   1 
ATOM   4111 C CB  . GLN B 1 169 ? 11.553  24.663  51.689 1.000 27.900 0  169 GLN B CB  1 
ATOM   4112 C CG  . GLN B 1 169 ? 10.724  23.587  52.385 1.000 32.990 0  169 GLN B CG  1 
ATOM   4113 C CD  . GLN B 1 169 ? 10.751  23.679  53.901 1.000 34.260 0  169 GLN B CD  1 
ATOM   4114 O OE1 . GLN B 1 169 ? 11.797  23.926  54.505 1.000 31.170 0  169 GLN B OE1 1 
ATOM   4115 N NE2 . GLN B 1 169 ? 9.599   23.458  54.525 1.000 33.460 0  169 GLN B NE2 1 
ATOM   4116 N N   . ALA B 1 170 ? 12.467  27.351  50.376 1.000 27.560 0  170 ALA B N   1 
ATOM   4117 C CA  . ALA B 1 170 ? 13.521  28.229  49.880 1.000 25.950 0  170 ALA B CA  1 
ATOM   4118 C C   . ALA B 1 170 ? 13.499  29.585  50.577 1.000 29.600 0  170 ALA B C   1 
ATOM   4119 O O   . ALA B 1 170 ? 14.552  30.106  50.962 1.000 30.050 0  170 ALA B O   1 
ATOM   4120 C CB  . ALA B 1 170 ? 13.389  28.394  48.368 1.000 25.470 0  170 ALA B CB  1 
ATOM   4121 N N   . HIS B 1 171 ? 12.308  30.168  50.763 1.000 28.680 0  171 HIS B N   1 
ATOM   4122 C CA  . HIS B 1 171 ? 12.231  31.445  51.471 1.000 29.850 0  171 HIS B CA  1 
ATOM   4123 C C   . HIS B 1 171 ? 12.663  31.300  52.923 1.000 31.280 0  171 HIS B C   1 
ATOM   4124 O O   . HIS B 1 171 ? 13.263  32.219  53.492 1.000 33.230 0  171 HIS B O   1 
ATOM   4125 C CB  . HIS B 1 171 ? 10.818  32.021  51.398 1.000 30.250 0  171 HIS B CB  1 
ATOM   4126 C CG  . HIS B 1 171 ? 10.725  33.453  51.835 1.000 30.290 0  171 HIS B CG  1 
ATOM   4127 N ND1 . HIS B 1 171 ? 11.711  34.380  51.568 1.000 30.740 0  171 HIS B ND1 1 
ATOM   4128 C CD2 . HIS B 1 171 ? 9.761   34.116  52.519 1.000 28.280 0  171 HIS B CD2 1 
ATOM   4129 C CE1 . HIS B 1 171 ? 11.359  35.551  52.069 1.000 27.830 0  171 HIS B CE1 1 
ATOM   4130 N NE2 . HIS B 1 171 ? 10.180  35.418  52.651 1.000 28.780 0  171 HIS B NE2 1 
ATOM   4131 N N   . GLU B 1 172 ? 12.359  30.158  53.545 1.000 30.060 0  172 GLU B N   1 
ATOM   4132 C CA  . GLU B 1 172 ? 12.730  29.983  54.943 1.000 30.170 0  172 GLU B CA  1 
ATOM   4133 C C   . GLU B 1 172 ? 14.239  29.855  55.106 1.000 32.020 0  172 GLU B C   1 
ATOM   4134 O O   . GLU B 1 172 ? 14.811  30.386  56.066 1.000 34.980 0  172 GLU B O   1 
ATOM   4135 C CB  . GLU B 1 172 ? 12.015  28.767  55.531 1.000 32.220 0  172 GLU B CB  1 
ATOM   4136 C CG  . GLU B 1 172 ? 12.374  28.478  56.977 1.000 32.810 0  172 GLU B CG  1 
ATOM   4137 C CD  . GLU B 1 172 ? 12.353  26.997  57.296 1.000 35.740 0  172 GLU B CD  1 
ATOM   4138 O OE1 . GLU B 1 172 ? 12.104  26.195  56.370 1.000 34.970 0  172 GLU B OE1 1 
ATOM   4139 O OE2 . GLU B 1 172 ? 12.574  26.637  58.472 1.000 35.810 -1 172 GLU B OE2 1 
ATOM   4140 N N   . HIS B 1 173 ? 14.908  29.165  54.180 1.000 30.260 0  173 HIS B N   1 
ATOM   4141 C CA  . HIS B 1 173 ? 16.339  28.918  54.319 1.000 30.710 0  173 HIS B CA  1 
ATOM   4142 C C   . HIS B 1 173 ? 17.219  29.870  53.518 1.000 33.270 0  173 HIS B C   1 
ATOM   4143 O O   . HIS B 1 173 ? 18.444  29.805  53.647 1.000 29.670 0  173 HIS B O   1 
ATOM   4144 C CB  . HIS B 1 173 ? 16.668  27.476  53.924 1.000 28.590 0  173 HIS B CB  1 
ATOM   4145 C CG  . HIS B 1 173 ? 16.017  26.459  54.804 1.000 29.390 0  173 HIS B CG  1 
ATOM   4146 N ND1 . HIS B 1 173 ? 15.178  25.481  54.318 1.000 30.460 0  173 HIS B ND1 1 
ATOM   4147 C CD2 . HIS B 1 173 ? 16.064  26.284  56.146 1.000 29.780 0  173 HIS B CD2 1 
ATOM   4148 C CE1 . HIS B 1 173 ? 14.745  24.739  55.320 1.000 29.250 0  173 HIS B CE1 1 
ATOM   4149 N NE2 . HIS B 1 173 ? 15.266  25.206  56.441 1.000 31.430 0  173 HIS B NE2 1 
ATOM   4150 N N   . ALA B 1 174 ? 16.640  30.751  52.710 1.000 34.050 0  174 ALA B N   1 
ATOM   4151 C CA  . ALA B 1 174 ? 17.397  31.754  51.960 1.000 32.980 0  174 ALA B CA  1 
ATOM   4152 C C   . ALA B 1 174 ? 16.597  33.045  51.950 1.000 33.400 0  174 ALA B C   1 
ATOM   4153 O O   . ALA B 1 174 ? 16.049  33.445  50.916 1.000 34.170 0  174 ALA B O   1 
ATOM   4154 C CB  . ALA B 1 174 ? 17.688  31.265  50.538 1.000 34.020 0  174 ALA B CB  1 
ATOM   4155 N N   . PRO B 1 175 ? 16.487  33.723  53.099 1.000 33.240 0  175 PRO B N   1 
ATOM   4156 C CA  . PRO B 1 175 ? 15.489  34.799  53.194 1.000 33.670 0  175 PRO B CA  1 
ATOM   4157 C C   . PRO B 1 175 ? 15.851  36.060  52.433 1.000 31.160 0  175 PRO B C   1 
ATOM   4158 O O   . PRO B 1 175 ? 14.975  36.895  52.212 1.000 30.010 0  175 PRO B O   1 
ATOM   4159 C CB  . PRO B 1 175 ? 15.392  35.060  54.694 1.000 32.310 0  175 PRO B CB  1 
ATOM   4160 C CG  . PRO B 1 175 ? 16.690  34.625  55.257 1.000 30.730 0  175 PRO B CG  1 
ATOM   4161 C CD  . PRO B 1 175 ? 17.180  33.493  54.379 1.000 32.320 0  175 PRO B CD  1 
ATOM   4162 N N   . LYS B 1 176 ? 17.097  36.262  52.042 1.000 33.090 0  176 LYS B N   1 
ATOM   4163 C CA  . LYS B 1 176 ? 17.394  37.479  51.314 1.000 32.840 0  176 LYS B CA  1 
ATOM   4164 C C   . LYS B 1 176 ? 17.596  37.257  49.822 1.000 31.980 0  176 LYS B C   1 
ATOM   4165 O O   . LYS B 1 176 ? 18.102  38.140  49.121 1.000 29.600 0  176 LYS B O   1 
ATOM   4166 C CB  . LYS B 1 176 ? 18.479  38.233  52.037 1.000 31.060 0  176 LYS B CB  1 
ATOM   4167 C CG  . LYS B 1 176 ? 18.151  38.042  53.528 1.000 34.880 0  176 LYS B CG  1 
ATOM   4168 C CD  . LYS B 1 176 ? 17.632  39.361  54.048 1.000 40.880 0  176 LYS B CD  1 
ATOM   4169 C CE  . LYS B 1 176 ? 17.867  39.715  55.479 1.000 48.480 0  176 LYS B CE  1 
ATOM   4170 N NZ  . LYS B 1 176 ? 18.261  41.136  55.374 1.000 52.020 1  176 LYS B NZ  1 
ATOM   4171 N N   . ALA B 1 177 ? 17.224  36.079  49.339 1.000 31.060 0  177 ALA B N   1 
ATOM   4172 C CA  . ALA B 1 177 ? 17.429  35.671  47.963 1.000 29.610 0  177 ALA B CA  1 
ATOM   4173 C C   . ALA B 1 177 ? 16.159  35.906  47.158 1.000 26.870 0  177 ALA B C   1 
ATOM   4174 O O   . ALA B 1 177 ? 15.044  35.762  47.662 1.000 27.820 0  177 ALA B O   1 
ATOM   4175 C CB  . ALA B 1 177 ? 17.838  34.199  47.891 1.000 29.250 0  177 ALA B CB  1 
ATOM   4176 N N   . GLN B 1 178 ? 16.350  36.302  45.904 1.000 25.120 0  178 GLN B N   1 
ATOM   4177 C CA  . GLN B 1 178 ? 15.259  36.397  44.944 1.000 25.280 0  178 GLN B CA  1 
ATOM   4178 C C   . GLN B 1 178 ? 14.797  34.999  44.548 1.000 25.470 0  178 GLN B C   1 
ATOM   4179 O O   . GLN B 1 178 ? 15.575  34.221  43.992 1.000 26.360 0  178 GLN B O   1 
ATOM   4180 C CB  . GLN B 1 178 ? 15.734  37.162  43.711 1.000 24.960 0  178 GLN B CB  1 
ATOM   4181 C CG  . GLN B 1 178 ? 14.657  37.846  42.880 1.000 24.890 0  178 GLN B CG  1 
ATOM   4182 C CD  . GLN B 1 178 ? 15.038  37.939  41.405 1.000 24.830 0  178 GLN B CD  1 
ATOM   4183 O OE1 . GLN B 1 178 ? 15.958  37.264  40.948 1.000 26.130 0  178 GLN B OE1 1 
ATOM   4184 N NE2 . GLN B 1 178 ? 14.341  38.792  40.661 1.000 24.830 0  178 GLN B NE2 1 
ATOM   4185 N N   . LEU B 1 179 ? 13.534  34.680  44.806 1.000 25.760 0  179 LEU B N   1 
ATOM   4186 C CA  . LEU B 1 179 ? 12.986  33.371  44.473 1.000 24.660 0  179 LEU B CA  1 
ATOM   4187 C C   . LEU B 1 179 ? 12.270  33.446  43.131 1.000 25.790 0  179 LEU B C   1 
ATOM   4188 O O   . LEU B 1 179 ? 11.383  34.289  42.941 1.000 26.630 0  179 LEU B O   1 
ATOM   4189 C CB  . LEU B 1 179 ? 12.030  32.886  45.561 1.000 24.700 0  179 LEU B CB  1 
ATOM   4190 C CG  . LEU B 1 179 ? 12.648  32.680  46.943 1.000 24.850 0  179 LEU B CG  1 
ATOM   4191 C CD1 . LEU B 1 179 ? 11.652  32.019  47.872 1.000 25.190 0  179 LEU B CD1 1 
ATOM   4192 C CD2 . LEU B 1 179 ? 13.923  31.859  46.849 1.000 26.440 0  179 LEU B CD2 1 
ATOM   4193 N N   . VAL B 1 180 ? 12.638  32.554  42.212 1.000 24.440 0  180 VAL B N   1 
ATOM   4194 C CA  . VAL B 1 180 ? 12.213  32.635  40.823 1.000 24.350 0  180 VAL B CA  1 
ATOM   4195 C C   . VAL B 1 180 ? 11.597  31.312  40.401 1.000 25.110 0  180 VAL B C   1 
ATOM   4196 O O   . VAL B 1 180 ? 12.098  30.238  40.754 1.000 26.640 0  180 VAL B O   1 
ATOM   4197 C CB  . VAL B 1 180 ? 13.403  32.977  39.899 1.000 27.210 0  180 VAL B CB  1 
ATOM   4198 C CG1 . VAL B 1 180 ? 12.938  33.145  38.460 1.000 25.680 0  180 VAL B CG1 1 
ATOM   4199 C CG2 . VAL B 1 180 ? 14.134  34.218  40.394 1.000 26.500 0  180 VAL B CG2 1 
ATOM   4200 N N   . TYR B 1 181 ? 10.520  31.386  39.629 1.000 24.900 0  181 TYR B N   1 
ATOM   4201 C CA  . TYR B 1 181 ? 10.080  30.239  38.846 1.000 24.200 0  181 TYR B CA  1 
ATOM   4202 C C   . TYR B 1 181 ? 10.622  30.418  37.435 1.000 24.770 0  181 TYR B C   1 
ATOM   4203 O O   . TYR B 1 181 ? 10.282  31.393  36.761 1.000 26.870 0  181 TYR B O   1 
ATOM   4204 C CB  . TYR B 1 181 ? 8.562   30.090  38.811 1.000 24.010 0  181 TYR B CB  1 
ATOM   4205 C CG  . TYR B 1 181 ? 8.160   29.050  37.795 1.000 25.170 0  181 TYR B CG  1 
ATOM   4206 C CD1 . TYR B 1 181 ? 8.358   27.699  38.049 1.000 24.920 0  181 TYR B CD1 1 
ATOM   4207 C CD2 . TYR B 1 181 ? 7.631   29.415  36.564 1.000 26.510 0  181 TYR B CD2 1 
ATOM   4208 C CE1 . TYR B 1 181 ? 8.017   26.739  37.116 1.000 25.700 0  181 TYR B CE1 1 
ATOM   4209 C CE2 . TYR B 1 181 ? 7.287   28.461  35.623 1.000 26.020 0  181 TYR B CE2 1 
ATOM   4210 C CZ  . TYR B 1 181 ? 7.483   27.124  35.906 1.000 25.780 0  181 TYR B CZ  1 
ATOM   4211 O OH  . TYR B 1 181 ? 7.142   26.167  34.975 1.000 27.470 0  181 TYR B OH  1 
ATOM   4212 N N   . ASN B 1 182 ? 11.454  29.485  36.992 1.000 24.030 0  182 ASN B N   1 
ATOM   4213 C CA  . ASN B 1 182 ? 12.195  29.625  35.745 1.000 24.670 0  182 ASN B CA  1 
ATOM   4214 C C   . ASN B 1 182 ? 11.663  28.632  34.720 1.000 24.840 0  182 ASN B C   1 
ATOM   4215 O O   . ASN B 1 182 ? 11.526  27.440  35.019 1.000 23.950 0  182 ASN B O   1 
ATOM   4216 C CB  . ASN B 1 182 ? 13.695  29.411  35.976 1.000 26.570 0  182 ASN B CB  1 
ATOM   4217 C CG  . ASN B 1 182 ? 14.527  29.728  34.748 1.000 24.920 0  182 ASN B CG  1 
ATOM   4218 O OD1 . ASN B 1 182 ? 14.732  30.894  34.407 1.000 25.040 0  182 ASN B OD1 1 
ATOM   4219 N ND2 . ASN B 1 182 ? 15.020  28.691  34.083 1.000 24.240 0  182 ASN B ND2 1 
ATOM   4220 N N   . ASP B 1 183 ? 11.357  29.124  33.519 1.000 23.990 0  183 ASP B N   1 
ATOM   4221 C CA  . ASP B 1 183 ? 10.799  28.258  32.487 1.000 24.810 0  183 ASP B CA  1 
ATOM   4222 C C   . ASP B 1 183 ? 10.902  28.978  31.148 1.000 24.000 0  183 ASP B C   1 
ATOM   4223 O O   . ASP B 1 183 ? 11.097  30.194  31.096 1.000 25.000 0  183 ASP B O   1 
ATOM   4224 C CB  . ASP B 1 183 ? 9.351   27.876  32.834 1.000 28.290 0  183 ASP B CB  1 
ATOM   4225 C CG  . ASP B 1 183 ? 8.757   26.837  31.895 1.000 27.720 0  183 ASP B CG  1 
ATOM   4226 O OD1 . ASP B 1 183 ? 9.433   26.432  30.928 1.000 27.700 0  183 ASP B OD1 1 
ATOM   4227 O OD2 . ASP B 1 183 ? 7.596   26.435  32.129 1.000 27.880 -1 183 ASP B OD2 1 
ATOM   4228 N N   . PHE B 1 184 ? 10.778  28.212  30.063 1.000 24.810 0  184 PHE B N   1 
ATOM   4229 C CA  . PHE B 1 184 ? 11.090  28.710  28.730 1.000 24.100 0  184 PHE B CA  1 
ATOM   4230 C C   . PHE B 1 184 ? 9.854   29.079  27.918 1.000 25.310 0  184 PHE B C   1 
ATOM   4231 O O   . PHE B 1 184 ? 9.918   29.093  26.684 1.000 26.670 0  184 PHE B O   1 
ATOM   4232 C CB  . PHE B 1 184 ? 11.943  27.696  27.959 1.000 25.130 0  184 PHE B CB  1 
ATOM   4233 C CG  . PHE B 1 184 ? 11.289  26.351  27.762 1.000 25.730 0  184 PHE B CG  1 
ATOM   4234 C CD1 . PHE B 1 184 ? 11.437  25.350  28.707 1.000 24.040 0  184 PHE B CD1 1 
ATOM   4235 C CD2 . PHE B 1 184 ? 10.558  26.075  26.615 1.000 26.030 0  184 PHE B CD2 1 
ATOM   4236 C CE1 . PHE B 1 184 ? 10.853  24.109  28.523 1.000 25.220 0  184 PHE B CE1 1 
ATOM   4237 C CE2 . PHE B 1 184 ? 9.971   24.836  26.429 1.000 27.200 0  184 PHE B CE2 1 
ATOM   4238 C CZ  . PHE B 1 184 ? 10.120  23.852  27.385 1.000 26.300 0  184 PHE B CZ  1 
ATOM   4239 N N   . MET B 1 185 ? 8.740   29.395  28.576 1.000 28.930 0  185 MET B N   1 
ATOM   4240 C CA  . MET B 1 185 ? 7.579   29.890  27.852 1.000 27.480 0  185 MET B CA  1 
ATOM   4241 C C   . MET B 1 185 ? 7.945   31.191  27.147 1.000 27.910 0  185 MET B C   1 
ATOM   4242 O O   . MET B 1 185 ? 8.791   31.957  27.614 1.000 28.460 0  185 MET B O   1 
ATOM   4243 C CB  . MET B 1 185 ? 6.410   30.125  28.808 1.000 27.360 0  185 MET B CB  1 
ATOM   4244 C CG  . MET B 1 185 ? 6.503   31.450  29.544 1.000 28.930 0  185 MET B CG  1 
ATOM   4245 S SD  . MET B 1 185 ? 7.892   31.549  30.684 1.000 28.340 0  185 MET B SD  1 
ATOM   4246 C CE  . MET B 1 185 ? 7.384   30.364  31.895 1.000 26.380 0  185 MET B CE  1 
ATOM   4247 N N   . GLY B 1 186 ? 7.306   31.445  26.008 1.000 29.860 0  186 GLY B N   1 
ATOM   4248 C CA  . GLY B 1 186 ? 7.639   32.618  25.235 1.000 28.670 0  186 GLY B CA  1 
ATOM   4249 C C   . GLY B 1 186 ? 6.612   32.982  24.185 1.000 28.470 0  186 GLY B C   1 
ATOM   4250 O O   . GLY B 1 186 ? 5.501   32.445  24.152 1.000 30.460 0  186 GLY B O   1 
ATOM   4251 N N   . PRO B 1 187 ? 6.964   33.927  23.311 1.000 30.620 0  187 PRO B N   1 
ATOM   4252 C CA  . PRO B 1 187 ? 6.021   34.352  22.268 1.000 30.680 0  187 PRO B CA  1 
ATOM   4253 C C   . PRO B 1 187 ? 5.761   33.229  21.276 1.000 30.270 0  187 PRO B C   1 
ATOM   4254 O O   . PRO B 1 187 ? 6.665   32.472  20.916 1.000 31.040 0  187 PRO B O   1 
ATOM   4255 C CB  . PRO B 1 187 ? 6.722   35.545  21.603 1.000 32.860 0  187 PRO B CB  1 
ATOM   4256 C CG  . PRO B 1 187 ? 7.949   35.834  22.423 1.000 29.640 0  187 PRO B CG  1 
ATOM   4257 C CD  . PRO B 1 187 ? 8.259   34.621  23.228 1.000 29.070 0  187 PRO B CD  1 
ATOM   4258 N N   . GLY B 1 188 ? 4.518   33.138  20.827 1.000 30.200 0  188 GLY B N   1 
ATOM   4259 C CA  . GLY B 1 188 ? 4.108   32.074  19.932 1.000 30.260 0  188 GLY B CA  1 
ATOM   4260 C C   . GLY B 1 188 ? 2.608   31.899  19.956 1.000 30.620 0  188 GLY B C   1 
ATOM   4261 O O   . GLY B 1 188 ? 1.898   32.482  20.776 1.000 30.000 0  188 GLY B O   1 
ATOM   4262 N N   . LEU B 1 189 ? 2.079   31.085  19.041 1.000 32.440 0  189 LEU B N   1 
ATOM   4263 C CA  . LEU B 1 189 ? 0.602   31.079  18.874 1.000 33.940 0  189 LEU B CA  1 
ATOM   4264 C C   . LEU B 1 189 ? -0.146  29.813  19.315 1.000 34.360 0  189 LEU B C   1 
ATOM   4265 O O   . LEU B 1 189 ? -1.277  29.973  19.776 1.000 37.150 0  189 LEU B O   1 
ATOM   4266 C CB  . LEU B 1 189 ? 0.334   31.398  17.404 1.000 35.110 0  189 LEU B CB  1 
ATOM   4267 C CG  . LEU B 1 189 ? 0.128   32.875  17.065 1.000 34.540 0  189 LEU B CG  1 
ATOM   4268 C CD1 . LEU B 1 189 ? -0.618  33.003  15.757 1.000 32.140 0  189 LEU B CD1 1 
ATOM   4269 C CD2 . LEU B 1 189 ? -0.619  33.572  18.180 1.000 33.320 0  189 LEU B CD2 1 
ATOM   4270 N N   . GLY B 1 190 ? 0.448   28.629  19.142 1.000 32.180 0  190 GLY B N   1 
ATOM   4271 C CA  . GLY B 1 190 ? -0.266  27.372  19.454 1.000 33.220 0  190 GLY B CA  1 
ATOM   4272 C C   . GLY B 1 190 ? 0.159   26.789  20.786 1.000 34.730 0  190 GLY B C   1 
ATOM   4273 O O   . GLY B 1 190 ? -0.233  27.347  21.829 1.000 31.340 0  190 GLY B O   1 
ATOM   4274 N N   . ASP B 1 191 ? 0.914   25.688  20.758 1.000 34.810 0  191 ASP B N   1 
ATOM   4275 C CA  . ASP B 1 191 ? 1.418   25.075  22.016 1.000 33.750 0  191 ASP B CA  1 
ATOM   4276 C C   . ASP B 1 191 ? 1.997   26.181  22.900 1.000 32.280 0  191 ASP B C   1 
ATOM   4277 O O   . ASP B 1 191 ? 1.859   26.087  24.139 1.000 31.100 0  191 ASP B O   1 
ATOM   4278 C CB  . ASP B 1 191 ? 2.435   23.981  21.735 1.000 33.620 0  191 ASP B CB  1 
ATOM   4279 C CG  . ASP B 1 191 ? 1.856   22.586  21.559 1.000 35.810 0  191 ASP B CG  1 
ATOM   4280 O OD1 . ASP B 1 191 ? 0.620   22.481  21.419 1.000 32.980 0  191 ASP B OD1 1 
ATOM   4281 O OD2 . ASP B 1 191 ? 2.645   21.619  21.562 1.000 35.380 -1 191 ASP B OD2 1 
ATOM   4282 N N   . ARG B 1 192 ? 2.620   27.189  22.282 1.000 30.030 0  192 ARG B N   1 
ATOM   4283 C CA  . ARG B 1 192 ? 3.218   28.261  23.066 1.000 31.060 0  192 ARG B CA  1 
ATOM   4284 C C   . ARG B 1 192 ? 2.167   28.998  23.885 1.000 30.050 0  192 ARG B C   1 
ATOM   4285 O O   . ARG B 1 192 ? 2.413   29.367  25.040 1.000 29.320 0  192 ARG B O   1 
ATOM   4286 C CB  . ARG B 1 192 ? 3.950   29.216  22.132 1.000 31.890 0  192 ARG B CB  1 
ATOM   4287 C CG  . ARG B 1 192 ? 5.050   28.536  21.344 1.000 28.990 0  192 ARG B CG  1 
ATOM   4288 C CD  . ARG B 1 192 ? 6.299   29.370  21.352 1.000 35.280 0  192 ARG B CD  1 
ATOM   4289 N NE  . ARG B 1 192 ? 7.340   28.800  22.197 1.000 37.540 0  192 ARG B NE  1 
ATOM   4290 C CZ  . ARG B 1 192 ? 8.428   29.456  22.579 1.000 35.740 0  192 ARG B CZ  1 
ATOM   4291 N NH1 . ARG B 1 192 ? 8.634   30.715  22.225 1.000 34.840 1  192 ARG B NH1 1 
ATOM   4292 N NH2 . ARG B 1 192 ? 9.324   28.838  23.344 1.000 33.510 0  192 ARG B NH2 1 
ATOM   4293 N N   . ALA B 1 193 ? 0.982   29.204  23.310 1.000 30.840 0  193 ALA B N   1 
ATOM   4294 C CA  . ALA B 1 193 ? -0.083  29.867  24.050 1.000 28.760 0  193 ALA B CA  1 
ATOM   4295 C C   . ALA B 1 193 ? -0.525  29.027  25.239 1.000 28.160 0  193 ALA B C   1 
ATOM   4296 O O   . ALA B 1 193 ? -0.794  29.564  26.320 1.000 28.640 0  193 ALA B O   1 
ATOM   4297 C CB  . ALA B 1 193 ? -1.262  30.157  23.123 1.000 28.650 0  193 ALA B CB  1 
ATOM   4298 N N   . LYS B 1 194 ? -0.578  27.704  25.070 1.000 28.950 0  194 LYS B N   1 
ATOM   4299 C CA  . LYS B 1 194 ? -0.944  26.833  26.182 1.000 29.110 0  194 LYS B CA  1 
ATOM   4300 C C   . LYS B 1 194 ? 0.127   26.829  27.271 1.000 27.370 0  194 LYS B C   1 
ATOM   4301 O O   . LYS B 1 194 ? -0.195  26.817  28.464 1.000 26.860 0  194 LYS B O   1 
ATOM   4302 C CB  . LYS B 1 194 ? -1.207  25.420  25.665 1.000 30.960 0  194 LYS B CB  1 
ATOM   4303 C CG  . LYS B 1 194 ? -2.224  25.379  24.533 1.000 33.140 0  194 LYS B CG  1 
ATOM   4304 C CD  . LYS B 1 194 ? -2.942  24.042  24.462 1.000 35.330 0  194 LYS B CD  1 
ATOM   4305 C CE  . LYS B 1 194 ? -3.647  23.874  23.130 1.000 35.540 0  194 LYS B CE  1 
ATOM   4306 N NZ  . LYS B 1 194 ? -3.995  25.195  22.535 1.000 44.140 1  194 LYS B NZ  1 
ATOM   4307 N N   . HIS B 1 195 ? 1.404   26.850  26.878 1.000 27.020 0  195 HIS B N   1 
ATOM   4308 C CA  . HIS B 1 195 ? 2.483   26.948  27.860 1.000 26.980 0  195 HIS B CA  1 
ATOM   4309 C C   . HIS B 1 195 ? 2.374   28.242  28.662 1.000 29.210 0  195 HIS B C   1 
ATOM   4310 O O   . HIS B 1 195 ? 2.452   28.235  29.901 1.000 29.500 0  195 HIS B O   1 
ATOM   4311 C CB  . HIS B 1 195 ? 3.836   26.858  27.151 1.000 29.770 0  195 HIS B CB  1 
ATOM   4312 C CG  . HIS B 1 195 ? 4.986   26.553  28.061 1.000 29.110 0  195 HIS B CG  1 
ATOM   4313 N ND1 . HIS B 1 195 ? 6.251   26.273  27.591 1.000 28.770 0  195 HIS B ND1 1 
ATOM   4314 C CD2 . HIS B 1 195 ? 5.065   26.487  29.412 1.000 30.030 0  195 HIS B CD2 1 
ATOM   4315 C CE1 . HIS B 1 195 ? 7.059   26.046  28.611 1.000 27.780 0  195 HIS B CE1 1 
ATOM   4316 N NE2 . HIS B 1 195 ? 6.363   26.169  29.728 1.000 29.440 0  195 HIS B NE2 1 
ATOM   4317 N N   . ARG B 1 196 ? 2.191   29.368  27.964 1.000 27.940 0  196 ARG B N   1 
ATOM   4318 C CA  . ARG B 1 196 ? 2.034   30.651  28.644 1.000 28.410 0  196 ARG B CA  1 
ATOM   4319 C C   . ARG B 1 196 ? 0.826   30.647  29.574 1.000 28.590 0  196 ARG B C   1 
ATOM   4320 O O   . ARG B 1 196 ? 0.890   31.179  30.689 1.000 28.730 0  196 ARG B O   1 
ATOM   4321 C CB  . ARG B 1 196 ? 1.916   31.779  27.619 1.000 26.400 0  196 ARG B CB  1 
ATOM   4322 C CG  . ARG B 1 196 ? 3.245   32.260  27.066 1.000 26.330 0  196 ARG B CG  1 
ATOM   4323 C CD  . ARG B 1 196 ? 3.067   33.524  26.252 1.000 26.860 0  196 ARG B CD  1 
ATOM   4324 N NE  . ARG B 1 196 ? 1.919   33.414  25.363 1.000 29.800 0  196 ARG B NE  1 
ATOM   4325 C CZ  . ARG B 1 196 ? 2.001   33.185  24.061 1.000 29.500 0  196 ARG B CZ  1 
ATOM   4326 N NH1 . ARG B 1 196 ? 3.169   33.061  23.454 1.000 26.510 1  196 ARG B NH1 1 
ATOM   4327 N NH2 . ARG B 1 196 ? 0.883   33.082  23.349 1.000 31.790 0  196 ARG B NH2 1 
ATOM   4328 N N   . ALA B 1 197 ? -0.287  30.051  29.132 1.000 27.340 0  197 ALA B N   1 
ATOM   4329 C CA  . ALA B 1 197 ? -1.493  30.043  29.955 1.000 26.570 0  197 ALA B CA  1 
ATOM   4330 C C   . ALA B 1 197 ? -1.303  29.200  31.210 1.000 28.130 0  197 ALA B C   1 
ATOM   4331 O O   . ALA B 1 197 ? -1.705  29.608  32.308 1.000 24.830 0  197 ALA B O   1 
ATOM   4332 C CB  . ALA B 1 197 ? -2.679  29.536  29.140 1.000 24.120 0  197 ALA B CB  1 
ATOM   4333 N N   . GLY B 1 198 ? -0.691  28.021  31.071 1.000 27.240 0  198 GLY B N   1 
ATOM   4334 C CA  . GLY B 1 198 ? -0.439  27.197  32.240 1.000 25.970 0  198 GLY B CA  1 
ATOM   4335 C C   . GLY B 1 198 ? 0.496   27.873  33.224 1.000 28.040 0  198 GLY B C   1 
ATOM   4336 O O   . GLY B 1 198 ? 0.324   27.761  34.443 1.000 28.620 0  198 GLY B O   1 
ATOM   4337 N N   . VAL B 1 199 ? 1.485   28.608  32.709 1.000 27.190 0  199 VAL B N   1 
ATOM   4338 C CA  . VAL B 1 199 ? 2.400   29.301  33.604 1.000 27.180 0  199 VAL B CA  1 
ATOM   4339 C C   . VAL B 1 199 ? 1.691   30.441  34.325 1.000 26.850 0  199 VAL B C   1 
ATOM   4340 O O   . VAL B 1 199 ? 1.895   30.654  35.528 1.000 28.380 0  199 VAL B O   1 
ATOM   4341 C CB  . VAL B 1 199 ? 3.630   29.794  32.826 1.000 27.780 0  199 VAL B CB  1 
ATOM   4342 C CG1 . VAL B 1 199 ? 4.458   30.716  33.699 1.000 25.970 0  199 VAL B CG1 1 
ATOM   4343 C CG2 . VAL B 1 199 ? 4.446   28.604  32.360 1.000 29.560 0  199 VAL B CG2 1 
ATOM   4344 N N   . LEU B 1 200 ? 0.856   31.196  33.607 1.000 25.120 0  200 LEU B N   1 
ATOM   4345 C CA  . LEU B 1 200 ? 0.040   32.208  34.268 1.000 26.900 0  200 LEU B CA  1 
ATOM   4346 C C   . LEU B 1 200 ? -0.813  31.588  35.367 1.000 28.190 0  200 LEU B C   1 
ATOM   4347 O O   . LEU B 1 200 ? -0.944  32.159  36.457 1.000 29.650 0  200 LEU B O   1 
ATOM   4348 C CB  . LEU B 1 200 ? -0.839  32.934  33.247 1.000 26.780 0  200 LEU B CB  1 
ATOM   4349 C CG  . LEU B 1 200 ? -0.240  34.167  32.566 1.000 29.950 0  200 LEU B CG  1 
ATOM   4350 C CD1 . LEU B 1 200 ? -1.349  35.107  32.122 1.000 29.120 0  200 LEU B CD1 1 
ATOM   4351 C CD2 . LEU B 1 200 ? 0.754   34.889  33.471 1.000 31.040 0  200 LEU B CD2 1 
ATOM   4352 N N   . LYS B 1 201 ? -1.389  30.413  35.104 1.000 24.130 0  201 LYS B N   1 
ATOM   4353 C CA  . LYS B 1 201 ? -2.205  29.740  36.113 1.000 26.070 0  201 LYS B CA  1 
ATOM   4354 C C   . LYS B 1 201 ? -1.381  29.395  37.348 1.000 27.070 0  201 LYS B C   1 
ATOM   4355 O O   . LYS B 1 201 ? -1.813  29.626  38.487 1.000 25.430 0  201 LYS B O   1 
ATOM   4356 C CB  . LYS B 1 201 ? -2.831  28.480  35.516 1.000 26.810 0  201 LYS B CB  1 
ATOM   4357 C CG  . LYS B 1 201 ? -4.114  28.036  36.191 1.000 27.450 0  201 LYS B CG  1 
ATOM   4358 C CD  . LYS B 1 201 ? -4.660  26.774  35.548 1.000 26.720 0  201 LYS B CD  1 
ATOM   4359 C CE  . LYS B 1 201 ? -6.068  26.476  36.033 1.000 29.650 0  201 LYS B CE  1 
ATOM   4360 N NZ  . LYS B 1 201 ? -6.261  25.021  36.284 1.000 35.690 1  201 LYS B NZ  1 
ATOM   4361 N N   . LEU B 1 202 ? -0.187  28.834  37.137 1.000 28.250 0  202 LEU B N   1 
ATOM   4362 C CA  . LEU B 1 202 ? 0.675   28.467  38.258 1.000 26.300 0  202 LEU B CA  1 
ATOM   4363 C C   . LEU B 1 202 ? 1.061   29.689  39.085 1.000 28.700 0  202 LEU B C   1 
ATOM   4364 O O   . LEU B 1 202 ? 1.015   29.658  40.321 1.000 30.970 0  202 LEU B O   1 
ATOM   4365 C CB  . LEU B 1 202 ? 1.921   27.752  37.741 1.000 27.130 0  202 LEU B CB  1 
ATOM   4366 C CG  . LEU B 1 202 ? 2.962   27.347  38.783 1.000 27.160 0  202 LEU B CG  1 
ATOM   4367 C CD1 . LEU B 1 202 ? 2.323   26.597  39.950 1.000 26.690 0  202 LEU B CD1 1 
ATOM   4368 C CD2 . LEU B 1 202 ? 4.037   26.510  38.126 1.000 27.170 0  202 LEU B CD2 1 
ATOM   4369 N N   . LEU B 1 203 ? 1.441   30.780  38.416 1.000 27.100 0  203 LEU B N   1 
ATOM   4370 C CA  . LEU B 1 203 ? 1.832   31.982  39.148 1.000 28.890 0  203 LEU B CA  1 
ATOM   4371 C C   . LEU B 1 203 ? 0.656   32.569  39.918 1.000 30.090 0  203 LEU B C   1 
ATOM   4372 O O   . LEU B 1 203 ? 0.813   33.010  41.064 1.000 28.880 0  203 LEU B O   1 
ATOM   4373 C CB  . LEU B 1 203 ? 2.415   33.024  38.192 1.000 30.970 0  203 LEU B CB  1 
ATOM   4374 C CG  . LEU B 1 203 ? 3.663   32.662  37.385 1.000 29.140 0  203 LEU B CG  1 
ATOM   4375 C CD1 . LEU B 1 203 ? 3.955   33.746  36.362 1.000 28.830 0  203 LEU B CD1 1 
ATOM   4376 C CD2 . LEU B 1 203 ? 4.856   32.457  38.299 1.000 26.760 0  203 LEU B CD2 1 
ATOM   4377 N N   . ALA B 1 204 ? -0.531  32.585  39.303 1.000 28.870 0  204 ALA B N   1 
ATOM   4378 C CA  . ALA B 1 204 ? -1.710  33.108  39.985 1.000 29.470 0  204 ALA B CA  1 
ATOM   4379 C C   . ALA B 1 204 ? -2.021  32.299  41.237 1.000 28.700 0  204 ALA B C   1 
ATOM   4380 O O   . ALA B 1 204 ? -2.279  32.863  42.306 1.000 28.700 0  204 ALA B O   1 
ATOM   4381 C CB  . ALA B 1 204 ? -2.908  33.119  39.037 1.000 26.340 0  204 ALA B CB  1 
ATOM   4382 N N   . GLU B 1 205 ? -1.998  30.968  41.125 1.000 28.700 0  205 GLU B N   1 
ATOM   4383 C CA  . GLU B 1 205 ? -2.298  30.148  42.295 1.000 28.260 0  205 GLU B CA  1 
ATOM   4384 C C   . GLU B 1 205 ? -1.235  30.315  43.373 1.000 29.870 0  205 GLU B C   1 
ATOM   4385 O O   . GLU B 1 205 ? -1.556  30.336  44.568 1.000 28.550 0  205 GLU B O   1 
ATOM   4386 C CB  . GLU B 1 205 ? -2.433  28.680  41.893 1.000 27.310 0  205 GLU B CB  1 
ATOM   4387 C CG  . GLU B 1 205 ? -3.057  27.799  42.966 1.000 31.220 0  205 GLU B CG  1 
ATOM   4388 C CD  . GLU B 1 205 ? -4.389  28.331  43.467 1.000 35.410 0  205 GLU B CD  1 
ATOM   4389 O OE1 . GLU B 1 205 ? -5.193  28.814  42.641 1.000 31.950 0  205 GLU B OE1 1 
ATOM   4390 O OE2 . GLU B 1 205 ? -4.631  28.264  44.693 1.000 36.030 -1 205 GLU B OE2 1 
ATOM   4391 N N   . LEU B 1 206 ? 0.032   30.461  42.974 1.000 30.890 0  206 LEU B N   1 
ATOM   4392 C CA  . LEU B 1 206 ? 1.096   30.630  43.958 1.000 29.420 0  206 LEU B CA  1 
ATOM   4393 C C   . LEU B 1 206 ? 0.959   31.952  44.704 1.000 32.780 0  206 LEU B C   1 
ATOM   4394 O O   . LEU B 1 206 ? 1.122   31.998  45.930 1.000 32.800 0  206 LEU B O   1 
ATOM   4395 C CB  . LEU B 1 206 ? 2.456   30.529  43.276 1.000 28.310 0  206 LEU B CB  1 
ATOM   4396 C CG  . LEU B 1 206 ? 2.848   29.086  42.963 1.000 30.540 0  206 LEU B CG  1 
ATOM   4397 C CD1 . LEU B 1 206 ? 4.178   29.039  42.235 1.000 28.420 0  206 LEU B CD1 1 
ATOM   4398 C CD2 . LEU B 1 206 ? 2.886   28.255  44.239 1.000 28.500 0  206 LEU B CD2 1 
ATOM   4399 N N   . LYS B 1 207 ? 0.658   33.038  43.988 1.000 32.120 0  207 LYS B N   1 
ATOM   4400 C CA  . LYS B 1 207 ? 0.429   34.309  44.669 1.000 32.020 0  207 LYS B CA  1 
ATOM   4401 C C   . LYS B 1 207 ? -0.831  34.270  45.524 1.000 30.280 0  207 LYS B C   1 
ATOM   4402 O O   . LYS B 1 207 ? -0.872  34.897  46.588 1.000 29.490 0  207 LYS B O   1 
ATOM   4403 C CB  . LYS B 1 207 ? 0.344   35.451  43.655 1.000 34.370 0  207 LYS B CB  1 
ATOM   4404 C CG  . LYS B 1 207 ? 1.663   36.176  43.406 1.000 34.660 0  207 LYS B CG  1 
ATOM   4405 C CD  . LYS B 1 207 ? 1.844   37.363  44.346 1.000 36.470 0  207 LYS B CD  1 
ATOM   4406 C CE  . LYS B 1 207 ? 3.290   37.841  44.355 1.000 36.310 0  207 LYS B CE  1 
ATOM   4407 N NZ  . LYS B 1 207 ? 3.883   37.850  45.722 1.000 36.030 1  207 LYS B NZ  1 
ATOM   4408 N N   . LYS B 1 208 ? -1.859  33.535  45.088 1.000 30.400 0  208 LYS B N   1 
ATOM   4409 C CA  . LYS B 1 208 ? -3.104  33.469  45.851 1.000 33.500 0  208 LYS B CA  1 
ATOM   4410 C C   . LYS B 1 208 ? -2.904  32.783  47.197 1.000 33.420 0  208 LYS B C   1 
ATOM   4411 O O   . LYS B 1 208 ? -3.474  33.208  48.210 1.000 31.170 0  208 LYS B O   1 
ATOM   4412 C CB  . LYS B 1 208 ? -4.177  32.743  45.039 1.000 33.620 0  208 LYS B CB  1 
ATOM   4413 C CG  . LYS B 1 208 ? -5.279  32.131  45.887 1.000 32.260 0  208 LYS B CG  1 
ATOM   4414 C CD  . LYS B 1 208 ? -6.251  31.327  45.042 1.000 35.640 0  208 LYS B CD  1 
ATOM   4415 C CE  . LYS B 1 208 ? -7.625  31.975  45.007 1.000 35.060 0  208 LYS B CE  1 
ATOM   4416 N NZ  . LYS B 1 208 ? -8.707  30.955  44.997 1.000 34.150 1  208 LYS B NZ  1 
ATOM   4417 N N   . ARG B 1 209 ? -2.090  31.730  47.232 1.000 30.950 0  209 ARG B N   1 
ATOM   4418 C CA  . ARG B 1 209 ? -1.894  30.950  48.447 1.000 29.970 0  209 ARG B CA  1 
ATOM   4419 C C   . ARG B 1 209 ? -0.943  31.612  49.432 1.000 30.540 0  209 ARG B C   1 
ATOM   4420 O O   . ARG B 1 209 ? -0.726  31.063  50.517 1.000 30.190 0  209 ARG B O   1 
ATOM   4421 C CB  . ARG B 1 209 ? -1.387  29.553  48.090 1.000 30.520 0  209 ARG B CB  1 
ATOM   4422 C CG  . ARG B 1 209 ? -2.414  28.731  47.338 1.000 33.530 0  209 ARG B CG  1 
ATOM   4423 C CD  . ARG B 1 209 ? -1.805  27.517  46.673 1.000 34.310 0  209 ARG B CD  1 
ATOM   4424 N NE  . ARG B 1 209 ? -2.818  26.506  46.398 1.000 36.680 0  209 ARG B NE  1 
ATOM   4425 C CZ  . ARG B 1 209 ? -2.736  25.240  46.783 1.000 37.800 0  209 ARG B CZ  1 
ATOM   4426 N NH1 . ARG B 1 209 ? -1.689  24.788  47.454 1.000 33.170 1  209 ARG B NH1 1 
ATOM   4427 N NH2 . ARG B 1 209 ? -3.726  24.403  46.480 1.000 36.010 0  209 ARG B NH2 1 
ATOM   4428 N N   . GLY B 1 210 ? -0.387  32.769  49.087 1.000 29.930 0  210 GLY B N   1 
ATOM   4429 C CA  . GLY B 1 210 ? 0.594   33.404  49.940 1.000 27.820 0  210 GLY B CA  1 
ATOM   4430 C C   . GLY B 1 210 ? 1.995   32.882  49.753 1.000 28.940 0  210 GLY B C   1 
ATOM   4431 O O   . GLY B 1 210 ? 2.857   33.138  50.599 1.000 29.400 0  210 GLY B O   1 
ATOM   4432 N N   . ALA B 1 211 ? 2.255   32.164  48.666 1.000 27.960 0  211 ALA B N   1 
ATOM   4433 C CA  . ALA B 1 211 ? 3.567   31.572  48.475 1.000 28.410 0  211 ALA B CA  1 
ATOM   4434 C C   . ALA B 1 211 ? 4.587   32.664  48.166 1.000 27.260 0  211 ALA B C   1 
ATOM   4435 O O   . ALA B 1 211 ? 4.279   33.618  47.446 1.000 28.990 0  211 ALA B O   1 
ATOM   4436 C CB  . ALA B 1 211 ? 3.541   30.541  47.346 1.000 28.900 0  211 ALA B CB  1 
ATOM   4437 N N   . PRO B 1 212 ? 5.794   32.566  48.711 1.000 26.350 0  212 PRO B N   1 
ATOM   4438 C CA  . PRO B 1 212 ? 6.826   33.598  48.496 1.000 25.030 0  212 PRO B CA  1 
ATOM   4439 C C   . PRO B 1 212 ? 7.566   33.412  47.177 1.000 24.850 0  212 PRO B C   1 
ATOM   4440 O O   . PRO B 1 212 ? 8.752   33.072  47.118 1.000 26.410 0  212 PRO B O   1 
ATOM   4441 C CB  . PRO B 1 212 ? 7.730   33.412  49.716 1.000 25.260 0  212 PRO B CB  1 
ATOM   4442 C CG  . PRO B 1 212 ? 7.610   31.962  50.052 1.000 25.960 0  212 PRO B CG  1 
ATOM   4443 C CD  . PRO B 1 212 ? 6.273   31.473  49.572 1.000 27.300 0  212 PRO B CD  1 
ATOM   4444 N N   . ILE B 1 213 ? 6.862   33.643  46.078 1.000 24.750 0  213 ILE B N   1 
ATOM   4445 C CA  . ILE B 1 213 ? 7.479   33.688  44.759 1.000 27.010 0  213 ILE B CA  1 
ATOM   4446 C C   . ILE B 1 213 ? 7.733   35.147  44.414 1.000 26.950 0  213 ILE B C   1 
ATOM   4447 O O   . ILE B 1 213 ? 6.830   35.988  44.527 1.000 25.370 0  213 ILE B O   1 
ATOM   4448 C CB  . ILE B 1 213 ? 6.603   33.004  43.696 1.000 24.480 0  213 ILE B CB  1 
ATOM   4449 C CG1 . ILE B 1 213 ? 7.144   33.310  42.301 1.000 24.380 0  213 ILE B CG1 1 
ATOM   4450 C CG2 . ILE B 1 213 ? 5.152   33.444  43.823 1.000 28.960 0  213 ILE B CG2 1 
ATOM   4451 C CD1 . ILE B 1 213 ? 6.873   32.225  41.305 1.000 26.560 0  213 ILE B CD1 1 
ATOM   4452 N N   . HIS B 1 214 ? 8.968   35.453  44.011 1.000 27.170 0  214 HIS B N   1 
ATOM   4453 C CA  . HIS B 1 214 ? 9.373   36.827  43.771 1.000 24.750 0  214 HIS B CA  1 
ATOM   4454 C C   . HIS B 1 214 ? 9.563   37.188  42.306 1.000 25.020 0  214 HIS B C   1 
ATOM   4455 O O   . HIS B 1 214 ? 9.506   38.376  41.979 1.000 26.780 0  214 HIS B O   1 
ATOM   4456 C CB  . HIS B 1 214 ? 10.668  37.132  44.531 1.000 24.840 0  214 HIS B CB  1 
ATOM   4457 C CG  . HIS B 1 214 ? 10.524  37.024  46.016 1.000 24.970 0  214 HIS B CG  1 
ATOM   4458 N ND1 . HIS B 1 214 ? 11.441  36.368  46.809 1.000 25.020 0  214 HIS B ND1 1 
ATOM   4459 C CD2 . HIS B 1 214 ? 9.565   37.483  46.853 1.000 25.090 0  214 HIS B CD2 1 
ATOM   4460 C CE1 . HIS B 1 214 ? 11.052  36.429  48.070 1.000 25.390 0  214 HIS B CE1 1 
ATOM   4461 N NE2 . HIS B 1 214 ? 9.916   37.100  48.124 1.000 26.490 0  214 HIS B NE2 1 
ATOM   4462 N N   . ALA B 1 215 ? 9.789   36.220  41.418 1.000 25.320 0  215 ALA B N   1 
ATOM   4463 C CA  . ALA B 1 215 ? 10.061  36.598  40.038 1.000 25.670 0  215 ALA B CA  1 
ATOM   4464 C C   . ALA B 1 215 ? 9.814   35.439  39.082 1.000 25.030 0  215 ALA B C   1 
ATOM   4465 O O   . ALA B 1 215 ? 9.799   34.264  39.469 1.000 25.570 0  215 ALA B O   1 
ATOM   4466 C CB  . ALA B 1 215 ? 11.497  37.107  39.884 1.000 25.190 0  215 ALA B CB  1 
ATOM   4467 N N   . LEU B 1 216 ? 9.631   35.805  37.815 1.000 24.740 0  216 LEU B N   1 
ATOM   4468 C CA  . LEU B 1 216 ? 9.558   34.863  36.708 1.000 24.810 0  216 LEU B CA  1 
ATOM   4469 C C   . LEU B 1 216 ? 10.850  34.929  35.906 1.000 26.480 0  216 LEU B C   1 
ATOM   4470 O O   . LEU B 1 216 ? 11.333  36.022  35.581 1.000 29.010 0  216 LEU B O   1 
ATOM   4471 C CB  . LEU B 1 216 ? 8.371   35.174  35.798 1.000 25.720 0  216 LEU B CB  1 
ATOM   4472 C CG  . LEU B 1 216 ? 8.244   34.347  34.517 1.000 26.360 0  216 LEU B CG  1 
ATOM   4473 C CD1 . LEU B 1 216 ? 8.297   32.852  34.797 1.000 25.170 0  216 LEU B CD1 1 
ATOM   4474 C CD2 . LEU B 1 216 ? 6.964   34.710  33.788 1.000 32.130 0  216 LEU B CD2 1 
ATOM   4475 N N   . GLY B 1 217 ? 11.399  33.762  35.584 1.000 26.910 0  217 GLY B N   1 
ATOM   4476 C CA  . GLY B 1 217 ? 12.577  33.677  34.752 1.000 24.840 0  217 GLY B CA  1 
ATOM   4477 C C   . GLY B 1 217 ? 12.242  33.218  33.350 1.000 25.790 0  217 GLY B C   1 
ATOM   4478 O O   . GLY B 1 217 ? 11.940  32.038  33.116 1.000 26.220 0  217 GLY B O   1 
ATOM   4479 N N   . LEU B 1 218 ? 12.268  34.169  32.416 1.000 26.350 0  218 LEU B N   1 
ATOM   4480 C CA  . LEU B 1 218 ? 12.111  33.912  30.989 1.000 26.350 0  218 LEU B CA  1 
ATOM   4481 C C   . LEU B 1 218 ? 13.449  33.400  30.473 1.000 27.500 0  218 LEU B C   1 
ATOM   4482 O O   . LEU B 1 218 ? 14.397  34.171  30.298 1.000 26.180 0  218 LEU B O   1 
ATOM   4483 C CB  . LEU B 1 218 ? 11.689  35.186  30.266 1.000 26.610 0  218 LEU B CB  1 
ATOM   4484 C CG  . LEU B 1 218 ? 10.770  36.125  31.055 1.000 25.390 0  218 LEU B CG  1 
ATOM   4485 C CD1 . LEU B 1 218 ? 10.679  37.494  30.399 1.000 25.160 0  218 LEU B CD1 1 
ATOM   4486 C CD2 . LEU B 1 218 ? 9.387   35.513  31.201 1.000 28.370 0  218 LEU B CD2 1 
ATOM   4487 N N   . GLN B 1 219 ? 13.536  32.085  30.250 1.000 27.510 0  219 GLN B N   1 
ATOM   4488 C CA  . GLN B 1 219 ? 14.773  31.491  29.748 1.000 24.430 0  219 GLN B CA  1 
ATOM   4489 C C   . GLN B 1 219 ? 15.219  32.143  28.447 1.000 24.570 0  219 GLN B C   1 
ATOM   4490 O O   . GLN B 1 219 ? 16.420  32.311  28.211 1.000 24.710 0  219 GLN B O   1 
ATOM   4491 C CB  . GLN B 1 219 ? 14.593  29.987  29.564 1.000 24.370 0  219 GLN B CB  1 
ATOM   4492 C CG  . GLN B 1 219 ? 14.424  29.242  30.871 1.000 24.270 0  219 GLN B CG  1 
ATOM   4493 C CD  . GLN B 1 219 ? 14.419  27.741  30.690 1.000 24.240 0  219 GLN B CD  1 
ATOM   4494 O OE1 . GLN B 1 219 ? 14.595  27.236  29.581 1.000 24.300 0  219 GLN B OE1 1 
ATOM   4495 N NE2 . GLN B 1 219 ? 14.211  27.017  31.783 1.000 24.180 0  219 GLN B NE2 1 
ATOM   4496 N N   . SER B 1 220 ? 14.267  32.508  27.588 1.000 26.640 0  220 SER B N   1 
ATOM   4497 C CA  . SER B 1 220 ? 14.546  33.263  26.366 1.000 25.450 0  220 SER B CA  1 
ATOM   4498 C C   . SER B 1 220 ? 15.479  32.494  25.432 1.000 24.840 0  220 SER B C   1 
ATOM   4499 O O   . SER B 1 220 ? 16.495  33.011  24.966 1.000 26.690 0  220 SER B O   1 
ATOM   4500 C CB  . SER B 1 220 ? 15.116  34.649  26.689 1.000 25.430 0  220 SER B CB  1 
ATOM   4501 O OG  . SER B 1 220 ? 14.212  35.415  27.462 1.000 27.150 0  220 SER B OG  1 
ATOM   4502 N N   . HIS B 1 221 ? 15.125  31.239  25.156 1.000 24.770 0  221 HIS B N   1 
ATOM   4503 C CA  . HIS B 1 221 ? 15.809  30.465  24.123 1.000 25.630 0  221 HIS B CA  1 
ATOM   4504 C C   . HIS B 1 221 ? 15.063  30.703  22.816 1.000 24.980 0  221 HIS B C   1 
ATOM   4505 O O   . HIS B 1 221 ? 14.278  29.879  22.346 1.000 28.430 0  221 HIS B O   1 
ATOM   4506 C CB  . HIS B 1 221 ? 15.860  28.988  24.489 1.000 27.630 0  221 HIS B CB  1 
ATOM   4507 C CG  . HIS B 1 221 ? 16.773  28.677  25.632 1.000 24.820 0  221 HIS B CG  1 
ATOM   4508 N ND1 . HIS B 1 221 ? 18.145  28.736  25.526 1.000 25.010 0  221 HIS B ND1 1 
ATOM   4509 C CD2 . HIS B 1 221 ? 16.509  28.302  26.905 1.000 24.680 0  221 HIS B CD2 1 
ATOM   4510 C CE1 . HIS B 1 221 ? 18.686  28.409  26.687 1.000 24.970 0  221 HIS B CE1 1 
ATOM   4511 N NE2 . HIS B 1 221 ? 17.715  28.141  27.539 1.000 24.780 0  221 HIS B NE2 1 
ATOM   4512 N N   . ILE B 1 222 ? 15.327  31.859  22.217 1.000 25.120 0  222 ILE B N   1 
ATOM   4513 C CA  . ILE B 1 222 ? 14.489  32.343  21.128 1.000 29.420 0  222 ILE B CA  1 
ATOM   4514 C C   . ILE B 1 222 ? 14.930  31.729  19.802 1.000 29.460 0  222 ILE B C   1 
ATOM   4515 O O   . ILE B 1 222 ? 16.058  31.256  19.641 1.000 29.560 0  222 ILE B O   1 
ATOM   4516 C CB  . ILE B 1 222 ? 14.507  33.881  21.069 1.000 28.260 0  222 ILE B CB  1 
ATOM   4517 C CG1 . ILE B 1 222 ? 15.798  34.381  20.425 1.000 27.200 0  222 ILE B CG1 1 
ATOM   4518 C CG2 . ILE B 1 222 ? 14.357  34.474  22.462 1.000 26.600 0  222 ILE B CG2 1 
ATOM   4519 C CD1 . ILE B 1 222 ? 15.816  35.869  20.208 1.000 28.250 0  222 ILE B CD1 1 
ATOM   4520 N N   . SER B 1 223 ? 14.005  31.719  18.844 1.000 30.370 0  223 SER B N   1 
ATOM   4521 C CA  . SER B 1 223 ? 14.280  31.253  17.489 1.000 33.390 0  223 SER B CA  1 
ATOM   4522 C C   . SER B 1 223 ? 13.447  32.087  16.519 1.000 35.700 0  223 SER B C   1 
ATOM   4523 O O   . SER B 1 223 ? 12.869  33.112  16.895 1.000 38.040 0  223 SER B O   1 
ATOM   4524 C CB  . SER B 1 223 ? 13.990  29.752  17.354 1.000 31.700 0  223 SER B CB  1 
ATOM   4525 O OG  . SER B 1 223 ? 12.739  29.417  17.929 1.000 31.510 0  223 SER B OG  1 
ATOM   4526 N N   . ALA B 1 224 ? 13.380  31.643  15.261 1.000 33.530 0  224 ALA B N   1 
ATOM   4527 C CA  . ALA B 1 224 ? 12.676  32.410  14.239 1.000 32.470 0  224 ALA B CA  1 
ATOM   4528 C C   . ALA B 1 224 ? 11.162  32.355  14.412 1.000 36.870 0  224 ALA B C   1 
ATOM   4529 O O   . ALA B 1 224 ? 10.461  33.242  13.912 1.000 39.400 0  224 ALA B O   1 
ATOM   4530 C CB  . ALA B 1 224 ? 13.058  31.914  12.845 1.000 31.760 0  224 ALA B CB  1 
ATOM   4531 N N   . GLY B 1 225 ? 10.644  31.350  15.112 1.000 34.320 0  225 GLY B N   1 
ATOM   4532 C CA  . GLY B 1 225 ? 9.228   31.285  15.403 1.000 37.330 0  225 GLY B CA  1 
ATOM   4533 C C   . GLY B 1 225 ? 8.775   32.166  16.542 1.000 39.910 0  225 GLY B C   1 
ATOM   4534 O O   . GLY B 1 225 ? 7.590   32.166  16.887 1.000 35.860 0  225 GLY B O   1 
ATOM   4535 N N   . ASP B 1 226 ? 9.692   32.927  17.135 1.000 38.030 0  226 ASP B N   1 
ATOM   4536 C CA  . ASP B 1 226 ? 9.361   33.938  18.128 1.000 38.750 0  226 ASP B CA  1 
ATOM   4537 C C   . ASP B 1 226 ? 9.351   35.333  17.528 1.000 38.760 0  226 ASP B C   1 
ATOM   4538 O O   . ASP B 1 226 ? 9.356   36.321  18.270 1.000 39.050 0  226 ASP B O   1 
ATOM   4539 C CB  . ASP B 1 226 ? 10.341  33.879  19.302 1.000 34.900 0  226 ASP B CB  1 
ATOM   4540 C CG  . ASP B 1 226 ? 10.284  32.561  20.047 1.000 34.110 0  226 ASP B CG  1 
ATOM   4541 O OD1 . ASP B 1 226 ? 9.545   31.652  19.611 1.000 36.980 0  226 ASP B OD1 1 
ATOM   4542 O OD2 . ASP B 1 226 ? 10.986  32.431  21.069 1.000 34.350 -1 226 ASP B OD2 1 
ATOM   4543 N N   . MET B 1 227 ? 9.334   35.428  16.200 1.000 40.330 0  227 MET B N   1 
ATOM   4544 C CA  . MET B 1 227 ? 9.297   36.720  15.533 1.000 38.030 0  227 MET B CA  1 
ATOM   4545 C C   . MET B 1 227 ? 8.022   37.463  15.912 1.000 41.050 0  227 MET B C   1 
ATOM   4546 O O   . MET B 1 227 ? 6.927   36.893  15.928 1.000 38.590 0  227 MET B O   1 
ATOM   4547 C CB  . MET B 1 227 ? 9.368   36.523  14.018 1.000 41.160 0  227 MET B CB  1 
ATOM   4548 C CG  . MET B 1 227 ? 9.931   37.698  13.230 1.000 43.690 0  227 MET B CG  1 
ATOM   4549 S SD  . MET B 1 227 ? 11.376  38.459  13.998 1.000 44.830 0  227 MET B SD  1 
ATOM   4550 C CE  . MET B 1 227 ? 10.932  40.187  13.887 1.000 40.750 0  227 MET B CE  1 
ATOM   4551 N N   . MET B 1 228 ? 8.175   38.750  16.222 1.000 40.370 0  228 MET B N   1 
ATOM   4552 C CA  . MET B 1 228 ? 7.085   39.557  16.738 1.000 38.240 0  228 MET B CA  1 
ATOM   4553 C C   . MET B 1 228 ? 6.780   40.773  15.882 1.000 38.300 0  228 MET B C   1 
ATOM   4554 O O   . MET B 1 228 ? 5.655   41.280  15.943 1.000 39.050 0  228 MET B O   1 
ATOM   4555 C CB  . MET B 1 228 ? 7.404   40.027  18.167 1.000 36.680 0  228 MET B CB  1 
ATOM   4556 C CG  . MET B 1 228 ? 7.158   38.985  19.244 1.000 34.050 0  228 MET B CG  1 
ATOM   4557 S SD  . MET B 1 228 ? 7.075   39.721  20.885 1.000 32.390 0  228 MET B SD  1 
ATOM   4558 C CE  . MET B 1 228 ? 8.807   39.732  21.333 1.000 30.750 0  228 MET B CE  1 
ATOM   4559 N N   . SER B 1 229 ? 7.733   41.243  15.086 1.000 41.490 0  229 SER B N   1 
ATOM   4560 C CA  . SER B 1 229 ? 7.524   42.383  14.207 1.000 44.220 0  229 SER B CA  1 
ATOM   4561 C C   . SER B 1 229 ? 7.001   41.919  12.849 1.000 41.230 0  229 SER B C   1 
ATOM   4562 O O   . SER B 1 229 ? 7.216   40.782  12.420 1.000 37.090 0  229 SER B O   1 
ATOM   4563 C CB  . SER B 1 229 ? 8.814   43.187  14.032 1.000 42.070 0  229 SER B CB  1 
ATOM   4564 O OG  . SER B 1 229 ? 9.515   42.785  12.869 1.000 47.360 0  229 SER B OG  1 
ATOM   4565 N N   . GLY B 1 230 ? 6.304   42.829  12.176 1.000 43.320 0  230 GLY B N   1 
ATOM   4566 C CA  . GLY B 1 230 ? 5.622   42.532  10.940 1.000 40.880 0  230 GLY B CA  1 
ATOM   4567 C C   . GLY B 1 230 ? 4.130   42.411  11.172 1.000 39.470 0  230 GLY B C   1 
ATOM   4568 O O   . GLY B 1 230 ? 3.676   41.997  12.244 1.000 39.280 0  230 GLY B O   1 
ATOM   4569 N N   . PRO B 1 231 ? 3.337   42.794  10.168 1.000 38.520 0  231 PRO B N   1 
ATOM   4570 C CA  . PRO B 1 231 ? 1.873   42.724  10.332 1.000 38.350 0  231 PRO B CA  1 
ATOM   4571 C C   . PRO B 1 231 ? 1.352   41.341  10.688 1.000 39.040 0  231 PRO B C   1 
ATOM   4572 O O   . PRO B 1 231 ? 0.480   41.221  11.560 1.000 37.470 0  231 PRO B O   1 
ATOM   4573 C CB  . PRO B 1 231 ? 1.356   43.199  8.966  1.000 37.130 0  231 PRO B CB  1 
ATOM   4574 C CG  . PRO B 1 231 ? 2.447   44.092  8.450  1.000 35.540 0  231 PRO B CG  1 
ATOM   4575 C CD  . PRO B 1 231 ? 3.727   43.452  8.909  1.000 37.410 0  231 PRO B CD  1 
ATOM   4576 N N   . ALA B 1 232 ? 1.866   40.289  10.045 1.000 37.800 0  232 ALA B N   1 
ATOM   4577 C CA  . ALA B 1 232 ? 1.376   38.937  10.303 1.000 39.140 0  232 ALA B CA  1 
ATOM   4578 C C   . ALA B 1 232 ? 1.607   38.480  11.741 1.000 40.080 0  232 ALA B C   1 
ATOM   4579 O O   . ALA B 1 232 ? 0.926   37.555  12.200 1.000 36.250 0  232 ALA B O   1 
ATOM   4580 C CB  . ALA B 1 232 ? 2.029   37.951  9.332  1.000 36.000 0  232 ALA B CB  1 
ATOM   4581 N N   . ASN B 1 233 ? 2.531   39.107  12.468 1.000 38.730 0  233 ASN B N   1 
ATOM   4582 C CA  . ASN B 1 233 ? 2.900   38.654  13.803 1.000 38.660 0  233 ASN B CA  1 
ATOM   4583 C C   . ASN B 1 233 ? 2.360   39.554  14.905 1.000 37.370 0  233 ASN B C   1 
ATOM   4584 O O   . ASN B 1 233 ? 2.751   39.391  16.069 1.000 38.680 0  233 ASN B O   1 
ATOM   4585 C CB  . ASN B 1 233 ? 4.423   38.559  13.923 1.000 41.100 0  233 ASN B CB  1 
ATOM   4586 C CG  . ASN B 1 233 ? 5.031   37.657  12.875 1.000 42.130 0  233 ASN B CG  1 
ATOM   4587 O OD1 . ASN B 1 233 ? 4.347   36.811  12.296 1.000 39.360 0  233 ASN B OD1 1 
ATOM   4588 N ND2 . ASN B 1 233 ? 6.323   37.837  12.617 1.000 42.060 0  233 ASN B ND2 1 
ATOM   4589 N N   . ALA B 1 234 ? 1.428   40.454  14.579 1.000 37.010 0  234 ALA B N   1 
ATOM   4590 C CA  . ALA B 1 234 ? 0.910   41.388  15.571 1.000 35.760 0  234 ALA B CA  1 
ATOM   4591 C C   . ALA B 1 234 ? 0.404   40.642  16.797 1.000 35.620 0  234 ALA B C   1 
ATOM   4592 O O   . ALA B 1 234 ? 0.777   40.962  17.933 1.000 35.350 0  234 ALA B O   1 
ATOM   4593 C CB  . ALA B 1 234 ? -0.199  42.242  14.954 1.000 34.170 0  234 ALA B CB  1 
ATOM   4594 N N   . ALA B 1 235 ? -0.400  39.598  16.575 1.000 36.030 0  235 ALA B N   1 
ATOM   4595 C CA  . ALA B 1 235 ? -0.959  38.850  17.694 1.000 37.340 0  235 ALA B CA  1 
ATOM   4596 C C   . ALA B 1 235 ? 0.147   38.233  18.536 1.000 35.690 0  235 ALA B C   1 
ATOM   4597 O O   . ALA B 1 235 ? 0.133   38.347  19.771 1.000 33.630 0  235 ALA B O   1 
ATOM   4598 C CB  . ALA B 1 235 ? -1.915  37.772  17.183 1.000 36.050 0  235 ALA B CB  1 
ATOM   4599 N N   . VAL B 1 236 ? 1.157   37.644  17.878 1.000 34.680 0  236 VAL B N   1 
ATOM   4600 C CA  . VAL B 1 236 ? 2.280   37.063  18.608 1.000 33.330 0  236 VAL B CA  1 
ATOM   4601 C C   . VAL B 1 236 ? 2.884   38.111  19.524 1.000 33.590 0  236 VAL B C   1 
ATOM   4602 O O   . VAL B 1 236 ? 3.206   37.839  20.688 1.000 32.120 0  236 VAL B O   1 
ATOM   4603 C CB  . VAL B 1 236 ? 3.327   36.496  17.629 1.000 34.710 0  236 VAL B CB  1 
ATOM   4604 C CG1 . VAL B 1 236 ? 4.699   36.449  18.284 1.000 34.530 0  236 VAL B CG1 1 
ATOM   4605 C CG2 . VAL B 1 236 ? 2.923   35.114  17.160 1.000 32.950 0  236 VAL B CG2 1 
ATOM   4606 N N   . LEU B 1 237 ? 3.012   39.339  19.023 1.000 33.050 0  237 LEU B N   1 
ATOM   4607 C CA  . LEU B 1 237 ? 3.520   40.415  19.858 1.000 33.370 0  237 LEU B CA  1 
ATOM   4608 C C   . LEU B 1 237 ? 2.520   40.752  20.955 1.000 32.640 0  237 LEU B C   1 
ATOM   4609 O O   . LEU B 1 237 ? 2.847   40.687  22.149 1.000 32.870 0  237 LEU B O   1 
ATOM   4610 C CB  . LEU B 1 237 ? 3.810   41.640  18.991 1.000 33.780 0  237 LEU B CB  1 
ATOM   4611 C CG  . LEU B 1 237 ? 4.102   43.001  19.619 1.000 32.750 0  237 LEU B CG  1 
ATOM   4612 C CD1 . LEU B 1 237 ? 5.085   42.897  20.779 1.000 34.810 0  237 LEU B CD1 1 
ATOM   4613 C CD2 . LEU B 1 237 ? 4.623   43.942  18.553 1.000 30.440 0  237 LEU B CD2 1 
ATOM   4614 N N   . ARG B 1 238 ? 1.267   41.003  20.562 1.000 32.190 0  238 ARG B N   1 
ATOM   4615 C CA  . ARG B 1 238 ? 0.249   41.429  21.516 1.000 32.600 0  238 ARG B CA  1 
ATOM   4616 C C   . ARG B 1 238 ? 0.171   40.475  22.695 1.000 31.060 0  238 ARG B C   1 
ATOM   4617 O O   . ARG B 1 238 ? 0.377   40.874  23.849 1.000 31.750 0  238 ARG B O   1 
ATOM   4618 C CB  . ARG B 1 238 ? -1.103  41.523  20.808 1.000 34.870 0  238 ARG B CB  1 
ATOM   4619 C CG  . ARG B 1 238 ? -2.282  41.822  21.719 1.000 34.940 0  238 ARG B CG  1 
ATOM   4620 C CD  . ARG B 1 238 ? -3.573  42.098  20.941 1.000 37.040 0  238 ARG B CD  1 
ATOM   4621 N NE  . ARG B 1 238 ? -3.582  41.547  19.588 1.000 40.110 0  238 ARG B NE  1 
ATOM   4622 C CZ  . ARG B 1 238 ? -3.208  42.207  18.499 1.000 41.070 0  238 ARG B CZ  1 
ATOM   4623 N NH1 . ARG B 1 238 ? -2.770  43.455  18.563 1.000 39.460 1  238 ARG B NH1 1 
ATOM   4624 N NH2 . ARG B 1 238 ? -3.264  41.596  17.319 1.000 40.570 0  238 ARG B NH2 1 
ATOM   4625 N N   . GLU B 1 239 ? -0.003  39.183  22.409 1.000 29.030 0  239 GLU B N   1 
ATOM   4626 C CA  . GLU B 1 239 ? -0.189  38.226  23.487 1.000 28.170 0  239 GLU B CA  1 
ATOM   4627 C C   . GLU B 1 239 ? 1.044   38.172  24.372 1.000 29.510 0  239 GLU B C   1 
ATOM   4628 O O   . GLU B 1 239 ? 0.925   38.178  25.605 1.000 29.790 0  239 GLU B O   1 
ATOM   4629 C CB  . GLU B 1 239 ? -0.521  36.846  22.920 1.000 26.880 0  239 GLU B CB  1 
ATOM   4630 C CG  . GLU B 1 239 ? -1.842  36.795  22.173 1.000 26.930 0  239 GLU B CG  1 
ATOM   4631 C CD  . GLU B 1 239 ? -2.990  37.382  22.976 1.000 28.740 0  239 GLU B CD  1 
ATOM   4632 O OE1 . GLU B 1 239 ? -3.106  37.063  24.178 1.000 30.860 0  239 GLU B OE1 1 
ATOM   4633 O OE2 . GLU B 1 239 ? -3.772  38.172  22.408 1.000 30.540 -1 239 GLU B OE2 1 
ATOM   4634 N N   . TRP B 1 240 ? 2.238   38.215  23.767 1.000 28.350 0  240 TRP B N   1 
ATOM   4635 C CA  . TRP B 1 240 ? 3.447   38.231  24.577 1.000 24.920 0  240 TRP B CA  1 
ATOM   4636 C C   . TRP B 1 240 ? 3.425   39.423  25.513 1.000 26.790 0  240 TRP B C   1 
ATOM   4637 O O   . TRP B 1 240 ? 3.539   39.268  26.736 1.000 27.160 0  240 TRP B O   1 
ATOM   4638 C CB  . TRP B 1 240 ? 4.688   38.263  23.682 1.000 29.230 0  240 TRP B CB  1 
ATOM   4639 C CG  . TRP B 1 240 ? 6.020   38.285  24.406 1.000 27.790 0  240 TRP B CG  1 
ATOM   4640 C CD1 . TRP B 1 240 ? 7.020   39.205  24.249 1.000 28.830 0  240 TRP B CD1 1 
ATOM   4641 C CD2 . TRP B 1 240 ? 6.504   37.335  25.369 1.000 26.930 0  240 TRP B CD2 1 
ATOM   4642 N NE1 . TRP B 1 240 ? 8.087   38.893  25.057 1.000 27.220 0  240 TRP B NE1 1 
ATOM   4643 C CE2 . TRP B 1 240 ? 7.797   37.750  25.754 1.000 28.660 0  240 TRP B CE2 1 
ATOM   4644 C CE3 . TRP B 1 240 ? 5.970   36.179  25.946 1.000 26.060 0  240 TRP B CE3 1 
ATOM   4645 C CZ2 . TRP B 1 240 ? 8.561   37.052  26.688 1.000 26.630 0  240 TRP B CZ2 1 
ATOM   4646 C CZ3 . TRP B 1 240 ? 6.730   35.489  26.876 1.000 27.230 0  240 TRP B CZ3 1 
ATOM   4647 C CH2 . TRP B 1 240 ? 8.012   35.926  27.235 1.000 26.530 0  240 TRP B CH2 1 
ATOM   4648 N N   . ARG B 1 241 ? 3.146   40.609  24.968 1.000 27.200 0  241 ARG B N   1 
ATOM   4649 C CA  . ARG B 1 241 ? 3.048   41.780  25.824 1.000 28.020 0  241 ARG B CA  1 
ATOM   4650 C C   . ARG B 1 241 ? 1.984   41.562  26.884 1.000 31.180 0  241 ARG B C   1 
ATOM   4651 O O   . ARG B 1 241 ? 2.248   41.723  28.085 1.000 30.250 0  241 ARG B O   1 
ATOM   4652 C CB  . ARG B 1 241 ? 2.742   43.024  24.989 1.000 30.580 0  241 ARG B CB  1 
ATOM   4653 C CG  . ARG B 1 241 ? 3.977   43.671  24.390 1.000 32.660 0  241 ARG B CG  1 
ATOM   4654 C CD  . ARG B 1 241 ? 3.788   45.163  24.224 1.000 34.810 0  241 ARG B CD  1 
ATOM   4655 N NE  . ARG B 1 241 ? 4.363   45.900  25.342 1.000 38.440 0  241 ARG B NE  1 
ATOM   4656 C CZ  . ARG B 1 241 ? 5.569   46.450  25.337 1.000 37.330 0  241 ARG B CZ  1 
ATOM   4657 N NH1 . ARG B 1 241 ? 6.352   46.390  24.273 1.000 34.770 1  241 ARG B NH1 1 
ATOM   4658 N NH2 . ARG B 1 241 ? 5.994   47.090  26.422 1.000 38.100 0  241 ARG B NH2 1 
ATOM   4659 N N   . LYS B 1 242 ? 0.818   41.047  26.471 1.000 29.010 0  242 LYS B N   1 
ATOM   4660 C CA  . LYS B 1 242 ? -0.236  40.805  27.444 1.000 29.740 0  242 LYS B CA  1 
ATOM   4661 C C   . LYS B 1 242 ? 0.260   39.858  28.518 1.000 29.740 0  242 LYS B C   1 
ATOM   4662 O O   . LYS B 1 242 ? 0.167   40.160  29.714 1.000 30.840 0  242 LYS B O   1 
ATOM   4663 C CB  . LYS B 1 242 ? -1.493  40.250  26.770 1.000 33.130 0  242 LYS B CB  1 
ATOM   4664 C CG  . LYS B 1 242 ? -2.715  40.278  27.691 1.000 36.610 0  242 LYS B CG  1 
ATOM   4665 C CD  . LYS B 1 242 ? -3.696  39.140  27.422 1.000 37.130 0  242 LYS B CD  1 
ATOM   4666 C CE  . LYS B 1 242 ? -5.019  39.665  26.876 1.000 38.890 0  242 LYS B CE  1 
ATOM   4667 N NZ  . LYS B 1 242 ? -6.197  39.085  27.589 1.000 40.400 1  242 LYS B NZ  1 
ATOM   4668 N N   . PHE B 1 243 ? 0.916   38.771  28.100 1.000 29.200 0  243 PHE B N   1 
ATOM   4669 C CA  . PHE B 1 243 ? 1.454   37.829  29.069 1.000 28.900 0  243 PHE B CA  1 
ATOM   4670 C C   . PHE B 1 243 ? 2.341   38.561  30.059 1.000 29.350 0  243 PHE B C   1 
ATOM   4671 O O   . PHE B 1 243 ? 2.067   38.578  31.268 1.000 29.430 0  243 PHE B O   1 
ATOM   4672 C CB  . PHE B 1 243 ? 2.233   36.720  28.356 1.000 28.300 0  243 PHE B CB  1 
ATOM   4673 C CG  . PHE B 1 243 ? 3.047   35.852  29.281 1.000 27.810 0  243 PHE B CG  1 
ATOM   4674 C CD1 . PHE B 1 243 ? 2.446   34.841  30.010 1.000 28.690 0  243 PHE B CD1 1 
ATOM   4675 C CD2 . PHE B 1 243 ? 4.414   36.044  29.418 1.000 27.550 0  243 PHE B CD2 1 
ATOM   4676 C CE1 . PHE B 1 243 ? 3.189   34.040  30.858 1.000 27.220 0  243 PHE B CE1 1 
ATOM   4677 C CE2 . PHE B 1 243 ? 5.161   35.247  30.266 1.000 25.650 0  243 PHE B CE2 1 
ATOM   4678 C CZ  . PHE B 1 243 ? 4.547   34.244  30.986 1.000 25.950 0  243 PHE B CZ  1 
ATOM   4679 N N   . LEU B 1 244 ? 3.341   39.279  29.540 1.000 25.570 0  244 LEU B N   1 
ATOM   4680 C CA  . LEU B 1 244 ? 4.273   39.940  30.441 1.000 26.570 0  244 LEU B CA  1 
ATOM   4681 C C   . LEU B 1 244 ? 3.537   40.932  31.326 1.000 28.920 0  244 LEU B C   1 
ATOM   4682 O O   . LEU B 1 244 ? 3.752   40.965  32.547 1.000 30.840 0  244 LEU B O   1 
ATOM   4683 C CB  . LEU B 1 244 ? 5.393   40.612  29.644 1.000 27.820 0  244 LEU B CB  1 
ATOM   4684 C CG  . LEU B 1 244 ? 6.437   39.650  29.053 1.000 28.290 0  244 LEU B CG  1 
ATOM   4685 C CD1 . LEU B 1 244 ? 7.362   40.347  28.063 1.000 26.120 0  244 LEU B CD1 1 
ATOM   4686 C CD2 . LEU B 1 244 ? 7.246   38.965  30.151 1.000 25.960 0  244 LEU B CD2 1 
ATOM   4687 N N   . ASP B 1 245 ? 2.559   41.641  30.755 1.000 28.720 0  245 ASP B N   1 
ATOM   4688 C CA  . ASP B 1 245 ? 1.793   42.598  31.543 1.000 29.260 0  245 ASP B CA  1 
ATOM   4689 C C   . ASP B 1 245 ? 1.184   41.919  32.760 1.000 31.280 0  245 ASP B C   1 
ATOM   4690 O O   . ASP B 1 245 ? 1.432   42.328  33.904 1.000 32.010 0  245 ASP B O   1 
ATOM   4691 C CB  . ASP B 1 245 ? 0.704   43.233  30.680 1.000 28.950 0  245 ASP B CB  1 
ATOM   4692 C CG  . ASP B 1 245 ? 1.228   44.351  29.801 1.000 28.650 0  245 ASP B CG  1 
ATOM   4693 O OD1 . ASP B 1 245 ? 2.436   44.656  29.879 1.000 26.920 0  245 ASP B OD1 1 
ATOM   4694 O OD2 . ASP B 1 245 ? 0.430   44.917  29.026 1.000 28.510 -1 245 ASP B OD2 1 
ATOM   4695 N N   . GLU B 1 246 ? 0.475   40.807  32.538 1.000 28.630 0  246 GLU B N   1 
ATOM   4696 C CA  . GLU B 1 246 ? -0.192  40.149  33.653 1.000 30.480 0  246 GLU B CA  1 
ATOM   4697 C C   . GLU B 1 246 ? 0.813   39.690  34.697 1.000 31.750 0  246 GLU B C   1 
ATOM   4698 O O   . GLU B 1 246 ? 0.547   39.786  35.902 1.000 29.850 0  246 GLU B O   1 
ATOM   4699 C CB  . GLU B 1 246 ? -1.068  38.994  33.166 1.000 32.590 0  246 GLU B CB  1 
ATOM   4700 C CG  . GLU B 1 246 ? -1.767  39.275  31.850 1.000 36.470 0  246 GLU B CG  1 
ATOM   4701 C CD  . GLU B 1 246 ? -3.182  38.724  31.809 1.000 43.710 0  246 GLU B CD  1 
ATOM   4702 O OE1 . GLU B 1 246 ? -3.471  37.855  30.956 1.000 40.120 0  246 GLU B OE1 1 
ATOM   4703 O OE2 . GLU B 1 246 ? -4.008  39.178  32.632 1.000 47.780 -1 246 GLU B OE2 1 
ATOM   4704 N N   . VAL B 1 247 ? 1.986   39.216  34.261 1.000 31.590 0  247 VAL B N   1 
ATOM   4705 C CA  . VAL B 1 247 ? 2.988   38.788  35.230 1.000 30.450 0  247 VAL B CA  1 
ATOM   4706 C C   . VAL B 1 247 ? 3.348   39.955  36.140 1.000 31.180 0  247 VAL B C   1 
ATOM   4707 O O   . VAL B 1 247 ? 3.278   39.852  37.372 1.000 32.660 0  247 VAL B O   1 
ATOM   4708 C CB  . VAL B 1 247 ? 4.222   38.210  34.517 1.000 33.030 0  247 VAL B CB  1 
ATOM   4709 C CG1 . VAL B 1 247 ? 5.465   38.344  35.393 1.000 32.000 0  247 VAL B CG1 1 
ATOM   4710 C CG2 . VAL B 1 247 ? 3.980   36.753  34.150 1.000 31.280 0  247 VAL B CG2 1 
ATOM   4711 N N   . THR B 1 248 ? 3.656   41.111  35.544 1.000 31.340 0  248 THR B N   1 
ATOM   4712 C CA  . THR B 1 248 ? 4.007   42.260  36.365 1.000 31.150 0  248 THR B CA  1 
ATOM   4713 C C   . THR B 1 248 ? 2.802   42.781  37.129 1.000 29.770 0  248 THR B C   1 
ATOM   4714 O O   . THR B 1 248 ? 2.973   43.515  38.108 1.000 33.500 0  248 THR B O   1 
ATOM   4715 C CB  . THR B 1 248 ? 4.624   43.369  35.506 1.000 32.920 0  248 THR B CB  1 
ATOM   4716 O OG1 . THR B 1 248 ? 3.770   43.649  34.391 1.000 32.770 0  248 THR B OG1 1 
ATOM   4717 C CG2 . THR B 1 248 ? 6.001   42.946  34.999 1.000 26.430 0  248 THR B CG2 1 
ATOM   4718 N N   . GLY B 1 249 ? 1.592   42.399  36.716 1.000 31.000 0  249 GLY B N   1 
ATOM   4719 C CA  . GLY B 1 249 ? 0.415   42.728  37.498 1.000 32.890 0  249 GLY B CA  1 
ATOM   4720 C C   . GLY B 1 249 ? 0.332   41.972  38.810 1.000 32.720 0  249 GLY B C   1 
ATOM   4721 O O   . GLY B 1 249 ? -0.225  42.483  39.784 1.000 31.130 0  249 GLY B O   1 
ATOM   4722 N N   . MET B 1 250 ? 0.873   40.752  38.859 1.000 31.420 0  250 MET B N   1 
ATOM   4723 C CA  . MET B 1 250 ? 0.885   39.996  40.105 1.000 30.490 0  250 MET B CA  1 
ATOM   4724 C C   . MET B 1 250 ? 1.978   40.445  41.070 1.000 32.830 0  250 MET B C   1 
ATOM   4725 O O   . MET B 1 250 ? 2.143   39.821  42.123 1.000 34.110 0  250 MET B O   1 
ATOM   4726 C CB  . MET B 1 250 ? 1.035   38.499  39.820 1.000 31.830 0  250 MET B CB  1 
ATOM   4727 C CG  . MET B 1 250 ? 0.372   38.034  38.539 1.000 31.030 0  250 MET B CG  1 
ATOM   4728 S SD  . MET B 1 250 ? 0.477   36.244  38.342 1.000 41.590 0  250 MET B SD  1 
ATOM   4729 C CE  . MET B 1 250 ? -0.085  36.040  36.653 1.000 28.980 0  250 MET B CE  1 
ATOM   4730 N N   . GLY B 1 251 ? 2.715   41.505  40.750 1.000 31.090 0  251 GLY B N   1 
ATOM   4731 C CA  . GLY B 1 251 ? 3.812   41.918  41.599 1.000 33.080 0  251 GLY B CA  1 
ATOM   4732 C C   . GLY B 1 251 ? 5.049   41.062  41.466 1.000 34.150 0  251 GLY B C   1 
ATOM   4733 O O   . GLY B 1 251 ? 5.810   40.927  42.431 1.000 33.510 0  251 GLY B O   1 
ATOM   4734 N N   . LEU B 1 252 ? 5.276   40.476  40.293 1.000 33.110 0  252 LEU B N   1 
ATOM   4735 C CA  . LEU B 1 252 ? 6.420   39.613  40.031 1.000 30.470 0  252 LEU B CA  1 
ATOM   4736 C C   . LEU B 1 252 ? 7.421   40.348  39.151 1.000 31.580 0  252 LEU B C   1 
ATOM   4737 O O   . LEU B 1 252 ? 7.038   40.968  38.153 1.000 32.050 0  252 LEU B O   1 
ATOM   4738 C CB  . LEU B 1 252 ? 5.976   38.315  39.347 1.000 30.420 0  252 LEU B CB  1 
ATOM   4739 C CG  . LEU B 1 252 ? 5.200   37.296  40.187 1.000 30.760 0  252 LEU B CG  1 
ATOM   4740 C CD1 . LEU B 1 252 ? 4.836   36.067  39.365 1.000 27.830 0  252 LEU B CD1 1 
ATOM   4741 C CD2 . LEU B 1 252 ? 6.002   36.902  41.416 1.000 28.220 0  252 LEU B CD2 1 
ATOM   4742 N N   . ASP B 1 253 ? 8.698   40.278  39.520 1.000 29.270 0  253 ASP B N   1 
ATOM   4743 C CA  . ASP B 1 253 ? 9.756   40.811  38.676 1.000 28.350 0  253 ASP B CA  1 
ATOM   4744 C C   . ASP B 1 253 ? 10.104  39.808  37.576 1.000 28.510 0  253 ASP B C   1 
ATOM   4745 O O   . ASP B 1 253 ? 9.580   38.692  37.522 1.000 25.600 0  253 ASP B O   1 
ATOM   4746 C CB  . ASP B 1 253 ? 10.986  41.157  39.512 1.000 27.490 0  253 ASP B CB  1 
ATOM   4747 C CG  . ASP B 1 253 ? 10.687  42.180  40.588 1.000 28.540 0  253 ASP B CG  1 
ATOM   4748 O OD1 . ASP B 1 253 ? 9.841   43.065  40.348 1.000 28.300 0  253 ASP B OD1 1 
ATOM   4749 O OD2 . ASP B 1 253 ? 11.303  42.101  41.672 1.000 31.520 -1 253 ASP B OD2 1 
ATOM   4750 N N   . LEU B 1 254 ? 11.011  40.212  36.688 1.000 28.160 0  254 LEU B N   1 
ATOM   4751 C CA  . LEU B 1 254 ? 11.384  39.412  35.534 1.000 27.240 0  254 LEU B CA  1 
ATOM   4752 C C   . LEU B 1 254 ? 12.890  39.211  35.496 1.000 28.270 0  254 LEU B C   1 
ATOM   4753 O O   . LEU B 1 254 ? 13.661  40.030  36.005 1.000 28.630 0  254 LEU B O   1 
ATOM   4754 C CB  . LEU B 1 254 ? 10.931  40.069  34.224 1.000 25.990 0  254 LEU B CB  1 
ATOM   4755 C CG  . LEU B 1 254 ? 9.420   40.175  34.041 1.000 27.170 0  254 LEU B CG  1 
ATOM   4756 C CD1 . LEU B 1 254 ? 9.077   41.046  32.839 1.000 24.790 0  254 LEU B CD1 1 
ATOM   4757 C CD2 . LEU B 1 254 ? 8.825   38.784  33.899 1.000 27.750 0  254 LEU B CD2 1 
ATOM   4758 N N   . LEU B 1 255 ? 13.300  38.104  34.883 1.000 28.910 0  255 LEU B N   1 
ATOM   4759 C CA  . LEU B 1 255 ? 14.698  37.881  34.543 1.000 26.870 0  255 LEU B CA  1 
ATOM   4760 C C   . LEU B 1 255 ? 14.782  37.285  33.148 1.000 26.760 0  255 LEU B C   1 
ATOM   4761 O O   . LEU B 1 255 ? 13.915  36.506  32.748 1.000 28.480 0  255 LEU B O   1 
ATOM   4762 C CB  . LEU B 1 255 ? 15.400  36.938  35.533 1.000 24.790 0  255 LEU B CB  1 
ATOM   4763 C CG  . LEU B 1 255 ? 15.544  37.277  37.014 1.000 24.680 0  255 LEU B CG  1 
ATOM   4764 C CD1 . LEU B 1 255 ? 14.282  36.943  37.763 1.000 25.980 0  255 LEU B CD1 1 
ATOM   4765 C CD2 . LEU B 1 255 ? 16.717  36.510  37.599 1.000 25.460 0  255 LEU B CD2 1 
ATOM   4766 N N   . ILE B 1 256 ? 15.821  37.652  32.409 1.000 24.980 0  256 ILE B N   1 
ATOM   4767 C CA  . ILE B 1 256 ? 16.243  36.896  31.238 1.000 26.010 0  256 ILE B CA  1 
ATOM   4768 C C   . ILE B 1 256 ? 17.396  36.016  31.699 1.000 25.670 0  256 ILE B C   1 
ATOM   4769 O O   . ILE B 1 256 ? 18.479  36.513  32.024 1.000 26.910 0  256 ILE B O   1 
ATOM   4770 C CB  . ILE B 1 256 ? 16.642  37.809  30.073 1.000 24.950 0  256 ILE B CB  1 
ATOM   4771 C CG1 . ILE B 1 256 ? 15.422  38.580  29.569 1.000 26.300 0  256 ILE B CG1 1 
ATOM   4772 C CG2 . ILE B 1 256 ? 17.246  36.992  28.947 1.000 25.990 0  256 ILE B CG2 1 
ATOM   4773 C CD1 . ILE B 1 256 ? 15.719  39.519  28.425 1.000 26.040 0  256 ILE B CD1 1 
ATOM   4774 N N   . THR B 1 257 ? 17.162  34.704  31.740 1.000 24.820 0  257 THR B N   1 
ATOM   4775 C CA  . THR B 1 257 ? 18.004  33.795  32.507 1.000 25.320 0  257 THR B CA  1 
ATOM   4776 C C   . THR B 1 257 ? 18.926  32.916  31.675 1.000 24.830 0  257 THR B C   1 
ATOM   4777 O O   . THR B 1 257 ? 19.963  32.493  32.185 1.000 24.920 0  257 THR B O   1 
ATOM   4778 C CB  . THR B 1 257 ? 17.133  32.883  33.384 1.000 25.810 0  257 THR B CB  1 
ATOM   4779 O OG1 . THR B 1 257 ? 16.077  32.320  32.595 1.000 24.480 0  257 THR B OG1 1 
ATOM   4780 C CG2 . THR B 1 257 ? 16.529  33.665  34.539 1.000 24.540 0  257 THR B CG2 1 
ATOM   4781 N N   . GLU B 1 258 ? 18.572  32.608  30.429 1.000 27.010 0  258 GLU B N   1 
ATOM   4782 C CA  . GLU B 1 258 ? 19.293  31.618  29.628 1.000 24.920 0  258 GLU B CA  1 
ATOM   4783 C C   . GLU B 1 258 ? 19.318  32.031  28.159 1.000 25.040 0  258 GLU B C   1 
ATOM   4784 O O   . GLU B 1 258 ? 18.971  31.255  27.269 1.000 26.000 0  258 GLU B O   1 
ATOM   4785 C CB  . GLU B 1 258 ? 18.655  30.235  29.764 1.000 24.800 0  258 GLU B CB  1 
ATOM   4786 C CG  . GLU B 1 258 ? 18.545  29.696  31.180 1.000 24.710 0  258 GLU B CG  1 
ATOM   4787 C CD  . GLU B 1 258 ? 17.920  28.314  31.238 1.000 24.600 0  258 GLU B CD  1 
ATOM   4788 O OE1 . GLU B 1 258 ? 17.763  27.673  30.176 1.000 24.620 0  258 GLU B OE1 1 
ATOM   4789 O OE2 . GLU B 1 258 ? 17.581  27.870  32.356 1.000 24.520 -1 258 GLU B OE2 1 
ATOM   4790 N N   . PHE B 1 259 ? 19.726  33.265  27.880 1.000 25.740 0  259 PHE B N   1 
ATOM   4791 C CA  . PHE B 1 259 ? 19.578  33.806  26.532 1.000 27.280 0  259 PHE B CA  1 
ATOM   4792 C C   . PHE B 1 259 ? 20.525  33.140  25.536 1.000 28.270 0  259 PHE B C   1 
ATOM   4793 O O   . PHE B 1 259 ? 21.720  32.979  25.805 1.000 28.250 0  259 PHE B O   1 
ATOM   4794 C CB  . PHE B 1 259 ? 19.819  35.315  26.532 1.000 27.860 0  259 PHE B CB  1 
ATOM   4795 C CG  . PHE B 1 259 ? 19.506  35.975  25.218 1.000 26.140 0  259 PHE B CG  1 
ATOM   4796 C CD1 . PHE B 1 259 ? 18.226  36.426  24.941 1.000 26.570 0  259 PHE B CD1 1 
ATOM   4797 C CD2 . PHE B 1 259 ? 20.492  36.144  24.257 1.000 27.440 0  259 PHE B CD2 1 
ATOM   4798 C CE1 . PHE B 1 259 ? 17.934  37.032  23.736 1.000 26.230 0  259 PHE B CE1 1 
ATOM   4799 C CE2 . PHE B 1 259 ? 20.205  36.747  23.048 1.000 27.390 0  259 PHE B CE2 1 
ATOM   4800 C CZ  . PHE B 1 259 ? 18.925  37.193  22.787 1.000 28.600 0  259 PHE B CZ  1 
ATOM   4801 N N   . ASP B 1 260 ? 19.975  32.768  24.378 1.000 26.490 0  260 ASP B N   1 
ATOM   4802 C CA  . ASP B 1 260 ? 20.722  32.464  23.160 1.000 25.710 0  260 ASP B CA  1 
ATOM   4803 C C   . ASP B 1 260 ? 19.717  32.421  22.016 1.000 26.120 0  260 ASP B C   1 
ATOM   4804 O O   . ASP B 1 260 ? 18.504  32.439  22.237 1.000 28.430 0  260 ASP B O   1 
ATOM   4805 C CB  . ASP B 1 260 ? 21.517  31.156  23.258 1.000 25.880 0  260 ASP B CB  1 
ATOM   4806 C CG  . ASP B 1 260 ? 20.668  29.971  23.698 1.000 27.640 0  260 ASP B CG  1 
ATOM   4807 O OD1 . ASP B 1 260 ? 19.423  30.032  23.595 1.000 27.760 0  260 ASP B OD1 1 
ATOM   4808 O OD2 . ASP B 1 260 ? 21.259  28.964  24.142 1.000 26.230 -1 260 ASP B OD2 1 
ATOM   4809 N N   . VAL B 1 261 ? 20.226  32.360  20.788 1.000 25.940 0  261 VAL B N   1 
ATOM   4810 C CA  . VAL B 1 261 ? 19.392  32.488  19.595 1.000 28.400 0  261 VAL B CA  1 
ATOM   4811 C C   . VAL B 1 261 ? 19.615  31.273  18.701 1.000 28.590 0  261 VAL B C   1 
ATOM   4812 O O   . VAL B 1 261 ? 20.707  31.096  18.150 1.000 29.570 0  261 VAL B O   1 
ATOM   4813 C CB  . VAL B 1 261 ? 19.679  33.784  18.824 1.000 29.660 0  261 VAL B CB  1 
ATOM   4814 C CG1 . VAL B 1 261 ? 18.730  33.911  17.646 1.000 28.460 0  261 VAL B CG1 1 
ATOM   4815 C CG2 . VAL B 1 261 ? 19.559  34.992  19.745 1.000 29.080 0  261 VAL B CG2 1 
ATOM   4816 N N   . ASN B 1 262 ? 18.585  30.444  18.554 1.000 29.210 0  262 ASN B N   1 
ATOM   4817 C CA  . ASN B 1 262 ? 18.652  29.279  17.677 1.000 30.770 0  262 ASN B CA  1 
ATOM   4818 C C   . ASN B 1 262 ? 18.585  29.726  16.218 1.000 30.540 0  262 ASN B C   1 
ATOM   4819 O O   . ASN B 1 262 ? 17.580  30.302  15.787 1.000 35.010 0  262 ASN B O   1 
ATOM   4820 C CB  . ASN B 1 262 ? 17.511  28.317  17.997 1.000 29.990 0  262 ASN B CB  1 
ATOM   4821 C CG  . ASN B 1 262 ? 17.669  26.969  17.314 1.000 32.830 0  262 ASN B CG  1 
ATOM   4822 O OD1 . ASN B 1 262 ? 17.884  26.890  16.104 1.000 32.020 0  262 ASN B OD1 1 
ATOM   4823 N ND2 . ASN B 1 262 ? 17.555  25.898  18.092 1.000 31.360 0  262 ASN B ND2 1 
ATOM   4824 N N   . ASP B 1 263 ? 19.638  29.444  15.450 1.000 28.720 0  263 ASP B N   1 
ATOM   4825 C CA  . ASP B 1 263 ? 19.789  29.970  14.097 1.000 30.600 0  263 ASP B CA  1 
ATOM   4826 C C   . ASP B 1 263 ? 19.370  28.974  13.017 1.000 32.410 0  263 ASP B C   1 
ATOM   4827 O O   . ASP B 1 263 ? 19.845  29.074  11.880 1.000 33.050 0  263 ASP B O   1 
ATOM   4828 C CB  . ASP B 1 263 ? 21.230  30.440  13.855 1.000 31.760 0  263 ASP B CB  1 
ATOM   4829 C CG  . ASP B 1 263 ? 22.259  29.303  13.894 1.000 31.040 0  263 ASP B CG  1 
ATOM   4830 O OD1 . ASP B 1 263 ? 21.921  28.129  13.626 1.000 29.320 0  263 ASP B OD1 1 
ATOM   4831 O OD2 . ASP B 1 263 ? 23.442  29.603  14.165 1.000 31.310 -1 263 ASP B OD2 1 
ATOM   4832 N N   . LYS B 1 264 ? 18.496  28.019  13.341 1.000 34.360 0  264 LYS B N   1 
ATOM   4833 C CA  . LYS B 1 264 ? 18.247  26.908  12.428 1.000 32.940 0  264 LYS B CA  1 
ATOM   4834 C C   . LYS B 1 264 ? 17.475  27.324  11.182 1.000 33.060 0  264 LYS B C   1 
ATOM   4835 O O   . LYS B 1 264 ? 17.513  26.604  10.179 1.000 32.280 0  264 LYS B O   1 
ATOM   4836 C CB  . LYS B 1 264 ? 17.481  25.803  13.159 1.000 31.200 0  264 LYS B CB  1 
ATOM   4837 C CG  . LYS B 1 264 ? 17.582  24.429  12.521 1.000 35.990 0  264 LYS B CG  1 
ATOM   4838 C CD  . LYS B 1 264 ? 16.379  23.564  12.877 1.000 35.890 0  264 LYS B CD  1 
ATOM   4839 C CE  . LYS B 1 264 ? 16.539  22.910  14.241 1.000 37.660 0  264 LYS B CE  1 
ATOM   4840 N NZ  . LYS B 1 264 ? 16.578  21.423  14.143 1.000 37.820 1  264 LYS B NZ  1 
ATOM   4841 N N   . ALA B 1 265 ? 16.807  28.475  11.208 1.000 32.980 0  265 ALA B N   1 
ATOM   4842 C CA  . ALA B 1 265 ? 16.046  28.959  10.067 1.000 32.420 0  265 ALA B CA  1 
ATOM   4843 C C   . ALA B 1 265 ? 16.818  29.965  9.222  1.000 34.810 0  265 ALA B C   1 
ATOM   4844 O O   . ALA B 1 265 ? 16.239  30.565  8.310  1.000 34.620 0  265 ALA B O   1 
ATOM   4845 C CB  . ALA B 1 265 ? 14.727  29.574  10.538 1.000 30.400 0  265 ALA B CB  1 
ATOM   4846 N N   . PHE B 1 266 ? 18.101  30.163  9.496  1.000 32.080 0  266 PHE B N   1 
ATOM   4847 C CA  . PHE B 1 266 ? 18.831  31.186  8.773  1.000 32.880 0  266 PHE B CA  1 
ATOM   4848 C C   . PHE B 1 266 ? 19.853  30.544  7.840  1.000 34.150 0  266 PHE B C   1 
ATOM   4849 O O   . PHE B 1 266 ? 20.311  29.426  8.096  1.000 33.970 0  266 PHE B O   1 
ATOM   4850 C CB  . PHE B 1 266 ? 19.542  32.135  9.745  1.000 33.030 0  266 PHE B CB  1 
ATOM   4851 C CG  . PHE B 1 266 ? 18.626  32.790  10.745 1.000 33.680 0  266 PHE B CG  1 
ATOM   4852 C CD1 . PHE B 1 266 ? 17.285  33.000  10.455 1.000 30.950 0  266 PHE B CD1 1 
ATOM   4853 C CD2 . PHE B 1 266 ? 19.114  33.214  11.972 1.000 35.050 0  266 PHE B CD2 1 
ATOM   4854 C CE1 . PHE B 1 266 ? 16.446  33.606  11.376 1.000 31.850 0  266 PHE B CE1 1 
ATOM   4855 C CE2 . PHE B 1 266 ? 18.281  33.823  12.895 1.000 34.340 0  266 PHE B CE2 1 
ATOM   4856 C CZ  . PHE B 1 266 ? 16.946  34.020  12.596 1.000 33.620 0  266 PHE B CZ  1 
ATOM   4857 N N   . PRO B 1 267 ? 20.223  31.214  6.746  1.000 35.890 0  267 PRO B N   1 
ATOM   4858 C CA  . PRO B 1 267 ? 21.090  30.576  5.749  1.000 36.750 0  267 PRO B CA  1 
ATOM   4859 C C   . PRO B 1 267 ? 22.416  30.133  6.350  1.000 34.960 0  267 PRO B C   1 
ATOM   4860 O O   . PRO B 1 267 ? 22.832  30.580  7.422  1.000 35.180 0  267 PRO B O   1 
ATOM   4861 C CB  . PRO B 1 267 ? 21.309  31.666  4.690  1.000 35.160 0  267 PRO B CB  1 
ATOM   4862 C CG  . PRO B 1 267 ? 20.389  32.782  5.022  1.000 32.070 0  267 PRO B CG  1 
ATOM   4863 C CD  . PRO B 1 267 ? 19.601  32.452  6.245  1.000 34.380 0  267 PRO B CD  1 
ATOM   4864 N N   . ALA B 1 268 ? 23.093  29.248  5.618  1.000 31.660 0  268 ALA B N   1 
ATOM   4865 C CA  . ALA B 1 268 ? 24.394  28.761  6.058  1.000 31.020 0  268 ALA B CA  1 
ATOM   4866 C C   . ALA B 1 268 ? 25.423  29.879  6.089  1.000 33.890 0  268 ALA B C   1 
ATOM   4867 O O   . ALA B 1 268 ? 26.355  29.842  6.901  1.000 35.550 0  268 ALA B O   1 
ATOM   4868 C CB  . ALA B 1 268 ? 24.858  27.631  5.141  1.000 29.970 0  268 ALA B CB  1 
ATOM   4869 N N   . ASP B 1 269 ? 25.267  30.872  5.216  1.000 33.400 0  269 ASP B N   1 
ATOM   4870 C CA  . ASP B 1 269 ? 26.214  31.975  5.119  1.000 33.550 0  269 ASP B CA  1 
ATOM   4871 C C   . ASP B 1 269 ? 26.387  32.674  6.461  1.000 34.330 0  269 ASP B C   1 
ATOM   4872 O O   . ASP B 1 269 ? 25.410  33.066  7.106  1.000 34.620 0  269 ASP B O   1 
ATOM   4873 C CB  . ASP B 1 269 ? 25.739  32.967  4.060  1.000 32.450 0  269 ASP B CB  1 
ATOM   4874 C CG  . ASP B 1 269 ? 26.733  34.071  3.817  1.000 33.260 0  269 ASP B CG  1 
ATOM   4875 O OD1 . ASP B 1 269 ? 27.671  33.852  3.023  1.000 36.680 0  269 ASP B OD1 1 
ATOM   4876 O OD2 . ASP B 1 269 ? 26.574  35.157  4.413  1.000 33.340 -1 269 ASP B OD2 1 
ATOM   4877 N N   . PHE B 1 270 ? 27.646  32.814  6.883  1.000 33.750 0  270 PHE B N   1 
ATOM   4878 C CA  . PHE B 1 270 ? 27.939  33.365  8.203  1.000 33.010 0  270 PHE B CA  1 
ATOM   4879 C C   . PHE B 1 270 ? 27.414  34.788  8.353  1.000 32.090 0  270 PHE B C   1 
ATOM   4880 O O   . PHE B 1 270 ? 26.883  35.150  9.409  1.000 31.400 0  270 PHE B O   1 
ATOM   4881 C CB  . PHE B 1 270 ? 29.445  33.322  8.463  1.000 32.440 0  270 PHE B CB  1 
ATOM   4882 C CG  . PHE B 1 270 ? 29.952  31.971  8.889  1.000 32.530 0  270 PHE B CG  1 
ATOM   4883 C CD1 . PHE B 1 270 ? 29.123  30.862  8.865  1.000 32.650 0  270 PHE B CD1 1 
ATOM   4884 C CD2 . PHE B 1 270 ? 31.262  31.811  9.309  1.000 33.070 0  270 PHE B CD2 1 
ATOM   4885 C CE1 . PHE B 1 270 ? 29.590  29.619  9.256  1.000 33.280 0  270 PHE B CE1 1 
ATOM   4886 C CE2 . PHE B 1 270 ? 31.735  30.572  9.701  1.000 31.690 0  270 PHE B CE2 1 
ATOM   4887 C CZ  . PHE B 1 270 ? 30.896  29.474  9.673  1.000 31.620 0  270 PHE B CZ  1 
ATOM   4888 N N   . ALA B 1 271 ? 27.542  35.609  7.309  1.000 31.950 0  271 ALA B N   1 
ATOM   4889 C CA  . ALA B 1 271 ? 27.134  37.006  7.423  1.000 30.150 0  271 ALA B CA  1 
ATOM   4890 C C   . ALA B 1 271 ? 25.621  37.124  7.544  1.000 30.370 0  271 ALA B C   1 
ATOM   4891 O O   . ALA B 1 271 ? 25.110  37.831  8.421  1.000 31.130 0  271 ALA B O   1 
ATOM   4892 C CB  . ALA B 1 271 ? 27.648  37.804  6.224  1.000 30.640 0  271 ALA B CB  1 
ATOM   4893 N N   . LYS B 1 272 ? 24.888  36.432  6.669  1.000 30.330 0  272 LYS B N   1 
ATOM   4894 C CA  . LYS B 1 272 ? 23.433  36.437  6.755  1.000 29.550 0  272 LYS B CA  1 
ATOM   4895 C C   . LYS B 1 272 ? 22.953  35.850  8.076  1.000 31.620 0  272 LYS B C   1 
ATOM   4896 O O   . LYS B 1 272 ? 22.015  36.371  8.689  1.000 34.550 0  272 LYS B O   1 
ATOM   4897 C CB  . LYS B 1 272 ? 22.832  35.665  5.580  1.000 30.620 0  272 LYS B CB  1 
ATOM   4898 C CG  . LYS B 1 272 ? 23.331  36.106  4.213  1.000 31.320 0  272 LYS B CG  1 
ATOM   4899 C CD  . LYS B 1 272 ? 22.410  35.606  3.113  1.000 32.400 0  272 LYS B CD  1 
ATOM   4900 C CE  . LYS B 1 272 ? 22.679  36.310  1.792  1.000 33.840 0  272 LYS B CE  1 
ATOM   4901 N NZ  . LYS B 1 272 ? 22.196  35.509  0.630  1.000 35.750 1  272 LYS B NZ  1 
ATOM   4902 N N   . ARG B 1 273 ? 23.594  34.774  8.543  1.000 30.840 0  273 ARG B N   1 
ATOM   4903 C CA  . ARG B 1 273 ? 23.156  34.156  9.791  1.000 31.120 0  273 ARG B CA  1 
ATOM   4904 C C   . ARG B 1 273 ? 23.393  35.073  10.983 1.000 30.350 0  273 ARG B C   1 
ATOM   4905 O O   . ARG B 1 273 ? 22.522  35.207  11.850 1.000 29.390 0  273 ARG B O   1 
ATOM   4906 C CB  . ARG B 1 273 ? 23.862  32.817  10.005 1.000 29.660 0  273 ARG B CB  1 
ATOM   4907 C CG  . ARG B 1 273 ? 22.915  31.721  10.458 1.000 32.350 0  273 ARG B CG  1 
ATOM   4908 C CD  . ARG B 1 273 ? 23.625  30.489  10.978 1.000 32.220 0  273 ARG B CD  1 
ATOM   4909 N NE  . ARG B 1 273 ? 24.523  29.903  9.993  1.000 33.300 0  273 ARG B NE  1 
ATOM   4910 C CZ  . ARG B 1 273 ? 25.465  29.017  10.282 1.000 33.360 0  273 ARG B CZ  1 
ATOM   4911 N NH1 . ARG B 1 273 ? 25.632  28.563  11.513 1.000 31.980 1  273 ARG B NH1 1 
ATOM   4912 N NH2 . ARG B 1 273 ? 26.255  28.569  9.310  1.000 34.330 0  273 ARG B NH2 1 
ATOM   4913 N N   . ASP B 1 274 ? 24.563  35.712  11.046 1.000 31.030 0  274 ASP B N   1 
ATOM   4914 C CA  . ASP B 1 274 ? 24.835  36.634  12.142 1.000 29.020 0  274 ASP B CA  1 
ATOM   4915 C C   . ASP B 1 274 ? 23.899  37.833  12.096 1.000 29.300 0  274 ASP B C   1 
ATOM   4916 O O   . ASP B 1 274 ? 23.392  38.273  13.135 1.000 30.760 0  274 ASP B O   1 
ATOM   4917 C CB  . ASP B 1 274 ? 26.293  37.088  12.104 1.000 29.220 0  274 ASP B CB  1 
ATOM   4918 C CG  . ASP B 1 274 ? 27.262  35.950  12.334 1.000 29.770 0  274 ASP B CG  1 
ATOM   4919 O OD1 . ASP B 1 274 ? 26.806  34.829  12.645 1.000 28.750 0  274 ASP B OD1 1 
ATOM   4920 O OD2 . ASP B 1 274 ? 28.482  36.179  12.205 1.000 32.370 -1 274 ASP B OD2 1 
ATOM   4921 N N   . ALA B 1 275 ? 23.636  38.362  10.898 1.000 30.840 0  275 ALA B N   1 
ATOM   4922 C CA  . ALA B 1 275 ? 22.721  39.492  10.782 1.000 29.590 0  275 ALA B CA  1 
ATOM   4923 C C   . ALA B 1 275 ? 21.311  39.106  11.208 1.000 29.690 0  275 ALA B C   1 
ATOM   4924 O O   . ALA B 1 275 ? 20.620  39.883  11.873 1.000 32.490 0  275 ALA B O   1 
ATOM   4925 C CB  . ALA B 1 275 ? 22.722  40.021  9.348  1.000 29.010 0  275 ALA B CB  1 
ATOM   4926 N N   . ALA B 1 276 ? 20.872  37.898  10.847 1.000 29.350 0  276 ALA B N   1 
ATOM   4927 C CA  . ALA B 1 276 ? 19.523  37.473  11.199 1.000 30.650 0  276 ALA B CA  1 
ATOM   4928 C C   . ALA B 1 276 ? 19.399  37.199  12.693 1.000 31.110 0  276 ALA B C   1 
ATOM   4929 O O   . ALA B 1 276 ? 18.393  37.564  13.313 1.000 31.470 0  276 ALA B O   1 
ATOM   4930 C CB  . ALA B 1 276 ? 19.130  36.247  10.379 1.000 28.790 0  276 ALA B CB  1 
ATOM   4931 N N   . THR B 1 277 ? 20.408  36.556  13.292 1.000 30.570 0  277 THR B N   1 
ATOM   4932 C CA  . THR B 1 277 ? 20.377  36.358  14.738 1.000 31.240 0  277 THR B CA  1 
ATOM   4933 C C   . THR B 1 277 ? 20.415  37.692  15.470 1.000 31.520 0  277 THR B C   1 
ATOM   4934 O O   . THR B 1 277 ? 19.753  37.850  16.501 1.000 31.360 0  277 THR B O   1 
ATOM   4935 C CB  . THR B 1 277 ? 21.536  35.463  15.198 1.000 29.540 0  277 THR B CB  1 
ATOM   4936 O OG1 . THR B 1 277 ? 22.781  35.973  14.707 1.000 29.940 0  277 THR B OG1 1 
ATOM   4937 C CG2 . THR B 1 277 ? 21.345  34.041  14.700 1.000 30.900 0  277 THR B CG2 1 
ATOM   4938 N N   . ALA B 1 278 ? 21.136  38.677  14.925 1.000 31.330 0  278 ALA B N   1 
ATOM   4939 C CA  . ALA B 1 278 ? 21.195  39.995  15.550 1.000 31.110 0  278 ALA B CA  1 
ATOM   4940 C C   . ALA B 1 278 ? 19.852  40.709  15.458 1.000 29.360 0  278 ALA B C   1 
ATOM   4941 O O   . ALA B 1 278 ? 19.386  41.305  16.435 1.000 29.870 0  278 ALA B O   1 
ATOM   4942 C CB  . ALA B 1 278 ? 22.301  40.829  14.907 1.000 28.970 0  278 ALA B CB  1 
ATOM   4943 N N   . ALA B 1 279 ? 19.226  40.683  14.279 1.000 29.080 0  279 ALA B N   1 
ATOM   4944 C CA  . ALA B 1 279 ? 17.927  41.331  14.120 1.000 30.980 0  279 ALA B CA  1 
ATOM   4945 C C   . ALA B 1 279 ? 16.872  40.670  14.997 1.000 30.200 0  279 ALA B C   1 
ATOM   4946 O O   . ALA B 1 279 ? 16.031  41.355  15.590 1.000 29.680 0  279 ALA B O   1 
ATOM   4947 C CB  . ALA B 1 279 ? 17.500  41.304  12.653 1.000 32.610 0  279 ALA B CB  1 
ATOM   4948 N N   . LEU B 1 280 ? 16.906  39.339  15.102 1.000 32.150 0  280 LEU B N   1 
ATOM   4949 C CA  . LEU B 1 280 ? 15.957  38.639  15.962 1.000 31.450 0  280 LEU B CA  1 
ATOM   4950 C C   . LEU B 1 280 ? 16.199  38.963  17.432 1.000 30.200 0  280 LEU B C   1 
ATOM   4951 O O   . LEU B 1 280 ? 15.244  39.168  18.196 1.000 31.620 0  280 LEU B O   1 
ATOM   4952 C CB  . LEU B 1 280 ? 16.052  37.136  15.722 1.000 29.400 0  280 LEU B CB  1 
ATOM   4953 C CG  . LEU B 1 280 ? 15.164  36.268  16.608 1.000 31.050 0  280 LEU B CG  1 
ATOM   4954 C CD1 . LEU B 1 280 ? 13.694  36.603  16.401 1.000 32.770 0  280 LEU B CD1 1 
ATOM   4955 C CD2 . LEU B 1 280 ? 15.442  34.811  16.324 1.000 31.400 0  280 LEU B CD2 1 
ATOM   4956 N N   . ALA B 1 281 ? 17.466  38.988  17.850 1.000 29.220 0  281 ALA B N   1 
ATOM   4957 C CA  . ALA B 1 281 ? 17.791  39.397  19.210 1.000 30.180 0  281 ALA B CA  1 
ATOM   4958 C C   . ALA B 1 281 ? 17.255  40.791  19.497 1.000 30.410 0  281 ALA B C   1 
ATOM   4959 O O   . ALA B 1 281 ? 16.640  41.025  20.541 1.000 28.230 0  281 ALA B O   1 
ATOM   4960 C CB  . ALA B 1 281 ? 19.303  39.343  19.426 1.000 29.860 0  281 ALA B CB  1 
ATOM   4961 N N   . ARG B 1 282 ? 17.487  41.733  18.579 1.000 31.750 0  282 ARG B N   1 
ATOM   4962 C CA  . ARG B 1 282 ? 17.005  43.100  18.760 1.000 30.910 0  282 ARG B CA  1 
ATOM   4963 C C   . ARG B 1 282 ? 15.487  43.129  18.879 1.000 29.170 0  282 ARG B C   1 
ATOM   4964 O O   . ARG B 1 282 ? 14.931  43.769  19.781 1.000 29.160 0  282 ARG B O   1 
ATOM   4965 C CB  . ARG B 1 282 ? 17.480  43.977  17.602 1.000 31.340 0  282 ARG B CB  1 
ATOM   4966 C CG  . ARG B 1 282 ? 17.298  45.470  17.815 1.000 33.460 0  282 ARG B CG  1 
ATOM   4967 C CD  . ARG B 1 282 ? 18.303  46.045  18.802 1.000 32.570 0  282 ARG B CD  1 
ATOM   4968 N NE  . ARG B 1 282 ? 18.034  47.454  19.070 1.000 36.390 0  282 ARG B NE  1 
ATOM   4969 C CZ  . ARG B 1 282 ? 18.417  48.456  18.290 1.000 36.180 0  282 ARG B CZ  1 
ATOM   4970 N NH1 . ARG B 1 282 ? 19.108  48.243  17.182 1.000 37.280 1  282 ARG B NH1 1 
ATOM   4971 N NH2 . ARG B 1 282 ? 18.087  49.702  18.621 1.000 36.730 0  282 ARG B NH2 1 
ATOM   4972 N N   . ASP B 1 283 ? 14.801  42.433  17.972 1.000 28.570 0  283 ASP B N   1 
ATOM   4973 C CA  . ASP B 1 283 ? 13.345  42.372  18.006 1.000 27.240 0  283 ASP B CA  1 
ATOM   4974 C C   . ASP B 1 283 ? 12.847  41.894  19.365 1.000 29.820 0  283 ASP B C   1 
ATOM   4975 O O   . ASP B 1 283 ? 12.001  42.541  19.994 1.000 28.830 0  283 ASP B O   1 
ATOM   4976 C CB  . ASP B 1 283 ? 12.849  41.454  16.889 1.000 28.350 0  283 ASP B CB  1 
ATOM   4977 C CG  . ASP B 1 283 ? 11.430  40.989  17.103 1.000 34.130 0  283 ASP B CG  1 
ATOM   4978 O OD1 . ASP B 1 283 ? 10.537  41.848  17.243 1.000 36.250 0  283 ASP B OD1 1 
ATOM   4979 O OD2 . ASP B 1 283 ? 11.205  39.761  17.125 1.000 37.890 -1 283 ASP B OD2 1 
ATOM   4980 N N   . TYR B 1 284 ? 13.354  40.749  19.828 1.000 30.310 0  284 TYR B N   1 
ATOM   4981 C CA  . TYR B 1 284 ? 12.881  40.190  21.093 1.000 28.310 0  284 TYR B CA  1 
ATOM   4982 C C   . TYR B 1 284 ? 13.250  41.078  22.278 1.000 27.420 0  284 TYR B C   1 
ATOM   4983 O O   . TYR B 1 284 ? 12.413  41.331  23.156 1.000 28.610 0  284 TYR B O   1 
ATOM   4984 C CB  . TYR B 1 284 ? 13.450  38.782  21.281 1.000 28.930 0  284 TYR B CB  1 
ATOM   4985 C CG  . TYR B 1 284 ? 13.120  38.132  22.610 1.000 28.490 0  284 TYR B CG  1 
ATOM   4986 C CD1 . TYR B 1 284 ? 11.954  37.395  22.774 1.000 26.980 0  284 TYR B CD1 1 
ATOM   4987 C CD2 . TYR B 1 284 ? 13.988  38.233  23.693 1.000 26.560 0  284 TYR B CD2 1 
ATOM   4988 C CE1 . TYR B 1 284 ? 11.651  36.793  23.985 1.000 26.280 0  284 TYR B CE1 1 
ATOM   4989 C CE2 . TYR B 1 284 ? 13.691  37.635  24.907 1.000 25.610 0  284 TYR B CE2 1 
ATOM   4990 C CZ  . TYR B 1 284 ? 12.522  36.916  25.044 1.000 26.520 0  284 TYR B CZ  1 
ATOM   4991 O OH  . TYR B 1 284 ? 12.223  36.316  26.249 1.000 26.500 0  284 TYR B OH  1 
ATOM   4992 N N   . LEU B 1 285 ? 14.488  41.579  22.308 1.000 29.600 0  285 LEU B N   1 
ATOM   4993 C CA  . LEU B 1 285 ? 15.001  42.278  23.480 1.000 27.000 0  285 LEU B CA  1 
ATOM   4994 C C   . LEU B 1 285 ? 14.432  43.683  23.623 1.000 26.990 0  285 LEU B C   1 
ATOM   4995 O O   . LEU B 1 285 ? 14.144  44.115  24.742 1.000 26.600 0  285 LEU B O   1 
ATOM   4996 C CB  . LEU B 1 285 ? 16.528  42.340  23.417 1.000 25.960 0  285 LEU B CB  1 
ATOM   4997 C CG  . LEU B 1 285 ? 17.313  41.044  23.650 1.000 26.930 0  285 LEU B CG  1 
ATOM   4998 C CD1 . LEU B 1 285 ? 18.810  41.321  23.686 1.000 27.250 0  285 LEU B CD1 1 
ATOM   4999 C CD2 . LEU B 1 285 ? 16.870  40.346  24.922 1.000 27.360 0  285 LEU B CD2 1 
ATOM   5000 N N   . ASP B 1 286 ? 14.253  44.415  22.519 1.000 27.650 0  286 ASP B N   1 
ATOM   5001 C CA  . ASP B 1 286 ? 13.658  45.743  22.623 1.000 29.840 0  286 ASP B CA  1 
ATOM   5002 C C   . ASP B 1 286 ? 12.263  45.668  23.227 1.000 27.720 0  286 ASP B C   1 
ATOM   5003 O O   . ASP B 1 286 ? 11.885  46.514  24.045 1.000 27.770 0  286 ASP B O   1 
ATOM   5004 C CB  . ASP B 1 286 ? 13.631  46.421  21.252 1.000 30.400 0  286 ASP B CB  1 
ATOM   5005 C CG  . ASP B 1 286 ? 14.850  47.301  21.017 1.000 31.010 0  286 ASP B CG  1 
ATOM   5006 O OD1 . ASP B 1 286 ? 15.650  47.477  21.957 1.000 30.480 0  286 ASP B OD1 1 
ATOM   5007 O OD2 . ASP B 1 286 ? 15.013  47.820  19.894 1.000 33.080 -1 286 ASP B OD2 1 
ATOM   5008 N N   . VAL B 1 287 ? 11.485  44.656  22.839 1.000 27.800 0  287 VAL B N   1 
ATOM   5009 C CA  . VAL B 1 287 ? 10.138  44.498  23.376 1.000 26.750 0  287 VAL B CA  1 
ATOM   5010 C C   . VAL B 1 287 ? 10.191  44.036  24.828 1.000 29.440 0  287 VAL B C   1 
ATOM   5011 O O   . VAL B 1 287 ? 9.537   44.614  25.705 1.000 30.290 0  287 VAL B O   1 
ATOM   5012 C CB  . VAL B 1 287 ? 9.327   43.522  22.506 1.000 26.480 0  287 VAL B CB  1 
ATOM   5013 C CG1 . VAL B 1 287 ? 7.935   43.341  23.080 1.000 30.650 0  287 VAL B CG1 1 
ATOM   5014 C CG2 . VAL B 1 287 ? 9.267   44.017  21.073 1.000 30.290 0  287 VAL B CG2 1 
ATOM   5015 N N   . THR B 1 288 ? 10.962  42.980  25.105 1.000 27.680 0  288 THR B N   1 
ATOM   5016 C CA  . THR B 1 288 ? 10.933  42.392  26.441 1.000 26.600 0  288 THR B CA  1 
ATOM   5017 C C   . THR B 1 288 ? 11.639  43.270  27.469 1.000 27.320 0  288 THR B C   1 
ATOM   5018 O O   . THR B 1 288 ? 11.239  43.294  28.639 1.000 26.180 0  288 THR B O   1 
ATOM   5019 C CB  . THR B 1 288 ? 11.553  40.998  26.416 1.000 25.160 0  288 THR B CB  1 
ATOM   5020 O OG1 . THR B 1 288 ? 11.193  40.345  25.194 1.000 27.250 0  288 THR B OG1 1 
ATOM   5021 C CG2 . THR B 1 288 ? 11.049  40.172  27.585 1.000 24.960 0  288 THR B CG2 1 
ATOM   5022 N N   . LEU B 1 289 ? 12.674  44.003  27.060 1.000 28.320 0  289 LEU B N   1 
ATOM   5023 C CA  . LEU B 1 289 ? 13.418  44.819  28.010 1.000 28.390 0  289 LEU B CA  1 
ATOM   5024 C C   . LEU B 1 289 ? 12.745  46.151  28.307 1.000 29.010 0  289 LEU B C   1 
ATOM   5025 O O   . LEU B 1 289 ? 13.228  46.885  29.175 1.000 31.210 0  289 LEU B O   1 
ATOM   5026 C CB  . LEU B 1 289 ? 14.842  45.061  27.510 1.000 25.700 0  289 LEU B CB  1 
ATOM   5027 C CG  . LEU B 1 289 ? 15.720  43.813  27.578 1.000 25.600 0  289 LEU B CG  1 
ATOM   5028 C CD1 . LEU B 1 289 ? 17.172  44.157  27.294 1.000 29.730 0  289 LEU B CD1 1 
ATOM   5029 C CD2 . LEU B 1 289 ? 15.573  43.141  28.933 1.000 25.420 0  289 LEU B CD2 1 
ATOM   5030 N N   . SER B 1 290 ? 11.660  46.490  27.611 1.000 26.510 0  290 SER B N   1 
ATOM   5031 C CA  . SER B 1 290 ? 10.908  47.690  27.956 1.000 28.040 0  290 SER B CA  1 
ATOM   5032 C C   . SER B 1 290 ? 10.054  47.495  29.203 1.000 27.230 0  290 SER B C   1 
ATOM   5033 O O   . SER B 1 290 ? 9.211   48.345  29.507 1.000 29.980 0  290 SER B O   1 
ATOM   5034 C CB  . SER B 1 290 ? 10.034  48.138  26.779 1.000 29.540 0  290 SER B CB  1 
ATOM   5035 O OG  . SER B 1 290 ? 9.101   47.141  26.404 1.000 30.430 0  290 SER B OG  1 
ATOM   5036 N N   . TYR B 1 291 ? 10.259  46.397  29.927 1.000 28.540 0  291 TYR B N   1 
ATOM   5037 C CA  . TYR B 1 291 ? 9.609   46.164  31.205 1.000 26.200 0  291 TYR B CA  1 
ATOM   5038 C C   . TYR B 1 291 ? 10.613  46.463  32.304 1.000 25.660 0  291 TYR B C   1 
ATOM   5039 O O   . TYR B 1 291 ? 11.583  45.707  32.466 1.000 27.180 0  291 TYR B O   1 
ATOM   5040 C CB  . TYR B 1 291 ? 9.113   44.724  31.302 1.000 27.350 0  291 TYR B CB  1 
ATOM   5041 C CG  . TYR B 1 291 ? 7.878   44.465  30.474 1.000 26.600 0  291 TYR B CG  1 
ATOM   5042 C CD1 . TYR B 1 291 ? 6.613   44.709  30.989 1.000 26.370 0  291 TYR B CD1 1 
ATOM   5043 C CD2 . TYR B 1 291 ? 7.977   44.001  29.167 1.000 26.230 0  291 TYR B CD2 1 
ATOM   5044 C CE1 . TYR B 1 291 ? 5.480   44.483  30.236 1.000 27.730 0  291 TYR B CE1 1 
ATOM   5045 C CE2 . TYR B 1 291 ? 6.844   43.774  28.404 1.000 28.640 0  291 TYR B CE2 1 
ATOM   5046 C CZ  . TYR B 1 291 ? 5.598   44.017  28.944 1.000 27.700 0  291 TYR B CZ  1 
ATOM   5047 O OH  . TYR B 1 291 ? 4.466   43.792  28.196 1.000 27.900 0  291 TYR B OH  1 
ATOM   5048 N N   . PRO B 1 292 ? 10.446  47.549  33.064 1.000 27.090 0  292 PRO B N   1 
ATOM   5049 C CA  . PRO B 1 292 ? 11.485  47.961  34.020 1.000 26.330 0  292 PRO B CA  1 
ATOM   5050 C C   . PRO B 1 292 ? 11.676  47.014  35.192 1.000 25.540 0  292 PRO B C   1 
ATOM   5051 O O   . PRO B 1 292 ? 12.580  47.239  36.001 1.000 27.910 0  292 PRO B O   1 
ATOM   5052 C CB  . PRO B 1 292 ? 11.003  49.342  34.500 1.000 26.680 0  292 PRO B CB  1 
ATOM   5053 C CG  . PRO B 1 292 ? 9.728   49.636  33.762 1.000 25.940 0  292 PRO B CG  1 
ATOM   5054 C CD  . PRO B 1 292 ? 9.231   48.371  33.163 1.000 25.750 0  292 PRO B CD  1 
ATOM   5055 N N   . THR B 1 293 ? 10.872  45.970  35.323 1.000 25.510 0  293 THR B N   1 
ATOM   5056 C CA  . THR B 1 293 ? 11.065  45.015  36.403 1.000 27.770 0  293 THR B CA  1 
ATOM   5057 C C   . THR B 1 293 ? 12.029  43.897  36.030 1.000 27.710 0  293 THR B C   1 
ATOM   5058 O O   . THR B 1 293 ? 12.298  43.024  36.862 1.000 28.740 0  293 THR B O   1 
ATOM   5059 C CB  . THR B 1 293 ? 9.719   44.424  36.836 1.000 26.710 0  293 THR B CB  1 
ATOM   5060 O OG1 . THR B 1 293 ? 8.885   44.244  35.685 1.000 26.390 0  293 THR B OG1 1 
ATOM   5061 C CG2 . THR B 1 293 ? 9.026   45.354  37.824 1.000 25.330 0  293 THR B CG2 1 
ATOM   5062 N N   . CYS B 1 294 ? 12.576  43.920  34.817 1.000 25.620 0  294 CYS B N   1 
ATOM   5063 C CA  . CYS B 1 294 ? 13.562  42.930  34.387 1.000 28.060 0  294 CYS B CA  1 
ATOM   5064 C C   . CYS B 1 294 ? 14.946  43.430  34.779 1.000 27.110 0  294 CYS B C   1 
ATOM   5065 O O   . CYS B 1 294 ? 15.636  44.089  34.001 1.000 27.290 0  294 CYS B O   1 
ATOM   5066 C CB  . CYS B 1 294 ? 13.452  42.690  32.887 1.000 29.080 0  294 CYS B CB  1 
ATOM   5067 S SG  . CYS B 1 294 ? 14.430  41.312  32.289 1.000 26.700 0  294 CYS B SG  1 
ATOM   5068 N N   . ARG B 1 295 ? 15.367  43.089  35.995 1.000 29.150 0  295 ARG B N   1 
ATOM   5069 C CA  . ARG B 1 295 ? 16.616  43.590  36.551 1.000 27.760 0  295 ARG B CA  1 
ATOM   5070 C C   . ARG B 1 295 ? 17.801  42.660  36.306 1.000 28.370 0  295 ARG B C   1 
ATOM   5071 O O   . ARG B 1 295 ? 18.924  42.991  36.712 1.000 27.660 0  295 ARG B O   1 
ATOM   5072 C CB  . ARG B 1 295 ? 16.465  43.837  38.059 1.000 25.580 0  295 ARG B CB  1 
ATOM   5073 C CG  . ARG B 1 295 ? 15.212  44.607  38.460 1.000 26.250 0  295 ARG B CG  1 
ATOM   5074 C CD  . ARG B 1 295 ? 15.375  45.238  39.843 1.000 26.120 0  295 ARG B CD  1 
ATOM   5075 N NE  . ARG B 1 295 ? 14.310  46.182  40.167 1.000 25.560 0  295 ARG B NE  1 
ATOM   5076 C CZ  . ARG B 1 295 ? 13.056  45.844  40.435 1.000 25.500 0  295 ARG B CZ  1 
ATOM   5077 N NH1 . ARG B 1 295 ? 12.668  44.580  40.460 1.000 25.690 1  295 ARG B NH1 1 
ATOM   5078 N NH2 . ARG B 1 295 ? 12.169  46.798  40.695 1.000 25.620 0  295 ARG B NH2 1 
ATOM   5079 N N   . ASP B 1 296 ? 17.598  41.530  35.628 1.000 25.170 0  296 ASP B N   1 
ATOM   5080 C CA  . ASP B 1 296 ? 18.674  40.576  35.402 1.000 28.140 0  296 ASP B CA  1 
ATOM   5081 C C   . ASP B 1 296 ? 18.654  40.077  33.965 1.000 28.300 0  296 ASP B C   1 
ATOM   5082 O O   . ASP B 1 296 ? 17.585  39.875  33.379 1.000 25.060 0  296 ASP B O   1 
ATOM   5083 C CB  . ASP B 1 296 ? 18.579  39.389  36.364 1.000 26.260 0  296 ASP B CB  1 
ATOM   5084 C CG  . ASP B 1 296 ? 18.937  39.768  37.784 1.000 25.970 0  296 ASP B CG  1 
ATOM   5085 O OD1 . ASP B 1 296 ? 20.141  39.746  38.113 1.000 28.220 0  296 ASP B OD1 1 
ATOM   5086 O OD2 . ASP B 1 296 ? 18.019  40.084  38.569 1.000 25.100 -1 296 ASP B OD2 1 
ATOM   5087 N N   . PHE B 1 297 ? 19.849  39.881  33.408 1.000 26.950 0  297 PHE B N   1 
ATOM   5088 C CA  . PHE B 1 297 ? 20.023  39.401  32.042 1.000 26.310 0  297 PHE B CA  1 
ATOM   5089 C C   . PHE B 1 297 ? 21.244  38.496  32.047 1.000 28.760 0  297 PHE B C   1 
ATOM   5090 O O   . PHE B 1 297 ? 22.324  38.923  32.461 1.000 26.080 0  297 PHE B O   1 
ATOM   5091 C CB  . PHE B 1 297 ? 20.201  40.575  31.065 1.000 26.690 0  297 PHE B CB  1 
ATOM   5092 C CG  . PHE B 1 297 ? 20.116  40.203  29.595 1.000 26.420 0  297 PHE B CG  1 
ATOM   5093 C CD1 . PHE B 1 297 ? 20.389  38.921  29.148 1.000 28.520 0  297 PHE B CD1 1 
ATOM   5094 C CD2 . PHE B 1 297 ? 19.768  41.162  28.657 1.000 29.290 0  297 PHE B CD2 1 
ATOM   5095 C CE1 . PHE B 1 297 ? 20.318  38.600  27.804 1.000 29.270 0  297 PHE B CE1 1 
ATOM   5096 C CE2 . PHE B 1 297 ? 19.691  40.845  27.309 1.000 29.480 0  297 PHE B CE2 1 
ATOM   5097 C CZ  . PHE B 1 297 ? 19.967  39.561  26.884 1.000 28.100 0  297 PHE B CZ  1 
ATOM   5098 N N   . LEU B 1 298 ? 21.070  37.248  31.607 1.000 26.720 0  298 LEU B N   1 
ATOM   5099 C CA  . LEU B 1 298 ? 22.160  36.284  31.541 1.000 27.350 0  298 LEU B CA  1 
ATOM   5100 C C   . LEU B 1 298 ? 22.182  35.605  30.179 1.000 28.050 0  298 LEU B C   1 
ATOM   5101 O O   . LEU B 1 298 ? 21.133  35.313  29.599 1.000 26.890 0  298 LEU B O   1 
ATOM   5102 C CB  . LEU B 1 298 ? 22.039  35.217  32.637 1.000 26.240 0  298 LEU B CB  1 
ATOM   5103 C CG  . LEU B 1 298 ? 22.090  35.694  34.088 1.000 25.950 0  298 LEU B CG  1 
ATOM   5104 C CD1 . LEU B 1 298 ? 20.684  35.887  34.647 1.000 26.150 0  298 LEU B CD1 1 
ATOM   5105 C CD2 . LEU B 1 298 ? 22.885  34.718  34.938 1.000 25.310 0  298 LEU B CD2 1 
ATOM   5106 N N   . LEU B 1 299 ? 23.389  35.360  29.678 1.000 30.010 0  299 LEU B N   1 
ATOM   5107 C CA  . LEU B 1 299 ? 23.603  34.592  28.460 1.000 29.060 0  299 LEU B CA  1 
ATOM   5108 C C   . LEU B 1 299 ? 23.910  33.151  28.837 1.000 28.870 0  299 LEU B C   1 
ATOM   5109 O O   . LEU B 1 299 ? 24.758  32.901  29.698 1.000 28.910 0  299 LEU B O   1 
ATOM   5110 C CB  . LEU B 1 299 ? 24.758  35.170  27.641 1.000 26.480 0  299 LEU B CB  1 
ATOM   5111 C CG  . LEU B 1 299 ? 24.615  36.586  27.090 1.000 27.890 0  299 LEU B CG  1 
ATOM   5112 C CD1 . LEU B 1 299 ? 25.986  37.138  26.741 1.000 27.280 0  299 LEU B CD1 1 
ATOM   5113 C CD2 . LEU B 1 299 ? 23.705  36.593  25.873 1.000 28.220 0  299 LEU B CD2 1 
ATOM   5114 N N   . TRP B 1 300 ? 23.259  32.204  28.165 1.000 29.630 0  300 TRP B N   1 
ATOM   5115 C CA  . TRP B 1 300 ? 23.537  30.788  28.398 1.000 27.110 0  300 TRP B CA  1 
ATOM   5116 C C   . TRP B 1 300 ? 24.840  30.423  27.684 1.000 26.490 0  300 TRP B C   1 
ATOM   5117 O O   . TRP B 1 300 ? 24.882  29.650  26.725 1.000 28.240 0  300 TRP B O   1 
ATOM   5118 C CB  . TRP B 1 300 ? 22.370  29.928  27.936 1.000 25.440 0  300 TRP B CB  1 
ATOM   5119 C CG  . TRP B 1 300 ? 22.186  28.703  28.772 1.000 26.020 0  300 TRP B CG  1 
ATOM   5120 C CD1 . TRP B 1 300 ? 22.126  27.415  28.331 1.000 25.350 0  300 TRP B CD1 1 
ATOM   5121 C CD2 . TRP B 1 300 ? 22.047  28.648  30.198 1.000 25.220 0  300 TRP B CD2 1 
ATOM   5122 N NE1 . TRP B 1 300 ? 21.960  26.561  29.392 1.000 25.260 0  300 TRP B NE1 1 
ATOM   5123 C CE2 . TRP B 1 300 ? 21.907  27.294  30.549 1.000 25.180 0  300 TRP B CE2 1 
ATOM   5124 C CE3 . TRP B 1 300 ? 22.025  29.612  31.211 1.000 25.180 0  300 TRP B CE3 1 
ATOM   5125 C CZ2 . TRP B 1 300 ? 21.751  26.878  31.870 1.000 25.960 0  300 TRP B CZ2 1 
ATOM   5126 C CZ3 . TRP B 1 300 ? 21.875  29.197  32.520 1.000 25.100 0  300 TRP B CZ3 1 
ATOM   5127 C CH2 . TRP B 1 300 ? 21.738  27.844  32.838 1.000 25.060 0  300 TRP B CH2 1 
ATOM   5128 N N   . GLY B 1 301 ? 25.929  30.992  28.195 1.000 26.900 0  301 GLY B N   1 
ATOM   5129 C CA  . GLY B 1 301 ? 27.200  30.945  27.503 1.000 26.410 0  301 GLY B CA  1 
ATOM   5130 C C   . GLY B 1 301 ? 27.297  32.070  26.495 1.000 28.530 0  301 GLY B C   1 
ATOM   5131 O O   . GLY B 1 301 ? 26.305  32.403  25.843 1.000 29.560 0  301 GLY B O   1 
ATOM   5132 N N   . MET B 1 302 ? 28.480  32.663  26.345 1.000 30.290 0  302 MET B N   1 
ATOM   5133 C CA  . MET B 1 302 ? 28.658  33.818  25.474 1.000 30.620 0  302 MET B CA  1 
ATOM   5134 C C   . MET B 1 302 ? 29.541  33.522  24.272 1.000 31.020 0  302 MET B C   1 
ATOM   5135 O O   . MET B 1 302 ? 29.843  34.436  23.501 1.000 29.750 0  302 MET B O   1 
ATOM   5136 C CB  . MET B 1 302 ? 29.236  34.990  26.263 1.000 28.870 0  302 MET B CB  1 
ATOM   5137 C CG  . MET B 1 302 ? 30.484  34.640  27.031 1.000 27.620 0  302 MET B CG  1 
ATOM   5138 S SD  . MET B 1 302 ? 30.436  35.379  28.666 1.000 36.450 0  302 MET B SD  1 
ATOM   5139 C CE  . MET B 1 302 ? 30.441  37.112  28.224 1.000 33.160 0  302 MET B CE  1 
ATOM   5140 N N   . ALA B 1 303 ? 29.949  32.270  24.086 1.000 30.000 0  303 ALA B N   1 
ATOM   5141 C CA  . ALA B 1 303 ? 30.726  31.863  22.927 1.000 29.430 0  303 ALA B CA  1 
ATOM   5142 C C   . ALA B 1 303 ? 30.031  30.684  22.266 1.000 30.920 0  303 ALA B C   1 
ATOM   5143 O O   . ALA B 1 303 ? 29.496  29.808  22.950 1.000 30.800 0  303 ALA B O   1 
ATOM   5144 C CB  . ALA B 1 303 ? 32.159  31.492  23.315 1.000 32.380 0  303 ALA B CB  1 
ATOM   5145 N N   . ASP B 1 304 ? 30.025  30.683  20.930 1.000 30.900 0  304 ASP B N   1 
ATOM   5146 C CA  . ASP B 1 304 ? 29.229  29.711  20.187 1.000 29.610 0  304 ASP B CA  1 
ATOM   5147 C C   . ASP B 1 304 ? 29.602  28.281  20.558 1.000 28.810 0  304 ASP B C   1 
ATOM   5148 O O   . ASP B 1 304 ? 28.725  27.430  20.740 1.000 27.500 0  304 ASP B O   1 
ATOM   5149 C CB  . ASP B 1 304 ? 29.399  29.933  18.682 1.000 29.790 0  304 ASP B CB  1 
ATOM   5150 C CG  . ASP B 1 304 ? 28.815  31.253  18.215 1.000 32.050 0  304 ASP B CG  1 
ATOM   5151 O OD1 . ASP B 1 304 ? 28.091  31.901  19.002 1.000 33.810 0  304 ASP B OD1 1 
ATOM   5152 O OD2 . ASP B 1 304 ? 29.082  31.645  17.059 1.000 30.910 -1 304 ASP B OD2 1 
ATOM   5153 N N   . HIS B 1 305 ? 30.900  28.000  20.681 1.000 30.280 0  305 HIS B N   1 
ATOM   5154 C CA  . HIS B 1 305 ? 31.358  26.626  20.842 1.000 29.090 0  305 HIS B CA  1 
ATOM   5155 C C   . HIS B 1 305 ? 31.040  26.049  22.215 1.000 32.770 0  305 HIS B C   1 
ATOM   5156 O O   . HIS B 1 305 ? 31.046  24.823  22.368 1.000 36.300 0  305 HIS B O   1 
ATOM   5157 C CB  . HIS B 1 305 ? 32.862  26.546  20.589 1.000 31.130 0  305 HIS B CB  1 
ATOM   5158 C CG  . HIS B 1 305 ? 33.682  27.288  21.597 1.000 31.030 0  305 HIS B CG  1 
ATOM   5159 N ND1 . HIS B 1 305 ? 33.657  28.662  21.708 1.000 32.450 0  305 HIS B ND1 1 
ATOM   5160 C CD2 . HIS B 1 305 ? 34.544  26.848  22.543 1.000 31.320 0  305 HIS B CD2 1 
ATOM   5161 C CE1 . HIS B 1 305 ? 34.473  29.036  22.678 1.000 33.500 0  305 HIS B CE1 1 
ATOM   5162 N NE2 . HIS B 1 305 ? 35.024  27.955  23.200 1.000 33.140 0  305 HIS B NE2 1 
ATOM   5163 N N   . VAL B 1 306 ? 30.764  26.890  23.215 1.000 33.290 0  306 VAL B N   1 
ATOM   5164 C CA  . VAL B 1 306 ? 30.427  26.408  24.551 1.000 30.430 0  306 VAL B CA  1 
ATOM   5165 C C   . VAL B 1 306 ? 28.927  26.340  24.778 1.000 30.990 0  306 VAL B C   1 
ATOM   5166 O O   . VAL B 1 306 ? 28.488  25.939  25.865 1.000 31.870 0  306 VAL B O   1 
ATOM   5167 C CB  . VAL B 1 306 ? 31.085  27.275  25.644 1.000 31.340 0  306 VAL B CB  1 
ATOM   5168 C CG1 . VAL B 1 306 ? 32.577  27.402  25.396 1.000 31.170 0  306 VAL B CG1 1 
ATOM   5169 C CG2 . VAL B 1 306 ? 30.427  28.646  25.720 1.000 28.400 0  306 VAL B CG2 1 
ATOM   5170 N N   . ASN B 1 307 ? 28.126  26.718  23.788 1.000 30.200 0  307 ASN B N   1 
ATOM   5171 C CA  . ASN B 1 307 ? 26.680  26.747  23.944 1.000 28.160 0  307 ASN B CA  1 
ATOM   5172 C C   . ASN B 1 307 ? 26.089  25.351  23.798 1.000 29.970 0  307 ASN B C   1 
ATOM   5173 O O   . ASN B 1 307 ? 26.541  24.550  22.973 1.000 31.350 0  307 ASN B O   1 
ATOM   5174 C CB  . ASN B 1 307 ? 26.053  27.690  22.920 1.000 26.610 0  307 ASN B CB  1 
ATOM   5175 C CG  . ASN B 1 307 ? 24.595  27.959  23.199 1.000 27.860 0  307 ASN B CG  1 
ATOM   5176 O OD1 . ASN B 1 307 ? 23.717  27.404  22.545 1.000 29.730 0  307 ASN B OD1 1 
ATOM   5177 N ND2 . ASN B 1 307 ? 24.325  28.811  24.181 1.000 26.120 0  307 ASN B ND2 1 
ATOM   5178 N N   . TRP B 1 308 ? 25.068  25.067  24.607 1.000 30.900 0  308 TRP B N   1 
ATOM   5179 C CA  . TRP B 1 308 ? 24.442  23.749  24.623 1.000 30.340 0  308 TRP B CA  1 
ATOM   5180 C C   . TRP B 1 308 ? 23.821  23.364  23.284 1.000 29.690 0  308 TRP B C   1 
ATOM   5181 O O   . TRP B 1 308 ? 23.647  22.170  23.019 1.000 30.160 0  308 TRP B O   1 
ATOM   5182 C CB  . TRP B 1 308 ? 23.370  23.701  25.710 1.000 26.420 0  308 TRP B CB  1 
ATOM   5183 C CG  . TRP B 1 308 ? 22.210  24.596  25.409 1.000 27.030 0  308 TRP B CG  1 
ATOM   5184 C CD1 . TRP B 1 308 ? 22.251  25.943  25.195 1.000 26.370 0  308 TRP B CD1 1 
ATOM   5185 C CD2 . TRP B 1 308 ? 20.838  24.210  25.269 1.000 28.800 0  308 TRP B CD2 1 
ATOM   5186 N NE1 . TRP B 1 308 ? 20.992  26.420  24.937 1.000 26.130 0  308 TRP B NE1 1 
ATOM   5187 C CE2 . TRP B 1 308 ? 20.105  25.376  24.976 1.000 27.110 0  308 TRP B CE2 1 
ATOM   5188 C CE3 . TRP B 1 308 ? 20.157  22.991  25.366 1.000 29.130 0  308 TRP B CE3 1 
ATOM   5189 C CZ2 . TRP B 1 308 ? 18.726  25.362  24.778 1.000 25.810 0  308 TRP B CZ2 1 
ATOM   5190 C CZ3 . TRP B 1 308 ? 18.787  22.980  25.170 1.000 30.360 0  308 TRP B CZ3 1 
ATOM   5191 C CH2 . TRP B 1 308 ? 18.087  24.158  24.878 1.000 29.360 0  308 TRP B CH2 1 
ATOM   5192 N N   . LEU B 1 309 ? 23.474  24.339  22.440 1.000 29.260 0  309 LEU B N   1 
ATOM   5193 C CA  . LEU B 1 309 ? 22.810  24.040  21.175 1.000 30.350 0  309 LEU B CA  1 
ATOM   5194 C C   . LEU B 1 309 ? 23.696  23.284  20.190 1.000 29.850 0  309 LEU B C   1 
ATOM   5195 O O   . LEU B 1 309 ? 23.177  22.759  19.199 1.000 28.900 0  309 LEU B O   1 
ATOM   5196 C CB  . LEU B 1 309 ? 22.302  25.338  20.537 1.000 29.090 0  309 LEU B CB  1 
ATOM   5197 C CG  . LEU B 1 309 ? 21.107  26.001  21.232 1.000 27.260 0  309 LEU B CG  1 
ATOM   5198 C CD1 . LEU B 1 309 ? 21.005  27.465  20.845 1.000 30.740 0  309 LEU B CD1 1 
ATOM   5199 C CD2 . LEU B 1 309 ? 19.809  25.277  20.918 1.000 29.960 0  309 LEU B CD2 1 
ATOM   5200 N N   . GLN B 1 310 ? 25.006  23.208  20.435 1.000 32.250 0  310 GLN B N   1 
ATOM   5201 C CA  . GLN B 1 310 ? 25.898  22.473  19.546 1.000 30.770 0  310 GLN B CA  1 
ATOM   5202 C C   . GLN B 1 310 ? 25.710  20.966  19.647 1.000 32.820 0  310 GLN B C   1 
ATOM   5203 O O   . GLN B 1 310 ? 26.059  20.244  18.706 1.000 33.800 0  310 GLN B O   1 
ATOM   5204 C CB  . GLN B 1 310 ? 27.352  22.835  19.840 1.000 27.420 0  310 GLN B CB  1 
ATOM   5205 C CG  . GLN B 1 310 ? 27.638  24.324  19.806 1.000 28.840 0  310 GLN B CG  1 
ATOM   5206 C CD  . GLN B 1 310 ? 27.541  24.910  18.408 1.000 29.710 0  310 GLN B CD  1 
ATOM   5207 O OE1 . GLN B 1 310 ? 27.400  24.186  17.423 1.000 30.750 0  310 GLN B OE1 1 
ATOM   5208 N NE2 . GLN B 1 310 ? 27.621  26.230  18.317 1.000 28.340 0  310 GLN B NE2 1 
ATOM   5209 N N   . VAL B 1 311 ? 25.171  20.480  20.759 1.000 31.870 0  311 VAL B N   1 
ATOM   5210 C CA  . VAL B 1 311 ? 25.052  19.049  21.001 1.000 33.080 0  311 VAL B CA  1 
ATOM   5211 C C   . VAL B 1 311 ? 23.606  18.621  21.196 1.000 35.380 0  311 VAL B C   1 
ATOM   5212 O O   . VAL B 1 311 ? 23.289  17.437  20.989 1.000 36.090 0  311 VAL B O   1 
ATOM   5213 C CB  . VAL B 1 311 ? 25.907  18.609  22.213 1.000 31.830 0  311 VAL B CB  1 
ATOM   5214 C CG1 . VAL B 1 311 ? 27.380  18.568  21.835 1.000 35.940 0  311 VAL B CG1 1 
ATOM   5215 C CG2 . VAL B 1 311 ? 25.671  19.534  23.400 1.000 35.180 0  311 VAL B CG2 1 
ATOM   5216 N N   . TRP B 1 312 ? 22.737  19.529  21.606 1.000 36.540 0  312 TRP B N   1 
ATOM   5217 C CA  . TRP B 1 312 ? 21.312  19.284  21.743 1.000 36.320 0  312 TRP B CA  1 
ATOM   5218 C C   . TRP B 1 312 ? 20.727  18.787  20.424 1.000 38.470 0  312 TRP B C   1 
ATOM   5219 O O   . TRP B 1 312 ? 20.833  19.492  19.408 1.000 35.720 0  312 TRP B O   1 
ATOM   5220 C CB  . TRP B 1 312 ? 20.638  20.579  22.173 1.000 34.800 0  312 TRP B CB  1 
ATOM   5221 C CG  . TRP B 1 312 ? 19.188  20.459  22.453 1.000 38.060 0  312 TRP B CG  1 
ATOM   5222 C CD1 . TRP B 1 312 ? 18.159  20.891  21.662 1.000 37.800 0  312 TRP B CD1 1 
ATOM   5223 C CD2 . TRP B 1 312 ? 18.589  19.885  23.616 1.000 39.160 0  312 TRP B CD2 1 
ATOM   5224 N NE1 . TRP B 1 312 ? 16.955  20.614  22.264 1.000 38.290 0  312 TRP B NE1 1 
ATOM   5225 C CE2 . TRP B 1 312 ? 17.192  19.997  23.465 1.000 37.890 0  312 TRP B CE2 1 
ATOM   5226 C CE3 . TRP B 1 312 ? 19.100  19.284  24.772 1.000 35.760 0  312 TRP B CE3 1 
ATOM   5227 C CZ2 . TRP B 1 312 ? 16.300  19.529  24.426 1.000 37.410 0  312 TRP B CZ2 1 
ATOM   5228 C CZ3 . TRP B 1 312 ? 18.214  18.821  25.722 1.000 35.860 0  312 TRP B CZ3 1 
ATOM   5229 C CH2 . TRP B 1 312 ? 16.828  18.946  25.545 1.000 36.230 0  312 TRP B CH2 1 
ATOM   5230 N N   . PRO B 1 313 ? 20.118  17.596  20.387 1.000 40.170 0  313 PRO B N   1 
ATOM   5231 C CA  . PRO B 1 313 ? 19.790  16.990  19.086 1.000 40.120 0  313 PRO B CA  1 
ATOM   5232 C C   . PRO B 1 313 ? 18.708  17.734  18.322 1.000 40.610 0  313 PRO B C   1 
ATOM   5233 O O   . PRO B 1 313 ? 18.741  17.748  17.085 1.000 41.490 0  313 PRO B O   1 
ATOM   5234 C CB  . PRO B 1 313 ? 19.345  15.568  19.457 1.000 37.940 0  313 PRO B CB  1 
ATOM   5235 C CG  . PRO B 1 313 ? 18.938  15.640  20.890 1.000 38.540 0  313 PRO B CG  1 
ATOM   5236 C CD  . PRO B 1 313 ? 19.720  16.752  21.528 1.000 37.580 0  313 PRO B CD  1 
ATOM   5237 N N   . ASP B 1 314 ? 17.748  18.349  19.014 1.000 39.660 0  314 ASP B N   1 
ATOM   5238 C CA  . ASP B 1 314 ? 16.652  19.037  18.341 1.000 41.760 0  314 ASP B CA  1 
ATOM   5239 C C   . ASP B 1 314 ? 17.096  20.279  17.581 1.000 40.270 0  314 ASP B C   1 
ATOM   5240 O O   . ASP B 1 314 ? 16.282  20.864  16.859 1.000 38.480 0  314 ASP B O   1 
ATOM   5241 C CB  . ASP B 1 314 ? 15.575  19.423  19.356 1.000 41.930 0  314 ASP B CB  1 
ATOM   5242 C CG  . ASP B 1 314 ? 14.184  19.050  18.896 1.000 49.050 0  314 ASP B CG  1 
ATOM   5243 O OD1 . ASP B 1 314 ? 14.066  18.279  17.918 1.000 46.660 0  314 ASP B OD1 1 
ATOM   5244 O OD2 . ASP B 1 314 ? 13.206  19.527  19.514 1.000 52.920 -1 314 ASP B OD2 1 
ATOM   5245 N N   . ALA B 1 315 ? 18.355  20.694  17.714 1.000 39.920 0  315 ALA B N   1 
ATOM   5246 C CA  . ALA B 1 315 ? 18.822  21.936  17.115 1.000 38.400 0  315 ALA B CA  1 
ATOM   5247 C C   . ALA B 1 315 ? 19.942  21.719  16.109 1.000 38.250 0  315 ALA B C   1 
ATOM   5248 O O   . ALA B 1 315 ? 20.519  22.701  15.622 1.000 37.900 0  315 ALA B O   1 
ATOM   5249 C CB  . ALA B 1 315 ? 19.278  22.911  18.203 1.000 33.450 0  315 ALA B CB  1 
ATOM   5250 N N   . LYS B 1 316 ? 20.272  20.472  15.787 1.000 39.890 0  316 LYS B N   1 
ATOM   5251 C CA  . LYS B 1 316 ? 21.258  20.216  14.748 1.000 39.270 0  316 LYS B CA  1 
ATOM   5252 C C   . LYS B 1 316 ? 20.734  20.700  13.403 1.000 37.650 0  316 LYS B C   1 
ATOM   5253 O O   . LYS B 1 316 ? 19.548  20.563  13.093 1.000 39.370 0  316 LYS B O   1 
ATOM   5254 C CB  . LYS B 1 316 ? 21.587  18.723  14.693 1.000 39.350 0  316 LYS B CB  1 
ATOM   5255 C CG  . LYS B 1 316 ? 22.611  18.333  13.641 1.000 39.700 0  316 LYS B CG  1 
ATOM   5256 C CD  . LYS B 1 316 ? 22.674  16.820  13.477 1.000 41.670 0  316 LYS B CD  1 
ATOM   5257 C CE  . LYS B 1 316 ? 23.408  16.428  12.202 1.000 42.700 0  316 LYS B CE  1 
ATOM   5258 N NZ  . LYS B 1 316 ? 22.940  17.213  11.026 1.000 41.700 1  316 LYS B NZ  1 
ATOM   5259 N N   . ARG B 1 317 ? 21.597  21.255  12.626 1.000 39.640 0  317 ARG B N   1 
ATOM   5260 C CA  . ARG B 1 317 ? 21.128  21.783  11.356 1.000 38.360 0  317 ARG B CA  1 
ATOM   5261 C C   . ARG B 1 317 ? 21.183  20.703  10.280 1.000 38.420 0  317 ARG B C   1 
ATOM   5262 O O   . ARG B 1 317 ? 22.004  19.784  10.358 1.000 39.450 0  317 ARG B O   1 
ATOM   5263 C CB  . ARG B 1 317 ? 21.974  22.981  10.935 1.000 39.640 0  317 ARG B CB  1 
ATOM   5264 C CG  . ARG B 1 317 ? 22.177  24.003  12.050 1.000 35.790 0  317 ARG B CG  1 
ATOM   5265 C CD  . ARG B 1 317 ? 23.008  25.194  11.598 1.000 33.280 0  317 ARG B CD  1 
ATOM   5266 N NE  . ARG B 1 317 ? 22.748  25.566  10.213 1.000 36.040 0  317 ARG B NE  1 
ATOM   5267 C CZ  . ARG B 1 317 ? 22.117  26.671  9.840  1.000 36.460 0  317 ARG B CZ  1 
ATOM   5268 N NH1 . ARG B 1 317 ? 21.635  27.526  10.727 1.000 34.820 1  317 ARG B NH1 1 
ATOM   5269 N NH2 . ARG B 1 317 ? 21.958  26.923  8.541  1.000 35.140 0  317 ARG B NH2 1 
ATOM   5270 N N   . PRO B 1 318 ? 20.293  20.762  9.288  1.000 41.190 0  318 PRO B N   1 
ATOM   5271 C CA  . PRO B 1 318 ? 20.349  19.764  8.208  1.000 40.410 0  318 PRO B CA  1 
ATOM   5272 C C   . PRO B 1 318 ? 21.685  19.747  7.492  1.000 39.200 0  318 PRO B C   1 
ATOM   5273 O O   . PRO B 1 318 ? 22.180  18.668  7.143  1.000 40.020 0  318 PRO B O   1 
ATOM   5274 C CB  . PRO B 1 318 ? 19.197  20.188  7.289  1.000 44.280 0  318 PRO B CB  1 
ATOM   5275 C CG  . PRO B 1 318 ? 18.220  20.831  8.219  1.000 46.030 0  318 PRO B CG  1 
ATOM   5276 C CD  . PRO B 1 318 ? 19.072  21.585  9.213  1.000 44.210 0  318 PRO B CD  1 
ATOM   5277 N N   . ASP B 1 319 ? 22.284  20.913  7.260  1.000 41.390 0  319 ASP B N   1 
ATOM   5278 C CA  . ASP B 1 319 ? 23.689  20.937  6.888  1.000 37.100 0  319 ASP B CA  1 
ATOM   5279 C C   . ASP B 1 319 ? 24.539  20.693  8.131  1.000 36.570 0  319 ASP B C   1 
ATOM   5280 O O   . ASP B 1 319 ? 24.121  20.949  9.262  1.000 39.580 0  319 ASP B O   1 
ATOM   5281 C CB  . ASP B 1 319 ? 24.071  22.271  6.237  1.000 34.430 0  319 ASP B CB  1 
ATOM   5282 C CG  . ASP B 1 319 ? 23.559  23.479  7.016  1.000 37.540 0  319 ASP B CG  1 
ATOM   5283 O OD1 . ASP B 1 319 ? 23.963  23.657  8.185  1.000 35.970 0  319 ASP B OD1 1 
ATOM   5284 O OD2 . ASP B 1 319 ? 22.773  24.268  6.449  1.000 38.550 -1 319 ASP B OD2 1 
ATOM   5285 N N   . GLY B 1 320 ? 25.760  20.225  7.917  1.000 37.730 0  320 GLY B N   1 
ATOM   5286 C CA  . GLY B 1 320 ? 26.572  19.801  9.043  1.000 39.880 0  320 GLY B CA  1 
ATOM   5287 C C   . GLY B 1 320 ? 27.096  20.916  9.926  1.000 36.570 0  320 GLY B C   1 
ATOM   5288 O O   . GLY B 1 320 ? 27.878  20.666  10.847 1.000 36.580 0  320 GLY B O   1 
ATOM   5289 N N   . LEU B 1 321 ? 26.661  22.145  9.669  1.000 36.180 0  321 LEU B N   1 
ATOM   5290 C CA  . LEU B 1 321 ? 27.292  23.321  10.248 1.000 33.640 0  321 LEU B CA  1 
ATOM   5291 C C   . LEU B 1 321 ? 26.922  23.511  11.715 1.000 33.960 0  321 LEU B C   1 
ATOM   5292 O O   . LEU B 1 321 ? 25.825  23.156  12.161 1.000 35.480 0  321 LEU B O   1 
ATOM   5293 C CB  . LEU B 1 321 ? 26.902  24.559  9.448  1.000 31.320 0  321 LEU B CB  1 
ATOM   5294 C CG  . LEU B 1 321 ? 27.249  24.345  7.977  1.000 31.640 0  321 LEU B CG  1 
ATOM   5295 C CD1 . LEU B 1 321 ? 26.562  25.367  7.121  1.000 29.830 0  321 LEU B CD1 1 
ATOM   5296 C CD2 . LEU B 1 321 ? 28.757  24.408  7.783  1.000 30.230 0  321 LEU B CD2 1 
ATOM   5297 N N   . ALA B 1 322 ? 27.860  24.083  12.462 1.000 31.640 0  322 ALA B N   1 
ATOM   5298 C CA  . ALA B 1 322 ? 27.649  24.402  13.863 1.000 29.190 0  322 ALA B CA  1 
ATOM   5299 C C   . ALA B 1 322 ? 26.759  25.628  14.012 1.000 30.930 0  322 ALA B C   1 
ATOM   5300 O O   . ALA B 1 322 ? 26.775  26.542  13.182 1.000 31.330 0  322 ALA B O   1 
ATOM   5301 C CB  . ALA B 1 322 ? 28.984  24.647  14.565 1.000 30.060 0  322 ALA B CB  1 
ATOM   5302 N N   . GLN B 1 323 ? 25.972  25.634  15.084 1.000 31.400 0  323 GLN B N   1 
ATOM   5303 C CA  . GLN B 1 323 ? 25.140  26.782  15.401 1.000 30.520 0  323 GLN B CA  1 
ATOM   5304 C C   . GLN B 1 323 ? 26.004  27.988  15.756 1.000 31.400 0  323 GLN B C   1 
ATOM   5305 O O   . GLN B 1 323 ? 27.140  27.852  16.217 1.000 31.380 0  323 GLN B O   1 
ATOM   5306 C CB  . GLN B 1 323 ? 24.202  26.451  16.561 1.000 29.550 0  323 GLN B CB  1 
ATOM   5307 C CG  . GLN B 1 323 ? 23.009  25.600  16.172 1.000 30.070 0  323 GLN B CG  1 
ATOM   5308 C CD  . GLN B 1 323 ? 21.698  26.340  16.329 1.000 30.080 0  323 GLN B CD  1 
ATOM   5309 O OE1 . GLN B 1 323 ? 21.681  27.529  16.639 1.000 30.170 0  323 GLN B OE1 1 
ATOM   5310 N NE2 . GLN B 1 323 ? 20.591  25.637  16.126 1.000 30.220 0  323 GLN B NE2 1 
ATOM   5311 N N   . ARG B 1 324 ? 25.457  29.183  15.516 1.000 32.000 0  324 ARG B N   1 
ATOM   5312 C CA  . ARG B 1 324 ? 26.094  30.449  15.876 1.000 31.260 0  324 ARG B CA  1 
ATOM   5313 C C   . ARG B 1 324 ? 25.171  31.235  16.803 1.000 31.540 0  324 ARG B C   1 
ATOM   5314 O O   . ARG B 1 324 ? 24.668  32.305  16.435 1.000 32.670 0  324 ARG B O   1 
ATOM   5315 C CB  . ARG B 1 324 ? 26.421  31.260  14.624 1.000 34.340 0  324 ARG B CB  1 
ATOM   5316 C CG  . ARG B 1 324 ? 27.258  30.507  13.600 1.000 34.250 0  324 ARG B CG  1 
ATOM   5317 C CD  . ARG B 1 324 ? 27.489  31.351  12.359 1.000 31.910 0  324 ARG B CD  1 
ATOM   5318 N NE  . ARG B 1 324 ? 28.189  32.591  12.679 1.000 32.140 0  324 ARG B NE  1 
ATOM   5319 C CZ  . ARG B 1 324 ? 29.483  32.668  12.957 1.000 31.390 0  324 ARG B CZ  1 
ATOM   5320 N NH1 . ARG B 1 324 ? 30.259  31.597  12.939 1.000 31.080 1  324 ARG B NH1 1 
ATOM   5321 N NH2 . ARG B 1 324 ? 30.012  33.851  13.254 1.000 30.650 0  324 ARG B NH2 1 
ATOM   5322 N N   . PRO B 1 325 ? 24.931  30.737  18.016 1.000 31.410 0  325 PRO B N   1 
ATOM   5323 C CA  . PRO B 1 325 ? 23.834  31.259  18.849 1.000 30.620 0  325 PRO B CA  1 
ATOM   5324 C C   . PRO B 1 325 ? 24.219  32.264  19.929 1.000 30.230 0  325 PRO B C   1 
ATOM   5325 O O   . PRO B 1 325 ? 23.324  32.706  20.658 1.000 28.700 0  325 PRO B O   1 
ATOM   5326 C CB  . PRO B 1 325 ? 23.312  29.973  19.499 1.000 27.440 0  325 PRO B CB  1 
ATOM   5327 C CG  . PRO B 1 325 ? 24.562  29.107  19.656 1.000 31.350 0  325 PRO B CG  1 
ATOM   5328 C CD  . PRO B 1 325 ? 25.618  29.622  18.689 1.000 29.320 0  325 PRO B CD  1 
ATOM   5329 N N   . THR B 1 326 ? 25.489  32.637  20.058 1.000 28.090 0  326 THR B N   1 
ATOM   5330 C CA  . THR B 1 326 ? 25.893  33.530  21.139 1.000 28.300 0  326 THR B CA  1 
ATOM   5331 C C   . THR B 1 326 ? 26.506  34.807  20.568 1.000 30.150 0  326 THR B C   1 
ATOM   5332 O O   . THR B 1 326 ? 26.766  34.875  19.360 1.000 31.340 0  326 THR B O   1 
ATOM   5333 C CB  . THR B 1 326 ? 26.883  32.813  22.059 1.000 28.990 0  326 THR B CB  1 
ATOM   5334 O OG1 . THR B 1 326 ? 28.152  32.725  21.403 1.000 30.490 0  326 THR B OG1 1 
ATOM   5335 C CG2 . THR B 1 326 ? 26.385  31.417  22.407 1.000 28.140 0  326 THR B CG2 1 
ATOM   5336 N N   . PRO B 1 327 ? 26.749  35.841  21.384 1.000 27.110 0  327 PRO B N   1 
ATOM   5337 C CA  . PRO B 1 327 ? 27.318  37.084  20.838 1.000 27.470 0  327 PRO B CA  1 
ATOM   5338 C C   . PRO B 1 327 ? 28.793  36.999  20.474 1.000 29.510 0  327 PRO B C   1 
ATOM   5339 O O   . PRO B 1 327 ? 29.337  37.979  19.952 1.000 29.510 0  327 PRO B O   1 
ATOM   5340 C CB  . PRO B 1 327 ? 27.103  38.099  21.970 1.000 29.570 0  327 PRO B CB  1 
ATOM   5341 C CG  . PRO B 1 327 ? 26.923  37.305  23.193 1.000 29.210 0  327 PRO B CG  1 
ATOM   5342 C CD  . PRO B 1 327 ? 26.338  35.993  22.791 1.000 28.120 0  327 PRO B CD  1 
ATOM   5343 N N   . TYR B 1 328 ? 29.469  35.884  20.737 1.000 27.770 0  328 TYR B N   1 
ATOM   5344 C CA  . TYR B 1 328 ? 30.862  35.717  20.353 1.000 30.560 0  328 TYR B CA  1 
ATOM   5345 C C   . TYR B 1 328 ? 31.032  34.394  19.623 1.000 31.600 0  328 TYR B C   1 
ATOM   5346 O O   . TYR B 1 328 ? 30.343  33.413  19.914 1.000 31.690 0  328 TYR B O   1 
ATOM   5347 C CB  . TYR B 1 328 ? 31.810  35.759  21.560 1.000 31.030 0  328 TYR B CB  1 
ATOM   5348 C CG  . TYR B 1 328 ? 31.918  37.106  22.237 1.000 31.100 0  328 TYR B CG  1 
ATOM   5349 C CD1 . TYR B 1 328 ? 30.873  37.607  23.004 1.000 29.050 0  328 TYR B CD1 1 
ATOM   5350 C CD2 . TYR B 1 328 ? 33.073  37.869  22.127 1.000 30.350 0  328 TYR B CD2 1 
ATOM   5351 C CE1 . TYR B 1 328 ? 30.972  38.834  23.629 1.000 29.810 0  328 TYR B CE1 1 
ATOM   5352 C CE2 . TYR B 1 328 ? 33.182  39.098  22.750 1.000 29.420 0  328 TYR B CE2 1 
ATOM   5353 C CZ  . TYR B 1 328 ? 32.128  39.577  23.501 1.000 30.960 0  328 TYR B CZ  1 
ATOM   5354 O OH  . TYR B 1 328 ? 32.227  40.799  24.123 1.000 29.930 0  328 TYR B OH  1 
ATOM   5355 N N   . ASP B 1 329 ? 31.955  34.383  18.664 1.000 31.120 0  329 ASP B N   1 
ATOM   5356 C CA  . ASP B 1 329 ? 32.215  33.181  17.889 1.000 33.380 0  329 ASP B CA  1 
ATOM   5357 C C   . ASP B 1 329 ? 33.174  32.274  18.656 1.000 31.380 0  329 ASP B C   1 
ATOM   5358 O O   . ASP B 1 329 ? 33.603  32.582  19.772 1.000 33.410 0  329 ASP B O   1 
ATOM   5359 C CB  . ASP B 1 329 ? 32.764  33.538  16.504 1.000 31.630 0  329 ASP B CB  1 
ATOM   5360 C CG  . ASP B 1 329 ? 34.079  34.316  16.558 1.000 35.440 0  329 ASP B CG  1 
ATOM   5361 O OD1 . ASP B 1 329 ? 34.604  34.572  17.664 1.000 33.950 0  329 ASP B OD1 1 
ATOM   5362 O OD2 . ASP B 1 329 ? 34.594  34.669  15.473 1.000 34.680 -1 329 ASP B OD2 1 
ATOM   5363 N N   . SER B 1 330 ? 33.516  31.135  18.051 1.000 30.160 0  330 SER B N   1 
ATOM   5364 C CA  . SER B 1 330 ? 34.400  30.178  18.707 1.000 31.130 0  330 SER B CA  1 
ATOM   5365 C C   . SER B 1 330 ? 35.790  30.750  18.955 1.000 32.630 0  330 SER B C   1 
ATOM   5366 O O   . SER B 1 330 ? 36.550  30.182  19.746 1.000 33.140 0  330 SER B O   1 
ATOM   5367 C CB  . SER B 1 330 ? 34.494  28.891  17.883 1.000 31.790 0  330 SER B CB  1 
ATOM   5368 O OG  . SER B 1 330 ? 34.553  29.162  16.494 1.000 32.980 0  330 SER B OG  1 
ATOM   5369 N N   . GLN B 1 331 ? 36.148  31.848  18.295 1.000 32.470 0  331 GLN B N   1 
ATOM   5370 C CA  . GLN B 1 331 ? 37.417  32.519  18.532 1.000 34.980 0  331 GLN B CA  1 
ATOM   5371 C C   . GLN B 1 331 ? 37.311  33.625  19.577 1.000 35.410 0  331 GLN B C   1 
ATOM   5372 O O   . GLN B 1 331 ? 38.249  34.416  19.722 1.000 34.520 0  331 GLN B O   1 
ATOM   5373 C CB  . GLN B 1 331 ? 37.955  33.099  17.222 1.000 34.850 0  331 GLN B CB  1 
ATOM   5374 C CG  . GLN B 1 331 ? 38.300  32.061  16.171 1.000 38.690 0  331 GLN B CG  1 
ATOM   5375 C CD  . GLN B 1 331 ? 39.783  32.023  15.865 1.000 44.560 0  331 GLN B CD  1 
ATOM   5376 O OE1 . GLN B 1 331 ? 40.616  32.242  16.746 1.000 46.160 0  331 GLN B OE1 1 
ATOM   5377 N NE2 . GLN B 1 331 ? 40.122  31.753  14.609 1.000 45.880 0  331 GLN B NE2 1 
ATOM   5378 N N   . LEU B 1 332 ? 36.189  33.695  20.298 1.000 32.190 0  332 LEU B N   1 
ATOM   5379 C CA  . LEU B 1 332 ? 35.953  34.707  21.331 1.000 32.730 0  332 LEU B CA  1 
ATOM   5380 C C   . LEU B 1 332 ? 36.007  36.125  20.763 1.000 34.550 0  332 LEU B C   1 
ATOM   5381 O O   . LEU B 1 332 ? 36.391  37.068  21.457 1.000 36.080 0  332 LEU B O   1 
ATOM   5382 C CB  . LEU B 1 332 ? 36.937  34.560  22.499 1.000 32.310 0  332 LEU B CB  1 
ATOM   5383 C CG  . LEU B 1 332 ? 36.998  33.236  23.272 1.000 31.400 0  332 LEU B CG  1 
ATOM   5384 C CD1 . LEU B 1 332 ? 37.498  33.465  24.690 1.000 29.200 0  332 LEU B CD1 1 
ATOM   5385 C CD2 . LEU B 1 332 ? 35.647  32.537  23.298 1.000 34.240 0  332 LEU B CD2 1 
ATOM   5386 N N   . ARG B 1 333 ? 35.613  36.287  19.497 1.000 32.100 0  333 ARG B N   1 
ATOM   5387 C CA  . ARG B 1 333 ? 35.472  37.568  18.814 1.000 31.340 0  333 ARG B CA  1 
ATOM   5388 C C   . ARG B 1 333 ? 34.008  37.986  18.764 1.000 32.800 0  333 ARG B C   1 
ATOM   5389 O O   . ARG B 1 333 ? 33.130  37.146  18.537 1.000 32.470 0  333 ARG B O   1 
ATOM   5390 C CB  . ARG B 1 333 ? 36.034  37.502  17.393 1.000 33.650 0  333 ARG B CB  1 
ATOM   5391 C CG  . ARG B 1 333 ? 37.250  36.606  17.254 1.000 36.370 0  333 ARG B CG  1 
ATOM   5392 C CD  . ARG B 1 333 ? 37.955  36.824  15.923 1.000 42.070 0  333 ARG B CD  1 
ATOM   5393 N NE  . ARG B 1 333 ? 37.741  35.721  14.993 1.000 43.950 0  333 ARG B NE  1 
ATOM   5394 C CZ  . ARG B 1 333 ? 37.016  35.803  13.886 1.000 44.140 0  333 ARG B CZ  1 
ATOM   5395 N NH1 . ARG B 1 333 ? 36.413  36.930  13.536 1.000 46.790 1  333 ARG B NH1 1 
ATOM   5396 N NH2 . ARG B 1 333 ? 36.896  34.731  13.107 1.000 38.960 0  333 ARG B NH2 1 
ATOM   5397 N N   . PRO B 1 334 ? 33.714  39.269  18.969 1.000 31.760 0  334 PRO B N   1 
ATOM   5398 C CA  . PRO B 1 334 ? 32.312  39.702  19.011 1.000 30.680 0  334 PRO B CA  1 
ATOM   5399 C C   . PRO B 1 334 ? 31.609  39.540  17.671 1.000 30.430 0  334 PRO B C   1 
ATOM   5400 O O   . PRO B 1 334 ? 32.173  39.817  16.609 1.000 29.310 0  334 PRO B O   1 
ATOM   5401 C CB  . PRO B 1 334 ? 32.409  41.179  19.413 1.000 29.390 0  334 PRO B CB  1 
ATOM   5402 C CG  . PRO B 1 334 ? 33.774  41.593  18.988 1.000 29.350 0  334 PRO B CG  1 
ATOM   5403 C CD  . PRO B 1 334 ? 34.643  40.389  19.191 1.000 30.850 0  334 PRO B CD  1 
ATOM   5404 N N   . LYS B 1 335 ? 30.368  39.086  17.742 1.000 30.790 0  335 LYS B N   1 
ATOM   5405 C CA  . LYS B 1 335 ? 29.475  38.928  16.608 1.000 29.010 0  335 LYS B CA  1 
ATOM   5406 C C   . LYS B 1 335 ? 28.477  40.070  16.586 1.000 29.510 0  335 LYS B C   1 
ATOM   5407 O O   . LYS B 1 335 ? 28.330  40.804  17.567 1.000 31.030 0  335 LYS B O   1 
ATOM   5408 C CB  . LYS B 1 335 ? 28.743  37.586  16.698 1.000 28.390 0  335 LYS B CB  1 
ATOM   5409 C CG  . LYS B 1 335 ? 29.631  36.359  16.566 1.000 29.840 0  335 LYS B CG  1 
ATOM   5410 C CD  . LYS B 1 335 ? 28.836  35.073  16.778 1.000 31.100 0  335 LYS B CD  1 
ATOM   5411 C CE  . LYS B 1 335 ? 27.469  35.135  16.102 1.000 31.190 0  335 LYS B CE  1 
ATOM   5412 N NZ  . LYS B 1 335 ? 26.524  34.110  16.629 1.000 30.020 1  335 LYS B NZ  1 
ATOM   5413 N N   . PRO B 1 336 ? 27.764  40.260  15.473 1.000 29.670 0  336 PRO B N   1 
ATOM   5414 C CA  . PRO B 1 336 ? 26.744  41.323  15.437 1.000 31.510 0  336 PRO B CA  1 
ATOM   5415 C C   . PRO B 1 336 ? 25.697  41.213  16.537 1.000 29.980 0  336 PRO B C   1 
ATOM   5416 O O   . PRO B 1 336 ? 25.074  42.228  16.880 1.000 31.600 0  336 PRO B O   1 
ATOM   5417 C CB  . PRO B 1 336 ? 26.117  41.158  14.048 1.000 30.400 0  336 PRO B CB  1 
ATOM   5418 C CG  . PRO B 1 336 ? 27.208  40.571  13.217 1.000 30.390 0  336 PRO B CG  1 
ATOM   5419 C CD  . PRO B 1 336 ? 28.053  39.722  14.131 1.000 29.470 0  336 PRO B CD  1 
ATOM   5420 N N   . MET B 1 337 ? 25.483  40.024  17.108 1.000 30.090 0  337 MET B N   1 
ATOM   5421 C CA  . MET B 1 337 ? 24.512  39.902  18.190 1.000 30.350 0  337 MET B CA  1 
ATOM   5422 C C   . MET B 1 337 ? 24.987  40.620  19.449 1.000 28.460 0  337 MET B C   1 
ATOM   5423 O O   . MET B 1 337 ? 24.162  41.127  20.217 1.000 30.640 0  337 MET B O   1 
ATOM   5424 C CB  . MET B 1 337 ? 24.217  38.426  18.480 1.000 29.660 0  337 MET B CB  1 
ATOM   5425 C CG  . MET B 1 337 ? 23.593  38.162  19.850 1.000 29.570 0  337 MET B CG  1 
ATOM   5426 S SD  . MET B 1 337 ? 23.532  36.421  20.306 1.000 31.070 0  337 MET B SD  1 
ATOM   5427 C CE  . MET B 1 337 ? 23.066  35.691  18.738 1.000 27.770 0  337 MET B CE  1 
ATOM   5428 N N   . ARG B 1 338 ? 26.301  40.683  19.679 1.000 28.100 0  338 ARG B N   1 
ATOM   5429 C CA  . ARG B 1 338 ? 26.813  41.478  20.791 1.000 30.010 0  338 ARG B CA  1 
ATOM   5430 C C   . ARG B 1 338 ? 26.446  42.947  20.631 1.000 30.640 0  338 ARG B C   1 
ATOM   5431 O O   . ARG B 1 338 ? 26.019  43.600  21.593 1.000 29.520 0  338 ARG B O   1 
ATOM   5432 C CB  . ARG B 1 338 ? 28.331  41.323  20.892 1.000 29.640 0  338 ARG B CB  1 
ATOM   5433 C CG  . ARG B 1 338 ? 28.894  41.639  22.265 1.000 28.900 0  338 ARG B CG  1 
ATOM   5434 C CD  . ARG B 1 338 ? 29.940  42.738  22.200 1.000 28.040 0  338 ARG B CD  1 
ATOM   5435 N NE  . ARG B 1 338 ? 30.345  43.172  23.532 1.000 27.970 0  338 ARG B NE  1 
ATOM   5436 C CZ  . ARG B 1 338 ? 30.245  44.416  23.979 1.000 27.990 0  338 ARG B CZ  1 
ATOM   5437 N NH1 . ARG B 1 338 ? 29.781  45.390  23.214 1.000 28.090 1  338 ARG B NH1 1 
ATOM   5438 N NH2 . ARG B 1 338 ? 30.617  44.688  25.226 1.000 27.930 0  338 ARG B NH2 1 
ATOM   5439 N N   . GLU B 1 339 ? 26.607  43.482  19.418 1.000 31.670 0  339 GLU B N   1 
ATOM   5440 C CA  . GLU B 1 339 ? 26.201  44.856  19.151 1.000 31.990 0  339 GLU B CA  1 
ATOM   5441 C C   . GLU B 1 339 ? 24.698  45.026  19.319 1.000 31.810 0  339 GLU B C   1 
ATOM   5442 O O   . GLU B 1 339 ? 24.242  46.037  19.859 1.000 35.460 0  339 GLU B O   1 
ATOM   5443 C CB  . GLU B 1 339 ? 26.643  45.275  17.749 1.000 33.430 0  339 GLU B CB  1 
ATOM   5444 C CG  . GLU B 1 339 ? 26.303  46.721  17.368 1.000 38.390 0  339 GLU B CG  1 
ATOM   5445 C CD  . GLU B 1 339 ? 26.441  47.711  18.522 1.000 39.210 0  339 GLU B CD  1 
ATOM   5446 O OE1 . GLU B 1 339 ? 27.520  47.762  19.153 1.000 38.640 0  339 GLU B OE1 1 
ATOM   5447 O OE2 . GLU B 1 339 ? 25.466  48.447  18.788 1.000 37.350 -1 339 GLU B OE2 1 
ATOM   5448 N N   . ALA B 1 340 ? 23.909  44.055  18.854 1.000 29.090 0  340 ALA B N   1 
ATOM   5449 C CA  . ALA B 1 340 ? 22.462  44.137  19.043 1.000 28.760 0  340 ALA B CA  1 
ATOM   5450 C C   . ALA B 1 340 ? 22.098  44.188  20.522 1.000 30.570 0  340 ALA B C   1 
ATOM   5451 O O   . ALA B 1 340 ? 21.246  44.988  20.934 1.000 31.920 0  340 ALA B O   1 
ATOM   5452 C CB  . ALA B 1 340 ? 21.774  42.954  18.361 1.000 29.100 0  340 ALA B CB  1 
ATOM   5453 N N   . ILE B 1 341 ? 22.735  43.344  21.338 1.000 29.230 0  341 ILE B N   1 
ATOM   5454 C CA  . ILE B 1 341 ? 22.445  43.332  22.769 1.000 30.100 0  341 ILE B CA  1 
ATOM   5455 C C   . ILE B 1 341 ? 22.839  44.662  23.396 1.000 31.830 0  341 ILE B C   1 
ATOM   5456 O O   . ILE B 1 341 ? 22.076  45.246  24.173 1.000 31.000 0  341 ILE B O   1 
ATOM   5457 C CB  . ILE B 1 341 ? 23.160  42.155  23.460 1.000 31.040 0  341 ILE B CB  1 
ATOM   5458 C CG1 . ILE B 1 341 ? 22.492  40.825  23.100 1.000 29.610 0  341 ILE B CG1 1 
ATOM   5459 C CG2 . ILE B 1 341 ? 23.170  42.352  24.974 1.000 27.930 0  341 ILE B CG2 1 
ATOM   5460 C CD1 . ILE B 1 341 ? 23.279  39.600  23.540 1.000 29.050 0  341 ILE B CD1 1 
ATOM   5461 N N   . ALA B 1 342 ? 24.028  45.169  23.051 1.000 30.970 0  342 ALA B N   1 
ATOM   5462 C CA  . ALA B 1 342 ? 24.463  46.462  23.572 1.000 30.290 0  342 ALA B CA  1 
ATOM   5463 C C   . ALA B 1 342 ? 23.493  47.565  23.173 1.000 33.600 0  342 ALA B C   1 
ATOM   5464 O O   . ALA B 1 342 ? 23.220  48.484  23.957 1.000 35.550 0  342 ALA B O   1 
ATOM   5465 C CB  . ALA B 1 342 ? 25.873  46.783  23.081 1.000 32.260 0  342 ALA B CB  1 
ATOM   5466 N N   . ALA B 1 343 ? 22.962  47.486  21.952 1.000 34.300 0  343 ALA B N   1 
ATOM   5467 C CA  . ALA B 1 343 ? 22.000  48.473  21.482 1.000 34.480 0  343 ALA B CA  1 
ATOM   5468 C C   . ALA B 1 343 ? 20.727  48.436  22.314 1.000 32.100 0  343 ALA B C   1 
ATOM   5469 O O   . ALA B 1 343 ? 20.249  49.472  22.791 1.000 31.540 0  343 ALA B O   1 
ATOM   5470 C CB  . ALA B 1 343 ? 21.686  48.219  20.006 1.000 31.840 0  343 ALA B CB  1 
ATOM   5471 N N   . SER B 1 344 ? 20.165  47.241  22.503 1.000 30.870 0  344 SER B N   1 
ATOM   5472 C CA  . SER B 1 344 ? 18.951  47.125  23.303 1.000 31.550 0  344 SER B CA  1 
ATOM   5473 C C   . SER B 1 344 ? 19.188  47.542  24.750 1.000 32.120 0  344 SER B C   1 
ATOM   5474 O O   . SER B 1 344 ? 18.276  48.067  25.401 1.000 31.590 0  344 SER B O   1 
ATOM   5475 C CB  . SER B 1 344 ? 18.407  45.699  23.231 1.000 28.470 0  344 SER B CB  1 
ATOM   5476 O OG  . SER B 1 344 ? 17.923  45.414  21.931 1.000 28.420 0  344 SER B OG  1 
ATOM   5477 N N   . LEU B 1 345 ? 20.398  47.314  25.268 1.000 29.110 0  345 LEU B N   1 
ATOM   5478 C CA  . LEU B 1 345 ? 20.711  47.722  26.634 1.000 28.570 0  345 LEU B CA  1 
ATOM   5479 C C   . LEU B 1 345 ? 20.820  49.239  26.748 1.000 30.430 0  345 LEU B C   1 
ATOM   5480 O O   . LEU B 1 345 ? 20.441  49.820  27.772 1.000 29.200 0  345 LEU B O   1 
ATOM   5481 C CB  . LEU B 1 345 ? 22.017  47.069  27.099 1.000 30.680 0  345 LEU B CB  1 
ATOM   5482 C CG  . LEU B 1 345 ? 22.183  45.547  27.196 1.000 29.020 0  345 LEU B CG  1 
ATOM   5483 C CD1 . LEU B 1 345 ? 23.624  45.191  27.552 1.000 30.010 0  345 LEU B CD1 1 
ATOM   5484 C CD2 . LEU B 1 345 ? 21.221  44.911  28.173 1.000 26.180 0  345 LEU B CD2 1 
ATOM   5485 N N   . ARG B 1 346 ? 21.343  49.898  25.711 1.000 31.150 0  346 ARG B N   1 
ATOM   5486 C CA  . ARG B 1 346 ? 21.480  51.351  25.755 1.000 27.680 0  346 ARG B CA  1 
ATOM   5487 C C   . ARG B 1 346 ? 20.124  52.041  25.658 1.000 30.270 0  346 ARG B C   1 
ATOM   5488 O O   . ARG B 1 346 ? 19.888  53.055  26.325 1.000 31.740 0  346 ARG B O   1 
ATOM   5489 C CB  . ARG B 1 346 ? 22.412  51.818  24.641 1.000 29.870 0  346 ARG B CB  1 
ATOM   5490 C CG  . ARG B 1 346 ? 23.890  51.644  24.966 1.000 32.610 0  346 ARG B CG  1 
ATOM   5491 C CD  . ARG B 1 346 ? 24.771  52.263  23.894 1.000 32.260 0  346 ARG B CD  1 
ATOM   5492 N NE  . ARG B 1 346 ? 25.458  51.242  23.110 1.000 37.090 0  346 ARG B NE  1 
ATOM   5493 C CZ  . ARG B 1 346 ? 25.127  50.906  21.870 1.000 36.610 0  346 ARG B CZ  1 
ATOM   5494 N NH1 . ARG B 1 346 ? 24.100  51.467  21.253 1.000 35.360 1  346 ARG B NH1 1 
ATOM   5495 N NH2 . ARG B 1 346 ? 25.834  49.974  21.240 1.000 35.750 0  346 ARG B NH2 1 
ATOM   5496 N N   . ALA B 1 347 ? 19.225  51.513  24.834 1.000 30.480 0  347 ALA B N   1 
ATOM   5497 C CA  . ALA B 1 347 ? 17.960  52.169  24.536 1.000 29.480 0  347 ALA B CA  1 
ATOM   5498 C C   . ALA B 1 347 ? 16.835  51.762  25.477 1.000 29.020 0  347 ALA B C   1 
ATOM   5499 O O   . ALA B 1 347 ? 15.719  52.275  25.340 1.000 30.250 0  347 ALA B O   1 
ATOM   5500 C CB  . ALA B 1 347 ? 17.545  51.879  23.090 1.000 32.330 0  347 ALA B CB  1 
ATOM   5501 N N   . MET B 1 348 ? 17.089  50.858  26.416 1.000 28.840 0  348 MET B N   1 
ATOM   5502 C CA  . MET B 1 348 ? 15.997  50.370  27.242 1.000 30.240 0  348 MET B CA  1 
ATOM   5503 C C   . MET B 1 348 ? 15.704  51.344  28.384 1.000 29.280 0  348 MET B C   1 
ATOM   5504 O O   . MET B 1 348 ? 16.591  52.080  28.826 1.000 28.790 0  348 MET B O   1 
ATOM   5505 C CB  . MET B 1 348 ? 16.333  48.997  27.811 1.000 28.170 0  348 MET B CB  1 
ATOM   5506 C CG  . MET B 1 348 ? 17.355  49.020  28.928 1.000 28.180 0  348 MET B CG  1 
ATOM   5507 S SD  . MET B 1 348 ? 17.561  47.406  29.705 1.000 29.790 0  348 MET B SD  1 
ATOM   5508 C CE  . MET B 1 348 ? 19.337  47.343  29.899 1.000 30.600 0  348 MET B CE  1 
ATOM   5509 N N   . PRO B 1 349 ? 14.465  51.377  28.868 1.000 26.570 0  349 PRO B N   1 
ATOM   5510 C CA  . PRO B 1 349 ? 14.148  52.252  30.004 1.000 28.180 0  349 PRO B CA  1 
ATOM   5511 C C   . PRO B 1 349 ? 14.894  51.829  31.262 1.000 30.030 0  349 PRO B C   1 
ATOM   5512 O O   . PRO B 1 349 ? 15.242  50.660  31.443 1.000 30.990 0  349 PRO B O   1 
ATOM   5513 C CB  . PRO B 1 349 ? 12.631  52.095  30.180 1.000 28.300 0  349 PRO B CB  1 
ATOM   5514 C CG  . PRO B 1 349 ? 12.137  51.345  29.003 1.000 30.060 0  349 PRO B CG  1 
ATOM   5515 C CD  . PRO B 1 349 ? 13.283  50.704  28.304 1.000 27.990 0  349 PRO B CD  1 
ATOM   5516 N N   . MET B 1 350 ? 15.141  52.810  32.131 1.000 29.370 0  350 MET B N   1 
ATOM   5517 C CA  . MET B 1 350 ? 15.709  52.540  33.445 1.000 28.380 0  350 MET B CA  1 
ATOM   5518 C C   . MET B 1 350 ? 14.847  51.538  34.202 1.000 27.400 0  350 MET B C   1 
ATOM   5519 O O   . MET B 1 350 ? 13.620  51.662  34.234 1.000 26.510 0  350 MET B O   1 
ATOM   5520 C CB  . MET B 1 350 ? 15.810  53.844  34.240 1.000 28.920 0  350 MET B CB  1 
ATOM   5521 C CG  . MET B 1 350 ? 16.824  53.854  35.375 1.000 28.660 0  350 MET B CG  1 
ATOM   5522 S SD  . MET B 1 350 ? 18.544  53.874  34.842 1.000 32.800 0  350 MET B SD  1 
ATOM   5523 C CE  . MET B 1 350 ? 19.370  53.819  36.430 1.000 28.920 0  350 MET B CE  1 
ATOM   5524 N N   . ARG B 1 351 ? 15.492  50.546  34.814 1.000 28.200 0  351 ARG B N   1 
ATOM   5525 C CA  . ARG B 1 351 ? 14.762  49.580  35.622 1.000 29.970 0  351 ARG B CA  1 
ATOM   5526 C C   . ARG B 1 351 ? 14.146  50.251  36.844 1.000 28.420 0  351 ARG B C   1 
ATOM   5527 O O   . ARG B 1 351 ? 14.607  51.294  37.312 1.000 27.350 0  351 ARG B O   1 
ATOM   5528 C CB  . ARG B 1 351 ? 15.662  48.428  36.078 1.000 29.810 0  351 ARG B CB  1 
ATOM   5529 C CG  . ARG B 1 351 ? 16.780  48.036  35.135 1.000 32.680 0  351 ARG B CG  1 
ATOM   5530 C CD  . ARG B 1 351 ? 16.294  47.214  33.953 1.000 31.420 0  351 ARG B CD  1 
ATOM   5531 N NE  . ARG B 1 351 ? 15.741  48.050  32.895 1.000 30.410 0  351 ARG B NE  1 
ATOM   5532 C CZ  . ARG B 1 351 ? 14.782  47.670  32.062 1.000 31.240 0  351 ARG B CZ  1 
ATOM   5533 N NH1 . ARG B 1 351 ? 14.252  46.458  32.126 1.000 28.510 1  351 ARG B NH1 1 
ATOM   5534 N NH2 . ARG B 1 351 ? 14.354  48.522  31.135 1.000 30.000 0  351 ARG B NH2 1 
ATOM   5535 N N   . LYS B 1 352 ? 13.075  49.642  37.346 1.000 28.690 0  352 LYS B N   1 
ATOM   5536 C CA  . LYS B 1 352 ? 12.453  50.107  38.575 1.000 26.750 0  352 LYS B CA  1 
ATOM   5537 C C   . LYS B 1 352 ? 13.412  49.916  39.746 1.000 26.040 0  352 LYS B C   1 
ATOM   5538 O O   . LYS B 1 352 ? 14.201  48.968  39.785 1.000 26.010 0  352 LYS B O   1 
ATOM   5539 C CB  . LYS B 1 352 ? 11.146  49.348  38.811 1.000 25.920 0  352 LYS B CB  1 
ATOM   5540 C CG  . LYS B 1 352 ? 10.447  49.611  40.135 1.000 26.010 0  352 LYS B CG  1 
ATOM   5541 C CD  . LYS B 1 352 ? 9.174   48.781  40.227 1.000 26.280 0  352 LYS B CD  1 
ATOM   5542 C CE  . LYS B 1 352 ? 8.499   48.909  41.584 1.000 31.320 0  352 LYS B CE  1 
ATOM   5543 N NZ  . LYS B 1 352 ? 7.427   47.884  41.773 1.000 29.870 1  352 LYS B NZ  1 
ATOM   5544 N N   . ALA B 1 353 ? 13.344  50.837  40.702 1.000 27.690 0  353 ALA B N   1 
ATOM   5545 C CA  . ALA B 1 353 ? 14.273  50.855  41.822 1.000 26.280 0  353 ALA B CA  1 
ATOM   5546 C C   . ALA B 1 353 ? 13.849  49.867  42.902 1.000 26.180 0  353 ALA B C   1 
ATOM   5547 O O   . ALA B 1 353 ? 14.436  48.793  43.035 1.000 26.050 0  353 ALA B O   1 
ATOM   5548 C CB  . ALA B 1 353 ? 14.375  52.260  42.398 1.000 26.530 0  353 ALA B CB  1 
HETATM 5549 O O   . HOH C 2 .   ? -12.213 -4.181  4.938  1.000 37.730 0  401 HOH A O   1 
HETATM 5550 O O   . HOH C 2 .   ? -2.484  -17.161 24.807 1.000 31.190 0  402 HOH A O   1 
HETATM 5551 O O   . HOH C 2 .   ? 21.914  3.218   6.723  1.000 31.180 0  403 HOH A O   1 
HETATM 5552 O O   . HOH C 2 .   ? 2.652   4.820   15.247 1.000 19.260 0  404 HOH A O   1 
HETATM 5553 O O   . HOH C 2 .   ? 23.392  -6.216  3.712  1.000 35.080 0  405 HOH A O   1 
HETATM 5554 O O   . HOH C 2 .   ? 24.097  -0.795  17.600 1.000 29.090 0  406 HOH A O   1 
HETATM 5555 O O   . HOH C 2 .   ? 8.623   -3.086  -8.267 1.000 30.880 0  407 HOH A O   1 
HETATM 5556 O O   . HOH C 2 .   ? 18.018  -18.722 15.648 1.000 29.880 0  408 HOH A O   1 
HETATM 5557 O O   . HOH C 2 .   ? -6.141  -15.715 20.521 1.000 25.030 0  409 HOH A O   1 
HETATM 5558 O O   . HOH C 2 .   ? -9.673  10.384  19.289 1.000 24.630 0  410 HOH A O   1 
HETATM 5559 O O   . HOH C 2 .   ? 3.059   2.009   5.003  1.000 22.370 0  411 HOH A O   1 
HETATM 5560 O O   . HOH C 2 .   ? 15.756  13.946  5.854  1.000 41.760 0  412 HOH A O   1 
HETATM 5561 O O   . HOH C 2 .   ? 19.755  -12.057 27.531 1.000 27.400 0  413 HOH A O   1 
HETATM 5562 O O   . HOH C 2 .   ? 17.952  -17.898 12.770 1.000 26.700 0  414 HOH A O   1 
HETATM 5563 O O   . HOH C 2 .   ? 5.118   16.258  11.211 1.000 25.620 0  415 HOH A O   1 
HETATM 5564 O O   . HOH C 2 .   ? 21.641  -11.283 6.467  1.000 35.490 0  416 HOH A O   1 
HETATM 5565 O O   . HOH C 2 .   ? 11.171  1.330   31.832 1.000 31.980 0  417 HOH A O   1 
HETATM 5566 O O   . HOH C 2 .   ? -18.199 20.093  8.928  1.000 26.530 0  418 HOH A O   1 
HETATM 5567 O O   . HOH C 2 .   ? -2.683  8.511   5.309  1.000 23.790 0  419 HOH A O   1 
HETATM 5568 O O   . HOH C 2 .   ? 1.149   20.493  6.889  1.000 26.110 0  420 HOH A O   1 
HETATM 5569 O O   . HOH C 2 .   ? -18.205 0.615   25.313 1.000 26.310 0  421 HOH A O   1 
HETATM 5570 O O   . HOH C 2 .   ? 7.140   -14.355 7.935  1.000 28.500 0  422 HOH A O   1 
HETATM 5571 O O   . HOH C 2 .   ? -4.459  -11.499 8.819  1.000 25.500 0  423 HOH A O   1 
HETATM 5572 O O   . HOH C 2 .   ? -12.588 -0.145  29.779 1.000 24.620 0  424 HOH A O   1 
HETATM 5573 O O   . HOH C 2 .   ? 1.191   12.540  9.836  1.000 26.240 0  425 HOH A O   1 
HETATM 5574 O O   . HOH C 2 .   ? -15.712 -6.185  8.573  1.000 27.790 0  426 HOH A O   1 
HETATM 5575 O O   . HOH C 2 .   ? 4.881   5.841   19.214 1.000 25.220 0  427 HOH A O   1 
HETATM 5576 O O   . HOH C 2 .   ? -14.452 24.383  12.964 1.000 24.760 0  428 HOH A O   1 
HETATM 5577 O O   . HOH C 2 .   ? 4.865   12.093  7.588  1.000 28.330 0  429 HOH A O   1 
HETATM 5578 O O   . HOH C 2 .   ? -2.835  -9.913  12.073 1.000 28.910 0  430 HOH A O   1 
HETATM 5579 O O   . HOH C 2 .   ? -4.608  -11.611 11.065 1.000 29.180 0  431 HOH A O   1 
HETATM 5580 O O   . HOH C 2 .   ? 11.160  -11.082 0.729  1.000 27.730 0  432 HOH A O   1 
HETATM 5581 O O   . HOH C 2 .   ? -18.563 0.571   4.879  1.000 27.940 0  433 HOH A O   1 
HETATM 5582 O O   . HOH C 2 .   ? 16.143  7.353   -6.686 1.000 28.580 0  434 HOH A O   1 
HETATM 5583 O O   . HOH C 2 .   ? -2.610  25.843  10.856 1.000 23.770 0  435 HOH A O   1 
HETATM 5584 O O   . HOH C 2 .   ? -9.762  4.717   31.100 1.000 25.670 0  436 HOH A O   1 
HETATM 5585 O O   . HOH C 2 .   ? 4.908   6.290   15.760 1.000 20.540 0  437 HOH A O   1 
HETATM 5586 O O   . HOH D 2 .   ? 25.296  11.889  46.477 1.000 26.870 0  401 HOH B O   1 
HETATM 5587 O O   . HOH D 2 .   ? 30.235  28.232  47.558 1.000 31.060 0  402 HOH B O   1 
HETATM 5588 O O   . HOH D 2 .   ? 23.893  27.576  40.045 1.000 29.120 0  403 HOH B O   1 
HETATM 5589 O O   . HOH D 2 .   ? -3.246  30.978  19.051 1.000 28.100 0  404 HOH B O   1 
HETATM 5590 O O   . HOH D 2 .   ? 5.408   44.908  12.878 1.000 33.440 0  405 HOH B O   1 
HETATM 5591 O O   . HOH D 2 .   ? 24.509  21.682  13.492 1.000 32.510 0  406 HOH B O   1 
HETATM 5592 O O   . HOH D 2 .   ? 33.672  27.900  14.670 1.000 25.380 0  407 HOH B O   1 
HETATM 5593 O O   . HOH D 2 .   ? 10.808  20.110  33.802 1.000 26.560 0  408 HOH B O   1 
HETATM 5594 O O   . HOH D 2 .   ? 8.002   29.884  18.942 1.000 33.430 0  409 HOH B O   1 
HETATM 5595 O O   . HOH D 2 .   ? 11.136  32.168  23.517 1.000 24.560 0  410 HOH B O   1 
HETATM 5596 O O   . HOH D 2 .   ? 22.892  44.057  42.012 1.000 28.440 0  411 HOH B O   1 
HETATM 5597 O O   . HOH D 2 .   ? 11.564  37.969  18.884 1.000 30.400 0  412 HOH B O   1 
HETATM 5598 O O   . HOH D 2 .   ? 35.311  23.662  31.284 1.000 29.050 0  413 HOH B O   1 
HETATM 5599 O O   . HOH D 2 .   ? 18.221  38.429  40.774 1.000 22.790 0  414 HOH B O   1 
HETATM 5600 O O   . HOH D 2 .   ? 40.934  18.135  28.302 1.000 32.610 0  415 HOH B O   1 
HETATM 5601 O O   . HOH D 2 .   ? 9.117   5.363   42.708 1.000 29.160 0  416 HOH B O   1 
HETATM 5602 O O   . HOH D 2 .   ? 20.944  30.937  49.364 1.000 32.800 0  417 HOH B O   1 
HETATM 5603 O O   . HOH D 2 .   ? 3.845   43.366  14.495 1.000 33.740 0  418 HOH B O   1 
HETATM 5604 O O   . HOH D 2 .   ? 30.636  16.473  24.244 1.000 40.590 0  419 HOH B O   1 
HETATM 5605 O O   . HOH D 2 .   ? 19.511  21.931  43.433 1.000 22.740 0  420 HOH B O   1 
HETATM 5606 O O   . HOH D 2 .   ? 22.357  17.970  30.877 1.000 31.130 0  421 HOH B O   1 
HETATM 5607 O O   . HOH D 2 .   ? 27.005  37.369  2.938  1.000 32.900 0  422 HOH B O   1 
HETATM 5608 O O   . HOH D 2 .   ? 18.745  44.600  42.486 1.000 25.330 0  423 HOH B O   1 
HETATM 5609 O O   . HOH D 2 .   ? 11.597  32.318  27.248 1.000 23.700 0  424 HOH B O   1 
HETATM 5610 O O   . HOH D 2 .   ? 1.748   24.359  18.547 1.000 26.530 0  425 HOH B O   1 
HETATM 5611 O O   . HOH D 2 .   ? 26.656  36.274  44.955 1.000 27.560 0  426 HOH B O   1 
HETATM 5612 O O   . HOH D 2 .   ? 29.326  20.639  42.108 1.000 24.250 0  427 HOH B O   1 
HETATM 5613 O O   . HOH D 2 .   ? 28.471  18.026  10.396 1.000 27.700 0  428 HOH B O   1 
HETATM 5614 O O   . HOH D 2 .   ? 28.042  51.462  34.453 1.000 33.470 0  429 HOH B O   1 
HETATM 5615 O O   . HOH D 2 .   ? -5.581  31.072  41.073 1.000 28.860 0  430 HOH B O   1 
HETATM 5616 O O   . HOH D 2 .   ? 8.865   38.240  50.430 1.000 25.980 0  431 HOH B O   1 
HETATM 5617 O O   . HOH D 2 .   ? 28.476  21.720  32.757 1.000 29.910 0  432 HOH B O   1 
HETATM 5618 O O   . HOH D 2 .   ? 0.020   35.433  26.151 1.000 28.610 0  433 HOH B O   1 
HETATM 5619 O O   . HOH D 2 .   ? 19.434  17.890  37.988 1.000 23.530 0  434 HOH B O   1 
HETATM 5620 O O   . HOH D 2 .   ? 30.091  28.660  13.254 1.000 26.210 0  435 HOH B O   1 
HETATM 5621 O O   . HOH D 2 .   ? 11.708  27.071  23.681 1.000 32.410 0  436 HOH B O   1 
HETATM 5622 O O   . HOH D 2 .   ? 17.678  28.533  21.626 1.000 31.700 0  437 HOH B O   1 
HETATM 5623 O O   . HOH D 2 .   ? 6.883   39.845  9.541  1.000 29.870 0  438 HOH B O   1 
HETATM 5624 O O   . HOH D 2 .   ? 19.954  37.027  39.846 1.000 23.920 0  439 HOH B O   1 
HETATM 5625 O O   . HOH D 2 .   ? 5.230   25.753  23.662 1.000 24.150 0  440 HOH B O   1 
HETATM 5626 O O   . HOH D 2 .   ? 10.763  13.651  28.551 1.000 37.390 0  441 HOH B O   1 
HETATM 5627 O O   . HOH D 2 .   ? 38.657  22.185  43.339 1.000 26.210 0  442 HOH B O   1 
HETATM 5628 O O   . HOH D 2 .   ? 18.365  40.169  43.125 1.000 25.920 0  443 HOH B O   1 
HETATM 5629 O O   . HOH D 2 .   ? 19.127  24.440  31.641 1.000 19.980 0  444 HOH B O   1 
# 
