data_8ZUB
# 
_entry.id   8ZUB 
# 
_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   8ZUB         pdb_00008zub 10.2210/pdb8zub/pdb 
WWPDB D_1300048505 ?            ?                   
# 
_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                        8ZUB 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-08 
_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           N 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8ZT9 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              948805786@qq.com 
_pdbx_contact_author.name_first         Ming 
_pdbx_contact_author.name_last          Yan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6340-6759 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Yan, M.'   1 ? 
'Zhang, H.' 2 ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Chem. 
_citation.journal_id_ASTM           BOCMBM 
_citation.journal_id_CSD            0368 
_citation.journal_id_ISSN           0045-2068 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            154 
_citation.language                  ? 
_citation.page_first                107988 
_citation.page_last                 107988 
_citation.title                     
;Development of pyrimidone derivatives as nonpeptidic and noncovalent 3-chymotrypsin-like protease (3CL pro ) inhibitors with anti-coronavirus activities.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bioorg.2024.107988 
_citation.pdbx_database_id_PubMed   39591689 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pan, F.'   1  ? 
primary 'Zhou, Q.'  2  ? 
primary 'Yan, M.'   3  ? 
primary 'Yang, S.'  4  ? 
primary 'Hu, R.'    5  ? 
primary 'Chen, Y.'  6  ? 
primary 'Wen, Y.'   7  ? 
primary 'Chao, Y.'  8  ? 
primary 'Xie, C.'   9  ? 
primary 'Ou, W.'    10 ? 
primary 'Li, Y.'    11 ? 
primary 'Zhang, H.' 12 ? 
primary 'Guo, D.'   13 ? 
primary 'Zhang, X.' 14 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase' 33292.965 2   3.4.22.69 ? ? ? 
2 non-polymer syn 
;6-[(6-chloranyl-2-pentyl-indazol-5-yl)amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
586.996   2   ?         ? ? ? 
3 water       nat water 18.015    534 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO, 3CLp, Main protease, Mpro, Non-structural protein 5, nsp5, SARS coronavirus main proteinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;6-[(6-chloranyl-2-pentyl-indazol-5-yl)amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
A1D80 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
# 
_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                   301 
_entity_src_gen.gene_src_common_name               '2019-nCoV, SARS-CoV-2' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
A1D80 non-polymer         . 
;6-[(6-chloranyl-2-pentyl-indazol-5-yl)amino]-3-[(1-methyl-1,2,4-triazol-3-yl)methyl]-1-[[2,4,5-tris(fluoranyl)phenyl]methyl]pyrimidine-2,4-dione
;
? 'C27 H26 Cl F3 N8 O2' 586.996 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
B 1 1   SER 1   1   ?   ?   ?   B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS 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 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1D80 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1D80 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1D80 1   401 401 A1D80 LIG A . 
D 2 A1D80 1   401 401 A1D80 LIG B . 
E 3 HOH   1   501 472 HOH   HOH A . 
E 3 HOH   2   502 512 HOH   HOH A . 
E 3 HOH   3   503 70  HOH   HOH A . 
E 3 HOH   4   504 418 HOH   HOH A . 
E 3 HOH   5   505 531 HOH   HOH A . 
E 3 HOH   6   506 514 HOH   HOH A . 
E 3 HOH   7   507 490 HOH   HOH A . 
E 3 HOH   8   508 538 HOH   HOH A . 
E 3 HOH   9   509 356 HOH   HOH A . 
E 3 HOH   10  510 484 HOH   HOH A . 
E 3 HOH   11  511 109 HOH   HOH A . 
E 3 HOH   12  512 352 HOH   HOH A . 
E 3 HOH   13  513 491 HOH   HOH A . 
E 3 HOH   14  514 337 HOH   HOH A . 
E 3 HOH   15  515 279 HOH   HOH A . 
E 3 HOH   16  516 494 HOH   HOH A . 
E 3 HOH   17  517 233 HOH   HOH A . 
E 3 HOH   18  518 282 HOH   HOH A . 
E 3 HOH   19  519 469 HOH   HOH A . 
E 3 HOH   20  520 471 HOH   HOH A . 
E 3 HOH   21  521 317 HOH   HOH A . 
E 3 HOH   22  522 135 HOH   HOH A . 
E 3 HOH   23  523 422 HOH   HOH A . 
E 3 HOH   24  524 529 HOH   HOH A . 
E 3 HOH   25  525 53  HOH   HOH A . 
E 3 HOH   26  526 269 HOH   HOH A . 
E 3 HOH   27  527 495 HOH   HOH A . 
E 3 HOH   28  528 136 HOH   HOH A . 
E 3 HOH   29  529 202 HOH   HOH A . 
E 3 HOH   30  530 523 HOH   HOH A . 
E 3 HOH   31  531 316 HOH   HOH A . 
E 3 HOH   32  532 283 HOH   HOH A . 
E 3 HOH   33  533 335 HOH   HOH A . 
E 3 HOH   34  534 90  HOH   HOH A . 
E 3 HOH   35  535 463 HOH   HOH A . 
E 3 HOH   36  536 411 HOH   HOH A . 
E 3 HOH   37  537 217 HOH   HOH A . 
E 3 HOH   38  538 539 HOH   HOH A . 
E 3 HOH   39  539 462 HOH   HOH A . 
E 3 HOH   40  540 110 HOH   HOH A . 
E 3 HOH   41  541 487 HOH   HOH A . 
E 3 HOH   42  542 483 HOH   HOH A . 
E 3 HOH   43  543 313 HOH   HOH A . 
E 3 HOH   44  544 15  HOH   HOH A . 
E 3 HOH   45  545 306 HOH   HOH A . 
E 3 HOH   46  546 339 HOH   HOH A . 
E 3 HOH   47  547 80  HOH   HOH A . 
E 3 HOH   48  548 16  HOH   HOH A . 
E 3 HOH   49  549 111 HOH   HOH A . 
E 3 HOH   50  550 280 HOH   HOH A . 
E 3 HOH   51  551 127 HOH   HOH A . 
E 3 HOH   52  552 75  HOH   HOH A . 
E 3 HOH   53  553 303 HOH   HOH A . 
E 3 HOH   54  554 489 HOH   HOH A . 
E 3 HOH   55  555 535 HOH   HOH A . 
E 3 HOH   56  556 530 HOH   HOH A . 
E 3 HOH   57  557 77  HOH   HOH A . 
E 3 HOH   58  558 439 HOH   HOH A . 
E 3 HOH   59  559 209 HOH   HOH A . 
E 3 HOH   60  560 434 HOH   HOH A . 
E 3 HOH   61  561 271 HOH   HOH A . 
E 3 HOH   62  562 125 HOH   HOH A . 
E 3 HOH   63  563 416 HOH   HOH A . 
E 3 HOH   64  564 395 HOH   HOH A . 
E 3 HOH   65  565 8   HOH   HOH A . 
E 3 HOH   66  566 35  HOH   HOH A . 
E 3 HOH   67  567 368 HOH   HOH A . 
E 3 HOH   68  568 453 HOH   HOH A . 
E 3 HOH   69  569 133 HOH   HOH A . 
E 3 HOH   70  570 9   HOH   HOH A . 
E 3 HOH   71  571 239 HOH   HOH A . 
E 3 HOH   72  572 343 HOH   HOH A . 
E 3 HOH   73  573 319 HOH   HOH A . 
E 3 HOH   74  574 143 HOH   HOH A . 
E 3 HOH   75  575 79  HOH   HOH A . 
E 3 HOH   76  576 208 HOH   HOH A . 
E 3 HOH   77  577 536 HOH   HOH A . 
E 3 HOH   78  578 85  HOH   HOH A . 
E 3 HOH   79  579 296 HOH   HOH A . 
E 3 HOH   80  580 91  HOH   HOH A . 
E 3 HOH   81  581 23  HOH   HOH A . 
E 3 HOH   82  582 201 HOH   HOH A . 
E 3 HOH   83  583 396 HOH   HOH A . 
E 3 HOH   84  584 405 HOH   HOH A . 
E 3 HOH   85  585 126 HOH   HOH A . 
E 3 HOH   86  586 65  HOH   HOH A . 
E 3 HOH   87  587 66  HOH   HOH A . 
E 3 HOH   88  588 26  HOH   HOH A . 
E 3 HOH   89  589 399 HOH   HOH A . 
E 3 HOH   90  590 198 HOH   HOH A . 
E 3 HOH   91  591 367 HOH   HOH A . 
E 3 HOH   92  592 286 HOH   HOH A . 
E 3 HOH   93  593 377 HOH   HOH A . 
E 3 HOH   94  594 107 HOH   HOH A . 
E 3 HOH   95  595 470 HOH   HOH A . 
E 3 HOH   96  596 177 HOH   HOH A . 
E 3 HOH   97  597 426 HOH   HOH A . 
E 3 HOH   98  598 166 HOH   HOH A . 
E 3 HOH   99  599 20  HOH   HOH A . 
E 3 HOH   100 600 4   HOH   HOH A . 
E 3 HOH   101 601 543 HOH   HOH A . 
E 3 HOH   102 602 141 HOH   HOH A . 
E 3 HOH   103 603 389 HOH   HOH A . 
E 3 HOH   104 604 281 HOH   HOH A . 
E 3 HOH   105 605 254 HOH   HOH A . 
E 3 HOH   106 606 260 HOH   HOH A . 
E 3 HOH   107 607 28  HOH   HOH A . 
E 3 HOH   108 608 315 HOH   HOH A . 
E 3 HOH   109 609 137 HOH   HOH A . 
E 3 HOH   110 610 171 HOH   HOH A . 
E 3 HOH   111 611 458 HOH   HOH A . 
E 3 HOH   112 612 322 HOH   HOH A . 
E 3 HOH   113 613 62  HOH   HOH A . 
E 3 HOH   114 614 447 HOH   HOH A . 
E 3 HOH   115 615 144 HOH   HOH A . 
E 3 HOH   116 616 361 HOH   HOH A . 
E 3 HOH   117 617 186 HOH   HOH A . 
E 3 HOH   118 618 180 HOH   HOH A . 
E 3 HOH   119 619 43  HOH   HOH A . 
E 3 HOH   120 620 370 HOH   HOH A . 
E 3 HOH   121 621 358 HOH   HOH A . 
E 3 HOH   122 622 430 HOH   HOH A . 
E 3 HOH   123 623 345 HOH   HOH A . 
E 3 HOH   124 624 105 HOH   HOH A . 
E 3 HOH   125 625 46  HOH   HOH A . 
E 3 HOH   126 626 400 HOH   HOH A . 
E 3 HOH   127 627 187 HOH   HOH A . 
E 3 HOH   128 628 445 HOH   HOH A . 
E 3 HOH   129 629 170 HOH   HOH A . 
E 3 HOH   130 630 123 HOH   HOH A . 
E 3 HOH   131 631 121 HOH   HOH A . 
E 3 HOH   132 632 448 HOH   HOH A . 
E 3 HOH   133 633 355 HOH   HOH A . 
E 3 HOH   134 634 73  HOH   HOH A . 
E 3 HOH   135 635 151 HOH   HOH A . 
E 3 HOH   136 636 428 HOH   HOH A . 
E 3 HOH   137 637 120 HOH   HOH A . 
E 3 HOH   138 638 76  HOH   HOH A . 
E 3 HOH   139 639 192 HOH   HOH A . 
E 3 HOH   140 640 115 HOH   HOH A . 
E 3 HOH   141 641 211 HOH   HOH A . 
E 3 HOH   142 642 363 HOH   HOH A . 
E 3 HOH   143 643 60  HOH   HOH A . 
E 3 HOH   144 644 235 HOH   HOH A . 
E 3 HOH   145 645 42  HOH   HOH A . 
E 3 HOH   146 646 357 HOH   HOH A . 
E 3 HOH   147 647 21  HOH   HOH A . 
E 3 HOH   148 648 18  HOH   HOH A . 
E 3 HOH   149 649 318 HOH   HOH A . 
E 3 HOH   150 650 108 HOH   HOH A . 
E 3 HOH   151 651 117 HOH   HOH A . 
E 3 HOH   152 652 394 HOH   HOH A . 
E 3 HOH   153 653 275 HOH   HOH A . 
E 3 HOH   154 654 244 HOH   HOH A . 
E 3 HOH   155 655 385 HOH   HOH A . 
E 3 HOH   156 656 168 HOH   HOH A . 
E 3 HOH   157 657 178 HOH   HOH A . 
E 3 HOH   158 658 122 HOH   HOH A . 
E 3 HOH   159 659 24  HOH   HOH A . 
E 3 HOH   160 660 392 HOH   HOH A . 
E 3 HOH   161 661 101 HOH   HOH A . 
E 3 HOH   162 662 270 HOH   HOH A . 
E 3 HOH   163 663 148 HOH   HOH A . 
E 3 HOH   164 664 5   HOH   HOH A . 
E 3 HOH   165 665 114 HOH   HOH A . 
E 3 HOH   166 666 488 HOH   HOH A . 
E 3 HOH   167 667 27  HOH   HOH A . 
E 3 HOH   168 668 360 HOH   HOH A . 
E 3 HOH   169 669 3   HOH   HOH A . 
E 3 HOH   170 670 52  HOH   HOH A . 
E 3 HOH   171 671 321 HOH   HOH A . 
E 3 HOH   172 672 55  HOH   HOH A . 
E 3 HOH   173 673 182 HOH   HOH A . 
E 3 HOH   174 674 311 HOH   HOH A . 
E 3 HOH   175 675 242 HOH   HOH A . 
E 3 HOH   176 676 213 HOH   HOH A . 
E 3 HOH   177 677 230 HOH   HOH A . 
E 3 HOH   178 678 183 HOH   HOH A . 
E 3 HOH   179 679 152 HOH   HOH A . 
E 3 HOH   180 680 477 HOH   HOH A . 
E 3 HOH   181 681 517 HOH   HOH A . 
E 3 HOH   182 682 155 HOH   HOH A . 
E 3 HOH   183 683 165 HOH   HOH A . 
E 3 HOH   184 684 92  HOH   HOH A . 
E 3 HOH   185 685 63  HOH   HOH A . 
E 3 HOH   186 686 215 HOH   HOH A . 
E 3 HOH   187 687 516 HOH   HOH A . 
E 3 HOH   188 688 1   HOH   HOH A . 
E 3 HOH   189 689 429 HOH   HOH A . 
E 3 HOH   190 690 97  HOH   HOH A . 
E 3 HOH   191 691 106 HOH   HOH A . 
E 3 HOH   192 692 485 HOH   HOH A . 
E 3 HOH   193 693 404 HOH   HOH A . 
E 3 HOH   194 694 359 HOH   HOH A . 
E 3 HOH   195 695 441 HOH   HOH A . 
E 3 HOH   196 696 139 HOH   HOH A . 
E 3 HOH   197 697 172 HOH   HOH A . 
E 3 HOH   198 698 425 HOH   HOH A . 
E 3 HOH   199 699 332 HOH   HOH A . 
E 3 HOH   200 700 56  HOH   HOH A . 
E 3 HOH   201 701 225 HOH   HOH A . 
E 3 HOH   202 702 252 HOH   HOH A . 
E 3 HOH   203 703 431 HOH   HOH A . 
E 3 HOH   204 704 38  HOH   HOH A . 
E 3 HOH   205 705 310 HOH   HOH A . 
E 3 HOH   206 706 272 HOH   HOH A . 
E 3 HOH   207 707 220 HOH   HOH A . 
E 3 HOH   208 708 493 HOH   HOH A . 
E 3 HOH   209 709 263 HOH   HOH A . 
E 3 HOH   210 710 250 HOH   HOH A . 
E 3 HOH   211 711 452 HOH   HOH A . 
E 3 HOH   212 712 222 HOH   HOH A . 
E 3 HOH   213 713 116 HOH   HOH A . 
E 3 HOH   214 714 336 HOH   HOH A . 
E 3 HOH   215 715 59  HOH   HOH A . 
E 3 HOH   216 716 460 HOH   HOH A . 
E 3 HOH   217 717 534 HOH   HOH A . 
E 3 HOH   218 718 353 HOH   HOH A . 
E 3 HOH   219 719 527 HOH   HOH A . 
E 3 HOH   220 720 240 HOH   HOH A . 
E 3 HOH   221 721 232 HOH   HOH A . 
E 3 HOH   222 722 537 HOH   HOH A . 
E 3 HOH   223 723 436 HOH   HOH A . 
E 3 HOH   224 724 309 HOH   HOH A . 
E 3 HOH   225 725 435 HOH   HOH A . 
E 3 HOH   226 726 174 HOH   HOH A . 
E 3 HOH   227 727 486 HOH   HOH A . 
E 3 HOH   228 728 380 HOH   HOH A . 
E 3 HOH   229 729 443 HOH   HOH A . 
E 3 HOH   230 730 410 HOH   HOH A . 
E 3 HOH   231 731 351 HOH   HOH A . 
E 3 HOH   232 732 478 HOH   HOH A . 
E 3 HOH   233 733 176 HOH   HOH A . 
E 3 HOH   234 734 446 HOH   HOH A . 
E 3 HOH   235 735 440 HOH   HOH A . 
E 3 HOH   236 736 444 HOH   HOH A . 
E 3 HOH   237 737 401 HOH   HOH A . 
E 3 HOH   238 738 289 HOH   HOH A . 
E 3 HOH   239 739 234 HOH   HOH A . 
E 3 HOH   240 740 290 HOH   HOH A . 
E 3 HOH   241 741 437 HOH   HOH A . 
E 3 HOH   242 742 147 HOH   HOH A . 
E 3 HOH   243 743 420 HOH   HOH A . 
E 3 HOH   244 744 451 HOH   HOH A . 
E 3 HOH   245 745 521 HOH   HOH A . 
E 3 HOH   246 746 314 HOH   HOH A . 
E 3 HOH   247 747 145 HOH   HOH A . 
E 3 HOH   248 748 406 HOH   HOH A . 
E 3 HOH   249 749 391 HOH   HOH A . 
E 3 HOH   250 750 93  HOH   HOH A . 
E 3 HOH   251 751 390 HOH   HOH A . 
E 3 HOH   252 752 331 HOH   HOH A . 
E 3 HOH   253 753 255 HOH   HOH A . 
E 3 HOH   254 754 140 HOH   HOH A . 
E 3 HOH   255 755 338 HOH   HOH A . 
E 3 HOH   256 756 188 HOH   HOH A . 
E 3 HOH   257 757 432 HOH   HOH A . 
E 3 HOH   258 758 532 HOH   HOH A . 
E 3 HOH   259 759 433 HOH   HOH A . 
E 3 HOH   260 760 196 HOH   HOH A . 
E 3 HOH   261 761 408 HOH   HOH A . 
E 3 HOH   262 762 294 HOH   HOH A . 
E 3 HOH   263 763 438 HOH   HOH A . 
E 3 HOH   264 764 161 HOH   HOH A . 
E 3 HOH   265 765 256 HOH   HOH A . 
E 3 HOH   266 766 312 HOH   HOH A . 
E 3 HOH   267 767 371 HOH   HOH A . 
E 3 HOH   268 768 258 HOH   HOH A . 
E 3 HOH   269 769 393 HOH   HOH A . 
E 3 HOH   270 770 520 HOH   HOH A . 
E 3 HOH   271 771 295 HOH   HOH A . 
E 3 HOH   272 772 266 HOH   HOH A . 
E 3 HOH   273 773 200 HOH   HOH A . 
E 3 HOH   274 774 265 HOH   HOH A . 
E 3 HOH   275 775 102 HOH   HOH A . 
E 3 HOH   276 776 344 HOH   HOH A . 
E 3 HOH   277 777 243 HOH   HOH A . 
E 3 HOH   278 778 383 HOH   HOH A . 
E 3 HOH   279 779 398 HOH   HOH A . 
E 3 HOH   280 780 449 HOH   HOH A . 
E 3 HOH   281 781 298 HOH   HOH A . 
E 3 HOH   282 782 533 HOH   HOH A . 
E 3 HOH   283 783 179 HOH   HOH A . 
E 3 HOH   284 784 354 HOH   HOH A . 
E 3 HOH   285 785 454 HOH   HOH A . 
E 3 HOH   286 786 374 HOH   HOH A . 
E 3 HOH   287 787 376 HOH   HOH A . 
E 3 HOH   288 788 300 HOH   HOH A . 
F 3 HOH   1   501 501 HOH   HOH B . 
F 3 HOH   2   502 511 HOH   HOH B . 
F 3 HOH   3   503 421 HOH   HOH B . 
F 3 HOH   4   504 508 HOH   HOH B . 
F 3 HOH   5   505 467 HOH   HOH B . 
F 3 HOH   6   506 304 HOH   HOH B . 
F 3 HOH   7   507 231 HOH   HOH B . 
F 3 HOH   8   508 191 HOH   HOH B . 
F 3 HOH   9   509 259 HOH   HOH B . 
F 3 HOH   10  510 505 HOH   HOH B . 
F 3 HOH   11  511 528 HOH   HOH B . 
F 3 HOH   12  512 330 HOH   HOH B . 
F 3 HOH   13  513 513 HOH   HOH B . 
F 3 HOH   14  514 459 HOH   HOH B . 
F 3 HOH   15  515 362 HOH   HOH B . 
F 3 HOH   16  516 503 HOH   HOH B . 
F 3 HOH   17  517 274 HOH   HOH B . 
F 3 HOH   18  518 305 HOH   HOH B . 
F 3 HOH   19  519 30  HOH   HOH B . 
F 3 HOH   20  520 89  HOH   HOH B . 
F 3 HOH   21  521 45  HOH   HOH B . 
F 3 HOH   22  522 86  HOH   HOH B . 
F 3 HOH   23  523 326 HOH   HOH B . 
F 3 HOH   24  524 346 HOH   HOH B . 
F 3 HOH   25  525 327 HOH   HOH B . 
F 3 HOH   26  526 497 HOH   HOH B . 
F 3 HOH   27  527 349 HOH   HOH B . 
F 3 HOH   28  528 397 HOH   HOH B . 
F 3 HOH   29  529 475 HOH   HOH B . 
F 3 HOH   30  530 162 HOH   HOH B . 
F 3 HOH   31  531 81  HOH   HOH B . 
F 3 HOH   32  532 207 HOH   HOH B . 
F 3 HOH   33  533 185 HOH   HOH B . 
F 3 HOH   34  534 509 HOH   HOH B . 
F 3 HOH   35  535 57  HOH   HOH B . 
F 3 HOH   36  536 492 HOH   HOH B . 
F 3 HOH   37  537 365 HOH   HOH B . 
F 3 HOH   38  538 350 HOH   HOH B . 
F 3 HOH   39  539 138 HOH   HOH B . 
F 3 HOH   40  540 277 HOH   HOH B . 
F 3 HOH   41  541 409 HOH   HOH B . 
F 3 HOH   42  542 88  HOH   HOH B . 
F 3 HOH   43  543 402 HOH   HOH B . 
F 3 HOH   44  544 94  HOH   HOH B . 
F 3 HOH   45  545 47  HOH   HOH B . 
F 3 HOH   46  546 364 HOH   HOH B . 
F 3 HOH   47  547 83  HOH   HOH B . 
F 3 HOH   48  548 41  HOH   HOH B . 
F 3 HOH   49  549 31  HOH   HOH B . 
F 3 HOH   50  550 224 HOH   HOH B . 
F 3 HOH   51  551 366 HOH   HOH B . 
F 3 HOH   52  552 149 HOH   HOH B . 
F 3 HOH   53  553 130 HOH   HOH B . 
F 3 HOH   54  554 193 HOH   HOH B . 
F 3 HOH   55  555 403 HOH   HOH B . 
F 3 HOH   56  556 156 HOH   HOH B . 
F 3 HOH   57  557 153 HOH   HOH B . 
F 3 HOH   58  558 333 HOH   HOH B . 
F 3 HOH   59  559 119 HOH   HOH B . 
F 3 HOH   60  560 82  HOH   HOH B . 
F 3 HOH   61  561 423 HOH   HOH B . 
F 3 HOH   62  562 348 HOH   HOH B . 
F 3 HOH   63  563 194 HOH   HOH B . 
F 3 HOH   64  564 474 HOH   HOH B . 
F 3 HOH   65  565 173 HOH   HOH B . 
F 3 HOH   66  566 100 HOH   HOH B . 
F 3 HOH   67  567 381 HOH   HOH B . 
F 3 HOH   68  568 154 HOH   HOH B . 
F 3 HOH   69  569 39  HOH   HOH B . 
F 3 HOH   70  570 540 HOH   HOH B . 
F 3 HOH   71  571 297 HOH   HOH B . 
F 3 HOH   72  572 456 HOH   HOH B . 
F 3 HOH   73  573 251 HOH   HOH B . 
F 3 HOH   74  574 157 HOH   HOH B . 
F 3 HOH   75  575 461 HOH   HOH B . 
F 3 HOH   76  576 164 HOH   HOH B . 
F 3 HOH   77  577 427 HOH   HOH B . 
F 3 HOH   78  578 268 HOH   HOH B . 
F 3 HOH   79  579 206 HOH   HOH B . 
F 3 HOH   80  580 32  HOH   HOH B . 
F 3 HOH   81  581 197 HOH   HOH B . 
F 3 HOH   82  582 189 HOH   HOH B . 
F 3 HOH   83  583 261 HOH   HOH B . 
F 3 HOH   84  584 95  HOH   HOH B . 
F 3 HOH   85  585 419 HOH   HOH B . 
F 3 HOH   86  586 96  HOH   HOH B . 
F 3 HOH   87  587 160 HOH   HOH B . 
F 3 HOH   88  588 500 HOH   HOH B . 
F 3 HOH   89  589 466 HOH   HOH B . 
F 3 HOH   90  590 481 HOH   HOH B . 
F 3 HOH   91  591 246 HOH   HOH B . 
F 3 HOH   92  592 14  HOH   HOH B . 
F 3 HOH   93  593 12  HOH   HOH B . 
F 3 HOH   94  594 184 HOH   HOH B . 
F 3 HOH   95  595 212 HOH   HOH B . 
F 3 HOH   96  596 40  HOH   HOH B . 
F 3 HOH   97  597 542 HOH   HOH B . 
F 3 HOH   98  598 324 HOH   HOH B . 
F 3 HOH   99  599 302 HOH   HOH B . 
F 3 HOH   100 600 247 HOH   HOH B . 
F 3 HOH   101 601 49  HOH   HOH B . 
F 3 HOH   102 602 34  HOH   HOH B . 
F 3 HOH   103 603 67  HOH   HOH B . 
F 3 HOH   104 604 13  HOH   HOH B . 
F 3 HOH   105 605 325 HOH   HOH B . 
F 3 HOH   106 606 10  HOH   HOH B . 
F 3 HOH   107 607 190 HOH   HOH B . 
F 3 HOH   108 608 104 HOH   HOH B . 
F 3 HOH   109 609 214 HOH   HOH B . 
F 3 HOH   110 610 7   HOH   HOH B . 
F 3 HOH   111 611 457 HOH   HOH B . 
F 3 HOH   112 612 25  HOH   HOH B . 
F 3 HOH   113 613 262 HOH   HOH B . 
F 3 HOH   114 614 44  HOH   HOH B . 
F 3 HOH   115 615 69  HOH   HOH B . 
F 3 HOH   116 616 216 HOH   HOH B . 
F 3 HOH   117 617 17  HOH   HOH B . 
F 3 HOH   118 618 384 HOH   HOH B . 
F 3 HOH   119 619 372 HOH   HOH B . 
F 3 HOH   120 620 181 HOH   HOH B . 
F 3 HOH   121 621 19  HOH   HOH B . 
F 3 HOH   122 622 267 HOH   HOH B . 
F 3 HOH   123 623 36  HOH   HOH B . 
F 3 HOH   124 624 50  HOH   HOH B . 
F 3 HOH   125 625 113 HOH   HOH B . 
F 3 HOH   126 626 169 HOH   HOH B . 
F 3 HOH   127 627 98  HOH   HOH B . 
F 3 HOH   128 628 504 HOH   HOH B . 
F 3 HOH   129 629 146 HOH   HOH B . 
F 3 HOH   130 630 61  HOH   HOH B . 
F 3 HOH   131 631 68  HOH   HOH B . 
F 3 HOH   132 632 51  HOH   HOH B . 
F 3 HOH   133 633 29  HOH   HOH B . 
F 3 HOH   134 634 58  HOH   HOH B . 
F 3 HOH   135 635 328 HOH   HOH B . 
F 3 HOH   136 636 163 HOH   HOH B . 
F 3 HOH   137 637 128 HOH   HOH B . 
F 3 HOH   138 638 71  HOH   HOH B . 
F 3 HOH   139 639 6   HOH   HOH B . 
F 3 HOH   140 640 245 HOH   HOH B . 
F 3 HOH   141 641 203 HOH   HOH B . 
F 3 HOH   142 642 131 HOH   HOH B . 
F 3 HOH   143 643 204 HOH   HOH B . 
F 3 HOH   144 644 455 HOH   HOH B . 
F 3 HOH   145 645 195 HOH   HOH B . 
F 3 HOH   146 646 524 HOH   HOH B . 
F 3 HOH   147 647 273 HOH   HOH B . 
F 3 HOH   148 648 299 HOH   HOH B . 
F 3 HOH   149 649 87  HOH   HOH B . 
F 3 HOH   150 650 64  HOH   HOH B . 
F 3 HOH   151 651 496 HOH   HOH B . 
F 3 HOH   152 652 506 HOH   HOH B . 
F 3 HOH   153 653 379 HOH   HOH B . 
F 3 HOH   154 654 278 HOH   HOH B . 
F 3 HOH   155 655 205 HOH   HOH B . 
F 3 HOH   156 656 526 HOH   HOH B . 
F 3 HOH   157 657 54  HOH   HOH B . 
F 3 HOH   158 658 33  HOH   HOH B . 
F 3 HOH   159 659 142 HOH   HOH B . 
F 3 HOH   160 660 37  HOH   HOH B . 
F 3 HOH   161 661 22  HOH   HOH B . 
F 3 HOH   162 662 11  HOH   HOH B . 
F 3 HOH   163 663 223 HOH   HOH B . 
F 3 HOH   164 664 236 HOH   HOH B . 
F 3 HOH   165 665 167 HOH   HOH B . 
F 3 HOH   166 666 219 HOH   HOH B . 
F 3 HOH   167 667 382 HOH   HOH B . 
F 3 HOH   168 668 84  HOH   HOH B . 
F 3 HOH   169 669 72  HOH   HOH B . 
F 3 HOH   170 670 347 HOH   HOH B . 
F 3 HOH   171 671 292 HOH   HOH B . 
F 3 HOH   172 672 129 HOH   HOH B . 
F 3 HOH   173 673 525 HOH   HOH B . 
F 3 HOH   174 674 134 HOH   HOH B . 
F 3 HOH   175 675 407 HOH   HOH B . 
F 3 HOH   176 676 276 HOH   HOH B . 
F 3 HOH   177 677 442 HOH   HOH B . 
F 3 HOH   178 678 307 HOH   HOH B . 
F 3 HOH   179 679 308 HOH   HOH B . 
F 3 HOH   180 680 132 HOH   HOH B . 
F 3 HOH   181 681 340 HOH   HOH B . 
F 3 HOH   182 682 248 HOH   HOH B . 
F 3 HOH   183 683 424 HOH   HOH B . 
F 3 HOH   184 684 342 HOH   HOH B . 
F 3 HOH   185 685 158 HOH   HOH B . 
F 3 HOH   186 686 334 HOH   HOH B . 
F 3 HOH   187 687 48  HOH   HOH B . 
F 3 HOH   188 688 112 HOH   HOH B . 
F 3 HOH   189 689 293 HOH   HOH B . 
F 3 HOH   190 690 2   HOH   HOH B . 
F 3 HOH   191 691 468 HOH   HOH B . 
F 3 HOH   192 692 329 HOH   HOH B . 
F 3 HOH   193 693 320 HOH   HOH B . 
F 3 HOH   194 694 510 HOH   HOH B . 
F 3 HOH   195 695 387 HOH   HOH B . 
F 3 HOH   196 696 175 HOH   HOH B . 
F 3 HOH   197 697 218 HOH   HOH B . 
F 3 HOH   198 698 373 HOH   HOH B . 
F 3 HOH   199 699 417 HOH   HOH B . 
F 3 HOH   200 700 253 HOH   HOH B . 
F 3 HOH   201 701 99  HOH   HOH B . 
F 3 HOH   202 702 285 HOH   HOH B . 
F 3 HOH   203 703 388 HOH   HOH B . 
F 3 HOH   204 704 544 HOH   HOH B . 
F 3 HOH   205 705 499 HOH   HOH B . 
F 3 HOH   206 706 323 HOH   HOH B . 
F 3 HOH   207 707 341 HOH   HOH B . 
F 3 HOH   208 708 226 HOH   HOH B . 
F 3 HOH   209 709 413 HOH   HOH B . 
F 3 HOH   210 710 476 HOH   HOH B . 
F 3 HOH   211 711 124 HOH   HOH B . 
F 3 HOH   212 712 159 HOH   HOH B . 
F 3 HOH   213 713 541 HOH   HOH B . 
F 3 HOH   214 714 415 HOH   HOH B . 
F 3 HOH   215 715 249 HOH   HOH B . 
F 3 HOH   216 716 264 HOH   HOH B . 
F 3 HOH   217 717 150 HOH   HOH B . 
F 3 HOH   218 718 237 HOH   HOH B . 
F 3 HOH   219 719 210 HOH   HOH B . 
F 3 HOH   220 720 288 HOH   HOH B . 
F 3 HOH   221 721 284 HOH   HOH B . 
F 3 HOH   222 722 369 HOH   HOH B . 
F 3 HOH   223 723 498 HOH   HOH B . 
F 3 HOH   224 724 227 HOH   HOH B . 
F 3 HOH   225 725 291 HOH   HOH B . 
F 3 HOH   226 726 103 HOH   HOH B . 
F 3 HOH   227 727 518 HOH   HOH B . 
F 3 HOH   228 728 522 HOH   HOH B . 
F 3 HOH   229 729 118 HOH   HOH B . 
F 3 HOH   230 730 74  HOH   HOH B . 
F 3 HOH   231 731 229 HOH   HOH B . 
F 3 HOH   232 732 301 HOH   HOH B . 
F 3 HOH   233 733 287 HOH   HOH B . 
F 3 HOH   234 734 414 HOH   HOH B . 
F 3 HOH   235 735 473 HOH   HOH B . 
F 3 HOH   236 736 375 HOH   HOH B . 
F 3 HOH   237 737 221 HOH   HOH B . 
F 3 HOH   238 738 228 HOH   HOH B . 
F 3 HOH   239 739 257 HOH   HOH B . 
F 3 HOH   240 740 199 HOH   HOH B . 
F 3 HOH   241 741 238 HOH   HOH B . 
F 3 HOH   242 742 78  HOH   HOH B . 
F 3 HOH   243 743 412 HOH   HOH B . 
F 3 HOH   244 744 378 HOH   HOH B . 
F 3 HOH   245 745 386 HOH   HOH B . 
F 3 HOH   246 746 450 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A TYR 154 ? CG  ? A TYR 154 CG  
2  1 Y 1 A TYR 154 ? CD1 ? A TYR 154 CD1 
3  1 Y 1 A TYR 154 ? CD2 ? A TYR 154 CD2 
4  1 Y 1 A TYR 154 ? CE1 ? A TYR 154 CE1 
5  1 Y 1 A TYR 154 ? CE2 ? A TYR 154 CE2 
6  1 Y 1 A TYR 154 ? CZ  ? A TYR 154 CZ  
7  1 Y 1 A TYR 154 ? OH  ? A TYR 154 OH  
8  1 Y 1 B TYR 154 ? CG  ? B TYR 154 CG  
9  1 Y 1 B TYR 154 ? CD1 ? B TYR 154 CD1 
10 1 Y 1 B TYR 154 ? CD2 ? B TYR 154 CD2 
11 1 Y 1 B TYR 154 ? CE1 ? B TYR 154 CE1 
12 1 Y 1 B TYR 154 ? CE2 ? B TYR 154 CE2 
13 1 Y 1 B TYR 154 ? CZ  ? B TYR 154 CZ  
14 1 Y 1 B TYR 154 ? OH  ? B TYR 154 OH  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0415 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.07 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZUB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.579 
_cell.length_a_esd                 ? 
_cell.length_b                     99.369 
_cell.length_b_esd                 ? 
_cell.length_c                     58.620 
_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                         8ZUB 
_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                   8ZUB 
_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             2.31 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.85 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Ammonium acetate, 15% (w/v) PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-01 
_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   0.979 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          17.50 
_reflns.entry_id                                       8ZUB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               48.66 
_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                                     55963 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.87 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.96 
_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                                   1 
_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                                    1.8 
_reflns_shell.d_res_low                                     1.864 
_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                             2857 
_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                                  0.996 
_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]                            -0.53 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -1.12 
_refine.aniso_B[2][2]                            -0.14 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            1.15 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.110 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE 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                                 8ZUB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             48.65 
_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                     53106 
_refine.ls_number_reflns_R_free                  2857 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15236 
_refine.ls_R_factor_R_free                       0.18751 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15044 
_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 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_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       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.113 
_refine.pdbx_overall_ESU_R_Free                  0.109 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_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                             2.251 
_refine.overall_SU_ML                            0.071 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        48.65 
_refine_hist.number_atoms_solvent             534 
_refine_hist.number_atoms_total               5255 
_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        4721 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.011  4925  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4527  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.590  1.655  6724  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.546  1.575  10415 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.685  5.000  627   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 22.710 7.308  26    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.597 10.000 779   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.077  0.200  746   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.010  0.020  5924  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1166  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.142  1.826  2463  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.142  1.826  2463  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.195  3.267  3096  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.195  3.268  3097  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.262  2.186  2462  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.261  2.186  2463  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.044  3.826  3626  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.708  21.51  5584  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.587  19.56  5439  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             203 
_refine_ls_shell.number_reflns_R_work             3892 
_refine_ls_shell.percent_reflns_obs               99.73 
_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                  0.181 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_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                  0.234 
# 
_struct.entry_id                     8ZUB 
_struct.title                        'The Crystal structure of mol075 bound to the main protease (3CLpro/Mpro) of SARS-CoV-2' 
_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        8ZUB 
_struct_keywords.text            'Inhibitor, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCS
;
_struct_ref.pdbx_align_begin           3264 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZUB A 1 ? 301 ? P0DTD1 3264 ? 3564 ? 1 301 
2 1 8ZUB B 1 ? 301 ? P0DTD1 3264 ? 3564 ? 1 301 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2170  ? 
1 MORE         -7    ? 
1 'SSA (A^2)'  25330 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 THR A 45  ? ASN A 51  ? THR A 45  ASN A 51  1 ? 7  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P15 AB6 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P16 AB7 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P17 AB8 THR B 226 ? LYS B 236 ? THR B 226 LYS B 236 1 ? 11 
HELX_P HELX_P18 AB9 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P19 AC1 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P20 AC2 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P21 AC3 THR B 292 ? SER B 301 ? THR B 292 SER B 301 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 LEU B 67  ? ALA B 70  ? LEU B 67  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 LYS B 100 ? PHE B 103 ? LYS B 100 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 18  O GLY A 29  ? O GLY A 29  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 88  ? O LYS A 88  N SER A 81  ? N SER A 81  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O CYS A 156 ? O CYS A 156 N ASP A 153 ? N ASP A 153 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 18  ? N VAL B 18  O GLY B 29  ? O GLY B 29  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N VAL B 36  ? N VAL B 36  O LEU B 89  ? O LEU B 89  
AA4 6 7 O LYS B 90  ? O LYS B 90  N ILE B 78  ? N ILE B 78  
AA5 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 100 ? N LYS B 100 O VAL B 157 ? O VAL B 157 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   8ZUB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 50.41   -128.36 
2 1 ASN A 51  ? ? -154.48 68.52   
3 1 ASN A 84  ? ? 52.23   -125.57 
4 1 TYR A 154 ? ? 58.85   -107.75 
5 1 PRO A 184 ? ? -84.00  36.82   
6 1 ASP B 33  ? ? 48.91   -129.12 
7 1 ASN B 84  ? ? 50.28   -120.76 
8 1 TYR B 154 ? ? 61.50   -111.24 
9 1 ARG B 217 ? ? -140.68 23.92   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 788 ? 5.86 . 
2 1 O ? B HOH 746 ? 7.08 . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     SER 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    SER 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
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 
A1D80 N1   N  N N 1   
A1D80 N3   N  N N 2   
A1D80 C4   C  Y N 3   
A1D80 C5   C  Y N 4   
A1D80 C6   C  Y N 5   
A1D80 C7   C  N N 6   
A1D80 C8   C  N N 7   
A1D80 C10  C  N N 8   
A1D80 C13  C  Y N 9   
A1D80 C15  C  Y N 10  
A1D80 C17  C  Y N 11  
A1D80 C20  C  Y N 12  
A1D80 C21  C  N N 13  
A1D80 C22  C  N N 14  
A1D80 C24  C  N N 15  
A1D80 C26  C  Y N 16  
A1D80 C1   C  Y N 17  
A1D80 C2   C  Y N 18  
A1D80 C3   C  Y N 19  
A1D80 F1   F  N N 20  
A1D80 F2   F  N N 21  
A1D80 F3   F  N N 22  
A1D80 N2   N  N N 23  
A1D80 C9   C  N N 24  
A1D80 C11  C  N N 25  
A1D80 O1   O  N N 26  
A1D80 O2   O  N N 27  
A1D80 C12  C  N N 28  
A1D80 C14  C  Y N 29  
A1D80 C16  C  Y N 30  
A1D80 C18  C  Y N 31  
A1D80 C19  C  Y N 32  
A1D80 CL1  CL N N 33  
A1D80 N4   N  Y N 34  
A1D80 N5   N  Y N 35  
A1D80 C23  C  N N 36  
A1D80 C25  C  N N 37  
A1D80 N6   N  Y N 38  
A1D80 N7   N  Y N 39  
A1D80 N8   N  Y N 40  
A1D80 C27  C  N N 41  
A1D80 H1   H  N N 42  
A1D80 H2   H  N N 43  
A1D80 H3   H  N N 44  
A1D80 H4   H  N N 45  
A1D80 H5   H  N N 46  
A1D80 H6   H  N N 47  
A1D80 H7   H  N N 48  
A1D80 H8   H  N N 49  
A1D80 H9   H  N N 50  
A1D80 H10  H  N N 51  
A1D80 H11  H  N N 52  
A1D80 H12  H  N N 53  
A1D80 H13  H  N N 54  
A1D80 H14  H  N N 55  
A1D80 H15  H  N N 56  
A1D80 H16  H  N N 57  
A1D80 H17  H  N N 58  
A1D80 H18  H  N N 59  
A1D80 H19  H  N N 60  
A1D80 H20  H  N N 61  
A1D80 H21  H  N N 62  
A1D80 H22  H  N N 63  
A1D80 H23  H  N N 64  
A1D80 H24  H  N N 65  
A1D80 H25  H  N N 66  
A1D80 H26  H  N N 67  
ALA   N    N  N N 68  
ALA   CA   C  N S 69  
ALA   C    C  N N 70  
ALA   O    O  N N 71  
ALA   CB   C  N N 72  
ALA   OXT  O  N N 73  
ALA   H    H  N N 74  
ALA   H2   H  N N 75  
ALA   HA   H  N N 76  
ALA   HB1  H  N N 77  
ALA   HB2  H  N N 78  
ALA   HB3  H  N N 79  
ALA   HXT  H  N N 80  
ARG   N    N  N N 81  
ARG   CA   C  N S 82  
ARG   C    C  N N 83  
ARG   O    O  N N 84  
ARG   CB   C  N N 85  
ARG   CG   C  N N 86  
ARG   CD   C  N N 87  
ARG   NE   N  N N 88  
ARG   CZ   C  N N 89  
ARG   NH1  N  N N 90  
ARG   NH2  N  N N 91  
ARG   OXT  O  N N 92  
ARG   H    H  N N 93  
ARG   H2   H  N N 94  
ARG   HA   H  N N 95  
ARG   HB2  H  N N 96  
ARG   HB3  H  N N 97  
ARG   HG2  H  N N 98  
ARG   HG3  H  N N 99  
ARG   HD2  H  N N 100 
ARG   HD3  H  N N 101 
ARG   HE   H  N N 102 
ARG   HH11 H  N N 103 
ARG   HH12 H  N N 104 
ARG   HH21 H  N N 105 
ARG   HH22 H  N N 106 
ARG   HXT  H  N N 107 
ASN   N    N  N N 108 
ASN   CA   C  N S 109 
ASN   C    C  N N 110 
ASN   O    O  N N 111 
ASN   CB   C  N N 112 
ASN   CG   C  N N 113 
ASN   OD1  O  N N 114 
ASN   ND2  N  N N 115 
ASN   OXT  O  N N 116 
ASN   H    H  N N 117 
ASN   H2   H  N N 118 
ASN   HA   H  N N 119 
ASN   HB2  H  N N 120 
ASN   HB3  H  N N 121 
ASN   HD21 H  N N 122 
ASN   HD22 H  N N 123 
ASN   HXT  H  N N 124 
ASP   N    N  N N 125 
ASP   CA   C  N S 126 
ASP   C    C  N N 127 
ASP   O    O  N N 128 
ASP   CB   C  N N 129 
ASP   CG   C  N N 130 
ASP   OD1  O  N N 131 
ASP   OD2  O  N N 132 
ASP   OXT  O  N N 133 
ASP   H    H  N N 134 
ASP   H2   H  N N 135 
ASP   HA   H  N N 136 
ASP   HB2  H  N N 137 
ASP   HB3  H  N N 138 
ASP   HD2  H  N N 139 
ASP   HXT  H  N N 140 
CYS   N    N  N N 141 
CYS   CA   C  N R 142 
CYS   C    C  N N 143 
CYS   O    O  N N 144 
CYS   CB   C  N N 145 
CYS   SG   S  N N 146 
CYS   OXT  O  N N 147 
CYS   H    H  N N 148 
CYS   H2   H  N N 149 
CYS   HA   H  N N 150 
CYS   HB2  H  N N 151 
CYS   HB3  H  N N 152 
CYS   HG   H  N N 153 
CYS   HXT  H  N N 154 
GLN   N    N  N N 155 
GLN   CA   C  N S 156 
GLN   C    C  N N 157 
GLN   O    O  N N 158 
GLN   CB   C  N N 159 
GLN   CG   C  N N 160 
GLN   CD   C  N N 161 
GLN   OE1  O  N N 162 
GLN   NE2  N  N N 163 
GLN   OXT  O  N N 164 
GLN   H    H  N N 165 
GLN   H2   H  N N 166 
GLN   HA   H  N N 167 
GLN   HB2  H  N N 168 
GLN   HB3  H  N N 169 
GLN   HG2  H  N N 170 
GLN   HG3  H  N N 171 
GLN   HE21 H  N N 172 
GLN   HE22 H  N N 173 
GLN   HXT  H  N N 174 
GLU   N    N  N N 175 
GLU   CA   C  N S 176 
GLU   C    C  N N 177 
GLU   O    O  N N 178 
GLU   CB   C  N N 179 
GLU   CG   C  N N 180 
GLU   CD   C  N N 181 
GLU   OE1  O  N N 182 
GLU   OE2  O  N N 183 
GLU   OXT  O  N N 184 
GLU   H    H  N N 185 
GLU   H2   H  N N 186 
GLU   HA   H  N N 187 
GLU   HB2  H  N N 188 
GLU   HB3  H  N N 189 
GLU   HG2  H  N N 190 
GLU   HG3  H  N N 191 
GLU   HE2  H  N N 192 
GLU   HXT  H  N N 193 
GLY   N    N  N N 194 
GLY   CA   C  N N 195 
GLY   C    C  N N 196 
GLY   O    O  N N 197 
GLY   OXT  O  N N 198 
GLY   H    H  N N 199 
GLY   H2   H  N N 200 
GLY   HA2  H  N N 201 
GLY   HA3  H  N N 202 
GLY   HXT  H  N N 203 
HIS   N    N  N N 204 
HIS   CA   C  N S 205 
HIS   C    C  N N 206 
HIS   O    O  N N 207 
HIS   CB   C  N N 208 
HIS   CG   C  Y N 209 
HIS   ND1  N  Y N 210 
HIS   CD2  C  Y N 211 
HIS   CE1  C  Y N 212 
HIS   NE2  N  Y N 213 
HIS   OXT  O  N N 214 
HIS   H    H  N N 215 
HIS   H2   H  N N 216 
HIS   HA   H  N N 217 
HIS   HB2  H  N N 218 
HIS   HB3  H  N N 219 
HIS   HD1  H  N N 220 
HIS   HD2  H  N N 221 
HIS   HE1  H  N N 222 
HIS   HE2  H  N N 223 
HIS   HXT  H  N N 224 
HOH   O    O  N N 225 
HOH   H1   H  N N 226 
HOH   H2   H  N N 227 
ILE   N    N  N N 228 
ILE   CA   C  N S 229 
ILE   C    C  N N 230 
ILE   O    O  N N 231 
ILE   CB   C  N S 232 
ILE   CG1  C  N N 233 
ILE   CG2  C  N N 234 
ILE   CD1  C  N N 235 
ILE   OXT  O  N N 236 
ILE   H    H  N N 237 
ILE   H2   H  N N 238 
ILE   HA   H  N N 239 
ILE   HB   H  N N 240 
ILE   HG12 H  N N 241 
ILE   HG13 H  N N 242 
ILE   HG21 H  N N 243 
ILE   HG22 H  N N 244 
ILE   HG23 H  N N 245 
ILE   HD11 H  N N 246 
ILE   HD12 H  N N 247 
ILE   HD13 H  N N 248 
ILE   HXT  H  N N 249 
LEU   N    N  N N 250 
LEU   CA   C  N S 251 
LEU   C    C  N N 252 
LEU   O    O  N N 253 
LEU   CB   C  N N 254 
LEU   CG   C  N N 255 
LEU   CD1  C  N N 256 
LEU   CD2  C  N N 257 
LEU   OXT  O  N N 258 
LEU   H    H  N N 259 
LEU   H2   H  N N 260 
LEU   HA   H  N N 261 
LEU   HB2  H  N N 262 
LEU   HB3  H  N N 263 
LEU   HG   H  N N 264 
LEU   HD11 H  N N 265 
LEU   HD12 H  N N 266 
LEU   HD13 H  N N 267 
LEU   HD21 H  N N 268 
LEU   HD22 H  N N 269 
LEU   HD23 H  N N 270 
LEU   HXT  H  N N 271 
LYS   N    N  N N 272 
LYS   CA   C  N S 273 
LYS   C    C  N N 274 
LYS   O    O  N N 275 
LYS   CB   C  N N 276 
LYS   CG   C  N N 277 
LYS   CD   C  N N 278 
LYS   CE   C  N N 279 
LYS   NZ   N  N N 280 
LYS   OXT  O  N N 281 
LYS   H    H  N N 282 
LYS   H2   H  N N 283 
LYS   HA   H  N N 284 
LYS   HB2  H  N N 285 
LYS   HB3  H  N N 286 
LYS   HG2  H  N N 287 
LYS   HG3  H  N N 288 
LYS   HD2  H  N N 289 
LYS   HD3  H  N N 290 
LYS   HE2  H  N N 291 
LYS   HE3  H  N N 292 
LYS   HZ1  H  N N 293 
LYS   HZ2  H  N N 294 
LYS   HZ3  H  N N 295 
LYS   HXT  H  N N 296 
MET   N    N  N N 297 
MET   CA   C  N S 298 
MET   C    C  N N 299 
MET   O    O  N N 300 
MET   CB   C  N N 301 
MET   CG   C  N N 302 
MET   SD   S  N N 303 
MET   CE   C  N N 304 
MET   OXT  O  N N 305 
MET   H    H  N N 306 
MET   H2   H  N N 307 
MET   HA   H  N N 308 
MET   HB2  H  N N 309 
MET   HB3  H  N N 310 
MET   HG2  H  N N 311 
MET   HG3  H  N N 312 
MET   HE1  H  N N 313 
MET   HE2  H  N N 314 
MET   HE3  H  N N 315 
MET   HXT  H  N N 316 
PHE   N    N  N N 317 
PHE   CA   C  N S 318 
PHE   C    C  N N 319 
PHE   O    O  N N 320 
PHE   CB   C  N N 321 
PHE   CG   C  Y N 322 
PHE   CD1  C  Y N 323 
PHE   CD2  C  Y N 324 
PHE   CE1  C  Y N 325 
PHE   CE2  C  Y N 326 
PHE   CZ   C  Y N 327 
PHE   OXT  O  N N 328 
PHE   H    H  N N 329 
PHE   H2   H  N N 330 
PHE   HA   H  N N 331 
PHE   HB2  H  N N 332 
PHE   HB3  H  N N 333 
PHE   HD1  H  N N 334 
PHE   HD2  H  N N 335 
PHE   HE1  H  N N 336 
PHE   HE2  H  N N 337 
PHE   HZ   H  N N 338 
PHE   HXT  H  N N 339 
PRO   N    N  N N 340 
PRO   CA   C  N S 341 
PRO   C    C  N N 342 
PRO   O    O  N N 343 
PRO   CB   C  N N 344 
PRO   CG   C  N N 345 
PRO   CD   C  N N 346 
PRO   OXT  O  N N 347 
PRO   H    H  N N 348 
PRO   HA   H  N N 349 
PRO   HB2  H  N N 350 
PRO   HB3  H  N N 351 
PRO   HG2  H  N N 352 
PRO   HG3  H  N N 353 
PRO   HD2  H  N N 354 
PRO   HD3  H  N N 355 
PRO   HXT  H  N N 356 
SER   N    N  N N 357 
SER   CA   C  N S 358 
SER   C    C  N N 359 
SER   O    O  N N 360 
SER   CB   C  N N 361 
SER   OG   O  N N 362 
SER   OXT  O  N N 363 
SER   H    H  N N 364 
SER   H2   H  N N 365 
SER   HA   H  N N 366 
SER   HB2  H  N N 367 
SER   HB3  H  N N 368 
SER   HG   H  N N 369 
SER   HXT  H  N N 370 
THR   N    N  N N 371 
THR   CA   C  N S 372 
THR   C    C  N N 373 
THR   O    O  N N 374 
THR   CB   C  N R 375 
THR   OG1  O  N N 376 
THR   CG2  C  N N 377 
THR   OXT  O  N N 378 
THR   H    H  N N 379 
THR   H2   H  N N 380 
THR   HA   H  N N 381 
THR   HB   H  N N 382 
THR   HG1  H  N N 383 
THR   HG21 H  N N 384 
THR   HG22 H  N N 385 
THR   HG23 H  N N 386 
THR   HXT  H  N N 387 
TRP   N    N  N N 388 
TRP   CA   C  N S 389 
TRP   C    C  N N 390 
TRP   O    O  N N 391 
TRP   CB   C  N N 392 
TRP   CG   C  Y N 393 
TRP   CD1  C  Y N 394 
TRP   CD2  C  Y N 395 
TRP   NE1  N  Y N 396 
TRP   CE2  C  Y N 397 
TRP   CE3  C  Y N 398 
TRP   CZ2  C  Y N 399 
TRP   CZ3  C  Y N 400 
TRP   CH2  C  Y N 401 
TRP   OXT  O  N N 402 
TRP   H    H  N N 403 
TRP   H2   H  N N 404 
TRP   HA   H  N N 405 
TRP   HB2  H  N N 406 
TRP   HB3  H  N N 407 
TRP   HD1  H  N N 408 
TRP   HE1  H  N N 409 
TRP   HE3  H  N N 410 
TRP   HZ2  H  N N 411 
TRP   HZ3  H  N N 412 
TRP   HH2  H  N N 413 
TRP   HXT  H  N N 414 
TYR   N    N  N N 415 
TYR   CA   C  N S 416 
TYR   C    C  N N 417 
TYR   O    O  N N 418 
TYR   CB   C  N N 419 
TYR   CG   C  Y N 420 
TYR   CD1  C  Y N 421 
TYR   CD2  C  Y N 422 
TYR   CE1  C  Y N 423 
TYR   CE2  C  Y N 424 
TYR   CZ   C  Y N 425 
TYR   OH   O  N N 426 
TYR   OXT  O  N N 427 
TYR   H    H  N N 428 
TYR   H2   H  N N 429 
TYR   HA   H  N N 430 
TYR   HB2  H  N N 431 
TYR   HB3  H  N N 432 
TYR   HD1  H  N N 433 
TYR   HD2  H  N N 434 
TYR   HE1  H  N N 435 
TYR   HE2  H  N N 436 
TYR   HH   H  N N 437 
TYR   HXT  H  N N 438 
VAL   N    N  N N 439 
VAL   CA   C  N S 440 
VAL   C    C  N N 441 
VAL   O    O  N N 442 
VAL   CB   C  N N 443 
VAL   CG1  C  N N 444 
VAL   CG2  C  N N 445 
VAL   OXT  O  N N 446 
VAL   H    H  N N 447 
VAL   H2   H  N N 448 
VAL   HA   H  N N 449 
VAL   HB   H  N N 450 
VAL   HG11 H  N N 451 
VAL   HG12 H  N N 452 
VAL   HG13 H  N N 453 
VAL   HG21 H  N N 454 
VAL   HG22 H  N N 455 
VAL   HG23 H  N N 456 
VAL   HXT  H  N N 457 
# 
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 
A1D80 C23 C24  sing N N 1   
A1D80 C23 C22  sing N N 2   
A1D80 C24 C25  sing N N 3   
A1D80 C21 C22  sing N N 4   
A1D80 C21 N4   sing N N 5   
A1D80 N4  N5   sing Y N 6   
A1D80 N4  C20  sing Y N 7   
A1D80 N5  C17  doub Y N 8   
A1D80 C20 C16  doub Y N 9   
A1D80 C17 C16  sing Y N 10  
A1D80 C17 C18  sing Y N 11  
A1D80 C16 C15  sing Y N 12  
A1D80 C18 C19  doub Y N 13  
A1D80 C15 C14  doub Y N 14  
A1D80 C19 C14  sing Y N 15  
A1D80 C19 CL1  sing N N 16  
A1D80 C14 N3   sing N N 17  
A1D80 N3  C11  sing N N 18  
A1D80 C10 C11  doub N N 19  
A1D80 C10 C9   sing N N 20  
A1D80 C11 N1   sing N N 21  
A1D80 O2  C9   doub N N 22  
A1D80 C9  N2   sing N N 23  
A1D80 N1  C7   sing N N 24  
A1D80 N1  C8   sing N N 25  
A1D80 C7  C2   sing N N 26  
A1D80 C2  C1   doub Y N 27  
A1D80 C2  C3   sing Y N 28  
A1D80 C1  C6   sing Y N 29  
A1D80 F1  C3   sing N N 30  
A1D80 C3  C4   doub Y N 31  
A1D80 C6  F3   sing N N 32  
A1D80 C6  C5   doub Y N 33  
A1D80 N2  C8   sing N N 34  
A1D80 N2  C12  sing N N 35  
A1D80 C8  O1   doub N N 36  
A1D80 C4  C5   sing Y N 37  
A1D80 C5  F2   sing N N 38  
A1D80 C12 C13  sing N N 39  
A1D80 N6  C13  doub Y N 40  
A1D80 N6  N7   sing Y N 41  
A1D80 C27 N7   sing N N 42  
A1D80 C13 N8   sing Y N 43  
A1D80 N7  C26  sing Y N 44  
A1D80 N8  C26  doub Y N 45  
A1D80 N3  H1   sing N N 46  
A1D80 C4  H2   sing N N 47  
A1D80 C7  H3   sing N N 48  
A1D80 C7  H4   sing N N 49  
A1D80 C10 H5   sing N N 50  
A1D80 C15 H6   sing N N 51  
A1D80 C20 H7   sing N N 52  
A1D80 C21 H8   sing N N 53  
A1D80 C21 H9   sing N N 54  
A1D80 C22 H10  sing N N 55  
A1D80 C22 H11  sing N N 56  
A1D80 C24 H12  sing N N 57  
A1D80 C24 H13  sing N N 58  
A1D80 C26 H14  sing N N 59  
A1D80 C1  H15  sing N N 60  
A1D80 C12 H16  sing N N 61  
A1D80 C12 H17  sing N N 62  
A1D80 C18 H18  sing N N 63  
A1D80 C23 H19  sing N N 64  
A1D80 C23 H20  sing N N 65  
A1D80 C25 H21  sing N N 66  
A1D80 C25 H22  sing N N 67  
A1D80 C25 H23  sing N N 68  
A1D80 C27 H24  sing N N 69  
A1D80 C27 H25  sing N N 70  
A1D80 C27 H26  sing N N 71  
ALA   N   CA   sing N N 72  
ALA   N   H    sing N N 73  
ALA   N   H2   sing N N 74  
ALA   CA  C    sing N N 75  
ALA   CA  CB   sing N N 76  
ALA   CA  HA   sing N N 77  
ALA   C   O    doub N N 78  
ALA   C   OXT  sing N N 79  
ALA   CB  HB1  sing N N 80  
ALA   CB  HB2  sing N N 81  
ALA   CB  HB3  sing N N 82  
ALA   OXT HXT  sing N N 83  
ARG   N   CA   sing N N 84  
ARG   N   H    sing N N 85  
ARG   N   H2   sing N N 86  
ARG   CA  C    sing N N 87  
ARG   CA  CB   sing N N 88  
ARG   CA  HA   sing N N 89  
ARG   C   O    doub N N 90  
ARG   C   OXT  sing N N 91  
ARG   CB  CG   sing N N 92  
ARG   CB  HB2  sing N N 93  
ARG   CB  HB3  sing N N 94  
ARG   CG  CD   sing N N 95  
ARG   CG  HG2  sing N N 96  
ARG   CG  HG3  sing N N 97  
ARG   CD  NE   sing N N 98  
ARG   CD  HD2  sing N N 99  
ARG   CD  HD3  sing N N 100 
ARG   NE  CZ   sing N N 101 
ARG   NE  HE   sing N N 102 
ARG   CZ  NH1  sing N N 103 
ARG   CZ  NH2  doub N N 104 
ARG   NH1 HH11 sing N N 105 
ARG   NH1 HH12 sing N N 106 
ARG   NH2 HH21 sing N N 107 
ARG   NH2 HH22 sing N N 108 
ARG   OXT HXT  sing N N 109 
ASN   N   CA   sing N N 110 
ASN   N   H    sing N N 111 
ASN   N   H2   sing N N 112 
ASN   CA  C    sing N N 113 
ASN   CA  CB   sing N N 114 
ASN   CA  HA   sing N N 115 
ASN   C   O    doub N N 116 
ASN   C   OXT  sing N N 117 
ASN   CB  CG   sing N N 118 
ASN   CB  HB2  sing N N 119 
ASN   CB  HB3  sing N N 120 
ASN   CG  OD1  doub N N 121 
ASN   CG  ND2  sing N N 122 
ASN   ND2 HD21 sing N N 123 
ASN   ND2 HD22 sing N N 124 
ASN   OXT HXT  sing N N 125 
ASP   N   CA   sing N N 126 
ASP   N   H    sing N N 127 
ASP   N   H2   sing N N 128 
ASP   CA  C    sing N N 129 
ASP   CA  CB   sing N N 130 
ASP   CA  HA   sing N N 131 
ASP   C   O    doub N N 132 
ASP   C   OXT  sing N N 133 
ASP   CB  CG   sing N N 134 
ASP   CB  HB2  sing N N 135 
ASP   CB  HB3  sing N N 136 
ASP   CG  OD1  doub N N 137 
ASP   CG  OD2  sing N N 138 
ASP   OD2 HD2  sing N N 139 
ASP   OXT HXT  sing N N 140 
CYS   N   CA   sing N N 141 
CYS   N   H    sing N N 142 
CYS   N   H2   sing N N 143 
CYS   CA  C    sing N N 144 
CYS   CA  CB   sing N N 145 
CYS   CA  HA   sing N N 146 
CYS   C   O    doub N N 147 
CYS   C   OXT  sing N N 148 
CYS   CB  SG   sing N N 149 
CYS   CB  HB2  sing N N 150 
CYS   CB  HB3  sing N N 151 
CYS   SG  HG   sing N N 152 
CYS   OXT HXT  sing N N 153 
GLN   N   CA   sing N N 154 
GLN   N   H    sing N N 155 
GLN   N   H2   sing N N 156 
GLN   CA  C    sing N N 157 
GLN   CA  CB   sing N N 158 
GLN   CA  HA   sing N N 159 
GLN   C   O    doub N N 160 
GLN   C   OXT  sing N N 161 
GLN   CB  CG   sing N N 162 
GLN   CB  HB2  sing N N 163 
GLN   CB  HB3  sing N N 164 
GLN   CG  CD   sing N N 165 
GLN   CG  HG2  sing N N 166 
GLN   CG  HG3  sing N N 167 
GLN   CD  OE1  doub N N 168 
GLN   CD  NE2  sing N N 169 
GLN   NE2 HE21 sing N N 170 
GLN   NE2 HE22 sing N N 171 
GLN   OXT HXT  sing N N 172 
GLU   N   CA   sing N N 173 
GLU   N   H    sing N N 174 
GLU   N   H2   sing N N 175 
GLU   CA  C    sing N N 176 
GLU   CA  CB   sing N N 177 
GLU   CA  HA   sing N N 178 
GLU   C   O    doub N N 179 
GLU   C   OXT  sing N N 180 
GLU   CB  CG   sing N N 181 
GLU   CB  HB2  sing N N 182 
GLU   CB  HB3  sing N N 183 
GLU   CG  CD   sing N N 184 
GLU   CG  HG2  sing N N 185 
GLU   CG  HG3  sing N N 186 
GLU   CD  OE1  doub N N 187 
GLU   CD  OE2  sing N N 188 
GLU   OE2 HE2  sing N N 189 
GLU   OXT HXT  sing N N 190 
GLY   N   CA   sing N N 191 
GLY   N   H    sing N N 192 
GLY   N   H2   sing N N 193 
GLY   CA  C    sing N N 194 
GLY   CA  HA2  sing N N 195 
GLY   CA  HA3  sing N N 196 
GLY   C   O    doub N N 197 
GLY   C   OXT  sing N N 198 
GLY   OXT HXT  sing N N 199 
HIS   N   CA   sing N N 200 
HIS   N   H    sing N N 201 
HIS   N   H2   sing N N 202 
HIS   CA  C    sing N N 203 
HIS   CA  CB   sing N N 204 
HIS   CA  HA   sing N N 205 
HIS   C   O    doub N N 206 
HIS   C   OXT  sing N N 207 
HIS   CB  CG   sing N N 208 
HIS   CB  HB2  sing N N 209 
HIS   CB  HB3  sing N N 210 
HIS   CG  ND1  sing Y N 211 
HIS   CG  CD2  doub Y N 212 
HIS   ND1 CE1  doub Y N 213 
HIS   ND1 HD1  sing N N 214 
HIS   CD2 NE2  sing Y N 215 
HIS   CD2 HD2  sing N N 216 
HIS   CE1 NE2  sing Y N 217 
HIS   CE1 HE1  sing N N 218 
HIS   NE2 HE2  sing N N 219 
HIS   OXT HXT  sing N N 220 
HOH   O   H1   sing N N 221 
HOH   O   H2   sing N N 222 
ILE   N   CA   sing N N 223 
ILE   N   H    sing N N 224 
ILE   N   H2   sing N N 225 
ILE   CA  C    sing N N 226 
ILE   CA  CB   sing N N 227 
ILE   CA  HA   sing N N 228 
ILE   C   O    doub N N 229 
ILE   C   OXT  sing N N 230 
ILE   CB  CG1  sing N N 231 
ILE   CB  CG2  sing N N 232 
ILE   CB  HB   sing N N 233 
ILE   CG1 CD1  sing N N 234 
ILE   CG1 HG12 sing N N 235 
ILE   CG1 HG13 sing N N 236 
ILE   CG2 HG21 sing N N 237 
ILE   CG2 HG22 sing N N 238 
ILE   CG2 HG23 sing N N 239 
ILE   CD1 HD11 sing N N 240 
ILE   CD1 HD12 sing N N 241 
ILE   CD1 HD13 sing N N 242 
ILE   OXT HXT  sing N N 243 
LEU   N   CA   sing N N 244 
LEU   N   H    sing N N 245 
LEU   N   H2   sing N N 246 
LEU   CA  C    sing N N 247 
LEU   CA  CB   sing N N 248 
LEU   CA  HA   sing N N 249 
LEU   C   O    doub N N 250 
LEU   C   OXT  sing N N 251 
LEU   CB  CG   sing N N 252 
LEU   CB  HB2  sing N N 253 
LEU   CB  HB3  sing N N 254 
LEU   CG  CD1  sing N N 255 
LEU   CG  CD2  sing N N 256 
LEU   CG  HG   sing N N 257 
LEU   CD1 HD11 sing N N 258 
LEU   CD1 HD12 sing N N 259 
LEU   CD1 HD13 sing N N 260 
LEU   CD2 HD21 sing N N 261 
LEU   CD2 HD22 sing N N 262 
LEU   CD2 HD23 sing N N 263 
LEU   OXT HXT  sing N N 264 
LYS   N   CA   sing N N 265 
LYS   N   H    sing N N 266 
LYS   N   H2   sing N N 267 
LYS   CA  C    sing N N 268 
LYS   CA  CB   sing N N 269 
LYS   CA  HA   sing N N 270 
LYS   C   O    doub N N 271 
LYS   C   OXT  sing N N 272 
LYS   CB  CG   sing N N 273 
LYS   CB  HB2  sing N N 274 
LYS   CB  HB3  sing N N 275 
LYS   CG  CD   sing N N 276 
LYS   CG  HG2  sing N N 277 
LYS   CG  HG3  sing N N 278 
LYS   CD  CE   sing N N 279 
LYS   CD  HD2  sing N N 280 
LYS   CD  HD3  sing N N 281 
LYS   CE  NZ   sing N N 282 
LYS   CE  HE2  sing N N 283 
LYS   CE  HE3  sing N N 284 
LYS   NZ  HZ1  sing N N 285 
LYS   NZ  HZ2  sing N N 286 
LYS   NZ  HZ3  sing N N 287 
LYS   OXT HXT  sing N N 288 
MET   N   CA   sing N N 289 
MET   N   H    sing N N 290 
MET   N   H2   sing N N 291 
MET   CA  C    sing N N 292 
MET   CA  CB   sing N N 293 
MET   CA  HA   sing N N 294 
MET   C   O    doub N N 295 
MET   C   OXT  sing N N 296 
MET   CB  CG   sing N N 297 
MET   CB  HB2  sing N N 298 
MET   CB  HB3  sing N N 299 
MET   CG  SD   sing N N 300 
MET   CG  HG2  sing N N 301 
MET   CG  HG3  sing N N 302 
MET   SD  CE   sing N N 303 
MET   CE  HE1  sing N N 304 
MET   CE  HE2  sing N N 305 
MET   CE  HE3  sing N N 306 
MET   OXT HXT  sing N N 307 
PHE   N   CA   sing N N 308 
PHE   N   H    sing N N 309 
PHE   N   H2   sing N N 310 
PHE   CA  C    sing N N 311 
PHE   CA  CB   sing N N 312 
PHE   CA  HA   sing N N 313 
PHE   C   O    doub N N 314 
PHE   C   OXT  sing N N 315 
PHE   CB  CG   sing N N 316 
PHE   CB  HB2  sing N N 317 
PHE   CB  HB3  sing N N 318 
PHE   CG  CD1  doub Y N 319 
PHE   CG  CD2  sing Y N 320 
PHE   CD1 CE1  sing Y N 321 
PHE   CD1 HD1  sing N N 322 
PHE   CD2 CE2  doub Y N 323 
PHE   CD2 HD2  sing N N 324 
PHE   CE1 CZ   doub Y N 325 
PHE   CE1 HE1  sing N N 326 
PHE   CE2 CZ   sing Y N 327 
PHE   CE2 HE2  sing N N 328 
PHE   CZ  HZ   sing N N 329 
PHE   OXT HXT  sing N N 330 
PRO   N   CA   sing N N 331 
PRO   N   CD   sing N N 332 
PRO   N   H    sing N N 333 
PRO   CA  C    sing N N 334 
PRO   CA  CB   sing N N 335 
PRO   CA  HA   sing N N 336 
PRO   C   O    doub N N 337 
PRO   C   OXT  sing N N 338 
PRO   CB  CG   sing N N 339 
PRO   CB  HB2  sing N N 340 
PRO   CB  HB3  sing N N 341 
PRO   CG  CD   sing N N 342 
PRO   CG  HG2  sing N N 343 
PRO   CG  HG3  sing N N 344 
PRO   CD  HD2  sing N N 345 
PRO   CD  HD3  sing N N 346 
PRO   OXT HXT  sing N N 347 
SER   N   CA   sing N N 348 
SER   N   H    sing N N 349 
SER   N   H2   sing N N 350 
SER   CA  C    sing N N 351 
SER   CA  CB   sing N N 352 
SER   CA  HA   sing N N 353 
SER   C   O    doub N N 354 
SER   C   OXT  sing N N 355 
SER   CB  OG   sing N N 356 
SER   CB  HB2  sing N N 357 
SER   CB  HB3  sing N N 358 
SER   OG  HG   sing N N 359 
SER   OXT HXT  sing N N 360 
THR   N   CA   sing N N 361 
THR   N   H    sing N N 362 
THR   N   H2   sing N N 363 
THR   CA  C    sing N N 364 
THR   CA  CB   sing N N 365 
THR   CA  HA   sing N N 366 
THR   C   O    doub N N 367 
THR   C   OXT  sing N N 368 
THR   CB  OG1  sing N N 369 
THR   CB  CG2  sing N N 370 
THR   CB  HB   sing N N 371 
THR   OG1 HG1  sing N N 372 
THR   CG2 HG21 sing N N 373 
THR   CG2 HG22 sing N N 374 
THR   CG2 HG23 sing N N 375 
THR   OXT HXT  sing N N 376 
TRP   N   CA   sing N N 377 
TRP   N   H    sing N N 378 
TRP   N   H2   sing N N 379 
TRP   CA  C    sing N N 380 
TRP   CA  CB   sing N N 381 
TRP   CA  HA   sing N N 382 
TRP   C   O    doub N N 383 
TRP   C   OXT  sing N N 384 
TRP   CB  CG   sing N N 385 
TRP   CB  HB2  sing N N 386 
TRP   CB  HB3  sing N N 387 
TRP   CG  CD1  doub Y N 388 
TRP   CG  CD2  sing Y N 389 
TRP   CD1 NE1  sing Y N 390 
TRP   CD1 HD1  sing N N 391 
TRP   CD2 CE2  doub Y N 392 
TRP   CD2 CE3  sing Y N 393 
TRP   NE1 CE2  sing Y N 394 
TRP   NE1 HE1  sing N N 395 
TRP   CE2 CZ2  sing Y N 396 
TRP   CE3 CZ3  doub Y N 397 
TRP   CE3 HE3  sing N N 398 
TRP   CZ2 CH2  doub Y N 399 
TRP   CZ2 HZ2  sing N N 400 
TRP   CZ3 CH2  sing Y N 401 
TRP   CZ3 HZ3  sing N N 402 
TRP   CH2 HH2  sing N N 403 
TRP   OXT HXT  sing N N 404 
TYR   N   CA   sing N N 405 
TYR   N   H    sing N N 406 
TYR   N   H2   sing N N 407 
TYR   CA  C    sing N N 408 
TYR   CA  CB   sing N N 409 
TYR   CA  HA   sing N N 410 
TYR   C   O    doub N N 411 
TYR   C   OXT  sing N N 412 
TYR   CB  CG   sing N N 413 
TYR   CB  HB2  sing N N 414 
TYR   CB  HB3  sing N N 415 
TYR   CG  CD1  doub Y N 416 
TYR   CG  CD2  sing Y N 417 
TYR   CD1 CE1  sing Y N 418 
TYR   CD1 HD1  sing N N 419 
TYR   CD2 CE2  doub Y N 420 
TYR   CD2 HD2  sing N N 421 
TYR   CE1 CZ   doub Y N 422 
TYR   CE1 HE1  sing N N 423 
TYR   CE2 CZ   sing Y N 424 
TYR   CE2 HE2  sing N N 425 
TYR   CZ  OH   sing N N 426 
TYR   OH  HH   sing N N 427 
TYR   OXT HXT  sing N N 428 
VAL   N   CA   sing N N 429 
VAL   N   H    sing N N 430 
VAL   N   H2   sing N N 431 
VAL   CA  C    sing N N 432 
VAL   CA  CB   sing N N 433 
VAL   CA  HA   sing N N 434 
VAL   C   O    doub N N 435 
VAL   C   OXT  sing N N 436 
VAL   CB  CG1  sing N N 437 
VAL   CB  CG2  sing N N 438 
VAL   CB  HB   sing N N 439 
VAL   CG1 HG11 sing N N 440 
VAL   CG1 HG12 sing N N 441 
VAL   CG1 HG13 sing N N 442 
VAL   CG2 HG21 sing N N 443 
VAL   CG2 HG22 sing N N 444 
VAL   CG2 HG23 sing N N 445 
VAL   OXT HXT  sing N N 446 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8HEF 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZUB 
_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]   0.017992 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005870 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010064 
_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]   0.017944 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H  ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 31.310  -7.639  28.190  1.00 65.99 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 31.009  -8.310  26.893  1.00 63.47 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 30.582  -7.325  25.798  1.00 55.34 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 30.600  -7.698  24.625  1.00 38.55 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 29.987  -9.399  27.075  1.00 66.66 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 30.551  -10.490 27.787  1.00 66.82 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 30.195  -6.096  26.182  1.00 48.24 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 30.060  -4.973  25.259  1.00 48.79 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 28.596  -4.580  25.063  1.00 46.95 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 27.725  -5.353  25.468  1.00 49.14 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? 28.339  -3.403  24.443  1.00 43.48 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? 26.966  -2.957  24.195  1.00 36.28 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? 26.784  -2.077  22.952  1.00 34.45 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? 27.126  -0.903  22.952  1.00 37.79 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? 26.409  -2.206  25.409  1.00 30.80 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? 24.944  -2.474  25.488  1.00 24.84 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? 24.508  -3.741  25.797  1.00 26.09 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? 24.028  -1.529  25.060  1.00 24.66 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? 23.169  -4.054  25.757  1.00 23.44 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? 22.685  -1.838  25.035  1.00 24.22 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? 22.261  -3.089  25.391  1.00 23.34 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? 26.119  -2.615  21.918  1.00 30.84 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? 25.912  -1.887  20.672  1.00 26.28 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? 24.459  -2.062  20.226  1.00 19.33 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? 23.834  -3.037  20.581  1.00 18.29 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? 26.783  -2.452  19.531  1.00 29.25 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? 28.295  -2.472  19.771  1.00 28.94 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? 29.022  -2.072  18.507  1.00 28.20 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? 30.390  -1.558  18.669  1.00 27.96 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? 30.871  -0.493  18.022  1.00 26.69 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? 30.055  0.277   17.324  1.00 26.39 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? 32.156  -0.170  18.076  1.00 27.79 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? 23.971  -1.163  19.379  1.00 18.90 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? 22.716  -1.397  18.691  1.00 21.87 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? 22.956  -2.605  17.791  1.00 20.66 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? 23.939  -2.645  17.080  1.00 24.97 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? 22.313  -0.234  17.800  1.00 26.69 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? 21.724  0.979   18.499  1.00 34.48 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? 20.274  0.815   18.821  1.00 37.63 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? 19.783  1.847   19.821  1.00 41.60 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? 20.250  3.222   19.519  1.00 41.62 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? 22.163  -3.622  17.965  1.00 17.26 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? 22.344  -4.857  17.222  1.00 17.58 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? 21.042  -5.190  16.501  1.00 15.66 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? 19.961  -5.206  17.124  1.00 15.98 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? 22.715  -5.936  18.228  1.00 20.31 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? 22.640  -7.316  17.717  1.00 29.64 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? 23.646  -8.463  18.736  1.00 38.96 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? 24.919  -7.425  19.444  1.00 28.24 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? 21.131  -5.398  15.174  1.00 12.14 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? 20.005  -5.795  14.354  1.00 10.16 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? 19.951  -7.313  14.244  1.00 9.42  ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? 20.961  -7.981  14.418  1.00 10.91 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? 20.126  -5.182  12.966  1.00 10.43 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? 18.794  -7.818  13.854  1.00 9.30  ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? 18.628  -9.192  13.468  1.00 10.45 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? 19.308  -9.434  12.147  1.00 9.36  ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? 19.343  -8.579  11.280  1.00 9.92  ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? 17.162  -9.572  13.332  1.00 12.73 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? 16.503  -9.711  14.671  1.00 15.72 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? 16.842  -10.760 15.509  1.00 17.40 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? 15.652  -8.742  15.147  1.00 17.85 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? 16.279  -10.869 16.772  1.00 20.44 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? 15.108  -8.850  16.421  1.00 17.50 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? 15.410  -9.919  17.214  1.00 18.66 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? 19.834  -10.642 11.934  1.00 10.19 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? 20.400  -10.985 10.640  1.00 10.85 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? 19.318  -10.838 9.577   1.00 11.57 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? 18.196  -11.278 9.802   1.00 13.30 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? 20.809  -12.462 10.814  1.00 10.90 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? 20.973  -12.616 12.308  1.00 11.25 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? 19.924  -11.730 12.925  1.00 10.90 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? 19.663  -10.243 8.425   1.00 10.59 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? 18.672  -9.766  7.464   1.00 10.69 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? 18.388  -10.763 6.330   1.00 10.69 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? 17.500  -10.535 5.500   1.00 10.07 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? 19.108  -8.409  6.947   1.00 11.08 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? 20.375  -8.489  6.302   1.00 11.39 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? 19.069  -11.917 6.317   1.00 10.55 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? 19.025  -12.734 5.097   1.00 11.56 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? 17.614  -13.205 4.752   1.00 11.66 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? 17.214  -13.263 3.587   1.00 11.70 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? 16.851  -13.580 5.770   1.00 12.38 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? 15.507  -14.073 5.509   1.00 13.56 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? 14.631  -13.021 4.858   1.00 12.47 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? 13.732  -13.382 4.114   1.00 14.65 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? 14.872  -14.539 6.815   1.00 14.84 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? 15.367  -15.881 7.332   1.00 17.92 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? 14.717  -16.309 8.634   1.00 20.58 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? 15.035  -17.733 9.037   1.00 27.33 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? 16.503  -17.955 9.142   1.00 31.21 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? 14.903  -11.741 5.126   1.00 11.31 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? 14.141  -10.660 4.515   1.00 11.39 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? 14.736  -10.263 3.163   1.00 11.31 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? 13.999  -9.948  2.235   1.00 10.23 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? 14.088  -9.475  5.484   1.00 11.86 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? 13.307  -8.310  4.874   1.00 11.20 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? 13.514  -9.944  6.798   1.00 12.20 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? 16.082  -10.335 3.016   1.00 12.18 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? 16.715  -10.009 1.746   1.00 10.96 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? 16.118  -10.802 0.571   1.00 11.50 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? 15.898  -10.243 -0.531  1.00 12.25 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? 18.219  -10.243 1.799   1.00 11.03 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? 18.940  -9.255  2.673   1.00 11.51 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? 20.366  -9.727  2.949   1.00 12.13 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? 21.060  -9.968  1.913   1.00 12.27 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? 20.768  -9.771  4.116   1.00 11.99 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? 15.857  -12.090 0.796   1.00 13.09 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? 15.366  -12.961 -0.258  1.00 13.67 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? 13.914  -12.664 -0.652  1.00 16.47 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? 13.364  -13.333 -1.532  1.00 16.96 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? 13.267  -11.698 0.030   1.00 14.30 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? 11.900  -11.323 -0.270  1.00 13.77 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? 11.788  -9.972  -0.959  1.00 12.62 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? 10.692  -9.567  -1.368  1.00 13.68 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? 11.061  -11.286 1.006   1.00 12.96 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? 10.964  -12.886 1.850   1.00 17.25 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? 12.889  -9.227  -1.111  1.00 12.13 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? 12.756  -7.879  -1.647  1.00 11.77 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? 12.718  -7.895  -3.182  1.00 12.58 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? 13.514  -8.602  -3.816  1.00 12.90 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? 13.910  -7.004  -1.156  1.00 12.19 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? 13.944  -6.947  0.356   1.00 12.16 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? 12.430  -6.356  1.127   1.00 14.76 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? 12.115  -4.812  0.272   1.00 15.84 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? 11.800  -7.103  -3.745  1.00 11.72 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? 11.636  -6.897  -5.174  1.00 12.54 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? 11.417  -5.418  -5.461  1.00 12.84 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? 11.267  -4.576  -4.568  1.00 11.25 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? 10.476  -7.751  -5.714  1.00 13.20 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? 10.670  -9.236  -5.482  1.00 13.61 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? 9.154   -7.300  -5.137  1.00 13.25 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? 11.434  -5.089  -6.759  1.00 12.84 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? 11.153  -3.767  -7.271  1.00 13.64 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? 9.765   -3.813  -7.900  1.00 16.14 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? 9.427   -4.765  -8.603  1.00 14.53 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? 12.255  -3.390  -8.268  1.00 16.51 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? 12.142  -1.975  -8.778  1.00 18.79 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? 13.257  -1.549  -9.702  1.00 22.20 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? 14.076  -2.357  -10.122 1.00 24.21 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? 13.316  -0.260  -9.953  1.00 27.18 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? 8.981   -2.762  -7.649  1.00 13.80 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? 7.690   -2.574  -8.263  1.00 13.98 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? 7.694   -1.242  -8.993  1.00 14.01 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? 8.031   -0.203  -8.432  1.00 12.78 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? 6.528   -2.645  -7.256  1.00 15.07 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? 5.177   -2.556  -7.957  1.00 16.27 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? 6.559   -3.873  -6.381  1.00 14.95 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? 7.139   -1.252  -10.225 1.00 14.18 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? 7.091   -0.079  -11.070 1.00 16.37 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? 5.678   0.017   -11.660 1.00 14.97 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? 5.082   -1.011  -11.992 1.00 17.04 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? 8.192   -0.101  -12.158 1.00 19.72 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? 9.512   -0.272  -11.609 1.00 20.45 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? 8.243   1.196   -12.932 1.00 19.01 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? 5.157   1.241   -11.677 1.00 15.28 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? 3.861   1.561   -12.270 1.00 17.21 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? 4.060   2.856   -13.044 1.00 17.78 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? 4.289   3.942   -12.490 1.00 16.95 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? 2.731   1.600   -11.235 1.00 22.10 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? 1.076   1.816   -11.962 1.00 30.21 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? 4.139   2.706   -14.380 1.00 21.93 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? 4.494   3.836   -15.212 1.00 21.11 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? 5.979   4.129   -15.069 1.00 21.77 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? 6.794   3.276   -15.376 1.00 24.34 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? 6.330   5.294   -14.522 1.00 20.40 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? 7.714   5.552   -14.164 1.00 23.80 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? 7.925   5.565   -12.646 1.00 21.60 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? 9.051   5.635   -12.187 1.00 22.17 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? 8.174   6.874   -14.758 1.00 28.27 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? 7.266   7.866   -14.297 1.00 30.57 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? 8.197   6.858   -16.270 1.00 29.88 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? 6.836   5.515   -11.874 1.00 18.89 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? 6.931   5.509   -10.416 1.00 16.92 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? 7.424   4.142   -9.946  1.00 14.52 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? 6.919   3.129   -10.416 1.00 14.58 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? 5.558   5.786   -9.805  1.00 16.89 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? 5.100   7.034   -10.342 1.00 18.27 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? 5.616   5.880   -8.294  1.00 14.92 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? 8.443   4.115   -9.068  1.00 13.43 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? 9.089   2.876   -8.669  1.00 14.73 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? 9.430   2.919   -7.173  1.00 12.26 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? 9.772   3.963   -6.639  1.00 12.88 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? 10.312  2.548   -9.550  1.00 18.95 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? 10.590  1.146   -9.389  1.00 21.74 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? 11.531  3.386   -9.229  1.00 20.58 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? 9.316   1.763   -6.537  1.00 11.62 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? 9.715   1.591   -5.140  1.00 11.59 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? 9.966   0.116   -4.849  1.00 11.45 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? 9.985   -0.721  -5.743  1.00 10.58 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? 8.650   2.209   -4.214  1.00 11.72 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? 7.168   1.959   -4.524  1.00 11.21 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? 6.827   0.465   -4.484  1.00 10.56 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? 6.331   2.704   -3.481  1.00 11.56 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? 10.154  -0.202  -3.558  1.00 10.65 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? 10.431  -1.562  -3.151  1.00 11.04 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? 9.147   -2.280  -2.768  1.00 10.92 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? 8.258   -1.660  -2.187  1.00 10.39 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? 11.386  -1.575  -1.951  1.00 10.87 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? 12.647  -0.803  -2.248  1.00 11.89 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? 13.554  -1.348  -2.867  1.00 13.43 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? 12.761  0.432   -1.771  1.00 11.59 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? 9.145   -3.599  -2.987  1.00 10.06 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? 8.084   -4.481  -2.527  1.00 10.78 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? 8.603   -5.715  -1.801  1.00 10.86 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? 9.796   -6.021  -1.858  1.00 10.40 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? 7.688   -6.411  -1.120  1.00 10.47 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? 7.973   -7.582  -0.312  1.00 11.09 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? 7.209   -8.772  -0.867  1.00 12.56 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? 5.993   -8.724  -0.881  1.00 12.41 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? 7.540   -7.290  1.120   1.00 10.60 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? 7.826   -8.333  2.194   1.00 10.88 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? 9.293   -8.380  2.539   1.00 11.84 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? 7.014   -8.043  3.466   1.00 11.54 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? 7.956   -9.779  -1.333  1.00 12.06 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? 7.427   -10.952 -2.027  1.00 11.58 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? 7.389   -12.143 -1.080  1.00 11.87 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? 8.432   -12.678 -0.670  1.00 11.84 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? 8.326   -11.198 -3.251  1.00 12.87 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? 7.912   -12.361 -4.103  1.00 14.66 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? 6.647   -12.862 -4.266  1.00 17.70 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? 8.771   -13.114 -4.980  1.00 15.21 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? 6.675   -13.917 -5.145  1.00 17.89 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? 7.954   -14.081 -5.611  1.00 16.99 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? 10.141  -13.064 -5.271  1.00 16.34 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? 8.480   -14.989 -6.535  1.00 16.75 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? 10.656  -13.979 -6.171  1.00 17.28 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? 9.821   -14.906 -6.800  1.00 17.93 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? 6.157   -12.537 -0.676  1.00 11.60 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? 5.929   -13.641 0.217   1.00 12.15 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? 4.934   -14.588 -0.432  1.00 14.39 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? 3.825   -14.153 -0.758  1.00 14.03 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? 5.332   -13.123 1.528   1.00 13.61 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? 6.194   -12.143 2.296   1.00 13.60 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? 5.372   -11.526 3.418   1.00 14.29 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? 7.446   -12.800 2.813   1.00 14.60 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? 5.314   -15.869 -0.533  1.00 17.14 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? 4.487   -16.811 -1.287  1.00 19.40 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? 4.213   -16.167 -2.637  1.00 17.69 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? 5.187   -15.806 -3.308  1.00 19.22 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? 3.287   -17.224 -0.435  1.00 20.71 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? 3.714   -17.935 0.832   1.00 23.68 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? 4.556   -18.863 0.736   1.00 28.39 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? 3.246   -17.548 1.919   1.00 24.97 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? 2.944   -16.069 -3.095  1.00 16.17 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? 2.665   -15.541 -4.412  1.00 16.26 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? 2.067   -14.130 -4.389  1.00 15.82 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? 1.390   -13.738 -5.350  1.00 15.01 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? 1.748   -16.482 -5.210  1.00 19.93 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? 0.375   -16.647 -4.596  1.00 23.36 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? 0.216   -16.337 -3.390  1.00 24.07 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -0.501  -17.188 -5.291  1.00 28.04 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? 2.386   -13.332 -3.352  1.00 16.51 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? 1.891   -11.969 -3.276  1.00 14.39 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? 3.050   -11.020 -3.037  1.00 12.33 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? 3.908   -11.346 -2.230  1.00 13.04 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? 0.885   -11.818 -2.135  1.00 15.60 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? 0.421   -10.375 -1.994  1.00 14.94 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -0.288  -12.739 -2.335  1.00 19.82 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? 2.977   -9.855  -3.666  1.00 12.32 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? 3.922   -8.774  -3.457  1.00 10.84 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? 3.155   -7.641  -2.766  1.00 12.05 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? 2.114   -7.198  -3.260  1.00 13.31 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? 4.579   -8.328  -4.761  1.00 11.17 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? 5.430   -7.120  -4.509  1.00 12.13 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? 5.429   -9.434  -5.401  1.00 12.10 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? 3.717   -7.189  -1.636  1.00 11.43 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? 3.168   -6.114  -0.809  1.00 10.59 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? 4.043   -4.895  -1.021  1.00 11.21 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? 5.271   -4.998  -0.909  1.00 12.42 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? 3.180   -6.478  0.677   1.00 10.64 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? 2.447   -7.763  1.016   1.00 11.12 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? 3.045   -8.995  0.815   1.00 11.84 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? 1.146   -7.747  1.495   1.00 12.89 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? 2.383   -10.173 1.069   1.00 12.54 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? 0.475   -8.924  1.779   1.00 13.65 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? 1.084   -10.133 1.534   1.00 14.36 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? 0.484   -11.358 1.731   1.00 18.62 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? 3.437   -3.744  -1.277  1.00 9.43  ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? 4.199   -2.526  -1.416  1.00 10.52 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? 3.307   -1.330  -1.100  1.00 10.24 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? 2.084   -1.442  -0.995  1.00 11.20 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? 4.843   -2.397  -2.788  1.00 10.56 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? 3.631   -2.055  -4.083  1.00 13.71 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? 3.896   -0.143  -0.884  1.00 10.14 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? 3.085   1.052   -0.668  1.00 10.58 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? 2.231   1.348   -1.899  1.00 11.94 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? 2.715   1.313   -3.052  1.00 10.99 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? 4.132   2.147   -0.368  1.00 10.39 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? 5.333   1.372   0.137   1.00 11.05 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? 5.336   0.126   -0.730  1.00 10.83 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? 0.976   1.765   -1.645  1.00 11.26 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? 0.069   2.027   -2.749  1.00 12.53 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? 0.489   3.291   -3.478  1.00 12.62 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? 0.034   3.495   -4.604  1.00 13.68 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -1.395  2.099   -2.309  1.00 12.73 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.710  3.234   -1.354  1.00 12.09 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -3.166  3.251   -0.954  1.00 11.83 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? -3.395  4.346   -0.011  1.00 11.94 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? -4.578  4.680   0.484   1.00 13.58 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? -5.662  3.994   0.127   1.00 13.03 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? -4.673  5.738   1.273   1.00 13.90 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? 1.334   4.129   -2.851  1.00 11.38 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? 1.833   5.327   -3.482  1.00 11.72 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? 2.408   5.035   -4.888  1.00 12.87 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? 2.544   5.961   -5.680  1.00 13.50 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? 2.843   6.031   -2.595  1.00 12.44 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? 3.029   7.486   -2.837  1.00 13.23 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? 2.012   8.400   -2.675  1.00 13.83 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? 4.107   8.179   -3.121  1.00 15.24 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? 2.500   9.612   -2.869  1.00 15.87 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? 3.766   9.516   -3.159  1.00 16.05 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? 2.852   3.806   -5.159  1.00 12.80 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? 3.477   3.468   -6.440  1.00 13.87 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? 2.486   3.679   -7.592  1.00 15.21 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? 2.929   3.921   -8.719  1.00 13.58 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? 3.979   2.015   -6.464  1.00 14.53 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? 2.850   1.014   -6.562  1.00 14.26 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? 4.971   1.774   -7.597  1.00 14.28 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? 1.175   3.691   -7.317  1.00 15.43 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? 0.232   3.876   -8.413  1.00 17.21 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? 0.124   5.340   -8.811  1.00 21.23 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -0.573  5.661   -9.784  1.00 26.75 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -1.149  3.241   -8.163  1.00 16.82 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -1.968  3.971   -7.099  1.00 18.22 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -1.007  1.774   -7.868  1.00 17.83 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -3.307  3.377   -6.797  1.00 18.96 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? 0.755   6.244   -8.080  1.00 17.11 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? 0.653   7.657   -8.403  1.00 16.83 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? 1.655   8.082   -9.474  1.00 20.94 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? 2.852   7.810   -9.382  1.00 22.41 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? 0.915   8.526   -7.182  1.00 15.87 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -0.266  8.340   -5.818  1.00 17.70 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? 1.168   8.883   -10.434 1.00 22.47 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? 2.052   9.750   -11.185 1.00 22.83 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? 2.512   10.916  -10.324 1.00 21.27 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? 1.977   11.229  -9.254  1.00 22.38 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? 1.376   10.322  -12.443 1.00 27.16 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? 0.669   11.484  -11.990 1.00 25.93 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? 0.487   9.338   -13.176 1.00 26.58 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? 3.511   11.635  -10.831 1.00 20.97 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? 4.005   12.828  -10.192 1.00 24.01 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? 2.870   13.738  -9.734  1.00 25.45 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? 2.905   14.278  -8.630  1.00 29.75 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? 4.931   13.563  -11.121 1.00 30.38 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? 5.509   14.642  -10.433 1.00 35.58 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? 1.891   13.976  -10.597 1.00 27.02 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? 0.874   14.960  -10.259 1.00 30.51 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? -0.083  14.356  -9.216  1.00 26.17 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -0.499  15.053  -8.290  1.00 28.02 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? 0.190   15.471  -11.529 1.00 36.80 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -0.365  14.373  -12.413 1.00 42.35 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -0.787  14.802  -13.811 1.00 57.13 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -1.635  15.718  -13.916 1.00 56.41 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -0.281  14.199  -14.793 1.00 58.73 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -0.303  13.040  -9.292  1.00 22.96 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.179  12.323  -8.371  1.00 21.01 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -0.634  12.380  -6.948  1.00 22.17 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -1.412  12.407  -5.997  1.00 19.79 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -1.352  10.866  -8.760  1.00 23.07 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.984  10.622  -10.111 1.00 26.02 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -2.885  11.417  -10.477 1.00 27.68 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -1.659  9.585   -10.730 1.00 24.76 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? 0.700   12.419  -6.816  1.00 20.06 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? 1.360   12.279  -5.524  1.00 19.69 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? 0.936   13.365  -4.548  1.00 20.68 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? 0.863   13.159  -3.335  1.00 19.13 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? 2.870   12.343  -5.728  1.00 19.00 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? 3.392   11.103  -6.328  1.00 20.33 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? 5.145   11.197  -6.720  0.93 21.76 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? 5.490   9.523   -7.235  1.00 24.89 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? 0.665   14.568  -5.061  1.00 22.69 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? 0.381   15.686  -4.179  1.00 25.33 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? -0.959  15.509  -3.476  1.00 23.40 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? -1.087  15.930  -2.334  1.00 26.51 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? 0.395   16.991  -4.986  1.00 30.12 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? 1.713   17.307  -5.703  1.00 37.40 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? 1.529   18.404  -6.761  1.00 39.37 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? 2.791   17.727  -4.706  1.00 37.72 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? -1.969  14.935  -4.151  1.00 22.14 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? -3.294  14.849  -3.564  1.00 22.04 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? -4.074  13.686  -4.151  1.00 20.78 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? -5.027  13.840  -4.929  1.00 22.83 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? -4.061  16.164  -3.732  1.00 25.01 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? -5.243  16.218  -2.788  1.00 28.32 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? -5.328  15.448  -1.830  1.00 31.41 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? -6.153  17.137  -3.031  1.00 34.32 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? -3.658  12.445  -3.851  1.00 17.65 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? -4.227  11.268  -4.508  1.00 16.08 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? -5.613  10.853  -4.004  1.00 18.14 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? -5.882  10.880  -2.812  1.00 17.44 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? -3.199  10.177  -4.153  1.00 15.75 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? -2.569  10.643  -2.883  1.00 16.46 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? -2.584  12.151  -2.882  1.00 17.32 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? -6.473  10.408  -4.930  1.00 17.46 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? -7.655  9.654   -4.582  1.00 17.40 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? -7.406  8.212   -4.971  1.00 16.78 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? -7.550  7.854   -6.126  1.00 18.87 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? -8.894  10.195  -5.305  1.00 20.08 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? -10.189 9.536   -4.884  1.00 20.91 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? -10.318 8.318   -4.827  1.00 20.31 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? -11.195 10.346  -4.612  1.00 27.67 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? -6.967  7.400   -4.016  1.00 16.05 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? -6.423  6.096   -4.321  1.00 14.05 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? -7.477  5.127   -4.864  1.00 15.43 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? -7.142  4.328   -5.723  1.00 17.16 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? -5.769  5.464   -3.093  1.00 14.21 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? -4.409  6.073   -2.793  1.00 13.21 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -3.303  5.753   -3.578  1.00 12.90 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? -4.234  6.977   -1.735  1.00 14.18 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -2.066  6.292   -3.301  1.00 12.34 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? -2.996  7.520   -1.449  1.00 13.25 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -1.910  7.150   -2.227  1.00 13.54 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -0.679  7.623   -1.893  1.00 15.26 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? -8.726  5.112   -4.377  1.00 15.44 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? -9.680  4.198   -4.988  1.00 19.31 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? -9.889  4.505   -6.479  1.00 16.53 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? -10.026 3.574   -7.279  1.00 17.70 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? -11.036 4.206   -4.302  1.00 21.95 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? -10.993 3.640   -2.912  1.00 27.83 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? -11.014 2.130   -2.785  1.00 31.95 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? -10.977 1.424   -3.815  1.00 32.27 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? -11.088 1.669   -1.631  1.00 35.58 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? -9.969  5.789   -6.812  1.00 18.47 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? -10.080 6.214   -8.200  1.00 20.13 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? -8.841  5.807   -8.990  1.00 22.28 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? -8.945  5.275   -10.093 1.00 21.76 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? -10.148 7.727   -8.321  1.00 23.66 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? -11.514 8.326   -8.105  1.00 27.61 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? -12.481 7.537   -7.984  1.00 29.91 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? -11.573 9.584   -8.087  1.00 31.70 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? -7.657  6.043   -8.412  1.00 18.20 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? -6.433  5.736   -9.136  1.00 18.18 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? -6.363  4.243   -9.393  1.00 18.14 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? -5.944  3.821   -10.472 1.00 20.88 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? -5.210  6.236   -8.350  1.00 19.25 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? -5.002  7.745   -8.310  1.00 19.94 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? -3.872  8.120   -7.355  1.00 21.27 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? -4.702  8.338   -9.686  1.00 23.61 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? -6.802  3.417   -8.443  1.00 16.85 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? -6.606  1.989   -8.566  1.00 18.12 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? -7.582  1.397   -9.596  1.00 19.46 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? -7.215  0.466   -10.328 1.00 18.14 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? -6.778  1.304   -7.204  1.00 21.60 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? -6.413  -0.184  -7.195  1.00 26.90 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -4.933  -0.384  -7.505  1.00 28.03 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? -6.785  -0.846  -5.887  1.00 28.91 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? -8.838  1.878   -9.594  1.00 19.58 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? -9.838  1.381   -10.535 1.00 18.00 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? -9.346  1.593   -11.966 1.00 18.89 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? -9.770  0.870   -12.876 1.00 20.68 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? -11.242 2.004   -10.288 1.00 20.56 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? -12.347 1.132   -10.883 1.00 27.65 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? -11.356 3.441   -10.775 1.00 19.85 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? -12.467 -0.199  -10.230 1.00 30.64 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? -8.459  2.575   -12.162 1.00 17.07 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? -8.005  2.958   -13.487 1.00 19.51 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? -6.767  2.174   -13.913 1.00 22.26 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? -6.226  2.462   -14.973 1.00 22.24 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? -7.725  4.453   -13.567 1.00 18.73 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? -8.959  5.314   -13.350 1.00 18.71 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? -8.654  6.764   -13.137 1.00 21.09 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? -9.899  7.458   -12.924 1.00 25.29 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? -10.081 8.574   -12.234 1.00 28.50 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? -9.048  9.256   -11.790 1.00 31.41 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? -11.314 8.993   -11.998 1.00 30.54 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? -6.359  1.193   -13.111 1.00 23.34 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -5.220  0.343   -13.398 1.00 25.63 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -5.656  -1.074  -13.710 1.00 24.82 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? -6.666  -1.547  -13.214 1.00 23.16 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -4.307  0.254   -12.171 1.00 25.56 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -3.658  1.562   -11.765 1.00 25.87 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -2.717  2.147   -12.795 1.00 33.63 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -2.285  3.566   -12.468 1.00 42.03 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -3.452  4.449   -12.186 1.00 48.86 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -4.836  -1.788  -14.490 1.00 26.31 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -5.005  -3.223  -14.622 1.00 26.61 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.691  -3.930  -14.270 1.00 23.74 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -2.658  -3.286  -14.097 1.00 23.47 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -5.440  -3.564  -16.018 1.00 35.40 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -4.438  -3.153  -16.929 1.00 36.71 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.732  -5.257  -14.241 1.00 24.04 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -2.573  -6.071  -13.895 1.00 23.94 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -1.341  -5.717  -14.712 1.00 27.20 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -0.222  -5.719  -14.183 1.00 27.06 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -2.901  -7.551  -14.019 1.00 23.70 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.936  -8.027  -13.044 1.00 26.15 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -4.071  -7.494  -11.941 1.00 25.45 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -4.610  -9.097  -13.415 1.00 23.86 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -1.533  -5.442  -16.011 1.00 28.74 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -0.405  -5.268  -16.920 1.00 27.86 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? 0.241   -3.893  -16.726 1.00 24.95 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? 1.294   -3.633  -17.278 1.00 27.65 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -0.822  -5.547  -18.383 1.00 29.48 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -1.527  -4.382  -18.994 1.00 33.41 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -2.892  -4.369  -19.195 1.00 42.90 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -1.095  -3.162  -19.396 1.00 42.26 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -3.264  -3.195  -19.712 1.00 42.82 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -2.191  -2.446  -19.854 1.00 43.89 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -0.322  -3.014  -15.884 1.00 21.14 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? 0.306   -1.743  -15.605 1.00 20.20 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? 1.398   -1.909  -14.536 1.00 19.35 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? 2.145   -0.972  -14.284 1.00 22.36 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -0.723  -0.696  -15.159 1.00 24.96 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -1.754  -0.334  -16.218 1.00 26.27 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -2.941  -0.270  -15.928 1.00 22.63 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -1.322  -0.127  -17.451 1.00 28.99 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? 1.496   -3.077  -13.913 1.00 19.95 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? 2.486   -3.248  -12.846 1.00 21.42 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? 3.634   -4.119  -13.317 1.00 23.30 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? 3.422   -5.244  -13.758 1.00 27.53 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? 1.877   -3.929  -11.624 1.00 22.02 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? 0.769   -3.124  -11.037 1.00 22.53 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? 1.051   -2.092  -10.154 1.00 26.17 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -0.545  -3.393  -11.359 1.00 20.78 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? 0.030   -1.338  -9.607  1.00 24.53 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -1.560  -2.619  -10.829 1.00 23.36 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -1.274  -1.582  -9.973  1.00 24.45 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? 4.847   -3.614  -13.121 1.00 20.09 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? 6.043   -4.379  -13.441 1.00 21.80 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? 6.727   -4.730  -12.124 1.00 20.71 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? 7.091   -3.825  -11.391 1.00 19.70 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? 6.941   -3.518  -14.333 1.00 24.63 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? 8.324   -4.090  -14.672 1.00 28.58 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? 8.227   -5.463  -15.347 1.00 32.36 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? 9.112   -3.126  -15.559 1.00 32.22 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? 6.820   -6.024  -11.846 1.00 18.10 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? 7.498   -6.547  -10.676 1.00 18.79 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? 8.751   -7.271  -11.172 1.00 20.56 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? 8.659   -8.163  -12.016 1.00 17.85 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? 6.616   -7.506  -9.871  1.00 18.42 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? 7.358   -8.025  -8.659  1.00 19.11 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? 5.317   -6.823  -9.463  1.00 20.55 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? 9.898   -6.867  -10.618 1.00 21.73 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? 11.179  -7.439  -10.960 1.00 23.44 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? 11.876  -7.967  -9.711  1.00 20.70 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? 12.036  -7.235  -8.727  1.00 18.50 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? 12.008  -6.344  -11.618 1.00 25.74 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? 11.442  -5.973  -12.986 1.00 30.12 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? 12.150  -4.766  -13.546 1.00 33.53 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? 11.994  -3.641  -13.076 1.00 34.58 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? 12.897  -4.987  -14.610 1.00 36.51 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? 12.248  -9.252  -9.766  1.00 20.47 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? 13.047  -9.881  -8.740  1.00 20.34 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? 14.422  -10.106 -9.347  1.00 27.24 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? 14.594  -11.056 -10.110 1.00 26.13 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? 12.440  -11.188 -8.316  1.00 23.45 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? 15.355  -9.205  -9.037  1.00 29.29 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? 16.575  -9.090  -9.820  1.00 34.20 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? 16.244  -8.694  -11.255 1.00 39.75 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? 15.598  -7.668  -11.480 1.00 44.82 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? 16.640  -9.551  -12.203 1.00 42.49 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? 16.366  -9.332  -13.616 1.00 48.15 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? 15.179  -10.175 -14.100 1.00 44.52 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? 14.776  -10.046 -15.245 1.00 47.59 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? 17.612  -9.594  -14.467 1.00 53.83 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? 18.349  -10.850 -14.058 1.00 56.64 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? 17.731  -11.867 -13.763 1.00 59.21 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? 19.668  -10.773 -13.989 1.00 64.26 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? 14.600  -11.026 -13.244 1.00 35.73 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? 13.426  -11.798 -13.612 1.00 31.08 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? 12.187  -10.934 -13.376 1.00 29.08 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? 12.047  -10.359 -12.308 1.00 27.00 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? 13.368  -13.100 -12.803 1.00 35.89 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? 11.992  -13.727 -12.815 1.00 40.52 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? 14.428  -14.080 -13.280 1.00 41.76 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? 11.292  -10.889 -14.358 1.00 24.12 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? 10.010  -10.201 -14.241 1.00 26.58 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? 8.981   -11.195 -13.701 1.00 27.12 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? 8.942   -12.337 -14.145 1.00 24.11 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? 9.641   -9.594  -15.597 1.00 30.50 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? 8.163   -9.278  -15.756 1.00 38.20 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? 7.824   -8.489  -17.002 1.00 46.79 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? 8.689   -8.115  -17.797 1.00 49.42 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? 6.544   -8.192  -17.152 1.00 42.08 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? 8.162   -10.781 -12.722 1.00 21.77 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? 7.108   -11.619 -12.185 1.00 24.44 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? 5.802   -11.071 -12.752 1.00 24.73 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? 5.507   -9.883  -12.623 1.00 28.17 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? 7.090   -11.600 -10.643 1.00 22.55 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? 8.426   -11.881 -9.964  1.00 21.26 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? 8.286   -11.809 -8.448  1.00 20.39 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? 8.962   -13.241 -10.368 1.00 24.54 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? 5.041   -11.941 -13.401 1.00 21.37 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? 3.804   -11.509 -14.023 1.00 23.01 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? 2.723   -11.344 -12.956 1.00 17.24 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? 2.464   -12.265 -12.201 1.00 18.50 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? 3.349   -12.552 -15.046 1.00 28.09 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? 2.173   -12.101 -15.897 1.00 34.75 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? 1.880   -13.130 -16.978 1.00 40.68 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? 1.394   -14.376 -16.386 1.00 45.24 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? 0.148   -14.851 -16.498 1.00 51.69 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -0.795  -14.139 -17.098 1.00 50.87 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? -0.152  -16.036 -15.986 1.00 47.37 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? 2.063   -10.190 -12.982 1.00 19.16 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? 0.997   -9.836  -12.049 1.00 17.65 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -0.331  -10.361 -12.596 1.00 19.41 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -0.660  -10.048 -13.735 1.00 19.96 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? 0.962   -8.313  -11.873 1.00 19.72 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -0.273  -7.843  -11.122 1.00 18.27 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? 2.257   -7.806  -11.218 1.00 20.16 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -1.021  -11.192 -11.815 1.00 20.77 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -2.290  -11.820 -12.222 1.00 21.61 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.462  -11.366 -11.345 1.00 22.68 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -4.609  -11.778 -11.504 1.00 20.43 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -2.140  -13.352 -12.238 1.00 22.16 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -1.809  -13.922 -10.860 1.00 22.62 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -1.094  -13.701 -13.279 1.00 21.81 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -1.926  -15.398 -10.735 1.00 23.08 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.206  -10.453 -10.418 1.00 21.25 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -4.283  -9.898  -9.626  1.00 21.21 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -3.767  -8.717  -8.815  1.00 20.39 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -2.571  -8.635  -8.513  1.00 17.44 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -4.683  -7.821  -8.440  1.00 20.58 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -4.285  -6.693  -7.605  1.00 20.97 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -5.437  -6.363  -6.655  1.00 22.58 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? -6.606  -6.564  -6.985  1.00 20.03 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -3.781  -5.510  -8.434  1.00 22.40 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -4.805  -4.917  -9.332  1.00 25.78 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -5.100  -5.426  -10.586 1.00 28.81 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -5.615  -3.858  -9.156  1.00 26.53 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -6.058  -4.686  -11.144 1.00 28.11 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? -6.401  -3.736  -10.292 1.00 26.51 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -5.081  -5.852  -5.468  1.00 19.22 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? -6.043  -5.299  -4.528  1.00 16.84 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? -5.279  -4.342  -3.618  1.00 19.28 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -4.030  -4.339  -3.652  1.00 17.41 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? -6.738  -6.377  -3.757  1.00 20.11 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? -5.826  -7.132  -2.994  1.00 22.64 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? -6.037  -3.529  -2.871  1.00 15.05 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? -5.471  -2.580  -1.936  1.00 15.35 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? -6.062  -2.895  -0.562  1.00 15.97 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? -7.254  -3.170  -0.450  1.00 14.69 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? -5.901  -1.204  -2.417  1.00 19.42 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? -5.624  -0.103  -1.542  1.00 20.66 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? -5.845  1.432   -2.455  1.00 19.49 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? -7.630  1.588   -2.595  1.00 21.98 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? -5.218  -2.927  0.469   1.00 12.90 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? -5.666  -3.021  1.842   1.00 12.95 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? -5.114  -1.781  2.555   1.00 13.57 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -3.924  -1.719  2.870   1.00 11.63 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? -5.147  -4.287  2.511   1.00 13.72 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? -5.531  -4.439  3.960   1.00 14.67 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? -5.012  -5.725  4.539   1.00 15.39 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? -4.262  -6.473  3.890   1.00 18.21 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? -5.440  -6.022  5.760   1.00 17.20 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? -5.984  -0.806  2.822   1.00 12.48 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? -5.537  0.479   3.370   1.00 11.74 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? -4.417  1.048   2.500   1.00 13.13 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? -4.597  1.157   1.293   1.00 13.33 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? -5.209  0.330   4.839   1.00 12.96 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? -6.369  -0.267  5.604   1.00 14.30 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? -7.463  0.298   5.536   1.00 17.99 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? -6.158  -1.411  6.233   1.00 14.27 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -3.243  1.382   3.087   1.00 10.73 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -2.191  2.003   2.303   1.00 11.40 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -1.254  0.983   1.634   1.00 10.31 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -0.211  1.395   1.081   1.00 11.23 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.397  2.960   3.173   1.00 12.58 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -2.459  4.245   3.890   1.00 15.17 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -1.561  -0.311  1.718   1.00 10.59 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -0.735  -1.338  1.070   1.00 11.99 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -1.395  -1.937  -0.184  1.00 12.47 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -2.555  -2.346  -0.170  1.00 15.23 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -0.389  -2.427  2.087   1.00 13.04 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? 0.110   -3.703  1.460   1.00 16.01 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? 0.669   -1.884  3.012   1.00 15.10 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -0.630  -1.982  -1.285  1.00 12.29 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -1.058  -2.671  -2.481  1.00 12.83 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -0.590  -4.117  -2.373  1.00 14.67 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? 0.528   -4.393  -1.914  1.00 14.26 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -0.451  -1.872  -3.633  1.00 13.73 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -0.740  -2.312  -5.060  1.00 16.39 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -2.147  -1.924  -5.461  1.00 16.57 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? 0.258   -1.670  -6.022  1.00 17.85 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -1.447  -5.021  -2.846  1.00 12.67 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -1.165  -6.448  -2.879  1.00 13.49 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -1.263  -6.923  -4.319  1.00 16.52 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -2.360  -6.910  -4.924  1.00 17.22 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -2.080  -7.214  -1.949  1.00 14.25 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -1.865  -6.862  -0.474  1.00 16.91 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -2.716  -7.624  0.519   1.00 19.91 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -4.203  -7.524  0.328   1.00 25.62 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -4.901  -8.091  1.510   1.00 24.69 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -0.122  -7.345  -4.861  1.00 14.76 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -0.084  -7.823  -6.238  1.00 15.36 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? 0.099   -9.342  -6.225  1.00 17.35 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? 1.093   -9.851  -5.730  1.00 15.74 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? 1.051   -7.152  -7.001  1.00 15.40 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? 1.034   -5.641  -7.035  1.00 16.51 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? 2.258   -5.095  -7.733  1.00 18.57 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -0.215  -5.122  -7.689  1.00 16.73 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -0.903  -10.080 -6.728  1.00 17.18 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -0.786  -11.516 -6.853  1.00 18.08 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? 0.095   -11.780 -8.065  1.00 16.24 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -0.141  -11.164 -9.092  1.00 18.30 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -2.153  -12.181 -7.058  1.00 21.92 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -2.124  -13.696 -6.873  1.00 25.89 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -3.488  -14.331 -6.951  1.00 31.71 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.462  -15.791 -6.545  1.00 38.93 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -4.741  -16.469 -6.880  1.00 42.85 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? 1.109   -12.652 -7.938  1.00 16.18 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? 1.969   -12.959 -9.071  1.00 16.31 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? 1.831   -14.458 -9.335  1.00 16.77 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? 1.306   -15.201 -8.513  1.00 18.59 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? 3.432   -12.539 -8.818  1.00 16.40 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? 3.549   -11.037 -8.747  1.00 17.80 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? 4.026   -13.135 -7.561  1.00 16.79 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? 2.304   -14.906 -10.493 1.00 22.94 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? 2.023   -16.279 -10.892 1.00 25.43 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? 3.131   -17.229 -10.438 1.00 30.52 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? 3.190   -18.358 -10.897 1.00 27.03 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? 1.769   -16.352 -12.397 1.00 29.29 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? 2.966   -16.010 -13.272 1.00 33.70 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? 4.014   -15.641 -12.734 1.00 33.18 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? 2.849   -16.151 -14.502 1.00 39.70 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? 4.048   -16.795 -9.566  1.00 28.43 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? 5.098   -17.692 -9.097  1.00 30.30 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? 5.326   -17.462 -7.614  1.00 24.72 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? 5.285   -16.316 -7.177  1.00 23.70 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? 6.368   -17.511 -9.937  1.00 37.56 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? 6.854   -16.196 -9.715  1.00 41.52 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? 6.138   -17.669 -11.424 1.00 43.29 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? 5.519   -18.551 -6.866  1.00 21.21 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? 5.753   -18.486 -5.435  1.00 20.74 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? 7.227   -18.176 -5.161  1.00 20.79 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? 8.124   -18.686 -5.837  1.00 21.28 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? 5.366   -19.786 -4.766  1.00 23.60 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? 7.483   -17.337 -4.151  1.00 20.00 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? 8.865   -17.084 -3.748  1.00 17.85 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? 9.407   -18.259 -2.941  1.00 16.12 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? 8.997   -18.486 -1.817  1.00 15.53 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? 8.946   -15.828 -2.871  1.00 15.72 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? 10.371  -15.511 -2.492  1.00 18.69 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? 11.302  -16.214 -2.901  1.00 15.87 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? 10.548  -14.418 -1.756  1.00 19.02 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? 10.394  -19.056 -3.429  1.00 20.94 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? 10.901  -20.177 -2.652  1.00 23.11 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? 11.687  -19.791 -1.403  1.00 20.27 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? 11.893  -20.616 -0.520  1.00 21.64 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? 11.869  -20.903 -3.598  1.00 23.64 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? 12.150  -19.965 -4.710  1.00 24.19 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? 11.084  -18.887 -4.697  1.00 23.37 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? 12.117  -18.517 -1.358  1.00 17.94 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? 12.838  -18.005 -0.205  1.00 18.47 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? 11.904  -17.440 0.875   1.00 16.53 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? 12.400  -16.865 1.853   1.00 16.82 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? 13.801  -16.920 -0.686  1.00 20.02 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? 14.749  -17.359 -1.794  1.00 24.11 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? 15.838  -16.378 -2.109  1.00 27.05 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? 16.834  -16.949 -3.096  1.00 32.01 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? 17.722  -17.914 -2.416  1.00 38.53 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? 10.579  -17.592 0.730   1.00 16.83 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? 9.645   -17.118 1.757   1.00 17.04 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? 9.953   -17.759 3.096   1.00 17.60 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? 9.878   -18.997 3.214   1.00 17.22 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? 8.176   -17.436 1.421   1.00 16.68 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? 7.953   -16.952 0.115   1.00 17.13 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? 7.235   -16.811 2.410   1.00 17.65 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? 10.198  -16.972 4.167   1.00 15.32 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? 10.410  -17.521 5.501   1.00 15.67 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? 9.065   -17.788 6.141   1.00 14.80 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? 8.053   -17.297 5.642   1.00 16.61 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? 11.157  -16.395 6.213   1.00 16.75 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? 10.577  -15.145 5.614   1.00 15.26 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? 10.314  -15.490 4.169   1.00 15.42 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? 9.065   -18.514 7.261   1.00 15.54 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? 7.947   -18.477 8.168   1.00 17.04 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? 7.772   -17.031 8.636   1.00 17.24 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? 8.760   -16.387 9.025   1.00 16.98 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? 8.178   -19.370 9.378   1.00 25.23 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? 8.173   -20.847 9.030   1.00 31.86 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? 8.192   -21.756 10.237  1.00 41.78 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? 8.542   -23.186 9.877   1.00 45.67 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? 9.445   -23.773 10.894  1.00 51.89 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? 6.534   -16.533 8.620   1.00 14.96 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? 6.380   -15.118 8.954   1.00 15.39 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? 5.019   -14.848 9.568   1.00 16.44 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? 4.082   -15.646 9.432   1.00 16.88 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? 6.587   -14.282 7.688   1.00 15.34 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? 5.417   -14.290 6.721   1.00 14.87 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? 5.311   -15.271 5.717   1.00 16.15 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? 4.395   -13.353 6.827   1.00 16.72 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? 4.249   -15.292 4.834   1.00 18.83 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? 3.308   -13.400 5.972   1.00 19.28 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? 3.239   -14.355 4.978   1.00 20.53 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? 2.146   -14.365 4.174   1.00 22.50 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? 4.908   -13.648 10.161  1.00 15.72 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? 3.637   -13.103 10.588  1.00 16.65 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? 3.672   -11.596 10.342  1.00 14.78 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? 4.759   -11.010 10.248  1.00 12.74 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? 3.459   -13.270 12.095  1.00 23.10 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? 3.432   -14.701 12.599  1.00 33.68 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? 2.932   -14.791 14.023  1.00 43.08 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? 4.023   -14.695 15.067  1.00 48.17 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? 4.810   -13.446 14.948  1.00 49.54 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? 2.482   -10.998 10.334  1.00 13.60 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? 2.341   -9.547  10.280  1.00 12.85 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? 1.927   -9.114  11.678  1.00 15.28 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? 0.996   -9.697  12.254  1.00 16.59 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? 1.345   -9.127  9.192   1.00 14.11 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? 1.743   -9.348  7.764   1.00 13.16 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? 3.062   -9.611  7.397   1.00 13.14 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? 0.811   -9.182  6.761   1.00 14.65 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? 3.406   -9.726  6.062   1.00 13.14 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? 1.168   -9.286  5.427   1.00 14.79 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? 2.471   -9.547  5.080   1.00 14.21 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? 2.639   -8.159  12.273  1.00 14.05 ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? 2.310   -7.719  13.621  1.00 15.31 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? 2.312   -6.200  13.654  1.00 16.94 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? 3.066   -5.556  12.919  1.00 16.75 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? 3.270   -8.274  14.678  1.00 18.88 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? 3.317   -9.800  14.660  1.00 20.89 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? 4.653   -7.660  14.549  1.00 19.65 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? 1.457   -5.634  14.503  1.00 13.56 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? 1.497   -4.203  14.731  1.00 15.45 ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? 2.175   -3.993  16.081  1.00 15.18 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? 1.704   -4.520  17.086  1.00 16.61 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? 0.077   -3.635  14.733  1.00 16.48 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? 0.021   -2.119  14.944  1.00 18.59 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.269  -1.468  14.536  1.00 15.63 ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.219  -0.028  14.732  1.00 16.62 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.042  0.878   13.784  1.00 15.74 ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -0.850  0.512   12.519  1.00 14.18 ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.031  2.160   14.113  1.00 14.50 ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? 3.234   -3.194  16.104  1.00 14.26 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? 3.980   -2.954  17.322  1.00 16.22 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? 3.472   -1.719  18.050  1.00 15.50 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? 2.755   -0.877  17.502  1.00 14.15 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? 5.501   -2.887  17.080  1.00 17.54 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? 5.840   -1.750  16.121  1.00 16.91 ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? 6.057   -4.246  16.681  1.00 20.86 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? 7.290   -1.449  16.047  1.00 20.30 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? 3.862   -1.658  19.333  1.00 16.55 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? 3.533   -0.567  20.227  1.00 19.86 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? 4.684   0.420   20.305  1.00 15.50 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? 5.850   0.061   20.125  1.00 14.55 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? 3.280   -1.130  21.621  1.00 26.73 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? 2.306   -2.297  21.643  1.00 32.86 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? 0.900   -1.819  21.855  1.00 38.95 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? 0.622   -1.064  22.785  1.00 48.77 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -0.009  -2.271  21.008  1.00 45.06 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? 4.435   1.679   20.698  1.00 18.15 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? 5.506   2.638   20.875  1.00 19.31 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? 6.468   2.134   21.942  1.00 18.15 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? 6.027   1.569   22.937  1.00 16.93 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? 4.830   3.950   21.319  1.00 22.42 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? 3.408   3.755   20.987  1.00 21.98 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? 3.116   2.269   21.002  1.00 22.08 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? 7.762   2.316   21.652  1.00 15.26 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? 8.851   1.892   22.504  1.00 17.18 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? 9.441   0.550   22.093  1.00 17.30 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? 10.516  0.186   22.554  1.00 18.79 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? 8.695   -0.216  21.293  1.00 14.33 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? 9.204   -1.494  20.827  1.00 14.03 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? 10.200  -1.248  19.696  1.00 12.57 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? 10.073  -0.275  18.939  1.00 13.62 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? 8.077   -2.413  20.364  1.00 16.00 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? 7.170   -2.829  21.517  1.00 19.60 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? 6.204   -3.955  21.236  1.00 26.85 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? 5.322   -3.898  20.377  1.00 25.39 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? 6.253   -4.961  22.100  1.00 35.44 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? 11.156  -2.178  19.561  1.00 12.04 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? 12.243  -2.001  18.615  1.00 11.90 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? 12.082  -3.025  17.491  1.00 10.19 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? 11.418  -4.059  17.620  1.00 10.62 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? 13.635  -2.119  19.253  1.00 13.65 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? 13.700  -3.377  19.923  1.00 14.11 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? 13.979  -0.969  20.172  1.00 14.90 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? 12.784  -2.753  16.399  1.00 10.39 ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? 12.787  -3.638  15.253  1.00 9.72  ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? 13.971  -3.296  14.385  1.00 9.54  ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? 14.551  -2.215  14.467  1.00 11.15 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? 11.495  -3.518  14.431  1.00 9.68  ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? 11.164  -2.141  13.955  1.00 11.27 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? 10.517  -1.248  14.801  1.00 12.44 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? 11.479  -1.718  12.677  1.00 11.35 ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? 10.181  0.021   14.352  1.00 12.85 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? 11.141  -0.447  12.229  1.00 13.41 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? 10.450  0.408   13.059  1.00 13.93 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? 14.310  -4.259  13.525  1.00 10.57 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? 15.359  -4.097  12.541  1.00 8.99  ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? 14.774  -3.574  11.237  1.00 9.50  ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? 13.727  -4.010  10.802  1.00 9.75  ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? 16.073  -5.426  12.307  1.00 8.67  ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? 16.715  -5.855  13.481  1.00 9.00  ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? 15.520  -2.677  10.592  1.00 10.06 ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? 15.150  -2.159  9.297   1.00 10.12 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? 16.134  -2.676  8.262   1.00 8.95  ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? 17.329  -2.512  8.456   1.00 9.05  ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? 15.126  -0.631  9.344   1.00 12.33 ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? 14.994  -0.036  7.962   1.00 13.84 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? 13.996  -0.124  10.211  1.00 14.13 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? 15.599  -3.139  7.124   1.00 8.69  ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? 16.411  -3.427  5.956   1.00 10.02 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? 16.131  -2.351  4.931   1.00 10.41 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? 15.088  -2.395  4.269   1.00 11.59 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? 16.096  -4.806  5.380   1.00 9.68  ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? 16.962  -5.202  4.176   1.00 11.35 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? 18.445  -5.366  4.561   1.00 12.44 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? 16.452  -6.470  3.542   1.00 12.31 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? 17.034  -1.363  4.848   1.00 10.19 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? 16.895  -0.292  3.871   1.00 9.75  ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? 17.229  -0.835  2.483   1.00 10.31 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? 18.248  -1.515  2.311   1.00 12.66 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? 17.827  0.846   4.262   1.00 11.08 ? 116 ALA   A CB  1 
ATOM   907  N  N   A CYS   A 1 117 ? 16.341  -0.603  1.513   0.80 10.45 ? 117 CYS   A N   1 
ATOM   908  N  N   B CYS   A 1 117 ? 16.396  -0.499  1.485   0.20 10.74 ? 117 CYS   A N   1 
ATOM   909  C  CA  A CYS   A 1 117 ? 16.541  -1.102  0.162   0.80 11.45 ? 117 CYS   A CA  1 
ATOM   910  C  CA  B CYS   A 1 117 ? 16.412  -1.142  0.173   0.20 11.10 ? 117 CYS   A CA  1 
ATOM   911  C  C   A CYS   A 1 117 ? 16.312  0.031   -0.835  0.80 11.78 ? 117 CYS   A C   1 
ATOM   912  C  C   B CYS   A 1 117 ? 16.151  -0.086  -0.912  0.20 11.85 ? 117 CYS   A C   1 
ATOM   913  O  O   A CYS   A 1 117 ? 15.597  0.983   -0.536  0.80 10.66 ? 117 CYS   A O   1 
ATOM   914  O  O   B CYS   A 1 117 ? 15.251  0.730   -0.747  0.20 11.47 ? 117 CYS   A O   1 
ATOM   915  C  CB  A CYS   A 1 117 ? 15.544  -2.189  -0.174  0.80 11.73 ? 117 CYS   A CB  1 
ATOM   916  C  CB  B CYS   A 1 117 ? 15.347  -2.238  0.160   0.20 10.78 ? 117 CYS   A CB  1 
ATOM   917  S  SG  A CYS   A 1 117 ? 15.712  -3.658  0.854   0.80 14.27 ? 117 CYS   A SG  1 
ATOM   918  S  SG  B CYS   A 1 117 ? 15.442  -3.426  -1.208  0.20 10.60 ? 117 CYS   A SG  1 
ATOM   919  N  N   . TYR   A 1 118 ? 16.934  -0.106  -2.008  1.00 12.59 ? 118 TYR   A N   1 
ATOM   920  C  CA  . TYR   A 1 118 ? 16.825  0.841   -3.124  1.00 15.87 ? 118 TYR   A CA  1 
ATOM   921  C  C   . TYR   A 1 118 ? 16.678  0.042   -4.423  1.00 16.61 ? 118 TYR   A C   1 
ATOM   922  O  O   . TYR   A 1 118 ? 17.424  -0.904  -4.664  1.00 17.64 ? 118 TYR   A O   1 
ATOM   923  C  CB  . TYR   A 1 118 ? 18.057  1.751   -3.118  1.00 16.01 ? 118 TYR   A CB  1 
ATOM   924  C  CG  . TYR   A 1 118 ? 18.114  2.547   -1.834  1.00 15.95 ? 118 TYR   A CG  1 
ATOM   925  C  CD1 . TYR   A 1 118 ? 17.363  3.713   -1.685  1.00 14.30 ? 118 TYR   A CD1 1 
ATOM   926  C  CD2 . TYR   A 1 118 ? 18.795  2.078   -0.723  1.00 13.93 ? 118 TYR   A CD2 1 
ATOM   927  C  CE1 . TYR   A 1 118 ? 17.349  4.411   -0.501  1.00 13.75 ? 118 TYR   A CE1 1 
ATOM   928  C  CE2 . TYR   A 1 118 ? 18.774  2.751   0.481   1.00 14.99 ? 118 TYR   A CE2 1 
ATOM   929  C  CZ  . TYR   A 1 118 ? 18.053  3.930   0.590   1.00 14.34 ? 118 TYR   A CZ  1 
ATOM   930  O  OH  . TYR   A 1 118 ? 17.965  4.533   1.796   1.00 12.89 ? 118 TYR   A OH  1 
ATOM   931  N  N   . ASN   A 1 119 ? 15.610  0.307   -5.187  1.00 19.65 ? 119 ASN   A N   1 
ATOM   932  C  CA  . ASN   A 1 119 ? 15.376  -0.393  -6.451  1.00 22.29 ? 119 ASN   A CA  1 
ATOM   933  C  C   . ASN   A 1 119 ? 15.336  -1.894  -6.249  1.00 20.35 ? 119 ASN   A C   1 
ATOM   934  O  O   . ASN   A 1 119 ? 15.849  -2.648  -7.065  1.00 21.28 ? 119 ASN   A O   1 
ATOM   935  C  CB  . ASN   A 1 119 ? 16.432  -0.028  -7.493  1.00 26.22 ? 119 ASN   A CB  1 
ATOM   936  C  CG  . ASN   A 1 119 ? 16.373  1.455   -7.797  1.00 34.19 ? 119 ASN   A CG  1 
ATOM   937  O  OD1 . ASN   A 1 119 ? 15.333  1.961   -8.229  1.00 38.30 ? 119 ASN   A OD1 1 
ATOM   938  N  ND2 . ASN   A 1 119 ? 17.453  2.158   -7.505  1.00 33.16 ? 119 ASN   A ND2 1 
ATOM   939  N  N   . GLY   A 1 120 ? 14.744  -2.341  -5.134  1.00 17.70 ? 120 GLY   A N   1 
ATOM   940  C  CA  . GLY   A 1 120 ? 14.615  -3.751  -4.844  1.00 16.82 ? 120 GLY   A CA  1 
ATOM   941  C  C   . GLY   A 1 120 ? 15.880  -4.420  -4.301  1.00 18.06 ? 120 GLY   A C   1 
ATOM   942  O  O   . GLY   A 1 120 ? 15.825  -5.610  -4.031  1.00 20.55 ? 120 GLY   A O   1 
ATOM   943  N  N   . SER   A 1 121 ? 16.972  -3.669  -4.130  1.00 16.91 ? 121 SER   A N   1 
ATOM   944  C  CA  A SER   A 1 121 ? 18.253  -4.218  -3.704  0.55 17.36 ? 121 SER   A CA  1 
ATOM   945  C  CA  B SER   A 1 121 ? 18.258  -4.213  -3.712  0.45 17.70 ? 121 SER   A CA  1 
ATOM   946  C  C   . SER   A 1 121 ? 18.584  -3.809  -2.268  1.00 16.43 ? 121 SER   A C   1 
ATOM   947  O  O   . SER   A 1 121 ? 18.701  -2.620  -1.932  1.00 14.31 ? 121 SER   A O   1 
ATOM   948  C  CB  A SER   A 1 121 ? 19.350  -3.780  -4.617  0.55 18.25 ? 121 SER   A CB  1 
ATOM   949  C  CB  B SER   A 1 121 ? 19.344  -3.758  -4.649  0.45 19.03 ? 121 SER   A CB  1 
ATOM   950  O  OG  A SER   A 1 121 ? 19.209  -4.401  -5.879  0.55 19.22 ? 121 SER   A OG  1 
ATOM   951  O  OG  B SER   A 1 121 ? 20.567  -4.428  -4.380  0.45 21.10 ? 121 SER   A OG  1 
ATOM   952  N  N   . PRO   A 1 122 ? 18.815  -4.770  -1.363  1.00 16.26 ? 122 PRO   A N   1 
ATOM   953  C  CA  . PRO   A 1 122 ? 19.126  -4.415  0.025   1.00 15.76 ? 122 PRO   A CA  1 
ATOM   954  C  C   . PRO   A 1 122 ? 20.413  -3.621  0.143   1.00 15.19 ? 122 PRO   A C   1 
ATOM   955  O  O   . PRO   A 1 122 ? 21.425  -3.942  -0.492  1.00 16.00 ? 122 PRO   A O   1 
ATOM   956  C  CB  . PRO   A 1 122 ? 19.216  -5.778  0.718   1.00 16.40 ? 122 PRO   A CB  1 
ATOM   957  C  CG  . PRO   A 1 122 ? 18.336  -6.659  -0.127  1.00 19.39 ? 122 PRO   A CG  1 
ATOM   958  C  CD  . PRO   A 1 122 ? 18.656  -6.223  -1.543  1.00 20.03 ? 122 PRO   A CD  1 
ATOM   959  N  N   . SER   A 1 123 ? 20.414  -2.636  1.032   1.00 13.03 ? 123 SER   A N   1 
ATOM   960  C  CA  . SER   A 1 123 ? 21.513  -1.688  1.135   1.00 15.56 ? 123 SER   A CA  1 
ATOM   961  C  C   . SER   A 1 123 ? 22.156  -1.694  2.530   1.00 14.77 ? 123 SER   A C   1 
ATOM   962  O  O   . SER   A 1 123 ? 23.386  -1.539  2.700   1.00 13.82 ? 123 SER   A O   1 
ATOM   963  C  CB  . SER   A 1 123 ? 21.015  -0.346  0.746   1.00 19.53 ? 123 SER   A CB  1 
ATOM   964  O  OG  . SER   A 1 123 ? 22.001  0.609   1.032   1.00 26.11 ? 123 SER   A OG  1 
ATOM   965  N  N   . GLY   A 1 124 ? 21.327  -1.787  3.574   1.00 12.19 ? 124 GLY   A N   1 
ATOM   966  C  CA  . GLY   A 1 124 ? 21.834  -1.681  4.929   1.00 11.61 ? 124 GLY   A CA  1 
ATOM   967  C  C   . GLY   A 1 124 ? 20.816  -2.172  5.947   1.00 10.92 ? 124 GLY   A C   1 
ATOM   968  O  O   . GLY   A 1 124 ? 19.623  -2.232  5.628   1.00 11.41 ? 124 GLY   A O   1 
ATOM   969  N  N   . VAL   A 1 125 ? 21.289  -2.477  7.152   1.00 10.06 ? 125 VAL   A N   1 
ATOM   970  C  CA  A VAL   A 1 125 ? 20.427  -2.976  8.217   0.63 9.86  ? 125 VAL   A CA  1 
ATOM   971  C  CA  B VAL   A 1 125 ? 20.434  -2.983  8.223   0.37 9.99  ? 125 VAL   A CA  1 
ATOM   972  C  C   . VAL   A 1 125 ? 20.811  -2.258  9.504   1.00 11.41 ? 125 VAL   A C   1 
ATOM   973  O  O   . VAL   A 1 125 ? 22.016  -2.133  9.860   1.00 11.28 ? 125 VAL   A O   1 
ATOM   974  C  CB  A VAL   A 1 125 ? 20.499  -4.509  8.353   0.63 11.33 ? 125 VAL   A CB  1 
ATOM   975  C  CB  B VAL   A 1 125 ? 20.530  -4.503  8.464   0.37 10.51 ? 125 VAL   A CB  1 
ATOM   976  C  CG1 A VAL   A 1 125 ? 21.914  -4.997  8.533   0.63 10.82 ? 125 VAL   A CG1 1 
ATOM   977  C  CG1 B VAL   A 1 125 ? 19.198  -5.074  8.971   0.37 10.08 ? 125 VAL   A CG1 1 
ATOM   978  C  CG2 A VAL   A 1 125 ? 19.622  -5.038  9.492   0.63 10.87 ? 125 VAL   A CG2 1 
ATOM   979  C  CG2 B VAL   A 1 125 ? 20.998  -5.261  7.241   0.37 9.98  ? 125 VAL   A CG2 1 
ATOM   980  N  N   . TYR   A 1 126 ? 19.775  -1.862  10.251  1.00 10.71 ? 126 TYR   A N   1 
ATOM   981  C  CA  . TYR   A 1 126 ? 20.004  -1.232  11.528  1.00 11.34 ? 126 TYR   A CA  1 
ATOM   982  C  C   . TYR   A 1 126 ? 18.746  -1.347  12.373  1.00 11.60 ? 126 TYR   A C   1 
ATOM   983  O  O   . TYR   A 1 126 ? 17.664  -1.623  11.854  1.00 12.19 ? 126 TYR   A O   1 
ATOM   984  C  CB  . TYR   A 1 126 ? 20.342  0.243   11.319  1.00 13.10 ? 126 TYR   A CB  1 
ATOM   985  C  CG  . TYR   A 1 126 ? 19.304  1.008   10.515  1.00 14.92 ? 126 TYR   A CG  1 
ATOM   986  C  CD1 . TYR   A 1 126 ? 18.218  1.622   11.148  1.00 18.13 ? 126 TYR   A CD1 1 
ATOM   987  C  CD2 . TYR   A 1 126 ? 19.451  1.163   9.153   1.00 18.58 ? 126 TYR   A CD2 1 
ATOM   988  C  CE1 . TYR   A 1 126 ? 17.277  2.335   10.414  1.00 20.53 ? 126 TYR   A CE1 1 
ATOM   989  C  CE2 . TYR   A 1 126 ? 18.525  1.877   8.409   1.00 19.65 ? 126 TYR   A CE2 1 
ATOM   990  C  CZ  . TYR   A 1 126 ? 17.438  2.454   9.042   1.00 20.42 ? 126 TYR   A CZ  1 
ATOM   991  O  OH  . TYR   A 1 126 ? 16.543  3.184   8.321   1.00 22.39 ? 126 TYR   A OH  1 
ATOM   992  N  N   . GLN   A 1 127 ? 18.913  -1.096  13.657  1.00 12.07 ? 127 GLN   A N   1 
ATOM   993  C  CA  . GLN   A 1 127 ? 17.845  -1.203  14.629  1.00 13.86 ? 127 GLN   A CA  1 
ATOM   994  C  C   . GLN   A 1 127 ? 17.213  0.164   14.891  1.00 15.87 ? 127 GLN   A C   1 
ATOM   995  O  O   . GLN   A 1 127 ? 17.959  1.142   15.042  1.00 18.64 ? 127 GLN   A O   1 
ATOM   996  C  CB  . GLN   A 1 127 ? 18.477  -1.486  15.997  1.00 20.82 ? 127 GLN   A CB  1 
ATOM   997  C  CG  . GLN   A 1 127 ? 18.524  -2.905  16.423  1.00 23.77 ? 127 GLN   A CG  1 
ATOM   998  C  CD  . GLN   A 1 127 ? 17.230  -3.660  16.373  1.00 24.28 ? 127 GLN   A CD  1 
ATOM   999  O  OE1 . GLN   A 1 127 ? 16.957  -4.300  15.362  1.00 26.21 ? 127 GLN   A OE1 1 
ATOM   1000 N  NE2 . GLN   A 1 127 ? 16.533  -3.711  17.494  1.00 25.26 ? 127 GLN   A NE2 1 
ATOM   1001 N  N   A CYS   A 1 128 ? 15.870  0.210   14.978  0.58 14.39 ? 128 CYS   A N   1 
ATOM   1002 N  N   B CYS   A 1 128 ? 15.885  0.243   15.003  0.42 14.99 ? 128 CYS   A N   1 
ATOM   1003 C  CA  A CYS   A 1 128 ? 15.098  1.420   15.248  0.58 14.65 ? 128 CYS   A CA  1 
ATOM   1004 C  CA  B CYS   A 1 128 ? 15.290  1.487   15.470  0.42 15.20 ? 128 CYS   A CA  1 
ATOM   1005 C  C   A CYS   A 1 128 ? 14.100  1.155   16.378  0.58 15.43 ? 128 CYS   A C   1 
ATOM   1006 C  C   B CYS   A 1 128 ? 14.102  1.168   16.376  0.42 15.71 ? 128 CYS   A C   1 
ATOM   1007 O  O   A CYS   A 1 128 ? 13.852  -0.006  16.692  0.58 13.73 ? 128 CYS   A O   1 
ATOM   1008 O  O   B CYS   A 1 128 ? 13.790  -0.001  16.607  0.42 14.30 ? 128 CYS   A O   1 
ATOM   1009 C  CB  A CYS   A 1 128 ? 14.279  1.774   14.011  0.58 16.30 ? 128 CYS   A CB  1 
ATOM   1010 C  CB  B CYS   A 1 128 ? 14.912  2.342   14.278  0.42 17.79 ? 128 CYS   A CB  1 
ATOM   1011 S  SG  A CYS   A 1 128 ? 15.180  2.767   12.805  0.58 25.62 ? 128 CYS   A SG  1 
ATOM   1012 S  SG  B CYS   A 1 128 ? 13.684  1.512   13.270  0.42 19.46 ? 128 CYS   A SG  1 
ATOM   1013 N  N   . ALA   A 1 129 ? 13.499  2.212   16.955  1.00 15.76 ? 129 ALA   A N   1 
ATOM   1014 C  CA  . ALA   A 1 129 ? 12.356  2.050   17.847  1.00 14.99 ? 129 ALA   A CA  1 
ATOM   1015 C  C   . ALA   A 1 129 ? 11.168  2.827   17.275  1.00 12.94 ? 129 ALA   A C   1 
ATOM   1016 O  O   . ALA   A 1 129 ? 11.344  3.867   16.662  1.00 14.36 ? 129 ALA   A O   1 
ATOM   1017 C  CB  . ALA   A 1 129 ? 12.645  2.477   19.273  1.00 18.38 ? 129 ALA   A CB  1 
ATOM   1018 N  N   . MET   A 1 130 ? 9.959   2.325   17.514  1.00 12.14 ? 130 MET   A N   1 
ATOM   1019 C  CA  . MET   A 1 130 ? 8.771   3.115   17.266  1.00 12.70 ? 130 MET   A CA  1 
ATOM   1020 C  C   . MET   A 1 130 ? 8.684   4.203   18.344  1.00 12.47 ? 130 MET   A C   1 
ATOM   1021 O  O   . MET   A 1 130 ? 8.666   3.867   19.521  1.00 15.15 ? 130 MET   A O   1 
ATOM   1022 C  CB  . MET   A 1 130 ? 7.559   2.209   17.307  1.00 13.00 ? 130 MET   A CB  1 
ATOM   1023 C  CG  . MET   A 1 130 ? 6.175   2.864   17.019  1.00 15.52 ? 130 MET   A CG  1 
ATOM   1024 S  SD  . MET   A 1 130 ? 6.094   3.725   15.463  1.00 18.42 ? 130 MET   A SD  1 
ATOM   1025 C  CE  . MET   A 1 130 ? 6.346   2.333   14.357  1.00 16.49 ? 130 MET   A CE  1 
ATOM   1026 N  N   . ARG   A 1 131 ? 8.698   5.471   17.966  1.00 12.63 ? 131 ARG   A N   1 
ATOM   1027 C  CA  . ARG   A 1 131 ? 8.699   6.560   18.953  1.00 12.68 ? 131 ARG   A CA  1 
ATOM   1028 C  C   . ARG   A 1 131 ? 7.310   6.648   19.562  1.00 13.17 ? 131 ARG   A C   1 
ATOM   1029 O  O   . ARG   A 1 131 ? 6.293   6.229   18.963  1.00 11.43 ? 131 ARG   A O   1 
ATOM   1030 C  CB  . ARG   A 1 131 ? 9.058   7.907   18.323  1.00 12.46 ? 131 ARG   A CB  1 
ATOM   1031 C  CG  . ARG   A 1 131 ? 10.409  8.002   17.595  1.00 12.97 ? 131 ARG   A CG  1 
ATOM   1032 C  CD  . ARG   A 1 131 ? 11.590  7.690   18.474  1.00 13.35 ? 131 ARG   A CD  1 
ATOM   1033 N  NE  . ARG   A 1 131 ? 11.559  8.466   19.717  1.00 15.78 ? 131 ARG   A NE  1 
ATOM   1034 C  CZ  . ARG   A 1 131 ? 12.265  8.140   20.793  1.00 15.31 ? 131 ARG   A CZ  1 
ATOM   1035 N  NH1 . ARG   A 1 131 ? 13.146  7.159   20.713  1.00 14.55 ? 131 ARG   A NH1 1 
ATOM   1036 N  NH2 . ARG   A 1 131 ? 12.049  8.760   21.950  1.00 14.33 ? 131 ARG   A NH2 1 
ATOM   1037 N  N   . PRO   A 1 132 ? 7.174   7.199   20.792  1.00 13.54 ? 132 PRO   A N   1 
ATOM   1038 C  CA  . PRO   A 1 132 ? 5.856   7.528   21.324  1.00 14.26 ? 132 PRO   A CA  1 
ATOM   1039 C  C   . PRO   A 1 132 ? 4.945   8.334   20.418  1.00 13.22 ? 132 PRO   A C   1 
ATOM   1040 O  O   . PRO   A 1 132 ? 3.738   8.121   20.513  1.00 16.03 ? 132 PRO   A O   1 
ATOM   1041 C  CB  . PRO   A 1 132 ? 6.208   8.266   22.621  1.00 14.35 ? 132 PRO   A CB  1 
ATOM   1042 C  CG  . PRO   A 1 132 ? 7.468   7.597   23.055  1.00 14.34 ? 132 PRO   A CG  1 
ATOM   1043 C  CD  . PRO   A 1 132 ? 8.250   7.499   21.764  1.00 14.66 ? 132 PRO   A CD  1 
ATOM   1044 N  N   . ASN   A 1 133 ? 5.489   9.197   19.546  1.00 12.43 ? 133 ASN   A N   1 
ATOM   1045 C  CA  . ASN   A 1 133 ? 4.696   9.980   18.603  1.00 12.86 ? 133 ASN   A CA  1 
ATOM   1046 C  C   . ASN   A 1 133 ? 4.501   9.285   17.248  1.00 12.39 ? 133 ASN   A C   1 
ATOM   1047 O  O   . ASN   A 1 133 ? 4.094   9.917   16.270  1.00 13.32 ? 133 ASN   A O   1 
ATOM   1048 C  CB  . ASN   A 1 133 ? 5.294   11.362  18.400  1.00 14.42 ? 133 ASN   A CB  1 
ATOM   1049 C  CG  . ASN   A 1 133 ? 6.587   11.403  17.619  1.00 14.17 ? 133 ASN   A CG  1 
ATOM   1050 O  OD1 . ASN   A 1 133 ? 7.162   10.362  17.260  1.00 13.29 ? 133 ASN   A OD1 1 
ATOM   1051 N  ND2 . ASN   A 1 133 ? 7.041   12.621  17.339  1.00 13.99 ? 133 ASN   A ND2 1 
ATOM   1052 N  N   . PHE   A 1 134 ? 4.856   8.001   17.200  1.00 13.37 ? 134 PHE   A N   1 
ATOM   1053 C  CA  . PHE   A 1 134 ? 4.634   7.092   16.067  1.00 13.99 ? 134 PHE   A CA  1 
ATOM   1054 C  C   . PHE   A 1 134 ? 5.438   7.465   14.829  1.00 15.09 ? 134 PHE   A C   1 
ATOM   1055 O  O   . PHE   A 1 134 ? 5.146   6.996   13.727  1.00 15.81 ? 134 PHE   A O   1 
ATOM   1056 C  CB  . PHE   A 1 134 ? 3.156   6.948   15.737  1.00 13.77 ? 134 PHE   A CB  1 
ATOM   1057 C  CG  . PHE   A 1 134 ? 2.354   6.248   16.806  1.00 15.76 ? 134 PHE   A CG  1 
ATOM   1058 C  CD1 . PHE   A 1 134 ? 2.437   4.880   16.959  1.00 18.54 ? 134 PHE   A CD1 1 
ATOM   1059 C  CD2 . PHE   A 1 134 ? 1.539   6.956   17.678  1.00 20.43 ? 134 PHE   A CD2 1 
ATOM   1060 C  CE1 . PHE   A 1 134 ? 1.747   4.217   17.964  1.00 21.07 ? 134 PHE   A CE1 1 
ATOM   1061 C  CE2 . PHE   A 1 134 ? 0.858   6.302   18.702  1.00 19.92 ? 134 PHE   A CE2 1 
ATOM   1062 C  CZ  . PHE   A 1 134 ? 0.950   4.938   18.832  1.00 20.31 ? 134 PHE   A CZ  1 
ATOM   1063 N  N   . THR   A 1 135 ? 6.535   8.182   15.024  1.00 14.14 ? 135 THR   A N   1 
ATOM   1064 C  CA  . THR   A 1 135 ? 7.547   8.270   14.005  1.00 13.58 ? 135 THR   A CA  1 
ATOM   1065 C  C   . THR   A 1 135 ? 8.674   7.288   14.305  1.00 13.59 ? 135 THR   A C   1 
ATOM   1066 O  O   . THR   A 1 135 ? 8.759   6.720   15.398  1.00 13.94 ? 135 THR   A O   1 
ATOM   1067 C  CB  . THR   A 1 135 ? 8.103   9.689   13.876  1.00 14.29 ? 135 THR   A CB  1 
ATOM   1068 O  OG1 . THR   A 1 135 ? 8.781   10.035  15.083  1.00 14.33 ? 135 THR   A OG1 1 
ATOM   1069 C  CG2 . THR   A 1 135 ? 6.994   10.681  13.605  1.00 13.65 ? 135 THR   A CG2 1 
ATOM   1070 N  N   . ILE   A 1 136 ? 9.538   7.117   13.313  1.00 13.77 ? 136 ILE   A N   1 
ATOM   1071 C  CA  . ILE   A 1 136 ? 10.802  6.454   13.547  1.00 14.61 ? 136 ILE   A CA  1 
ATOM   1072 C  C   . ILE   A 1 136 ? 11.941  7.350   13.114  1.00 14.37 ? 136 ILE   A C   1 
ATOM   1073 O  O   . ILE   A 1 136 ? 11.883  8.103   12.140  1.00 13.92 ? 136 ILE   A O   1 
ATOM   1074 C  CB  . ILE   A 1 136 ? 10.844  5.035   12.949  1.00 18.87 ? 136 ILE   A CB  1 
ATOM   1075 C  CG1 . ILE   A 1 136 ? 11.153  5.015   11.465  1.00 22.67 ? 136 ILE   A CG1 1 
ATOM   1076 C  CG2 . ILE   A 1 136 ? 9.578   4.244   13.291  1.00 18.27 ? 136 ILE   A CG2 1 
ATOM   1077 C  CD1 . ILE   A 1 136 ? 11.396  3.632   10.920  1.00 25.18 ? 136 ILE   A CD1 1 
ATOM   1078 N  N   . LYS   A 1 137 ? 13.049  7.261   13.862  1.00 14.64 ? 137 LYS   A N   1 
ATOM   1079 C  CA  . LYS   A 1 137 ? 14.237  8.016   13.505  1.00 16.76 ? 137 LYS   A CA  1 
ATOM   1080 C  C   . LYS   A 1 137 ? 15.130  7.077   12.715  1.00 18.87 ? 137 LYS   A C   1 
ATOM   1081 O  O   . LYS   A 1 137 ? 16.014  6.396   13.258  1.00 19.81 ? 137 LYS   A O   1 
ATOM   1082 C  CB  . LYS   A 1 137 ? 14.946  8.572   14.739  1.00 20.96 ? 137 LYS   A CB  1 
ATOM   1083 C  CG  . LYS   A 1 137 ? 14.071  9.428   15.639  1.00 25.48 ? 137 LYS   A CG  1 
ATOM   1084 C  CD  . LYS   A 1 137 ? 14.837  10.053  16.768  1.00 29.28 ? 137 LYS   A CD  1 
ATOM   1085 C  CE  . LYS   A 1 137 ? 14.029  11.064  17.550  1.00 35.14 ? 137 LYS   A CE  1 
ATOM   1086 N  NZ  . LYS   A 1 137 ? 14.717  11.396  18.826  1.00 41.52 ? 137 LYS   A NZ  1 
ATOM   1087 N  N   . GLY   A 1 138 ? 14.785  6.949   11.429  1.00 17.35 ? 138 GLY   A N   1 
ATOM   1088 C  CA  . GLY   A 1 138 ? 15.489  6.057   10.559  1.00 16.01 ? 138 GLY   A CA  1 
ATOM   1089 C  C   . GLY   A 1 138 ? 16.628  6.728   9.823   1.00 17.62 ? 138 GLY   A C   1 
ATOM   1090 O  O   . GLY   A 1 138 ? 16.936  7.922   10.001  1.00 17.98 ? 138 GLY   A O   1 
ATOM   1091 N  N   A SER   A 1 139 ? 17.211  5.899   8.972   0.66 17.00 ? 139 SER   A N   1 
ATOM   1092 N  N   B SER   A 1 139 ? 17.269  5.905   8.989   0.34 17.69 ? 139 SER   A N   1 
ATOM   1093 C  CA  A SER   A 1 139 ? 18.243  6.244   8.017   0.66 18.01 ? 139 SER   A CA  1 
ATOM   1094 C  CA  B SER   A 1 139 ? 18.271  6.312   8.017   0.34 18.48 ? 139 SER   A CA  1 
ATOM   1095 C  C   A SER   A 1 139 ? 17.733  5.767   6.668   0.66 19.26 ? 139 SER   A C   1 
ATOM   1096 C  C   B SER   A 1 139 ? 17.819  5.813   6.649   0.34 18.63 ? 139 SER   A C   1 
ATOM   1097 O  O   A SER   A 1 139 ? 17.815  4.578   6.333   0.66 21.91 ? 139 SER   A O   1 
ATOM   1098 O  O   B SER   A 1 139 ? 18.079  4.672   6.249   0.34 20.67 ? 139 SER   A O   1 
ATOM   1099 C  CB  A SER   A 1 139 ? 19.543  5.588   8.358   0.66 18.71 ? 139 SER   A CB  1 
ATOM   1100 C  CB  B SER   A 1 139 ? 19.641  5.792   8.354   0.34 19.51 ? 139 SER   A CB  1 
ATOM   1101 O  OG  A SER   A 1 139 ? 20.095  6.155   9.535   0.66 18.82 ? 139 SER   A OG  1 
ATOM   1102 O  OG  B SER   A 1 139 ? 20.598  6.225   7.388   0.34 20.47 ? 139 SER   A OG  1 
ATOM   1103 N  N   . PHE   A 1 140 ? 17.102  6.689   5.953   1.00 16.66 ? 140 PHE   A N   1 
ATOM   1104 C  CA  . PHE   A 1 140 ? 16.480  6.375   4.702   1.00 13.79 ? 140 PHE   A CA  1 
ATOM   1105 C  C   . PHE   A 1 140 ? 16.733  7.538   3.758   1.00 14.27 ? 140 PHE   A C   1 
ATOM   1106 O  O   . PHE   A 1 140 ? 16.619  8.704   4.175   1.00 15.40 ? 140 PHE   A O   1 
ATOM   1107 C  CB  . PHE   A 1 140 ? 14.970  6.245   4.863   1.00 12.66 ? 140 PHE   A CB  1 
ATOM   1108 C  CG  . PHE   A 1 140 ? 14.455  5.035   5.607   1.00 12.59 ? 140 PHE   A CG  1 
ATOM   1109 C  CD1 . PHE   A 1 140 ? 14.696  3.755   5.150   1.00 12.94 ? 140 PHE   A CD1 1 
ATOM   1110 C  CD2 . PHE   A 1 140 ? 13.716  5.185   6.754   1.00 13.26 ? 140 PHE   A CD2 1 
ATOM   1111 C  CE1 . PHE   A 1 140 ? 14.162  2.645   5.786   1.00 14.25 ? 140 PHE   A CE1 1 
ATOM   1112 C  CE2 . PHE   A 1 140 ? 13.184  4.072   7.398   1.00 13.57 ? 140 PHE   A CE2 1 
ATOM   1113 C  CZ  . PHE   A 1 140 ? 13.382  2.814   6.908   1.00 14.03 ? 140 PHE   A CZ  1 
ATOM   1114 N  N   . LEU   A 1 141 ? 16.978  7.182   2.505   1.00 13.89 ? 141 LEU   A N   1 
ATOM   1115 C  CA  . LEU   A 1 141 ? 17.163  8.141   1.424   1.00 15.50 ? 141 LEU   A CA  1 
ATOM   1116 C  C   . LEU   A 1 141 ? 16.027  8.016   0.428   1.00 14.07 ? 141 LEU   A C   1 
ATOM   1117 O  O   . LEU   A 1 141 ? 15.218  7.086   0.478   1.00 13.55 ? 141 LEU   A O   1 
ATOM   1118 C  CB  . LEU   A 1 141 ? 18.515  7.885   0.758   1.00 15.97 ? 141 LEU   A CB  1 
ATOM   1119 C  CG  . LEU   A 1 141 ? 19.708  8.042   1.698   1.00 20.06 ? 141 LEU   A CG  1 
ATOM   1120 C  CD1 . LEU   A 1 141 ? 20.980  7.622   0.987   1.00 23.20 ? 141 LEU   A CD1 1 
ATOM   1121 C  CD2 . LEU   A 1 141 ? 19.820  9.465   2.197   1.00 22.53 ? 141 LEU   A CD2 1 
ATOM   1122 N  N   . ASN   A 1 142 ? 16.016  8.942   -0.546  1.00 13.76 ? 142 ASN   A N   1 
ATOM   1123 C  CA  . ASN   A 1 142 ? 15.115  8.822   -1.679  1.00 15.83 ? 142 ASN   A CA  1 
ATOM   1124 C  C   . ASN   A 1 142 ? 15.273  7.436   -2.310  1.00 15.36 ? 142 ASN   A C   1 
ATOM   1125 O  O   . ASN   A 1 142 ? 16.389  6.978   -2.562  1.00 16.11 ? 142 ASN   A O   1 
ATOM   1126 C  CB  . ASN   A 1 142 ? 15.428  9.848   -2.773  1.00 19.38 ? 142 ASN   A CB  1 
ATOM   1127 C  CG  . ASN   A 1 142 ? 15.150  11.289  -2.389  1.00 27.14 ? 142 ASN   A CG  1 
ATOM   1128 O  OD1 . ASN   A 1 142 ? 15.513  11.753  -1.312  1.00 36.57 ? 142 ASN   A OD1 1 
ATOM   1129 N  ND2 . ASN   A 1 142 ? 14.524  12.028  -3.283  1.00 32.87 ? 142 ASN   A ND2 1 
ATOM   1130 N  N   . GLY   A 1 143 ? 14.145  6.768   -2.523  1.00 15.34 ? 143 GLY   A N   1 
ATOM   1131 C  CA  . GLY   A 1 143 ? 14.047  5.450   -3.141  1.00 13.75 ? 143 GLY   A CA  1 
ATOM   1132 C  C   . GLY   A 1 143 ? 13.921  4.304   -2.126  1.00 11.23 ? 143 GLY   A C   1 
ATOM   1133 O  O   . GLY   A 1 143 ? 13.865  3.152   -2.547  1.00 12.67 ? 143 GLY   A O   1 
ATOM   1134 N  N   . SER   A 1 144 ? 13.911  4.619   -0.829  1.00 11.36 ? 144 SER   A N   1 
ATOM   1135 C  CA  . SER   A 1 144 ? 13.776  3.622   0.236   1.00 10.53 ? 144 SER   A CA  1 
ATOM   1136 C  C   . SER   A 1 144 ? 12.315  3.203   0.468   1.00 10.36 ? 144 SER   A C   1 
ATOM   1137 O  O   . SER   A 1 144 ? 12.056  2.227   1.186   1.00 10.24 ? 144 SER   A O   1 
ATOM   1138 C  CB  . SER   A 1 144 ? 14.360  4.145   1.485   1.00 11.85 ? 144 SER   A CB  1 
ATOM   1139 O  OG  . SER   A 1 144 ? 13.728  5.345   1.891   1.00 9.87  ? 144 SER   A OG  1 
ATOM   1140 N  N   . CYS   A 1 145 ? 11.344  3.962   -0.099  1.00 9.64  ? 145 CYS   A N   1 
ATOM   1141 C  CA  . CYS   A 1 145 ? 9.929   3.648   0.064   1.00 9.83  ? 145 CYS   A CA  1 
ATOM   1142 C  C   . CYS   A 1 145 ? 9.672   2.147   -0.153  1.00 10.30 ? 145 CYS   A C   1 
ATOM   1143 O  O   . CYS   A 1 145 ? 10.090  1.555   -1.156  1.00 10.99 ? 145 CYS   A O   1 
ATOM   1144 C  CB  . CYS   A 1 145 ? 9.087   4.487   -0.884  1.00 11.23 ? 145 CYS   A CB  1 
ATOM   1145 S  SG  . CYS   A 1 145 ? 7.298   4.542   -0.541  1.00 11.70 ? 145 CYS   A SG  1 
ATOM   1146 N  N   . GLY   A 1 146 ? 8.977   1.511   0.795   1.00 8.58  ? 146 GLY   A N   1 
ATOM   1147 C  CA  . GLY   A 1 146 ? 8.678   0.076   0.718   1.00 8.93  ? 146 GLY   A CA  1 
ATOM   1148 C  C   . GLY   A 1 146 ? 9.637   -0.837  1.486   1.00 9.20  ? 146 GLY   A C   1 
ATOM   1149 O  O   . GLY   A 1 146 ? 9.395   -2.046  1.610   1.00 9.79  ? 146 GLY   A O   1 
ATOM   1150 N  N   . SER   A 1 147 ? 10.740  -0.270  1.990   1.00 9.23  ? 147 SER   A N   1 
ATOM   1151 C  CA  . SER   A 1 147 ? 11.625  -1.001  2.874   1.00 9.43  ? 147 SER   A CA  1 
ATOM   1152 C  C   . SER   A 1 147 ? 10.841  -1.453  4.108   1.00 9.22  ? 147 SER   A C   1 
ATOM   1153 O  O   . SER   A 1 147 ? 9.973   -0.705  4.561   1.00 9.07  ? 147 SER   A O   1 
ATOM   1154 C  CB  . SER   A 1 147 ? 12.757  -0.111  3.323   1.00 9.40  ? 147 SER   A CB  1 
ATOM   1155 O  OG  . SER   A 1 147 ? 13.615  0.282   2.211   1.00 10.53 ? 147 SER   A OG  1 
ATOM   1156 N  N   . VAL   A 1 148 ? 11.246  -2.576  4.725   1.00 9.52  ? 148 VAL   A N   1 
ATOM   1157 C  CA  . VAL   A 1 148 ? 10.475  -3.146  5.815   1.00 9.64  ? 148 VAL   A CA  1 
ATOM   1158 C  C   . VAL   A 1 148 ? 11.295  -3.231  7.096   1.00 9.43  ? 148 VAL   A C   1 
ATOM   1159 O  O   . VAL   A 1 148 ? 12.529  -3.308  7.106   1.00 10.76 ? 148 VAL   A O   1 
ATOM   1160 C  CB  . VAL   A 1 148 ? 9.832   -4.505  5.508   1.00 10.16 ? 148 VAL   A CB  1 
ATOM   1161 C  CG1 . VAL   A 1 148 ? 8.829   -4.364  4.378   1.00 10.04 ? 148 VAL   A CG1 1 
ATOM   1162 C  CG2 . VAL   A 1 148 ? 10.861  -5.579  5.205   1.00 11.47 ? 148 VAL   A CG2 1 
ATOM   1163 N  N   . GLY   A 1 149 ? 10.541  -3.203  8.189   1.00 8.91  ? 149 GLY   A N   1 
ATOM   1164 C  CA  . GLY   A 1 149 ? 11.051  -3.450  9.514   1.00 8.46  ? 149 GLY   A CA  1 
ATOM   1165 C  C   . GLY   A 1 149 ? 10.479  -4.762  10.079  1.00 8.81  ? 149 GLY   A C   1 
ATOM   1166 O  O   . GLY   A 1 149 ? 9.356   -5.141  9.708   1.00 9.37  ? 149 GLY   A O   1 
ATOM   1167 N  N   . PHE   A 1 150 ? 11.282  -5.444  10.899  1.00 8.03  ? 150 PHE   A N   1 
ATOM   1168 C  CA  . PHE   A 1 150 ? 10.963  -6.791  11.340  1.00 9.36  ? 150 PHE   A CA  1 
ATOM   1169 C  C   . PHE   A 1 150 ? 11.710  -7.162  12.628  1.00 9.90  ? 150 PHE   A C   1 
ATOM   1170 O  O   . PHE   A 1 150 ? 12.716  -6.563  13.019  1.00 9.26  ? 150 PHE   A O   1 
ATOM   1171 C  CB  . PHE   A 1 150 ? 11.282  -7.779  10.211  1.00 9.71  ? 150 PHE   A CB  1 
ATOM   1172 C  CG  . PHE   A 1 150 ? 12.729  -7.795  9.828   1.00 10.77 ? 150 PHE   A CG  1 
ATOM   1173 C  CD1 . PHE   A 1 150 ? 13.239  -6.816  8.996   1.00 12.10 ? 150 PHE   A CD1 1 
ATOM   1174 C  CD2 . PHE   A 1 150 ? 13.617  -8.685  10.418  1.00 12.17 ? 150 PHE   A CD2 1 
ATOM   1175 C  CE1 . PHE   A 1 150 ? 14.603  -6.765  8.727   1.00 13.43 ? 150 PHE   A CE1 1 
ATOM   1176 C  CE2 . PHE   A 1 150 ? 14.978  -8.625  10.155  1.00 13.31 ? 150 PHE   A CE2 1 
ATOM   1177 C  CZ  . PHE   A 1 150 ? 15.460  -7.684  9.275   1.00 13.27 ? 150 PHE   A CZ  1 
ATOM   1178 N  N   . ASN   A 1 151 ? 11.193  -8.232  13.262  1.00 11.08 ? 151 ASN   A N   1 
ATOM   1179 C  CA  . ASN   A 1 151 ? 11.886  -8.930  14.327  1.00 11.35 ? 151 ASN   A CA  1 
ATOM   1180 C  C   . ASN   A 1 151 ? 11.928  -10.409 13.948  1.00 11.75 ? 151 ASN   A C   1 
ATOM   1181 O  O   . ASN   A 1 151 ? 11.120  -10.823 13.140  1.00 11.47 ? 151 ASN   A O   1 
ATOM   1182 C  CB  . ASN   A 1 151 ? 11.182  -8.741  15.656  1.00 12.83 ? 151 ASN   A CB  1 
ATOM   1183 C  CG  . ASN   A 1 151 ? 11.414  -7.367  16.240  1.00 14.42 ? 151 ASN   A CG  1 
ATOM   1184 O  OD1 . ASN   A 1 151 ? 12.501  -7.037  16.695  1.00 20.04 ? 151 ASN   A OD1 1 
ATOM   1185 N  ND2 . ASN   A 1 151 ? 10.427  -6.524  16.117  1.00 14.26 ? 151 ASN   A ND2 1 
ATOM   1186 N  N   . ILE   A 1 152 ? 12.908  -11.154 14.466  1.00 11.93 ? 152 ILE   A N   1 
ATOM   1187 C  CA  . ILE   A 1 152 ? 12.993  -12.580 14.190  1.00 14.48 ? 152 ILE   A CA  1 
ATOM   1188 C  C   . ILE   A 1 152 ? 12.970  -13.322 15.518  1.00 18.01 ? 152 ILE   A C   1 
ATOM   1189 O  O   . ILE   A 1 152 ? 13.700  -12.954 16.428  1.00 19.43 ? 152 ILE   A O   1 
ATOM   1190 C  CB  . ILE   A 1 152 ? 14.242  -12.951 13.377  1.00 16.39 ? 152 ILE   A CB  1 
ATOM   1191 C  CG1 . ILE   A 1 152 ? 14.314  -12.124 12.097  1.00 18.27 ? 152 ILE   A CG1 1 
ATOM   1192 C  CG2 . ILE   A 1 152 ? 14.266  -14.447 13.092  1.00 18.08 ? 152 ILE   A CG2 1 
ATOM   1193 C  CD1 . ILE   A 1 152 ? 15.511  -12.450 11.234  1.00 21.43 ? 152 ILE   A CD1 1 
ATOM   1194 N  N   . ASP   A 1 153 ? 12.130  -14.357 15.591  1.00 21.08 ? 153 ASP   A N   1 
ATOM   1195 C  CA  . ASP   A 1 153 ? 12.054  -15.223 16.765  1.00 26.36 ? 153 ASP   A CA  1 
ATOM   1196 C  C   . ASP   A 1 153 ? 12.178  -16.660 16.274  1.00 29.97 ? 153 ASP   A C   1 
ATOM   1197 O  O   . ASP   A 1 153 ? 11.378  -17.113 15.461  1.00 27.07 ? 153 ASP   A O   1 
ATOM   1198 C  CB  . ASP   A 1 153 ? 10.740  -15.028 17.521  1.00 33.29 ? 153 ASP   A CB  1 
ATOM   1199 C  CG  . ASP   A 1 153 ? 10.543  -13.633 18.103  1.00 47.28 ? 153 ASP   A CG  1 
ATOM   1200 O  OD1 . ASP   A 1 153 ? 10.659  -13.507 19.355  1.00 62.91 ? 153 ASP   A OD1 1 
ATOM   1201 O  OD2 . ASP   A 1 153 ? 10.255  -12.667 17.314  1.00 55.17 ? 153 ASP   A OD2 1 
ATOM   1202 N  N   . TYR   A 1 154 ? 13.241  -17.339 16.705  1.00 33.97 ? 154 TYR   A N   1 
ATOM   1203 C  CA  . TYR   A 1 154 ? 13.544  -18.671 16.222  1.00 37.74 ? 154 TYR   A CA  1 
ATOM   1204 C  C   . TYR   A 1 154 ? 13.709  -18.547 14.710  1.00 39.97 ? 154 TYR   A C   1 
ATOM   1205 O  O   . TYR   A 1 154 ? 14.676  -17.956 14.217  1.00 45.50 ? 154 TYR   A O   1 
ATOM   1206 C  CB  . TYR   A 1 154 ? 12.463  -19.607 16.778  1.00 40.09 ? 154 TYR   A CB  1 
ATOM   1207 N  N   . ASP   A 1 155 ? 12.744  -19.051 13.957  1.00 36.01 ? 155 ASP   A N   1 
ATOM   1208 C  CA  . ASP   A 1 155 ? 12.903  -18.991 12.515  1.00 37.73 ? 155 ASP   A CA  1 
ATOM   1209 C  C   . ASP   A 1 155 ? 11.786  -18.150 11.887  1.00 30.32 ? 155 ASP   A C   1 
ATOM   1210 O  O   . ASP   A 1 155 ? 11.637  -18.171 10.669  1.00 30.35 ? 155 ASP   A O   1 
ATOM   1211 C  CB  . ASP   A 1 155 ? 12.969  -20.414 11.961  1.00 41.82 ? 155 ASP   A CB  1 
ATOM   1212 C  CG  . ASP   A 1 155 ? 11.714  -21.227 12.238  1.00 54.55 ? 155 ASP   A CG  1 
ATOM   1213 O  OD1 . ASP   A 1 155 ? 10.923  -20.812 13.126  1.00 57.55 ? 155 ASP   A OD1 1 
ATOM   1214 O  OD2 . ASP   A 1 155 ? 11.511  -22.251 11.543  1.00 57.68 ? 155 ASP   A OD2 1 
ATOM   1215 N  N   . CYS   A 1 156 ? 11.007  -17.423 12.717  1.00 24.89 ? 156 CYS   A N   1 
ATOM   1216 C  CA  . CYS   A 1 156 ? 9.810   -16.763 12.235  1.00 20.18 ? 156 CYS   A CA  1 
ATOM   1217 C  C   . CYS   A 1 156 ? 10.019  -15.240 12.169  1.00 16.92 ? 156 CYS   A C   1 
ATOM   1218 O  O   . CYS   A 1 156 ? 10.424  -14.632 13.147  1.00 18.61 ? 156 CYS   A O   1 
ATOM   1219 C  CB  . CYS   A 1 156 ? 8.619   -17.103 13.117  1.00 24.88 ? 156 CYS   A CB  1 
ATOM   1220 S  SG  . CYS   A 1 156 ? 7.103   -16.277 12.586  1.00 28.53 ? 156 CYS   A SG  1 
ATOM   1221 N  N   . VAL   A 1 157 ? 9.819   -14.666 10.981  1.00 15.02 ? 157 VAL   A N   1 
ATOM   1222 C  CA  . VAL   A 1 157 ? 9.977   -13.237 10.806  1.00 13.71 ? 157 VAL   A CA  1 
ATOM   1223 C  C   . VAL   A 1 157 ? 8.642   -12.575 11.099  1.00 12.78 ? 157 VAL   A C   1 
ATOM   1224 O  O   . VAL   A 1 157 ? 7.660   -12.894 10.436  1.00 14.63 ? 157 VAL   A O   1 
ATOM   1225 C  CB  . VAL   A 1 157 ? 10.463  -12.896 9.395   1.00 13.22 ? 157 VAL   A CB  1 
ATOM   1226 C  CG1 . VAL   A 1 157 ? 10.632  -11.393 9.188   1.00 13.49 ? 157 VAL   A CG1 1 
ATOM   1227 C  CG2 . VAL   A 1 157 ? 11.766  -13.633 9.113   1.00 15.22 ? 157 VAL   A CG2 1 
ATOM   1228 N  N   . SER   A 1 158 ? 8.649   -11.612 12.026  1.00 13.37 ? 158 SER   A N   1 
ATOM   1229 C  CA  . SER   A 1 158 ? 7.479   -10.794 12.325  1.00 12.48 ? 158 SER   A CA  1 
ATOM   1230 C  C   . SER   A 1 158 ? 7.672   -9.424  11.689  1.00 10.97 ? 158 SER   A C   1 
ATOM   1231 O  O   . SER   A 1 158 ? 8.501   -8.623  12.151  1.00 10.63 ? 158 SER   A O   1 
ATOM   1232 C  CB  . SER   A 1 158 ? 7.276   -10.648 13.826  1.00 14.58 ? 158 SER   A CB  1 
ATOM   1233 O  OG  . SER   A 1 158 ? 6.841   -11.884 14.399  1.00 18.12 ? 158 SER   A OG  1 
ATOM   1234 N  N   . PHE   A 1 159 ? 6.987   -9.188  10.590  1.00 10.67 ? 159 PHE   A N   1 
ATOM   1235 C  CA  . PHE   A 1 159 ? 7.117   -7.914  9.897   1.00 10.99 ? 159 PHE   A CA  1 
ATOM   1236 C  C   . PHE   A 1 159 ? 6.201   -6.914  10.595  1.00 11.62 ? 159 PHE   A C   1 
ATOM   1237 O  O   . PHE   A 1 159 ? 5.007   -7.198  10.760  1.00 12.71 ? 159 PHE   A O   1 
ATOM   1238 C  CB  . PHE   A 1 159 ? 6.653   -8.054  8.457   1.00 11.12 ? 159 PHE   A CB  1 
ATOM   1239 C  CG  . PHE   A 1 159 ? 7.547   -8.882  7.571   1.00 10.59 ? 159 PHE   A CG  1 
ATOM   1240 C  CD1 . PHE   A 1 159 ? 8.769   -8.383  7.123   1.00 11.25 ? 159 PHE   A CD1 1 
ATOM   1241 C  CD2 . PHE   A 1 159 ? 7.210   -10.184 7.247   1.00 10.29 ? 159 PHE   A CD2 1 
ATOM   1242 C  CE1 . PHE   A 1 159 ? 9.597   -9.158  6.325   1.00 11.43 ? 159 PHE   A CE1 1 
ATOM   1243 C  CE2 . PHE   A 1 159 ? 8.030   -10.936 6.415   1.00 11.23 ? 159 PHE   A CE2 1 
ATOM   1244 C  CZ  . PHE   A 1 159 ? 9.230   -10.427 5.987   1.00 11.35 ? 159 PHE   A CZ  1 
ATOM   1245 N  N   . CYS   A 1 160 ? 6.722   -5.735  10.915  1.00 12.60 ? 160 CYS   A N   1 
ATOM   1246 C  CA  . CYS   A 1 160 ? 5.935   -4.775  11.685  1.00 12.66 ? 160 CYS   A CA  1 
ATOM   1247 C  C   . CYS   A 1 160 ? 5.884   -3.384  11.051  1.00 10.91 ? 160 CYS   A C   1 
ATOM   1248 O  O   . CYS   A 1 160 ? 5.075   -2.554  11.488  1.00 12.04 ? 160 CYS   A O   1 
ATOM   1249 C  CB  . CYS   A 1 160 ? 6.465   -4.655  13.091  1.00 13.17 ? 160 CYS   A CB  1 
ATOM   1250 S  SG  . CYS   A 1 160 ? 8.202   -4.171  13.195  1.00 13.32 ? 160 CYS   A SG  1 
ATOM   1251 N  N   . TYR   A 1 161 ? 6.702   -3.114  10.040  1.00 8.69  ? 161 TYR   A N   1 
ATOM   1252 C  CA  . TYR   A 1 161 ? 6.799   -1.766  9.510   1.00 8.54  ? 161 TYR   A CA  1 
ATOM   1253 C  C   . TYR   A 1 161 ? 7.079   -1.821  8.005   1.00 8.73  ? 161 TYR   A C   1 
ATOM   1254 O  O   . TYR   A 1 161 ? 7.880   -2.647  7.544   1.00 8.87  ? 161 TYR   A O   1 
ATOM   1255 C  CB  . TYR   A 1 161 ? 7.929   -0.990  10.206  1.00 8.87  ? 161 TYR   A CB  1 
ATOM   1256 C  CG  . TYR   A 1 161 ? 8.147   0.443   9.702   1.00 9.22  ? 161 TYR   A CG  1 
ATOM   1257 C  CD1 . TYR   A 1 161 ? 7.319   1.488   10.126  1.00 9.49  ? 161 TYR   A CD1 1 
ATOM   1258 C  CD2 . TYR   A 1 161 ? 9.160   0.784   8.790   1.00 9.48  ? 161 TYR   A CD2 1 
ATOM   1259 C  CE1 . TYR   A 1 161 ? 7.528   2.801   9.725   1.00 9.18  ? 161 TYR   A CE1 1 
ATOM   1260 C  CE2 . TYR   A 1 161 ? 9.376   2.107   8.383   1.00 9.48  ? 161 TYR   A CE2 1 
ATOM   1261 C  CZ  . TYR   A 1 161 ? 8.523   3.109   8.796   1.00 10.52 ? 161 TYR   A CZ  1 
ATOM   1262 O  OH  . TYR   A 1 161 ? 8.678   4.416   8.362   1.00 10.35 ? 161 TYR   A OH  1 
ATOM   1263 N  N   . MET   A 1 162 ? 6.369   -0.983  7.259   1.00 8.23  ? 162 MET   A N   1 
ATOM   1264 C  CA  . MET   A 1 162 ? 6.657   -0.714  5.855   1.00 8.71  ? 162 MET   A CA  1 
ATOM   1265 C  C   . MET   A 1 162 ? 6.871   0.787   5.723   1.00 8.81  ? 162 MET   A C   1 
ATOM   1266 O  O   . MET   A 1 162 ? 5.993   1.574   6.052   1.00 9.70  ? 162 MET   A O   1 
ATOM   1267 C  CB  . MET   A 1 162 ? 5.550   -1.183  4.891   1.00 9.83  ? 162 MET   A CB  1 
ATOM   1268 C  CG  . MET   A 1 162 ? 5.955   -0.919  3.430   1.00 11.83 ? 162 MET   A CG  1 
ATOM   1269 S  SD  . MET   A 1 162 ? 4.837   -1.773  2.287   1.00 17.38 ? 162 MET   A SD  1 
ATOM   1270 C  CE  . MET   A 1 162 ? 5.739   -3.309  2.164   1.00 22.40 ? 162 MET   A CE  1 
ATOM   1271 N  N   . HIS   A 1 163 ? 8.049   1.173   5.226   1.00 7.79  ? 163 HIS   A N   1 
ATOM   1272 C  CA  . HIS   A 1 163 ? 8.430   2.574   5.119   1.00 8.62  ? 163 HIS   A CA  1 
ATOM   1273 C  C   . HIS   A 1 163 ? 7.681   3.289   3.996   1.00 8.72  ? 163 HIS   A C   1 
ATOM   1274 O  O   . HIS   A 1 163 ? 7.629   2.798   2.882   1.00 9.88  ? 163 HIS   A O   1 
ATOM   1275 C  CB  . HIS   A 1 163 ? 9.912   2.712   4.802   1.00 8.42  ? 163 HIS   A CB  1 
ATOM   1276 C  CG  . HIS   A 1 163 ? 10.399  4.125   4.802   1.00 8.26  ? 163 HIS   A CG  1 
ATOM   1277 N  ND1 . HIS   A 1 163 ? 10.035  4.993   5.810   1.00 8.43  ? 163 HIS   A ND1 1 
ATOM   1278 C  CD2 . HIS   A 1 163 ? 11.171  4.803   3.963   1.00 9.13  ? 163 HIS   A CD2 1 
ATOM   1279 C  CE1 . HIS   A 1 163 ? 10.585  6.191   5.543   1.00 9.75  ? 163 HIS   A CE1 1 
ATOM   1280 N  NE2 . HIS   A 1 163 ? 11.282  6.087   4.425   1.00 9.40  ? 163 HIS   A NE2 1 
ATOM   1281 N  N   . HIS   A 1 164 ? 7.117   4.466   4.312   1.00 9.39  ? 164 HIS   A N   1 
ATOM   1282 C  CA  . HIS   A 1 164 ? 6.457   5.275   3.293   1.00 9.79  ? 164 HIS   A CA  1 
ATOM   1283 C  C   . HIS   A 1 164 ? 7.195   6.589   3.061   1.00 10.94 ? 164 HIS   A C   1 
ATOM   1284 O  O   . HIS   A 1 164 ? 7.545   6.909   1.903   1.00 11.91 ? 164 HIS   A O   1 
ATOM   1285 C  CB  . HIS   A 1 164 ? 4.977   5.556   3.598   1.00 10.14 ? 164 HIS   A CB  1 
ATOM   1286 C  CG  . HIS   A 1 164 ? 4.091   4.398   3.360   1.00 10.28 ? 164 HIS   A CG  1 
ATOM   1287 N  ND1 . HIS   A 1 164 ? 4.253   3.171   3.971   1.00 10.94 ? 164 HIS   A ND1 1 
ATOM   1288 C  CD2 . HIS   A 1 164 ? 3.010   4.276   2.559   1.00 10.25 ? 164 HIS   A CD2 1 
ATOM   1289 C  CE1 . HIS   A 1 164 ? 3.309   2.345   3.532   1.00 10.75 ? 164 HIS   A CE1 1 
ATOM   1290 N  NE2 . HIS   A 1 164 ? 2.542   3.004   2.711   1.00 11.91 ? 164 HIS   A NE2 1 
ATOM   1291 N  N   . MET   A 1 165 ? 7.365   7.396   4.118   1.00 10.84 ? 165 MET   A N   1 
ATOM   1292 C  CA  . MET   A 1 165 ? 7.840   8.746   3.848   1.00 12.43 ? 165 MET   A CA  1 
ATOM   1293 C  C   . MET   A 1 165 ? 8.759   9.366   4.892   1.00 11.09 ? 165 MET   A C   1 
ATOM   1294 O  O   . MET   A 1 165 ? 8.821   8.919   6.025   1.00 10.04 ? 165 MET   A O   1 
ATOM   1295 C  CB  . MET   A 1 165 ? 6.640   9.679   3.656   1.00 16.00 ? 165 MET   A CB  1 
ATOM   1296 C  CG  . MET   A 1 165 ? 5.582   9.523   4.641   1.00 17.99 ? 165 MET   A CG  1 
ATOM   1297 S  SD  . MET   A 1 165 ? 4.044   10.373  4.068   0.80 16.60 ? 165 MET   A SD  1 
ATOM   1298 C  CE  . MET   A 1 165 ? 3.371   10.602  5.717   1.00 18.58 ? 165 MET   A CE  1 
ATOM   1299 N  N   . GLU   A 1 166 ? 9.449   10.451  4.481   1.00 12.18 ? 166 GLU   A N   1 
ATOM   1300 C  CA  . GLU   A 1 166 ? 10.237  11.258  5.384   1.00 13.27 ? 166 GLU   A CA  1 
ATOM   1301 C  C   . GLU   A 1 166 ? 9.496   12.570  5.632   1.00 14.65 ? 166 GLU   A C   1 
ATOM   1302 O  O   . GLU   A 1 166 ? 9.094   13.214  4.661   1.00 16.29 ? 166 GLU   A O   1 
ATOM   1303 C  CB  . GLU   A 1 166 ? 11.653  11.560  4.854   1.00 15.12 ? 166 GLU   A CB  1 
ATOM   1304 C  CG  . GLU   A 1 166 ? 12.565  12.221  5.873   1.00 17.69 ? 166 GLU   A CG  1 
ATOM   1305 C  CD  . GLU   A 1 166 ? 14.003  12.354  5.390   1.00 23.03 ? 166 GLU   A CD  1 
ATOM   1306 O  OE1 . GLU   A 1 166 ? 14.694  11.332  5.289   1.00 18.89 ? 166 GLU   A OE1 1 
ATOM   1307 O  OE2 . GLU   A 1 166 ? 14.391  13.503  5.005   1.00 24.20 ? 166 GLU   A OE2 1 
ATOM   1308 N  N   . LEU   A 1 167 ? 9.343   12.953  6.898   1.00 13.55 ? 167 LEU   A N   1 
ATOM   1309 C  CA  . LEU   A 1 167 ? 8.717   14.220  7.271   1.00 16.16 ? 167 LEU   A CA  1 
ATOM   1310 C  C   . LEU   A 1 167 ? 9.736   15.353  7.155   1.00 18.02 ? 167 LEU   A C   1 
ATOM   1311 O  O   . LEU   A 1 167 ? 10.959  15.125  7.128   1.00 16.94 ? 167 LEU   A O   1 
ATOM   1312 C  CB  . LEU   A 1 167 ? 8.211   14.112  8.710   1.00 16.90 ? 167 LEU   A CB  1 
ATOM   1313 C  CG  . LEU   A 1 167 ? 7.287   12.915  8.963   1.00 16.05 ? 167 LEU   A CG  1 
ATOM   1314 C  CD1 . LEU   A 1 167 ? 6.609   13.068  10.303  1.00 18.34 ? 167 LEU   A CD1 1 
ATOM   1315 C  CD2 . LEU   A 1 167 ? 6.274   12.795  7.864   1.00 16.79 ? 167 LEU   A CD2 1 
ATOM   1316 N  N   . PRO   A 1 168 ? 9.265   16.617  7.063   1.00 18.73 ? 168 PRO   A N   1 
ATOM   1317 C  CA  . PRO   A 1 168 ? 10.170  17.775  7.030   1.00 20.56 ? 168 PRO   A CA  1 
ATOM   1318 C  C   . PRO   A 1 168 ? 11.249  17.844  8.106   1.00 19.23 ? 168 PRO   A C   1 
ATOM   1319 O  O   . PRO   A 1 168 ? 12.329  18.402  7.848   1.00 20.58 ? 168 PRO   A O   1 
ATOM   1320 C  CB  . PRO   A 1 168 ? 9.204   18.956  7.227   1.00 19.98 ? 168 PRO   A CB  1 
ATOM   1321 C  CG  . PRO   A 1 168 ? 7.967   18.473  6.509   1.00 20.83 ? 168 PRO   A CG  1 
ATOM   1322 C  CD  . PRO   A 1 168 ? 7.857   17.008  6.912   1.00 21.78 ? 168 PRO   A CD  1 
ATOM   1323 N  N   . THR   A 1 169 ? 10.972  17.301  9.300   1.00 18.30 ? 169 THR   A N   1 
ATOM   1324 C  CA  . THR   A 1 169 ? 11.940  17.270  10.380  1.00 18.61 ? 169 THR   A CA  1 
ATOM   1325 C  C   . THR   A 1 169 ? 13.020  16.202  10.166  1.00 20.40 ? 169 THR   A C   1 
ATOM   1326 O  O   . THR   A 1 169 ? 14.020  16.228  10.862  1.00 22.84 ? 169 THR   A O   1 
ATOM   1327 C  CB  . THR   A 1 169 ? 11.317  17.035  11.758  1.00 21.30 ? 169 THR   A CB  1 
ATOM   1328 O  OG1 . THR   A 1 169 ? 10.576  15.814  11.727  1.00 21.36 ? 169 THR   A OG1 1 
ATOM   1329 C  CG2 . THR   A 1 169 ? 10.426  18.177  12.231  1.00 20.52 ? 169 THR   A CG2 1 
ATOM   1330 N  N   . GLY   A 1 170 ? 12.861  15.299  9.199   1.00 18.78 ? 170 GLY   A N   1 
ATOM   1331 C  CA  . GLY   A 1 170 ? 13.879  14.308  8.911   1.00 15.72 ? 170 GLY   A CA  1 
ATOM   1332 C  C   . GLY   A 1 170 ? 13.608  12.965  9.586   1.00 16.59 ? 170 GLY   A C   1 
ATOM   1333 O  O   . GLY   A 1 170 ? 14.390  12.048  9.420   1.00 17.59 ? 170 GLY   A O   1 
ATOM   1334 N  N   . VAL   A 1 171 ? 12.510  12.850  10.341  1.00 13.21 ? 171 VAL   A N   1 
ATOM   1335 C  CA  . VAL   A 1 171 ? 12.034  11.559  10.823  1.00 13.33 ? 171 VAL   A CA  1 
ATOM   1336 C  C   . VAL   A 1 171 ? 11.108  10.919  9.795   1.00 12.16 ? 171 VAL   A C   1 
ATOM   1337 O  O   . VAL   A 1 171 ? 10.800  11.499  8.760   1.00 11.99 ? 171 VAL   A O   1 
ATOM   1338 C  CB  . VAL   A 1 171 ? 11.321  11.721  12.170  1.00 13.61 ? 171 VAL   A CB  1 
ATOM   1339 C  CG1 . VAL   A 1 171 ? 12.224  12.337  13.223  1.00 15.56 ? 171 VAL   A CG1 1 
ATOM   1340 C  CG2 . VAL   A 1 171 ? 10.059  12.551  12.008  1.00 14.44 ? 171 VAL   A CG2 1 
ATOM   1341 N  N   . HIS   A 1 172 ? 10.726  9.657   10.081  1.00 11.49 ? 172 HIS   A N   1 
ATOM   1342 C  CA  . HIS   A 1 172 ? 10.124  8.786   9.089   1.00 11.08 ? 172 HIS   A CA  1 
ATOM   1343 C  C   . HIS   A 1 172 ? 8.784   8.253   9.563   1.00 11.09 ? 172 HIS   A C   1 
ATOM   1344 O  O   . HIS   A 1 172 ? 8.490   8.182   10.779  1.00 11.68 ? 172 HIS   A O   1 
ATOM   1345 C  CB  . HIS   A 1 172 ? 11.077  7.629   8.806   1.00 11.93 ? 172 HIS   A CB  1 
ATOM   1346 C  CG  . HIS   A 1 172 ? 12.344  8.168   8.244   1.00 12.54 ? 172 HIS   A CG  1 
ATOM   1347 N  ND1 . HIS   A 1 172 ? 13.516  8.237   8.983   1.00 12.31 ? 172 HIS   A ND1 1 
ATOM   1348 C  CD2 . HIS   A 1 172 ? 12.566  8.797   7.082   1.00 11.60 ? 172 HIS   A CD2 1 
ATOM   1349 C  CE1 . HIS   A 1 172 ? 14.445  8.847   8.226   1.00 12.65 ? 172 HIS   A CE1 1 
ATOM   1350 N  NE2 . HIS   A 1 172 ? 13.900  9.202   7.069   1.00 12.99 ? 172 HIS   A NE2 1 
ATOM   1351 N  N   . ALA   A 1 173 ? 7.899   8.036   8.573   1.00 10.44 ? 173 ALA   A N   1 
ATOM   1352 C  CA  . ALA   A 1 173 ? 6.564   7.554   8.849   1.00 10.33 ? 173 ALA   A CA  1 
ATOM   1353 C  C   . ALA   A 1 173 ? 6.189   6.426   7.900   1.00 9.38  ? 173 ALA   A C   1 
ATOM   1354 O  O   . ALA   A 1 173 ? 6.579   6.394   6.747   1.00 10.30 ? 173 ALA   A O   1 
ATOM   1355 C  CB  . ALA   A 1 173 ? 5.583   8.697   8.714   1.00 11.55 ? 173 ALA   A CB  1 
ATOM   1356 N  N   . GLY   A 1 174 ? 5.457   5.462   8.422   1.00 8.84  ? 174 GLY   A N   1 
ATOM   1357 C  CA  . GLY   A 1 174 ? 5.056   4.326   7.627   1.00 9.61  ? 174 GLY   A CA  1 
ATOM   1358 C  C   . GLY   A 1 174 ? 3.920   3.560   8.308   1.00 8.90  ? 174 GLY   A C   1 
ATOM   1359 O  O   . GLY   A 1 174 ? 3.285   4.038   9.230   1.00 9.27  ? 174 GLY   A O   1 
ATOM   1360 N  N   . THR   A 1 175 ? 3.677   2.355   7.814   1.00 8.84  ? 175 THR   A N   1 
ATOM   1361 C  CA  . THR   A 1 175 ? 2.501   1.594   8.101   1.00 8.77  ? 175 THR   A CA  1 
ATOM   1362 C  C   . THR   A 1 175 ? 2.900   0.241   8.622   1.00 9.45  ? 175 THR   A C   1 
ATOM   1363 O  O   . THR   A 1 175 ? 4.053   -0.184  8.515   1.00 8.78  ? 175 THR   A O   1 
ATOM   1364 C  CB  . THR   A 1 175 ? 1.613   1.419   6.857   1.00 9.55  ? 175 THR   A CB  1 
ATOM   1365 O  OG1 . THR   A 1 175 ? 2.259   0.589   5.897   1.00 9.73  ? 175 THR   A OG1 1 
ATOM   1366 C  CG2 . THR   A 1 175 ? 1.231   2.721   6.206   1.00 9.84  ? 175 THR   A CG2 1 
ATOM   1367 N  N   . ASP   A 1 176 ? 1.892   -0.460  9.158   1.00 8.74  ? 176 ASP   A N   1 
ATOM   1368 C  CA  . ASP   A 1 176 ? 2.049   -1.885  9.346   1.00 9.85  ? 176 ASP   A CA  1 
ATOM   1369 C  C   . ASP   A 1 176 ? 1.786   -2.599  8.016   1.00 9.98  ? 176 ASP   A C   1 
ATOM   1370 O  O   . ASP   A 1 176 ? 1.566   -1.968  6.991   1.00 9.26  ? 176 ASP   A O   1 
ATOM   1371 C  CB  . ASP   A 1 176 ? 1.169   -2.311  10.528  1.00 11.07 ? 176 ASP   A CB  1 
ATOM   1372 C  CG  . ASP   A 1 176 ? -0.319  -2.178  10.307  1.00 13.06 ? 176 ASP   A CG  1 
ATOM   1373 O  OD1 . ASP   A 1 176 ? -0.758  -2.113  9.145   1.00 14.04 ? 176 ASP   A OD1 1 
ATOM   1374 O  OD2 . ASP   A 1 176 ? -1.040  -2.195  11.361  1.00 15.78 ? 176 ASP   A OD2 1 
ATOM   1375 N  N   . LEU   A 1 177 ? 1.838   -3.932  8.012   1.00 10.02 ? 177 LEU   A N   1 
ATOM   1376 C  CA  . LEU   A 1 177 ? 1.699   -4.660  6.773   1.00 11.68 ? 177 LEU   A CA  1 
ATOM   1377 C  C   . LEU   A 1 177 ? 0.236   -4.896  6.437   1.00 13.89 ? 177 LEU   A C   1 
ATOM   1378 O  O   . LEU   A 1 177 ? -0.035  -5.442  5.367   1.00 14.24 ? 177 LEU   A O   1 
ATOM   1379 C  CB  . LEU   A 1 177 ? 2.515   -5.957  6.811   1.00 12.86 ? 177 LEU   A CB  1 
ATOM   1380 C  CG  . LEU   A 1 177 ? 3.975   -5.839  6.344   1.00 14.19 ? 177 LEU   A CG  1 
ATOM   1381 C  CD1 . LEU   A 1 177 ? 4.061   -5.482  4.879   1.00 15.67 ? 177 LEU   A CD1 1 
ATOM   1382 C  CD2 . LEU   A 1 177 ? 4.760   -4.883  7.246   1.00 15.40 ? 177 LEU   A CD2 1 
ATOM   1383 N  N   . GLU   A 1 178 ? -0.695  -4.374  7.266   1.00 13.18 ? 178 GLU   A N   1 
ATOM   1384 C  CA  . GLU   A 1 178 ? -2.084  -4.279  6.861   1.00 13.91 ? 178 GLU   A CA  1 
ATOM   1385 C  C   . GLU   A 1 178 ? -2.388  -2.890  6.323   1.00 12.62 ? 178 GLU   A C   1 
ATOM   1386 O  O   . GLU   A 1 178 ? -3.529  -2.589  6.020   1.00 13.10 ? 178 GLU   A O   1 
ATOM   1387 C  CB  . GLU   A 1 178 ? -3.025  -4.558  8.033   1.00 16.84 ? 178 GLU   A CB  1 
ATOM   1388 C  CG  . GLU   A 1 178 ? -2.915  -5.934  8.649   1.00 20.98 ? 178 GLU   A CG  1 
ATOM   1389 C  CD  . GLU   A 1 178 ? -3.938  -6.142  9.763   1.00 28.13 ? 178 GLU   A CD  1 
ATOM   1390 O  OE1 . GLU   A 1 178 ? -4.249  -5.157  10.500  1.00 35.18 ? 178 GLU   A OE1 1 
ATOM   1391 O  OE2 . GLU   A 1 178 ? -4.459  -7.265  9.874   1.00 40.04 ? 178 GLU   A OE2 1 
ATOM   1392 N  N   . GLY   A 1 179 ? -1.372  -2.030  6.188   1.00 11.57 ? 179 GLY   A N   1 
ATOM   1393 C  CA  . GLY   A 1 179 ? -1.531  -0.779  5.500   1.00 10.93 ? 179 GLY   A CA  1 
ATOM   1394 C  C   . GLY   A 1 179 ? -2.034  0.366   6.371   1.00 9.90  ? 179 GLY   A C   1 
ATOM   1395 O  O   . GLY   A 1 179 ? -2.342  1.422   5.838   1.00 10.01 ? 179 GLY   A O   1 
ATOM   1396 N  N   . ASN   A 1 180 ? -2.114  0.174   7.680   1.00 10.83 ? 180 ASN   A N   1 
ATOM   1397 C  CA  . ASN   A 1 180 ? -2.493  1.264   8.592   1.00 11.55 ? 180 ASN   A CA  1 
ATOM   1398 C  C   . ASN   A 1 180 ? -1.271  2.052   9.077   1.00 10.22 ? 180 ASN   A C   1 
ATOM   1399 O  O   . ASN   A 1 180 ? -0.321  1.461   9.606   1.00 10.13 ? 180 ASN   A O   1 
ATOM   1400 C  CB  . ASN   A 1 180 ? -3.213  0.694   9.799   1.00 13.43 ? 180 ASN   A CB  1 
ATOM   1401 C  CG  . ASN   A 1 180 ? -4.506  0.008   9.426   1.00 16.42 ? 180 ASN   A CG  1 
ATOM   1402 O  OD1 . ASN   A 1 180 ? -4.686  -1.173  9.719   1.00 24.10 ? 180 ASN   A OD1 1 
ATOM   1403 N  ND2 . ASN   A 1 180 ? -5.364  0.722   8.752   1.00 14.38 ? 180 ASN   A ND2 1 
ATOM   1404 N  N   . PHE   A 1 181 ? -1.271  3.392   8.910   1.00 10.43 ? 181 PHE   A N   1 
ATOM   1405 C  CA  . PHE   A 1 181 ? -0.165  4.187   9.431   1.00 9.72  ? 181 PHE   A CA  1 
ATOM   1406 C  C   . PHE   A 1 181 ? -0.016  4.011   10.926  1.00 10.21 ? 181 PHE   A C   1 
ATOM   1407 O  O   . PHE   A 1 181 ? -0.996  3.829   11.644  1.00 11.34 ? 181 PHE   A O   1 
ATOM   1408 C  CB  . PHE   A 1 181 ? -0.321  5.679   9.096   1.00 10.69 ? 181 PHE   A CB  1 
ATOM   1409 C  CG  . PHE   A 1 181 ? 0.362   6.084   7.820   1.00 10.63 ? 181 PHE   A CG  1 
ATOM   1410 C  CD1 . PHE   A 1 181 ? 1.685   6.480   7.833   1.00 11.55 ? 181 PHE   A CD1 1 
ATOM   1411 C  CD2 . PHE   A 1 181 ? -0.300  6.023   6.594   1.00 10.97 ? 181 PHE   A CD2 1 
ATOM   1412 C  CE1 . PHE   A 1 181 ? 2.333   6.777   6.653   1.00 10.55 ? 181 PHE   A CE1 1 
ATOM   1413 C  CE2 . PHE   A 1 181 ? 0.354   6.302   5.415   1.00 11.84 ? 181 PHE   A CE2 1 
ATOM   1414 C  CZ  . PHE   A 1 181 ? 1.672   6.729   5.445   1.00 11.90 ? 181 PHE   A CZ  1 
ATOM   1415 N  N   . TYR   A 1 182 ? 1.220   4.055   11.366  1.00 9.13  ? 182 TYR   A N   1 
ATOM   1416 C  CA  . TYR   A 1 182 ? 1.547   4.415   12.729  1.00 9.88  ? 182 TYR   A CA  1 
ATOM   1417 C  C   . TYR   A 1 182 ? 1.460   5.928   12.787  1.00 9.78  ? 182 TYR   A C   1 
ATOM   1418 O  O   . TYR   A 1 182 ? 2.114   6.600   12.009  1.00 9.98  ? 182 TYR   A O   1 
ATOM   1419 C  CB  . TYR   A 1 182 ? 2.950   3.914   13.056  1.00 9.61  ? 182 TYR   A CB  1 
ATOM   1420 C  CG  . TYR   A 1 182 ? 3.100   2.397   13.112  1.00 10.00 ? 182 TYR   A CG  1 
ATOM   1421 C  CD1 . TYR   A 1 182 ? 2.731   1.711   14.270  1.00 10.29 ? 182 TYR   A CD1 1 
ATOM   1422 C  CD2 . TYR   A 1 182 ? 3.572   1.650   12.016  1.00 9.80  ? 182 TYR   A CD2 1 
ATOM   1423 C  CE1 . TYR   A 1 182 ? 2.825   0.325   14.356  1.00 10.32 ? 182 TYR   A CE1 1 
ATOM   1424 C  CE2 . TYR   A 1 182 ? 3.755   0.283   12.145  1.00 9.38  ? 182 TYR   A CE2 1 
ATOM   1425 C  CZ  . TYR   A 1 182 ? 3.348   -0.380  13.285  1.00 9.59  ? 182 TYR   A CZ  1 
ATOM   1426 O  OH  . TYR   A 1 182 ? 3.496   -1.727  13.371  1.00 10.04 ? 182 TYR   A OH  1 
ATOM   1427 N  N   . GLY   A 1 183 ? 0.622   6.458   13.669  1.00 10.87 ? 183 GLY   A N   1 
ATOM   1428 C  CA  . GLY   A 1 183 ? 0.525   7.901   13.821  1.00 11.43 ? 183 GLY   A CA  1 
ATOM   1429 C  C   . GLY   A 1 183 ? -0.485  8.558   12.888  1.00 12.91 ? 183 GLY   A C   1 
ATOM   1430 O  O   . GLY   A 1 183 ? -1.122  7.926   12.005  1.00 12.91 ? 183 GLY   A O   1 
ATOM   1431 N  N   . PRO   A 1 184 ? -0.620  9.895   13.046  1.00 13.36 ? 184 PRO   A N   1 
ATOM   1432 C  CA  . PRO   A 1 184 ? -1.666  10.659  12.366  1.00 14.04 ? 184 PRO   A CA  1 
ATOM   1433 C  C   . PRO   A 1 184 ? -1.329  11.084  10.944  1.00 12.33 ? 184 PRO   A C   1 
ATOM   1434 O  O   . PRO   A 1 184 ? -1.704  12.157  10.466  1.00 15.72 ? 184 PRO   A O   1 
ATOM   1435 C  CB  . PRO   A 1 184 ? -1.795  11.894  13.285  1.00 15.17 ? 184 PRO   A CB  1 
ATOM   1436 C  CG  . PRO   A 1 184 ? -0.348  12.130  13.742  1.00 16.30 ? 184 PRO   A CG  1 
ATOM   1437 C  CD  . PRO   A 1 184 ? 0.165   10.720  13.983  1.00 14.52 ? 184 PRO   A CD  1 
ATOM   1438 N  N   . PHE   A 1 185 ? -0.629  10.221  10.210  1.00 11.23 ? 185 PHE   A N   1 
ATOM   1439 C  CA  . PHE   A 1 185 ? -0.078  10.595  8.919   1.00 11.75 ? 185 PHE   A CA  1 
ATOM   1440 C  C   . PHE   A 1 185 ? -0.914  10.024  7.781   1.00 12.30 ? 185 PHE   A C   1 
ATOM   1441 O  O   . PHE   A 1 185 ? -1.710  9.121   7.996   1.00 14.45 ? 185 PHE   A O   1 
ATOM   1442 C  CB  . PHE   A 1 185 ? 1.344   10.054  8.814   1.00 12.09 ? 185 PHE   A CB  1 
ATOM   1443 C  CG  . PHE   A 1 185 ? 2.194   10.508  9.945   1.00 12.17 ? 185 PHE   A CG  1 
ATOM   1444 C  CD1 . PHE   A 1 185 ? 2.404   11.861  10.147  1.00 14.52 ? 185 PHE   A CD1 1 
ATOM   1445 C  CD2 . PHE   A 1 185 ? 2.732   9.610   10.840  1.00 12.64 ? 185 PHE   A CD2 1 
ATOM   1446 C  CE1 . PHE   A 1 185 ? 3.131   12.319  11.234  1.00 14.69 ? 185 PHE   A CE1 1 
ATOM   1447 C  CE2 . PHE   A 1 185 ? 3.451   10.061  11.927  1.00 13.92 ? 185 PHE   A CE2 1 
ATOM   1448 C  CZ  . PHE   A 1 185 ? 3.637   11.421  12.135  1.00 15.72 ? 185 PHE   A CZ  1 
ATOM   1449 N  N   . VAL   A 1 186 ? -0.734  10.606  6.588   1.00 13.44 ? 186 VAL   A N   1 
ATOM   1450 C  CA  . VAL   A 1 186 ? -1.386  10.170  5.377   1.00 12.72 ? 186 VAL   A CA  1 
ATOM   1451 C  C   . VAL   A 1 186 ? -0.379  10.097  4.224   1.00 12.46 ? 186 VAL   A C   1 
ATOM   1452 O  O   . VAL   A 1 186 ? 0.605   10.831  4.156   1.00 13.15 ? 186 VAL   A O   1 
ATOM   1453 C  CB  . VAL   A 1 186 ? -2.595  11.078  5.048   1.00 15.92 ? 186 VAL   A CB  1 
ATOM   1454 C  CG1 . VAL   A 1 186 ? -3.580  11.133  6.217   1.00 17.80 ? 186 VAL   A CG1 1 
ATOM   1455 C  CG2 . VAL   A 1 186 ? -2.171  12.470  4.695   1.00 18.27 ? 186 VAL   A CG2 1 
ATOM   1456 N  N   . ASP   A 1 187 ? -0.654  9.186   3.300   1.00 11.85 ? 187 ASP   A N   1 
ATOM   1457 C  CA  . ASP   A 1 187 ? 0.221   8.888   2.178   1.00 12.54 ? 187 ASP   A CA  1 
ATOM   1458 C  C   . ASP   A 1 187 ? -0.042  9.862   1.041   1.00 14.00 ? 187 ASP   A C   1 
ATOM   1459 O  O   . ASP   A 1 187 ? -0.594  9.515   0.012   1.00 16.07 ? 187 ASP   A O   1 
ATOM   1460 C  CB  . ASP   A 1 187 ? 0.155   7.425   1.754   1.00 11.54 ? 187 ASP   A CB  1 
ATOM   1461 C  CG  . ASP   A 1 187 ? -1.203  6.749   1.560   1.00 11.97 ? 187 ASP   A CG  1 
ATOM   1462 O  OD1 . ASP   A 1 187 ? -2.247  7.280   2.079   1.00 10.82 ? 187 ASP   A OD1 1 
ATOM   1463 O  OD2 . ASP   A 1 187 ? -1.172  5.642   0.972   1.00 11.06 ? 187 ASP   A OD2 1 
ATOM   1464 N  N   . ARG   A 1 188 ? 0.402   11.093  1.256   1.00 15.89 ? 188 ARG   A N   1 
ATOM   1465 C  CA  . ARG   A 1 188 ? 0.266   12.168  0.294   1.00 17.93 ? 188 ARG   A CA  1 
ATOM   1466 C  C   . ARG   A 1 188 ? 1.549   12.973  0.394   1.00 18.50 ? 188 ARG   A C   1 
ATOM   1467 O  O   . ARG   A 1 188 ? 2.074   13.100  1.484   1.00 17.48 ? 188 ARG   A O   1 
ATOM   1468 C  CB  . ARG   A 1 188 ? -0.980  12.957  0.722   1.00 20.85 ? 188 ARG   A CB  1 
ATOM   1469 C  CG  . ARG   A 1 188 ? -1.023  14.414  0.327   1.00 30.37 ? 188 ARG   A CG  1 
ATOM   1470 C  CD  . ARG   A 1 188 ? -2.400  14.999  0.649   1.00 31.62 ? 188 ARG   A CD  1 
ATOM   1471 N  NE  . ARG   A 1 188 ? -2.500  16.230  -0.126  1.00 38.24 ? 188 ARG   A NE  1 
ATOM   1472 C  CZ  . ARG   A 1 188 ? -3.145  17.325  0.234   1.00 36.43 ? 188 ARG   A CZ  1 
ATOM   1473 N  NH1 . ARG   A 1 188 ? -4.026  17.300  1.216   1.00 38.89 ? 188 ARG   A NH1 1 
ATOM   1474 N  NH2 . ARG   A 1 188 ? -2.962  18.431  -0.466  1.00 43.64 ? 188 ARG   A NH2 1 
ATOM   1475 N  N   . GLN   A 1 189 ? 2.014   13.557  -0.711  1.00 19.58 ? 189 GLN   A N   1 
ATOM   1476 C  CA  . GLN   A 1 189 ? 3.168   14.440  -0.679  1.00 20.52 ? 189 GLN   A CA  1 
ATOM   1477 C  C   . GLN   A 1 189 ? 2.743   15.840  -0.252  1.00 21.96 ? 189 GLN   A C   1 
ATOM   1478 O  O   . GLN   A 1 189 ? 2.540   16.723  -1.079  1.00 22.90 ? 189 GLN   A O   1 
ATOM   1479 C  CB  . GLN   A 1 189 ? 3.821   14.419  -2.068  1.00 22.07 ? 189 GLN   A CB  1 
ATOM   1480 C  CG  . GLN   A 1 189 ? 5.176   15.114  -2.117  1.00 26.00 ? 189 GLN   A CG  1 
ATOM   1481 C  CD  . GLN   A 1 189 ? 5.730   15.193  -3.523  1.00 32.83 ? 189 GLN   A CD  1 
ATOM   1482 O  OE1 . GLN   A 1 189 ? 5.471   14.347  -4.370  1.00 40.36 ? 189 GLN   A OE1 1 
ATOM   1483 N  NE2 . GLN   A 1 189 ? 6.551   16.196  -3.777  1.00 34.01 ? 189 GLN   A NE2 1 
ATOM   1484 N  N   . THR   A 1 190 ? 2.539   16.017  1.041   1.00 19.77 ? 190 THR   A N   1 
ATOM   1485 C  CA  . THR   A 1 190 ? 2.245   17.292  1.661   1.00 23.91 ? 190 THR   A CA  1 
ATOM   1486 C  C   . THR   A 1 190 ? 3.016   17.332  2.984   1.00 25.33 ? 190 THR   A C   1 
ATOM   1487 O  O   . THR   A 1 190 ? 3.231   16.278  3.589   1.00 23.22 ? 190 THR   A O   1 
ATOM   1488 C  CB  . THR   A 1 190 ? 0.721   17.432  1.828   1.00 28.01 ? 190 THR   A CB  1 
ATOM   1489 O  OG1 . THR   A 1 190 ? 0.388   18.788  2.111   1.00 36.87 ? 190 THR   A OG1 1 
ATOM   1490 C  CG2 . THR   A 1 190 ? 0.181   16.583  2.962   1.00 28.36 ? 190 THR   A CG2 1 
ATOM   1491 N  N   . ALA   A 1 191 ? 3.460   18.520  3.422   1.00 20.90 ? 191 ALA   A N   1 
ATOM   1492 C  CA  . ALA   A 1 191 ? 4.192   18.655  4.671   1.00 21.34 ? 191 ALA   A CA  1 
ATOM   1493 C  C   . ALA   A 1 191 ? 3.349   18.223  5.868   1.00 19.91 ? 191 ALA   A C   1 
ATOM   1494 O  O   . ALA   A 1 191 ? 2.219   18.665  6.041   1.00 20.67 ? 191 ALA   A O   1 
ATOM   1495 C  CB  . ALA   A 1 191 ? 4.685   20.075  4.854   1.00 23.75 ? 191 ALA   A CB  1 
ATOM   1496 N  N   . GLN   A 1 192 ? 3.898   17.309  6.668   1.00 17.13 ? 192 GLN   A N   1 
ATOM   1497 C  CA  . GLN   A 1 192 ? 3.223   16.751  7.829   1.00 16.49 ? 192 GLN   A CA  1 
ATOM   1498 C  C   . GLN   A 1 192 ? 4.152   16.785  9.038   1.00 16.89 ? 192 GLN   A C   1 
ATOM   1499 O  O   . GLN   A 1 192 ? 5.266   16.291  8.985   1.00 19.85 ? 192 GLN   A O   1 
ATOM   1500 C  CB  . GLN   A 1 192 ? 2.774   15.327  7.492   1.00 14.73 ? 192 GLN   A CB  1 
ATOM   1501 C  CG  . GLN   A 1 192 ? 1.707   15.313  6.417   1.00 14.83 ? 192 GLN   A CG  1 
ATOM   1502 C  CD  . GLN   A 1 192 ? 1.311   13.892  6.064   1.00 13.45 ? 192 GLN   A CD  1 
ATOM   1503 O  OE1 . GLN   A 1 192 ? 0.786   13.141  6.882   1.00 13.58 ? 192 GLN   A OE1 1 
ATOM   1504 N  NE2 . GLN   A 1 192 ? 1.544   13.531  4.825   1.00 14.42 ? 192 GLN   A NE2 1 
ATOM   1505 N  N   . ALA   A 1 193 ? 3.636   17.315  10.138  1.00 17.84 ? 193 ALA   A N   1 
ATOM   1506 C  CA  . ALA   A 1 193 ? 4.300   17.345  11.436  1.00 18.09 ? 193 ALA   A CA  1 
ATOM   1507 C  C   . ALA   A 1 193 ? 3.772   16.213  12.300  1.00 17.92 ? 193 ALA   A C   1 
ATOM   1508 O  O   . ALA   A 1 193 ? 2.617   15.788  12.168  1.00 15.30 ? 193 ALA   A O   1 
ATOM   1509 C  CB  . ALA   A 1 193 ? 4.055   18.671  12.099  1.00 19.51 ? 193 ALA   A CB  1 
ATOM   1510 N  N   . ALA   A 1 194 ? 4.647   15.704  13.190  1.00 17.08 ? 194 ALA   A N   1 
ATOM   1511 C  CA  . ALA   A 1 194 ? 4.246   14.764  14.229  1.00 17.89 ? 194 ALA   A CA  1 
ATOM   1512 C  C   . ALA   A 1 194 ? 3.906   15.486  15.530  1.00 17.21 ? 194 ALA   A C   1 
ATOM   1513 O  O   . ALA   A 1 194 ? 4.220   16.662  15.710  1.00 19.12 ? 194 ALA   A O   1 
ATOM   1514 C  CB  . ALA   A 1 194 ? 5.370   13.761  14.470  1.00 16.60 ? 194 ALA   A CB  1 
ATOM   1515 N  N   . GLY   A 1 195 ? 3.224   14.765  16.416  1.00 17.94 ? 195 GLY   A N   1 
ATOM   1516 C  CA  . GLY   A 1 195 ? 3.029   15.150  17.809  1.00 20.52 ? 195 GLY   A CA  1 
ATOM   1517 C  C   . GLY   A 1 195 ? 4.369   15.329  18.513  1.00 21.17 ? 195 GLY   A C   1 
ATOM   1518 O  O   . GLY   A 1 195 ? 5.428   14.912  18.026  1.00 16.16 ? 195 GLY   A O   1 
ATOM   1519 N  N   . THR   A 1 196 ? 4.342   16.014  19.651  1.00 22.22 ? 196 THR   A N   1 
ATOM   1520 C  CA  . THR   A 1 196 ? 5.568   16.195  20.401  1.00 22.05 ? 196 THR   A CA  1 
ATOM   1521 C  C   . THR   A 1 196 ? 6.004   14.822  20.897  1.00 20.59 ? 196 THR   A C   1 
ATOM   1522 O  O   . THR   A 1 196 ? 5.199   13.997  21.308  1.00 23.41 ? 196 THR   A O   1 
ATOM   1523 C  CB  . THR   A 1 196 ? 5.390   17.265  21.482  1.00 29.83 ? 196 THR   A CB  1 
ATOM   1524 O  OG1 . THR   A 1 196 ? 4.354   16.807  22.344  1.00 37.41 ? 196 THR   A OG1 1 
ATOM   1525 C  CG2 . THR   A 1 196 ? 5.011   18.600  20.892  1.00 26.47 ? 196 THR   A CG2 1 
ATOM   1526 N  N   . ASP   A 1 197 ? 7.302   14.578  20.823  1.00 19.36 ? 197 ASP   A N   1 
ATOM   1527 C  CA  . ASP   A 1 197 ? 7.792   13.258  21.181  1.00 19.11 ? 197 ASP   A CA  1 
ATOM   1528 C  C   . ASP   A 1 197 ? 8.148   13.256  22.658  1.00 19.34 ? 197 ASP   A C   1 
ATOM   1529 O  O   . ASP   A 1 197 ? 8.245   14.307  23.290  1.00 20.96 ? 197 ASP   A O   1 
ATOM   1530 C  CB  . ASP   A 1 197 ? 8.965   12.838  20.327  1.00 18.58 ? 197 ASP   A CB  1 
ATOM   1531 C  CG  . ASP   A 1 197 ? 9.160   11.337  20.216  1.00 17.82 ? 197 ASP   A CG  1 
ATOM   1532 O  OD1 . ASP   A 1 197 ? 8.212   10.544  20.513  1.00 17.01 ? 197 ASP   A OD1 1 
ATOM   1533 O  OD2 . ASP   A 1 197 ? 10.283  10.978  19.886  1.00 17.12 ? 197 ASP   A OD2 1 
ATOM   1534 N  N   . THR   A 1 198 ? 8.221   12.057  23.205  1.00 16.80 ? 198 THR   A N   1 
ATOM   1535 C  CA  . THR   A 1 198 ? 8.608   11.824  24.580  1.00 16.05 ? 198 THR   A CA  1 
ATOM   1536 C  C   . THR   A 1 198 ? 9.653   10.713  24.589  1.00 15.57 ? 198 THR   A C   1 
ATOM   1537 O  O   . THR   A 1 198 ? 9.866   10.048  23.565  1.00 15.55 ? 198 THR   A O   1 
ATOM   1538 C  CB  . THR   A 1 198 ? 7.391   11.428  25.419  1.00 21.15 ? 198 THR   A CB  1 
ATOM   1539 O  OG1 . THR   A 1 198 ? 6.715   10.363  24.762  1.00 22.17 ? 198 THR   A OG1 1 
ATOM   1540 C  CG2 . THR   A 1 198 ? 6.400   12.555  25.635  1.00 24.27 ? 198 THR   A CG2 1 
ATOM   1541 N  N   . THR   A 1 199 ? 10.302  10.551  25.740  1.00 13.79 ? 199 THR   A N   1 
ATOM   1542 C  CA  . THR   A 1 199 ? 11.348  9.570   25.953  1.00 13.57 ? 199 THR   A CA  1 
ATOM   1543 C  C   . THR   A 1 199 ? 10.800  8.257   26.523  1.00 13.49 ? 199 THR   A C   1 
ATOM   1544 O  O   . THR   A 1 199 ? 9.890   8.224   27.379  1.00 13.47 ? 199 THR   A O   1 
ATOM   1545 C  CB  . THR   A 1 199 ? 12.452  10.190  26.794  1.00 15.09 ? 199 THR   A CB  1 
ATOM   1546 O  OG1 . THR   A 1 199 ? 12.922  11.377  26.144  1.00 15.07 ? 199 THR   A OG1 1 
ATOM   1547 C  CG2 . THR   A 1 199 ? 13.586  9.229   27.025  1.00 14.83 ? 199 THR   A CG2 1 
ATOM   1548 N  N   . ILE   A 1 200 ? 11.303  7.128   25.985  1.00 12.25 ? 200 ILE   A N   1 
ATOM   1549 C  CA  . ILE   A 1 200 ? 10.756  5.831   26.350  1.00 11.78 ? 200 ILE   A CA  1 
ATOM   1550 C  C   . ILE   A 1 200 ? 11.420  5.375   27.656  1.00 11.63 ? 200 ILE   A C   1 
ATOM   1551 O  O   . ILE   A 1 200 ? 12.513  4.826   27.668  1.00 10.18 ? 200 ILE   A O   1 
ATOM   1552 C  CB  . ILE   A 1 200 ? 10.924  4.787   25.230  1.00 11.47 ? 200 ILE   A CB  1 
ATOM   1553 C  CG1 . ILE   A 1 200 ? 10.356  5.298   23.901  1.00 14.34 ? 200 ILE   A CG1 1 
ATOM   1554 C  CG2 . ILE   A 1 200 ? 10.314  3.489   25.656  1.00 12.35 ? 200 ILE   A CG2 1 
ATOM   1555 C  CD1 . ILE   A 1 200 ? 11.123  4.782   22.717  1.00 14.89 ? 200 ILE   A CD1 1 
ATOM   1556 N  N   . THR   A 1 201 ? 10.743  5.641   28.795  1.00 11.89 ? 201 THR   A N   1 
ATOM   1557 C  CA  . THR   A 1 201 ? 11.335  5.463   30.124  1.00 11.61 ? 201 THR   A CA  1 
ATOM   1558 C  C   . THR   A 1 201 ? 11.807  4.046   30.426  1.00 10.00 ? 201 THR   A C   1 
ATOM   1559 O  O   . THR   A 1 201 ? 12.930  3.866   30.879  1.00 11.41 ? 201 THR   A O   1 
ATOM   1560 C  CB  . THR   A 1 201 ? 10.328  5.885   31.206  1.00 11.90 ? 201 THR   A CB  1 
ATOM   1561 O  OG1 . THR   A 1 201 ? 9.841   7.134   30.742  1.00 12.26 ? 201 THR   A OG1 1 
ATOM   1562 C  CG2 . THR   A 1 201 ? 10.931  6.038   32.581  1.00 12.45 ? 201 THR   A CG2 1 
ATOM   1563 N  N   . VAL   A 1 202 ? 10.994  3.047   30.151  1.00 10.71 ? 202 VAL   A N   1 
ATOM   1564 C  CA  . VAL   A 1 202 ? 11.338  1.664   30.475  1.00 10.95 ? 202 VAL   A CA  1 
ATOM   1565 C  C   . VAL   A 1 202 ? 12.615  1.303   29.698  1.00 11.09 ? 202 VAL   A C   1 
ATOM   1566 O  O   . VAL   A 1 202 ? 13.455  0.574   30.205  1.00 11.87 ? 202 VAL   A O   1 
ATOM   1567 C  CB  . VAL   A 1 202 ? 10.189  0.677   30.178  1.00 12.22 ? 202 VAL   A CB  1 
ATOM   1568 C  CG1 . VAL   A 1 202 ? 9.773   0.667   28.704  1.00 12.46 ? 202 VAL   A CG1 1 
ATOM   1569 C  CG2 . VAL   A 1 202 ? 10.527  -0.730  30.673  1.00 11.38 ? 202 VAL   A CG2 1 
ATOM   1570 N  N   . ASN   A 1 203 ? 12.766  1.817   28.472  1.00 11.08 ? 203 ASN   A N   1 
ATOM   1571 C  CA  . ASN   A 1 203 ? 13.981  1.562   27.690  1.00 11.12 ? 203 ASN   A CA  1 
ATOM   1572 C  C   . ASN   A 1 203 ? 15.224  2.229   28.270  1.00 11.08 ? 203 ASN   A C   1 
ATOM   1573 O  O   . ASN   A 1 203 ? 16.315  1.662   28.223  1.00 11.89 ? 203 ASN   A O   1 
ATOM   1574 C  CB  . ASN   A 1 203 ? 13.799  1.947   26.226  1.00 11.02 ? 203 ASN   A CB  1 
ATOM   1575 C  CG  . ASN   A 1 203 ? 12.809  1.064   25.489  1.00 10.52 ? 203 ASN   A CG  1 
ATOM   1576 O  OD1 . ASN   A 1 203 ? 12.220  0.131   26.016  1.00 11.16 ? 203 ASN   A OD1 1 
ATOM   1577 N  ND2 . ASN   A 1 203 ? 12.602  1.359   24.221  1.00 10.85 ? 203 ASN   A ND2 1 
ATOM   1578 N  N   . VAL   A 1 204 ? 15.104  3.473   28.738  1.00 10.98 ? 204 VAL   A N   1 
ATOM   1579 C  CA  . VAL   A 1 204 ? 16.218  4.144   29.391  1.00 10.82 ? 204 VAL   A CA  1 
ATOM   1580 C  C   . VAL   A 1 204 ? 16.632  3.320   30.606  1.00 10.55 ? 204 VAL   A C   1 
ATOM   1581 O  O   . VAL   A 1 204 ? 17.826  3.142   30.832  1.00 11.97 ? 204 VAL   A O   1 
ATOM   1582 C  CB  . VAL   A 1 204 ? 15.893  5.599   29.765  1.00 10.84 ? 204 VAL   A CB  1 
ATOM   1583 C  CG1 . VAL   A 1 204 ? 17.003  6.246   30.595  1.00 10.96 ? 204 VAL   A CG1 1 
ATOM   1584 C  CG2 . VAL   A 1 204 ? 15.587  6.469   28.550  1.00 11.99 ? 204 VAL   A CG2 1 
ATOM   1585 N  N   . LEU   A 1 205 ? 15.654  2.813   31.366  1.00 10.87 ? 205 LEU   A N   1 
ATOM   1586 C  CA  . LEU   A 1 205 ? 16.013  2.014   32.532  1.00 12.06 ? 205 LEU   A CA  1 
ATOM   1587 C  C   . LEU   A 1 205 ? 16.742  0.723   32.125  1.00 12.59 ? 205 LEU   A C   1 
ATOM   1588 O  O   . LEU   A 1 205 ? 17.732  0.354   32.772  1.00 12.69 ? 205 LEU   A O   1 
ATOM   1589 C  CB  . LEU   A 1 205 ? 14.789  1.703   33.386  1.00 12.29 ? 205 LEU   A CB  1 
ATOM   1590 C  CG  . LEU   A 1 205 ? 14.162  2.926   34.048  1.00 13.77 ? 205 LEU   A CG  1 
ATOM   1591 C  CD1 . LEU   A 1 205 ? 12.798  2.591   34.639  1.00 15.19 ? 205 LEU   A CD1 1 
ATOM   1592 C  CD2 . LEU   A 1 205 ? 15.068  3.475   35.123  1.00 14.95 ? 205 LEU   A CD2 1 
ATOM   1593 N  N   . ALA   A 1 206 ? 16.239  0.047   31.088  1.00 11.14 ? 206 ALA   A N   1 
ATOM   1594 C  CA  . ALA   A 1 206 ? 16.917  -1.134  30.538  1.00 13.13 ? 206 ALA   A CA  1 
ATOM   1595 C  C   . ALA   A 1 206 ? 18.382  -0.841  30.180  1.00 12.42 ? 206 ALA   A C   1 
ATOM   1596 O  O   . ALA   A 1 206 ? 19.293  -1.615  30.523  1.00 14.99 ? 206 ALA   A O   1 
ATOM   1597 C  CB  . ALA   A 1 206 ? 16.108  -1.644  29.351  1.00 12.04 ? 206 ALA   A CB  1 
ATOM   1598 N  N   . TRP   A 1 207 ? 18.622  0.277   29.525  1.00 13.08 ? 207 TRP   A N   1 
ATOM   1599 C  CA  . TRP   A 1 207 ? 19.957  0.660   29.098  1.00 15.18 ? 207 TRP   A CA  1 
ATOM   1600 C  C   . TRP   A 1 207 ? 20.854  0.992   30.281  1.00 14.64 ? 207 TRP   A C   1 
ATOM   1601 O  O   . TRP   A 1 207 ? 22.059  0.690   30.260  1.00 14.74 ? 207 TRP   A O   1 
ATOM   1602 C  CB  . TRP   A 1 207 ? 19.826  1.828   28.137  1.00 15.07 ? 207 TRP   A CB  1 
ATOM   1603 C  CG  . TRP   A 1 207 ? 21.098  2.477   27.679  1.00 16.91 ? 207 TRP   A CG  1 
ATOM   1604 C  CD1 . TRP   A 1 207 ? 21.994  2.056   26.727  1.00 17.62 ? 207 TRP   A CD1 1 
ATOM   1605 C  CD2 . TRP   A 1 207 ? 21.562  3.748   28.126  1.00 17.98 ? 207 TRP   A CD2 1 
ATOM   1606 N  NE1 . TRP   A 1 207 ? 22.971  2.996   26.553  1.00 17.86 ? 207 TRP   A NE1 1 
ATOM   1607 C  CE2 . TRP   A 1 207 ? 22.744  4.035   27.390  1.00 18.62 ? 207 TRP   A CE2 1 
ATOM   1608 C  CE3 . TRP   A 1 207 ? 21.086  4.668   29.063  1.00 18.65 ? 207 TRP   A CE3 1 
ATOM   1609 C  CZ2 . TRP   A 1 207 ? 23.447  5.220   27.563  1.00 20.51 ? 207 TRP   A CZ2 1 
ATOM   1610 C  CZ3 . TRP   A 1 207 ? 21.782  5.846   29.218  1.00 20.18 ? 207 TRP   A CZ3 1 
ATOM   1611 C  CH2 . TRP   A 1 207 ? 22.935  6.109   28.486  1.00 19.54 ? 207 TRP   A CH2 1 
ATOM   1612 N  N   . LEU   A 1 208 ? 20.297  1.604   31.332  1.00 14.43 ? 208 LEU   A N   1 
ATOM   1613 C  CA  . LEU   A 1 208 ? 21.108  1.851   32.533  1.00 14.52 ? 208 LEU   A CA  1 
ATOM   1614 C  C   . LEU   A 1 208 ? 21.541  0.528   33.164  1.00 13.34 ? 208 LEU   A C   1 
ATOM   1615 O  O   . LEU   A 1 208 ? 22.637  0.426   33.725  1.00 16.96 ? 208 LEU   A O   1 
ATOM   1616 C  CB  . LEU   A 1 208 ? 20.332  2.714   33.531  1.00 13.09 ? 208 LEU   A CB  1 
ATOM   1617 C  CG  . LEU   A 1 208 ? 20.080  4.163   33.137  1.00 13.59 ? 208 LEU   A CG  1 
ATOM   1618 C  CD1 . LEU   A 1 208 ? 19.249  4.860   34.194  1.00 14.42 ? 208 LEU   A CD1 1 
ATOM   1619 C  CD2 . LEU   A 1 208 ? 21.354  4.914   32.932  1.00 14.73 ? 208 LEU   A CD2 1 
ATOM   1620 N  N   . TYR   A 1 209 ? 20.671  -0.464  33.145  1.00 13.93 ? 209 TYR   A N   1 
ATOM   1621 C  CA  . TYR   A 1 209 ? 20.996  -1.796  33.606  1.00 14.49 ? 209 TYR   A CA  1 
ATOM   1622 C  C   . TYR   A 1 209 ? 22.089  -2.422  32.738  1.00 17.31 ? 209 TYR   A C   1 
ATOM   1623 O  O   . TYR   A 1 209 ? 23.013  -3.067  33.248  1.00 17.64 ? 209 TYR   A O   1 
ATOM   1624 C  CB  . TYR   A 1 209 ? 19.796  -2.737  33.630  1.00 14.34 ? 209 TYR   A CB  1 
ATOM   1625 C  CG  . TYR   A 1 209 ? 18.938  -2.629  34.875  1.00 14.55 ? 209 TYR   A CG  1 
ATOM   1626 C  CD1 . TYR   A 1 209 ? 19.400  -3.087  36.095  1.00 15.65 ? 209 TYR   A CD1 1 
ATOM   1627 C  CD2 . TYR   A 1 209 ? 17.654  -2.092  34.833  1.00 15.32 ? 209 TYR   A CD2 1 
ATOM   1628 C  CE1 . TYR   A 1 209 ? 18.625  -3.002  37.240  1.00 15.23 ? 209 TYR   A CE1 1 
ATOM   1629 C  CE2 . TYR   A 1 209 ? 16.852  -2.037  35.959  1.00 17.06 ? 209 TYR   A CE2 1 
ATOM   1630 C  CZ  . TYR   A 1 209 ? 17.351  -2.483  37.181  1.00 16.69 ? 209 TYR   A CZ  1 
ATOM   1631 O  OH  . TYR   A 1 209 ? 16.597  -2.405  38.330  1.00 18.06 ? 209 TYR   A OH  1 
ATOM   1632 N  N   . ALA   A 1 210 ? 21.980  -2.272  31.412  1.00 18.08 ? 210 ALA   A N   1 
ATOM   1633 C  CA  . ALA   A 1 210 ? 23.101  -2.698  30.564  1.00 17.15 ? 210 ALA   A CA  1 
ATOM   1634 C  C   . ALA   A 1 210 ? 24.393  -2.022  31.003  1.00 16.11 ? 210 ALA   A C   1 
ATOM   1635 O  O   . ALA   A 1 210 ? 25.436  -2.670  31.008  1.00 22.39 ? 210 ALA   A O   1 
ATOM   1636 C  CB  . ALA   A 1 210 ? 22.834  -2.377  29.119  1.00 17.25 ? 210 ALA   A CB  1 
ATOM   1637 N  N   . ALA   A 1 211 ? 24.369  -0.707  31.254  1.00 16.85 ? 211 ALA   A N   1 
ATOM   1638 C  CA  . ALA   A 1 211 ? 25.546  -0.009  31.701  1.00 18.34 ? 211 ALA   A CA  1 
ATOM   1639 C  C   . ALA   A 1 211 ? 26.116  -0.676  32.962  1.00 19.02 ? 211 ALA   A C   1 
ATOM   1640 O  O   . ALA   A 1 211 ? 27.310  -0.954  33.035  1.00 20.38 ? 211 ALA   A O   1 
ATOM   1641 C  CB  . ALA   A 1 211 ? 25.270  1.452   31.864  1.00 18.84 ? 211 ALA   A CB  1 
ATOM   1642 N  N   . VAL   A 1 212 ? 25.274  -1.016  33.928  1.00 21.06 ? 212 VAL   A N   1 
ATOM   1643 C  CA  . VAL   A 1 212 ? 25.781  -1.619  35.156  1.00 21.44 ? 212 VAL   A CA  1 
ATOM   1644 C  C   . VAL   A 1 212 ? 26.418  -2.982  34.857  1.00 24.89 ? 212 VAL   A C   1 
ATOM   1645 O  O   . VAL   A 1 212 ? 27.521  -3.288  35.347  1.00 25.18 ? 212 VAL   A O   1 
ATOM   1646 C  CB  . VAL   A 1 212 ? 24.674  -1.726  36.215  1.00 21.75 ? 212 VAL   A CB  1 
ATOM   1647 C  CG1 . VAL   A 1 212 ? 25.126  -2.570  37.408  1.00 23.37 ? 212 VAL   A CG1 1 
ATOM   1648 C  CG2 . VAL   A 1 212 ? 24.255  -0.334  36.633  1.00 21.37 ? 212 VAL   A CG2 1 
ATOM   1649 N  N   . ILE   A 1 213 ? 25.722  -3.790  34.057  1.00 23.20 ? 213 ILE   A N   1 
ATOM   1650 C  CA  . ILE   A 1 213 ? 26.217  -5.109  33.659  1.00 26.01 ? 213 ILE   A CA  1 
ATOM   1651 C  C   . ILE   A 1 213 ? 27.599  -4.989  33.014  1.00 26.54 ? 213 ILE   A C   1 
ATOM   1652 O  O   . ILE   A 1 213 ? 28.426  -5.872  33.209  1.00 27.64 ? 213 ILE   A O   1 
ATOM   1653 C  CB  . ILE   A 1 213 ? 25.218  -5.818  32.729  1.00 25.04 ? 213 ILE   A CB  1 
ATOM   1654 C  CG1 . ILE   A 1 213 ? 23.985  -6.250  33.519  1.00 22.52 ? 213 ILE   A CG1 1 
ATOM   1655 C  CG2 . ILE   A 1 213 ? 25.885  -6.998  32.000  1.00 25.94 ? 213 ILE   A CG2 1 
ATOM   1656 C  CD1 . ILE   A 1 213 ? 22.789  -6.578  32.695  1.00 23.16 ? 213 ILE   A CD1 1 
ATOM   1657 N  N   . ASN   A 1 214 ? 27.847  -3.892  32.288  1.00 25.72 ? 214 ASN   A N   1 
ATOM   1658 C  CA  . ASN   A 1 214 ? 29.105  -3.664  31.587  1.00 28.99 ? 214 ASN   A CA  1 
ATOM   1659 C  C   . ASN   A 1 214 ? 30.072  -2.792  32.397  1.00 31.59 ? 214 ASN   A C   1 
ATOM   1660 O  O   . ASN   A 1 214 ? 31.032  -2.261  31.837  1.00 30.86 ? 214 ASN   A O   1 
ATOM   1661 C  CB  . ASN   A 1 214 ? 28.806  -3.062  30.214  1.00 28.69 ? 214 ASN   A CB  1 
ATOM   1662 C  CG  . ASN   A 1 214 ? 28.357  -4.125  29.236  1.00 33.35 ? 214 ASN   A CG  1 
ATOM   1663 O  OD1 . ASN   A 1 214 ? 29.197  -4.820  28.670  1.00 32.36 ? 214 ASN   A OD1 1 
ATOM   1664 N  ND2 . ASN   A 1 214 ? 27.051  -4.297  29.066  1.00 29.79 ? 214 ASN   A ND2 1 
ATOM   1665 N  N   . GLY   A 1 215 ? 29.777  -2.555  33.687  1.00 31.53 ? 215 GLY   A N   1 
ATOM   1666 C  CA  . GLY   A 1 215 ? 30.727  -1.966  34.626  1.00 32.12 ? 215 GLY   A CA  1 
ATOM   1667 C  C   . GLY   A 1 215 ? 30.715  -0.443  34.720  1.00 29.91 ? 215 GLY   A C   1 
ATOM   1668 O  O   . GLY   A 1 215 ? 31.623  0.131   35.296  1.00 30.91 ? 215 GLY   A O   1 
ATOM   1669 N  N   . ASP   A 1 216 ? 29.716  0.234   34.152  1.00 25.33 ? 216 ASP   A N   1 
ATOM   1670 C  CA  . ASP   A 1 216 ? 29.645  1.684   34.177  1.00 26.82 ? 216 ASP   A CA  1 
ATOM   1671 C  C   . ASP   A 1 216 ? 28.547  2.043   35.189  1.00 31.33 ? 216 ASP   A C   1 
ATOM   1672 O  O   . ASP   A 1 216 ? 27.371  1.846   34.858  1.00 26.94 ? 216 ASP   A O   1 
ATOM   1673 C  CB  . ASP   A 1 216 ? 29.366  2.158   32.747  1.00 32.33 ? 216 ASP   A CB  1 
ATOM   1674 C  CG  . ASP   A 1 216 ? 29.853  3.530   32.314  1.00 38.29 ? 216 ASP   A CG  1 
ATOM   1675 O  OD1 . ASP   A 1 216 ? 30.306  4.317   33.171  1.00 34.63 ? 216 ASP   A OD1 1 
ATOM   1676 O  OD2 . ASP   A 1 216 ? 29.746  3.807   31.078  1.00 37.40 ? 216 ASP   A OD2 1 
ATOM   1677 N  N   . ARG   A 1 217 ? 28.937  2.454   36.424  1.00 26.39 ? 217 ARG   A N   1 
ATOM   1678 C  CA  . ARG   A 1 217 ? 28.014  2.541   37.558  1.00 25.51 ? 217 ARG   A CA  1 
ATOM   1679 C  C   . ARG   A 1 217 ? 28.032  3.890   38.257  1.00 21.43 ? 217 ARG   A C   1 
ATOM   1680 O  O   . ARG   A 1 217 ? 27.408  4.044   39.302  1.00 23.23 ? 217 ARG   A O   1 
ATOM   1681 C  CB  . ARG   A 1 217 ? 28.362  1.538   38.651  1.00 27.54 ? 217 ARG   A CB  1 
ATOM   1682 C  CG  . ARG   A 1 217 ? 28.299  0.081   38.249  1.00 28.21 ? 217 ARG   A CG  1 
ATOM   1683 C  CD  . ARG   A 1 217 ? 29.020  -0.752  39.283  1.00 28.34 ? 217 ARG   A CD  1 
ATOM   1684 N  NE  . ARG   A 1 217 ? 28.221  -0.830  40.498  1.00 25.81 ? 217 ARG   A NE  1 
ATOM   1685 C  CZ  . ARG   A 1 217 ? 27.436  -1.841  40.825  1.00 23.56 ? 217 ARG   A CZ  1 
ATOM   1686 N  NH1 . ARG   A 1 217 ? 27.370  -2.913  40.061  1.00 25.98 ? 217 ARG   A NH1 1 
ATOM   1687 N  NH2 . ARG   A 1 217 ? 26.661  -1.758  41.893  1.00 25.27 ? 217 ARG   A NH2 1 
ATOM   1688 N  N   . TRP   A 1 218 ? 28.647  4.897   37.662  1.00 20.75 ? 218 TRP   A N   1 
ATOM   1689 C  CA  . TRP   A 1 218 ? 28.848  6.164   38.332  1.00 20.91 ? 218 TRP   A CA  1 
ATOM   1690 C  C   . TRP   A 1 218 ? 27.530  6.829   38.732  1.00 23.01 ? 218 TRP   A C   1 
ATOM   1691 O  O   . TRP   A 1 218 ? 27.515  7.642   39.646  1.00 20.48 ? 218 TRP   A O   1 
ATOM   1692 C  CB  . TRP   A 1 218 ? 29.711  7.072   37.462  1.00 22.39 ? 218 TRP   A CB  1 
ATOM   1693 C  CG  . TRP   A 1 218 ? 29.080  7.563   36.178  1.00 23.57 ? 218 TRP   A CG  1 
ATOM   1694 C  CD1 . TRP   A 1 218 ? 29.326  7.078   34.919  1.00 24.12 ? 218 TRP   A CD1 1 
ATOM   1695 C  CD2 . TRP   A 1 218 ? 28.175  8.672   36.011  1.00 23.49 ? 218 TRP   A CD2 1 
ATOM   1696 N  NE1 . TRP   A 1 218 ? 28.596  7.778   33.988  1.00 22.68 ? 218 TRP   A NE1 1 
ATOM   1697 C  CE2 . TRP   A 1 218 ? 27.893  8.764   34.625  1.00 23.21 ? 218 TRP   A CE2 1 
ATOM   1698 C  CE3 . TRP   A 1 218 ? 27.550  9.574   36.882  1.00 25.58 ? 218 TRP   A CE3 1 
ATOM   1699 C  CZ2 . TRP   A 1 218 ? 27.020  9.717   34.117  1.00 26.43 ? 218 TRP   A CZ2 1 
ATOM   1700 C  CZ3 . TRP   A 1 218 ? 26.685  10.521  36.377  1.00 27.37 ? 218 TRP   A CZ3 1 
ATOM   1701 C  CH2 . TRP   A 1 218 ? 26.438  10.601  35.008  1.00 27.09 ? 218 TRP   A CH2 1 
ATOM   1702 N  N   . PHE   A 1 219 ? 26.427  6.495   38.032  1.00 19.78 ? 219 PHE   A N   1 
ATOM   1703 C  CA  . PHE   A 1 219 ? 25.162  7.190   38.176  1.00 19.83 ? 219 PHE   A CA  1 
ATOM   1704 C  C   . PHE   A 1 219 ? 24.294  6.588   39.276  1.00 18.33 ? 219 PHE   A C   1 
ATOM   1705 O  O   . PHE   A 1 219 ? 23.256  7.156   39.552  1.00 22.02 ? 219 PHE   A O   1 
ATOM   1706 C  CB  . PHE   A 1 219 ? 24.401  7.174   36.835  1.00 19.17 ? 219 PHE   A CB  1 
ATOM   1707 C  CG  . PHE   A 1 219 ? 24.325  5.813   36.230  1.00 17.61 ? 219 PHE   A CG  1 
ATOM   1708 C  CD1 . PHE   A 1 219 ? 23.314  4.933   36.582  1.00 17.35 ? 219 PHE   A CD1 1 
ATOM   1709 C  CD2 . PHE   A 1 219 ? 25.312  5.388   35.349  1.00 19.34 ? 219 PHE   A CD2 1 
ATOM   1710 C  CE1 . PHE   A 1 219 ? 23.297  3.641   36.087  1.00 19.90 ? 219 PHE   A CE1 1 
ATOM   1711 C  CE2 . PHE   A 1 219 ? 25.282  4.104   34.830  1.00 19.07 ? 219 PHE   A CE2 1 
ATOM   1712 C  CZ  . PHE   A 1 219 ? 24.273  3.238   35.205  1.00 19.68 ? 219 PHE   A CZ  1 
ATOM   1713 N  N   . LEU   A 1 220 ? 24.660  5.425   39.845  1.00 18.95 ? 220 LEU   A N   1 
ATOM   1714 C  CA  . LEU   A 1 220 ? 23.859  4.809   40.892  1.00 17.47 ? 220 LEU   A CA  1 
ATOM   1715 C  C   . LEU   A 1 220 ? 23.899  5.683   42.147  1.00 22.63 ? 220 LEU   A C   1 
ATOM   1716 O  O   . LEU   A 1 220 ? 24.869  6.379   42.417  1.00 20.33 ? 220 LEU   A O   1 
ATOM   1717 C  CB  . LEU   A 1 220 ? 24.367  3.405   41.197  1.00 18.85 ? 220 LEU   A CB  1 
ATOM   1718 C  CG  . LEU   A 1 220 ? 24.246  2.369   40.087  1.00 17.00 ? 220 LEU   A CG  1 
ATOM   1719 C  CD1 . LEU   A 1 220 ? 24.697  1.022   40.614  1.00 19.08 ? 220 LEU   A CD1 1 
ATOM   1720 C  CD2 . LEU   A 1 220 ? 22.818  2.273   39.517  1.00 17.35 ? 220 LEU   A CD2 1 
ATOM   1721 N  N   . ASN   A 1 221 ? 22.810  5.645   42.907  1.00 25.93 ? 221 ASN   A N   1 
ATOM   1722 C  CA  . ASN   A 1 221 ? 22.805  6.315   44.199  1.00 30.85 ? 221 ASN   A CA  1 
ATOM   1723 C  C   . ASN   A 1 221 ? 21.996  5.458   45.173  1.00 36.71 ? 221 ASN   A C   1 
ATOM   1724 O  O   . ASN   A 1 221 ? 21.751  4.281   44.912  1.00 33.30 ? 221 ASN   A O   1 
ATOM   1725 C  CB  . ASN   A 1 221 ? 22.300  7.744   44.038  1.00 28.18 ? 221 ASN   A CB  1 
ATOM   1726 C  CG  . ASN   A 1 221 ? 20.877  7.804   43.545  1.00 36.07 ? 221 ASN   A CG  1 
ATOM   1727 O  OD1 . ASN   A 1 221 ? 20.012  7.048   43.992  1.00 40.68 ? 221 ASN   A OD1 1 
ATOM   1728 N  ND2 . ASN   A 1 221 ? 20.621  8.684   42.596  1.00 40.62 ? 221 ASN   A ND2 1 
ATOM   1729 N  N   . ARG   A 1 222 ? 21.592  6.030   46.312  1.00 39.27 ? 222 ARG   A N   1 
ATOM   1730 C  CA  . ARG   A 1 222 ? 20.706  5.290   47.205  1.00 42.50 ? 222 ARG   A CA  1 
ATOM   1731 C  C   . ARG   A 1 222 ? 19.550  6.165   47.653  1.00 41.04 ? 222 ARG   A C   1 
ATOM   1732 O  O   . ARG   A 1 222 ? 18.937  5.941   48.688  1.00 41.21 ? 222 ARG   A O   1 
ATOM   1733 C  CB  . ARG   A 1 222 ? 21.484  4.754   48.397  1.00 41.84 ? 222 ARG   A CB  1 
ATOM   1734 C  CG  . ARG   A 1 222 ? 22.615  3.819   47.992  1.00 47.42 ? 222 ARG   A CG  1 
ATOM   1735 C  CD  . ARG   A 1 222 ? 23.700  3.884   49.032  1.00 42.42 ? 222 ARG   A CD  1 
ATOM   1736 N  NE  . ARG   A 1 222 ? 24.007  5.281   49.324  1.00 46.03 ? 222 ARG   A NE  1 
ATOM   1737 C  CZ  . ARG   A 1 222 ? 23.776  5.908   50.491  1.00 50.61 ? 222 ARG   A CZ  1 
ATOM   1738 N  NH1 . ARG   A 1 222 ? 23.080  5.320   51.452  1.00 48.36 ? 222 ARG   A NH1 1 
ATOM   1739 N  NH2 . ARG   A 1 222 ? 24.231  7.140   50.690  1.00 44.02 ? 222 ARG   A NH2 1 
ATOM   1740 N  N   . PHE   A 1 223 ? 19.231  7.169   46.850  1.00 39.04 ? 223 PHE   A N   1 
ATOM   1741 C  CA  . PHE   A 1 223 ? 17.912  7.732   46.976  1.00 42.30 ? 223 PHE   A CA  1 
ATOM   1742 C  C   . PHE   A 1 223 ? 16.941  6.574   46.738  1.00 41.42 ? 223 PHE   A C   1 
ATOM   1743 O  O   . PHE   A 1 223 ? 17.263  5.527   46.169  1.00 49.00 ? 223 PHE   A O   1 
ATOM   1744 C  CB  . PHE   A 1 223 ? 17.780  8.956   46.071  1.00 43.84 ? 223 PHE   A CB  1 
ATOM   1745 C  CG  . PHE   A 1 223 ? 18.768  10.061  46.373  1.00 54.29 ? 223 PHE   A CG  1 
ATOM   1746 C  CD1 . PHE   A 1 223 ? 18.896  10.580  47.657  1.00 54.74 ? 223 PHE   A CD1 1 
ATOM   1747 C  CD2 . PHE   A 1 223 ? 19.565  10.595  45.369  1.00 55.40 ? 223 PHE   A CD2 1 
ATOM   1748 C  CE1 . PHE   A 1 223 ? 19.807  11.591  47.925  1.00 54.93 ? 223 PHE   A CE1 1 
ATOM   1749 C  CE2 . PHE   A 1 223 ? 20.469  11.613  45.641  1.00 54.56 ? 223 PHE   A CE2 1 
ATOM   1750 C  CZ  . PHE   A 1 223 ? 20.589  12.108  46.917  1.00 53.43 ? 223 PHE   A CZ  1 
ATOM   1751 N  N   . THR   A 1 224 ? 15.751  6.729   47.271  1.00 44.19 ? 224 THR   A N   1 
ATOM   1752 C  CA  . THR   A 1 224 ? 14.730  5.732   47.070  1.00 39.24 ? 224 THR   A CA  1 
ATOM   1753 C  C   . THR   A 1 224 ? 13.551  6.519   46.535  1.00 34.55 ? 224 THR   A C   1 
ATOM   1754 O  O   . THR   A 1 224 ? 13.439  7.723   46.763  1.00 34.39 ? 224 THR   A O   1 
ATOM   1755 C  CB  . THR   A 1 224 ? 14.534  4.951   48.374  1.00 50.81 ? 224 THR   A CB  1 
ATOM   1756 O  OG1 . THR   A 1 224 ? 13.777  3.775   48.079  1.00 51.05 ? 224 THR   A OG1 1 
ATOM   1757 C  CG2 . THR   A 1 224 ? 13.893  5.796   49.458  1.00 49.04 ? 224 THR   A CG2 1 
ATOM   1758 N  N   . THR   A 1 225 ? 12.707  5.874   45.757  1.00 24.41 ? 225 THR   A N   1 
ATOM   1759 C  CA  . THR   A 1 225 ? 11.532  6.567   45.278  1.00 22.29 ? 225 THR   A CA  1 
ATOM   1760 C  C   . THR   A 1 225 ? 10.426  5.542   45.220  1.00 19.55 ? 225 THR   A C   1 
ATOM   1761 O  O   . THR   A 1 225 ? 10.699  4.345   45.146  1.00 23.56 ? 225 THR   A O   1 
ATOM   1762 C  CB  . THR   A 1 225 ? 11.778  7.216   43.901  1.00 20.95 ? 225 THR   A CB  1 
ATOM   1763 O  OG1 . THR   A 1 225 ? 10.623  7.946   43.492  1.00 22.00 ? 225 THR   A OG1 1 
ATOM   1764 C  CG2 . THR   A 1 225 ? 12.096  6.192   42.826  1.00 21.22 ? 225 THR   A CG2 1 
ATOM   1765 N  N   . THR   A 1 226 ? 9.205   6.050   45.205  1.00 18.33 ? 226 THR   A N   1 
ATOM   1766 C  CA  . THR   A 1 226 ? 8.025   5.286   44.912  1.00 17.49 ? 226 THR   A CA  1 
ATOM   1767 C  C   . THR   A 1 226 ? 7.820   5.390   43.406  1.00 18.01 ? 226 THR   A C   1 
ATOM   1768 O  O   . THR   A 1 226 ? 8.384   6.285   42.771  1.00 16.72 ? 226 THR   A O   1 
ATOM   1769 C  CB  . THR   A 1 226 ? 6.761   5.784   45.624  1.00 18.80 ? 226 THR   A CB  1 
ATOM   1770 O  OG1 . THR   A 1 226 ? 6.448   7.095   45.148  1.00 18.69 ? 226 THR   A OG1 1 
ATOM   1771 C  CG2 . THR   A 1 226 ? 6.874   5.798   47.141  1.00 21.95 ? 226 THR   A CG2 1 
ATOM   1772 N  N   . LEU   A 1 227 ? 7.065   4.439   42.872  1.00 15.54 ? 227 LEU   A N   1 
ATOM   1773 C  CA  . LEU   A 1 227 ? 6.727   4.460   41.463  1.00 16.98 ? 227 LEU   A CA  1 
ATOM   1774 C  C   . LEU   A 1 227 ? 5.987   5.769   41.156  1.00 17.01 ? 227 LEU   A C   1 
ATOM   1775 O  O   . LEU   A 1 227 ? 6.267   6.462   40.158  1.00 16.00 ? 227 LEU   A O   1 
ATOM   1776 C  CB  . LEU   A 1 227 ? 5.856   3.242   41.142  1.00 16.21 ? 227 LEU   A CB  1 
ATOM   1777 C  CG  . LEU   A 1 227 ? 5.453   3.071   39.681  1.00 17.53 ? 227 LEU   A CG  1 
ATOM   1778 C  CD1 . LEU   A 1 227 ? 6.675   2.945   38.794  1.00 16.98 ? 227 LEU   A CD1 1 
ATOM   1779 C  CD2 . LEU   A 1 227 ? 4.549   1.869   39.470  1.00 18.96 ? 227 LEU   A CD2 1 
ATOM   1780 N  N   . ASN   A 1 228 ? 5.024   6.126   42.022  1.00 15.03 ? 228 ASN   A N   1 
ATOM   1781 C  CA  . ASN   A 1 228 ? 4.226   7.307   41.780  1.00 17.34 ? 228 ASN   A CA  1 
ATOM   1782 C  C   . ASN   A 1 228 ? 5.101   8.556   41.746  1.00 15.47 ? 228 ASN   A C   1 
ATOM   1783 O  O   . ASN   A 1 228 ? 4.902   9.397   40.868  1.00 17.50 ? 228 ASN   A O   1 
ATOM   1784 C  CB  . ASN   A 1 228 ? 3.098   7.515   42.793  1.00 20.03 ? 228 ASN   A CB  1 
ATOM   1785 C  CG  . ASN   A 1 228 ? 2.305   8.747   42.395  1.00 24.38 ? 228 ASN   A CG  1 
ATOM   1786 O  OD1 . ASN   A 1 228 ? 1.587   8.743   41.403  1.00 25.84 ? 228 ASN   A OD1 1 
ATOM   1787 N  ND2 . ASN   A 1 228 ? 2.520   9.853   43.086  1.00 26.87 ? 228 ASN   A ND2 1 
ATOM   1788 N  N   . ASP   A 1 229 ? 6.009   8.721   42.706  1.00 17.40 ? 229 ASP   A N   1 
ATOM   1789 C  CA  . ASP   A 1 229 ? 6.862   9.906   42.741  1.00 17.39 ? 229 ASP   A CA  1 
ATOM   1790 C  C   . ASP   A 1 229 ? 7.860   9.931   41.578  1.00 17.64 ? 229 ASP   A C   1 
ATOM   1791 O  O   . ASP   A 1 229 ? 8.160   10.982  41.013  1.00 17.59 ? 229 ASP   A O   1 
ATOM   1792 C  CB  . ASP   A 1 229 ? 7.564   10.054  44.075  1.00 18.38 ? 229 ASP   A CB  1 
ATOM   1793 C  CG  . ASP   A 1 229 ? 6.559   10.360  45.195  1.00 22.44 ? 229 ASP   A CG  1 
ATOM   1794 O  OD1 . ASP   A 1 229 ? 5.440   10.812  44.889  1.00 22.06 ? 229 ASP   A OD1 1 
ATOM   1795 O  OD2 . ASP   A 1 229 ? 6.901   10.100  46.333  1.00 26.08 ? 229 ASP   A OD2 1 
ATOM   1796 N  N   . PHE   A 1 230 ? 8.300   8.761   41.138  1.00 14.96 ? 230 PHE   A N   1 
ATOM   1797 C  CA  . PHE   A 1 230 ? 9.141   8.738   39.949  1.00 14.11 ? 230 PHE   A CA  1 
ATOM   1798 C  C   . PHE   A 1 230 ? 8.328   9.235   38.759  1.00 14.02 ? 230 PHE   A C   1 
ATOM   1799 O  O   . PHE   A 1 230 ? 8.817   10.054  37.967  1.00 15.31 ? 230 PHE   A O   1 
ATOM   1800 C  CB  . PHE   A 1 230 ? 9.677   7.326   39.710  1.00 14.69 ? 230 PHE   A CB  1 
ATOM   1801 C  CG  . PHE   A 1 230 ? 10.357  7.199   38.372  1.00 14.54 ? 230 PHE   A CG  1 
ATOM   1802 C  CD1 . PHE   A 1 230 ? 11.611  7.726   38.171  1.00 15.76 ? 230 PHE   A CD1 1 
ATOM   1803 C  CD2 . PHE   A 1 230 ? 9.695   6.608   37.309  1.00 14.82 ? 230 PHE   A CD2 1 
ATOM   1804 C  CE1 . PHE   A 1 230 ? 12.212  7.680   36.919  1.00 16.16 ? 230 PHE   A CE1 1 
ATOM   1805 C  CE2 . PHE   A 1 230 ? 10.300  6.534   36.064  1.00 15.83 ? 230 PHE   A CE2 1 
ATOM   1806 C  CZ  . PHE   A 1 230 ? 11.561  7.064   35.876  1.00 15.94 ? 230 PHE   A CZ  1 
ATOM   1807 N  N   . ASN   A 1 231 ? 7.104   8.720   38.604  1.00 12.66 ? 231 ASN   A N   1 
ATOM   1808 C  CA  . ASN   A 1 231 ? 6.255   9.052   37.480  1.00 14.85 ? 231 ASN   A CA  1 
ATOM   1809 C  C   . ASN   A 1 231 ? 5.929   10.547  37.437  1.00 14.01 ? 231 ASN   A C   1 
ATOM   1810 O  O   . ASN   A 1 231 ? 5.799   11.100  36.341  1.00 16.35 ? 231 ASN   A O   1 
ATOM   1811 C  CB  . ASN   A 1 231 ? 4.992   8.219   37.402  1.00 15.15 ? 231 ASN   A CB  1 
ATOM   1812 C  CG  . ASN   A 1 231 ? 5.297   6.872   36.746  1.00 18.92 ? 231 ASN   A CG  1 
ATOM   1813 O  OD1 . ASN   A 1 231 ? 6.073   6.812   35.813  1.00 22.16 ? 231 ASN   A OD1 1 
ATOM   1814 N  ND2 . ASN   A 1 231 ? 4.715   5.806   37.229  1.00 19.18 ? 231 ASN   A ND2 1 
ATOM   1815 N  N   . LEU   A 1 232 ? 5.811   11.195  38.610  1.00 14.33 ? 232 LEU   A N   1 
ATOM   1816 C  CA  . LEU   A 1 232 ? 5.560   12.635  38.587  1.00 14.49 ? 232 LEU   A CA  1 
ATOM   1817 C  C   . LEU   A 1 232 ? 6.747   13.346  37.938  1.00 13.50 ? 232 LEU   A C   1 
ATOM   1818 O  O   . LEU   A 1 232 ? 6.536   14.291  37.173  1.00 16.33 ? 232 LEU   A O   1 
ATOM   1819 C  CB  . LEU   A 1 232 ? 5.340   13.178  40.010  1.00 14.70 ? 232 LEU   A CB  1 
ATOM   1820 C  CG  . LEU   A 1 232 ? 4.046   12.773  40.703  1.00 15.09 ? 232 LEU   A CG  1 
ATOM   1821 C  CD1 . LEU   A 1 232 ? 4.080   13.188  42.171  1.00 15.99 ? 232 LEU   A CD1 1 
ATOM   1822 C  CD2 . LEU   A 1 232 ? 2.828   13.361  40.038  1.00 18.21 ? 232 LEU   A CD2 1 
ATOM   1823 N  N   . VAL   A 1 233 ? 7.967   12.985  38.335  1.00 13.85 ? 233 VAL   A N   1 
ATOM   1824 C  CA  . VAL   A 1 233 ? 9.158   13.638  37.785  1.00 16.48 ? 233 VAL   A CA  1 
ATOM   1825 C  C   . VAL   A 1 233 ? 9.303   13.281  36.302  1.00 18.98 ? 233 VAL   A C   1 
ATOM   1826 O  O   . VAL   A 1 233 ? 9.551   14.149  35.441  1.00 16.12 ? 233 VAL   A O   1 
ATOM   1827 C  CB  . VAL   A 1 233 ? 10.417  13.323  38.602  1.00 17.75 ? 233 VAL   A CB  1 
ATOM   1828 C  CG1 . VAL   A 1 233 ? 11.703  13.855  37.954  1.00 20.67 ? 233 VAL   A CG1 1 
ATOM   1829 C  CG2 . VAL   A 1 233 ? 10.290  13.836  40.028  1.00 20.30 ? 233 VAL   A CG2 1 
ATOM   1830 N  N   . ALA   A 1 234 ? 9.083   12.000  35.966  1.00 17.60 ? 234 ALA   A N   1 
ATOM   1831 C  CA  . ALA   A 1 234 ? 9.147   11.599  34.558  1.00 20.91 ? 234 ALA   A CA  1 
ATOM   1832 C  C   . ALA   A 1 234 ? 8.252   12.463  33.670  1.00 19.92 ? 234 ALA   A C   1 
ATOM   1833 O  O   . ALA   A 1 234 ? 8.690   12.965  32.621  1.00 21.25 ? 234 ALA   A O   1 
ATOM   1834 C  CB  . ALA   A 1 234 ? 8.775   10.146  34.422  1.00 23.54 ? 234 ALA   A CB  1 
ATOM   1835 N  N   . MET   A 1 235 ? 6.996   12.621  34.092  1.00 19.40 ? 235 MET   A N   1 
ATOM   1836 C  CA  . MET   A 1 235 ? 5.987   13.356  33.370  1.00 21.87 ? 235 MET   A CA  1 
ATOM   1837 C  C   . MET   A 1 235 ? 6.482   14.785  33.145  1.00 20.23 ? 235 MET   A C   1 
ATOM   1838 O  O   . MET   A 1 235 ? 6.334   15.312  32.046  1.00 19.65 ? 235 MET   A O   1 
ATOM   1839 C  CB  . MET   A 1 235 ? 4.670   13.384  34.140  1.00 25.06 ? 235 MET   A CB  1 
ATOM   1840 C  CG  . MET   A 1 235 ? 3.761   12.167  33.909  1.00 36.11 ? 235 MET   A CG  1 
ATOM   1841 S  SD  . MET   A 1 235 ? 2.265   12.275  34.976  1.00 45.77 ? 235 MET   A SD  1 
ATOM   1842 C  CE  . MET   A 1 235 ? 1.145   13.034  33.803  1.00 43.49 ? 235 MET   A CE  1 
ATOM   1843 N  N   . LYS   A 1 236 ? 7.092   15.360  34.180  1.00 19.38 ? 236 LYS   A N   1 
ATOM   1844 C  CA  . LYS   A 1 236 ? 7.589   16.734  34.146  1.00 18.84 ? 236 LYS   A CA  1 
ATOM   1845 C  C   . LYS   A 1 236 ? 8.647   16.899  33.062  1.00 20.27 ? 236 LYS   A C   1 
ATOM   1846 O  O   . LYS   A 1 236 ? 8.696   17.937  32.411  1.00 21.95 ? 236 LYS   A O   1 
ATOM   1847 C  CB  . LYS   A 1 236 ? 8.193   17.118  35.493  1.00 20.27 ? 236 LYS   A CB  1 
ATOM   1848 C  CG  . LYS   A 1 236 ? 8.566   18.591  35.633  1.00 20.54 ? 236 LYS   A CG  1 
ATOM   1849 C  CD  . LYS   A 1 236 ? 9.178   18.912  36.992  1.00 22.72 ? 236 LYS   A CD  1 
ATOM   1850 C  CE  . LYS   A 1 236 ? 9.670   20.339  37.135  1.00 24.55 ? 236 LYS   A CE  1 
ATOM   1851 N  NZ  . LYS   A 1 236 ? 10.664  20.410  38.234  1.00 26.35 ? 236 LYS   A NZ  1 
ATOM   1852 N  N   . TYR   A 1 237 ? 9.457   15.857  32.813  1.00 22.18 ? 237 TYR   A N   1 
ATOM   1853 C  CA  . TYR   A 1 237 ? 10.544  15.897  31.833  1.00 19.41 ? 237 TYR   A CA  1 
ATOM   1854 C  C   . TYR   A 1 237 ? 10.204  15.263  30.479  1.00 18.98 ? 237 TYR   A C   1 
ATOM   1855 O  O   . TYR   A 1 237 ? 11.130  14.925  29.720  1.00 17.40 ? 237 TYR   A O   1 
ATOM   1856 C  CB  . TYR   A 1 237 ? 11.716  15.181  32.492  1.00 20.00 ? 237 TYR   A CB  1 
ATOM   1857 C  CG  . TYR   A 1 237 ? 12.470  16.006  33.519  1.00 23.00 ? 237 TYR   A CG  1 
ATOM   1858 C  CD1 . TYR   A 1 237 ? 13.469  16.897  33.116  1.00 26.65 ? 237 TYR   A CD1 1 
ATOM   1859 C  CD2 . TYR   A 1 237 ? 12.134  15.959  34.868  1.00 22.67 ? 237 TYR   A CD2 1 
ATOM   1860 C  CE1 . TYR   A 1 237 ? 14.140  17.693  34.037  1.00 25.74 ? 237 TYR   A CE1 1 
ATOM   1861 C  CE2 . TYR   A 1 237 ? 12.802  16.751  35.792  1.00 27.59 ? 237 TYR   A CE2 1 
ATOM   1862 C  CZ  . TYR   A 1 237 ? 13.806  17.614  35.371  1.00 27.03 ? 237 TYR   A CZ  1 
ATOM   1863 O  OH  . TYR   A 1 237 ? 14.479  18.384  36.283  1.00 26.27 ? 237 TYR   A OH  1 
ATOM   1864 N  N   . ASN   A 1 238 ? 8.916   15.064  30.181  1.00 18.06 ? 238 ASN   A N   1 
ATOM   1865 C  CA  . ASN   A 1 238 ? 8.453   14.526  28.898  1.00 19.46 ? 238 ASN   A CA  1 
ATOM   1866 C  C   . ASN   A 1 238 ? 8.984   13.109  28.688  1.00 17.29 ? 238 ASN   A C   1 
ATOM   1867 O  O   . ASN   A 1 238 ? 9.407   12.747  27.595  1.00 20.62 ? 238 ASN   A O   1 
ATOM   1868 C  CB  . ASN   A 1 238 ? 8.767   15.475  27.742  1.00 21.93 ? 238 ASN   A CB  1 
ATOM   1869 C  CG  . ASN   A 1 238 ? 7.787   16.622  27.780  1.00 26.43 ? 238 ASN   A CG  1 
ATOM   1870 O  OD1 . ASN   A 1 238 ? 6.602   16.450  27.500  1.00 32.99 ? 238 ASN   A OD1 1 
ATOM   1871 N  ND2 . ASN   A 1 238 ? 8.254   17.760  28.240  1.00 31.73 ? 238 ASN   A ND2 1 
ATOM   1872 N  N   . TYR   A 1 239 ? 8.913   12.330  29.772  1.00 16.10 ? 239 TYR   A N   1 
ATOM   1873 C  CA  . TYR   A 1 239 ? 9.208   10.916  29.790  1.00 15.38 ? 239 TYR   A CA  1 
ATOM   1874 C  C   . TYR   A 1 239 ? 7.894   10.176  29.921  1.00 17.09 ? 239 TYR   A C   1 
ATOM   1875 O  O   . TYR   A 1 239 ? 7.003   10.613  30.663  1.00 17.72 ? 239 TYR   A O   1 
ATOM   1876 C  CB  . TYR   A 1 239 ? 10.114  10.479  30.943  1.00 14.90 ? 239 TYR   A CB  1 
ATOM   1877 C  CG  . TYR   A 1 239 ? 11.596  10.560  30.656  1.00 14.52 ? 239 TYR   A CG  1 
ATOM   1878 C  CD1 . TYR   A 1 239 ? 12.194  11.721  30.192  1.00 14.97 ? 239 TYR   A CD1 1 
ATOM   1879 C  CD2 . TYR   A 1 239 ? 12.386  9.427   30.814  1.00 15.10 ? 239 TYR   A CD2 1 
ATOM   1880 C  CE1 . TYR   A 1 239 ? 13.538  11.743  29.878  1.00 17.35 ? 239 TYR   A CE1 1 
ATOM   1881 C  CE2 . TYR   A 1 239 ? 13.733  9.434   30.501  1.00 15.70 ? 239 TYR   A CE2 1 
ATOM   1882 C  CZ  . TYR   A 1 239 ? 14.301  10.591  30.026  1.00 17.93 ? 239 TYR   A CZ  1 
ATOM   1883 O  OH  . TYR   A 1 239 ? 15.645  10.563  29.816  1.00 19.59 ? 239 TYR   A OH  1 
ATOM   1884 N  N   . GLU   A 1 240 ? 7.781   9.050   29.202  1.00 15.49 ? 240 GLU   A N   1 
ATOM   1885 C  CA  . GLU   A 1 240 ? 6.593   8.223   29.277  1.00 16.22 ? 240 GLU   A CA  1 
ATOM   1886 C  C   . GLU   A 1 240 ? 6.413   7.659   30.685  1.00 16.68 ? 240 GLU   A C   1 
ATOM   1887 O  O   . GLU   A 1 240 ? 7.362   7.402   31.429  1.00 15.04 ? 240 GLU   A O   1 
ATOM   1888 C  CB  . GLU   A 1 240 ? 6.660   7.046   28.289  1.00 18.69 ? 240 GLU   A CB  1 
ATOM   1889 C  CG  . GLU   A 1 240 ? 6.516   7.488   26.855  1.00 21.96 ? 240 GLU   A CG  1 
ATOM   1890 C  CD  . GLU   A 1 240 ? 5.111   7.977   26.514  1.00 28.47 ? 240 GLU   A CD  1 
ATOM   1891 O  OE1 . GLU   A 1 240 ? 4.183   7.149   26.544  1.00 33.98 ? 240 GLU   A OE1 1 
ATOM   1892 O  OE2 . GLU   A 1 240 ? 4.941   9.167   26.211  1.00 25.25 ? 240 GLU   A OE2 1 
ATOM   1893 N  N   . PRO   A 1 241 ? 5.149   7.415   31.077  1.00 22.52 ? 241 PRO   A N   1 
ATOM   1894 C  CA  . PRO   A 1 241 ? 4.879   6.732   32.331  1.00 23.09 ? 241 PRO   A CA  1 
ATOM   1895 C  C   . PRO   A 1 241 ? 5.551   5.367   32.384  1.00 16.83 ? 241 PRO   A C   1 
ATOM   1896 O  O   . PRO   A 1 241 ? 5.651   4.689   31.341  1.00 17.99 ? 241 PRO   A O   1 
ATOM   1897 C  CB  . PRO   A 1 241 ? 3.366   6.465   32.279  1.00 26.69 ? 241 PRO   A CB  1 
ATOM   1898 C  CG  . PRO   A 1 241 ? 2.824   7.486   31.319  1.00 28.18 ? 241 PRO   A CG  1 
ATOM   1899 C  CD  . PRO   A 1 241 ? 3.928   7.696   30.304  1.00 24.75 ? 241 PRO   A CD  1 
ATOM   1900 N  N   . LEU   A 1 242 ? 6.004   5.007   33.591  1.00 16.28 ? 242 LEU   A N   1 
ATOM   1901 C  CA  . LEU   A 1 242 ? 6.453   3.640   33.882  1.00 15.33 ? 242 LEU   A CA  1 
ATOM   1902 C  C   . LEU   A 1 242 ? 5.333   2.915   34.596  1.00 17.14 ? 242 LEU   A C   1 
ATOM   1903 O  O   . LEU   A 1 242 ? 4.940   3.344   35.669  1.00 16.40 ? 242 LEU   A O   1 
ATOM   1904 C  CB  . LEU   A 1 242 ? 7.703   3.693   34.761  1.00 15.20 ? 242 LEU   A CB  1 
ATOM   1905 C  CG  . LEU   A 1 242 ? 8.469   2.388   34.887  1.00 16.10 ? 242 LEU   A CG  1 
ATOM   1906 C  CD1 . LEU   A 1 242 ? 9.144   2.058   33.556  1.00 15.86 ? 242 LEU   A CD1 1 
ATOM   1907 C  CD2 . LEU   A 1 242 ? 9.474   2.454   36.014  1.00 16.79 ? 242 LEU   A CD2 1 
ATOM   1908 N  N   . THR   A 1 243 ? 4.885   1.796   34.024  1.00 18.33 ? 243 THR   A N   1 
ATOM   1909 C  CA  . THR   A 1 243 ? 3.818   1.000   34.602  1.00 20.00 ? 243 THR   A CA  1 
ATOM   1910 C  C   . THR   A 1 243 ? 4.333   -0.125  35.507  1.00 19.87 ? 243 THR   A C   1 
ATOM   1911 O  O   . THR   A 1 243 ? 5.492   -0.508  35.488  1.00 18.44 ? 243 THR   A O   1 
ATOM   1912 C  CB  . THR   A 1 243 ? 2.970   0.412   33.476  1.00 21.83 ? 243 THR   A CB  1 
ATOM   1913 O  OG1 . THR   A 1 243 ? 3.739   -0.579  32.784  1.00 21.79 ? 243 THR   A OG1 1 
ATOM   1914 C  CG2 . THR   A 1 243 ? 2.495   1.475   32.514  1.00 22.07 ? 243 THR   A CG2 1 
ATOM   1915 N  N   . GLN   A 1 244 ? 3.431   -0.775  36.241  1.00 19.11 ? 244 GLN   A N   1 
ATOM   1916 C  CA  . GLN   A 1 244 ? 3.838   -1.924  37.031  1.00 22.46 ? 244 GLN   A CA  1 
ATOM   1917 C  C   . GLN   A 1 244 ? 4.277   -3.067  36.108  1.00 20.01 ? 244 GLN   A C   1 
ATOM   1918 O  O   . GLN   A 1 244 ? 5.192   -3.803  36.446  1.00 20.76 ? 244 GLN   A O   1 
ATOM   1919 C  CB  . GLN   A 1 244 ? 2.729   -2.390  37.986  1.00 24.82 ? 244 GLN   A CB  1 
ATOM   1920 C  CG  . GLN   A 1 244 ? 3.180   -3.546  38.890  1.00 25.48 ? 244 GLN   A CG  1 
ATOM   1921 C  CD  . GLN   A 1 244 ? 4.379   -3.260  39.763  1.00 26.53 ? 244 GLN   A CD  1 
ATOM   1922 O  OE1 . GLN   A 1 244 ? 4.518   -2.183  40.343  1.00 30.60 ? 244 GLN   A OE1 1 
ATOM   1923 N  NE2 . GLN   A 1 244 ? 5.297   -4.218  39.853  1.00 27.34 ? 244 GLN   A NE2 1 
ATOM   1924 N  N   . ASP   A 1 245 ? 3.670   -3.189  34.930  1.00 23.30 ? 245 ASP   A N   1 
ATOM   1925 C  CA  . ASP   A 1 245 ? 4.090   -4.217  33.982  1.00 23.61 ? 245 ASP   A CA  1 
ATOM   1926 C  C   . ASP   A 1 245 ? 5.528   -3.944  33.553  1.00 21.49 ? 245 ASP   A C   1 
ATOM   1927 O  O   . ASP   A 1 245 ? 6.316   -4.868  33.407  1.00 21.44 ? 245 ASP   A O   1 
ATOM   1928 C  CB  . ASP   A 1 245 ? 3.184   -4.284  32.753  1.00 28.54 ? 245 ASP   A CB  1 
ATOM   1929 C  CG  . ASP   A 1 245 ? 3.488   -5.488  31.858  1.00 42.41 ? 245 ASP   A CG  1 
ATOM   1930 O  OD1 . ASP   A 1 245 ? 3.732   -6.608  32.411  1.00 51.20 ? 245 ASP   A OD1 1 
ATOM   1931 O  OD2 . ASP   A 1 245 ? 3.508   -5.311  30.616  1.00 49.98 ? 245 ASP   A OD2 1 
ATOM   1932 N  N   . HIS   A 1 246 ? 5.872   -2.664  33.326  1.00 17.63 ? 246 HIS   A N   1 
ATOM   1933 C  CA  . HIS   A 1 246 ? 7.238   -2.305  32.985  1.00 16.87 ? 246 HIS   A CA  1 
ATOM   1934 C  C   . HIS   A 1 246 ? 8.173   -2.738  34.104  1.00 16.36 ? 246 HIS   A C   1 
ATOM   1935 O  O   . HIS   A 1 246 ? 9.275   -3.250  33.869  1.00 17.39 ? 246 HIS   A O   1 
ATOM   1936 C  CB  . HIS   A 1 246 ? 7.416   -0.800  32.716  1.00 15.27 ? 246 HIS   A CB  1 
ATOM   1937 C  CG  . HIS   A 1 246 ? 6.757   -0.288  31.479  1.00 16.17 ? 246 HIS   A CG  1 
ATOM   1938 N  ND1 . HIS   A 1 246 ? 6.230   0.985   31.387  1.00 17.63 ? 246 HIS   A ND1 1 
ATOM   1939 C  CD2 . HIS   A 1 246 ? 6.609   -0.837  30.246  1.00 16.73 ? 246 HIS   A CD2 1 
ATOM   1940 C  CE1 . HIS   A 1 246 ? 5.732   1.167   30.174  1.00 18.72 ? 246 HIS   A CE1 1 
ATOM   1941 N  NE2 . HIS   A 1 246 ? 5.942   0.059   29.454  1.00 19.34 ? 246 HIS   A NE2 1 
ATOM   1942 N  N   . VAL   A 1 247 ? 7.783   -2.447  35.350  1.00 16.65 ? 247 VAL   A N   1 
ATOM   1943 C  CA  . VAL   A 1 247 ? 8.589   -2.859  36.478  1.00 16.15 ? 247 VAL   A CA  1 
ATOM   1944 C  C   . VAL   A 1 247 ? 8.817   -4.379  36.457  1.00 18.47 ? 247 VAL   A C   1 
ATOM   1945 O  O   . VAL   A 1 247 ? 9.942   -4.852  36.708  1.00 19.46 ? 247 VAL   A O   1 
ATOM   1946 C  CB  . VAL   A 1 247 ? 7.946   -2.374  37.790  1.00 17.16 ? 247 VAL   A CB  1 
ATOM   1947 C  CG1 . VAL   A 1 247 ? 8.679   -2.904  39.002  1.00 18.92 ? 247 VAL   A CG1 1 
ATOM   1948 C  CG2 . VAL   A 1 247 ? 7.865   -0.849  37.859  1.00 17.55 ? 247 VAL   A CG2 1 
ATOM   1949 N  N   . ASP   A 1 248 ? 7.751   -5.118  36.129  1.00 19.32 ? 248 ASP   A N   1 
ATOM   1950 C  CA  . ASP   A 1 248 ? 7.785   -6.576  36.062  1.00 22.14 ? 248 ASP   A CA  1 
ATOM   1951 C  C   . ASP   A 1 248 ? 8.764   -7.035  34.988  1.00 22.65 ? 248 ASP   A C   1 
ATOM   1952 O  O   . ASP   A 1 248 ? 9.570   -7.923  35.220  1.00 22.31 ? 248 ASP   A O   1 
ATOM   1953 C  CB  . ASP   A 1 248 ? 6.405   -7.184  35.810  1.00 26.27 ? 248 ASP   A CB  1 
ATOM   1954 C  CG  . ASP   A 1 248 ? 5.436   -7.012  36.967  1.00 30.36 ? 248 ASP   A CG  1 
ATOM   1955 O  OD1 . ASP   A 1 248 ? 5.900   -6.726  38.083  1.00 33.74 ? 248 ASP   A OD1 1 
ATOM   1956 O  OD2 . ASP   A 1 248 ? 4.223   -7.157  36.745  1.00 35.52 ? 248 ASP   A OD2 1 
ATOM   1957 N  N   . ILE   A 1 249 ? 8.704   -6.409  33.823  1.00 22.04 ? 249 ILE   A N   1 
ATOM   1958 C  CA  . ILE   A 1 249 ? 9.567   -6.769  32.713  1.00 25.43 ? 249 ILE   A CA  1 
ATOM   1959 C  C   . ILE   A 1 249 ? 11.031  -6.483  33.036  1.00 24.68 ? 249 ILE   A C   1 
ATOM   1960 O  O   . ILE   A 1 249 ? 11.904  -7.117  32.459  1.00 24.04 ? 249 ILE   A O   1 
ATOM   1961 C  CB  . ILE   A 1 249 ? 9.084   -6.053  31.443  1.00 26.88 ? 249 ILE   A CB  1 
ATOM   1962 C  CG1 . ILE   A 1 249 ? 7.744   -6.625  30.986  1.00 29.47 ? 249 ILE   A CG1 1 
ATOM   1963 C  CG2 . ILE   A 1 249 ? 10.128  -6.111  30.357  1.00 31.50 ? 249 ILE   A CG2 1 
ATOM   1964 C  CD1 . ILE   A 1 249 ? 6.917   -5.663  30.155  1.00 33.23 ? 249 ILE   A CD1 1 
ATOM   1965 N  N   . LEU   A 1 250 ? 11.321  -5.507  33.909  1.00 18.87 ? 250 LEU   A N   1 
ATOM   1966 C  CA  . LEU   A 1 250 ? 12.697  -5.213  34.274  1.00 18.32 ? 250 LEU   A CA  1 
ATOM   1967 C  C   . LEU   A 1 250 ? 13.189  -6.157  35.372  1.00 19.18 ? 250 LEU   A C   1 
ATOM   1968 O  O   . LEU   A 1 250 ? 14.362  -6.099  35.724  1.00 21.82 ? 250 LEU   A O   1 
ATOM   1969 C  CB  . LEU   A 1 250 ? 12.831  -3.752  34.703  1.00 17.85 ? 250 LEU   A CB  1 
ATOM   1970 C  CG  . LEU   A 1 250 ? 12.694  -2.726  33.581  1.00 15.75 ? 250 LEU   A CG  1 
ATOM   1971 C  CD1 . LEU   A 1 250 ? 12.365  -1.355  34.149  1.00 16.77 ? 250 LEU   A CD1 1 
ATOM   1972 C  CD2 . LEU   A 1 250 ? 14.004  -2.652  32.799  1.00 15.13 ? 250 LEU   A CD2 1 
ATOM   1973 N  N   . GLY   A 1 251 ? 12.312  -7.035  35.876  1.00 22.60 ? 251 GLY   A N   1 
ATOM   1974 C  CA  . GLY   A 1 251 ? 12.672  -7.894  37.000  1.00 24.19 ? 251 GLY   A CA  1 
ATOM   1975 C  C   . GLY   A 1 251 ? 13.942  -8.706  36.747  1.00 24.28 ? 251 GLY   A C   1 
ATOM   1976 O  O   . GLY   A 1 251 ? 14.878  -8.719  37.546  1.00 26.09 ? 251 GLY   A O   1 
ATOM   1977 N  N   . PRO   A 1 252 ? 14.047  -9.447  35.623  1.00 27.36 ? 252 PRO   A N   1 
ATOM   1978 C  CA  . PRO   A 1 252 ? 15.255  -10.235 35.370  1.00 26.74 ? 252 PRO   A CA  1 
ATOM   1979 C  C   . PRO   A 1 252 ? 16.543  -9.419  35.406  1.00 23.84 ? 252 PRO   A C   1 
ATOM   1980 O  O   . PRO   A 1 252 ? 17.573  -9.904  35.879  1.00 23.70 ? 252 PRO   A O   1 
ATOM   1981 C  CB  . PRO   A 1 252 ? 14.978  -10.837 33.982  1.00 29.44 ? 252 PRO   A CB  1 
ATOM   1982 C  CG  . PRO   A 1 252 ? 13.477  -10.943 33.941  1.00 32.93 ? 252 PRO   A CG  1 
ATOM   1983 C  CD  . PRO   A 1 252 ? 13.004  -9.668  34.615  1.00 28.32 ? 252 PRO   A CD  1 
ATOM   1984 N  N   . LEU   A 1 253 ? 16.519  -8.163  34.914  1.00 20.80 ? 253 LEU   A N   1 
ATOM   1985 C  CA  . LEU   A 1 253 ? 17.719  -7.333  34.946  1.00 19.51 ? 253 LEU   A CA  1 
ATOM   1986 C  C   . LEU   A 1 253 ? 18.017  -6.866  36.369  1.00 20.11 ? 253 LEU   A C   1 
ATOM   1987 O  O   . LEU   A 1 253 ? 19.177  -6.715  36.751  1.00 19.84 ? 253 LEU   A O   1 
ATOM   1988 C  CB  . LEU   A 1 253 ? 17.566  -6.110  34.031  1.00 20.38 ? 253 LEU   A CB  1 
ATOM   1989 C  CG  . LEU   A 1 253 ? 17.570  -6.392  32.528  1.00 20.70 ? 253 LEU   A CG  1 
ATOM   1990 C  CD1 . LEU   A 1 253 ? 17.253  -5.135  31.728  1.00 20.82 ? 253 LEU   A CD1 1 
ATOM   1991 C  CD2 . LEU   A 1 253 ? 18.918  -6.965  32.093  1.00 20.15 ? 253 LEU   A CD2 1 
ATOM   1992 N  N   A SER   A 1 254 ? 16.962  -6.567  37.118  0.75 21.50 ? 254 SER   A N   1 
ATOM   1993 N  N   B SER   A 1 254 ? 16.953  -6.603  37.136  0.25 22.48 ? 254 SER   A N   1 
ATOM   1994 C  CA  A SER   A 1 254 ? 17.123  -6.191  38.516  0.75 21.27 ? 254 SER   A CA  1 
ATOM   1995 C  CA  B SER   A 1 254 ? 17.094  -6.194  38.526  0.25 23.91 ? 254 SER   A CA  1 
ATOM   1996 C  C   A SER   A 1 254 ? 17.792  -7.330  39.293  0.75 25.23 ? 254 SER   A C   1 
ATOM   1997 C  C   B SER   A 1 254 ? 17.740  -7.316  39.338  0.25 26.03 ? 254 SER   A C   1 
ATOM   1998 O  O   A SER   A 1 254 ? 18.753  -7.106  40.020  0.75 25.23 ? 254 SER   A O   1 
ATOM   1999 O  O   B SER   A 1 254 ? 18.635  -7.068  40.142  0.25 26.00 ? 254 SER   A O   1 
ATOM   2000 C  CB  A SER   A 1 254 ? 15.784  -5.820  39.101  0.75 22.13 ? 254 SER   A CB  1 
ATOM   2001 C  CB  B SER   A 1 254 ? 15.762  -5.766  39.110  0.25 24.94 ? 254 SER   A CB  1 
ATOM   2002 O  OG  A SER   A 1 254 ? 15.881  -5.529  40.489  0.75 20.41 ? 254 SER   A OG  1 
ATOM   2003 O  OG  B SER   A 1 254 ? 14.836  -6.844  39.176  0.25 25.64 ? 254 SER   A OG  1 
ATOM   2004 N  N   . ALA   A 1 255 ? 17.286  -8.551  39.101  1.00 26.80 ? 255 ALA   A N   1 
ATOM   2005 C  CA  . ALA   A 1 255 ? 17.807  -9.729  39.796  1.00 33.33 ? 255 ALA   A CA  1 
ATOM   2006 C  C   . ALA   A 1 255 ? 19.282  -9.965  39.471  1.00 34.20 ? 255 ALA   A C   1 
ATOM   2007 O  O   . ALA   A 1 255 ? 20.098  -10.151 40.372  1.00 35.82 ? 255 ALA   A O   1 
ATOM   2008 C  CB  . ALA   A 1 255 ? 16.964  -10.926 39.443  1.00 34.48 ? 255 ALA   A CB  1 
ATOM   2009 N  N   . GLN   A 1 256 ? 19.643  -9.867  38.190  1.00 33.76 ? 256 GLN   A N   1 
ATOM   2010 C  CA  . GLN   A 1 256 ? 21.015  -10.043 37.748  1.00 32.92 ? 256 GLN   A CA  1 
ATOM   2011 C  C   . GLN   A 1 256 ? 21.947  -9.067  38.461  1.00 34.82 ? 256 GLN   A C   1 
ATOM   2012 O  O   . GLN   A 1 256 ? 22.979  -9.468  38.977  1.00 34.79 ? 256 GLN   A O   1 
ATOM   2013 C  CB  . GLN   A 1 256 ? 21.075  -9.904  36.224  1.00 35.75 ? 256 GLN   A CB  1 
ATOM   2014 C  CG  . GLN   A 1 256 ? 22.479  -9.950  35.638  1.00 40.78 ? 256 GLN   A CG  1 
ATOM   2015 C  CD  . GLN   A 1 256 ? 22.456  -10.085 34.133  1.00 46.23 ? 256 GLN   A CD  1 
ATOM   2016 O  OE1 . GLN   A 1 256 ? 21.414  -10.328 33.524  1.00 50.49 ? 256 GLN   A OE1 1 
ATOM   2017 N  NE2 . GLN   A 1 256 ? 23.609  -9.905  33.506  1.00 50.58 ? 256 GLN   A NE2 1 
ATOM   2018 N  N   . THR   A 1 257 ? 21.579  -7.785  38.534  1.00 28.19 ? 257 THR   A N   1 
ATOM   2019 C  CA  . THR   A 1 257 ? 22.512  -6.775  38.981  1.00 24.82 ? 257 THR   A CA  1 
ATOM   2020 C  C   . THR   A 1 257 ? 22.399  -6.519  40.480  1.00 21.88 ? 257 THR   A C   1 
ATOM   2021 O  O   . THR   A 1 257 ? 23.239  -5.828  41.020  1.00 24.47 ? 257 THR   A O   1 
ATOM   2022 C  CB  . THR   A 1 257 ? 22.273  -5.451  38.254  1.00 26.68 ? 257 THR   A CB  1 
ATOM   2023 O  OG1 . THR   A 1 257 ? 20.900  -5.094  38.481  1.00 23.29 ? 257 THR   A OG1 1 
ATOM   2024 C  CG2 . THR   A 1 257 ? 22.600  -5.566  36.777  1.00 26.18 ? 257 THR   A CG2 1 
ATOM   2025 N  N   . GLY   A 1 258 ? 21.330  -6.993  41.100  1.00 23.21 ? 258 GLY   A N   1 
ATOM   2026 C  CA  . GLY   A 1 258 ? 21.079  -6.703  42.505  1.00 28.02 ? 258 GLY   A CA  1 
ATOM   2027 C  C   . GLY   A 1 258 ? 20.519  -5.303  42.762  1.00 27.88 ? 258 GLY   A C   1 
ATOM   2028 O  O   . GLY   A 1 258 ? 20.438  -4.875  43.914  1.00 26.72 ? 258 GLY   A O   1 
ATOM   2029 N  N   . ILE   A 1 259 ? 20.143  -4.573  41.701  1.00 26.99 ? 259 ILE   A N   1 
ATOM   2030 C  CA  . ILE   A 1 259 ? 19.638  -3.214  41.855  1.00 24.39 ? 259 ILE   A CA  1 
ATOM   2031 C  C   . ILE   A 1 259 ? 18.126  -3.228  41.671  1.00 22.25 ? 259 ILE   A C   1 
ATOM   2032 O  O   . ILE   A 1 259 ? 17.641  -3.545  40.590  1.00 23.78 ? 259 ILE   A O   1 
ATOM   2033 C  CB  . ILE   A 1 259 ? 20.313  -2.262  40.855  1.00 23.36 ? 259 ILE   A CB  1 
ATOM   2034 C  CG1 . ILE   A 1 259 ? 21.832  -2.351  40.992  1.00 26.10 ? 259 ILE   A CG1 1 
ATOM   2035 C  CG2 . ILE   A 1 259 ? 19.786  -0.836  41.017  1.00 23.80 ? 259 ILE   A CG2 1 
ATOM   2036 C  CD1 . ILE   A 1 259 ? 22.580  -1.443  40.123  1.00 25.76 ? 259 ILE   A CD1 1 
ATOM   2037 N  N   . ALA   A 1 260 ? 17.375  -2.866  42.721  1.00 19.48 ? 260 ALA   A N   1 
ATOM   2038 C  CA  . ALA   A 1 260 ? 15.920  -2.853  42.610  1.00 19.01 ? 260 ALA   A CA  1 
ATOM   2039 C  C   . ALA   A 1 260 ? 15.544  -1.869  41.500  1.00 15.73 ? 260 ALA   A C   1 
ATOM   2040 O  O   . ALA   A 1 260 ? 16.188  -0.821  41.353  1.00 15.57 ? 260 ALA   A O   1 
ATOM   2041 C  CB  . ALA   A 1 260 ? 15.264  -2.451  43.917  1.00 21.82 ? 260 ALA   A CB  1 
ATOM   2042 N  N   . VAL   A 1 261 ? 14.419  -2.147  40.860  1.00 16.27 ? 261 VAL   A N   1 
ATOM   2043 C  CA  . VAL   A 1 261 ? 13.910  -1.290  39.806  1.00 14.93 ? 261 VAL   A CA  1 
ATOM   2044 C  C   . VAL   A 1 261 ? 13.683  0.122   40.337  1.00 16.18 ? 261 VAL   A C   1 
ATOM   2045 O  O   . VAL   A 1 261 ? 14.085  1.101   39.729  1.00 12.96 ? 261 VAL   A O   1 
ATOM   2046 C  CB  . VAL   A 1 261 ? 12.621  -1.867  39.222  1.00 14.68 ? 261 VAL   A CB  1 
ATOM   2047 C  CG1 . VAL   A 1 261 ? 11.999  -0.922  38.207  1.00 16.65 ? 261 VAL   A CG1 1 
ATOM   2048 C  CG2 . VAL   A 1 261 ? 12.844  -3.249  38.599  1.00 16.59 ? 261 VAL   A CG2 1 
ATOM   2049 N  N   . LEU   A 1 262 ? 13.055  0.248   41.505  1.00 15.89 ? 262 LEU   A N   1 
ATOM   2050 C  CA  . LEU   A 1 262 ? 12.819  1.590   42.030  1.00 17.80 ? 262 LEU   A CA  1 
ATOM   2051 C  C   . LEU   A 1 262 ? 14.093  2.306   42.460  1.00 17.71 ? 262 LEU   A C   1 
ATOM   2052 O  O   . LEU   A 1 262 ? 14.125  3.534   42.430  1.00 16.11 ? 262 LEU   A O   1 
ATOM   2053 C  CB  . LEU   A 1 262 ? 11.798  1.539   43.170  1.00 19.57 ? 262 LEU   A CB  1 
ATOM   2054 C  CG  . LEU   A 1 262 ? 10.381  1.207   42.743  1.00 20.67 ? 262 LEU   A CG  1 
ATOM   2055 C  CD1 . LEU   A 1 262 ? 9.489   1.066   43.975  1.00 22.67 ? 262 LEU   A CD1 1 
ATOM   2056 C  CD2 . LEU   A 1 262 ? 9.793   2.243   41.783  1.00 21.38 ? 262 LEU   A CD2 1 
ATOM   2057 N  N   . ASP   A 1 263 ? 15.175  1.590   42.752  1.00 16.59 ? 263 ASP   A N   1 
ATOM   2058 C  CA  . ASP   A 1 263 ? 16.452  2.249   42.961  1.00 18.55 ? 263 ASP   A CA  1 
ATOM   2059 C  C   . ASP   A 1 263 ? 17.042  2.759   41.633  1.00 17.22 ? 263 ASP   A C   1 
ATOM   2060 O  O   . ASP   A 1 263 ? 17.664  3.823   41.560  1.00 17.88 ? 263 ASP   A O   1 
ATOM   2061 C  CB  . ASP   A 1 263 ? 17.414  1.307   43.672  1.00 21.59 ? 263 ASP   A CB  1 
ATOM   2062 C  CG  . ASP   A 1 263 ? 17.087  1.025   45.135  1.00 28.65 ? 263 ASP   A CG  1 
ATOM   2063 O  OD1 . ASP   A 1 263 ? 16.095  1.551   45.638  1.00 31.41 ? 263 ASP   A OD1 1 
ATOM   2064 O  OD2 . ASP   A 1 263 ? 17.847  0.262   45.758  1.00 36.83 ? 263 ASP   A OD2 1 
ATOM   2065 N  N   . MET   A 1 264 ? 16.878  1.981   40.552  1.00 17.77 ? 264 MET   A N   1 
ATOM   2066 C  CA  . MET   A 1 264 ? 17.297  2.478   39.242  1.00 15.65 ? 264 MET   A CA  1 
ATOM   2067 C  C   . MET   A 1 264 ? 16.481  3.721   38.853  1.00 14.07 ? 264 MET   A C   1 
ATOM   2068 O  O   . MET   A 1 264 ? 17.001  4.682   38.286  1.00 14.57 ? 264 MET   A O   1 
ATOM   2069 C  CB  . MET   A 1 264 ? 17.199  1.390   38.162  1.00 14.84 ? 264 MET   A CB  1 
ATOM   2070 C  CG  . MET   A 1 264 ? 17.966  1.814   36.940  1.00 16.32 ? 264 MET   A CG  1 
ATOM   2071 S  SD  . MET   A 1 264 ? 19.765  1.971   37.259  1.00 17.63 ? 264 MET   A SD  1 
ATOM   2072 C  CE  . MET   A 1 264 ? 20.211  0.276   36.987  1.00 15.82 ? 264 MET   A CE  1 
ATOM   2073 N  N   . CYS   A 1 265 ? 15.178  3.716   39.155  1.00 13.53 ? 265 CYS   A N   1 
ATOM   2074 C  CA  . CYS   A 1 265 ? 14.333  4.889   38.978  1.00 13.71 ? 265 CYS   A CA  1 
ATOM   2075 C  C   . CYS   A 1 265 ? 14.880  6.117   39.721  1.00 15.56 ? 265 CYS   A C   1 
ATOM   2076 O  O   . CYS   A 1 265 ? 14.896  7.233   39.178  1.00 14.34 ? 265 CYS   A O   1 
ATOM   2077 C  CB  . CYS   A 1 265 ? 12.912  4.583   39.438  1.00 14.71 ? 265 CYS   A CB  1 
ATOM   2078 S  SG  . CYS   A 1 265 ? 11.956  3.501   38.345  1.00 16.50 ? 265 CYS   A SG  1 
ATOM   2079 N  N   . ALA   A 1 266 ? 15.316  5.928   40.978  1.00 17.34 ? 266 ALA   A N   1 
ATOM   2080 C  CA  . ALA   A 1 266 ? 15.900  7.026   41.738  1.00 18.31 ? 266 ALA   A CA  1 
ATOM   2081 C  C   . ALA   A 1 266 ? 17.163  7.548   41.057  1.00 18.00 ? 266 ALA   A C   1 
ATOM   2082 O  O   . ALA   A 1 266 ? 17.385  8.755   41.026  1.00 16.66 ? 266 ALA   A O   1 
ATOM   2083 C  CB  . ALA   A 1 266 ? 16.170  6.588   43.162  1.00 19.32 ? 266 ALA   A CB  1 
ATOM   2084 N  N   . SER   A 1 267 ? 17.971  6.645   40.467  1.00 16.82 ? 267 SER   A N   1 
ATOM   2085 C  CA  . SER   A 1 267 ? 19.141  7.070   39.718  1.00 18.38 ? 267 SER   A CA  1 
ATOM   2086 C  C   . SER   A 1 267 ? 18.759  7.888   38.488  1.00 15.35 ? 267 SER   A C   1 
ATOM   2087 O  O   . SER   A 1 267 ? 19.372  8.917   38.240  1.00 15.02 ? 267 SER   A O   1 
ATOM   2088 C  CB  . SER   A 1 267 ? 20.001  5.900   39.340  1.00 22.58 ? 267 SER   A CB  1 
ATOM   2089 O  OG  . SER   A 1 267 ? 20.380  5.204   40.511  1.00 26.31 ? 267 SER   A OG  1 
ATOM   2090 N  N   . LEU   A 1 268 ? 17.772  7.419   37.712  1.00 15.24 ? 268 LEU   A N   1 
ATOM   2091 C  CA  . LEU   A 1 268 ? 17.317  8.160   36.553  1.00 13.70 ? 268 LEU   A CA  1 
ATOM   2092 C  C   . LEU   A 1 268 ? 16.748  9.522   36.971  1.00 13.89 ? 268 LEU   A C   1 
ATOM   2093 O  O   . LEU   A 1 268 ? 16.976  10.538  36.315  1.00 13.91 ? 268 LEU   A O   1 
ATOM   2094 C  CB  . LEU   A 1 268 ? 16.311  7.302   35.785  1.00 14.01 ? 268 LEU   A CB  1 
ATOM   2095 C  CG  . LEU   A 1 268 ? 15.662  7.961   34.564  1.00 13.10 ? 268 LEU   A CG  1 
ATOM   2096 C  CD1 . LEU   A 1 268 ? 16.679  8.524   33.585  1.00 14.50 ? 268 LEU   A CD1 1 
ATOM   2097 C  CD2 . LEU   A 1 268 ? 14.740  6.993   33.847  1.00 14.20 ? 268 LEU   A CD2 1 
ATOM   2098 N  N   . LYS   A 1 269 ? 15.990  9.575   38.065  1.00 14.74 ? 269 LYS   A N   1 
ATOM   2099 C  CA  . LYS   A 1 269 ? 15.423  10.839  38.504  1.00 17.66 ? 269 LYS   A CA  1 
ATOM   2100 C  C   . LYS   A 1 269 ? 16.525  11.870  38.689  1.00 16.62 ? 269 LYS   A C   1 
ATOM   2101 O  O   . LYS   A 1 269 ? 16.358  13.013  38.274  1.00 17.54 ? 269 LYS   A O   1 
ATOM   2102 C  CB  . LYS   A 1 269 ? 14.574  10.635  39.772  1.00 20.58 ? 269 LYS   A CB  1 
ATOM   2103 C  CG  . LYS   A 1 269 ? 13.821  11.864  40.254  1.00 24.45 ? 269 LYS   A CG  1 
ATOM   2104 C  CD  . LYS   A 1 269 ? 13.213  11.725  41.663  1.00 26.13 ? 269 LYS   A CD  1 
ATOM   2105 C  CE  . LYS   A 1 269 ? 12.122  10.681  41.785  1.00 26.93 ? 269 LYS   A CE  1 
ATOM   2106 N  NZ  . LYS   A 1 269 ? 11.587  10.637  43.170  1.00 25.55 ? 269 LYS   A NZ  1 
ATOM   2107 N  N   . GLU   A 1 270 ? 17.635  11.472  39.309  1.00 16.93 ? 270 GLU   A N   1 
ATOM   2108 C  CA  . GLU   A 1 270 ? 18.733  12.385  39.599  1.00 21.04 ? 270 GLU   A CA  1 
ATOM   2109 C  C   . GLU   A 1 270 ? 19.436  12.804  38.305  1.00 21.53 ? 270 GLU   A C   1 
ATOM   2110 O  O   . GLU   A 1 270 ? 19.835  13.955  38.150  1.00 22.00 ? 270 GLU   A O   1 
ATOM   2111 C  CB  . GLU   A 1 270 ? 19.722  11.731  40.560  1.00 24.21 ? 270 GLU   A CB  1 
ATOM   2112 C  CG  . GLU   A 1 270 ? 19.175  11.591  41.978  1.00 31.65 ? 270 GLU   A CG  1 
ATOM   2113 C  CD  . GLU   A 1 270 ? 18.689  12.902  42.594  1.00 39.95 ? 270 GLU   A CD  1 
ATOM   2114 O  OE1 . GLU   A 1 270 ? 19.506  13.856  42.627  1.00 45.76 ? 270 GLU   A OE1 1 
ATOM   2115 O  OE2 . GLU   A 1 270 ? 17.479  12.990  42.990  1.00 39.71 ? 270 GLU   A OE2 1 
ATOM   2116 N  N   . LEU   A 1 271 ? 19.565  11.865  37.357  1.00 22.79 ? 271 LEU   A N   1 
ATOM   2117 C  CA  . LEU   A 1 271 ? 20.126  12.218  36.058  1.00 20.94 ? 271 LEU   A CA  1 
ATOM   2118 C  C   . LEU   A 1 271 ? 19.252  13.264  35.384  1.00 20.94 ? 271 LEU   A C   1 
ATOM   2119 O  O   . LEU   A 1 271 ? 19.790  14.208  34.773  1.00 22.86 ? 271 LEU   A O   1 
ATOM   2120 C  CB  . LEU   A 1 271 ? 20.283  10.972  35.172  1.00 18.69 ? 271 LEU   A CB  1 
ATOM   2121 C  CG  . LEU   A 1 271 ? 21.403  10.016  35.547  1.00 19.55 ? 271 LEU   A CG  1 
ATOM   2122 C  CD1 . LEU   A 1 271 ? 21.312  8.708   34.788  1.00 20.82 ? 271 LEU   A CD1 1 
ATOM   2123 C  CD2 . LEU   A 1 271 ? 22.778  10.647  35.330  1.00 23.97 ? 271 LEU   A CD2 1 
ATOM   2124 N  N   . LEU   A 1 272 ? 17.914  13.126  35.477  1.00 17.69 ? 272 LEU   A N   1 
ATOM   2125 C  CA  . LEU   A 1 272 ? 17.059  14.106  34.842  1.00 19.02 ? 272 LEU   A CA  1 
ATOM   2126 C  C   . LEU   A 1 272 ? 17.179  15.467  35.514  1.00 22.80 ? 272 LEU   A C   1 
ATOM   2127 O  O   . LEU   A 1 272 ? 17.172  16.488  34.831  1.00 20.96 ? 272 LEU   A O   1 
ATOM   2128 C  CB  . LEU   A 1 272 ? 15.610  13.661  34.834  1.00 18.76 ? 272 LEU   A CB  1 
ATOM   2129 C  CG  . LEU   A 1 272 ? 15.327  12.411  34.003  1.00 19.22 ? 272 LEU   A CG  1 
ATOM   2130 C  CD1 . LEU   A 1 272 ? 13.879  12.019  34.101  1.00 19.37 ? 272 LEU   A CD1 1 
ATOM   2131 C  CD2 . LEU   A 1 272 ? 15.731  12.626  32.554  1.00 21.34 ? 272 LEU   A CD2 1 
ATOM   2132 N  N   . GLN   A 1 273 ? 17.240  15.471  36.850  1.00 23.62 ? 273 GLN   A N   1 
ATOM   2133 C  CA  . GLN   A 1 273 ? 17.240  16.721  37.597  1.00 25.34 ? 273 GLN   A CA  1 
ATOM   2134 C  C   . GLN   A 1 273 ? 18.592  17.426  37.520  1.00 26.64 ? 273 GLN   A C   1 
ATOM   2135 O  O   . GLN   A 1 273 ? 18.599  18.654  37.477  1.00 32.93 ? 273 GLN   A O   1 
ATOM   2136 C  CB  . GLN   A 1 273 ? 16.843  16.461  39.049  1.00 25.57 ? 273 GLN   A CB  1 
ATOM   2137 C  CG  . GLN   A 1 273 ? 15.384  16.071  39.184  1.00 26.48 ? 273 GLN   A CG  1 
ATOM   2138 C  CD  . GLN   A 1 273 ? 14.980  15.730  40.602  1.00 27.14 ? 273 GLN   A CD  1 
ATOM   2139 O  OE1 . GLN   A 1 273 ? 15.779  15.319  41.441  1.00 29.81 ? 273 GLN   A OE1 1 
ATOM   2140 N  NE2 . GLN   A 1 273 ? 13.696  15.847  40.852  1.00 29.02 ? 273 GLN   A NE2 1 
ATOM   2141 N  N   . ASN   A 1 274 ? 19.698  16.681  37.492  1.00 28.79 ? 274 ASN   A N   1 
ATOM   2142 C  CA  . ASN   A 1 274 ? 21.042  17.244  37.573  1.00 32.23 ? 274 ASN   A CA  1 
ATOM   2143 C  C   . ASN   A 1 274 ? 21.787  17.257  36.243  1.00 35.32 ? 274 ASN   A C   1 
ATOM   2144 O  O   . ASN   A 1 274 ? 22.771  17.984  36.128  1.00 38.42 ? 274 ASN   A O   1 
ATOM   2145 C  CB  . ASN   A 1 274 ? 21.977  16.457  38.498  1.00 35.76 ? 274 ASN   A CB  1 
ATOM   2146 C  CG  . ASN   A 1 274 ? 21.449  16.362  39.912  1.00 41.55 ? 274 ASN   A CG  1 
ATOM   2147 O  OD1 . ASN   A 1 274 ? 20.573  17.132  40.298  1.00 44.78 ? 274 ASN   A OD1 1 
ATOM   2148 N  ND2 . ASN   A 1 274 ? 21.952  15.404  40.674  1.00 45.79 ? 274 ASN   A ND2 1 
ATOM   2149 N  N   . GLY   A 1 275 ? 21.399  16.403  35.286  1.00 32.84 ? 275 GLY   A N   1 
ATOM   2150 C  CA  . GLY   A 1 275 ? 22.196  16.185  34.084  1.00 34.61 ? 275 GLY   A CA  1 
ATOM   2151 C  C   . GLY   A 1 275 ? 23.353  15.214  34.307  1.00 34.46 ? 275 GLY   A C   1 
ATOM   2152 O  O   . GLY   A 1 275 ? 23.545  14.667  35.401  1.00 32.66 ? 275 GLY   A O   1 
ATOM   2153 N  N   . MET   A 1 276 ? 24.115  14.975  33.236  1.00 32.66 ? 276 MET   A N   1 
ATOM   2154 C  CA  . MET   A 1 276 ? 25.214  14.024  33.274  1.00 36.02 ? 276 MET   A CA  1 
ATOM   2155 C  C   . MET   A 1 276 ? 26.546  14.711  33.577  1.00 38.08 ? 276 MET   A C   1 
ATOM   2156 O  O   . MET   A 1 276 ? 27.530  14.038  33.902  1.00 38.86 ? 276 MET   A O   1 
ATOM   2157 C  CB  . MET   A 1 276 ? 25.268  13.265  31.943  1.00 38.37 ? 276 MET   A CB  1 
ATOM   2158 C  CG  . MET   A 1 276 ? 24.113  12.289  31.821  1.00 37.78 ? 276 MET   A CG  1 
ATOM   2159 S  SD  . MET   A 1 276 ? 23.930  11.579  30.192  0.83 41.61 ? 276 MET   A SD  1 
ATOM   2160 C  CE  . MET   A 1 276 ? 25.345  10.485  30.250  1.00 33.51 ? 276 MET   A CE  1 
ATOM   2161 N  N   . ASN   A 1 277 ? 26.568  16.047  33.461  1.00 48.81 ? 277 ASN   A N   1 
ATOM   2162 C  CA  . ASN   A 1 277 ? 27.722  16.863  33.820  1.00 51.92 ? 277 ASN   A CA  1 
ATOM   2163 C  C   . ASN   A 1 277 ? 28.932  16.399  33.017  1.00 46.42 ? 277 ASN   A C   1 
ATOM   2164 O  O   . ASN   A 1 277 ? 29.972  16.066  33.583  1.00 44.48 ? 277 ASN   A O   1 
ATOM   2165 C  CB  . ASN   A 1 277 ? 27.971  16.859  35.330  1.00 58.18 ? 277 ASN   A CB  1 
ATOM   2166 C  CG  . ASN   A 1 277 ? 26.735  17.298  36.090  1.00 68.15 ? 277 ASN   A CG  1 
ATOM   2167 O  OD1 . ASN   A 1 277 ? 26.149  18.335  35.779  1.00 74.03 ? 277 ASN   A OD1 1 
ATOM   2168 N  ND2 . ASN   A 1 277 ? 26.299  16.496  37.048  1.00 65.62 ? 277 ASN   A ND2 1 
ATOM   2169 N  N   . GLY   A 1 278 ? 28.734  16.322  31.698  1.00 44.00 ? 278 GLY   A N   1 
ATOM   2170 C  CA  . GLY   A 1 278 ? 29.791  15.986  30.759  1.00 42.39 ? 278 GLY   A CA  1 
ATOM   2171 C  C   . GLY   A 1 278 ? 30.322  14.566  30.921  1.00 44.99 ? 278 GLY   A C   1 
ATOM   2172 O  O   . GLY   A 1 278 ? 31.318  14.222  30.297  1.00 48.03 ? 278 GLY   A O   1 
ATOM   2173 N  N   . ARG   A 1 279 ? 29.681  13.734  31.752  1.00 37.21 ? 279 ARG   A N   1 
ATOM   2174 C  CA  . ARG   A 1 279 ? 30.094  12.349  31.840  1.00 36.90 ? 279 ARG   A CA  1 
ATOM   2175 C  C   . ARG   A 1 279 ? 29.353  11.574  30.761  1.00 31.86 ? 279 ARG   A C   1 
ATOM   2176 O  O   . ARG   A 1 279 ? 28.407  12.095  30.186  1.00 34.09 ? 279 ARG   A O   1 
ATOM   2177 C  CB  . ARG   A 1 279 ? 29.836  11.789  33.237  1.00 40.45 ? 279 ARG   A CB  1 
ATOM   2178 C  CG  . ARG   A 1 279 ? 30.625  12.493  34.330  1.00 43.85 ? 279 ARG   A CG  1 
ATOM   2179 C  CD  . ARG   A 1 279 ? 30.832  11.591  35.537  1.00 50.17 ? 279 ARG   A CD  1 
ATOM   2180 N  NE  . ARG   A 1 279 ? 31.642  10.422  35.195  1.00 51.89 ? 279 ARG   A NE  1 
ATOM   2181 C  CZ  . ARG   A 1 279 ? 32.141  9.549   36.070  1.00 48.84 ? 279 ARG   A CZ  1 
ATOM   2182 N  NH1 . ARG   A 1 279 ? 31.933  9.703   37.362  1.00 47.74 ? 279 ARG   A NH1 1 
ATOM   2183 N  NH2 . ARG   A 1 279 ? 32.863  8.526   35.648  1.00 48.11 ? 279 ARG   A NH2 1 
ATOM   2184 N  N   . THR   A 1 280 ? 29.762  10.327  30.503  1.00 29.40 ? 280 THR   A N   1 
ATOM   2185 C  CA  . THR   A 1 280 ? 29.070  9.509   29.523  1.00 29.32 ? 280 THR   A CA  1 
ATOM   2186 C  C   . THR   A 1 280 ? 28.629  8.190   30.158  1.00 26.49 ? 280 THR   A C   1 
ATOM   2187 O  O   . THR   A 1 280 ? 29.195  7.744   31.143  1.00 26.39 ? 280 THR   A O   1 
ATOM   2188 C  CB  . THR   A 1 280 ? 29.933  9.260   28.276  1.00 29.07 ? 280 THR   A CB  1 
ATOM   2189 O  OG1 . THR   A 1 280 ? 31.096  8.522   28.661  1.00 29.10 ? 280 THR   A OG1 1 
ATOM   2190 C  CG2 . THR   A 1 280 ? 30.295  10.547  27.571  1.00 31.51 ? 280 THR   A CG2 1 
ATOM   2191 N  N   . ILE   A 1 281 ? 27.642  7.545   29.545  1.00 21.31 ? 281 ILE   A N   1 
ATOM   2192 C  CA  . ILE   A 1 281 ? 27.237  6.206   29.924  1.00 19.86 ? 281 ILE   A CA  1 
ATOM   2193 C  C   . ILE   A 1 281 ? 27.324  5.315   28.696  1.00 22.57 ? 281 ILE   A C   1 
ATOM   2194 O  O   . ILE   A 1 281 ? 26.690  5.596   27.674  1.00 21.89 ? 281 ILE   A O   1 
ATOM   2195 C  CB  . ILE   A 1 281 ? 25.807  6.237   30.527  1.00 19.98 ? 281 ILE   A CB  1 
ATOM   2196 C  CG1 . ILE   A 1 281 ? 25.748  7.161   31.752  1.00 20.34 ? 281 ILE   A CG1 1 
ATOM   2197 C  CG2 . ILE   A 1 281 ? 25.335  4.815   30.796  1.00 18.75 ? 281 ILE   A CG2 1 
ATOM   2198 C  CD1 . ILE   A 1 281 ? 24.359  7.466   32.312  1.00 21.40 ? 281 ILE   A CD1 1 
ATOM   2199 N  N   . LEU   A 1 282 ? 28.046  4.194   28.809  1.00 20.92 ? 282 LEU   A N   1 
ATOM   2200 C  CA  . LEU   A 1 282 ? 28.307  3.336   27.661  1.00 22.82 ? 282 LEU   A CA  1 
ATOM   2201 C  C   . LEU   A 1 282 ? 28.716  4.171   26.449  1.00 24.19 ? 282 LEU   A C   1 
ATOM   2202 O  O   . LEU   A 1 282 ? 28.239  3.913   25.336  1.00 28.94 ? 282 LEU   A O   1 
ATOM   2203 C  CB  . LEU   A 1 282 ? 27.046  2.525   27.336  1.00 24.24 ? 282 LEU   A CB  1 
ATOM   2204 C  CG  . LEU   A 1 282 ? 26.729  1.414   28.330  1.00 23.33 ? 282 LEU   A CG  1 
ATOM   2205 C  CD1 . LEU   A 1 282 ? 25.344  0.842   28.059  1.00 23.88 ? 282 LEU   A CD1 1 
ATOM   2206 C  CD2 . LEU   A 1 282 ? 27.803  0.324   28.304  1.00 23.42 ? 282 LEU   A CD2 1 
ATOM   2207 N  N   . GLY   A 1 283 ? 29.534  5.200   26.679  1.00 23.96 ? 283 GLY   A N   1 
ATOM   2208 C  CA  . GLY   A 1 283 ? 30.101  5.989   25.590  1.00 27.76 ? 283 GLY   A CA  1 
ATOM   2209 C  C   . GLY   A 1 283 ? 29.139  7.046   25.045  1.00 29.20 ? 283 GLY   A C   1 
ATOM   2210 O  O   . GLY   A 1 283 ? 29.493  7.765   24.124  1.00 29.96 ? 283 GLY   A O   1 
ATOM   2211 N  N   . SER   A 1 284 ? 27.926  7.155   25.621  1.00 26.05 ? 284 SER   A N   1 
ATOM   2212 C  CA  . SER   A 1 284 ? 26.926  8.108   25.168  1.00 23.97 ? 284 SER   A CA  1 
ATOM   2213 C  C   . SER   A 1 284 ? 26.859  9.313   26.100  1.00 26.14 ? 284 SER   A C   1 
ATOM   2214 O  O   . SER   A 1 284 ? 26.839  9.175   27.322  1.00 24.41 ? 284 SER   A O   1 
ATOM   2215 C  CB  . SER   A 1 284 ? 25.585  7.419   25.041  1.00 23.54 ? 284 SER   A CB  1 
ATOM   2216 O  OG  . SER   A 1 284 ? 24.577  8.353   24.751  1.00 23.98 ? 284 SER   A OG  1 
ATOM   2217 N  N   . ALA   A 1 285 ? 26.757  10.497  25.502  1.00 23.62 ? 285 ALA   A N   1 
ATOM   2218 C  CA  . ALA   A 1 285 ? 26.519  11.732  26.233  1.00 25.54 ? 285 ALA   A CA  1 
ATOM   2219 C  C   . ALA   A 1 285 ? 25.035  11.973  26.526  1.00 26.72 ? 285 ALA   A C   1 
ATOM   2220 O  O   . ALA   A 1 285 ? 24.716  12.913  27.259  1.00 28.01 ? 285 ALA   A O   1 
ATOM   2221 C  CB  . ALA   A 1 285 ? 27.099  12.898  25.460  1.00 26.96 ? 285 ALA   A CB  1 
ATOM   2222 N  N   . LEU   A 1 286 ? 24.139  11.145  25.969  1.00 26.08 ? 286 LEU   A N   1 
ATOM   2223 C  CA  . LEU   A 1 286 ? 22.694  11.323  26.099  1.00 25.38 ? 286 LEU   A CA  1 
ATOM   2224 C  C   . LEU   A 1 286 ? 22.095  10.028  26.633  1.00 22.17 ? 286 LEU   A C   1 
ATOM   2225 O  O   . LEU   A 1 286 ? 22.667  8.958   26.431  1.00 23.88 ? 286 LEU   A O   1 
ATOM   2226 C  CB  . LEU   A 1 286 ? 22.062  11.614  24.729  1.00 29.57 ? 286 LEU   A CB  1 
ATOM   2227 C  CG  . LEU   A 1 286 ? 22.529  12.875  23.994  1.00 32.96 ? 286 LEU   A CG  1 
ATOM   2228 C  CD1 . LEU   A 1 286 ? 22.001  12.886  22.566  1.00 35.15 ? 286 LEU   A CD1 1 
ATOM   2229 C  CD2 . LEU   A 1 286 ? 22.097  14.139  24.719  1.00 32.96 ? 286 LEU   A CD2 1 
ATOM   2230 N  N   . LEU   A 1 287 ? 20.909  10.126  27.261  1.00 20.66 ? 287 LEU   A N   1 
ATOM   2231 C  CA  . LEU   A 1 287 ? 20.228  8.953   27.775  1.00 18.60 ? 287 LEU   A CA  1 
ATOM   2232 C  C   . LEU   A 1 287 ? 19.550  8.229   26.621  1.00 20.28 ? 287 LEU   A C   1 
ATOM   2233 O  O   . LEU   A 1 287 ? 18.684  8.788   25.967  1.00 26.17 ? 287 LEU   A O   1 
ATOM   2234 C  CB  . LEU   A 1 287 ? 19.218  9.391   28.834  1.00 19.78 ? 287 LEU   A CB  1 
ATOM   2235 C  CG  . LEU   A 1 287 ? 19.852  10.030  30.063  1.00 21.32 ? 287 LEU   A CG  1 
ATOM   2236 C  CD1 . LEU   A 1 287 ? 18.799  10.555  31.030  1.00 25.35 ? 287 LEU   A CD1 1 
ATOM   2237 C  CD2 . LEU   A 1 287 ? 20.780  9.077   30.754  1.00 23.21 ? 287 LEU   A CD2 1 
ATOM   2238 N  N   . GLU   A 1 288 ? 19.984  7.005   26.368  1.00 16.39 ? 288 GLU   A N   1 
ATOM   2239 C  CA  . GLU   A 1 288 ? 19.559  6.216   25.227  1.00 17.94 ? 288 GLU   A CA  1 
ATOM   2240 C  C   . GLU   A 1 288 ? 18.227  5.529   25.539  1.00 14.12 ? 288 GLU   A C   1 
ATOM   2241 O  O   . GLU   A 1 288 ? 18.122  4.824   26.536  1.00 12.76 ? 288 GLU   A O   1 
ATOM   2242 C  CB  . GLU   A 1 288 ? 20.699  5.233   24.935  1.00 20.26 ? 288 GLU   A CB  1 
ATOM   2243 C  CG  . GLU   A 1 288 ? 20.420  4.242   23.841  1.00 27.34 ? 288 GLU   A CG  1 
ATOM   2244 C  CD  . GLU   A 1 288 ? 20.196  4.934   22.505  1.00 33.78 ? 288 GLU   A CD  1 
ATOM   2245 O  OE1 . GLU   A 1 288 ? 19.129  4.652   21.867  1.00 29.41 ? 288 GLU   A OE1 1 
ATOM   2246 O  OE2 . GLU   A 1 288 ? 21.044  5.829   22.160  1.00 32.52 ? 288 GLU   A OE2 1 
ATOM   2247 N  N   . ASP   A 1 289 ? 17.223  5.650   24.648  1.00 11.81 ? 289 ASP   A N   1 
ATOM   2248 C  CA  . ASP   A 1 289 ? 15.915  5.023   24.887  1.00 12.86 ? 289 ASP   A CA  1 
ATOM   2249 C  C   . ASP   A 1 289 ? 15.472  4.073   23.763  1.00 12.83 ? 289 ASP   A C   1 
ATOM   2250 O  O   . ASP   A 1 289 ? 14.304  3.697   23.730  1.00 12.40 ? 289 ASP   A O   1 
ATOM   2251 C  CB  . ASP   A 1 289 ? 14.839  6.086   25.170  1.00 13.41 ? 289 ASP   A CB  1 
ATOM   2252 C  CG  . ASP   A 1 289 ? 14.338  6.841   23.943  1.00 15.82 ? 289 ASP   A CG  1 
ATOM   2253 O  OD1 . ASP   A 1 289 ? 15.046  6.821   22.892  1.00 15.62 ? 289 ASP   A OD1 1 
ATOM   2254 O  OD2 . ASP   A 1 289 ? 13.256  7.429   24.049  1.00 13.77 ? 289 ASP   A OD2 1 
ATOM   2255 N  N   . GLU   A 1 290 ? 16.389  3.581   22.893  1.00 14.18 ? 290 GLU   A N   1 
ATOM   2256 C  CA  . GLU   A 1 290 ? 15.969  2.649   21.843  1.00 15.89 ? 290 GLU   A CA  1 
ATOM   2257 C  C   . GLU   A 1 290 ? 16.470  1.211   22.067  1.00 15.37 ? 290 GLU   A C   1 
ATOM   2258 O  O   . GLU   A 1 290 ? 16.597  0.421   21.124  1.00 15.95 ? 290 GLU   A O   1 
ATOM   2259 C  CB  . GLU   A 1 290 ? 16.318  3.260   20.478  1.00 17.85 ? 290 GLU   A CB  1 
ATOM   2260 C  CG  . GLU   A 1 290 ? 15.512  4.541   20.208  1.00 18.98 ? 290 GLU   A CG  1 
ATOM   2261 C  CD  . GLU   A 1 290 ? 15.325  4.942   18.752  1.00 20.62 ? 290 GLU   A CD  1 
ATOM   2262 O  OE1 . GLU   A 1 290 ? 15.848  4.198   17.876  1.00 17.65 ? 290 GLU   A OE1 1 
ATOM   2263 O  OE2 . GLU   A 1 290 ? 14.656  5.994   18.490  1.00 19.33 ? 290 GLU   A OE2 1 
ATOM   2264 N  N   . PHE   A 1 291 ? 16.715  0.816   23.333  1.00 13.02 ? 291 PHE   A N   1 
ATOM   2265 C  CA  . PHE   A 1 291 ? 16.894  -0.567  23.718  1.00 13.63 ? 291 PHE   A CA  1 
ATOM   2266 C  C   . PHE   A 1 291 ? 15.814  -0.977  24.700  1.00 14.48 ? 291 PHE   A C   1 
ATOM   2267 O  O   . PHE   A 1 291 ? 15.660  -0.375  25.760  1.00 16.00 ? 291 PHE   A O   1 
ATOM   2268 C  CB  . PHE   A 1 291 ? 18.217  -0.844  24.442  1.00 15.96 ? 291 PHE   A CB  1 
ATOM   2269 C  CG  . PHE   A 1 291 ? 19.453  -0.557  23.658  1.00 16.89 ? 291 PHE   A CG  1 
ATOM   2270 C  CD1 . PHE   A 1 291 ? 20.005  -1.529  22.831  1.00 21.26 ? 291 PHE   A CD1 1 
ATOM   2271 C  CD2 . PHE   A 1 291 ? 20.075  0.672   23.733  1.00 17.47 ? 291 PHE   A CD2 1 
ATOM   2272 C  CE1 . PHE   A 1 291 ? 21.182  -1.278  22.138  1.00 20.24 ? 291 PHE   A CE1 1 
ATOM   2273 C  CE2 . PHE   A 1 291 ? 21.227  0.923   23.005  1.00 22.27 ? 291 PHE   A CE2 1 
ATOM   2274 C  CZ  . PHE   A 1 291 ? 21.767  -0.045  22.202  1.00 18.95 ? 291 PHE   A CZ  1 
ATOM   2275 N  N   . THR   A 1 292 ? 15.068  -2.005  24.352  1.00 13.60 ? 292 THR   A N   1 
ATOM   2276 C  CA  . THR   A 1 292 ? 14.088  -2.585  25.234  1.00 14.81 ? 292 THR   A CA  1 
ATOM   2277 C  C   . THR   A 1 292 ? 14.732  -3.521  26.259  1.00 16.13 ? 292 THR   A C   1 
ATOM   2278 O  O   . THR   A 1 292 ? 15.884  -3.976  26.104  1.00 15.66 ? 292 THR   A O   1 
ATOM   2279 C  CB  . THR   A 1 292 ? 13.050  -3.410  24.480  1.00 15.77 ? 292 THR   A CB  1 
ATOM   2280 O  OG1 . THR   A 1 292 ? 13.725  -4.583  24.010  1.00 15.88 ? 292 THR   A OG1 1 
ATOM   2281 C  CG2 . THR   A 1 292 ? 12.395  -2.650  23.359  1.00 14.55 ? 292 THR   A CG2 1 
ATOM   2282 N  N   . PRO   A 1 293 ? 14.004  -3.838  27.346  1.00 15.18 ? 293 PRO   A N   1 
ATOM   2283 C  CA  . PRO   A 1 293 ? 14.488  -4.833  28.297  1.00 15.29 ? 293 PRO   A CA  1 
ATOM   2284 C  C   . PRO   A 1 293 ? 14.844  -6.185  27.652  1.00 17.21 ? 293 PRO   A C   1 
ATOM   2285 O  O   . PRO   A 1 293 ? 15.853  -6.778  27.999  1.00 17.91 ? 293 PRO   A O   1 
ATOM   2286 C  CB  . PRO   A 1 293 ? 13.335  -4.945  29.297  1.00 15.24 ? 293 PRO   A CB  1 
ATOM   2287 C  CG  . PRO   A 1 293 ? 12.670  -3.595  29.246  1.00 15.40 ? 293 PRO   A CG  1 
ATOM   2288 C  CD  . PRO   A 1 293 ? 12.734  -3.206  27.772  1.00 16.88 ? 293 PRO   A CD  1 
ATOM   2289 N  N   . PHE   A 1 294 ? 14.060  -6.626  26.659  1.00 17.89 ? 294 PHE   A N   1 
ATOM   2290 C  CA  . PHE   A 1 294 ? 14.330  -7.850  25.903  1.00 18.40 ? 294 PHE   A CA  1 
ATOM   2291 C  C   . PHE   A 1 294 ? 15.613  -7.689  25.100  1.00 17.33 ? 294 PHE   A C   1 
ATOM   2292 O  O   . PHE   A 1 294 ? 16.415  -8.636  25.047  1.00 20.15 ? 294 PHE   A O   1 
ATOM   2293 C  CB  . PHE   A 1 294 ? 13.147  -8.212  25.002  1.00 21.26 ? 294 PHE   A CB  1 
ATOM   2294 C  CG  . PHE   A 1 294 ? 13.450  -9.283  23.980  1.00 29.07 ? 294 PHE   A CG  1 
ATOM   2295 C  CD1 . PHE   A 1 294 ? 13.104  -10.602 24.225  1.00 35.86 ? 294 PHE   A CD1 1 
ATOM   2296 C  CD2 . PHE   A 1 294 ? 14.085  -8.972  22.787  1.00 32.83 ? 294 PHE   A CD2 1 
ATOM   2297 C  CE1 . PHE   A 1 294 ? 13.402  -11.597 23.302  1.00 37.08 ? 294 PHE   A CE1 1 
ATOM   2298 C  CE2 . PHE   A 1 294 ? 14.352  -9.961  21.849  1.00 40.73 ? 294 PHE   A CE2 1 
ATOM   2299 C  CZ  . PHE   A 1 294 ? 14.018  -11.273 22.115  1.00 38.27 ? 294 PHE   A CZ  1 
ATOM   2300 N  N   . ASP   A 1 295 ? 15.823  -6.515  24.490  1.00 17.97 ? 295 ASP   A N   1 
ATOM   2301 C  CA  . ASP   A 1 295 ? 17.035  -6.249  23.736  1.00 18.52 ? 295 ASP   A CA  1 
ATOM   2302 C  C   . ASP   A 1 295 ? 18.249  -6.403  24.649  1.00 21.28 ? 295 ASP   A C   1 
ATOM   2303 O  O   . ASP   A 1 295 ? 19.303  -6.894  24.246  1.00 19.38 ? 295 ASP   A O   1 
ATOM   2304 C  CB  . ASP   A 1 295 ? 17.052  -4.863  23.126  1.00 18.61 ? 295 ASP   A CB  1 
ATOM   2305 C  CG  . ASP   A 1 295 ? 16.037  -4.649  22.005  1.00 20.71 ? 295 ASP   A CG  1 
ATOM   2306 O  OD1 . ASP   A 1 295 ? 15.604  -5.674  21.437  1.00 23.97 ? 295 ASP   A OD1 1 
ATOM   2307 O  OD2 . ASP   A 1 295 ? 15.670  -3.441  21.743  1.00 17.86 ? 295 ASP   A OD2 1 
ATOM   2308 N  N   . VAL   A 1 296 ? 18.149  -5.872  25.869  1.00 15.59 ? 296 VAL   A N   1 
ATOM   2309 C  CA  . VAL   A 1 296 ? 19.315  -5.903  26.753  1.00 17.30 ? 296 VAL   A CA  1 
ATOM   2310 C  C   . VAL   A 1 296 ? 19.579  -7.355  27.163  1.00 19.28 ? 296 VAL   A C   1 
ATOM   2311 O  O   . VAL   A 1 296 ? 20.744  -7.757  27.177  1.00 22.68 ? 296 VAL   A O   1 
ATOM   2312 C  CB  . VAL   A 1 296 ? 19.109  -4.963  27.971  1.00 18.00 ? 296 VAL   A CB  1 
ATOM   2313 C  CG1 . VAL   A 1 296 ? 20.193  -5.104  29.060  1.00 19.48 ? 296 VAL   A CG1 1 
ATOM   2314 C  CG2 . VAL   A 1 296 ? 19.001  -3.515  27.507  1.00 18.98 ? 296 VAL   A CG2 1 
ATOM   2315 N  N   . VAL   A 1 297 ? 18.525  -8.104  27.523  1.00 22.27 ? 297 VAL   A N   1 
ATOM   2316 C  CA  . VAL   A 1 297 ? 18.659  -9.486  27.992  1.00 27.48 ? 297 VAL   A CA  1 
ATOM   2317 C  C   . VAL   A 1 297 ? 19.331  -10.348 26.920  1.00 29.76 ? 297 VAL   A C   1 
ATOM   2318 O  O   . VAL   A 1 297 ? 20.203  -11.175 27.223  1.00 32.63 ? 297 VAL   A O   1 
ATOM   2319 C  CB  . VAL   A 1 297 ? 17.298  -10.062 28.433  1.00 30.36 ? 297 VAL   A CB  1 
ATOM   2320 C  CG1 . VAL   A 1 297 ? 17.279  -11.582 28.526  1.00 31.96 ? 297 VAL   A CG1 1 
ATOM   2321 C  CG2 . VAL   A 1 297 ? 16.864  -9.457  29.760  1.00 32.79 ? 297 VAL   A CG2 1 
ATOM   2322 N  N   . ARG   A 1 298 ? 18.926  -10.115 25.667  1.00 28.54 ? 298 ARG   A N   1 
ATOM   2323 C  CA  . ARG   A 1 298 ? 19.378  -10.863 24.498  1.00 32.58 ? 298 ARG   A CA  1 
ATOM   2324 C  C   . ARG   A 1 298 ? 20.853  -10.568 24.235  1.00 30.83 ? 298 ARG   A C   1 
ATOM   2325 O  O   . ARG   A 1 298 ? 21.628  -11.456 23.881  1.00 34.99 ? 298 ARG   A O   1 
ATOM   2326 C  CB  . ARG   A 1 298 ? 18.433  -10.540 23.328  1.00 35.43 ? 298 ARG   A CB  1 
ATOM   2327 C  CG  . ARG   A 1 298 ? 18.925  -10.830 21.910  1.00 42.23 ? 298 ARG   A CG  1 
ATOM   2328 C  CD  . ARG   A 1 298 ? 17.919  -10.342 20.851  1.00 42.11 ? 298 ARG   A CD  1 
ATOM   2329 N  NE  . ARG   A 1 298 ? 18.502  -9.696  19.669  1.00 43.09 ? 298 ARG   A NE  1 
ATOM   2330 C  CZ  . ARG   A 1 298 ? 19.342  -10.265 18.790  1.00 44.85 ? 298 ARG   A CZ  1 
ATOM   2331 N  NH1 . ARG   A 1 298 ? 19.666  -11.544 18.910  1.00 48.09 ? 298 ARG   A NH1 1 
ATOM   2332 N  NH2 . ARG   A 1 298 ? 19.839  -9.561  17.775  1.00 33.94 ? 298 ARG   A NH2 1 
ATOM   2333 N  N   . GLN   A 1 299 ? 21.285  -9.330  24.412  1.00 29.34 ? 299 GLN   A N   1 
ATOM   2334 C  CA  . GLN   A 1 299 ? 22.654  -9.000  24.083  1.00 27.39 ? 299 GLN   A CA  1 
ATOM   2335 C  C   . GLN   A 1 299 ? 23.579  -9.230  25.288  1.00 33.19 ? 299 GLN   A C   1 
ATOM   2336 O  O   . GLN   A 1 299 ? 24.796  -9.332  25.128  1.00 34.78 ? 299 GLN   A O   1 
ATOM   2337 C  CB  . GLN   A 1 299 ? 22.722  -7.583  23.536  1.00 28.70 ? 299 GLN   A CB  1 
ATOM   2338 C  CG  . GLN   A 1 299 ? 24.126  -7.010  23.485  1.00 28.81 ? 299 GLN   A CG  1 
ATOM   2339 C  CD  . GLN   A 1 299 ? 24.233  -5.749  22.660  1.00 29.55 ? 299 GLN   A CD  1 
ATOM   2340 O  OE1 . GLN   A 1 299 ? 25.324  -5.228  22.434  1.00 26.97 ? 299 GLN   A OE1 1 
ATOM   2341 N  NE2 . GLN   A 1 299 ? 23.102  -5.239  22.188  1.00 28.81 ? 299 GLN   A NE2 1 
ATOM   2342 N  N   . CYS   A 1 300 ? 23.041  -9.277  26.506  1.00 29.82 ? 300 CYS   A N   1 
ATOM   2343 C  CA  . CYS   A 1 300 ? 23.926  -9.363  27.658  1.00 31.88 ? 300 CYS   A CA  1 
ATOM   2344 C  C   . CYS   A 1 300 ? 23.967  -10.800 28.188  1.00 35.22 ? 300 CYS   A C   1 
ATOM   2345 O  O   . CYS   A 1 300 ? 24.834  -11.115 29.000  1.00 42.13 ? 300 CYS   A O   1 
ATOM   2346 C  CB  . CYS   A 1 300 ? 23.547  -8.362  28.744  1.00 26.56 ? 300 CYS   A CB  1 
ATOM   2347 S  SG  . CYS   A 1 300 ? 23.915  -6.626  28.372  0.83 31.41 ? 300 CYS   A SG  1 
ATOM   2348 N  N   . SER   A 1 301 ? 23.116  -11.694 27.665  1.00 37.83 ? 301 SER   A N   1 
ATOM   2349 C  CA  . SER   A 1 301 ? 22.952  -13.028 28.239  1.00 41.11 ? 301 SER   A CA  1 
ATOM   2350 C  C   . SER   A 1 301 ? 22.730  -14.075 27.137  1.00 41.60 ? 301 SER   A C   1 
ATOM   2351 O  O   . SER   A 1 301 ? 22.138  -13.697 26.099  1.00 45.53 ? 301 SER   A O   1 
ATOM   2352 C  CB  . SER   A 1 301 ? 21.808  -13.058 29.232  1.00 41.83 ? 301 SER   A CB  1 
ATOM   2353 O  OG  . SER   A 1 301 ? 21.808  -11.886 30.037  1.00 42.58 ? 301 SER   A OG  1 
ATOM   2354 N  N   . GLY   B 1 2   ? 20.612  11.845  12.712  1.00 52.84 ? 2   GLY   B N   1 
ATOM   2355 C  CA  . GLY   B 1 2   ? 21.293  12.244  11.464  1.00 52.44 ? 2   GLY   B CA  1 
ATOM   2356 C  C   . GLY   B 1 2   ? 22.164  11.118  10.913  1.00 52.28 ? 2   GLY   B C   1 
ATOM   2357 O  O   . GLY   B 1 2   ? 22.049  10.757  9.740   1.00 52.02 ? 2   GLY   B O   1 
ATOM   2358 N  N   . PHE   B 1 3   ? 23.027  10.570  11.780  1.00 46.77 ? 3   PHE   B N   1 
ATOM   2359 C  CA  . PHE   B 1 3   ? 23.920  9.488   11.402  1.00 42.75 ? 3   PHE   B CA  1 
ATOM   2360 C  C   . PHE   B 1 3   ? 23.819  8.381   12.440  1.00 40.10 ? 3   PHE   B C   1 
ATOM   2361 O  O   . PHE   B 1 3   ? 23.880  8.651   13.637  1.00 40.79 ? 3   PHE   B O   1 
ATOM   2362 C  CB  . PHE   B 1 3   ? 25.359  9.996   11.271  1.00 44.43 ? 3   PHE   B CB  1 
ATOM   2363 C  CG  . PHE   B 1 3   ? 25.549  10.937  10.111  1.00 40.18 ? 3   PHE   B CG  1 
ATOM   2364 C  CD1 . PHE   B 1 3   ? 25.799  10.451  8.835   1.00 39.79 ? 3   PHE   B CD1 1 
ATOM   2365 C  CD2 . PHE   B 1 3   ? 25.376  12.304  10.278  1.00 41.19 ? 3   PHE   B CD2 1 
ATOM   2366 C  CE1 . PHE   B 1 3   ? 25.931  11.310  7.757   1.00 33.55 ? 3   PHE   B CE1 1 
ATOM   2367 C  CE2 . PHE   B 1 3   ? 25.505  13.167  9.203   1.00 36.99 ? 3   PHE   B CE2 1 
ATOM   2368 C  CZ  . PHE   B 1 3   ? 25.782  12.673  7.948   1.00 38.10 ? 3   PHE   B CZ  1 
ATOM   2369 N  N   . ARG   B 1 4   ? 23.713  7.134   11.971  1.00 34.30 ? 4   ARG   B N   1 
ATOM   2370 C  CA  . ARG   B 1 4   ? 23.826  5.996   12.874  1.00 33.80 ? 4   ARG   B CA  1 
ATOM   2371 C  C   . ARG   B 1 4   ? 24.702  4.905   12.259  1.00 24.18 ? 4   ARG   B C   1 
ATOM   2372 O  O   . ARG   B 1 4   ? 24.966  4.932   11.073  1.00 23.11 ? 4   ARG   B O   1 
ATOM   2373 C  CB  . ARG   B 1 4   ? 22.432  5.450   13.158  1.00 39.96 ? 4   ARG   B CB  1 
ATOM   2374 C  CG  . ARG   B 1 4   ? 21.624  5.246   11.890  1.00 43.74 ? 4   ARG   B CG  1 
ATOM   2375 C  CD  . ARG   B 1 4   ? 20.769  4.008   11.970  1.00 49.99 ? 4   ARG   B CD  1 
ATOM   2376 N  NE  . ARG   B 1 4   ? 19.978  3.911   13.188  1.00 48.55 ? 4   ARG   B NE  1 
ATOM   2377 C  CZ  . ARG   B 1 4   ? 18.880  4.614   13.429  1.00 47.07 ? 4   ARG   B CZ  1 
ATOM   2378 N  NH1 . ARG   B 1 4   ? 18.510  5.580   12.604  1.00 50.36 ? 4   ARG   B NH1 1 
ATOM   2379 N  NH2 . ARG   B 1 4   ? 18.173  4.366   14.516  1.00 45.78 ? 4   ARG   B NH2 1 
ATOM   2380 N  N   . LYS   B 1 5   ? 25.168  3.978   13.095  1.00 27.69 ? 5   LYS   B N   1 
ATOM   2381 C  CA  . LYS   B 1 5   ? 25.953  2.833   12.638  1.00 25.86 ? 5   LYS   B CA  1 
ATOM   2382 C  C   . LYS   B 1 5   ? 24.999  2.002   11.765  1.00 24.86 ? 5   LYS   B C   1 
ATOM   2383 O  O   . LYS   B 1 5   ? 23.940  1.668   12.261  1.00 27.40 ? 5   LYS   B O   1 
ATOM   2384 C  CB  . LYS   B 1 5   ? 26.483  2.107   13.880  1.00 29.38 ? 5   LYS   B CB  1 
ATOM   2385 C  CG  . LYS   B 1 5   ? 27.763  2.658   14.514  1.00 31.23 ? 5   LYS   B CG  1 
ATOM   2386 C  CD  . LYS   B 1 5   ? 27.803  4.141   14.685  1.00 33.89 ? 5   LYS   B CD  1 
ATOM   2387 C  CE  . LYS   B 1 5   ? 29.204  4.693   14.867  1.00 32.15 ? 5   LYS   B CE  1 
ATOM   2388 N  NZ  . LYS   B 1 5   ? 29.763  4.337   16.199  1.00 34.54 ? 5   LYS   B NZ  1 
ATOM   2389 N  N   . MET   B 1 6   ? 25.273  1.794   10.464  1.00 21.21 ? 6   MET   B N   1 
ATOM   2390 C  CA  . MET   B 1 6   ? 24.486  0.851   9.673   1.00 20.48 ? 6   MET   B CA  1 
ATOM   2391 C  C   . MET   B 1 6   ? 25.381  -0.300  9.228   1.00 15.15 ? 6   MET   B C   1 
ATOM   2392 O  O   . MET   B 1 6   ? 26.489  -0.029  8.755   1.00 17.09 ? 6   MET   B O   1 
ATOM   2393 C  CB  . MET   B 1 6   ? 23.899  1.492   8.427   1.00 24.18 ? 6   MET   B CB  1 
ATOM   2394 C  CG  . MET   B 1 6   ? 22.841  2.524   8.764   1.00 31.29 ? 6   MET   B CG  1 
ATOM   2395 S  SD  . MET   B 1 6   ? 22.435  3.485   7.317   0.63 33.85 ? 6   MET   B SD  1 
ATOM   2396 C  CE  . MET   B 1 6   ? 22.160  2.141   6.189   1.00 27.12 ? 6   MET   B CE  1 
ATOM   2397 N  N   . ALA   B 1 7   ? 24.903  -1.540  9.403   1.00 13.12 ? 7   ALA   B N   1 
ATOM   2398 C  CA  . ALA   B 1 7   ? 25.618  -2.706  8.915   1.00 11.48 ? 7   ALA   B CA  1 
ATOM   2399 C  C   . ALA   B 1 7   ? 25.258  -2.973  7.454   1.00 10.74 ? 7   ALA   B C   1 
ATOM   2400 O  O   . ALA   B 1 7   ? 24.191  -2.589  6.964   1.00 9.99  ? 7   ALA   B O   1 
ATOM   2401 C  CB  . ALA   B 1 7   ? 25.270  -3.916  9.769   1.00 12.43 ? 7   ALA   B CB  1 
ATOM   2402 N  N   . PHE   B 1 8   ? 26.088  -3.780  6.791   1.00 11.05 ? 8   PHE   B N   1 
ATOM   2403 C  CA  . PHE   B 1 8   ? 25.729  -4.329  5.506   1.00 10.87 ? 8   PHE   B CA  1 
ATOM   2404 C  C   . PHE   B 1 8   ? 24.681  -5.406  5.713   1.00 11.19 ? 8   PHE   B C   1 
ATOM   2405 O  O   . PHE   B 1 8   ? 24.690  -6.092  6.723   1.00 9.90  ? 8   PHE   B O   1 
ATOM   2406 C  CB  . PHE   B 1 8   ? 26.930  -4.913  4.774   1.00 11.43 ? 8   PHE   B CB  1 
ATOM   2407 C  CG  . PHE   B 1 8   ? 27.814  -3.847  4.185   1.00 14.24 ? 8   PHE   B CG  1 
ATOM   2408 C  CD1 . PHE   B 1 8   ? 27.421  -3.187  3.033   1.00 17.09 ? 8   PHE   B CD1 1 
ATOM   2409 C  CD2 . PHE   B 1 8   ? 28.962  -3.466  4.830   1.00 16.93 ? 8   PHE   B CD2 1 
ATOM   2410 C  CE1 . PHE   B 1 8   ? 28.214  -2.173  2.508   1.00 19.83 ? 8   PHE   B CE1 1 
ATOM   2411 C  CE2 . PHE   B 1 8   ? 29.759  -2.466  4.294   1.00 18.00 ? 8   PHE   B CE2 1 
ATOM   2412 C  CZ  . PHE   B 1 8   ? 29.390  -1.844  3.133   1.00 16.48 ? 8   PHE   B CZ  1 
ATOM   2413 N  N   . PRO   B 1 9   ? 23.801  -5.673  4.720   1.00 11.58 ? 9   PRO   B N   1 
ATOM   2414 C  CA  . PRO   B 1 9   ? 22.906  -6.822  4.825   1.00 12.18 ? 9   PRO   B CA  1 
ATOM   2415 C  C   . PRO   B 1 9   ? 23.762  -8.091  5.009   1.00 10.84 ? 9   PRO   B C   1 
ATOM   2416 O  O   . PRO   B 1 9   ? 24.798  -8.237  4.371   1.00 13.10 ? 9   PRO   B O   1 
ATOM   2417 C  CB  . PRO   B 1 9   ? 22.151  -6.822  3.511   1.00 12.64 ? 9   PRO   B CB  1 
ATOM   2418 C  CG  . PRO   B 1 9   ? 22.292  -5.384  3.015   1.00 13.02 ? 9   PRO   B CG  1 
ATOM   2419 C  CD  . PRO   B 1 9   ? 23.685  -4.960  3.454   1.00 12.71 ? 9   PRO   B CD  1 
ATOM   2420 N  N   . SER   B 1 10  ? 23.322  -8.975  5.890   1.00 10.66 ? 10  SER   B N   1 
ATOM   2421 C  CA  . SER   B 1 10  ? 24.166  -10.073 6.344   1.00 10.30 ? 10  SER   B CA  1 
ATOM   2422 C  C   . SER   B 1 10  ? 23.916  -11.377 5.573   1.00 9.88  ? 10  SER   B C   1 
ATOM   2423 O  O   . SER   B 1 10  ? 24.608  -12.353 5.855   1.00 10.25 ? 10  SER   B O   1 
ATOM   2424 C  CB  . SER   B 1 10  ? 24.022  -10.248 7.802   1.00 10.62 ? 10  SER   B CB  1 
ATOM   2425 O  OG  . SER   B 1 10  ? 22.655  -10.488 8.152   1.00 11.00 ? 10  SER   B OG  1 
ATOM   2426 N  N   . GLY   B 1 11  ? 22.906  -11.460 4.688   1.00 9.55  ? 11  GLY   B N   1 
ATOM   2427 C  CA  . GLY   B 1 11  ? 22.505  -12.731 4.088   1.00 11.38 ? 11  GLY   B CA  1 
ATOM   2428 C  C   . GLY   B 1 11  ? 23.634  -13.542 3.444   1.00 11.80 ? 11  GLY   B C   1 
ATOM   2429 O  O   . GLY   B 1 11  ? 23.737  -14.768 3.635   1.00 11.30 ? 11  GLY   B O   1 
ATOM   2430 N  N   . LYS   B 1 12  ? 24.467  -12.835 2.679   1.00 12.33 ? 12  LYS   B N   1 
ATOM   2431 C  CA  . LYS   B 1 12  ? 25.542  -13.482 1.939   1.00 13.22 ? 12  LYS   B CA  1 
ATOM   2432 C  C   . LYS   B 1 12  ? 26.502  -14.166 2.905   1.00 12.91 ? 12  LYS   B C   1 
ATOM   2433 O  O   . LYS   B 1 12  ? 27.108  -15.174 2.520   1.00 13.46 ? 12  LYS   B O   1 
ATOM   2434 C  CB  . LYS   B 1 12  ? 26.273  -12.478 1.066   1.00 14.17 ? 12  LYS   B CB  1 
ATOM   2435 C  CG  . LYS   B 1 12  ? 25.546  -12.018 -0.186  1.00 17.94 ? 12  LYS   B CG  1 
ATOM   2436 C  CD  . LYS   B 1 12  ? 26.449  -11.120 -1.016  1.00 21.87 ? 12  LYS   B CD  1 
ATOM   2437 C  CE  . LYS   B 1 12  ? 25.937  -10.868 -2.415  1.00 29.17 ? 12  LYS   B CE  1 
ATOM   2438 N  NZ  . LYS   B 1 12  ? 24.714  -10.047 -2.386  1.00 32.80 ? 12  LYS   B NZ  1 
ATOM   2439 N  N   . VAL   B 1 13  ? 26.644  -13.634 4.128   1.00 9.15  ? 13  VAL   B N   1 
ATOM   2440 C  CA  . VAL   B 1 13  ? 27.536  -14.240 5.103   1.00 9.95  ? 13  VAL   B CA  1 
ATOM   2441 C  C   . VAL   B 1 13  ? 26.800  -15.310 5.927   1.00 9.81  ? 13  VAL   B C   1 
ATOM   2442 O  O   . VAL   B 1 13  ? 27.380  -16.355 6.268   1.00 10.19 ? 13  VAL   B O   1 
ATOM   2443 C  CB  . VAL   B 1 13  ? 28.149  -13.155 5.990   1.00 10.19 ? 13  VAL   B CB  1 
ATOM   2444 C  CG1 . VAL   B 1 13  ? 29.034  -13.728 7.077   1.00 10.72 ? 13  VAL   B CG1 1 
ATOM   2445 C  CG2 . VAL   B 1 13  ? 28.941  -12.164 5.154   1.00 11.09 ? 13  VAL   B CG2 1 
ATOM   2446 N  N   . GLU   B 1 14  ? 25.512  -15.048 6.254   1.00 9.17  ? 14  GLU   B N   1 
ATOM   2447 C  CA  . GLU   B 1 14  ? 24.727  -16.051 6.984   1.00 9.68  ? 14  GLU   B CA  1 
ATOM   2448 C  C   . GLU   B 1 14  ? 24.785  -17.435 6.344   1.00 9.26  ? 14  GLU   B C   1 
ATOM   2449 O  O   . GLU   B 1 14  ? 24.918  -18.461 7.056   1.00 9.45  ? 14  GLU   B O   1 
ATOM   2450 C  CB  . GLU   B 1 14  ? 23.255  -15.642 7.084   1.00 10.67 ? 14  GLU   B CB  1 
ATOM   2451 C  CG  . GLU   B 1 14  ? 22.995  -14.479 8.023   1.00 11.37 ? 14  GLU   B CG  1 
ATOM   2452 C  CD  . GLU   B 1 14  ? 21.591  -13.911 7.816   1.00 13.71 ? 14  GLU   B CD  1 
ATOM   2453 O  OE1 . GLU   B 1 14  ? 20.637  -14.712 7.945   1.00 13.95 ? 14  GLU   B OE1 1 
ATOM   2454 O  OE2 . GLU   B 1 14  ? 21.476  -12.714 7.481   1.00 14.49 ? 14  GLU   B OE2 1 
ATOM   2455 N  N   . GLY   B 1 15  ? 24.744  -17.475 5.009   1.00 9.78  ? 15  GLY   B N   1 
ATOM   2456 C  CA  . GLY   B 1 15  ? 24.765  -18.731 4.276   1.00 11.54 ? 15  GLY   B CA  1 
ATOM   2457 C  C   . GLY   B 1 15  ? 26.131  -19.436 4.272   1.00 11.81 ? 15  GLY   B C   1 
ATOM   2458 O  O   . GLY   B 1 15  ? 26.224  -20.555 3.758   1.00 11.62 ? 15  GLY   B O   1 
ATOM   2459 N  N   . CYS   B 1 16  ? 27.155  -18.802 4.864   1.00 10.39 ? 16  CYS   B N   1 
ATOM   2460 C  CA  . CYS   B 1 16  ? 28.466  -19.413 5.001   1.00 9.49  ? 16  CYS   B CA  1 
ATOM   2461 C  C   . CYS   B 1 16  ? 28.802  -19.826 6.420   1.00 9.43  ? 16  CYS   B C   1 
ATOM   2462 O  O   . CYS   B 1 16  ? 29.850  -20.410 6.619   1.00 7.96  ? 16  CYS   B O   1 
ATOM   2463 C  CB  . CYS   B 1 16  ? 29.531  -18.441 4.573   1.00 9.96  ? 16  CYS   B CB  1 
ATOM   2464 S  SG  . CYS   B 1 16  ? 29.286  -17.947 2.856   1.00 13.81 ? 16  CYS   B SG  1 
ATOM   2465 N  N   . MET   B 1 17  ? 27.922  -19.621 7.422   1.00 9.38  ? 17  MET   B N   1 
ATOM   2466 C  CA  . MET   B 1 17  ? 28.337  -19.902 8.790   1.00 9.40  ? 17  MET   B CA  1 
ATOM   2467 C  C   . MET   B 1 17  ? 28.069  -21.368 9.134   1.00 9.89  ? 17  MET   B C   1 
ATOM   2468 O  O   . MET   B 1 17  ? 26.983  -21.889 8.840   1.00 10.80 ? 17  MET   B O   1 
ATOM   2469 C  CB  . MET   B 1 17  ? 27.579  -19.041 9.806   1.00 10.49 ? 17  MET   B CB  1 
ATOM   2470 C  CG  . MET   B 1 17  ? 27.853  -17.550 9.610   1.00 11.60 ? 17  MET   B CG  1 
ATOM   2471 S  SD  . MET   B 1 17  ? 29.600  -17.119 9.552   1.00 13.74 ? 17  MET   B SD  1 
ATOM   2472 C  CE  . MET   B 1 17  ? 30.276  -17.771 11.091  1.00 15.80 ? 17  MET   B CE  1 
ATOM   2473 N  N   . VAL   B 1 18  ? 29.054  -22.001 9.765   1.00 10.08 ? 18  VAL   B N   1 
ATOM   2474 C  CA  . VAL   B 1 18  ? 28.946  -23.380 10.237  1.00 9.85  ? 18  VAL   B CA  1 
ATOM   2475 C  C   . VAL   B 1 18  ? 29.503  -23.471 11.638  1.00 10.08 ? 18  VAL   B C   1 
ATOM   2476 O  O   . VAL   B 1 18  ? 30.059  -22.502 12.181  1.00 10.75 ? 18  VAL   B O   1 
ATOM   2477 C  CB  . VAL   B 1 18  ? 29.673  -24.352 9.284   1.00 9.84  ? 18  VAL   B CB  1 
ATOM   2478 C  CG1 . VAL   B 1 18  ? 29.081  -24.337 7.875   1.00 10.16 ? 18  VAL   B CG1 1 
ATOM   2479 C  CG2 . VAL   B 1 18  ? 31.164  -24.054 9.246   1.00 10.85 ? 18  VAL   B CG2 1 
ATOM   2480 N  N   . GLN   B 1 19  ? 29.344  -24.655 12.263  1.00 10.63 ? 19  GLN   B N   1 
ATOM   2481 C  CA  . GLN   B 1 19  ? 29.967  -24.911 13.546  1.00 11.87 ? 19  GLN   B CA  1 
ATOM   2482 C  C   . GLN   B 1 19  ? 31.065  -25.952 13.379  1.00 11.46 ? 19  GLN   B C   1 
ATOM   2483 O  O   . GLN   B 1 19  ? 30.885  -26.883 12.608  1.00 11.53 ? 19  GLN   B O   1 
ATOM   2484 C  CB  . GLN   B 1 19  ? 28.983  -25.346 14.642  1.00 16.70 ? 19  GLN   B CB  1 
ATOM   2485 C  CG  . GLN   B 1 19  ? 27.777  -26.104 14.211  1.00 22.04 ? 19  GLN   B CG  1 
ATOM   2486 C  CD  . GLN   B 1 19  ? 26.890  -26.459 15.402  1.00 26.83 ? 19  GLN   B CD  1 
ATOM   2487 O  OE1 . GLN   B 1 19  ? 27.305  -26.446 16.563  1.00 22.94 ? 19  GLN   B OE1 1 
ATOM   2488 N  NE2 . GLN   B 1 19  ? 25.660  -26.814 15.079  1.00 30.73 ? 19  GLN   B NE2 1 
ATOM   2489 N  N   . VAL   B 1 20  ? 32.141  -25.799 14.158  1.00 11.02 ? 20  VAL   B N   1 
ATOM   2490 C  CA  . VAL   B 1 20  ? 33.268  -26.723 14.173  1.00 10.50 ? 20  VAL   B CA  1 
ATOM   2491 C  C   . VAL   B 1 20  ? 33.515  -27.141 15.618  1.00 11.29 ? 20  VAL   B C   1 
ATOM   2492 O  O   . VAL   B 1 20  ? 33.608  -26.305 16.515  1.00 11.04 ? 20  VAL   B O   1 
ATOM   2493 C  CB  . VAL   B 1 20  ? 34.538  -26.127 13.555  1.00 11.17 ? 20  VAL   B CB  1 
ATOM   2494 C  CG1 . VAL   B 1 20  ? 35.688  -27.136 13.496  1.00 11.65 ? 20  VAL   B CG1 1 
ATOM   2495 C  CG2 . VAL   B 1 20  ? 34.238  -25.532 12.185  1.00 11.50 ? 20  VAL   B CG2 1 
ATOM   2496 N  N   . THR   B 1 21  ? 33.665  -28.448 15.810  1.00 11.60 ? 21  THR   B N   1 
ATOM   2497 C  CA  . THR   B 1 21  ? 33.857  -29.027 17.123  1.00 12.16 ? 21  THR   B CA  1 
ATOM   2498 C  C   . THR   B 1 21  ? 34.978  -30.053 17.060  1.00 12.52 ? 21  THR   B C   1 
ATOM   2499 O  O   . THR   B 1 21  ? 35.037  -30.875 16.156  1.00 13.44 ? 21  THR   B O   1 
ATOM   2500 C  CB  . THR   B 1 21  ? 32.583  -29.722 17.598  1.00 14.88 ? 21  THR   B CB  1 
ATOM   2501 O  OG1 . THR   B 1 21  ? 31.474  -28.830 17.660  1.00 15.82 ? 21  THR   B OG1 1 
ATOM   2502 C  CG2 . THR   B 1 21  ? 32.728  -30.386 18.953  1.00 17.58 ? 21  THR   B CG2 1 
ATOM   2503 N  N   . CYS   B 1 22  ? 35.816  -29.965 18.071  1.00 14.36 ? 22  CYS   B N   1 
ATOM   2504 C  CA  . CYS   B 1 22  ? 36.864  -30.907 18.373  1.00 17.79 ? 22  CYS   B CA  1 
ATOM   2505 C  C   . CYS   B 1 22  ? 36.725  -31.349 19.811  1.00 17.83 ? 22  CYS   B C   1 
ATOM   2506 O  O   . CYS   B 1 22  ? 37.081  -30.560 20.699  1.00 19.16 ? 22  CYS   B O   1 
ATOM   2507 C  CB  . CYS   B 1 22  ? 38.203  -30.226 18.309  1.00 20.91 ? 22  CYS   B CB  1 
ATOM   2508 S  SG  . CYS   B 1 22  ? 38.872  -30.249 16.657  1.00 28.16 ? 22  CYS   B SG  1 
ATOM   2509 N  N   . GLY   B 1 23  ? 36.345  -32.614 20.007  1.00 18.17 ? 23  GLY   B N   1 
ATOM   2510 C  CA  . GLY   B 1 23  ? 36.003  -33.096 21.353  1.00 19.36 ? 23  GLY   B CA  1 
ATOM   2511 C  C   . GLY   B 1 23  ? 34.744  -32.415 21.854  1.00 18.02 ? 23  GLY   B C   1 
ATOM   2512 O  O   . GLY   B 1 23  ? 33.704  -32.554 21.244  1.00 21.11 ? 23  GLY   B O   1 
ATOM   2513 N  N   . THR   B 1 24  ? 34.860  -31.604 22.931  1.00 18.01 ? 24  THR   B N   1 
ATOM   2514 C  CA  . THR   B 1 24  ? 33.751  -30.755 23.330  1.00 19.72 ? 24  THR   B CA  1 
ATOM   2515 C  C   . THR   B 1 24  ? 34.029  -29.295 22.955  1.00 17.58 ? 24  THR   B C   1 
ATOM   2516 O  O   . THR   B 1 24  ? 33.164  -28.437 23.173  1.00 23.59 ? 24  THR   B O   1 
ATOM   2517 C  CB  . THR   B 1 24  ? 33.436  -30.875 24.840  1.00 22.89 ? 24  THR   B CB  1 
ATOM   2518 O  OG1 . THR   B 1 24  ? 34.636  -30.517 25.532  1.00 23.63 ? 24  THR   B OG1 1 
ATOM   2519 C  CG2 . THR   B 1 24  ? 32.970  -32.267 25.216  1.00 26.19 ? 24  THR   B CG2 1 
ATOM   2520 N  N   . THR   B 1 25  ? 35.206  -29.000 22.415  1.00 18.16 ? 25  THR   B N   1 
ATOM   2521 C  CA  . THR   B 1 25  ? 35.552  -27.616 22.121  1.00 18.11 ? 25  THR   B CA  1 
ATOM   2522 C  C   . THR   B 1 25  ? 34.769  -27.235 20.862  1.00 18.55 ? 25  THR   B C   1 
ATOM   2523 O  O   . THR   B 1 25  ? 34.871  -27.918 19.846  1.00 15.24 ? 25  THR   B O   1 
ATOM   2524 C  CB  . THR   B 1 25  ? 37.055  -27.375 21.996  1.00 19.28 ? 25  THR   B CB  1 
ATOM   2525 O  OG1 . THR   B 1 25  ? 37.756  -27.855 23.156  1.00 19.95 ? 25  THR   B OG1 1 
ATOM   2526 C  CG2 . THR   B 1 25  ? 37.397  -25.904 21.799  1.00 18.67 ? 25  THR   B CG2 1 
ATOM   2527 N  N   . THR   B 1 26  ? 33.998  -26.148 20.910  1.00 17.99 ? 26  THR   B N   1 
ATOM   2528 C  CA  . THR   B 1 26  ? 33.178  -25.844 19.758  1.00 19.32 ? 26  THR   B CA  1 
ATOM   2529 C  C   . THR   B 1 26  ? 33.237  -24.347 19.469  1.00 16.95 ? 26  THR   B C   1 
ATOM   2530 O  O   . THR   B 1 26  ? 33.322  -23.535 20.392  1.00 17.98 ? 26  THR   B O   1 
ATOM   2531 C  CB  . THR   B 1 26  ? 31.771  -26.394 19.989  1.00 25.00 ? 26  THR   B CB  1 
ATOM   2532 O  OG1 . THR   B 1 26  ? 31.012  -26.266 18.788  1.00 27.28 ? 26  THR   B OG1 1 
ATOM   2533 C  CG2 . THR   B 1 26  ? 31.045  -25.666 21.095  1.00 28.99 ? 26  THR   B CG2 1 
ATOM   2534 N  N   . LEU   B 1 27  ? 33.108  -23.981 18.186  1.00 13.43 ? 27  LEU   B N   1 
ATOM   2535 C  CA  . LEU   B 1 27  ? 33.101  -22.566 17.822  1.00 11.52 ? 27  LEU   B CA  1 
ATOM   2536 C  C   . LEU   B 1 27  ? 32.536  -22.416 16.403  1.00 10.56 ? 27  LEU   B C   1 
ATOM   2537 O  O   . LEU   B 1 27  ? 32.048  -23.388 15.809  1.00 10.18 ? 27  LEU   B O   1 
ATOM   2538 C  CB  . LEU   B 1 27  ? 34.486  -21.943 18.007  1.00 12.20 ? 27  LEU   B CB  1 
ATOM   2539 C  CG  . LEU   B 1 27  ? 35.732  -22.687 17.511  1.00 12.24 ? 27  LEU   B CG  1 
ATOM   2540 C  CD1 . LEU   B 1 27  ? 35.616  -22.992 16.004  1.00 11.28 ? 27  LEU   B CD1 1 
ATOM   2541 C  CD2 . LEU   B 1 27  ? 37.018  -21.919 17.785  1.00 13.01 ? 27  LEU   B CD2 1 
ATOM   2542 N  N   . ASN   B 1 28  ? 32.550  -21.190 15.879  1.00 9.25  ? 28  ASN   B N   1 
ATOM   2543 C  CA  . ASN   B 1 28  ? 31.986  -20.931 14.563  1.00 8.62  ? 28  ASN   B CA  1 
ATOM   2544 C  C   . ASN   B 1 28  ? 33.070  -21.020 13.491  1.00 8.06  ? 28  ASN   B C   1 
ATOM   2545 O  O   . ASN   B 1 28  ? 34.240  -20.679 13.743  1.00 9.16  ? 28  ASN   B O   1 
ATOM   2546 C  CB  . ASN   B 1 28  ? 31.396  -19.512 14.533  1.00 9.45  ? 28  ASN   B CB  1 
ATOM   2547 C  CG  . ASN   B 1 28  ? 30.326  -19.388 15.604  1.00 11.95 ? 28  ASN   B CG  1 
ATOM   2548 O  OD1 . ASN   B 1 28  ? 29.227  -19.911 15.444  1.00 13.03 ? 28  ASN   B OD1 1 
ATOM   2549 N  ND2 . ASN   B 1 28  ? 30.646  -18.693 16.683  1.00 14.68 ? 28  ASN   B ND2 1 
ATOM   2550 N  N   . GLY   B 1 29  ? 32.664  -21.470 12.307  1.00 7.45  ? 29  GLY   B N   1 
ATOM   2551 C  CA  . GLY   B 1 29  ? 33.520  -21.380 11.133  1.00 8.40  ? 29  GLY   B CA  1 
ATOM   2552 C  C   . GLY   B 1 29  ? 32.825  -20.821 9.900   1.00 8.98  ? 29  GLY   B C   1 
ATOM   2553 O  O   . GLY   B 1 29  ? 31.606  -20.648 9.895   1.00 9.93  ? 29  GLY   B O   1 
ATOM   2554 N  N   . LEU   B 1 30  ? 33.643  -20.559 8.876   1.00 8.66  ? 30  LEU   B N   1 
ATOM   2555 C  CA  . LEU   B 1 30  ? 33.206  -19.928 7.635   1.00 8.79  ? 30  LEU   B CA  1 
ATOM   2556 C  C   . LEU   B 1 30  ? 33.427  -20.892 6.484   1.00 8.13  ? 30  LEU   B C   1 
ATOM   2557 O  O   . LEU   B 1 30  ? 34.566  -21.262 6.192   1.00 7.67  ? 30  LEU   B O   1 
ATOM   2558 C  CB  . LEU   B 1 30  ? 34.018  -18.649 7.472   1.00 10.52 ? 30  LEU   B CB  1 
ATOM   2559 C  CG  . LEU   B 1 30  ? 33.627  -17.739 6.313   1.00 10.64 ? 30  LEU   B CG  1 
ATOM   2560 C  CD1 . LEU   B 1 30  ? 32.248  -17.080 6.526   1.00 11.18 ? 30  LEU   B CD1 1 
ATOM   2561 C  CD2 . LEU   B 1 30  ? 34.666  -16.680 6.101   1.00 11.24 ? 30  LEU   B CD2 1 
ATOM   2562 N  N   . TRP   B 1 31  ? 32.334  -21.231 5.803   1.00 7.81  ? 31  TRP   B N   1 
ATOM   2563 C  CA  . TRP   B 1 31  ? 32.335  -22.203 4.723   1.00 7.39  ? 31  TRP   B CA  1 
ATOM   2564 C  C   . TRP   B 1 31  ? 32.264  -21.512 3.374   1.00 7.33  ? 31  TRP   B C   1 
ATOM   2565 O  O   . TRP   B 1 31  ? 31.204  -21.006 2.989   1.00 8.42  ? 31  TRP   B O   1 
ATOM   2566 C  CB  . TRP   B 1 31  ? 31.169  -23.190 4.943   1.00 7.68  ? 31  TRP   B CB  1 
ATOM   2567 C  CG  . TRP   B 1 31  ? 31.006  -24.328 3.944   1.00 8.16  ? 31  TRP   B CG  1 
ATOM   2568 C  CD1 . TRP   B 1 31  ? 31.925  -24.937 3.137   1.00 8.85  ? 31  TRP   B CD1 1 
ATOM   2569 C  CD2 . TRP   B 1 31  ? 29.754  -24.994 3.678   1.00 8.38  ? 31  TRP   B CD2 1 
ATOM   2570 N  NE1 . TRP   B 1 31  ? 31.338  -25.912 2.368   1.00 8.32  ? 31  TRP   B NE1 1 
ATOM   2571 C  CE2 . TRP   B 1 31  ? 30.024  -26.001 2.715   1.00 9.13  ? 31  TRP   B CE2 1 
ATOM   2572 C  CE3 . TRP   B 1 31  ? 28.452  -24.882 4.200   1.00 9.63  ? 31  TRP   B CE3 1 
ATOM   2573 C  CZ2 . TRP   B 1 31  ? 29.018  -26.822 2.219   1.00 10.25 ? 31  TRP   B CZ2 1 
ATOM   2574 C  CZ3 . TRP   B 1 31  ? 27.472  -25.739 3.744   1.00 10.54 ? 31  TRP   B CZ3 1 
ATOM   2575 C  CH2 . TRP   B 1 31  ? 27.743  -26.643 2.710   1.00 9.53  ? 31  TRP   B CH2 1 
ATOM   2576 N  N   . LEU   B 1 32  ? 33.385  -21.531 2.646   1.00 7.56  ? 32  LEU   B N   1 
ATOM   2577 C  CA  . LEU   B 1 32  ? 33.485  -20.892 1.329   1.00 8.14  ? 32  LEU   B CA  1 
ATOM   2578 C  C   . LEU   B 1 32  ? 34.001  -21.923 0.347   1.00 7.49  ? 32  LEU   B C   1 
ATOM   2579 O  O   . LEU   B 1 32  ? 35.055  -22.504 0.581   1.00 8.28  ? 32  LEU   B O   1 
ATOM   2580 C  CB  . LEU   B 1 32  ? 34.432  -19.682 1.392   1.00 8.55  ? 32  LEU   B CB  1 
ATOM   2581 C  CG  . LEU   B 1 32  ? 34.005  -18.598 2.368   1.00 8.94  ? 32  LEU   B CG  1 
ATOM   2582 C  CD1 . LEU   B 1 32  ? 35.157  -17.632 2.599   1.00 9.36  ? 32  LEU   B CD1 1 
ATOM   2583 C  CD2 . LEU   B 1 32  ? 32.772  -17.845 1.868   1.00 9.68  ? 32  LEU   B CD2 1 
ATOM   2584 N  N   . ASP   B 1 33  ? 33.289  -22.111 -0.784  1.00 8.50  ? 33  ASP   B N   1 
ATOM   2585 C  CA  . ASP   B 1 33  ? 33.617  -23.216 -1.686  1.00 10.55 ? 33  ASP   B CA  1 
ATOM   2586 C  C   . ASP   B 1 33  ? 33.739  -24.494 -0.852  1.00 9.90  ? 33  ASP   B C   1 
ATOM   2587 O  O   . ASP   B 1 33  ? 32.830  -24.781 -0.067  1.00 10.55 ? 33  ASP   B O   1 
ATOM   2588 C  CB  . ASP   B 1 33  ? 34.836  -22.873 -2.555  1.00 12.69 ? 33  ASP   B CB  1 
ATOM   2589 C  CG  . ASP   B 1 33  ? 34.556  -21.654 -3.422  1.00 14.96 ? 33  ASP   B CG  1 
ATOM   2590 O  OD1 . ASP   B 1 33  ? 33.485  -21.619 -4.065  1.00 18.54 ? 33  ASP   B OD1 1 
ATOM   2591 O  OD2 . ASP   B 1 33  ? 35.357  -20.710 -3.382  1.00 16.83 ? 33  ASP   B OD2 1 
ATOM   2592 N  N   . ASP   B 1 34  ? 34.840  -25.264 -0.989  1.00 10.06 ? 34  ASP   B N   1 
ATOM   2593 C  CA  . ASP   B 1 34  ? 34.965  -26.523 -0.257  1.00 11.34 ? 34  ASP   B CA  1 
ATOM   2594 C  C   . ASP   B 1 34  ? 35.952  -26.395 0.901   1.00 10.01 ? 34  ASP   B C   1 
ATOM   2595 O  O   . ASP   B 1 34  ? 36.544  -27.383 1.307   1.00 10.68 ? 34  ASP   B O   1 
ATOM   2596 C  CB  . ASP   B 1 34  ? 35.350  -27.660 -1.186  1.00 13.81 ? 34  ASP   B CB  1 
ATOM   2597 C  CG  . ASP   B 1 34  ? 36.674  -27.459 -1.877  1.00 15.62 ? 34  ASP   B CG  1 
ATOM   2598 O  OD1 . ASP   B 1 34  ? 37.214  -26.358 -1.805  1.00 15.27 ? 34  ASP   B OD1 1 
ATOM   2599 O  OD2 . ASP   B 1 34  ? 37.183  -28.464 -2.401  1.00 18.36 ? 34  ASP   B OD2 1 
ATOM   2600 N  N   . VAL   B 1 35  ? 36.063  -25.206 1.523   1.00 9.00  ? 35  VAL   B N   1 
ATOM   2601 C  CA  . VAL   B 1 35  ? 36.944  -25.052 2.672   1.00 9.59  ? 35  VAL   B CA  1 
ATOM   2602 C  C   . VAL   B 1 35  ? 36.189  -24.374 3.810   1.00 8.93  ? 35  VAL   B C   1 
ATOM   2603 O  O   . VAL   B 1 35  ? 35.437  -23.440 3.564   1.00 8.99  ? 35  VAL   B O   1 
ATOM   2604 C  CB  . VAL   B 1 35  ? 38.195  -24.212 2.350   1.00 11.14 ? 35  VAL   B CB  1 
ATOM   2605 C  CG1 . VAL   B 1 35  ? 39.103  -24.033 3.577   1.00 10.81 ? 35  VAL   B CG1 1 
ATOM   2606 C  CG2 . VAL   B 1 35  ? 38.924  -24.823 1.173   1.00 12.04 ? 35  VAL   B CG2 1 
ATOM   2607 N  N   . VAL   B 1 36  ? 36.400  -24.861 5.024   1.00 8.44  ? 36  VAL   B N   1 
ATOM   2608 C  CA  . VAL   B 1 36  ? 35.925  -24.203 6.227   1.00 8.21  ? 36  VAL   B CA  1 
ATOM   2609 C  C   . VAL   B 1 36  ? 37.110  -23.599 6.967   1.00 8.20  ? 36  VAL   B C   1 
ATOM   2610 O  O   . VAL   B 1 36  ? 38.117  -24.257 7.235   1.00 8.50  ? 36  VAL   B O   1 
ATOM   2611 C  CB  . VAL   B 1 36  ? 35.136  -25.180 7.129   1.00 8.13  ? 36  VAL   B CB  1 
ATOM   2612 C  CG1 . VAL   B 1 36  ? 34.831  -24.580 8.500   1.00 9.17  ? 36  VAL   B CG1 1 
ATOM   2613 C  CG2 . VAL   B 1 36  ? 33.879  -25.621 6.416   1.00 9.08  ? 36  VAL   B CG2 1 
ATOM   2614 N  N   . TYR   B 1 37  ? 36.988  -22.305 7.267   1.00 8.40  ? 37  TYR   B N   1 
ATOM   2615 C  CA  . TYR   B 1 37  ? 37.983  -21.564 8.015   1.00 8.31  ? 37  TYR   B CA  1 
ATOM   2616 C  C   . TYR   B 1 37  ? 37.495  -21.335 9.454   1.00 8.65  ? 37  TYR   B C   1 
ATOM   2617 O  O   . TYR   B 1 37  ? 36.363  -20.895 9.685   1.00 8.31  ? 37  TYR   B O   1 
ATOM   2618 C  CB  . TYR   B 1 37  ? 38.206  -20.194 7.359   1.00 9.44  ? 37  TYR   B CB  1 
ATOM   2619 C  CG  . TYR   B 1 37  ? 38.568  -20.247 5.891   1.00 9.75  ? 37  TYR   B CG  1 
ATOM   2620 C  CD1 . TYR   B 1 37  ? 37.592  -20.453 4.920   1.00 9.83  ? 37  TYR   B CD1 1 
ATOM   2621 C  CD2 . TYR   B 1 37  ? 39.887  -20.133 5.469   1.00 11.28 ? 37  TYR   B CD2 1 
ATOM   2622 C  CE1 . TYR   B 1 37  ? 37.942  -20.617 3.585   1.00 10.55 ? 37  TYR   B CE1 1 
ATOM   2623 C  CE2 . TYR   B 1 37  ? 40.221  -20.224 4.126   1.00 11.13 ? 37  TYR   B CE2 1 
ATOM   2624 C  CZ  . TYR   B 1 37  ? 39.260  -20.491 3.184   1.00 11.32 ? 37  TYR   B CZ  1 
ATOM   2625 O  OH  . TYR   B 1 37  ? 39.595  -20.645 1.836   1.00 11.72 ? 37  TYR   B OH  1 
ATOM   2626 N  N   . CYS   B 1 38  ? 38.362  -21.550 10.448  1.00 9.09  ? 38  CYS   B N   1 
ATOM   2627 C  CA  . CYS   B 1 38  ? 37.970  -21.294 11.822  1.00 10.12 ? 38  CYS   B CA  1 
ATOM   2628 C  C   . CYS   B 1 38  ? 39.211  -21.074 12.672  1.00 10.18 ? 38  CYS   B C   1 
ATOM   2629 O  O   . CYS   B 1 38  ? 40.317  -21.343 12.193  1.00 10.37 ? 38  CYS   B O   1 
ATOM   2630 C  CB  . CYS   B 1 38  ? 37.125  -22.410 12.407  1.00 10.19 ? 38  CYS   B CB  1 
ATOM   2631 S  SG  . CYS   B 1 38  ? 38.069  -23.927 12.726  1.00 13.59 ? 38  CYS   B SG  1 
ATOM   2632 N  N   . PRO   B 1 39  ? 39.064  -20.494 13.881  1.00 10.08 ? 39  PRO   B N   1 
ATOM   2633 C  CA  . PRO   B 1 39  ? 40.206  -20.309 14.773  1.00 9.90  ? 39  PRO   B CA  1 
ATOM   2634 C  C   . PRO   B 1 39  ? 40.832  -21.663 15.110  1.00 11.19 ? 39  PRO   B C   1 
ATOM   2635 O  O   . PRO   B 1 39  ? 40.108  -22.597 15.450  1.00 11.21 ? 39  PRO   B O   1 
ATOM   2636 C  CB  . PRO   B 1 39  ? 39.624  -19.614 16.004  1.00 10.69 ? 39  PRO   B CB  1 
ATOM   2637 C  CG  . PRO   B 1 39  ? 38.381  -18.928 15.441  1.00 10.92 ? 39  PRO   B CG  1 
ATOM   2638 C  CD  . PRO   B 1 39  ? 37.828  -19.955 14.466  1.00 10.34 ? 39  PRO   B CD  1 
ATOM   2639 N  N   . ARG   B 1 40  ? 42.166  -21.721 15.110  1.00 12.10 ? 40  ARG   B N   1 
ATOM   2640 C  CA  . ARG   B 1 40  ? 42.833  -22.993 15.400  1.00 14.03 ? 40  ARG   B CA  1 
ATOM   2641 C  C   . ARG   B 1 40  ? 42.677  -23.374 16.864  1.00 13.59 ? 40  ARG   B C   1 
ATOM   2642 O  O   . ARG   B 1 40  ? 42.834  -24.550 17.220  1.00 14.29 ? 40  ARG   B O   1 
ATOM   2643 C  CB  . ARG   B 1 40  ? 44.300  -22.922 14.973  1.00 15.43 ? 40  ARG   B CB  1 
ATOM   2644 C  CG  . ARG   B 1 40  ? 45.134  -21.974 15.806  1.00 16.22 ? 40  ARG   B CG  1 
ATOM   2645 C  CD  . ARG   B 1 40  ? 46.599  -22.044 15.440  1.00 18.02 ? 40  ARG   B CD  1 
ATOM   2646 N  NE  . ARG   B 1 40  ? 47.331  -21.073 16.230  1.00 21.65 ? 40  ARG   B NE  1 
ATOM   2647 C  CZ  . ARG   B 1 40  ? 48.660  -20.927 16.214  1.00 21.02 ? 40  ARG   B CZ  1 
ATOM   2648 N  NH1 . ARG   B 1 40  ? 49.398  -21.679 15.426  1.00 21.28 ? 40  ARG   B NH1 1 
ATOM   2649 N  NH2 . ARG   B 1 40  ? 49.248  -20.094 17.060  1.00 21.64 ? 40  ARG   B NH2 1 
ATOM   2650 N  N   . HIS   B 1 41  ? 42.237  -22.421 17.729  1.00 13.73 ? 41  HIS   B N   1 
ATOM   2651 C  CA  . HIS   B 1 41  ? 41.919  -22.673 19.122  1.00 14.72 ? 41  HIS   B CA  1 
ATOM   2652 C  C   . HIS   B 1 41  ? 40.966  -23.854 19.326  1.00 14.03 ? 41  HIS   B C   1 
ATOM   2653 O  O   . HIS   B 1 41  ? 40.904  -24.453 20.398  1.00 16.27 ? 41  HIS   B O   1 
ATOM   2654 C  CB  . HIS   B 1 41  ? 41.415  -21.387 19.820  1.00 16.86 ? 41  HIS   B CB  1 
ATOM   2655 C  CG  . HIS   B 1 41  ? 41.600  -21.327 21.295  1.00 20.53 ? 41  HIS   B CG  1 
ATOM   2656 N  ND1 . HIS   B 1 41  ? 42.867  -21.230 21.830  1.00 22.96 ? 41  HIS   B ND1 1 
ATOM   2657 C  CD2 . HIS   B 1 41  ? 40.756  -21.274 22.345  1.00 22.39 ? 41  HIS   B CD2 1 
ATOM   2658 C  CE1 . HIS   B 1 41  ? 42.773  -21.147 23.165  1.00 23.89 ? 41  HIS   B CE1 1 
ATOM   2659 N  NE2 . HIS   B 1 41  ? 41.508  -21.162 23.495  1.00 22.34 ? 41  HIS   B NE2 1 
ATOM   2660 N  N   . VAL   B 1 42  ? 40.139  -24.193 18.330  1.00 12.80 ? 42  VAL   B N   1 
ATOM   2661 C  CA  . VAL   B 1 42  ? 39.222  -25.298 18.467  1.00 12.50 ? 42  VAL   B CA  1 
ATOM   2662 C  C   . VAL   B 1 42  ? 39.934  -26.620 18.815  1.00 12.29 ? 42  VAL   B C   1 
ATOM   2663 O  O   . VAL   B 1 42  ? 39.258  -27.480 19.352  1.00 14.40 ? 42  VAL   B O   1 
ATOM   2664 C  CB  . VAL   B 1 42  ? 38.361  -25.430 17.195  1.00 11.87 ? 42  VAL   B CB  1 
ATOM   2665 C  CG1 . VAL   B 1 42  ? 39.136  -25.935 15.994  1.00 12.59 ? 42  VAL   B CG1 1 
ATOM   2666 C  CG2 . VAL   B 1 42  ? 37.080  -26.230 17.385  1.00 12.38 ? 42  VAL   B CG2 1 
ATOM   2667 N  N   . ILE   B 1 43  ? 41.204  -26.800 18.459  1.00 16.18 ? 43  ILE   B N   1 
ATOM   2668 C  CA  . ILE   B 1 43  ? 41.873  -28.096 18.668  1.00 18.93 ? 43  ILE   B CA  1 
ATOM   2669 C  C   . ILE   B 1 43  ? 42.382  -28.231 20.108  1.00 23.02 ? 43  ILE   B C   1 
ATOM   2670 O  O   . ILE   B 1 43  ? 42.883  -29.286 20.503  1.00 22.65 ? 43  ILE   B O   1 
ATOM   2671 C  CB  . ILE   B 1 43  ? 43.027  -28.322 17.674  1.00 18.66 ? 43  ILE   B CB  1 
ATOM   2672 C  CG1 . ILE   B 1 43  ? 44.240  -27.413 17.896  1.00 18.86 ? 43  ILE   B CG1 1 
ATOM   2673 C  CG2 . ILE   B 1 43  ? 42.520  -28.256 16.250  1.00 18.75 ? 43  ILE   B CG2 1 
ATOM   2674 C  CD1 . ILE   B 1 43  ? 45.359  -27.641 16.897  1.00 20.29 ? 43  ILE   B CD1 1 
ATOM   2675 N  N   A CYS   B 1 44  ? 42.256  -27.140 20.873  0.50 17.81 ? 44  CYS   B N   1 
ATOM   2676 N  N   B CYS   B 1 44  ? 42.299  -27.155 20.876  0.50 22.93 ? 44  CYS   B N   1 
ATOM   2677 C  CA  A CYS   B 1 44  ? 42.633  -27.104 22.275  0.50 17.94 ? 44  CYS   B CA  1 
ATOM   2678 C  CA  B CYS   B 1 44  ? 42.854  -27.143 22.213  0.50 27.90 ? 44  CYS   B CA  1 
ATOM   2679 C  C   A CYS   B 1 44  ? 41.619  -27.821 23.147  0.50 20.73 ? 44  CYS   B C   1 
ATOM   2680 C  C   B CYS   B 1 44  ? 41.799  -27.655 23.207  0.50 26.24 ? 44  CYS   B C   1 
ATOM   2681 O  O   A CYS   B 1 44  ? 40.416  -27.572 23.105  0.50 19.91 ? 44  CYS   B O   1 
ATOM   2682 O  O   B CYS   B 1 44  ? 40.675  -27.161 23.210  0.50 28.98 ? 44  CYS   B O   1 
ATOM   2683 C  CB  A CYS   B 1 44  ? 42.803  -25.664 22.758  0.50 13.98 ? 44  CYS   B CB  1 
ATOM   2684 C  CB  B CYS   B 1 44  ? 43.389  -25.728 22.438  0.50 27.30 ? 44  CYS   B CB  1 
ATOM   2685 S  SG  A CYS   B 1 44  ? 44.233  -24.897 22.008  0.50 11.08 ? 44  CYS   B SG  1 
ATOM   2686 S  SG  B CYS   B 1 44  ? 42.831  -25.023 23.993  0.50 47.79 ? 44  CYS   B SG  1 
ATOM   2687 N  N   . THR   B 1 45  ? 42.134  -28.705 24.005  1.00 24.81 ? 45  THR   B N   1 
ATOM   2688 C  CA  . THR   B 1 45  ? 41.327  -29.135 25.131  1.00 23.36 ? 45  THR   B CA  1 
ATOM   2689 C  C   . THR   B 1 45  ? 41.430  -28.037 26.181  1.00 24.50 ? 45  THR   B C   1 
ATOM   2690 O  O   . THR   B 1 45  ? 42.317  -27.208 26.089  1.00 25.24 ? 45  THR   B O   1 
ATOM   2691 C  CB  . THR   B 1 45  ? 41.812  -30.456 25.765  1.00 26.73 ? 45  THR   B CB  1 
ATOM   2692 O  OG1 . THR   B 1 45  ? 43.115  -30.198 26.304  1.00 24.91 ? 45  THR   B OG1 1 
ATOM   2693 C  CG2 . THR   B 1 45  ? 41.868  -31.606 24.780  1.00 26.13 ? 45  THR   B CG2 1 
ATOM   2694 N  N   . SER   B 1 46  ? 40.589  -28.067 27.211  1.00 28.10 ? 46  SER   B N   1 
ATOM   2695 C  CA  . SER   B 1 46  ? 40.701  -27.094 28.294  1.00 34.84 ? 46  SER   B CA  1 
ATOM   2696 C  C   . SER   B 1 46  ? 42.117  -26.972 28.869  1.00 32.93 ? 46  SER   B C   1 
ATOM   2697 O  O   . SER   B 1 46  ? 42.509  -25.879 29.266  1.00 34.83 ? 46  SER   B O   1 
ATOM   2698 C  CB  . SER   B 1 46  ? 39.718  -27.396 29.384  1.00 39.52 ? 46  SER   B CB  1 
ATOM   2699 O  OG  . SER   B 1 46  ? 38.416  -27.507 28.838  1.00 42.78 ? 46  SER   B OG  1 
ATOM   2700 N  N   . GLU   B 1 47  ? 42.888  -28.065 28.927  1.00 29.82 ? 47  GLU   B N   1 
ATOM   2701 C  CA  . GLU   B 1 47  ? 44.209  -28.042 29.555  1.00 35.27 ? 47  GLU   B CA  1 
ATOM   2702 C  C   . GLU   B 1 47  ? 45.273  -27.457 28.631  1.00 31.54 ? 47  GLU   B C   1 
ATOM   2703 O  O   . GLU   B 1 47  ? 46.375  -27.128 29.077  1.00 36.19 ? 47  GLU   B O   1 
ATOM   2704 C  CB  . GLU   B 1 47  ? 44.634  -29.460 29.958  1.00 37.55 ? 47  GLU   B CB  1 
ATOM   2705 C  CG  . GLU   B 1 47  ? 43.770  -30.051 31.060  1.00 39.94 ? 47  GLU   B CG  1 
ATOM   2706 C  CD  . GLU   B 1 47  ? 42.290  -30.230 30.743  1.00 41.27 ? 47  GLU   B CD  1 
ATOM   2707 O  OE1 . GLU   B 1 47  ? 41.488  -29.644 31.482  1.00 45.88 ? 47  GLU   B OE1 1 
ATOM   2708 O  OE2 . GLU   B 1 47  ? 41.941  -30.934 29.738  1.00 41.75 ? 47  GLU   B OE2 1 
ATOM   2709 N  N   . ASP   B 1 48  ? 44.949  -27.383 27.338  1.00 23.38 ? 48  ASP   B N   1 
ATOM   2710 C  CA  . ASP   B 1 48  ? 45.809  -26.844 26.301  1.00 27.06 ? 48  ASP   B CA  1 
ATOM   2711 C  C   . ASP   B 1 48  ? 45.674  -25.323 26.164  1.00 23.83 ? 48  ASP   B C   1 
ATOM   2712 O  O   . ASP   B 1 48  ? 46.574  -24.694 25.628  1.00 29.44 ? 48  ASP   B O   1 
ATOM   2713 C  CB  . ASP   B 1 48  ? 45.475  -27.502 24.953  1.00 28.17 ? 48  ASP   B CB  1 
ATOM   2714 C  CG  . ASP   B 1 48  ? 45.674  -29.014 24.943  1.00 34.46 ? 48  ASP   B CG  1 
ATOM   2715 O  OD1 . ASP   B 1 48  ? 46.692  -29.437 25.498  1.00 33.25 ? 48  ASP   B OD1 1 
ATOM   2716 O  OD2 . ASP   B 1 48  ? 44.813  -29.755 24.360  1.00 28.86 ? 48  ASP   B OD2 1 
ATOM   2717 N  N   . MET   B 1 49  ? 44.580  -24.760 26.660  1.00 24.58 ? 49  MET   B N   1 
ATOM   2718 C  CA  . MET   B 1 49  ? 44.143  -23.417 26.271  1.00 29.78 ? 49  MET   B CA  1 
ATOM   2719 C  C   . MET   B 1 49  ? 45.066  -22.328 26.820  1.00 34.16 ? 49  MET   B C   1 
ATOM   2720 O  O   . MET   B 1 49  ? 45.224  -21.303 26.175  1.00 30.98 ? 49  MET   B O   1 
ATOM   2721 C  CB  . MET   B 1 49  ? 42.708  -23.155 26.750  1.00 28.65 ? 49  MET   B CB  1 
ATOM   2722 C  CG  . MET   B 1 49  ? 41.638  -23.687 25.799  1.00 27.75 ? 49  MET   B CG  1 
ATOM   2723 S  SD  . MET   B 1 49  ? 39.970  -23.733 26.439  0.90 26.23 ? 49  MET   B SD  1 
ATOM   2724 C  CE  . MET   B 1 49  ? 39.078  -24.585 25.138  1.00 29.97 ? 49  MET   B CE  1 
ATOM   2725 N  N   . LEU   B 1 50  ? 45.691  -22.580 27.984  1.00 39.63 ? 50  LEU   B N   1 
ATOM   2726 C  CA  . LEU   B 1 50  ? 46.578  -21.629 28.646  1.00 40.65 ? 50  LEU   B CA  1 
ATOM   2727 C  C   . LEU   B 1 50  ? 47.838  -21.413 27.809  1.00 38.61 ? 50  LEU   B C   1 
ATOM   2728 O  O   . LEU   B 1 50  ? 48.256  -20.280 27.550  1.00 39.41 ? 50  LEU   B O   1 
ATOM   2729 C  CB  . LEU   B 1 50  ? 46.937  -22.166 30.035  1.00 46.93 ? 50  LEU   B CB  1 
ATOM   2730 C  CG  . LEU   B 1 50  ? 45.809  -22.860 30.817  1.00 58.93 ? 50  LEU   B CG  1 
ATOM   2731 C  CD1 . LEU   B 1 50  ? 46.319  -23.447 32.135  1.00 61.03 ? 50  LEU   B CD1 1 
ATOM   2732 C  CD2 . LEU   B 1 50  ? 44.641  -21.920 31.083  1.00 61.96 ? 50  LEU   B CD2 1 
ATOM   2733 N  N   . ASN   B 1 51  ? 48.455  -22.518 27.389  1.00 35.09 ? 51  ASN   B N   1 
ATOM   2734 C  CA  . ASN   B 1 51  ? 49.739  -22.448 26.728  1.00 37.20 ? 51  ASN   B CA  1 
ATOM   2735 C  C   . ASN   B 1 51  ? 49.825  -23.573 25.697  1.00 35.15 ? 51  ASN   B C   1 
ATOM   2736 O  O   . ASN   B 1 51  ? 50.538  -24.555 25.875  1.00 30.80 ? 51  ASN   B O   1 
ATOM   2737 C  CB  . ASN   B 1 51  ? 50.873  -22.485 27.757  1.00 41.32 ? 51  ASN   B CB  1 
ATOM   2738 C  CG  . ASN   B 1 51  ? 52.229  -22.406 27.104  1.00 49.06 ? 51  ASN   B CG  1 
ATOM   2739 O  OD1 . ASN   B 1 51  ? 52.569  -21.398 26.485  1.00 54.71 ? 51  ASN   B OD1 1 
ATOM   2740 N  ND2 . ASN   B 1 51  ? 52.995  -23.480 27.209  1.00 57.16 ? 51  ASN   B ND2 1 
ATOM   2741 N  N   . PRO   B 1 52  ? 49.072  -23.464 24.583  1.00 31.78 ? 52  PRO   B N   1 
ATOM   2742 C  CA  . PRO   B 1 52  ? 49.031  -24.526 23.584  1.00 28.86 ? 52  PRO   B CA  1 
ATOM   2743 C  C   . PRO   B 1 52  ? 50.293  -24.671 22.755  1.00 27.38 ? 52  PRO   B C   1 
ATOM   2744 O  O   . PRO   B 1 52  ? 50.930  -23.699 22.354  1.00 26.11 ? 52  PRO   B O   1 
ATOM   2745 C  CB  . PRO   B 1 52  ? 47.884  -24.120 22.639  1.00 28.91 ? 52  PRO   B CB  1 
ATOM   2746 C  CG  . PRO   B 1 52  ? 47.679  -22.636 22.891  1.00 28.49 ? 52  PRO   B CG  1 
ATOM   2747 C  CD  . PRO   B 1 52  ? 48.157  -22.356 24.293  1.00 27.86 ? 52  PRO   B CD  1 
ATOM   2748 N  N   . ASN   B 1 53  ? 50.611  -25.932 22.438  1.00 28.08 ? 53  ASN   B N   1 
ATOM   2749 C  CA  . ASN   B 1 53  ? 51.570  -26.200 21.397  1.00 31.71 ? 53  ASN   B CA  1 
ATOM   2750 C  C   . ASN   B 1 53  ? 50.780  -26.645 20.175  1.00 27.72 ? 53  ASN   B C   1 
ATOM   2751 O  O   . ASN   B 1 53  ? 50.447  -27.823 20.066  1.00 26.08 ? 53  ASN   B O   1 
ATOM   2752 C  CB  . ASN   B 1 53  ? 52.575  -27.278 21.808  1.00 32.27 ? 53  ASN   B CB  1 
ATOM   2753 C  CG  . ASN   B 1 53  ? 53.686  -27.433 20.804  1.00 34.53 ? 53  ASN   B CG  1 
ATOM   2754 O  OD1 . ASN   B 1 53  ? 53.497  -27.344 19.592  1.00 34.62 ? 53  ASN   B OD1 1 
ATOM   2755 N  ND2 . ASN   B 1 53  ? 54.881  -27.658 21.313  1.00 37.40 ? 53  ASN   B ND2 1 
ATOM   2756 N  N   . TYR   B 1 54  ? 50.467  -25.694 19.290  1.00 27.62 ? 54  TYR   B N   1 
ATOM   2757 C  CA  . TYR   B 1 54  ? 49.492  -25.976 18.245  1.00 26.36 ? 54  TYR   B CA  1 
ATOM   2758 C  C   . TYR   B 1 54  ? 50.065  -26.954 17.213  1.00 27.09 ? 54  TYR   B C   1 
ATOM   2759 O  O   . TYR   B 1 54  ? 49.319  -27.761 16.654  1.00 25.19 ? 54  TYR   B O   1 
ATOM   2760 C  CB  . TYR   B 1 54  ? 49.066  -24.693 17.528  1.00 23.75 ? 54  TYR   B CB  1 
ATOM   2761 C  CG  . TYR   B 1 54  ? 48.065  -23.873 18.320  1.00 20.73 ? 54  TYR   B CG  1 
ATOM   2762 C  CD1 . TYR   B 1 54  ? 46.763  -24.303 18.488  1.00 20.80 ? 54  TYR   B CD1 1 
ATOM   2763 C  CD2 . TYR   B 1 54  ? 48.432  -22.660 18.898  1.00 23.90 ? 54  TYR   B CD2 1 
ATOM   2764 C  CE1 . TYR   B 1 54  ? 45.846  -23.574 19.222  1.00 19.36 ? 54  TYR   B CE1 1 
ATOM   2765 C  CE2 . TYR   B 1 54  ? 47.509  -21.901 19.597  1.00 21.10 ? 54  TYR   B CE2 1 
ATOM   2766 C  CZ  . TYR   B 1 54  ? 46.207  -22.341 19.736  1.00 19.44 ? 54  TYR   B CZ  1 
ATOM   2767 O  OH  . TYR   B 1 54  ? 45.283  -21.628 20.444  1.00 19.28 ? 54  TYR   B OH  1 
ATOM   2768 N  N   . GLU   B 1 55  ? 51.370  -26.854 16.927  1.00 27.55 ? 55  GLU   B N   1 
ATOM   2769 C  CA  . GLU   B 1 55  ? 52.001  -27.832 16.043  1.00 30.73 ? 55  GLU   B CA  1 
ATOM   2770 C  C   . GLU   B 1 55  ? 51.818  -29.223 16.657  1.00 28.37 ? 55  GLU   B C   1 
ATOM   2771 O  O   . GLU   B 1 55  ? 51.453  -30.166 15.953  1.00 34.31 ? 55  GLU   B O   1 
ATOM   2772 C  CB  . GLU   B 1 55  ? 53.475  -27.526 15.765  1.00 33.15 ? 55  GLU   B CB  1 
ATOM   2773 C  CG  . GLU   B 1 55  ? 53.681  -26.337 14.849  1.00 38.91 ? 55  GLU   B CG  1 
ATOM   2774 C  CD  . GLU   B 1 55  ? 53.554  -24.985 15.538  1.00 44.01 ? 55  GLU   B CD  1 
ATOM   2775 O  OE1 . GLU   B 1 55  ? 53.481  -24.962 16.797  1.00 40.23 ? 55  GLU   B OE1 1 
ATOM   2776 O  OE2 . GLU   B 1 55  ? 53.509  -23.954 14.821  1.00 47.65 ? 55  GLU   B OE2 1 
ATOM   2777 N  N   . ASP   B 1 56  ? 52.009  -29.347 17.970  1.00 30.17 ? 56  ASP   B N   1 
ATOM   2778 C  CA  . ASP   B 1 56  ? 51.937  -30.651 18.617  1.00 33.41 ? 56  ASP   B CA  1 
ATOM   2779 C  C   . ASP   B 1 56  ? 50.515  -31.184 18.619  1.00 31.64 ? 56  ASP   B C   1 
ATOM   2780 O  O   . ASP   B 1 56  ? 50.296  -32.387 18.457  1.00 29.85 ? 56  ASP   B O   1 
ATOM   2781 C  CB  . ASP   B 1 56  ? 52.378  -30.637 20.084  1.00 41.72 ? 56  ASP   B CB  1 
ATOM   2782 C  CG  . ASP   B 1 56  ? 52.382  -32.021 20.715  1.00 47.61 ? 56  ASP   B CG  1 
ATOM   2783 O  OD1 . ASP   B 1 56  ? 53.086  -32.898 20.190  1.00 59.42 ? 56  ASP   B OD1 1 
ATOM   2784 O  OD2 . ASP   B 1 56  ? 51.662  -32.221 21.708  1.00 54.18 ? 56  ASP   B OD2 1 
ATOM   2785 N  N   . LEU   B 1 57  ? 49.561  -30.285 18.888  1.00 23.80 ? 57  LEU   B N   1 
ATOM   2786 C  CA  . LEU   B 1 57  ? 48.161  -30.647 18.989  1.00 24.13 ? 57  LEU   B CA  1 
ATOM   2787 C  C   . LEU   B 1 57  ? 47.661  -31.082 17.616  1.00 24.77 ? 57  LEU   B C   1 
ATOM   2788 O  O   . LEU   B 1 57  ? 46.895  -32.037 17.522  1.00 26.59 ? 57  LEU   B O   1 
ATOM   2789 C  CB  . LEU   B 1 57  ? 47.393  -29.428 19.502  1.00 27.55 ? 57  LEU   B CB  1 
ATOM   2790 C  CG  . LEU   B 1 57  ? 47.635  -29.104 20.969  1.00 31.45 ? 57  LEU   B CG  1 
ATOM   2791 C  CD1 . LEU   B 1 57  ? 46.988  -27.771 21.349  1.00 29.89 ? 57  LEU   B CD1 1 
ATOM   2792 C  CD2 . LEU   B 1 57  ? 47.102  -30.219 21.855  1.00 32.74 ? 57  LEU   B CD2 1 
ATOM   2793 N  N   . LEU   B 1 58  ? 48.125  -30.398 16.566  1.00 24.46 ? 58  LEU   B N   1 
ATOM   2794 C  CA  . LEU   B 1 58  ? 47.596  -30.626 15.226  1.00 26.51 ? 58  LEU   B CA  1 
ATOM   2795 C  C   . LEU   B 1 58  ? 48.129  -31.935 14.632  1.00 28.32 ? 58  LEU   B C   1 
ATOM   2796 O  O   . LEU   B 1 58  ? 47.379  -32.670 13.989  1.00 27.68 ? 58  LEU   B O   1 
ATOM   2797 C  CB  . LEU   B 1 58  ? 47.896  -29.431 14.321  1.00 25.46 ? 58  LEU   B CB  1 
ATOM   2798 C  CG  . LEU   B 1 58  ? 47.184  -29.495 12.971  1.00 30.86 ? 58  LEU   B CG  1 
ATOM   2799 C  CD1 . LEU   B 1 58  ? 45.676  -29.466 13.146  1.00 31.70 ? 58  LEU   B CD1 1 
ATOM   2800 C  CD2 . LEU   B 1 58  ? 47.648  -28.383 12.045  1.00 33.85 ? 58  LEU   B CD2 1 
ATOM   2801 N  N   . ILE   B 1 59  ? 49.383  -32.297 14.913  1.00 31.09 ? 59  ILE   B N   1 
ATOM   2802 C  CA  . ILE   B 1 59  ? 49.945  -33.505 14.308  1.00 33.48 ? 59  ILE   B CA  1 
ATOM   2803 C  C   . ILE   B 1 59  ? 49.285  -34.750 14.899  1.00 29.85 ? 59  ILE   B C   1 
ATOM   2804 O  O   . ILE   B 1 59  ? 49.343  -35.817 14.294  1.00 27.10 ? 59  ILE   B O   1 
ATOM   2805 C  CB  . ILE   B 1 59  ? 51.489  -33.567 14.376  1.00 38.96 ? 59  ILE   B CB  1 
ATOM   2806 C  CG1 . ILE   B 1 59  ? 52.015  -33.788 15.793  1.00 45.14 ? 59  ILE   B CG1 1 
ATOM   2807 C  CG2 . ILE   B 1 59  ? 52.130  -32.372 13.690  1.00 42.21 ? 59  ILE   B CG2 1 
ATOM   2808 C  CD1 . ILE   B 1 59  ? 52.171  -35.256 16.162  1.00 48.57 ? 59  ILE   B CD1 1 
ATOM   2809 N  N   . ARG   B 1 60  ? 48.618  -34.618 16.049  1.00 26.97 ? 60  ARG   B N   1 
ATOM   2810 C  CA  . ARG   B 1 60  ? 47.881  -35.720 16.642  1.00 27.80 ? 60  ARG   B CA  1 
ATOM   2811 C  C   . ARG   B 1 60  ? 46.451  -35.813 16.107  1.00 26.23 ? 60  ARG   B C   1 
ATOM   2812 O  O   . ARG   B 1 60  ? 45.700  -36.687 16.501  1.00 29.73 ? 60  ARG   B O   1 
ATOM   2813 C  CB  . ARG   B 1 60  ? 47.807  -35.537 18.159  1.00 34.43 ? 60  ARG   B CB  1 
ATOM   2814 C  CG  . ARG   B 1 60  ? 49.175  -35.412 18.809  1.00 44.18 ? 60  ARG   B CG  1 
ATOM   2815 C  CD  . ARG   B 1 60  ? 49.224  -35.794 20.273  1.00 55.75 ? 60  ARG   B CD  1 
ATOM   2816 N  NE  . ARG   B 1 60  ? 50.619  -35.841 20.692  1.00 67.80 ? 60  ARG   B NE  1 
ATOM   2817 C  CZ  . ARG   B 1 60  ? 51.075  -36.432 21.793  1.00 85.18 ? 60  ARG   B CZ  1 
ATOM   2818 N  NH1 . ARG   B 1 60  ? 50.256  -37.077 22.608  1.00 86.83 ? 60  ARG   B NH1 1 
ATOM   2819 N  NH2 . ARG   B 1 60  ? 52.368  -36.379 22.072  1.00 96.42 ? 60  ARG   B NH2 1 
ATOM   2820 N  N   . LYS   B 1 61  ? 46.064  -34.887 15.235  1.00 24.91 ? 61  LYS   B N   1 
ATOM   2821 C  CA  . LYS   B 1 61  ? 44.717  -34.875 14.698  1.00 24.35 ? 61  LYS   B CA  1 
ATOM   2822 C  C   . LYS   B 1 61  ? 44.705  -35.500 13.318  1.00 21.49 ? 61  LYS   B C   1 
ATOM   2823 O  O   . LYS   B 1 61  ? 45.669  -35.387 12.553  1.00 23.79 ? 61  LYS   B O   1 
ATOM   2824 C  CB  . LYS   B 1 61  ? 44.188  -33.445 14.544  1.00 28.96 ? 61  LYS   B CB  1 
ATOM   2825 C  CG  . LYS   B 1 61  ? 43.823  -32.702 15.826  1.00 33.52 ? 61  LYS   B CG  1 
ATOM   2826 C  CD  . LYS   B 1 61  ? 42.947  -33.468 16.778  1.00 37.65 ? 61  LYS   B CD  1 
ATOM   2827 C  CE  . LYS   B 1 61  ? 42.110  -32.589 17.692  1.00 44.76 ? 61  LYS   B CE  1 
ATOM   2828 N  NZ  . LYS   B 1 61  ? 40.743  -32.330 17.151  1.00 48.51 ? 61  LYS   B NZ  1 
ATOM   2829 N  N   A SER   B 1 62  ? 43.572  -36.111 12.971  0.50 20.30 ? 62  SER   B N   1 
ATOM   2830 N  N   B SER   B 1 62  ? 43.549  -36.095 13.006  0.50 19.81 ? 62  SER   B N   1 
ATOM   2831 C  CA  A SER   B 1 62  ? 43.293  -36.455 11.598  0.50 18.74 ? 62  SER   B CA  1 
ATOM   2832 C  CA  B SER   B 1 62  ? 43.211  -36.596 11.694  0.50 17.80 ? 62  SER   B CA  1 
ATOM   2833 C  C   A SER   B 1 62  ? 41.941  -35.868 11.213  0.50 16.88 ? 62  SER   B C   1 
ATOM   2834 C  C   B SER   B 1 62  ? 41.913  -35.927 11.236  0.50 16.47 ? 62  SER   B C   1 
ATOM   2835 O  O   A SER   B 1 62  ? 41.223  -35.327 12.056  0.50 18.02 ? 62  SER   B O   1 
ATOM   2836 O  O   B SER   B 1 62  ? 41.195  -35.360 12.062  0.50 17.54 ? 62  SER   B O   1 
ATOM   2837 C  CB  A SER   B 1 62  ? 43.311  -37.951 11.386  0.50 21.40 ? 62  SER   B CB  1 
ATOM   2838 C  CB  B SER   B 1 62  ? 43.072  -38.110 11.733  0.50 19.44 ? 62  SER   B CB  1 
ATOM   2839 O  OG  A SER   B 1 62  ? 42.180  -38.553 11.993  0.50 23.18 ? 62  SER   B OG  1 
ATOM   2840 O  OG  B SER   B 1 62  ? 44.300  -38.746 12.088  0.50 19.52 ? 62  SER   B OG  1 
ATOM   2841 N  N   . ASN   B 1 63  ? 41.601  -36.039 9.943   1.00 15.86 ? 63  ASN   B N   1 
ATOM   2842 C  CA  . ASN   B 1 63  ? 40.375  -35.495 9.370   1.00 15.81 ? 63  ASN   B CA  1 
ATOM   2843 C  C   . ASN   B 1 63  ? 39.161  -35.943 10.190  1.00 15.13 ? 63  ASN   B C   1 
ATOM   2844 O  O   . ASN   B 1 63  ? 38.211  -35.178 10.428  1.00 14.42 ? 63  ASN   B O   1 
ATOM   2845 C  CB  . ASN   B 1 63  ? 40.239  -35.965 7.919   1.00 14.35 ? 63  ASN   B CB  1 
ATOM   2846 C  CG  . ASN   B 1 63  ? 41.218  -35.300 6.968   1.00 15.90 ? 63  ASN   B CG  1 
ATOM   2847 O  OD1 . ASN   B 1 63  ? 41.743  -34.214 7.222   1.00 14.21 ? 63  ASN   B OD1 1 
ATOM   2848 N  ND2 . ASN   B 1 63  ? 41.478  -35.981 5.882   1.00 16.16 ? 63  ASN   B ND2 1 
ATOM   2849 N  N   . HIS   B 1 64  ? 39.180  -37.224 10.630  1.00 15.11 ? 64  HIS   B N   1 
ATOM   2850 C  CA  . HIS   B 1 64  ? 38.020  -37.795 11.294  1.00 18.32 ? 64  HIS   B CA  1 
ATOM   2851 C  C   . HIS   B 1 64  ? 37.790  -37.228 12.708  1.00 18.19 ? 64  HIS   B C   1 
ATOM   2852 O  O   . HIS   B 1 64  ? 36.751  -37.527 13.273  1.00 18.00 ? 64  HIS   B O   1 
ATOM   2853 C  CB  . HIS   B 1 64  ? 38.086  -39.338 11.240  1.00 22.41 ? 64  HIS   B CB  1 
ATOM   2854 C  CG  . HIS   B 1 64  ? 39.085  -39.883 12.175  1.00 28.69 ? 64  HIS   B CG  1 
ATOM   2855 N  ND1 . HIS   B 1 64  ? 40.331  -40.329 11.778  1.00 38.62 ? 64  HIS   B ND1 1 
ATOM   2856 C  CD2 . HIS   B 1 64  ? 39.074  -39.953 13.507  1.00 35.38 ? 64  HIS   B CD2 1 
ATOM   2857 C  CE1 . HIS   B 1 64  ? 41.007  -40.722 12.856  1.00 37.68 ? 64  HIS   B CE1 1 
ATOM   2858 N  NE2 . HIS   B 1 64  ? 40.259  -40.510 13.917  1.00 39.45 ? 64  HIS   B NE2 1 
ATOM   2859 N  N   . ASN   B 1 65  ? 38.690  -36.374 13.247  1.00 15.56 ? 65  ASN   B N   1 
ATOM   2860 C  CA  . ASN   B 1 65  ? 38.567  -35.789 14.579  1.00 15.69 ? 65  ASN   B CA  1 
ATOM   2861 C  C   . ASN   B 1 65  ? 37.726  -34.495 14.569  1.00 14.95 ? 65  ASN   B C   1 
ATOM   2862 O  O   . ASN   B 1 65  ? 37.408  -33.947 15.630  1.00 15.00 ? 65  ASN   B O   1 
ATOM   2863 C  CB  . ASN   B 1 65  ? 39.954  -35.507 15.196  1.00 18.02 ? 65  ASN   B CB  1 
ATOM   2864 C  CG  . ASN   B 1 65  ? 40.757  -36.778 15.439  1.00 20.04 ? 65  ASN   B CG  1 
ATOM   2865 O  OD1 . ASN   B 1 65  ? 41.900  -36.914 15.007  1.00 20.38 ? 65  ASN   B OD1 1 
ATOM   2866 N  ND2 . ASN   B 1 65  ? 40.146  -37.742 16.101  1.00 24.55 ? 65  ASN   B ND2 1 
ATOM   2867 N  N   . PHE   B 1 66  ? 37.432  -33.952 13.377  1.00 12.95 ? 66  PHE   B N   1 
ATOM   2868 C  CA  . PHE   B 1 66  ? 36.767  -32.666 13.232  1.00 12.48 ? 66  PHE   B CA  1 
ATOM   2869 C  C   . PHE   B 1 66  ? 35.307  -32.865 12.846  1.00 11.94 ? 66  PHE   B C   1 
ATOM   2870 O  O   . PHE   B 1 66  ? 35.003  -33.474 11.820  1.00 11.54 ? 66  PHE   B O   1 
ATOM   2871 C  CB  . PHE   B 1 66  ? 37.456  -31.854 12.131  1.00 12.97 ? 66  PHE   B CB  1 
ATOM   2872 C  CG  . PHE   B 1 66  ? 38.876  -31.506 12.450  1.00 14.85 ? 66  PHE   B CG  1 
ATOM   2873 C  CD1 . PHE   B 1 66  ? 39.159  -30.434 13.280  1.00 16.31 ? 66  PHE   B CD1 1 
ATOM   2874 C  CD2 . PHE   B 1 66  ? 39.927  -32.210 11.883  1.00 15.75 ? 66  PHE   B CD2 1 
ATOM   2875 C  CE1 . PHE   B 1 66  ? 40.477  -30.105 13.557  1.00 18.31 ? 66  PHE   B CE1 1 
ATOM   2876 C  CE2 . PHE   B 1 66  ? 41.246  -31.875 12.147  1.00 18.03 ? 66  PHE   B CE2 1 
ATOM   2877 C  CZ  . PHE   B 1 66  ? 41.513  -30.820 13.003  1.00 17.72 ? 66  PHE   B CZ  1 
ATOM   2878 N  N   . LEU   B 1 67  ? 34.398  -32.324 13.664  1.00 11.87 ? 67  LEU   B N   1 
ATOM   2879 C  CA  . LEU   B 1 67  ? 32.979  -32.299 13.378  1.00 11.59 ? 67  LEU   B CA  1 
ATOM   2880 C  C   . LEU   B 1 67  ? 32.584  -30.916 12.870  1.00 11.29 ? 67  LEU   B C   1 
ATOM   2881 O  O   . LEU   B 1 67  ? 32.629  -29.952 13.659  1.00 12.55 ? 67  LEU   B O   1 
ATOM   2882 C  CB  . LEU   B 1 67  ? 32.200  -32.581 14.670  1.00 13.06 ? 67  LEU   B CB  1 
ATOM   2883 C  CG  . LEU   B 1 67  ? 30.686  -32.561 14.517  1.00 13.55 ? 67  LEU   B CG  1 
ATOM   2884 C  CD1 . LEU   B 1 67  ? 30.219  -33.616 13.526  1.00 15.92 ? 67  LEU   B CD1 1 
ATOM   2885 C  CD2 . LEU   B 1 67  ? 29.966  -32.720 15.866  1.00 13.93 ? 67  LEU   B CD2 1 
ATOM   2886 N  N   . VAL   B 1 68  ? 32.231  -30.848 11.593  1.00 10.40 ? 68  VAL   B N   1 
ATOM   2887 C  CA  . VAL   B 1 68  ? 31.757  -29.625 10.944  1.00 11.22 ? 68  VAL   B CA  1 
ATOM   2888 C  C   . VAL   B 1 68  ? 30.281  -29.828 10.631  1.00 12.28 ? 68  VAL   B C   1 
ATOM   2889 O  O   . VAL   B 1 68  ? 29.921  -30.831 10.032  1.00 11.08 ? 68  VAL   B O   1 
ATOM   2890 C  CB  . VAL   B 1 68  ? 32.548  -29.339 9.650   1.00 12.38 ? 68  VAL   B CB  1 
ATOM   2891 C  CG1 . VAL   B 1 68  ? 32.034  -28.098 8.955   1.00 13.39 ? 68  VAL   B CG1 1 
ATOM   2892 C  CG2 . VAL   B 1 68  ? 34.032  -29.220 9.888   1.00 13.04 ? 68  VAL   B CG2 1 
ATOM   2893 N  N   . GLN   B 1 69  ? 29.425  -28.879 11.041  1.00 11.99 ? 69  GLN   B N   1 
ATOM   2894 C  CA  . GLN   B 1 69  ? 27.999  -28.990 10.844  1.00 11.45 ? 69  GLN   B CA  1 
ATOM   2895 C  C   . GLN   B 1 69  ? 27.423  -27.698 10.289  1.00 11.26 ? 69  GLN   B C   1 
ATOM   2896 O  O   . GLN   B 1 69  ? 27.696  -26.631 10.831  1.00 11.11 ? 69  GLN   B O   1 
ATOM   2897 C  CB  . GLN   B 1 69  ? 27.338  -29.328 12.183  1.00 13.81 ? 69  GLN   B CB  1 
ATOM   2898 C  CG  . GLN   B 1 69  ? 27.721  -30.700 12.721  1.00 15.12 ? 69  GLN   B CG  1 
ATOM   2899 C  CD  . GLN   B 1 69  ? 27.328  -30.851 14.170  1.00 15.85 ? 69  GLN   B CD  1 
ATOM   2900 O  OE1 . GLN   B 1 69  ? 27.730  -30.105 15.063  1.00 16.33 ? 69  GLN   B OE1 1 
ATOM   2901 N  NE2 . GLN   B 1 69  ? 26.438  -31.786 14.378  1.00 17.99 ? 69  GLN   B NE2 1 
ATOM   2902 N  N   . ALA   B 1 70  ? 26.646  -27.815 9.222   1.00 12.05 ? 70  ALA   B N   1 
ATOM   2903 C  CA  . ALA   B 1 70  ? 25.821  -26.742 8.696   1.00 14.52 ? 70  ALA   B CA  1 
ATOM   2904 C  C   . ALA   B 1 70  ? 24.416  -26.943 9.275   1.00 17.18 ? 70  ALA   B C   1 
ATOM   2905 O  O   . ALA   B 1 70  ? 23.721  -27.915 8.931   1.00 15.38 ? 70  ALA   B O   1 
ATOM   2906 C  CB  . ALA   B 1 70  ? 25.835  -26.768 7.185   1.00 16.26 ? 70  ALA   B CB  1 
ATOM   2907 N  N   . GLY   B 1 71  ? 24.080  -26.152 10.299  1.00 18.64 ? 71  GLY   B N   1 
ATOM   2908 C  CA  . GLY   B 1 71  ? 22.982  -26.552 11.160  1.00 21.56 ? 71  GLY   B CA  1 
ATOM   2909 C  C   . GLY   B 1 71  ? 23.231  -27.933 11.775  1.00 20.38 ? 71  GLY   B C   1 
ATOM   2910 O  O   . GLY   B 1 71  ? 24.192  -28.111 12.502  1.00 23.55 ? 71  GLY   B O   1 
ATOM   2911 N  N   . ASN   B 1 72  ? 22.377  -28.910 11.507  1.00 20.68 ? 72  ASN   B N   1 
ATOM   2912 C  CA  . ASN   B 1 72  ? 22.582  -30.252 12.050  1.00 24.43 ? 72  ASN   B CA  1 
ATOM   2913 C  C   . ASN   B 1 72  ? 23.157  -31.210 11.011  1.00 22.30 ? 72  ASN   B C   1 
ATOM   2914 O  O   . ASN   B 1 72  ? 23.275  -32.414 11.272  1.00 21.52 ? 72  ASN   B O   1 
ATOM   2915 C  CB  . ASN   B 1 72  ? 21.299  -30.907 12.571  1.00 31.20 ? 72  ASN   B CB  1 
ATOM   2916 C  CG  . ASN   B 1 72  ? 20.860  -30.374 13.921  1.00 37.01 ? 72  ASN   B CG  1 
ATOM   2917 O  OD1 . ASN   B 1 72  ? 21.684  -29.991 14.752  1.00 44.24 ? 72  ASN   B OD1 1 
ATOM   2918 N  ND2 . ASN   B 1 72  ? 19.558  -30.332 14.129  1.00 40.82 ? 72  ASN   B ND2 1 
ATOM   2919 N  N   . VAL   B 1 73  ? 23.542  -30.678 9.840   1.00 18.85 ? 73  VAL   B N   1 
ATOM   2920 C  CA  . VAL   B 1 73  ? 24.017  -31.521 8.769   1.00 15.90 ? 73  VAL   B CA  1 
ATOM   2921 C  C   . VAL   B 1 73  ? 25.543  -31.576 8.842   1.00 14.96 ? 73  VAL   B C   1 
ATOM   2922 O  O   . VAL   B 1 73  ? 26.204  -30.547 8.751   1.00 13.58 ? 73  VAL   B O   1 
ATOM   2923 C  CB  . VAL   B 1 73  ? 23.541  -30.964 7.428   1.00 19.44 ? 73  VAL   B CB  1 
ATOM   2924 C  CG1 . VAL   B 1 73  ? 24.141  -31.722 6.268   1.00 21.33 ? 73  VAL   B CG1 1 
ATOM   2925 C  CG2 . VAL   B 1 73  ? 22.016  -30.945 7.334   1.00 22.11 ? 73  VAL   B CG2 1 
ATOM   2926 N  N   . GLN   B 1 74  ? 26.103  -32.776 8.988   1.00 12.57 ? 74  GLN   B N   1 
ATOM   2927 C  CA  . GLN   B 1 74  ? 27.546  -32.932 9.066   1.00 13.29 ? 74  GLN   B CA  1 
ATOM   2928 C  C   . GLN   B 1 74  ? 28.162  -32.780 7.679   1.00 12.31 ? 74  GLN   B C   1 
ATOM   2929 O  O   . GLN   B 1 74  ? 27.665  -33.360 6.719   1.00 14.08 ? 74  GLN   B O   1 
ATOM   2930 C  CB  . GLN   B 1 74  ? 27.975  -34.306 9.589   1.00 14.23 ? 74  GLN   B CB  1 
ATOM   2931 C  CG  . GLN   B 1 74  ? 29.474  -34.495 9.609   1.00 16.28 ? 74  GLN   B CG  1 
ATOM   2932 C  CD  . GLN   B 1 74  ? 29.871  -35.772 10.306  1.00 20.01 ? 74  GLN   B CD  1 
ATOM   2933 O  OE1 . GLN   B 1 74  ? 29.020  -36.608 10.615  1.00 22.38 ? 74  GLN   B OE1 1 
ATOM   2934 N  NE2 . GLN   B 1 74  ? 31.157  -35.937 10.536  1.00 17.64 ? 74  GLN   B NE2 1 
ATOM   2935 N  N   . LEU   B 1 75  ? 29.249  -32.022 7.586   1.00 12.15 ? 75  LEU   B N   1 
ATOM   2936 C  CA  . LEU   B 1 75  ? 30.063  -31.967 6.372   1.00 12.70 ? 75  LEU   B CA  1 
ATOM   2937 C  C   . LEU   B 1 75  ? 31.339  -32.781 6.617   1.00 13.01 ? 75  LEU   B C   1 
ATOM   2938 O  O   . LEU   B 1 75  ? 32.124  -32.427 7.496   1.00 14.61 ? 75  LEU   B O   1 
ATOM   2939 C  CB  . LEU   B 1 75  ? 30.418  -30.503 6.085   1.00 14.04 ? 75  LEU   B CB  1 
ATOM   2940 C  CG  . LEU   B 1 75  ? 29.271  -29.531 5.895   1.00 18.07 ? 75  LEU   B CG  1 
ATOM   2941 C  CD1 . LEU   B 1 75  ? 29.853  -28.147 5.594   1.00 19.84 ? 75  LEU   B CD1 1 
ATOM   2942 C  CD2 . LEU   B 1 75  ? 28.330  -29.978 4.783   1.00 21.83 ? 75  LEU   B CD2 1 
ATOM   2943 N  N   . ARG   B 1 76  ? 31.609  -33.788 5.784   1.00 14.13 ? 76  ARG   B N   1 
ATOM   2944 C  CA  . ARG   B 1 76  ? 32.772  -34.645 5.971   1.00 15.24 ? 76  ARG   B CA  1 
ATOM   2945 C  C   . ARG   B 1 76  ? 34.063  -33.893 5.621   1.00 13.78 ? 76  ARG   B C   1 
ATOM   2946 O  O   . ARG   B 1 76  ? 34.221  -33.344 4.516   1.00 13.37 ? 76  ARG   B O   1 
ATOM   2947 C  CB  . ARG   B 1 76  ? 32.671  -35.890 5.082   1.00 21.09 ? 76  ARG   B CB  1 
ATOM   2948 C  CG  . ARG   B 1 76  ? 33.859  -36.843 5.177   1.00 23.14 ? 76  ARG   B CG  1 
ATOM   2949 C  CD  . ARG   B 1 76  ? 33.679  -38.140 4.383   1.00 30.01 ? 76  ARG   B CD  1 
ATOM   2950 N  NE  . ARG   B 1 76  ? 33.607  -37.904 2.939   1.00 31.54 ? 76  ARG   B NE  1 
ATOM   2951 C  CZ  . ARG   B 1 76  ? 34.546  -38.198 2.036   1.00 37.48 ? 76  ARG   B CZ  1 
ATOM   2952 N  NH1 . ARG   B 1 76  ? 35.626  -38.898 2.370   1.00 36.66 ? 76  ARG   B NH1 1 
ATOM   2953 N  NH2 . ARG   B 1 76  ? 34.370  -37.814 0.774   1.00 33.76 ? 76  ARG   B NH2 1 
ATOM   2954 N  N   . VAL   B 1 77  ? 35.024  -33.958 6.539   1.00 11.82 ? 77  VAL   B N   1 
ATOM   2955 C  CA  . VAL   B 1 77  ? 36.320  -33.314 6.356   1.00 10.84 ? 77  VAL   B CA  1 
ATOM   2956 C  C   . VAL   B 1 77  ? 37.256  -34.256 5.599   1.00 12.74 ? 77  VAL   B C   1 
ATOM   2957 O  O   . VAL   B 1 77  ? 37.407  -35.431 5.996   1.00 13.36 ? 77  VAL   B O   1 
ATOM   2958 C  CB  . VAL   B 1 77  ? 36.889  -32.902 7.714   1.00 11.51 ? 77  VAL   B CB  1 
ATOM   2959 C  CG1 . VAL   B 1 77  ? 38.302  -32.349 7.608   1.00 10.81 ? 77  VAL   B CG1 1 
ATOM   2960 C  CG2 . VAL   B 1 77  ? 35.945  -31.887 8.354   1.00 10.96 ? 77  VAL   B CG2 1 
ATOM   2961 N  N   . ILE   B 1 78  ? 37.903  -33.730 4.567   1.00 11.77 ? 78  ILE   B N   1 
ATOM   2962 C  CA  . ILE   B 1 78  ? 38.758  -34.567 3.727   1.00 12.96 ? 78  ILE   B CA  1 
ATOM   2963 C  C   . ILE   B 1 78  ? 40.193  -34.060 3.700   1.00 15.72 ? 78  ILE   B C   1 
ATOM   2964 O  O   . ILE   B 1 78  ? 41.040  -34.627 2.953   1.00 15.32 ? 78  ILE   B O   1 
ATOM   2965 C  CB  . ILE   B 1 78  ? 38.169  -34.713 2.323   1.00 14.01 ? 78  ILE   B CB  1 
ATOM   2966 C  CG1 . ILE   B 1 78  ? 38.049  -33.391 1.568   1.00 15.68 ? 78  ILE   B CG1 1 
ATOM   2967 C  CG2 . ILE   B 1 78  ? 36.836  -35.438 2.399   1.00 14.93 ? 78  ILE   B CG2 1 
ATOM   2968 C  CD1 . ILE   B 1 78  ? 37.617  -33.527 0.119   1.00 16.78 ? 78  ILE   B CD1 1 
ATOM   2969 N  N   . GLY   B 1 79  ? 40.483  -32.976 4.448   1.00 12.90 ? 79  GLY   B N   1 
ATOM   2970 C  CA  . GLY   B 1 79  ? 41.841  -32.466 4.506   1.00 12.93 ? 79  GLY   B CA  1 
ATOM   2971 C  C   . GLY   B 1 79  ? 41.917  -31.387 5.576   1.00 14.53 ? 79  GLY   B C   1 
ATOM   2972 O  O   . GLY   B 1 79  ? 40.892  -30.807 5.919   1.00 12.27 ? 79  GLY   B O   1 
ATOM   2973 N  N   . HIS   B 1 80  ? 43.092  -31.160 6.155   1.00 13.30 ? 80  HIS   B N   1 
ATOM   2974 C  CA  . HIS   B 1 80  ? 43.177  -30.117 7.172   1.00 14.24 ? 80  HIS   B CA  1 
ATOM   2975 C  C   . HIS   B 1 80  ? 44.566  -29.500 7.127   1.00 16.19 ? 80  HIS   B C   1 
ATOM   2976 O  O   . HIS   B 1 80  ? 45.525  -30.186 6.802   1.00 16.57 ? 80  HIS   B O   1 
ATOM   2977 C  CB  . HIS   B 1 80  ? 42.877  -30.673 8.570   1.00 16.25 ? 80  HIS   B CB  1 
ATOM   2978 C  CG  . HIS   B 1 80  ? 43.854  -31.704 9.071   1.00 19.18 ? 80  HIS   B CG  1 
ATOM   2979 N  ND1 . HIS   B 1 80  ? 43.763  -33.027 8.692   1.00 17.89 ? 80  HIS   B ND1 1 
ATOM   2980 C  CD2 . HIS   B 1 80  ? 44.923  -31.606 9.906   1.00 19.63 ? 80  HIS   B CD2 1 
ATOM   2981 C  CE1 . HIS   B 1 80  ? 44.741  -33.714 9.295   1.00 21.04 ? 80  HIS   B CE1 1 
ATOM   2982 N  NE2 . HIS   B 1 80  ? 45.458  -32.876 10.036  1.00 19.87 ? 80  HIS   B NE2 1 
ATOM   2983 N  N   . SER   B 1 81  ? 44.663  -28.198 7.430   1.00 15.32 ? 81  SER   B N   1 
ATOM   2984 C  CA  . SER   B 1 81  ? 45.958  -27.550 7.549   1.00 16.51 ? 81  SER   B CA  1 
ATOM   2985 C  C   . SER   B 1 81  ? 45.782  -26.299 8.405   1.00 20.02 ? 81  SER   B C   1 
ATOM   2986 O  O   . SER   B 1 81  ? 44.651  -25.925 8.713   1.00 15.12 ? 81  SER   B O   1 
ATOM   2987 C  CB  . SER   B 1 81  ? 46.545  -27.231 6.214   1.00 17.83 ? 81  SER   B CB  1 
ATOM   2988 O  OG  . SER   B 1 81  ? 45.807  -26.248 5.538   1.00 19.84 ? 81  SER   B OG  1 
ATOM   2989 N  N   . MET   B 1 82  ? 46.912  -25.707 8.800   1.00 18.80 ? 82  MET   B N   1 
ATOM   2990 C  CA  . MET   B 1 82  ? 46.892  -24.564 9.693   1.00 20.16 ? 82  MET   B CA  1 
ATOM   2991 C  C   . MET   B 1 82  ? 47.693  -23.483 8.992   1.00 19.79 ? 82  MET   B C   1 
ATOM   2992 O  O   . MET   B 1 82  ? 48.722  -23.772 8.408   1.00 18.60 ? 82  MET   B O   1 
ATOM   2993 C  CB  . MET   B 1 82  ? 47.508  -24.975 11.029  1.00 23.35 ? 82  MET   B CB  1 
ATOM   2994 C  CG  . MET   B 1 82  ? 47.941  -23.877 11.945  1.00 25.37 ? 82  MET   B CG  1 
ATOM   2995 S  SD  . MET   B 1 82  ? 48.314  -24.536 13.575  1.00 26.47 ? 82  MET   B SD  1 
ATOM   2996 C  CE  . MET   B 1 82  ? 49.997  -25.140 13.395  1.00 28.32 ? 82  MET   B CE  1 
ATOM   2997 N  N   . GLN   B 1 83  ? 47.145  -22.279 8.932   1.00 17.05 ? 83  GLN   B N   1 
ATOM   2998 C  CA  . GLN   B 1 83  ? 47.805  -21.143 8.327   1.00 18.00 ? 83  GLN   B CA  1 
ATOM   2999 C  C   . GLN   B 1 83  ? 47.787  -20.066 9.398   1.00 19.02 ? 83  GLN   B C   1 
ATOM   3000 O  O   . GLN   B 1 83  ? 46.701  -19.632 9.760   1.00 16.30 ? 83  GLN   B O   1 
ATOM   3001 C  CB  . GLN   B 1 83  ? 47.115  -20.682 7.044   1.00 18.88 ? 83  GLN   B CB  1 
ATOM   3002 C  CG  . GLN   B 1 83  ? 47.648  -19.359 6.510   1.00 20.97 ? 83  GLN   B CG  1 
ATOM   3003 C  CD  . GLN   B 1 83  ? 46.931  -18.923 5.270   1.00 24.38 ? 83  GLN   B CD  1 
ATOM   3004 O  OE1 . GLN   B 1 83  ? 45.824  -19.373 4.984   1.00 27.23 ? 83  GLN   B OE1 1 
ATOM   3005 N  NE2 . GLN   B 1 83  ? 47.541  -18.030 4.523   1.00 25.84 ? 83  GLN   B NE2 1 
ATOM   3006 N  N   . ASN   B 1 84  ? 48.964  -19.746 9.968   1.00 18.15 ? 84  ASN   B N   1 
ATOM   3007 C  CA  . ASN   B 1 84  ? 49.029  -18.837 11.100  1.00 17.22 ? 84  ASN   B CA  1 
ATOM   3008 C  C   . ASN   B 1 84  ? 48.035  -19.281 12.169  1.00 17.06 ? 84  ASN   B C   1 
ATOM   3009 O  O   . ASN   B 1 84  ? 48.110  -20.412 12.660  1.00 17.43 ? 84  ASN   B O   1 
ATOM   3010 C  CB  . ASN   B 1 84  ? 48.862  -17.406 10.588  1.00 17.65 ? 84  ASN   B CB  1 
ATOM   3011 C  CG  . ASN   B 1 84  ? 49.823  -17.074 9.481   1.00 20.16 ? 84  ASN   B CG  1 
ATOM   3012 O  OD1 . ASN   B 1 84  ? 51.026  -17.258 9.654   1.00 22.03 ? 84  ASN   B OD1 1 
ATOM   3013 N  ND2 . ASN   B 1 84  ? 49.309  -16.568 8.377   1.00 19.46 ? 84  ASN   B ND2 1 
ATOM   3014 N  N   . CYS   B 1 85  ? 47.049  -18.436 12.566  1.00 14.05 ? 85  CYS   B N   1 
ATOM   3015 C  CA  . CYS   B 1 85  ? 46.151  -18.820 13.636  1.00 13.45 ? 85  CYS   B CA  1 
ATOM   3016 C  C   . CYS   B 1 85  ? 44.796  -19.374 13.156  1.00 11.84 ? 85  CYS   B C   1 
ATOM   3017 O  O   . CYS   B 1 85  ? 43.875  -19.510 13.962  1.00 11.90 ? 85  CYS   B O   1 
ATOM   3018 C  CB  . CYS   B 1 85  ? 45.879  -17.669 14.585  1.00 15.81 ? 85  CYS   B CB  1 
ATOM   3019 S  SG  . CYS   B 1 85  ? 47.405  -17.064 15.368  1.00 19.09 ? 85  CYS   B SG  1 
ATOM   3020 N  N   A VAL   B 1 86  ? 44.706  -19.760 11.889  0.44 12.14 ? 86  VAL   B N   1 
ATOM   3021 N  N   B VAL   B 1 86  ? 44.659  -19.631 11.860  0.56 12.23 ? 86  VAL   B N   1 
ATOM   3022 C  CA  A VAL   B 1 86  ? 43.443  -20.219 11.313  0.44 12.36 ? 86  VAL   B CA  1 
ATOM   3023 C  CA  B VAL   B 1 86  ? 43.432  -20.257 11.362  0.56 12.58 ? 86  VAL   B CA  1 
ATOM   3024 C  C   A VAL   B 1 86  ? 43.584  -21.639 10.758  0.44 12.35 ? 86  VAL   B C   1 
ATOM   3025 C  C   B VAL   B 1 86  ? 43.706  -21.719 10.999  0.56 12.40 ? 86  VAL   B C   1 
ATOM   3026 O  O   A VAL   B 1 86  ? 44.489  -21.922 9.957   0.44 12.59 ? 86  VAL   B O   1 
ATOM   3027 O  O   B VAL   B 1 86  ? 44.816  -22.118 10.618  0.56 12.31 ? 86  VAL   B O   1 
ATOM   3028 C  CB  A VAL   B 1 86  ? 42.979  -19.221 10.239  0.44 13.05 ? 86  VAL   B CB  1 
ATOM   3029 C  CB  B VAL   B 1 86  ? 42.767  -19.531 10.173  0.56 13.71 ? 86  VAL   B CB  1 
ATOM   3030 C  CG1 A VAL   B 1 86  ? 42.046  -19.831 9.201   0.44 12.66 ? 86  VAL   B CG1 1 
ATOM   3031 C  CG1 B VAL   B 1 86  ? 42.101  -18.227 10.597  0.56 16.51 ? 86  VAL   B CG1 1 
ATOM   3032 C  CG2 A VAL   B 1 86  ? 42.345  -18.001 10.911  0.44 14.65 ? 86  VAL   B CG2 1 
ATOM   3033 C  CG2 B VAL   B 1 86  ? 43.687  -19.296 8.989   0.56 13.49 ? 86  VAL   B CG2 1 
ATOM   3034 N  N   . LEU   B 1 87  ? 42.642  -22.509 11.181  1.00 12.44 ? 87  LEU   B N   1 
ATOM   3035 C  CA  . LEU   B 1 87  ? 42.508  -23.854 10.674  1.00 13.16 ? 87  LEU   B CA  1 
ATOM   3036 C  C   . LEU   B 1 87  ? 41.662  -23.824 9.394   1.00 13.40 ? 87  LEU   B C   1 
ATOM   3037 O  O   . LEU   B 1 87  ? 40.663  -23.096 9.294   1.00 12.54 ? 87  LEU   B O   1 
ATOM   3038 C  CB  . LEU   B 1 87  ? 41.882  -24.659 11.797  1.00 14.43 ? 87  LEU   B CB  1 
ATOM   3039 C  CG  . LEU   B 1 87  ? 41.683  -26.147 11.614  1.00 17.57 ? 87  LEU   B CG  1 
ATOM   3040 C  CD1 . LEU   B 1 87  ? 43.003  -26.877 11.634  1.00 19.35 ? 87  LEU   B CD1 1 
ATOM   3041 C  CD2 . LEU   B 1 87  ? 40.794  -26.685 12.724  1.00 18.74 ? 87  LEU   B CD2 1 
ATOM   3042 N  N   . LYS   B 1 88  ? 42.141  -24.570 8.402   1.00 11.73 ? 88  LYS   B N   1 
ATOM   3043 C  CA  . LYS   B 1 88  ? 41.476  -24.709 7.123   1.00 11.79 ? 88  LYS   B CA  1 
ATOM   3044 C  C   . LYS   B 1 88  ? 41.079  -26.176 6.983   1.00 12.33 ? 88  LYS   B C   1 
ATOM   3045 O  O   . LYS   B 1 88  ? 41.964  -27.053 6.925   1.00 11.48 ? 88  LYS   B O   1 
ATOM   3046 C  CB  . LYS   B 1 88  ? 42.380  -24.238 6.001   1.00 13.74 ? 88  LYS   B CB  1 
ATOM   3047 C  CG  . LYS   B 1 88  ? 42.603  -22.739 6.021   1.00 15.74 ? 88  LYS   B CG  1 
ATOM   3048 C  CD  . LYS   B 1 88  ? 43.367  -22.271 4.810   1.00 18.95 ? 88  LYS   B CD  1 
ATOM   3049 C  CE  . LYS   B 1 88  ? 44.818  -22.659 4.827   1.00 21.93 ? 88  LYS   B CE  1 
ATOM   3050 N  NZ  . LYS   B 1 88  ? 45.532  -21.988 3.688   1.00 23.89 ? 88  LYS   B NZ  1 
ATOM   3051 N  N   . LEU   B 1 89  ? 39.778  -26.433 6.999   1.00 10.10 ? 89  LEU   B N   1 
ATOM   3052 C  CA  . LEU   B 1 89  ? 39.315  -27.799 6.803   1.00 10.85 ? 89  LEU   B CA  1 
ATOM   3053 C  C   . LEU   B 1 89  ? 38.713  -27.938 5.415   1.00 10.51 ? 89  LEU   B C   1 
ATOM   3054 O  O   . LEU   B 1 89  ? 37.685  -27.326 5.066   1.00 10.42 ? 89  LEU   B O   1 
ATOM   3055 C  CB  . LEU   B 1 89  ? 38.313  -28.102 7.915   1.00 12.21 ? 89  LEU   B CB  1 
ATOM   3056 C  CG  . LEU   B 1 89  ? 38.835  -27.872 9.326   1.00 12.64 ? 89  LEU   B CG  1 
ATOM   3057 C  CD1 . LEU   B 1 89  ? 37.698  -28.076 10.303  1.00 13.91 ? 89  LEU   B CD1 1 
ATOM   3058 C  CD2 . LEU   B 1 89  ? 39.992  -28.806 9.642   1.00 13.90 ? 89  LEU   B CD2 1 
ATOM   3059 N  N   . LYS   B 1 90  ? 39.297  -28.851 4.623   1.00 10.37 ? 90  LYS   B N   1 
ATOM   3060 C  CA  . LYS   B 1 90  ? 38.704  -29.128 3.336   1.00 11.02 ? 90  LYS   B CA  1 
ATOM   3061 C  C   . LYS   B 1 90  ? 37.553  -30.103 3.547   1.00 9.91  ? 90  LYS   B C   1 
ATOM   3062 O  O   . LYS   B 1 90  ? 37.683  -31.078 4.281   1.00 10.99 ? 90  LYS   B O   1 
ATOM   3063 C  CB  . LYS   B 1 90  ? 39.771  -29.665 2.390   1.00 13.47 ? 90  LYS   B CB  1 
ATOM   3064 C  CG  . LYS   B 1 90  ? 39.253  -29.873 0.979   1.00 16.97 ? 90  LYS   B CG  1 
ATOM   3065 C  CD  . LYS   B 1 90  ? 40.299  -30.563 0.118   1.00 21.30 ? 90  LYS   B CD  1 
ATOM   3066 C  CE  . LYS   B 1 90  ? 39.962  -30.549 -1.356  1.00 29.39 ? 90  LYS   B CE  1 
ATOM   3067 N  NZ  . LYS   B 1 90  ? 41.097  -31.079 -2.162  1.00 33.45 ? 90  LYS   B NZ  1 
ATOM   3068 N  N   . VAL   B 1 91  ? 36.405  -29.807 2.954   1.00 10.77 ? 91  VAL   B N   1 
ATOM   3069 C  CA  . VAL   B 1 91  ? 35.205  -30.639 3.103   1.00 11.04 ? 91  VAL   B CA  1 
ATOM   3070 C  C   . VAL   B 1 91  ? 34.797  -31.165 1.735   1.00 11.19 ? 91  VAL   B C   1 
ATOM   3071 O  O   . VAL   B 1 91  ? 35.261  -30.666 0.689   1.00 11.16 ? 91  VAL   B O   1 
ATOM   3072 C  CB  . VAL   B 1 91  ? 34.027  -29.885 3.781   1.00 10.98 ? 91  VAL   B CB  1 
ATOM   3073 C  CG1 . VAL   B 1 91  ? 34.340  -29.632 5.234   1.00 11.29 ? 91  VAL   B CG1 1 
ATOM   3074 C  CG2 . VAL   B 1 91  ? 33.694  -28.594 3.044   1.00 10.10 ? 91  VAL   B CG2 1 
ATOM   3075 N  N   . ASP   B 1 92  ? 33.927  -32.183 1.713   1.00 12.99 ? 92  ASP   B N   1 
ATOM   3076 C  CA  . ASP   B 1 92  ? 33.622  -32.857 0.457   1.00 13.79 ? 92  ASP   B CA  1 
ATOM   3077 C  C   . ASP   B 1 92  ? 32.480  -32.193 -0.315  1.00 14.18 ? 92  ASP   B C   1 
ATOM   3078 O  O   . ASP   B 1 92  ? 32.195  -32.635 -1.433  1.00 15.67 ? 92  ASP   B O   1 
ATOM   3079 C  CB  . ASP   B 1 92  ? 33.317  -34.338 0.687   1.00 18.11 ? 92  ASP   B CB  1 
ATOM   3080 C  CG  . ASP   B 1 92  ? 32.004  -34.644 1.382   1.00 20.35 ? 92  ASP   B CG  1 
ATOM   3081 O  OD1 . ASP   B 1 92  ? 31.290  -33.678 1.820   1.00 19.57 ? 92  ASP   B OD1 1 
ATOM   3082 O  OD2 . ASP   B 1 92  ? 31.725  -35.897 1.561   1.00 23.12 ? 92  ASP   B OD2 1 
ATOM   3083 N  N   . THR   B 1 93  ? 31.967  -31.037 0.163   1.00 12.02 ? 93  THR   B N   1 
ATOM   3084 C  CA  . THR   B 1 93  ? 30.846  -30.323 -0.445  1.00 11.03 ? 93  THR   B CA  1 
ATOM   3085 C  C   . THR   B 1 93  ? 31.184  -28.839 -0.596  1.00 10.20 ? 93  THR   B C   1 
ATOM   3086 O  O   . THR   B 1 93  ? 31.590  -28.212 0.396   1.00 10.95 ? 93  THR   B O   1 
ATOM   3087 C  CB  . THR   B 1 93  ? 29.579  -30.459 0.419   1.00 11.93 ? 93  THR   B CB  1 
ATOM   3088 O  OG1 . THR   B 1 93  ? 29.361  -31.844 0.637   1.00 13.90 ? 93  THR   B OG1 1 
ATOM   3089 C  CG2 . THR   B 1 93  ? 28.341  -29.848 -0.203  1.00 11.76 ? 93  THR   B CG2 1 
ATOM   3090 N  N   . ALA   B 1 94  ? 31.079  -28.352 -1.816  1.00 10.14 ? 94  ALA   B N   1 
ATOM   3091 C  CA  . ALA   B 1 94  ? 31.248  -26.945 -2.127  1.00 11.08 ? 94  ALA   B CA  1 
ATOM   3092 C  C   . ALA   B 1 94  ? 29.977  -26.213 -1.699  1.00 10.65 ? 94  ALA   B C   1 
ATOM   3093 O  O   . ALA   B 1 94  ? 28.872  -26.615 -2.059  1.00 11.83 ? 94  ALA   B O   1 
ATOM   3094 C  CB  . ALA   B 1 94  ? 31.551  -26.714 -3.596  1.00 13.24 ? 94  ALA   B CB  1 
ATOM   3095 N  N   . ASN   B 1 95  ? 30.130  -25.150 -0.891  1.00 9.41  ? 95  ASN   B N   1 
ATOM   3096 C  CA  . ASN   B 1 95  ? 28.967  -24.437 -0.376  1.00 9.54  ? 95  ASN   B CA  1 
ATOM   3097 C  C   . ASN   B 1 95  ? 28.208  -23.773 -1.517  1.00 9.86  ? 95  ASN   B C   1 
ATOM   3098 O  O   . ASN   B 1 95  ? 28.689  -22.836 -2.144  1.00 10.22 ? 95  ASN   B O   1 
ATOM   3099 C  CB  . ASN   B 1 95  ? 29.371  -23.375 0.661   1.00 9.72  ? 95  ASN   B CB  1 
ATOM   3100 C  CG  . ASN   B 1 95  ? 28.172  -22.683 1.286   1.00 9.71  ? 95  ASN   B CG  1 
ATOM   3101 O  OD1 . ASN   B 1 95  ? 27.012  -22.928 0.914   1.00 9.59  ? 95  ASN   B OD1 1 
ATOM   3102 N  ND2 . ASN   B 1 95  ? 28.439  -21.773 2.212   1.00 10.50 ? 95  ASN   B ND2 1 
ATOM   3103 N  N   . PRO   B 1 96  ? 26.962  -24.169 -1.823  1.00 10.51 ? 96  PRO   B N   1 
ATOM   3104 C  CA  . PRO   B 1 96  ? 26.235  -23.548 -2.930  1.00 11.55 ? 96  PRO   B CA  1 
ATOM   3105 C  C   . PRO   B 1 96  ? 25.831  -22.085 -2.698  1.00 12.13 ? 96  PRO   B C   1 
ATOM   3106 O  O   . PRO   B 1 96  ? 25.428  -21.377 -3.642  1.00 12.90 ? 96  PRO   B O   1 
ATOM   3107 C  CB  . PRO   B 1 96  ? 24.977  -24.431 -3.050  1.00 12.63 ? 96  PRO   B CB  1 
ATOM   3108 C  CG  . PRO   B 1 96  ? 25.287  -25.666 -2.278  1.00 12.72 ? 96  PRO   B CG  1 
ATOM   3109 C  CD  . PRO   B 1 96  ? 26.222  -25.268 -1.182  1.00 11.83 ? 96  PRO   B CD  1 
ATOM   3110 N  N   . LYS   B 1 97  ? 25.926  -21.628 -1.455  1.00 11.07 ? 97  LYS   B N   1 
ATOM   3111 C  CA  . LYS   B 1 97  ? 25.645  -20.230 -1.115  1.00 13.35 ? 97  LYS   B CA  1 
ATOM   3112 C  C   . LYS   B 1 97  ? 26.918  -19.385 -1.049  1.00 12.56 ? 97  LYS   B C   1 
ATOM   3113 O  O   . LYS   B 1 97  ? 26.854  -18.216 -0.637  1.00 11.32 ? 97  LYS   B O   1 
ATOM   3114 C  CB  . LYS   B 1 97  ? 24.907  -20.159 0.218   1.00 15.77 ? 97  LYS   B CB  1 
ATOM   3115 C  CG  . LYS   B 1 97  ? 23.484  -20.670 0.125   1.00 20.97 ? 97  LYS   B CG  1 
ATOM   3116 C  CD  . LYS   B 1 97  ? 23.431  -22.053 0.539   1.00 28.87 ? 97  LYS   B CD  1 
ATOM   3117 C  CE  . LYS   B 1 97  ? 22.312  -22.869 -0.080  1.00 29.66 ? 97  LYS   B CE  1 
ATOM   3118 N  NZ  . LYS   B 1 97  ? 22.680  -24.277 0.082   1.00 19.42 ? 97  LYS   B NZ  1 
ATOM   3119 N  N   . THR   B 1 98  ? 28.054  -19.917 -1.520  1.00 10.74 ? 98  THR   B N   1 
ATOM   3120 C  CA  . THR   B 1 98  ? 29.267  -19.115 -1.502  1.00 11.47 ? 98  THR   B CA  1 
ATOM   3121 C  C   . THR   B 1 98  ? 29.086  -17.840 -2.325  1.00 11.67 ? 98  THR   B C   1 
ATOM   3122 O  O   . THR   B 1 98  ? 28.756  -17.911 -3.501  1.00 10.44 ? 98  THR   B O   1 
ATOM   3123 C  CB  . THR   B 1 98  ? 30.466  -19.886 -2.068  1.00 11.33 ? 98  THR   B CB  1 
ATOM   3124 O  OG1 . THR   B 1 98  ? 30.596  -21.117 -1.346  1.00 11.30 ? 98  THR   B OG1 1 
ATOM   3125 C  CG2 . THR   B 1 98  ? 31.770  -19.118 -1.993  1.00 11.98 ? 98  THR   B CG2 1 
ATOM   3126 N  N   . PRO   B 1 99  ? 29.335  -16.644 -1.773  1.00 11.71 ? 99  PRO   B N   1 
ATOM   3127 C  CA  . PRO   B 1 99  ? 29.288  -15.422 -2.566  1.00 14.34 ? 99  PRO   B CA  1 
ATOM   3128 C  C   . PRO   B 1 99  ? 30.598  -15.173 -3.277  1.00 14.04 ? 99  PRO   B C   1 
ATOM   3129 O  O   . PRO   B 1 99  ? 31.614  -15.800 -2.971  1.00 13.23 ? 99  PRO   B O   1 
ATOM   3130 C  CB  . PRO   B 1 99  ? 29.073  -14.341 -1.491  1.00 13.02 ? 99  PRO   B CB  1 
ATOM   3131 C  CG  . PRO   B 1 99  ? 29.838  -14.885 -0.309  1.00 13.30 ? 99  PRO   B CG  1 
ATOM   3132 C  CD  . PRO   B 1 99  ? 29.680  -16.381 -0.374  1.00 11.84 ? 99  PRO   B CD  1 
ATOM   3133 N  N   . LYS   B 1 100 ? 30.590  -14.207 -4.199  1.00 13.56 ? 100 LYS   B N   1 
ATOM   3134 C  CA  . LYS   B 1 100 ? 31.871  -13.668 -4.631  1.00 15.28 ? 100 LYS   B CA  1 
ATOM   3135 C  C   . LYS   B 1 100 ? 32.543  -13.078 -3.392  1.00 13.22 ? 100 LYS   B C   1 
ATOM   3136 O  O   . LYS   B 1 100 ? 31.863  -12.371 -2.638  1.00 14.26 ? 100 LYS   B O   1 
ATOM   3137 C  CB  . LYS   B 1 100 ? 31.704  -12.525 -5.626  1.00 20.43 ? 100 LYS   B CB  1 
ATOM   3138 C  CG  . LYS   B 1 100 ? 30.978  -12.868 -6.909  1.00 27.09 ? 100 LYS   B CG  1 
ATOM   3139 C  CD  . LYS   B 1 100 ? 30.792  -11.654 -7.798  1.00 39.86 ? 100 LYS   B CD  1 
ATOM   3140 C  CE  . LYS   B 1 100 ? 29.396  -11.578 -8.381  1.00 50.02 ? 100 LYS   B CE  1 
ATOM   3141 N  NZ  . LYS   B 1 100 ? 29.176  -10.327 -9.147  1.00 55.86 ? 100 LYS   B NZ  1 
ATOM   3142 N  N   . TYR   B 1 101 ? 33.817  -13.384 -3.183  1.00 12.70 ? 101 TYR   B N   1 
ATOM   3143 C  CA  . TYR   B 1 101 ? 34.483  -12.961 -1.971  1.00 12.99 ? 101 TYR   B CA  1 
ATOM   3144 C  C   . TYR   B 1 101 ? 35.970  -12.696 -2.170  1.00 14.41 ? 101 TYR   B C   1 
ATOM   3145 O  O   . TYR   B 1 101 ? 36.614  -13.180 -3.118  1.00 15.04 ? 101 TYR   B O   1 
ATOM   3146 C  CB  . TYR   B 1 101 ? 34.294  -13.943 -0.802  1.00 14.58 ? 101 TYR   B CB  1 
ATOM   3147 C  CG  . TYR   B 1 101 ? 35.159  -15.187 -0.907  1.00 14.08 ? 101 TYR   B CG  1 
ATOM   3148 C  CD1 . TYR   B 1 101 ? 34.704  -16.293 -1.590  1.00 14.61 ? 101 TYR   B CD1 1 
ATOM   3149 C  CD2 . TYR   B 1 101 ? 36.411  -15.242 -0.301  1.00 15.16 ? 101 TYR   B CD2 1 
ATOM   3150 C  CE1 . TYR   B 1 101 ? 35.497  -17.421 -1.725  1.00 18.58 ? 101 TYR   B CE1 1 
ATOM   3151 C  CE2 . TYR   B 1 101 ? 37.191  -16.379 -0.398  1.00 17.18 ? 101 TYR   B CE2 1 
ATOM   3152 C  CZ  . TYR   B 1 101 ? 36.734  -17.463 -1.111  1.00 19.97 ? 101 TYR   B CZ  1 
ATOM   3153 O  OH  . TYR   B 1 101 ? 37.542  -18.560 -1.187  1.00 27.52 ? 101 TYR   B OH  1 
ATOM   3154 N  N   . LYS   B 1 102 ? 36.521  -11.985 -1.190  1.00 13.32 ? 102 LYS   B N   1 
ATOM   3155 C  CA  . LYS   B 1 102 ? 37.943  -11.868 -1.007  1.00 16.65 ? 102 LYS   B CA  1 
ATOM   3156 C  C   . LYS   B 1 102 ? 38.293  -11.708 0.459   1.00 14.84 ? 102 LYS   B C   1 
ATOM   3157 O  O   . LYS   B 1 102 ? 37.455  -11.407 1.304   1.00 14.50 ? 102 LYS   B O   1 
ATOM   3158 C  CB  . LYS   B 1 102 ? 38.477  -10.736 -1.887  1.00 21.67 ? 102 LYS   B CB  1 
ATOM   3159 C  CG  . LYS   B 1 102 ? 38.245  -9.342  -1.386  1.00 28.96 ? 102 LYS   B CG  1 
ATOM   3160 C  CD  . LYS   B 1 102 ? 38.915  -8.314  -2.296  1.00 35.68 ? 102 LYS   B CD  1 
ATOM   3161 C  CE  . LYS   B 1 102 ? 37.949  -7.557  -3.178  1.00 43.18 ? 102 LYS   B CE  1 
ATOM   3162 N  NZ  . LYS   B 1 102 ? 38.471  -6.197  -3.479  1.00 46.94 ? 102 LYS   B NZ  1 
ATOM   3163 N  N   . PHE   B 1 103 ? 39.569  -11.973 0.759   1.00 12.50 ? 103 PHE   B N   1 
ATOM   3164 C  CA  . PHE   B 1 103 ? 40.104  -11.784 2.087   1.00 12.19 ? 103 PHE   B CA  1 
ATOM   3165 C  C   . PHE   B 1 103 ? 40.961  -10.516 2.094   1.00 15.26 ? 103 PHE   B C   1 
ATOM   3166 O  O   . PHE   B 1 103 ? 41.815  -10.368 1.217   1.00 15.54 ? 103 PHE   B O   1 
ATOM   3167 C  CB  . PHE   B 1 103 ? 40.947  -12.985 2.500   1.00 13.39 ? 103 PHE   B CB  1 
ATOM   3168 C  CG  . PHE   B 1 103 ? 40.220  -14.296 2.734   1.00 13.49 ? 103 PHE   B CG  1 
ATOM   3169 C  CD1 . PHE   B 1 103 ? 38.848  -14.341 2.886   1.00 13.31 ? 103 PHE   B CD1 1 
ATOM   3170 C  CD2 . PHE   B 1 103 ? 40.927  -15.494 2.786   1.00 14.55 ? 103 PHE   B CD2 1 
ATOM   3171 C  CE1 . PHE   B 1 103 ? 38.194  -15.550 3.100   1.00 13.90 ? 103 PHE   B CE1 1 
ATOM   3172 C  CE2 . PHE   B 1 103 ? 40.281  -16.698 3.015   1.00 13.45 ? 103 PHE   B CE2 1 
ATOM   3173 C  CZ  . PHE   B 1 103 ? 38.906  -16.727 3.189   1.00 13.58 ? 103 PHE   B CZ  1 
ATOM   3174 N  N   . VAL   B 1 104 ? 40.663  -9.579  2.995   1.00 13.70 ? 104 VAL   B N   1 
ATOM   3175 C  CA  . VAL   B 1 104 ? 41.437  -8.343  3.069   1.00 15.58 ? 104 VAL   B CA  1 
ATOM   3176 C  C   . VAL   B 1 104 ? 41.921  -8.124  4.489   1.00 15.99 ? 104 VAL   B C   1 
ATOM   3177 O  O   . VAL   B 1 104 ? 41.306  -8.553  5.465   1.00 17.01 ? 104 VAL   B O   1 
ATOM   3178 C  CB  . VAL   B 1 104 ? 40.638  -7.131  2.571   1.00 17.18 ? 104 VAL   B CB  1 
ATOM   3179 C  CG1 . VAL   B 1 104 ? 40.032  -7.331  1.199   1.00 19.29 ? 104 VAL   B CG1 1 
ATOM   3180 C  CG2 . VAL   B 1 104 ? 39.549  -6.772  3.559   1.00 19.44 ? 104 VAL   B CG2 1 
ATOM   3181 N  N   . ARG   B 1 105 ? 43.035  -7.404  4.643   1.00 13.93 ? 105 ARG   B N   1 
ATOM   3182 C  CA  . ARG   B 1 105 ? 43.472  -7.005  5.962   1.00 13.79 ? 105 ARG   B CA  1 
ATOM   3183 C  C   . ARG   B 1 105 ? 43.267  -5.496  6.091   1.00 14.55 ? 105 ARG   B C   1 
ATOM   3184 O  O   . ARG   B 1 105 ? 43.778  -4.725  5.299   1.00 14.27 ? 105 ARG   B O   1 
ATOM   3185 C  CB  . ARG   B 1 105 ? 44.926  -7.402  6.163   1.00 14.36 ? 105 ARG   B CB  1 
ATOM   3186 C  CG  . ARG   B 1 105 ? 45.474  -7.170  7.545   1.00 15.79 ? 105 ARG   B CG  1 
ATOM   3187 C  CD  . ARG   B 1 105 ? 46.909  -7.614  7.686   1.00 16.49 ? 105 ARG   B CD  1 
ATOM   3188 N  NE  . ARG   B 1 105 ? 47.449  -7.329  9.005   1.00 16.06 ? 105 ARG   B NE  1 
ATOM   3189 C  CZ  . ARG   B 1 105 ? 47.196  -8.010  10.116  1.00 18.13 ? 105 ARG   B CZ  1 
ATOM   3190 N  NH1 . ARG   B 1 105 ? 46.471  -9.119  10.079  1.00 19.14 ? 105 ARG   B NH1 1 
ATOM   3191 N  NH2 . ARG   B 1 105 ? 47.690  -7.626  11.280  1.00 19.72 ? 105 ARG   B NH2 1 
ATOM   3192 N  N   . ILE   B 1 106 ? 42.487  -5.076  7.086   1.00 14.62 ? 106 ILE   B N   1 
ATOM   3193 C  CA  . ILE   B 1 106 ? 42.107  -3.674  7.191   1.00 15.40 ? 106 ILE   B CA  1 
ATOM   3194 C  C   . ILE   B 1 106 ? 43.101  -2.926  8.059   1.00 16.24 ? 106 ILE   B C   1 
ATOM   3195 O  O   . ILE   B 1 106 ? 43.839  -3.514  8.836   1.00 16.57 ? 106 ILE   B O   1 
ATOM   3196 C  CB  . ILE   B 1 106 ? 40.674  -3.480  7.735   1.00 14.76 ? 106 ILE   B CB  1 
ATOM   3197 C  CG1 . ILE   B 1 106 ? 40.490  -4.129  9.102   1.00 15.69 ? 106 ILE   B CG1 1 
ATOM   3198 C  CG2 . ILE   B 1 106 ? 39.673  -3.933  6.674   1.00 15.67 ? 106 ILE   B CG2 1 
ATOM   3199 C  CD1 . ILE   B 1 106 ? 39.181  -3.774  9.719   1.00 18.06 ? 106 ILE   B CD1 1 
ATOM   3200 N  N   . GLN   B 1 107 ? 43.021  -1.572  7.982   1.00 16.14 ? 107 GLN   B N   1 
ATOM   3201 C  CA  . GLN   B 1 107 ? 43.777  -0.686  8.858   1.00 16.17 ? 107 GLN   B CA  1 
ATOM   3202 C  C   . GLN   B 1 107 ? 42.907  -0.190  10.004  1.00 16.05 ? 107 GLN   B C   1 
ATOM   3203 O  O   . GLN   B 1 107 ? 41.678  -0.115  9.843   1.00 15.54 ? 107 GLN   B O   1 
ATOM   3204 C  CB  . GLN   B 1 107 ? 44.242  0.581   8.129   1.00 17.78 ? 107 GLN   B CB  1 
ATOM   3205 C  CG  . GLN   B 1 107 ? 45.384  0.341   7.195   1.00 19.94 ? 107 GLN   B CG  1 
ATOM   3206 C  CD  . GLN   B 1 107 ? 46.601  -0.124  7.951   1.00 21.79 ? 107 GLN   B CD  1 
ATOM   3207 O  OE1 . GLN   B 1 107 ? 46.905  -1.316  7.982   1.00 25.02 ? 107 GLN   B OE1 1 
ATOM   3208 N  NE2 . GLN   B 1 107 ? 47.307  0.820   8.553   1.00 19.84 ? 107 GLN   B NE2 1 
ATOM   3209 N  N   . PRO   B 1 108 ? 43.505  0.246   11.132  1.00 16.27 ? 108 PRO   B N   1 
ATOM   3210 C  CA  . PRO   B 1 108 ? 42.778  0.974   12.174  1.00 16.55 ? 108 PRO   B CA  1 
ATOM   3211 C  C   . PRO   B 1 108 ? 41.993  2.137   11.603  1.00 16.54 ? 108 PRO   B C   1 
ATOM   3212 O  O   . PRO   B 1 108 ? 42.465  2.802   10.695  1.00 16.48 ? 108 PRO   B O   1 
ATOM   3213 C  CB  . PRO   B 1 108 ? 43.850  1.441   13.168  1.00 20.17 ? 108 PRO   B CB  1 
ATOM   3214 C  CG  . PRO   B 1 108 ? 44.927  0.404   13.009  1.00 21.13 ? 108 PRO   B CG  1 
ATOM   3215 C  CD  . PRO   B 1 108 ? 44.920  0.057   11.528  1.00 20.43 ? 108 PRO   B CD  1 
ATOM   3216 N  N   . GLY   B 1 109 ? 40.767  2.310   12.131  1.00 16.16 ? 109 GLY   B N   1 
ATOM   3217 C  CA  . GLY   B 1 109 ? 39.854  3.323   11.642  1.00 14.95 ? 109 GLY   B CA  1 
ATOM   3218 C  C   . GLY   B 1 109 ? 38.823  2.747   10.685  1.00 15.73 ? 109 GLY   B C   1 
ATOM   3219 O  O   . GLY   B 1 109 ? 37.745  3.306   10.570  1.00 16.06 ? 109 GLY   B O   1 
ATOM   3220 N  N   . GLN   B 1 110 ? 39.182  1.702   9.921   1.00 12.73 ? 110 GLN   B N   1 
ATOM   3221 C  CA  . GLN   B 1 110 ? 38.239  1.139   8.975   1.00 14.49 ? 110 GLN   B CA  1 
ATOM   3222 C  C   . GLN   B 1 110 ? 37.134  0.445   9.748   1.00 13.95 ? 110 GLN   B C   1 
ATOM   3223 O  O   . GLN   B 1 110 ? 37.338  -0.149  10.796  1.00 14.81 ? 110 GLN   B O   1 
ATOM   3224 C  CB  . GLN   B 1 110 ? 38.937  0.190   7.997   1.00 17.12 ? 110 GLN   B CB  1 
ATOM   3225 C  CG  . GLN   B 1 110 ? 39.900  0.895   7.018   1.00 19.69 ? 110 GLN   B CG  1 
ATOM   3226 C  CD  . GLN   B 1 110 ? 40.388  -0.079  5.962   1.00 23.74 ? 110 GLN   B CD  1 
ATOM   3227 O  OE1 . GLN   B 1 110 ? 41.504  -0.569  5.997   1.00 19.66 ? 110 GLN   B OE1 1 
ATOM   3228 N  NE2 . GLN   B 1 110 ? 39.505  -0.450  5.045   1.00 29.37 ? 110 GLN   B NE2 1 
ATOM   3229 N  N   . THR   B 1 111 ? 35.926  0.535   9.184   1.00 13.66 ? 111 THR   B N   1 
ATOM   3230 C  CA  . THR   B 1 111 ? 34.764  -0.065  9.797   1.00 13.40 ? 111 THR   B CA  1 
ATOM   3231 C  C   . THR   B 1 111 ? 34.383  -1.325  9.010   1.00 11.89 ? 111 THR   B C   1 
ATOM   3232 O  O   . THR   B 1 111 ? 34.839  -1.538  7.899   1.00 13.80 ? 111 THR   B O   1 
ATOM   3233 C  CB  . THR   B 1 111 ? 33.583  0.911   9.837   1.00 12.89 ? 111 THR   B CB  1 
ATOM   3234 O  OG1 . THR   B 1 111 ? 33.371  1.409   8.528   1.00 14.10 ? 111 THR   B OG1 1 
ATOM   3235 C  CG2 . THR   B 1 111 ? 33.797  2.048   10.822  1.00 14.66 ? 111 THR   B CG2 1 
ATOM   3236 N  N   . PHE   B 1 112 ? 33.600  -2.178  9.653   1.00 12.67 ? 112 PHE   B N   1 
ATOM   3237 C  CA  . PHE   B 1 112 ? 33.117  -3.403  9.040   1.00 12.26 ? 112 PHE   B CA  1 
ATOM   3238 C  C   . PHE   B 1 112 ? 31.878  -3.847  9.808   1.00 11.01 ? 112 PHE   B C   1 
ATOM   3239 O  O   . PHE   B 1 112 ? 31.670  -3.453  10.933  1.00 10.91 ? 112 PHE   B O   1 
ATOM   3240 C  CB  . PHE   B 1 112 ? 34.226  -4.463  9.043   1.00 11.71 ? 112 PHE   B CB  1 
ATOM   3241 C  CG  . PHE   B 1 112 ? 34.855  -4.732  10.389  1.00 12.32 ? 112 PHE   B CG  1 
ATOM   3242 C  CD1 . PHE   B 1 112 ? 35.916  -3.965  10.852  1.00 13.54 ? 112 PHE   B CD1 1 
ATOM   3243 C  CD2 . PHE   B 1 112 ? 34.410  -5.780  11.175  1.00 12.37 ? 112 PHE   B CD2 1 
ATOM   3244 C  CE1 . PHE   B 1 112 ? 36.491  -4.242  12.091  1.00 15.66 ? 112 PHE   B CE1 1 
ATOM   3245 C  CE2 . PHE   B 1 112 ? 34.975  -6.064  12.406  1.00 14.65 ? 112 PHE   B CE2 1 
ATOM   3246 C  CZ  . PHE   B 1 112 ? 36.046  -5.315  12.853  1.00 15.96 ? 112 PHE   B CZ  1 
ATOM   3247 N  N   . SER   B 1 113 ? 31.081  -4.737  9.189   1.00 10.09 ? 113 SER   B N   1 
ATOM   3248 C  CA  . SER   B 1 113 ? 29.930  -5.335  9.820   1.00 9.41  ? 113 SER   B CA  1 
ATOM   3249 C  C   . SER   B 1 113 ? 30.374  -6.631  10.479  1.00 9.37  ? 113 SER   B C   1 
ATOM   3250 O  O   . SER   B 1 113 ? 31.109  -7.387  9.872   1.00 9.31  ? 113 SER   B O   1 
ATOM   3251 C  CB  . SER   B 1 113 ? 28.870  -5.603  8.779   1.00 10.72 ? 113 SER   B CB  1 
ATOM   3252 O  OG  . SER   B 1 113 ? 28.410  -4.365  8.220   1.00 11.10 ? 113 SER   B OG  1 
ATOM   3253 N  N   . VAL   B 1 114 ? 29.881  -6.888  11.670  1.00 9.17  ? 114 VAL   B N   1 
ATOM   3254 C  CA  . VAL   B 1 114 ? 30.095  -8.152  12.348  1.00 10.86 ? 114 VAL   B CA  1 
ATOM   3255 C  C   . VAL   B 1 114 ? 28.790  -8.938  12.356  1.00 10.96 ? 114 VAL   B C   1 
ATOM   3256 O  O   . VAL   B 1 114 ? 27.733  -8.443  12.813  1.00 11.50 ? 114 VAL   B O   1 
ATOM   3257 C  CB  . VAL   B 1 114 ? 30.591  -7.907  13.789  1.00 12.72 ? 114 VAL   B CB  1 
ATOM   3258 C  CG1 . VAL   B 1 114 ? 30.558  -9.179  14.621  1.00 13.91 ? 114 VAL   B CG1 1 
ATOM   3259 C  CG2 . VAL   B 1 114 ? 31.990  -7.280  13.757  1.00 14.61 ? 114 VAL   B CG2 1 
ATOM   3260 N  N   . LEU   B 1 115 ? 28.874  -10.220 11.967  1.00 9.76  ? 115 LEU   B N   1 
ATOM   3261 C  CA  . LEU   B 1 115 ? 27.774  -11.129 12.189  1.00 10.95 ? 115 LEU   B CA  1 
ATOM   3262 C  C   . LEU   B 1 115 ? 28.064  -12.014 13.400  1.00 11.30 ? 115 LEU   B C   1 
ATOM   3263 O  O   . LEU   B 1 115 ? 28.861  -12.941 13.324  1.00 10.53 ? 115 LEU   B O   1 
ATOM   3264 C  CB  . LEU   B 1 115 ? 27.493  -11.965 10.939  1.00 10.13 ? 115 LEU   B CB  1 
ATOM   3265 C  CG  . LEU   B 1 115 ? 26.312  -12.925 11.042  1.00 9.88  ? 115 LEU   B CG  1 
ATOM   3266 C  CD1 . LEU   B 1 115 ? 24.976  -12.192 11.155  1.00 9.84  ? 115 LEU   B CD1 1 
ATOM   3267 C  CD2 . LEU   B 1 115 ? 26.311  -13.855 9.837   1.00 9.90  ? 115 LEU   B CD2 1 
ATOM   3268 N  N   . ALA   B 1 116 ? 27.488  -11.657 14.550  1.00 11.70 ? 116 ALA   B N   1 
ATOM   3269 C  CA  . ALA   B 1 116 ? 27.709  -12.417 15.775  1.00 11.59 ? 116 ALA   B CA  1 
ATOM   3270 C  C   . ALA   B 1 116 ? 26.955  -13.731 15.714  1.00 12.77 ? 116 ALA   B C   1 
ATOM   3271 O  O   . ALA   B 1 116 ? 25.750  -13.754 15.442  1.00 14.01 ? 116 ALA   B O   1 
ATOM   3272 C  CB  . ALA   B 1 116 ? 27.303  -11.593 16.977  1.00 13.51 ? 116 ALA   B CB  1 
ATOM   3273 N  N   A CYS   B 1 117 ? 27.676  -14.846 15.893  0.73 11.23 ? 117 CYS   B N   1 
ATOM   3274 N  N   B CYS   B 1 117 ? 27.661  -14.817 16.046  0.27 12.74 ? 117 CYS   B N   1 
ATOM   3275 C  CA  A CYS   B 1 117 ? 27.076  -16.160 15.786  0.73 11.84 ? 117 CYS   B CA  1 
ATOM   3276 C  CA  B CYS   B 1 117 ? 27.221  -16.167 15.750  0.27 13.38 ? 117 CYS   B CA  1 
ATOM   3277 C  C   A CYS   B 1 117 ? 27.429  -16.999 17.009  0.73 13.34 ? 117 CYS   B C   1 
ATOM   3278 C  C   B CYS   B 1 117 ? 27.489  -17.061 16.962  0.27 14.29 ? 117 CYS   B C   1 
ATOM   3279 O  O   A CYS   B 1 117 ? 28.484  -16.809 17.615  0.73 13.77 ? 117 CYS   B O   1 
ATOM   3280 O  O   B CYS   B 1 117 ? 28.544  -16.940 17.579  0.27 14.67 ? 117 CYS   B O   1 
ATOM   3281 C  CB  A CYS   B 1 117 ? 27.618  -16.946 14.591  0.73 12.84 ? 117 CYS   B CB  1 
ATOM   3282 C  CB  B CYS   B 1 117 ? 27.998  -16.661 14.531  0.27 13.75 ? 117 CYS   B CB  1 
ATOM   3283 S  SG  A CYS   B 1 117 ? 27.265  -16.209 12.979  0.73 15.48 ? 117 CYS   B SG  1 
ATOM   3284 S  SG  B CYS   B 1 117 ? 27.184  -17.965 13.573  0.27 14.52 ? 117 CYS   B SG  1 
ATOM   3285 N  N   . TYR   B 1 118 ? 26.534  -17.942 17.296  1.00 15.76 ? 118 TYR   B N   1 
ATOM   3286 C  CA  . TYR   B 1 118 ? 26.665  -18.875 18.414  1.00 15.45 ? 118 TYR   B CA  1 
ATOM   3287 C  C   . TYR   B 1 118 ? 26.313  -20.264 17.886  1.00 15.59 ? 118 TYR   B C   1 
ATOM   3288 O  O   . TYR   B 1 118 ? 25.262  -20.457 17.287  1.00 16.47 ? 118 TYR   B O   1 
ATOM   3289 C  CB  . TYR   B 1 118 ? 25.820  -18.432 19.625  1.00 15.31 ? 118 TYR   B CB  1 
ATOM   3290 C  CG  . TYR   B 1 118 ? 26.256  -17.061 20.090  1.00 16.01 ? 118 TYR   B CG  1 
ATOM   3291 C  CD1 . TYR   B 1 118 ? 27.371  -16.898 20.918  1.00 15.87 ? 118 TYR   B CD1 1 
ATOM   3292 C  CD2 . TYR   B 1 118 ? 25.664  -15.916 19.584  1.00 17.02 ? 118 TYR   B CD2 1 
ATOM   3293 C  CE1 . TYR   B 1 118 ? 27.837  -15.646 21.262  1.00 16.51 ? 118 TYR   B CE1 1 
ATOM   3294 C  CE2 . TYR   B 1 118 ? 26.128  -14.658 19.918  1.00 16.47 ? 118 TYR   B CE2 1 
ATOM   3295 C  CZ  . TYR   B 1 118 ? 27.217  -14.523 20.755  1.00 16.45 ? 118 TYR   B CZ  1 
ATOM   3296 O  OH  . TYR   B 1 118 ? 27.711  -13.286 21.037  1.00 17.32 ? 118 TYR   B OH  1 
ATOM   3297 N  N   . ASN   B 1 119 ? 27.227  -21.237 18.067  1.00 19.24 ? 119 ASN   B N   1 
ATOM   3298 C  CA  . ASN   B 1 119 ? 26.979  -22.606 17.620  1.00 20.74 ? 119 ASN   B CA  1 
ATOM   3299 C  C   . ASN   B 1 119 ? 26.604  -22.644 16.147  1.00 19.56 ? 119 ASN   B C   1 
ATOM   3300 O  O   . ASN   B 1 119 ? 25.738  -23.404 15.707  1.00 19.97 ? 119 ASN   B O   1 
ATOM   3301 C  CB  . ASN   B 1 119 ? 25.867  -23.268 18.434  1.00 26.51 ? 119 ASN   B CB  1 
ATOM   3302 C  CG  . ASN   B 1 119 ? 26.273  -23.336 19.888  1.00 32.49 ? 119 ASN   B CG  1 
ATOM   3303 O  OD1 . ASN   B 1 119 ? 27.285  -23.944 20.219  1.00 40.08 ? 119 ASN   B OD1 1 
ATOM   3304 N  ND2 . ASN   B 1 119 ? 25.556  -22.635 20.744  1.00 40.46 ? 119 ASN   B ND2 1 
ATOM   3305 N  N   . GLY   B 1 120 ? 27.283  -21.829 15.340  1.00 18.20 ? 120 GLY   B N   1 
ATOM   3306 C  CA  . GLY   B 1 120 ? 27.022  -21.837 13.913  1.00 18.17 ? 120 GLY   B CA  1 
ATOM   3307 C  C   . GLY   B 1 120 ? 25.760  -21.107 13.475  1.00 19.22 ? 120 GLY   B C   1 
ATOM   3308 O  O   . GLY   B 1 120 ? 25.489  -21.142 12.284  1.00 20.60 ? 120 GLY   B O   1 
ATOM   3309 N  N   . SER   B 1 121 ? 25.015  -20.479 14.412  1.00 18.79 ? 121 SER   B N   1 
ATOM   3310 C  CA  A SER   B 1 121 ? 23.742  -19.838 14.124  0.39 17.59 ? 121 SER   B CA  1 
ATOM   3311 C  CA  B SER   B 1 121 ? 23.728  -19.842 14.159  0.61 17.53 ? 121 SER   B CA  1 
ATOM   3312 C  C   . SER   B 1 121 ? 23.866  -18.323 14.292  1.00 17.36 ? 121 SER   B C   1 
ATOM   3313 O  O   . SER   B 1 121 ? 24.152  -17.832 15.389  1.00 15.97 ? 121 SER   B O   1 
ATOM   3314 C  CB  A SER   B 1 121 ? 22.650  -20.380 15.000  0.39 17.60 ? 121 SER   B CB  1 
ATOM   3315 C  CB  B SER   B 1 121 ? 22.684  -20.334 15.134  0.61 17.64 ? 121 SER   B CB  1 
ATOM   3316 O  OG  A SER   B 1 121 ? 22.360  -21.728 14.663  0.39 16.67 ? 121 SER   B OG  1 
ATOM   3317 O  OG  B SER   B 1 121 ? 21.383  -19.852 14.807  0.61 16.65 ? 121 SER   B OG  1 
ATOM   3318 N  N   . PRO   B 1 122 ? 23.642  -17.535 13.215  1.00 16.22 ? 122 PRO   B N   1 
ATOM   3319 C  CA  . PRO   B 1 122 ? 23.731  -16.086 13.356  1.00 15.88 ? 122 PRO   B CA  1 
ATOM   3320 C  C   . PRO   B 1 122 ? 22.706  -15.540 14.326  1.00 14.98 ? 122 PRO   B C   1 
ATOM   3321 O  O   . PRO   B 1 122 ? 21.537  -15.888 14.222  1.00 17.25 ? 122 PRO   B O   1 
ATOM   3322 C  CB  . PRO   B 1 122 ? 23.426  -15.589 11.940  1.00 17.38 ? 122 PRO   B CB  1 
ATOM   3323 C  CG  . PRO   B 1 122 ? 23.924  -16.725 11.040  1.00 19.67 ? 122 PRO   B CG  1 
ATOM   3324 C  CD  . PRO   B 1 122 ? 23.484  -17.950 11.813  1.00 18.21 ? 122 PRO   B CD  1 
ATOM   3325 N  N   . SER   B 1 123 ? 23.141  -14.581 15.134  1.00 14.96 ? 123 SER   B N   1 
ATOM   3326 C  CA  . SER   B 1 123 ? 22.319  -14.010 16.165  1.00 15.98 ? 123 SER   B CA  1 
ATOM   3327 C  C   . SER   B 1 123 ? 22.070  -12.519 15.955  1.00 14.38 ? 123 SER   B C   1 
ATOM   3328 O  O   . SER   B 1 123 ? 21.015  -12.006 16.298  1.00 13.93 ? 123 SER   B O   1 
ATOM   3329 C  CB  . SER   B 1 123 ? 23.013  -14.244 17.463  1.00 19.65 ? 123 SER   B CB  1 
ATOM   3330 O  OG  . SER   B 1 123 ? 22.332  -13.603 18.484  1.00 30.03 ? 123 SER   B OG  1 
ATOM   3331 N  N   . GLY   B 1 124 ? 23.057  -11.794 15.455  1.00 12.28 ? 124 GLY   B N   1 
ATOM   3332 C  CA  . GLY   B 1 124 ? 22.900  -10.353 15.326  1.00 12.36 ? 124 GLY   B CA  1 
ATOM   3333 C  C   . GLY   B 1 124 ? 23.966  -9.739  14.437  1.00 11.76 ? 124 GLY   B C   1 
ATOM   3334 O  O   . GLY   B 1 124 ? 25.021  -10.354 14.236  1.00 11.20 ? 124 GLY   B O   1 
ATOM   3335 N  N   A VAL   B 1 125 ? 23.702  -8.524  13.916  0.63 10.49 ? 125 VAL   B N   1 
ATOM   3336 N  N   B VAL   B 1 125 ? 23.672  -8.524  13.956  0.37 11.18 ? 125 VAL   B N   1 
ATOM   3337 C  CA  A VAL   B 1 125 ? 24.639  -7.850  13.032  0.63 10.49 ? 125 VAL   B CA  1 
ATOM   3338 C  CA  B VAL   B 1 125 ? 24.542  -7.788  13.064  0.37 11.30 ? 125 VAL   B CA  1 
ATOM   3339 C  C   A VAL   B 1 125 ? 24.754  -6.376  13.420  0.63 11.61 ? 125 VAL   B C   1 
ATOM   3340 C  C   B VAL   B 1 125 ? 24.796  -6.413  13.673  0.37 11.89 ? 125 VAL   B C   1 
ATOM   3341 O  O   A VAL   B 1 125 ? 23.731  -5.720  13.658  0.63 9.94  ? 125 VAL   B O   1 
ATOM   3342 O  O   B VAL   B 1 125 ? 23.919  -5.843  14.324  0.37 10.26 ? 125 VAL   B O   1 
ATOM   3343 C  CB  A VAL   B 1 125 ? 24.259  -7.996  11.541  0.63 11.16 ? 125 VAL   B CB  1 
ATOM   3344 C  CB  B VAL   B 1 125 ? 23.910  -7.645  11.666  0.37 12.07 ? 125 VAL   B CB  1 
ATOM   3345 C  CG1 A VAL   B 1 125 ? 22.944  -7.305  11.178  0.63 10.47 ? 125 VAL   B CG1 1 
ATOM   3346 C  CG1 B VAL   B 1 125 ? 24.965  -7.343  10.622  0.37 12.30 ? 125 VAL   B CG1 1 
ATOM   3347 C  CG2 A VAL   B 1 125 ? 25.375  -7.485  10.652  0.63 11.88 ? 125 VAL   B CG2 1 
ATOM   3348 C  CG2 B VAL   B 1 125 ? 23.100  -8.870  11.268  0.37 12.01 ? 125 VAL   B CG2 1 
ATOM   3349 N  N   . TYR   B 1 126 ? 26.006  -5.884  13.476  1.00 11.74 ? 126 TYR   B N   1 
ATOM   3350 C  CA  . TYR   B 1 126 ? 26.275  -4.503  13.854  1.00 13.80 ? 126 TYR   B CA  1 
ATOM   3351 C  C   . TYR   B 1 126 ? 27.558  -4.021  13.199  1.00 13.33 ? 126 TYR   B C   1 
ATOM   3352 O  O   . TYR   B 1 126 ? 28.393  -4.831  12.772  1.00 12.82 ? 126 TYR   B O   1 
ATOM   3353 C  CB  . TYR   B 1 126 ? 26.322  -4.399  15.377  1.00 15.07 ? 126 TYR   B CB  1 
ATOM   3354 C  CG  . TYR   B 1 126 ? 27.400  -5.252  16.023  1.00 15.35 ? 126 TYR   B CG  1 
ATOM   3355 C  CD1 . TYR   B 1 126 ? 28.715  -4.801  16.132  1.00 17.49 ? 126 TYR   B CD1 1 
ATOM   3356 C  CD2 . TYR   B 1 126 ? 27.095  -6.478  16.587  1.00 19.11 ? 126 TYR   B CD2 1 
ATOM   3357 C  CE1 . TYR   B 1 126 ? 29.712  -5.574  16.703  1.00 18.42 ? 126 TYR   B CE1 1 
ATOM   3358 C  CE2 . TYR   B 1 126 ? 28.084  -7.248  17.168  1.00 19.84 ? 126 TYR   B CE2 1 
ATOM   3359 C  CZ  . TYR   B 1 126 ? 29.389  -6.807  17.234  1.00 20.03 ? 126 TYR   B CZ  1 
ATOM   3360 O  OH  . TYR   B 1 126 ? 30.351  -7.576  17.864  1.00 22.22 ? 126 TYR   B OH  1 
ATOM   3361 N  N   . GLN   B 1 127 ? 27.731  -2.697  13.162  1.00 13.27 ? 127 GLN   B N   1 
ATOM   3362 C  CA  . GLN   B 1 127 ? 28.927  -2.104  12.573  1.00 15.65 ? 127 GLN   B CA  1 
ATOM   3363 C  C   . GLN   B 1 127 ? 29.929  -1.807  13.672  1.00 15.66 ? 127 GLN   B C   1 
ATOM   3364 O  O   . GLN   B 1 127 ? 29.567  -1.417  14.780  1.00 15.85 ? 127 GLN   B O   1 
ATOM   3365 C  CB  . GLN   B 1 127 ? 28.632  -0.770  11.856  1.00 18.58 ? 127 GLN   B CB  1 
ATOM   3366 C  CG  . GLN   B 1 127 ? 29.568  -0.532  10.679  1.00 26.59 ? 127 GLN   B CG  1 
ATOM   3367 C  CD  . GLN   B 1 127 ? 29.720  0.849   10.070  1.00 33.15 ? 127 GLN   B CD  1 
ATOM   3368 O  OE1 . GLN   B 1 127 ? 29.660  1.898   10.724  1.00 37.65 ? 127 GLN   B OE1 1 
ATOM   3369 N  NE2 . GLN   B 1 127 ? 30.057  0.844   8.788   1.00 30.90 ? 127 GLN   B NE2 1 
ATOM   3370 N  N   . CYS   B 1 128 ? 31.216  -1.964  13.407  1.00 16.12 ? 128 CYS   B N   1 
ATOM   3371 C  CA  . CYS   B 1 128 ? 32.171  -1.445  14.377  1.00 20.46 ? 128 CYS   B CA  1 
ATOM   3372 C  C   . CYS   B 1 128 ? 33.459  -1.063  13.684  1.00 18.23 ? 128 CYS   B C   1 
ATOM   3373 O  O   . CYS   B 1 128 ? 33.578  -1.216  12.484  1.00 16.58 ? 128 CYS   B O   1 
ATOM   3374 C  CB  . CYS   B 1 128 ? 32.452  -2.425  15.475  1.00 28.61 ? 128 CYS   B CB  1 
ATOM   3375 S  SG  . CYS   B 1 128 ? 33.137  -3.888  14.713  1.00 34.04 ? 128 CYS   B SG  1 
ATOM   3376 N  N   . ALA   B 1 129 ? 34.380  -0.456  14.442  1.00 20.08 ? 129 ALA   B N   1 
ATOM   3377 C  CA  . ALA   B 1 129 ? 35.615  0.016   13.859  1.00 17.60 ? 129 ALA   B CA  1 
ATOM   3378 C  C   . ALA   B 1 129 ? 36.795  -0.688  14.515  1.00 14.74 ? 129 ALA   B C   1 
ATOM   3379 O  O   . ALA   B 1 129 ? 36.756  -1.015  15.679  1.00 19.02 ? 129 ALA   B O   1 
ATOM   3380 C  CB  . ALA   B 1 129 ? 35.789  1.507   14.037  1.00 19.75 ? 129 ALA   B CB  1 
ATOM   3381 N  N   A MET   B 1 130 ? 37.852  -0.874  13.739  0.32 15.05 ? 130 MET   B N   1 
ATOM   3382 N  N   B MET   B 1 130 ? 37.859  -0.875  13.743  0.68 14.04 ? 130 MET   B N   1 
ATOM   3383 C  CA  A MET   B 1 130 ? 39.102  -1.287  14.329  0.32 15.07 ? 130 MET   B CA  1 
ATOM   3384 C  CA  B MET   B 1 130 ? 39.128  -1.309  14.294  0.68 14.07 ? 130 MET   B CA  1 
ATOM   3385 C  C   A MET   B 1 130 ? 39.737  -0.084  15.019  0.32 14.99 ? 130 MET   B C   1 
ATOM   3386 C  C   B MET   B 1 130 ? 39.788  -0.117  14.998  0.68 14.17 ? 130 MET   B C   1 
ATOM   3387 O  O   A MET   B 1 130 ? 39.927  0.963   14.403  0.32 14.20 ? 130 MET   B O   1 
ATOM   3388 O  O   B MET   B 1 130 ? 40.050  0.902   14.363  0.68 13.06 ? 130 MET   B O   1 
ATOM   3389 C  CB  A MET   B 1 130 ? 40.052  -1.820  13.269  0.32 15.32 ? 130 MET   B CB  1 
ATOM   3390 C  CB  B MET   B 1 130 ? 40.013  -1.825  13.161  0.68 14.30 ? 130 MET   B CB  1 
ATOM   3391 C  CG  A MET   B 1 130 ? 41.440  -1.946  13.797  0.32 15.97 ? 130 MET   B CG  1 
ATOM   3392 C  CG  B MET   B 1 130 ? 41.407  -2.234  13.588  0.68 15.33 ? 130 MET   B CG  1 
ATOM   3393 S  SD  A MET   B 1 130 ? 42.103  -3.459  13.182  0.32 15.80 ? 130 MET   B SD  1 
ATOM   3394 S  SD  B MET   B 1 130 ? 41.449  -3.650  14.613  0.68 15.84 ? 130 MET   B SD  1 
ATOM   3395 C  CE  A MET   B 1 130 ? 41.107  -4.607  14.135  0.32 17.47 ? 130 MET   B CE  1 
ATOM   3396 C  CE  B MET   B 1 130 ? 40.792  -4.884  13.477  0.68 16.96 ? 130 MET   B CE  1 
ATOM   3397 N  N   . ARG   B 1 131 ? 40.038  -0.247  16.308  1.00 15.69 ? 131 ARG   B N   1 
ATOM   3398 C  CA  . ARG   B 1 131 ? 40.699  0.808   17.077  1.00 16.58 ? 131 ARG   B CA  1 
ATOM   3399 C  C   . ARG   B 1 131 ? 42.171  0.905   16.706  1.00 17.18 ? 131 ARG   B C   1 
ATOM   3400 O  O   . ARG   B 1 131 ? 42.772  -0.056  16.211  1.00 17.75 ? 131 ARG   B O   1 
ATOM   3401 C  CB  . ARG   B 1 131 ? 40.562  0.566   18.578  1.00 16.31 ? 131 ARG   B CB  1 
ATOM   3402 C  CG  . ARG   B 1 131 ? 39.145  0.539   19.123  1.00 16.35 ? 131 ARG   B CG  1 
ATOM   3403 C  CD  . ARG   B 1 131 ? 38.300  1.721   18.687  1.00 16.12 ? 131 ARG   B CD  1 
ATOM   3404 N  NE  . ARG   B 1 131 ? 38.930  2.996   19.031  1.00 15.00 ? 131 ARG   B NE  1 
ATOM   3405 C  CZ  . ARG   B 1 131 ? 38.422  4.189   18.757  1.00 15.74 ? 131 ARG   B CZ  1 
ATOM   3406 N  NH1 . ARG   B 1 131 ? 37.241  4.279   18.173  1.00 14.56 ? 131 ARG   B NH1 1 
ATOM   3407 N  NH2 . ARG   B 1 131 ? 39.118  5.289   19.037  1.00 15.25 ? 131 ARG   B NH2 1 
ATOM   3408 N  N   . PRO   B 1 132 ? 42.822  2.087   16.881  1.00 16.12 ? 132 PRO   B N   1 
ATOM   3409 C  CA  . PRO   B 1 132 ? 44.265  2.193   16.666  1.00 18.02 ? 132 PRO   B CA  1 
ATOM   3410 C  C   . PRO   B 1 132 ? 45.163  1.209   17.419  1.00 18.60 ? 132 PRO   B C   1 
ATOM   3411 O  O   . PRO   B 1 132 ? 46.253  0.938   16.934  1.00 24.50 ? 132 PRO   B O   1 
ATOM   3412 C  CB  . PRO   B 1 132 ? 44.580  3.644   17.104  1.00 17.38 ? 132 PRO   B CB  1 
ATOM   3413 C  CG  . PRO   B 1 132 ? 43.278  4.382   16.728  1.00 16.77 ? 132 PRO   B CG  1 
ATOM   3414 C  CD  . PRO   B 1 132 ? 42.197  3.399   17.176  1.00 16.21 ? 132 PRO   B CD  1 
ATOM   3415 N  N   . ASN   B 1 133 ? 44.695  0.681   18.542  1.00 17.49 ? 133 ASN   B N   1 
ATOM   3416 C  CA  . ASN   B 1 133 ? 45.428  -0.317  19.311  1.00 19.92 ? 133 ASN   B CA  1 
ATOM   3417 C  C   . ASN   B 1 133 ? 45.067  -1.748  18.884  1.00 21.85 ? 133 ASN   B C   1 
ATOM   3418 O  O   . ASN   B 1 133 ? 45.285  -2.669  19.661  1.00 21.48 ? 133 ASN   B O   1 
ATOM   3419 C  CB  . ASN   B 1 133 ? 45.180  -0.204  20.808  1.00 19.08 ? 133 ASN   B CB  1 
ATOM   3420 C  CG  . ASN   B 1 133 ? 43.773  -0.442  21.330  1.00 20.31 ? 133 ASN   B CG  1 
ATOM   3421 O  OD1 . ASN   B 1 133 ? 42.816  -0.702  20.594  1.00 23.38 ? 133 ASN   B OD1 1 
ATOM   3422 N  ND2 . ASN   B 1 133 ? 43.605  -0.279  22.624  1.00 21.62 ? 133 ASN   B ND2 1 
ATOM   3423 N  N   . PHE   B 1 134 ? 44.350  -1.871  17.757  1.00 20.50 ? 134 PHE   B N   1 
ATOM   3424 C  CA  . PHE   B 1 134 ? 44.053  -3.160  17.105  1.00 21.56 ? 134 PHE   B CA  1 
ATOM   3425 C  C   . PHE   B 1 134 ? 43.082  -4.033  17.882  1.00 22.19 ? 134 PHE   B C   1 
ATOM   3426 O  O   . PHE   B 1 134 ? 42.984  -5.237  17.644  1.00 26.40 ? 134 PHE   B O   1 
ATOM   3427 C  CB  . PHE   B 1 134 ? 45.350  -3.921  16.825  1.00 20.98 ? 134 PHE   B CB  1 
ATOM   3428 C  CG  . PHE   B 1 134 ? 46.186  -3.265  15.779  1.00 22.17 ? 134 PHE   B CG  1 
ATOM   3429 C  CD1 . PHE   B 1 134 ? 45.748  -3.166  14.473  1.00 25.22 ? 134 PHE   B CD1 1 
ATOM   3430 C  CD2 . PHE   B 1 134 ? 47.375  -2.653  16.117  1.00 27.39 ? 134 PHE   B CD2 1 
ATOM   3431 C  CE1 . PHE   B 1 134 ? 46.516  -2.556  13.498  1.00 31.01 ? 134 PHE   B CE1 1 
ATOM   3432 C  CE2 . PHE   B 1 134 ? 48.122  -2.014  15.142  1.00 25.25 ? 134 PHE   B CE2 1 
ATOM   3433 C  CZ  . PHE   B 1 134 ? 47.699  -1.956  13.846  1.00 29.81 ? 134 PHE   B CZ  1 
ATOM   3434 N  N   . THR   B 1 135 ? 42.271  -3.424  18.719  1.00 18.62 ? 135 THR   B N   1 
ATOM   3435 C  CA  . THR   B 1 135 ? 41.129  -4.076  19.314  1.00 18.46 ? 135 THR   B CA  1 
ATOM   3436 C  C   . THR   B 1 135 ? 39.860  -3.534  18.671  1.00 18.81 ? 135 THR   B C   1 
ATOM   3437 O  O   . THR   B 1 135 ? 39.902  -2.529  17.946  1.00 19.68 ? 135 THR   B O   1 
ATOM   3438 C  CB  . THR   B 1 135 ? 41.059  -3.883  20.835  1.00 21.62 ? 135 THR   B CB  1 
ATOM   3439 O  OG1 . THR   B 1 135 ? 40.806  -2.511  21.193  1.00 20.37 ? 135 THR   B OG1 1 
ATOM   3440 C  CG2 . THR   B 1 135 ? 42.322  -4.368  21.531  1.00 22.24 ? 135 THR   B CG2 1 
ATOM   3441 N  N   . ILE   B 1 136 ? 38.761  -4.237  18.901  1.00 19.01 ? 136 ILE   B N   1 
ATOM   3442 C  CA  . ILE   B 1 136 ? 37.451  -3.729  18.517  1.00 19.65 ? 136 ILE   B CA  1 
ATOM   3443 C  C   . ILE   B 1 136 ? 36.583  -3.680  19.761  1.00 20.53 ? 136 ILE   B C   1 
ATOM   3444 O  O   . ILE   B 1 136 ? 36.631  -4.531  20.636  1.00 18.78 ? 136 ILE   B O   1 
ATOM   3445 C  CB  . ILE   B 1 136 ? 36.833  -4.513  17.340  1.00 23.06 ? 136 ILE   B CB  1 
ATOM   3446 C  CG1 . ILE   B 1 136 ? 36.190  -5.818  17.773  1.00 25.33 ? 136 ILE   B CG1 1 
ATOM   3447 C  CG2 . ILE   B 1 136 ? 37.857  -4.746  16.219  1.00 23.77 ? 136 ILE   B CG2 1 
ATOM   3448 C  CD1 . ILE   B 1 136 ? 35.565  -6.600  16.602  1.00 24.87 ? 136 ILE   B CD1 1 
ATOM   3449 N  N   . LYS   B 1 137 ? 35.798  -2.603  19.845  1.00 21.60 ? 137 LYS   B N   1 
ATOM   3450 C  CA  . LYS   B 1 137 ? 34.786  -2.480  20.871  1.00 26.17 ? 137 LYS   B CA  1 
ATOM   3451 C  C   . LYS   B 1 137 ? 33.526  -3.143  20.324  1.00 24.87 ? 137 LYS   B C   1 
ATOM   3452 O  O   . LYS   B 1 137 ? 32.602  -2.496  19.816  1.00 25.91 ? 137 LYS   B O   1 
ATOM   3453 C  CB  . LYS   B 1 137 ? 34.588  -1.008  21.242  1.00 29.79 ? 137 LYS   B CB  1 
ATOM   3454 C  CG  . LYS   B 1 137 ? 35.814  -0.331  21.833  1.00 37.86 ? 137 LYS   B CG  1 
ATOM   3455 C  CD  . LYS   B 1 137 ? 35.587  1.153   22.171  1.00 45.01 ? 137 LYS   B CD  1 
ATOM   3456 C  CE  . LYS   B 1 137 ? 36.317  1.612   23.414  1.00 51.26 ? 137 LYS   B CE  1 
ATOM   3457 N  NZ  . LYS   B 1 137 ? 35.664  1.098   24.647  1.00 57.31 ? 137 LYS   B NZ  1 
ATOM   3458 N  N   . GLY   B 1 138 ? 33.546  -4.475  20.347  1.00 22.45 ? 138 GLY   B N   1 
ATOM   3459 C  CA  . GLY   B 1 138 ? 32.438  -5.260  19.873  1.00 21.86 ? 138 GLY   B CA  1 
ATOM   3460 C  C   . GLY   B 1 138 ? 31.435  -5.556  20.970  1.00 22.88 ? 138 GLY   B C   1 
ATOM   3461 O  O   . GLY   B 1 138 ? 31.522  -5.049  22.084  1.00 26.20 ? 138 GLY   B O   1 
ATOM   3462 N  N   . SER   B 1 139 ? 30.515  -6.428  20.601  1.00 21.20 ? 139 SER   B N   1 
ATOM   3463 C  CA  . SER   B 1 139 ? 29.517  -6.992  21.470  1.00 20.67 ? 139 SER   B CA  1 
ATOM   3464 C  C   . SER   B 1 139 ? 29.506  -8.482  21.173  1.00 22.09 ? 139 SER   B C   1 
ATOM   3465 O  O   . SER   B 1 139 ? 29.042  -8.942  20.126  1.00 19.02 ? 139 SER   B O   1 
ATOM   3466 C  CB  . SER   B 1 139 ? 28.140  -6.352  21.272  1.00 22.01 ? 139 SER   B CB  1 
ATOM   3467 O  OG  . SER   B 1 139 ? 27.206  -6.973  22.111  1.00 25.16 ? 139 SER   B OG  1 
ATOM   3468 N  N   . PHE   B 1 140 ? 30.074  -9.241  22.101  1.00 20.20 ? 140 PHE   B N   1 
ATOM   3469 C  CA  . PHE   B 1 140 ? 30.249  -10.668 21.891  1.00 18.45 ? 140 PHE   B CA  1 
ATOM   3470 C  C   . PHE   B 1 140 ? 30.105  -11.392 23.231  1.00 19.72 ? 140 PHE   B C   1 
ATOM   3471 O  O   . PHE   B 1 140 ? 30.675  -10.947 24.237  1.00 23.02 ? 140 PHE   B O   1 
ATOM   3472 C  CB  . PHE   B 1 140 ? 31.655  -10.939 21.367  1.00 19.79 ? 140 PHE   B CB  1 
ATOM   3473 C  CG  . PHE   B 1 140 ? 31.966  -10.592 19.938  1.00 17.39 ? 140 PHE   B CG  1 
ATOM   3474 C  CD1 . PHE   B 1 140 ? 31.321  -11.224 18.881  1.00 18.64 ? 140 PHE   B CD1 1 
ATOM   3475 C  CD2 . PHE   B 1 140 ? 32.952  -9.675  19.645  1.00 18.07 ? 140 PHE   B CD2 1 
ATOM   3476 C  CE1 . PHE   B 1 140 ? 31.668  -10.929 17.568  1.00 19.89 ? 140 PHE   B CE1 1 
ATOM   3477 C  CE2 . PHE   B 1 140 ? 33.289  -9.366  18.327  1.00 19.52 ? 140 PHE   B CE2 1 
ATOM   3478 C  CZ  . PHE   B 1 140 ? 32.668  -10.021 17.288  1.00 18.82 ? 140 PHE   B CZ  1 
ATOM   3479 N  N   . LEU   B 1 141 ? 29.375  -12.504 23.221  1.00 19.49 ? 141 LEU   B N   1 
ATOM   3480 C  CA  . LEU   B 1 141 ? 29.282  -13.382 24.381  1.00 22.08 ? 141 LEU   B CA  1 
ATOM   3481 C  C   . LEU   B 1 141 ? 30.199  -14.591 24.196  1.00 22.14 ? 141 LEU   B C   1 
ATOM   3482 O  O   . LEU   B 1 141 ? 30.812  -14.795 23.143  1.00 19.05 ? 141 LEU   B O   1 
ATOM   3483 C  CB  . LEU   B 1 141 ? 27.830  -13.817 24.526  1.00 22.93 ? 141 LEU   B CB  1 
ATOM   3484 C  CG  . LEU   B 1 141 ? 26.825  -12.686 24.791  1.00 28.36 ? 141 LEU   B CG  1 
ATOM   3485 C  CD1 . LEU   B 1 141 ? 25.436  -13.258 24.978  1.00 29.59 ? 141 LEU   B CD1 1 
ATOM   3486 C  CD2 . LEU   B 1 141 ? 27.231  -11.854 25.999  1.00 28.27 ? 141 LEU   B CD2 1 
ATOM   3487 N  N   . ASN   B 1 142 ? 30.334  -15.372 25.281  1.00 22.78 ? 142 ASN   B N   1 
ATOM   3488 C  CA  . ASN   B 1 142 ? 30.929  -16.697 25.188  1.00 22.98 ? 142 ASN   B CA  1 
ATOM   3489 C  C   . ASN   B 1 142 ? 30.253  -17.516 24.076  1.00 18.84 ? 142 ASN   B C   1 
ATOM   3490 O  O   . ASN   B 1 142 ? 29.031  -17.638 24.030  1.00 18.78 ? 142 ASN   B O   1 
ATOM   3491 C  CB  . ASN   B 1 142 ? 30.846  -17.430 26.534  1.00 26.69 ? 142 ASN   B CB  1 
ATOM   3492 C  CG  . ASN   B 1 142 ? 31.721  -18.668 26.552  1.00 33.39 ? 142 ASN   B CG  1 
ATOM   3493 O  OD1 . ASN   B 1 142 ? 32.784  -18.709 25.923  1.00 32.05 ? 142 ASN   B OD1 1 
ATOM   3494 N  ND2 . ASN   B 1 142 ? 31.322  -19.659 27.331  1.00 37.29 ? 142 ASN   B ND2 1 
ATOM   3495 N  N   . GLY   B 1 143 ? 31.082  -18.135 23.193  1.00 19.32 ? 143 GLY   B N   1 
ATOM   3496 C  CA  . GLY   B 1 143 ? 30.566  -18.950 22.105  1.00 17.34 ? 143 GLY   B CA  1 
ATOM   3497 C  C   . GLY   B 1 143 ? 30.622  -18.237 20.748  1.00 15.12 ? 143 GLY   B C   1 
ATOM   3498 O  O   . GLY   B 1 143 ? 30.318  -18.842 19.716  1.00 14.21 ? 143 GLY   B O   1 
ATOM   3499 N  N   . SER   B 1 144 ? 31.019  -16.965 20.779  1.00 16.51 ? 144 SER   B N   1 
ATOM   3500 C  CA  . SER   B 1 144 ? 31.115  -16.125 19.572  1.00 14.89 ? 144 SER   B CA  1 
ATOM   3501 C  C   . SER   B 1 144 ? 32.384  -16.343 18.753  1.00 14.41 ? 144 SER   B C   1 
ATOM   3502 O  O   . SER   B 1 144 ? 32.454  -15.853 17.632  1.00 14.13 ? 144 SER   B O   1 
ATOM   3503 C  CB  . SER   B 1 144 ? 31.000  -14.672 19.973  1.00 14.95 ? 144 SER   B CB  1 
ATOM   3504 O  OG  . SER   B 1 144 ? 32.071  -14.277 20.830  1.00 15.13 ? 144 SER   B OG  1 
ATOM   3505 N  N   . CYS   B 1 145 ? 33.433  -16.993 19.318  1.00 13.23 ? 145 CYS   B N   1 
ATOM   3506 C  CA  . CYS   B 1 145 ? 34.705  -17.256 18.646  1.00 13.13 ? 145 CYS   B CA  1 
ATOM   3507 C  C   . CYS   B 1 145 ? 34.436  -17.783 17.230  1.00 11.53 ? 145 CYS   B C   1 
ATOM   3508 O  O   . CYS   B 1 145 ? 33.595  -18.705 17.055  1.00 10.77 ? 145 CYS   B O   1 
ATOM   3509 C  CB  . CYS   B 1 145 ? 35.474  -18.310 19.446  1.00 14.28 ? 145 CYS   B CB  1 
ATOM   3510 S  SG  . CYS   B 1 145 ? 37.201  -18.441 18.989  1.00 16.71 ? 145 CYS   B SG  1 
ATOM   3511 N  N   . GLY   B 1 146 ? 35.121  -17.153 16.252  1.00 10.30 ? 146 GLY   B N   1 
ATOM   3512 C  CA  . GLY   B 1 146 ? 34.983  -17.542 14.867  1.00 11.52 ? 146 GLY   B CA  1 
ATOM   3513 C  C   . GLY   B 1 146 ? 33.922  -16.762 14.095  1.00 12.02 ? 146 GLY   B C   1 
ATOM   3514 O  O   . GLY   B 1 146 ? 33.864  -16.932 12.889  1.00 10.74 ? 146 GLY   B O   1 
ATOM   3515 N  N   . SER   B 1 147 ? 33.143  -15.895 14.786  1.00 11.74 ? 147 SER   B N   1 
ATOM   3516 C  CA  . SER   B 1 147 ? 32.308  -14.899 14.125  1.00 12.21 ? 147 SER   B CA  1 
ATOM   3517 C  C   . SER   B 1 147 ? 33.188  -14.007 13.231  1.00 11.05 ? 147 SER   B C   1 
ATOM   3518 O  O   . SER   B 1 147 ? 34.340  -13.744 13.585  1.00 10.99 ? 147 SER   B O   1 
ATOM   3519 C  CB  . SER   B 1 147 ? 31.572  -14.067 15.161  1.00 11.17 ? 147 SER   B CB  1 
ATOM   3520 O  OG  . SER   B 1 147 ? 30.596  -14.862 15.887  1.00 11.34 ? 147 SER   B OG  1 
ATOM   3521 N  N   . VAL   B 1 148 ? 32.632  -13.505 12.102  1.00 10.18 ? 148 VAL   B N   1 
ATOM   3522 C  CA  . VAL   B 1 148 ? 33.428  -12.778 11.135  1.00 9.74  ? 148 VAL   B CA  1 
ATOM   3523 C  C   . VAL   B 1 148 ? 32.863  -11.389 10.938  1.00 8.83  ? 148 VAL   B C   1 
ATOM   3524 O  O   . VAL   B 1 148 ? 31.661  -11.113 11.139  1.00 8.04  ? 148 VAL   B O   1 
ATOM   3525 C  CB  . VAL   B 1 148 ? 33.601  -13.507 9.782   1.00 11.40 ? 148 VAL   B CB  1 
ATOM   3526 C  CG1 . VAL   B 1 148 ? 34.264  -14.862 9.969   1.00 11.66 ? 148 VAL   B CG1 1 
ATOM   3527 C  CG2 . VAL   B 1 148 ? 32.288  -13.689 9.022   1.00 11.68 ? 148 VAL   B CG2 1 
ATOM   3528 N  N   . GLY   B 1 149 ? 33.807  -10.562 10.536  1.00 8.53  ? 149 GLY   B N   1 
ATOM   3529 C  CA  . GLY   B 1 149 ? 33.582  -9.206  10.071  1.00 8.92  ? 149 GLY   B CA  1 
ATOM   3530 C  C   . GLY   B 1 149 ? 33.875  -9.056  8.588   1.00 9.38  ? 149 GLY   B C   1 
ATOM   3531 O  O   . GLY   B 1 149 ? 34.756  -9.719  8.003   1.00 9.66  ? 149 GLY   B O   1 
ATOM   3532 N  N   . PHE   B 1 150 ? 33.135  -8.137  7.958   1.00 8.47  ? 150 PHE   B N   1 
ATOM   3533 C  CA  . PHE   B 1 150 ? 33.086  -8.018  6.518   1.00 8.99  ? 150 PHE   B CA  1 
ATOM   3534 C  C   . PHE   B 1 150 ? 32.544  -6.647  6.087   1.00 9.43  ? 150 PHE   B C   1 
ATOM   3535 O  O   . PHE   B 1 150 ? 31.817  -5.967  6.810   1.00 8.39  ? 150 PHE   B O   1 
ATOM   3536 C  CB  . PHE   B 1 150 ? 32.234  -9.146  5.910   1.00 9.71  ? 150 PHE   B CB  1 
ATOM   3537 C  CG  . PHE   B 1 150 ? 30.784  -9.105  6.313   1.00 10.93 ? 150 PHE   B CG  1 
ATOM   3538 C  CD1 . PHE   B 1 150 ? 30.384  -9.600  7.544   1.00 13.39 ? 150 PHE   B CD1 1 
ATOM   3539 C  CD2 . PHE   B 1 150 ? 29.832  -8.500  5.520   1.00 10.75 ? 150 PHE   B CD2 1 
ATOM   3540 C  CE1 . PHE   B 1 150 ? 29.055  -9.515  7.949   1.00 13.79 ? 150 PHE   B CE1 1 
ATOM   3541 C  CE2 . PHE   B 1 150 ? 28.510  -8.413  5.932   1.00 12.27 ? 150 PHE   B CE2 1 
ATOM   3542 C  CZ  . PHE   B 1 150 ? 28.121  -8.919  7.142   1.00 13.62 ? 150 PHE   B CZ  1 
ATOM   3543 N  N   . ASN   B 1 151 ? 32.871  -6.322  4.837   1.00 10.53 ? 151 ASN   B N   1 
ATOM   3544 C  CA  . ASN   B 1 151 ? 32.270  -5.271  4.025   1.00 11.89 ? 151 ASN   B CA  1 
ATOM   3545 C  C   . ASN   B 1 151 ? 31.770  -5.868  2.719   1.00 12.69 ? 151 ASN   B C   1 
ATOM   3546 O  O   . ASN   B 1 151 ? 32.230  -6.915  2.301   1.00 12.86 ? 151 ASN   B O   1 
ATOM   3547 C  CB  . ASN   B 1 151 ? 33.280  -4.163  3.705   1.00 12.98 ? 151 ASN   B CB  1 
ATOM   3548 C  CG  . ASN   B 1 151 ? 33.549  -3.315  4.927   1.00 16.84 ? 151 ASN   B CG  1 
ATOM   3549 O  OD1 . ASN   B 1 151 ? 32.732  -2.477  5.298   1.00 21.38 ? 151 ASN   B OD1 1 
ATOM   3550 N  ND2 . ASN   B 1 151 ? 34.615  -3.597  5.627   1.00 15.58 ? 151 ASN   B ND2 1 
ATOM   3551 N  N   . ILE   B 1 152 ? 30.787  -5.216  2.096   1.00 14.72 ? 152 ILE   B N   1 
ATOM   3552 C  CA  . ILE   B 1 152 ? 30.271  -5.697  0.828   1.00 16.08 ? 152 ILE   B CA  1 
ATOM   3553 C  C   . ILE   B 1 152 ? 30.405  -4.560  -0.186  1.00 21.56 ? 152 ILE   B C   1 
ATOM   3554 O  O   . ILE   B 1 152 ? 29.956  -3.435  0.081   1.00 19.80 ? 152 ILE   B O   1 
ATOM   3555 C  CB  . ILE   B 1 152 ? 28.840  -6.230  0.932   1.00 18.46 ? 152 ILE   B CB  1 
ATOM   3556 C  CG1 . ILE   B 1 152 ? 28.710  -7.290  2.033   1.00 16.00 ? 152 ILE   B CG1 1 
ATOM   3557 C  CG2 . ILE   B 1 152 ? 28.425  -6.738  -0.448  1.00 20.29 ? 152 ILE   B CG2 1 
ATOM   3558 C  CD1 . ILE   B 1 152 ? 27.324  -7.945  2.174   1.00 17.48 ? 152 ILE   B CD1 1 
ATOM   3559 N  N   . ASP   B 1 153 ? 31.055  -4.856  -1.312  1.00 23.44 ? 153 ASP   B N   1 
ATOM   3560 C  CA  . ASP   B 1 153 ? 31.322  -3.859  -2.341  1.00 30.72 ? 153 ASP   B CA  1 
ATOM   3561 C  C   . ASP   B 1 153 ? 30.795  -4.468  -3.631  1.00 35.79 ? 153 ASP   B C   1 
ATOM   3562 O  O   . ASP   B 1 153 ? 31.344  -5.466  -4.097  1.00 28.89 ? 153 ASP   B O   1 
ATOM   3563 C  CB  . ASP   B 1 153 ? 32.803  -3.474  -2.307  1.00 34.66 ? 153 ASP   B CB  1 
ATOM   3564 C  CG  . ASP   B 1 153 ? 33.299  -3.197  -0.886  1.00 49.68 ? 153 ASP   B CG  1 
ATOM   3565 O  OD1 . ASP   B 1 153 ? 32.798  -2.202  -0.279  1.00 54.17 ? 153 ASP   B OD1 1 
ATOM   3566 O  OD2 . ASP   B 1 153 ? 34.154  -3.999  -0.355  1.00 49.54 ? 153 ASP   B OD2 1 
ATOM   3567 N  N   . TYR   B 1 154 ? 29.657  -3.913  -4.090  1.00 44.29 ? 154 TYR   B N   1 
ATOM   3568 C  CA  . TYR   B 1 154 ? 28.840  -4.453  -5.168  1.00 46.93 ? 154 TYR   B CA  1 
ATOM   3569 C  C   . TYR   B 1 154 ? 28.339  -5.838  -4.748  1.00 48.27 ? 154 TYR   B C   1 
ATOM   3570 O  O   . TYR   B 1 154 ? 27.520  -5.958  -3.837  1.00 45.39 ? 154 TYR   B O   1 
ATOM   3571 C  CB  . TYR   B 1 154 ? 29.637  -4.350  -6.475  1.00 48.34 ? 154 TYR   B CB  1 
ATOM   3572 N  N   . ASP   B 1 155 ? 28.822  -6.897  -5.396  1.00 43.36 ? 155 ASP   B N   1 
ATOM   3573 C  CA  . ASP   B 1 155 ? 28.314  -8.221  -5.061  1.00 44.22 ? 155 ASP   B CA  1 
ATOM   3574 C  C   . ASP   B 1 155 ? 29.365  -9.030  -4.301  1.00 30.70 ? 155 ASP   B C   1 
ATOM   3575 O  O   . ASP   B 1 155 ? 29.172  -10.226 -4.064  1.00 31.61 ? 155 ASP   B O   1 
ATOM   3576 C  CB  . ASP   B 1 155 ? 27.816  -8.933  -6.321  1.00 49.91 ? 155 ASP   B CB  1 
ATOM   3577 C  CG  . ASP   B 1 155 ? 26.302  -9.104  -6.390  1.00 62.40 ? 155 ASP   B CG  1 
ATOM   3578 O  OD1 . ASP   B 1 155 ? 25.630  -9.033  -5.321  1.00 61.90 ? 155 ASP   B OD1 1 
ATOM   3579 O  OD2 . ASP   B 1 155 ? 25.792  -9.313  -7.519  1.00 74.76 ? 155 ASP   B OD2 1 
ATOM   3580 N  N   . CYS   B 1 156 ? 30.454  -8.368  -3.903  1.00 23.83 ? 156 CYS   B N   1 
ATOM   3581 C  CA  . CYS   B 1 156 ? 31.608  -9.086  -3.404  1.00 20.89 ? 156 CYS   B CA  1 
ATOM   3582 C  C   . CYS   B 1 156 ? 31.764  -8.814  -1.911  1.00 17.03 ? 156 CYS   B C   1 
ATOM   3583 O  O   . CYS   B 1 156 ? 31.798  -7.661  -1.490  1.00 17.86 ? 156 CYS   B O   1 
ATOM   3584 C  CB  . CYS   B 1 156 ? 32.859  -8.678  -4.162  1.00 21.55 ? 156 CYS   B CB  1 
ATOM   3585 S  SG  . CYS   B 1 156 ? 34.372  -9.494  -3.608  1.00 23.33 ? 156 CYS   B SG  1 
ATOM   3586 N  N   . VAL   B 1 157 ? 31.856  -9.896  -1.125  1.00 14.53 ? 157 VAL   B N   1 
ATOM   3587 C  CA  . VAL   B 1 157 ? 32.097  -9.817  0.308   1.00 11.91 ? 157 VAL   B CA  1 
ATOM   3588 C  C   . VAL   B 1 157 ? 33.603  -9.835  0.587   1.00 10.64 ? 157 VAL   B C   1 
ATOM   3589 O  O   . VAL   B 1 157 ? 34.302  -10.806 0.286   1.00 11.42 ? 157 VAL   B O   1 
ATOM   3590 C  CB  . VAL   B 1 157 ? 31.405  -10.967 1.084   1.00 11.31 ? 157 VAL   B CB  1 
ATOM   3591 C  CG1 . VAL   B 1 157 ? 31.625  -10.772 2.571   1.00 10.46 ? 157 VAL   B CG1 1 
ATOM   3592 C  CG2 . VAL   B 1 157 ? 29.941  -11.062 0.748   1.00 11.33 ? 157 VAL   B CG2 1 
ATOM   3593 N  N   A SER   B 1 158 ? 34.099  -8.737  1.154   0.71 11.78 ? 158 SER   B N   1 
ATOM   3594 N  N   B SER   B 1 158 ? 34.102  -8.767  1.218   0.29 11.04 ? 158 SER   B N   1 
ATOM   3595 C  CA  A SER   B 1 158 ? 35.468  -8.680  1.654   0.71 11.06 ? 158 SER   B CA  1 
ATOM   3596 C  CA  B SER   B 1 158 ? 35.494  -8.701  1.654   0.29 10.59 ? 158 SER   B CA  1 
ATOM   3597 C  C   A SER   B 1 158 ? 35.461  -9.029  3.139   0.71 10.95 ? 158 SER   B C   1 
ATOM   3598 C  C   B SER   B 1 158 ? 35.610  -8.984  3.148   0.29 10.53 ? 158 SER   B C   1 
ATOM   3599 O  O   A SER   B 1 158 ? 34.985  -8.248  3.943   0.71 11.21 ? 158 SER   B O   1 
ATOM   3600 O  O   B SER   B 1 158 ? 35.497  -8.081  3.971   0.29 10.56 ? 158 SER   B O   1 
ATOM   3601 C  CB  A SER   B 1 158 ? 36.130  -7.332  1.406   0.71 12.56 ? 158 SER   B CB  1 
ATOM   3602 C  CB  B SER   B 1 158 ? 36.112  -7.375  1.353   0.29 11.05 ? 158 SER   B CB  1 
ATOM   3603 O  OG  A SER   B 1 158 ? 36.159  -7.032  -0.000  0.71 14.09 ? 158 SER   B OG  1 
ATOM   3604 O  OG  B SER   B 1 158 ? 35.200  -6.347  1.670   0.29 11.15 ? 158 SER   B OG  1 
ATOM   3605 N  N   . PHE   B 1 159 ? 35.934  -10.230 3.479   1.00 10.31 ? 159 PHE   B N   1 
ATOM   3606 C  CA  . PHE   B 1 159 ? 36.078  -10.633 4.872   1.00 9.56  ? 159 PHE   B CA  1 
ATOM   3607 C  C   . PHE   B 1 159 ? 37.366  -10.065 5.453   1.00 11.72 ? 159 PHE   B C   1 
ATOM   3608 O  O   . PHE   B 1 159 ? 38.439  -10.283 4.867   1.00 14.08 ? 159 PHE   B O   1 
ATOM   3609 C  CB  . PHE   B 1 159 ? 36.137  -12.163 4.943   1.00 9.71  ? 159 PHE   B CB  1 
ATOM   3610 C  CG  . PHE   B 1 159 ? 34.865  -12.867 4.529   1.00 9.27  ? 159 PHE   B CG  1 
ATOM   3611 C  CD1 . PHE   B 1 159 ? 33.796  -12.943 5.404   1.00 8.98  ? 159 PHE   B CD1 1 
ATOM   3612 C  CD2 . PHE   B 1 159 ? 34.720  -13.419 3.272   1.00 9.25  ? 159 PHE   B CD2 1 
ATOM   3613 C  CE1 . PHE   B 1 159 ? 32.632  -13.570 5.013   1.00 9.05  ? 159 PHE   B CE1 1 
ATOM   3614 C  CE2 . PHE   B 1 159 ? 33.565  -14.069 2.891   1.00 8.87  ? 159 PHE   B CE2 1 
ATOM   3615 C  CZ  . PHE   B 1 159 ? 32.520  -14.128 3.770   1.00 9.52  ? 159 PHE   B CZ  1 
ATOM   3616 N  N   . CYS   B 1 160 ? 37.267  -9.343  6.579   1.00 10.67 ? 160 CYS   B N   1 
ATOM   3617 C  CA  . CYS   B 1 160 ? 38.436  -8.718  7.165   1.00 11.98 ? 160 CYS   B CA  1 
ATOM   3618 C  C   . CYS   B 1 160 ? 38.776  -9.155  8.583   1.00 12.33 ? 160 CYS   B C   1 
ATOM   3619 O  O   . CYS   B 1 160 ? 39.857  -8.770  9.075   1.00 14.89 ? 160 CYS   B O   1 
ATOM   3620 C  CB  . CYS   B 1 160 ? 38.288  -7.211  7.159   1.00 13.03 ? 160 CYS   B CB  1 
ATOM   3621 S  SG  . CYS   B 1 160 ? 36.789  -6.596  7.967   0.91 13.18 ? 160 CYS   B SG  1 
ATOM   3622 N  N   . TYR   B 1 161 ? 37.877  -9.856  9.284   1.00 9.77  ? 161 TYR   B N   1 
ATOM   3623 C  CA  . TYR   B 1 161 ? 38.038  -10.105 10.698  1.00 10.63 ? 161 TYR   B CA  1 
ATOM   3624 C  C   . TYR   B 1 161 ? 37.437  -11.464 11.051  1.00 10.56 ? 161 TYR   B C   1 
ATOM   3625 O  O   . TYR   B 1 161 ? 36.361  -11.805 10.569  1.00 9.69  ? 161 TYR   B O   1 
ATOM   3626 C  CB  . TYR   B 1 161 ? 37.367  -9.043  11.577  1.00 11.08 ? 161 TYR   B CB  1 
ATOM   3627 C  CG  . TYR   B 1 161 ? 37.480  -9.217  13.080  1.00 10.87 ? 161 TYR   B CG  1 
ATOM   3628 C  CD1 . TYR   B 1 161 ? 38.664  -8.905  13.749  1.00 12.55 ? 161 TYR   B CD1 1 
ATOM   3629 C  CD2 . TYR   B 1 161 ? 36.417  -9.696  13.848  1.00 11.44 ? 161 TYR   B CD2 1 
ATOM   3630 C  CE1 . TYR   B 1 161 ? 38.778  -9.029  15.126  1.00 13.30 ? 161 TYR   B CE1 1 
ATOM   3631 C  CE2 . TYR   B 1 161 ? 36.543  -9.879  15.225  1.00 12.34 ? 161 TYR   B CE2 1 
ATOM   3632 C  CZ  . TYR   B 1 161 ? 37.733  -9.551  15.866  1.00 12.30 ? 161 TYR   B CZ  1 
ATOM   3633 O  OH  . TYR   B 1 161 ? 37.837  -9.694  17.250  1.00 14.86 ? 161 TYR   B OH  1 
ATOM   3634 N  N   . MET   B 1 162 ? 38.161  -12.230 11.860  1.00 9.64  ? 162 MET   B N   1 
ATOM   3635 C  CA  . MET   B 1 162 ? 37.639  -13.422 12.506  1.00 9.44  ? 162 MET   B CA  1 
ATOM   3636 C  C   . MET   B 1 162 ? 37.876  -13.293 14.015  1.00 10.57 ? 162 MET   B C   1 
ATOM   3637 O  O   . MET   B 1 162 ? 39.020  -13.058 14.450  1.00 10.33 ? 162 MET   B O   1 
ATOM   3638 C  CB  . MET   B 1 162 ? 38.282  -14.710 11.975  1.00 10.89 ? 162 MET   B CB  1 
ATOM   3639 C  CG  . MET   B 1 162 ? 37.736  -15.915 12.672  1.00 12.19 ? 162 MET   B CG  1 
ATOM   3640 S  SD  . MET   B 1 162 ? 38.240  -17.471 11.848  1.00 18.02 ? 162 MET   B SD  1 
ATOM   3641 C  CE  . MET   B 1 162 ? 36.919  -17.629 10.640  1.00 18.62 ? 162 MET   B CE  1 
ATOM   3642 N  N   . HIS   B 1 163 ? 36.797  -13.364 14.804  1.00 10.10 ? 163 HIS   B N   1 
ATOM   3643 C  CA  . HIS   B 1 163 ? 36.854  -13.079 16.232  1.00 11.08 ? 163 HIS   B CA  1 
ATOM   3644 C  C   . HIS   B 1 163 ? 37.522  -14.242 16.985  1.00 11.72 ? 163 HIS   B C   1 
ATOM   3645 O  O   . HIS   B 1 163 ? 37.210  -15.409 16.726  1.00 11.30 ? 163 HIS   B O   1 
ATOM   3646 C  CB  . HIS   B 1 163 ? 35.441  -12.933 16.764  1.00 11.42 ? 163 HIS   B CB  1 
ATOM   3647 C  CG  . HIS   B 1 163 ? 35.389  -12.606 18.189  1.00 12.29 ? 163 HIS   B CG  1 
ATOM   3648 N  ND1 . HIS   B 1 163 ? 36.196  -11.620 18.718  1.00 13.57 ? 163 HIS   B ND1 1 
ATOM   3649 C  CD2 . HIS   B 1 163 ? 34.691  -13.109 19.183  1.00 12.98 ? 163 HIS   B CD2 1 
ATOM   3650 C  CE1 . HIS   B 1 163 ? 35.984  -11.549 20.018  1.00 15.78 ? 163 HIS   B CE1 1 
ATOM   3651 N  NE2 . HIS   B 1 163 ? 35.079  -12.434 20.340  1.00 13.47 ? 163 HIS   B NE2 1 
ATOM   3652 N  N   . HIS   B 1 164 ? 38.498  -13.940 17.845  1.00 12.31 ? 164 HIS   B N   1 
ATOM   3653 C  CA  . HIS   B 1 164 ? 39.121  -14.982 18.661  1.00 13.27 ? 164 HIS   B CA  1 
ATOM   3654 C  C   . HIS   B 1 164 ? 38.808  -14.772 20.141  1.00 16.77 ? 164 HIS   B C   1 
ATOM   3655 O  O   . HIS   B 1 164 ? 38.286  -15.668 20.804  1.00 18.47 ? 164 HIS   B O   1 
ATOM   3656 C  CB  . HIS   B 1 164 ? 40.626  -15.085 18.370  1.00 13.54 ? 164 HIS   B CB  1 
ATOM   3657 C  CG  . HIS   B 1 164 ? 41.010  -15.682 17.046  1.00 14.28 ? 164 HIS   B CG  1 
ATOM   3658 N  ND1 . HIS   B 1 164 ? 41.840  -16.791 16.934  1.00 14.90 ? 164 HIS   B ND1 1 
ATOM   3659 C  CD2 . HIS   B 1 164 ? 40.731  -15.301 15.789  1.00 13.83 ? 164 HIS   B CD2 1 
ATOM   3660 C  CE1 . HIS   B 1 164 ? 42.031  -17.042 15.647  1.00 15.03 ? 164 HIS   B CE1 1 
ATOM   3661 N  NE2 . HIS   B 1 164 ? 41.350  -16.171 14.916  1.00 15.08 ? 164 HIS   B NE2 1 
ATOM   3662 N  N   . MET   B 1 165 ? 39.096  -13.591 20.700  1.00 18.32 ? 165 MET   B N   1 
ATOM   3663 C  CA  . MET   B 1 165 ? 39.070  -13.535 22.143  1.00 19.15 ? 165 MET   B CA  1 
ATOM   3664 C  C   . MET   B 1 165 ? 38.628  -12.177 22.673  1.00 17.88 ? 165 MET   B C   1 
ATOM   3665 O  O   . MET   B 1 165 ? 38.705  -11.165 21.962  1.00 18.11 ? 165 MET   B O   1 
ATOM   3666 C  CB  . MET   B 1 165 ? 40.450  -13.885 22.700  1.00 21.21 ? 165 MET   B CB  1 
ATOM   3667 C  CG  . MET   B 1 165 ? 41.564  -13.147 22.117  1.00 23.81 ? 165 MET   B CG  1 
ATOM   3668 S  SD  . MET   B 1 165 ? 43.161  -13.953 22.524  0.79 25.81 ? 165 MET   B SD  1 
ATOM   3669 C  CE  . MET   B 1 165 ? 44.242  -12.613 22.078  1.00 28.41 ? 165 MET   B CE  1 
ATOM   3670 N  N   . GLU   B 1 166 ? 38.154  -12.221 23.914  1.00 19.23 ? 166 GLU   B N   1 
ATOM   3671 C  CA  . GLU   B 1 166 ? 37.885  -11.031 24.695  1.00 22.55 ? 166 GLU   B CA  1 
ATOM   3672 C  C   . GLU   B 1 166 ? 39.039  -10.778 25.668  1.00 26.29 ? 166 GLU   B C   1 
ATOM   3673 O  O   . GLU   B 1 166 ? 39.531  -11.700 26.319  1.00 26.51 ? 166 GLU   B O   1 
ATOM   3674 C  CB  . GLU   B 1 166 ? 36.539  -11.141 25.399  1.00 27.60 ? 166 GLU   B CB  1 
ATOM   3675 C  CG  . GLU   B 1 166 ? 36.124  -9.815  26.030  1.00 32.93 ? 166 GLU   B CG  1 
ATOM   3676 C  CD  . GLU   B 1 166 ? 34.737  -9.772  26.650  1.00 37.46 ? 166 GLU   B CD  1 
ATOM   3677 O  OE1 . GLU   B 1 166 ? 34.676  -9.764  27.900  1.00 37.98 ? 166 GLU   B OE1 1 
ATOM   3678 O  OE2 . GLU   B 1 166 ? 33.716  -9.738  25.879  1.00 32.75 ? 166 GLU   B OE2 1 
ATOM   3679 N  N   . LEU   B 1 167 ? 39.477  -9.516  25.724  1.00 27.09 ? 167 LEU   B N   1 
ATOM   3680 C  CA  . LEU   B 1 167 ? 40.595  -9.081  26.548  1.00 28.46 ? 167 LEU   B CA  1 
ATOM   3681 C  C   . LEU   B 1 167 ? 40.061  -8.640  27.895  1.00 26.95 ? 167 LEU   B C   1 
ATOM   3682 O  O   . LEU   B 1 167 ? 38.887  -8.339  28.010  1.00 24.06 ? 167 LEU   B O   1 
ATOM   3683 C  CB  . LEU   B 1 167 ? 41.291  -7.881  25.896  1.00 29.78 ? 167 LEU   B CB  1 
ATOM   3684 C  CG  . LEU   B 1 167 ? 41.968  -8.127  24.553  1.00 30.57 ? 167 LEU   B CG  1 
ATOM   3685 C  CD1 . LEU   B 1 167 ? 42.938  -7.007  24.245  1.00 34.54 ? 167 LEU   B CD1 1 
ATOM   3686 C  CD2 . LEU   B 1 167 ? 42.697  -9.467  24.516  1.00 31.59 ? 167 LEU   B CD2 1 
ATOM   3687 N  N   . PRO   B 1 168 ? 40.917  -8.565  28.948  1.00 36.02 ? 168 PRO   B N   1 
ATOM   3688 C  CA  . PRO   B 1 168 ? 40.484  -8.136  30.283  1.00 37.44 ? 168 PRO   B CA  1 
ATOM   3689 C  C   . PRO   B 1 168 ? 39.598  -6.895  30.342  1.00 33.17 ? 168 PRO   B C   1 
ATOM   3690 O  O   . PRO   B 1 168 ? 38.665  -6.859  31.133  1.00 36.08 ? 168 PRO   B O   1 
ATOM   3691 C  CB  . PRO   B 1 168 ? 41.829  -7.905  31.000  1.00 36.67 ? 168 PRO   B CB  1 
ATOM   3692 C  CG  . PRO   B 1 168 ? 42.725  -8.978  30.399  1.00 38.65 ? 168 PRO   B CG  1 
ATOM   3693 C  CD  . PRO   B 1 168 ? 42.331  -8.972  28.935  1.00 38.28 ? 168 PRO   B CD  1 
ATOM   3694 N  N   . THR   B 1 169 ? 39.853  -5.885  29.502  1.00 34.34 ? 169 THR   B N   1 
ATOM   3695 C  CA  . THR   B 1 169 ? 39.074  -4.648  29.549  1.00 32.02 ? 169 THR   B CA  1 
ATOM   3696 C  C   . THR   B 1 169 ? 37.694  -4.774  28.888  1.00 29.60 ? 169 THR   B C   1 
ATOM   3697 O  O   . THR   B 1 169 ? 36.885  -3.849  28.924  1.00 29.02 ? 169 THR   B O   1 
ATOM   3698 C  CB  . THR   B 1 169 ? 39.870  -3.503  28.914  1.00 36.47 ? 169 THR   B CB  1 
ATOM   3699 O  OG1 . THR   B 1 169 ? 40.290  -3.895  27.600  1.00 32.45 ? 169 THR   B OG1 1 
ATOM   3700 C  CG2 . THR   B 1 169 ? 41.064  -3.105  29.756  1.00 35.42 ? 169 THR   B CG2 1 
ATOM   3701 N  N   . GLY   B 1 170 ? 37.423  -5.881  28.199  1.00 24.39 ? 170 GLY   B N   1 
ATOM   3702 C  CA  . GLY   B 1 170 ? 36.118  -6.078  27.602  1.00 24.64 ? 170 GLY   B CA  1 
ATOM   3703 C  C   . GLY   B 1 170 ? 36.109  -5.845  26.091  1.00 23.11 ? 170 GLY   B C   1 
ATOM   3704 O  O   . GLY   B 1 170 ? 35.074  -6.018  25.440  1.00 24.69 ? 170 GLY   B O   1 
ATOM   3705 N  N   . VAL   B 1 171 ? 37.241  -5.408  25.553  1.00 21.71 ? 171 VAL   B N   1 
ATOM   3706 C  CA  . VAL   B 1 171 ? 37.407  -5.267  24.119  1.00 21.37 ? 171 VAL   B CA  1 
ATOM   3707 C  C   . VAL   B 1 171 ? 37.817  -6.610  23.513  1.00 19.32 ? 171 VAL   B C   1 
ATOM   3708 O  O   . VAL   B 1 171 ? 38.068  -7.589  24.211  1.00 20.49 ? 171 VAL   B O   1 
ATOM   3709 C  CB  . VAL   B 1 171 ? 38.407  -4.139  23.797  1.00 22.26 ? 171 VAL   B CB  1 
ATOM   3710 C  CG1 . VAL   B 1 171 ? 37.923  -2.844  24.439  1.00 25.39 ? 171 VAL   B CG1 1 
ATOM   3711 C  CG2 . VAL   B 1 171 ? 39.838  -4.455  24.208  1.00 23.17 ? 171 VAL   B CG2 1 
ATOM   3712 N  N   . HIS   B 1 172 ? 37.834  -6.639  22.185  1.00 19.41 ? 172 HIS   B N   1 
ATOM   3713 C  CA  . HIS   B 1 172 ? 37.879  -7.891  21.457  1.00 17.06 ? 172 HIS   B CA  1 
ATOM   3714 C  C   . HIS   B 1 172 ? 39.080  -7.922  20.540  1.00 16.25 ? 172 HIS   B C   1 
ATOM   3715 O  O   . HIS   B 1 172 ? 39.516  -6.894  20.030  1.00 15.81 ? 172 HIS   B O   1 
ATOM   3716 C  CB  . HIS   B 1 172 ? 36.538  -8.057  20.728  1.00 17.59 ? 172 HIS   B CB  1 
ATOM   3717 C  CG  . HIS   B 1 172 ? 35.414  -8.125  21.695  1.00 17.84 ? 172 HIS   B CG  1 
ATOM   3718 N  ND1 . HIS   B 1 172 ? 34.468  -7.122  21.813  1.00 17.08 ? 172 HIS   B ND1 1 
ATOM   3719 C  CD2 . HIS   B 1 172 ? 35.134  -9.033  22.650  1.00 17.18 ? 172 HIS   B CD2 1 
ATOM   3720 C  CE1 . HIS   B 1 172 ? 33.618  -7.436  22.779  1.00 19.19 ? 172 HIS   B CE1 1 
ATOM   3721 N  NE2 . HIS   B 1 172 ? 33.983  -8.614  23.281  1.00 17.29 ? 172 HIS   B NE2 1 
ATOM   3722 N  N   . ALA   B 1 173 ? 39.639  -9.141  20.355  1.00 14.06 ? 173 ALA   B N   1 
ATOM   3723 C  CA  . ALA   B 1 173 ? 40.810  -9.323  19.545  1.00 13.31 ? 173 ALA   B CA  1 
ATOM   3724 C  C   . ALA   B 1 173 ? 40.585  -10.507 18.613  1.00 12.27 ? 173 ALA   B C   1 
ATOM   3725 O  O   . ALA   B 1 173 ? 39.913  -11.499 18.955  1.00 15.09 ? 173 ALA   B O   1 
ATOM   3726 C  CB  . ALA   B 1 173 ? 42.066  -9.542  20.352  1.00 13.47 ? 173 ALA   B CB  1 
ATOM   3727 N  N   . GLY   B 1 174 ? 41.182  -10.376 17.448  1.00 13.67 ? 174 GLY   B N   1 
ATOM   3728 C  CA  . GLY   B 1 174 ? 41.056  -11.374 16.398  1.00 12.78 ? 174 GLY   B CA  1 
ATOM   3729 C  C   . GLY   B 1 174 ? 42.027  -11.207 15.253  1.00 12.37 ? 174 GLY   B C   1 
ATOM   3730 O  O   . GLY   B 1 174 ? 42.987  -10.432 15.301  1.00 15.70 ? 174 GLY   B O   1 
ATOM   3731 N  N   . THR   B 1 175 ? 41.782  -11.977 14.166  1.00 11.63 ? 175 THR   B N   1 
ATOM   3732 C  CA  . THR   B 1 175 ? 42.717  -12.140 13.076  1.00 11.32 ? 175 THR   B CA  1 
ATOM   3733 C  C   . THR   B 1 175 ? 42.058  -11.758 11.770  1.00 11.85 ? 175 THR   B C   1 
ATOM   3734 O  O   . THR   B 1 175 ? 40.841  -11.548 11.700  1.00 12.07 ? 175 THR   B O   1 
ATOM   3735 C  CB  . THR   B 1 175 ? 43.219  -13.603 12.971  1.00 12.75 ? 175 THR   B CB  1 
ATOM   3736 O  OG1 . THR   B 1 175 ? 42.105  -14.398 12.542  1.00 12.29 ? 175 THR   B OG1 1 
ATOM   3737 C  CG2 . THR   B 1 175 ? 43.809  -14.106 14.263  1.00 12.91 ? 175 THR   B CG2 1 
ATOM   3738 N  N   . ASP   B 1 176 ? 42.866  -11.649 10.713  1.00 11.27 ? 176 ASP   B N   1 
ATOM   3739 C  CA  . ASP   B 1 176 ? 42.332  -11.617 9.378   1.00 11.84 ? 176 ASP   B CA  1 
ATOM   3740 C  C   . ASP   B 1 176 ? 42.030  -13.071 8.977   1.00 10.69 ? 176 ASP   B C   1 
ATOM   3741 O  O   . ASP   B 1 176 ? 42.216  -13.986 9.786   1.00 11.80 ? 176 ASP   B O   1 
ATOM   3742 C  CB  . ASP   B 1 176 ? 43.272  -10.877 8.422   1.00 14.00 ? 176 ASP   B CB  1 
ATOM   3743 C  CG  . ASP   B 1 176 ? 44.619  -11.526 8.205   1.00 16.27 ? 176 ASP   B CG  1 
ATOM   3744 O  OD1 . ASP   B 1 176 ? 44.744  -12.752 8.498   1.00 18.33 ? 176 ASP   B OD1 1 
ATOM   3745 O  OD2 . ASP   B 1 176 ? 45.546  -10.792 7.770   1.00 18.45 ? 176 ASP   B OD2 1 
ATOM   3746 N  N   . LEU   B 1 177 ? 41.555  -13.290 7.755   1.00 11.02 ? 177 LEU   B N   1 
ATOM   3747 C  CA  . LEU   B 1 177 ? 41.144  -14.626 7.313   1.00 12.19 ? 177 LEU   B CA  1 
ATOM   3748 C  C   . LEU   B 1 177 ? 42.348  -15.445 6.851   1.00 15.00 ? 177 LEU   B C   1 
ATOM   3749 O  O   . LEU   B 1 177 ? 42.187  -16.624 6.505   1.00 13.14 ? 177 LEU   B O   1 
ATOM   3750 C  CB  . LEU   B 1 177 ? 40.053  -14.584 6.237   1.00 12.96 ? 177 LEU   B CB  1 
ATOM   3751 C  CG  . LEU   B 1 177 ? 38.636  -14.566 6.812   1.00 12.41 ? 177 LEU   B CG  1 
ATOM   3752 C  CD1 . LEU   B 1 177 ? 38.330  -15.919 7.474   1.00 15.20 ? 177 LEU   B CD1 1 
ATOM   3753 C  CD2 . LEU   B 1 177 ? 38.418  -13.442 7.801   1.00 13.21 ? 177 LEU   B CD2 1 
ATOM   3754 N  N   . GLU   B 1 178 ? 43.554  -14.847 6.870   1.00 14.98 ? 178 GLU   B N   1 
ATOM   3755 C  CA  . GLU   B 1 178 ? 44.813  -15.588 6.729   1.00 16.95 ? 178 GLU   B CA  1 
ATOM   3756 C  C   . GLU   B 1 178 ? 45.416  -15.942 8.081   1.00 16.38 ? 178 GLU   B C   1 
ATOM   3757 O  O   . GLU   B 1 178 ? 46.500  -16.563 8.158   1.00 17.85 ? 178 GLU   B O   1 
ATOM   3758 C  CB  . GLU   B 1 178 ? 45.808  -14.791 5.873   1.00 20.17 ? 178 GLU   B CB  1 
ATOM   3759 C  CG  . GLU   B 1 178 ? 45.384  -14.646 4.443   1.00 24.50 ? 178 GLU   B CG  1 
ATOM   3760 C  CD  . GLU   B 1 178 ? 46.453  -13.997 3.570   1.00 32.63 ? 178 GLU   B CD  1 
ATOM   3761 O  OE1 . GLU   B 1 178 ? 47.094  -13.044 4.029   1.00 31.61 ? 178 GLU   B OE1 1 
ATOM   3762 O  OE2 . GLU   B 1 178 ? 46.640  -14.450 2.440   1.00 37.84 ? 178 GLU   B OE2 1 
ATOM   3763 N  N   . GLY   B 1 179 ? 44.678  -15.660 9.173   1.00 13.64 ? 179 GLY   B N   1 
ATOM   3764 C  CA  . GLY   B 1 179 ? 45.036  -16.057 10.520  1.00 13.56 ? 179 GLY   B CA  1 
ATOM   3765 C  C   . GLY   B 1 179 ? 46.110  -15.211 11.177  1.00 15.65 ? 179 GLY   B C   1 
ATOM   3766 O  O   . GLY   B 1 179 ? 46.642  -15.596 12.212  1.00 13.79 ? 179 GLY   B O   1 
ATOM   3767 N  N   . ASN   B 1 180 ? 46.393  -14.027 10.619  1.00 16.74 ? 180 ASN   B N   1 
ATOM   3768 C  CA  . ASN   B 1 180 ? 47.334  -13.126 11.277  1.00 16.93 ? 180 ASN   B CA  1 
ATOM   3769 C  C   . ASN   B 1 180 ? 46.559  -12.181 12.193  1.00 17.81 ? 180 ASN   B C   1 
ATOM   3770 O  O   . ASN   B 1 180 ? 45.668  -11.469 11.704  1.00 15.30 ? 180 ASN   B O   1 
ATOM   3771 C  CB  . ASN   B 1 180 ? 48.150  -12.309 10.283  1.00 18.21 ? 180 ASN   B CB  1 
ATOM   3772 C  CG  . ASN   B 1 180 ? 49.105  -13.140 9.438   1.00 18.30 ? 180 ASN   B CG  1 
ATOM   3773 O  OD1 . ASN   B 1 180 ? 49.903  -13.890 9.965   1.00 22.15 ? 180 ASN   B OD1 1 
ATOM   3774 N  ND2 . ASN   B 1 180 ? 48.991  -13.061 8.135   1.00 22.55 ? 180 ASN   B ND2 1 
ATOM   3775 N  N   . PHE   B 1 181 ? 46.885  -12.212 13.488  1.00 14.29 ? 181 PHE   B N   1 
ATOM   3776 C  CA  . PHE   B 1 181 ? 46.272  -11.302 14.450  1.00 15.07 ? 181 PHE   B CA  1 
ATOM   3777 C  C   . PHE   B 1 181 ? 46.455  -9.844  14.051  1.00 15.38 ? 181 PHE   B C   1 
ATOM   3778 O  O   . PHE   B 1 181 ? 47.456  -9.454  13.455  1.00 15.05 ? 181 PHE   B O   1 
ATOM   3779 C  CB  . PHE   B 1 181 ? 46.820  -11.462 15.872  1.00 15.24 ? 181 PHE   B CB  1 
ATOM   3780 C  CG  . PHE   B 1 181 ? 46.041  -12.385 16.744  1.00 15.89 ? 181 PHE   B CG  1 
ATOM   3781 C  CD1 . PHE   B 1 181 ? 44.949  -11.917 17.443  1.00 15.09 ? 181 PHE   B CD1 1 
ATOM   3782 C  CD2 . PHE   B 1 181 ? 46.328  -13.752 16.800  1.00 14.66 ? 181 PHE   B CD2 1 
ATOM   3783 C  CE1 . PHE   B 1 181 ? 44.195  -12.771 18.228  1.00 15.94 ? 181 PHE   B CE1 1 
ATOM   3784 C  CE2 . PHE   B 1 181 ? 45.548  -14.598 17.573  1.00 15.24 ? 181 PHE   B CE2 1 
ATOM   3785 C  CZ  . PHE   B 1 181 ? 44.492  -14.114 18.278  1.00 15.15 ? 181 PHE   B CZ  1 
ATOM   3786 N  N   . TYR   B 1 182 ? 45.410  -9.073  14.353  1.00 15.40 ? 182 TYR   B N   1 
ATOM   3787 C  CA  . TYR   B 1 182 ? 45.499  -7.623  14.438  1.00 14.89 ? 182 TYR   B CA  1 
ATOM   3788 C  C   . TYR   B 1 182 ? 46.039  -7.306  15.830  1.00 16.01 ? 182 TYR   B C   1 
ATOM   3789 O  O   . TYR   B 1 182 ? 45.477  -7.700  16.840  1.00 17.08 ? 182 TYR   B O   1 
ATOM   3790 C  CB  . TYR   B 1 182 ? 44.118  -6.994  14.219  1.00 14.23 ? 182 TYR   B CB  1 
ATOM   3791 C  CG  . TYR   B 1 182 ? 43.536  -7.125  12.837  1.00 14.32 ? 182 TYR   B CG  1 
ATOM   3792 C  CD1 . TYR   B 1 182 ? 43.933  -6.292  11.805  1.00 14.31 ? 182 TYR   B CD1 1 
ATOM   3793 C  CD2 . TYR   B 1 182 ? 42.568  -8.088  12.547  1.00 13.80 ? 182 TYR   B CD2 1 
ATOM   3794 C  CE1 . TYR   B 1 182 ? 43.397  -6.386  10.546  1.00 14.84 ? 182 TYR   B CE1 1 
ATOM   3795 C  CE2 . TYR   B 1 182 ? 42.044  -8.205  11.279  1.00 13.04 ? 182 TYR   B CE2 1 
ATOM   3796 C  CZ  . TYR   B 1 182 ? 42.446  -7.353  10.276  1.00 13.39 ? 182 TYR   B CZ  1 
ATOM   3797 O  OH  . TYR   B 1 182 ? 41.965  -7.368  9.013   1.00 11.95 ? 182 TYR   B OH  1 
ATOM   3798 N  N   . GLY   B 1 183 ? 47.189  -6.640  15.857  1.00 20.31 ? 183 GLY   B N   1 
ATOM   3799 C  CA  . GLY   B 1 183 ? 47.802  -6.269  17.109  1.00 19.98 ? 183 GLY   B CA  1 
ATOM   3800 C  C   . GLY   B 1 183 ? 48.726  -7.338  17.670  1.00 25.20 ? 183 GLY   B C   1 
ATOM   3801 O  O   . GLY   B 1 183 ? 48.874  -8.426  17.094  1.00 22.76 ? 183 GLY   B O   1 
ATOM   3802 N  N   . PRO   B 1 184 ? 49.361  -7.023  18.826  1.00 28.46 ? 184 PRO   B N   1 
ATOM   3803 C  CA  . PRO   B 1 184 ? 50.318  -7.929  19.473  1.00 27.27 ? 184 PRO   B CA  1 
ATOM   3804 C  C   . PRO   B 1 184 ? 49.608  -8.873  20.430  1.00 29.68 ? 184 PRO   B C   1 
ATOM   3805 O  O   . PRO   B 1 184 ? 49.802  -8.799  21.645  1.00 36.69 ? 184 PRO   B O   1 
ATOM   3806 C  CB  . PRO   B 1 184 ? 51.202  -6.896  20.199  1.00 26.51 ? 184 PRO   B CB  1 
ATOM   3807 C  CG  . PRO   B 1 184 ? 50.210  -5.870  20.701  1.00 27.73 ? 184 PRO   B CG  1 
ATOM   3808 C  CD  . PRO   B 1 184 ? 49.218  -5.739  19.553  1.00 29.23 ? 184 PRO   B CD  1 
ATOM   3809 N  N   . PHE   B 1 185 ? 48.713  -9.701  19.887  1.00 22.57 ? 185 PHE   B N   1 
ATOM   3810 C  CA  . PHE   B 1 185 ? 47.985  -10.665 20.675  1.00 22.25 ? 185 PHE   B CA  1 
ATOM   3811 C  C   . PHE   B 1 185 ? 48.334  -12.036 20.105  1.00 16.50 ? 185 PHE   B C   1 
ATOM   3812 O  O   . PHE   B 1 185 ? 48.816  -12.126 18.982  1.00 19.70 ? 185 PHE   B O   1 
ATOM   3813 C  CB  . PHE   B 1 185 ? 46.475  -10.391 20.655  1.00 20.89 ? 185 PHE   B CB  1 
ATOM   3814 C  CG  . PHE   B 1 185 ? 46.114  -8.982  21.039  1.00 21.67 ? 185 PHE   B CG  1 
ATOM   3815 C  CD1 . PHE   B 1 185 ? 46.307  -8.552  22.335  1.00 21.43 ? 185 PHE   B CD1 1 
ATOM   3816 C  CD2 . PHE   B 1 185 ? 45.636  -8.086  20.103  1.00 22.46 ? 185 PHE   B CD2 1 
ATOM   3817 C  CE1 . PHE   B 1 185 ? 45.989  -7.261  22.710  1.00 24.03 ? 185 PHE   B CE1 1 
ATOM   3818 C  CE2 . PHE   B 1 185 ? 45.330  -6.783  20.472  1.00 24.34 ? 185 PHE   B CE2 1 
ATOM   3819 C  CZ  . PHE   B 1 185 ? 45.494  -6.380  21.780  1.00 24.20 ? 185 PHE   B CZ  1 
ATOM   3820 N  N   . VAL   B 1 186 ? 48.156  -13.019 20.957  1.00 20.90 ? 186 VAL   B N   1 
ATOM   3821 C  CA  . VAL   B 1 186 ? 48.377  -14.417 20.619  1.00 20.57 ? 186 VAL   B CA  1 
ATOM   3822 C  C   . VAL   B 1 186 ? 47.155  -15.206 21.087  1.00 18.81 ? 186 VAL   B C   1 
ATOM   3823 O  O   . VAL   B 1 186 ? 46.463  -14.875 22.046  1.00 17.38 ? 186 VAL   B O   1 
ATOM   3824 C  CB  . VAL   B 1 186 ? 49.684  -14.956 21.256  1.00 22.25 ? 186 VAL   B CB  1 
ATOM   3825 C  CG1 . VAL   B 1 186 ? 50.927  -14.257 20.746  1.00 24.77 ? 186 VAL   B CG1 1 
ATOM   3826 C  CG2 . VAL   B 1 186 ? 49.618  -14.881 22.748  1.00 24.88 ? 186 VAL   B CG2 1 
ATOM   3827 N  N   . ASP   B 1 187 ? 46.913  -16.368 20.432  1.00 19.28 ? 187 ASP   B N   1 
ATOM   3828 C  CA  . ASP   B 1 187 ? 45.769  -17.190 20.759  1.00 21.77 ? 187 ASP   B CA  1 
ATOM   3829 C  C   . ASP   B 1 187 ? 46.063  -18.161 21.903  1.00 26.22 ? 187 ASP   B C   1 
ATOM   3830 O  O   . ASP   B 1 187 ? 46.112  -19.383 21.746  1.00 25.59 ? 187 ASP   B O   1 
ATOM   3831 C  CB  . ASP   B 1 187 ? 45.220  -17.925 19.526  1.00 20.00 ? 187 ASP   B CB  1 
ATOM   3832 C  CG  . ASP   B 1 187 ? 46.204  -18.613 18.614  1.00 20.52 ? 187 ASP   B CG  1 
ATOM   3833 O  OD1 . ASP   B 1 187 ? 47.471  -18.395 18.729  1.00 20.47 ? 187 ASP   B OD1 1 
ATOM   3834 O  OD2 . ASP   B 1 187 ? 45.705  -19.329 17.715  1.00 21.12 ? 187 ASP   B OD2 1 
ATOM   3835 N  N   . ARG   B 1 188 ? 46.133  -17.610 23.102  1.00 27.09 ? 188 ARG   B N   1 
ATOM   3836 C  CA  . ARG   B 1 188 ? 46.261  -18.394 24.314  1.00 31.40 ? 188 ARG   B CA  1 
ATOM   3837 C  C   . ARG   B 1 188 ? 45.364  -17.719 25.330  1.00 28.42 ? 188 ARG   B C   1 
ATOM   3838 O  O   . ARG   B 1 188 ? 45.228  -16.498 25.278  1.00 27.08 ? 188 ARG   B O   1 
ATOM   3839 C  CB  . ARG   B 1 188 ? 47.671  -18.329 24.913  1.00 34.57 ? 188 ARG   B CB  1 
ATOM   3840 C  CG  . ARG   B 1 188 ? 48.810  -18.507 23.928  1.00 44.85 ? 188 ARG   B CG  1 
ATOM   3841 C  CD  . ARG   B 1 188 ? 50.133  -18.027 24.499  1.00 49.11 ? 188 ARG   B CD  1 
ATOM   3842 N  NE  . ARG   B 1 188 ? 50.266  -18.369 25.908  1.00 58.50 ? 188 ARG   B NE  1 
ATOM   3843 C  CZ  . ARG   B 1 188 ? 51.343  -18.150 26.660  1.00 59.37 ? 188 ARG   B CZ  1 
ATOM   3844 N  NH1 . ARG   B 1 188 ? 52.411  -17.551 26.154  1.00 55.83 ? 188 ARG   B NH1 1 
ATOM   3845 N  NH2 . ARG   B 1 188 ? 51.337  -18.544 27.924  1.00 56.36 ? 188 ARG   B NH2 1 
ATOM   3846 N  N   . GLN   B 1 189 ? 44.813  -18.505 26.250  1.00 27.32 ? 189 GLN   B N   1 
ATOM   3847 C  CA  . GLN   B 1 189 ? 43.961  -17.984 27.293  1.00 31.83 ? 189 GLN   B CA  1 
ATOM   3848 C  C   . GLN   B 1 189 ? 44.854  -17.534 28.451  1.00 34.97 ? 189 GLN   B C   1 
ATOM   3849 O  O   . GLN   B 1 189 ? 44.975  -18.230 29.460  1.00 39.10 ? 189 GLN   B O   1 
ATOM   3850 C  CB  . GLN   B 1 189 ? 42.941  -19.049 27.663  1.00 34.80 ? 189 GLN   B CB  1 
ATOM   3851 C  CG  . GLN   B 1 189 ? 41.854  -18.580 28.613  1.00 38.74 ? 189 GLN   B CG  1 
ATOM   3852 C  CD  . GLN   B 1 189 ? 40.808  -19.661 28.722  1.00 44.34 ? 189 GLN   B CD  1 
ATOM   3853 O  OE1 . GLN   B 1 189 ? 41.107  -20.803 29.070  1.00 47.46 ? 189 GLN   B OE1 1 
ATOM   3854 N  NE2 . GLN   B 1 189 ? 39.579  -19.323 28.364  1.00 50.16 ? 189 GLN   B NE2 1 
ATOM   3855 N  N   . THR   B 1 190 ? 45.540  -16.412 28.211  1.00 38.07 ? 190 THR   B N   1 
ATOM   3856 C  CA  . THR   B 1 190 ? 46.255  -15.633 29.212  1.00 39.80 ? 190 THR   B CA  1 
ATOM   3857 C  C   . THR   B 1 190 ? 45.795  -14.184 29.092  1.00 38.76 ? 190 THR   B C   1 
ATOM   3858 O  O   . THR   B 1 190 ? 45.398  -13.768 28.005  1.00 31.10 ? 190 THR   B O   1 
ATOM   3859 C  CB  . THR   B 1 190 ? 47.772  -15.672 28.993  1.00 43.18 ? 190 THR   B CB  1 
ATOM   3860 O  OG1 . THR   B 1 190 ? 48.081  -15.031 27.752  1.00 50.64 ? 190 THR   B OG1 1 
ATOM   3861 C  CG2 . THR   B 1 190 ? 48.338  -17.072 28.955  1.00 48.25 ? 190 THR   B CG2 1 
ATOM   3862 N  N   . ALA   B 1 191 ? 45.861  -13.437 30.202  1.00 38.79 ? 191 ALA   B N   1 
ATOM   3863 C  CA  . ALA   B 1 191 ? 45.579  -12.004 30.204  1.00 38.12 ? 191 ALA   B CA  1 
ATOM   3864 C  C   . ALA   B 1 191 ? 46.609  -11.272 29.348  1.00 33.88 ? 191 ALA   B C   1 
ATOM   3865 O  O   . ALA   B 1 191 ? 47.813  -11.389 29.555  1.00 35.19 ? 191 ALA   B O   1 
ATOM   3866 C  CB  . ALA   B 1 191 ? 45.579  -11.454 31.615  1.00 39.76 ? 191 ALA   B CB  1 
ATOM   3867 N  N   . GLN   B 1 192 ? 46.115  -10.563 28.332  1.00 31.15 ? 192 GLN   B N   1 
ATOM   3868 C  CA  . GLN   B 1 192 ? 46.932  -9.735  27.477  1.00 32.70 ? 192 GLN   B CA  1 
ATOM   3869 C  C   . GLN   B 1 192 ? 46.287  -8.356  27.507  1.00 31.03 ? 192 GLN   B C   1 
ATOM   3870 O  O   . GLN   B 1 192 ? 45.074  -8.245  27.384  1.00 36.28 ? 192 GLN   B O   1 
ATOM   3871 C  CB  . GLN   B 1 192 ? 46.963  -10.270 26.041  1.00 30.01 ? 192 GLN   B CB  1 
ATOM   3872 C  CG  . GLN   B 1 192 ? 47.430  -11.714 25.951  1.00 30.70 ? 192 GLN   B CG  1 
ATOM   3873 C  CD  . GLN   B 1 192 ? 47.166  -12.349 24.611  1.00 23.53 ? 192 GLN   B CD  1 
ATOM   3874 O  OE1 . GLN   B 1 192 ? 47.634  -11.879 23.578  1.00 22.96 ? 192 GLN   B OE1 1 
ATOM   3875 N  NE2 . GLN   B 1 192 ? 46.508  -13.493 24.648  1.00 26.65 ? 192 GLN   B NE2 1 
ATOM   3876 N  N   . ALA   B 1 193 ? 47.102  -7.323  27.618  1.00 30.73 ? 193 ALA   B N   1 
ATOM   3877 C  CA  . ALA   B 1 193 ? 46.544  -5.983  27.688  1.00 32.16 ? 193 ALA   B CA  1 
ATOM   3878 C  C   . ALA   B 1 193 ? 46.646  -5.337  26.314  1.00 26.43 ? 193 ALA   B C   1 
ATOM   3879 O  O   . ALA   B 1 193 ? 47.644  -5.462  25.617  1.00 29.52 ? 193 ALA   B O   1 
ATOM   3880 C  CB  . ALA   B 1 193 ? 47.256  -5.174  28.741  1.00 30.70 ? 193 ALA   B CB  1 
ATOM   3881 N  N   . ALA   B 1 194 ? 45.596  -4.619  25.933  1.00 31.27 ? 194 ALA   B N   1 
ATOM   3882 C  CA  . ALA   B 1 194 ? 45.688  -3.736  24.785  1.00 35.38 ? 194 ALA   B CA  1 
ATOM   3883 C  C   . ALA   B 1 194 ? 46.494  -2.490  25.155  1.00 36.49 ? 194 ALA   B C   1 
ATOM   3884 O  O   . ALA   B 1 194 ? 46.348  -1.979  26.260  1.00 38.81 ? 194 ALA   B O   1 
ATOM   3885 C  CB  . ALA   B 1 194 ? 44.295  -3.380  24.341  1.00 38.78 ? 194 ALA   B CB  1 
ATOM   3886 N  N   . GLY   B 1 195 ? 47.381  -2.074  24.243  1.00 34.02 ? 195 GLY   B N   1 
ATOM   3887 C  CA  . GLY   B 1 195 ? 48.064  -0.790  24.284  1.00 39.60 ? 195 GLY   B CA  1 
ATOM   3888 C  C   . GLY   B 1 195 ? 47.095  0.375   24.477  1.00 36.45 ? 195 GLY   B C   1 
ATOM   3889 O  O   . GLY   B 1 195 ? 45.878  0.220   24.366  1.00 33.33 ? 195 GLY   B O   1 
ATOM   3890 N  N   . THR   B 1 196 ? 47.637  1.543   24.839  1.00 32.73 ? 196 THR   B N   1 
ATOM   3891 C  CA  . THR   B 1 196 ? 46.792  2.711   25.031  1.00 29.15 ? 196 THR   B CA  1 
ATOM   3892 C  C   . THR   B 1 196 ? 46.107  3.030   23.711  1.00 23.34 ? 196 THR   B C   1 
ATOM   3893 O  O   . THR   B 1 196 ? 46.759  3.005   22.679  1.00 31.33 ? 196 THR   B O   1 
ATOM   3894 C  CB  . THR   B 1 196 ? 47.627  3.921   25.463  1.00 31.26 ? 196 THR   B CB  1 
ATOM   3895 O  OG1 . THR   B 1 196 ? 48.432  3.494   26.561  1.00 34.17 ? 196 THR   B OG1 1 
ATOM   3896 C  CG2 . THR   B 1 196 ? 46.761  5.092   25.861  1.00 34.02 ? 196 THR   B CG2 1 
ATOM   3897 N  N   . ASP   B 1 197 ? 44.839  3.408   23.764  1.00 24.15 ? 197 ASP   B N   1 
ATOM   3898 C  CA  . ASP   B 1 197 ? 44.107  3.688   22.533  1.00 22.90 ? 197 ASP   B CA  1 
ATOM   3899 C  C   . ASP   B 1 197 ? 44.203  5.188   22.263  1.00 22.86 ? 197 ASP   B C   1 
ATOM   3900 O  O   . ASP   B 1 197 ? 44.527  5.960   23.171  1.00 22.44 ? 197 ASP   B O   1 
ATOM   3901 C  CB  . ASP   B 1 197 ? 42.649  3.239   22.608  1.00 22.44 ? 197 ASP   B CB  1 
ATOM   3902 C  CG  . ASP   B 1 197 ? 42.078  3.015   21.217  1.00 24.81 ? 197 ASP   B CG  1 
ATOM   3903 O  OD1 . ASP   B 1 197 ? 42.889  2.742   20.280  1.00 22.98 ? 197 ASP   B OD1 1 
ATOM   3904 O  OD2 . ASP   B 1 197 ? 40.865  3.101   21.073  1.00 21.70 ? 197 ASP   B OD2 1 
ATOM   3905 N  N   . THR   B 1 198 ? 43.950  5.562   21.012  1.00 18.55 ? 198 THR   B N   1 
ATOM   3906 C  CA  . THR   B 1 198 ? 43.959  6.950   20.564  1.00 17.69 ? 198 THR   B CA  1 
ATOM   3907 C  C   . THR   B 1 198 ? 42.703  7.223   19.744  1.00 17.37 ? 198 THR   B C   1 
ATOM   3908 O  O   . THR   B 1 198 ? 41.994  6.299   19.371  1.00 14.22 ? 198 THR   B O   1 
ATOM   3909 C  CB  . THR   B 1 198 ? 45.216  7.228   19.750  1.00 19.66 ? 198 THR   B CB  1 
ATOM   3910 O  OG1 . THR   B 1 198 ? 45.393  6.196   18.769  1.00 22.01 ? 198 THR   B OG1 1 
ATOM   3911 C  CG2 . THR   B 1 198 ? 46.455  7.300   20.625  1.00 22.87 ? 198 THR   B CG2 1 
ATOM   3912 N  N   . THR   B 1 199 ? 42.483  8.496   19.402  1.00 13.13 ? 199 THR   B N   1 
ATOM   3913 C  CA  . THR   B 1 199 ? 41.320  8.889   18.618  1.00 12.76 ? 199 THR   B CA  1 
ATOM   3914 C  C   . THR   B 1 199 ? 41.659  8.796   17.135  1.00 11.44 ? 199 THR   B C   1 
ATOM   3915 O  O   . THR   B 1 199 ? 42.749  9.137   16.726  1.00 15.61 ? 199 THR   B O   1 
ATOM   3916 C  CB  . THR   B 1 199 ? 40.865  10.303  18.989  1.00 13.10 ? 199 THR   B CB  1 
ATOM   3917 O  OG1 . THR   B 1 199 ? 40.515  10.263  20.370  1.00 14.00 ? 199 THR   B OG1 1 
ATOM   3918 C  CG2 . THR   B 1 199 ? 39.690  10.796  18.168  1.00 14.59 ? 199 THR   B CG2 1 
ATOM   3919 N  N   . ILE   B 1 200 ? 40.721  8.258   16.349  1.00 11.52 ? 200 ILE   B N   1 
ATOM   3920 C  CA  . ILE   B 1 200 ? 40.908  8.032   14.919  1.00 11.13 ? 200 ILE   B CA  1 
ATOM   3921 C  C   . ILE   B 1 200 ? 40.650  9.335   14.149  1.00 10.98 ? 200 ILE   B C   1 
ATOM   3922 O  O   . ILE   B 1 200 ? 39.505  9.656   13.769  1.00 10.40 ? 200 ILE   B O   1 
ATOM   3923 C  CB  . ILE   B 1 200 ? 39.988  6.924   14.409  1.00 11.77 ? 200 ILE   B CB  1 
ATOM   3924 C  CG1 . ILE   B 1 200 ? 40.120  5.631   15.230  1.00 13.05 ? 200 ILE   B CG1 1 
ATOM   3925 C  CG2 . ILE   B 1 200 ? 40.312  6.711   12.946  1.00 11.45 ? 200 ILE   B CG2 1 
ATOM   3926 C  CD1 . ILE   B 1 200 ? 39.002  4.648   15.023  1.00 12.91 ? 200 ILE   B CD1 1 
ATOM   3927 N  N   . THR   B 1 201 ? 41.734  10.067  13.924  1.00 10.57 ? 201 THR   B N   1 
ATOM   3928 C  CA  . THR   B 1 201 ? 41.672  11.400  13.330  1.00 10.95 ? 201 THR   B CA  1 
ATOM   3929 C  C   . THR   B 1 201 ? 40.947  11.444  11.990  1.00 9.72  ? 201 THR   B C   1 
ATOM   3930 O  O   . THR   B 1 201 ? 40.120  12.339  11.777  1.00 8.93  ? 201 THR   B O   1 
ATOM   3931 C  CB  . THR   B 1 201 ? 43.085  11.929  13.158  1.00 11.35 ? 201 THR   B CB  1 
ATOM   3932 O  OG1 . THR   B 1 201 ? 43.712  11.760  14.437  1.00 12.79 ? 201 THR   B OG1 1 
ATOM   3933 C  CG2 . THR   B 1 201 ? 43.064  13.357  12.701  1.00 13.32 ? 201 THR   B CG2 1 
ATOM   3934 N  N   . VAL   B 1 202 ? 41.245  10.497  11.088  1.00 8.73  ? 202 VAL   B N   1 
ATOM   3935 C  CA  . VAL   B 1 202 ? 40.627  10.533  9.763   1.00 9.50  ? 202 VAL   B CA  1 
ATOM   3936 C  C   . VAL   B 1 202 ? 39.103  10.448  9.847   1.00 9.60  ? 202 VAL   B C   1 
ATOM   3937 O  O   . VAL   B 1 202 ? 38.395  11.106  9.064   1.00 9.50  ? 202 VAL   B O   1 
ATOM   3938 C  CB  . VAL   B 1 202 ? 41.199  9.454   8.820   1.00 10.54 ? 202 VAL   B CB  1 
ATOM   3939 C  CG1 . VAL   B 1 202 ? 40.927  8.052   9.330   1.00 10.56 ? 202 VAL   B CG1 1 
ATOM   3940 C  CG2 . VAL   B 1 202 ? 40.709  9.649   7.382   1.00 12.39 ? 202 VAL   B CG2 1 
ATOM   3941 N  N   . ASN   B 1 203 ? 38.593  9.695   10.837  1.00 8.96  ? 203 ASN   B N   1 
ATOM   3942 C  CA  . ASN   B 1 203 ? 37.167  9.532   10.999  1.00 9.58  ? 203 ASN   B CA  1 
ATOM   3943 C  C   . ASN   B 1 203 ? 36.546  10.763  11.683  1.00 8.95  ? 203 ASN   B C   1 
ATOM   3944 O  O   . ASN   B 1 203 ? 35.446  11.157  11.305  1.00 9.74  ? 203 ASN   B O   1 
ATOM   3945 C  CB  . ASN   B 1 203 ? 36.799  8.272   11.769  1.00 8.57  ? 203 ASN   B CB  1 
ATOM   3946 C  CG  . ASN   B 1 203 ? 37.151  7.022   11.002  1.00 9.27  ? 203 ASN   B CG  1 
ATOM   3947 O  OD1 . ASN   B 1 203 ? 37.507  7.063   9.828   1.00 9.30  ? 203 ASN   B OD1 1 
ATOM   3948 N  ND2 . ASN   B 1 203 ? 37.031  5.893   11.648  1.00 8.66  ? 203 ASN   B ND2 1 
ATOM   3949 N  N   . VAL   B 1 204 ? 37.262  11.393  12.595  1.00 9.86  ? 204 VAL   B N   1 
ATOM   3950 C  CA  . VAL   B 1 204 ? 36.769  12.665  13.143  1.00 10.48 ? 204 VAL   B CA  1 
ATOM   3951 C  C   . VAL   B 1 204 ? 36.658  13.709  12.033  1.00 9.69  ? 204 VAL   B C   1 
ATOM   3952 O  O   . VAL   B 1 204 ? 35.642  14.429  11.929  1.00 10.20 ? 204 VAL   B O   1 
ATOM   3953 C  CB  . VAL   B 1 204 ? 37.632  13.204  14.298  1.00 11.67 ? 204 VAL   B CB  1 
ATOM   3954 C  CG1 . VAL   B 1 204 ? 37.224  14.635  14.673  1.00 11.58 ? 204 VAL   B CG1 1 
ATOM   3955 C  CG2 . VAL   B 1 204 ? 37.609  12.286  15.514  1.00 12.84 ? 204 VAL   B CG2 1 
ATOM   3956 N  N   . LEU   B 1 205 ? 37.653  13.765  11.136  1.00 9.42  ? 205 LEU   B N   1 
ATOM   3957 C  CA  . LEU   B 1 205 ? 37.573  14.697  10.016  1.00 9.76  ? 205 LEU   B CA  1 
ATOM   3958 C  C   . LEU   B 1 205 ? 36.361  14.370  9.131   1.00 9.66  ? 205 LEU   B C   1 
ATOM   3959 O  O   . LEU   B 1 205 ? 35.675  15.286  8.644   1.00 10.26 ? 205 LEU   B O   1 
ATOM   3960 C  CB  . LEU   B 1 205 ? 38.878  14.675  9.213   1.00 10.35 ? 205 LEU   B CB  1 
ATOM   3961 C  CG  . LEU   B 1 205 ? 40.075  15.236  9.959   1.00 11.15 ? 205 LEU   B CG  1 
ATOM   3962 C  CD1 . LEU   B 1 205 ? 41.342  14.888  9.233   1.00 11.22 ? 205 LEU   B CD1 1 
ATOM   3963 C  CD2 . LEU   B 1 205 ? 39.947  16.748  10.152  1.00 11.50 ? 205 LEU   B CD2 1 
ATOM   3964 N  N   . ALA   B 1 206 ? 36.074  13.080  8.891   1.00 9.64  ? 206 ALA   B N   1 
ATOM   3965 C  CA  . ALA   B 1 206 ? 34.922  12.710  8.081   1.00 9.38  ? 206 ALA   B CA  1 
ATOM   3966 C  C   . ALA   B 1 206 ? 33.649  13.230  8.730   1.00 9.71  ? 206 ALA   B C   1 
ATOM   3967 O  O   . ALA   B 1 206 ? 32.715  13.674  8.045   1.00 10.39 ? 206 ALA   B O   1 
ATOM   3968 C  CB  . ALA   B 1 206 ? 34.852  11.201  7.931   1.00 10.07 ? 206 ALA   B CB  1 
ATOM   3969 N  N   . TRP   B 1 207 ? 33.618  13.130  10.065  1.00 10.01 ? 207 TRP   B N   1 
ATOM   3970 C  CA  . TRP   B 1 207 ? 32.463  13.560  10.842  1.00 12.16 ? 207 TRP   B CA  1 
ATOM   3971 C  C   . TRP   B 1 207 ? 32.280  15.082  10.759  1.00 10.84 ? 207 TRP   B C   1 
ATOM   3972 O  O   . TRP   B 1 207 ? 31.142  15.568  10.656  1.00 12.64 ? 207 TRP   B O   1 
ATOM   3973 C  CB  . TRP   B 1 207 ? 32.659  13.109  12.302  1.00 11.99 ? 207 TRP   B CB  1 
ATOM   3974 C  CG  . TRP   B 1 207 ? 31.558  13.489  13.259  1.00 14.90 ? 207 TRP   B CG  1 
ATOM   3975 C  CD1 . TRP   B 1 207 ? 31.569  14.419  14.247  1.00 16.69 ? 207 TRP   B CD1 1 
ATOM   3976 C  CD2 . TRP   B 1 207 ? 30.271  12.870  13.300  1.00 17.80 ? 207 TRP   B CD2 1 
ATOM   3977 N  NE1 . TRP   B 1 207 ? 30.356  14.442  14.899  1.00 18.99 ? 207 TRP   B NE1 1 
ATOM   3978 C  CE2 . TRP   B 1 207 ? 29.549  13.497  14.338  1.00 20.57 ? 207 TRP   B CE2 1 
ATOM   3979 C  CE3 . TRP   B 1 207 ? 29.661  11.877  12.540  1.00 21.11 ? 207 TRP   B CE3 1 
ATOM   3980 C  CZ2 . TRP   B 1 207 ? 28.259  13.109  14.657  1.00 25.18 ? 207 TRP   B CZ2 1 
ATOM   3981 C  CZ3 . TRP   B 1 207 ? 28.363  11.520  12.844  1.00 25.71 ? 207 TRP   B CZ3 1 
ATOM   3982 C  CH2 . TRP   B 1 207 ? 27.690  12.117  13.902  1.00 23.50 ? 207 TRP   B CH2 1 
ATOM   3983 N  N   . LEU   B 1 208 ? 33.372  15.827  10.750  1.00 12.10 ? 208 LEU   B N   1 
ATOM   3984 C  CA  . LEU   B 1 208 ? 33.271  17.265  10.531  1.00 11.88 ? 208 LEU   B CA  1 
ATOM   3985 C  C   . LEU   B 1 208 ? 32.754  17.582  9.124   1.00 12.42 ? 208 LEU   B C   1 
ATOM   3986 O  O   . LEU   B 1 208 ? 32.004  18.553  8.932   1.00 12.37 ? 208 LEU   B O   1 
ATOM   3987 C  CB  . LEU   B 1 208 ? 34.608  17.960  10.773  1.00 12.01 ? 208 LEU   B CB  1 
ATOM   3988 C  CG  . LEU   B 1 208 ? 35.168  17.870  12.198  1.00 13.13 ? 208 LEU   B CG  1 
ATOM   3989 C  CD1 . LEU   B 1 208 ? 36.491  18.564  12.270  1.00 15.13 ? 208 LEU   B CD1 1 
ATOM   3990 C  CD2 . LEU   B 1 208 ? 34.207  18.476  13.208  1.00 13.20 ? 208 LEU   B CD2 1 
ATOM   3991 N  N   . TYR   B 1 209 ? 33.216  16.846  8.117   1.00 10.79 ? 209 TYR   B N   1 
ATOM   3992 C  CA  . TYR   B 1 209 ? 32.671  17.010  6.771   1.00 10.53 ? 209 TYR   B CA  1 
ATOM   3993 C  C   . TYR   B 1 209 ? 31.166  16.724  6.749   1.00 10.20 ? 209 TYR   B C   1 
ATOM   3994 O  O   . TYR   B 1 209 ? 30.408  17.430  6.072   1.00 10.74 ? 209 TYR   B O   1 
ATOM   3995 C  CB  . TYR   B 1 209 ? 33.402  16.162  5.731   1.00 10.22 ? 209 TYR   B CB  1 
ATOM   3996 C  CG  . TYR   B 1 209 ? 34.720  16.754  5.238   1.00 10.73 ? 209 TYR   B CG  1 
ATOM   3997 C  CD1 . TYR   B 1 209 ? 34.708  17.841  4.370   1.00 11.37 ? 209 TYR   B CD1 1 
ATOM   3998 C  CD2 . TYR   B 1 209 ? 35.946  16.224  5.618   1.00 10.18 ? 209 TYR   B CD2 1 
ATOM   3999 C  CE1 . TYR   B 1 209 ? 35.889  18.429  3.942   1.00 11.17 ? 209 TYR   B CE1 1 
ATOM   4000 C  CE2 . TYR   B 1 209 ? 37.131  16.724  5.104   1.00 10.52 ? 209 TYR   B CE2 1 
ATOM   4001 C  CZ  . TYR   B 1 209 ? 37.102  17.875  4.321   1.00 11.57 ? 209 TYR   B CZ  1 
ATOM   4002 O  OH  . TYR   B 1 209 ? 38.276  18.378  3.859   1.00 11.91 ? 209 TYR   B OH  1 
ATOM   4003 N  N   . ALA   B 1 210 ? 30.734  15.662  7.444   1.00 10.56 ? 210 ALA   B N   1 
ATOM   4004 C  CA  . ALA   B 1 210 ? 29.334  15.299  7.527   1.00 11.61 ? 210 ALA   B CA  1 
ATOM   4005 C  C   . ALA   B 1 210 ? 28.535  16.469  8.090   1.00 11.80 ? 210 ALA   B C   1 
ATOM   4006 O  O   . ALA   B 1 210 ? 27.439  16.757  7.595   1.00 11.26 ? 210 ALA   B O   1 
ATOM   4007 C  CB  . ALA   B 1 210 ? 29.091  14.051  8.333   1.00 10.72 ? 210 ALA   B CB  1 
ATOM   4008 N  N   . ALA   B 1 211 ? 29.090  17.106  9.107   1.00 12.48 ? 211 ALA   B N   1 
ATOM   4009 C  CA  . ALA   B 1 211 ? 28.421  18.221  9.747   1.00 13.48 ? 211 ALA   B CA  1 
ATOM   4010 C  C   . ALA   B 1 211 ? 28.306  19.389  8.766   1.00 11.93 ? 211 ALA   B C   1 
ATOM   4011 O  O   . ALA   B 1 211 ? 27.252  19.995  8.641   1.00 11.97 ? 211 ALA   B O   1 
ATOM   4012 C  CB  . ALA   B 1 211 ? 29.195  18.616  10.957  1.00 13.59 ? 211 ALA   B CB  1 
ATOM   4013 N  N   . VAL   B 1 212 ? 29.391  19.684  8.043   1.00 12.37 ? 212 VAL   B N   1 
ATOM   4014 C  CA  . VAL   B 1 212 ? 29.336  20.726  7.011   1.00 11.98 ? 212 VAL   B CA  1 
ATOM   4015 C  C   . VAL   B 1 212 ? 28.262  20.395  5.983   1.00 11.62 ? 212 VAL   B C   1 
ATOM   4016 O  O   . VAL   B 1 212 ? 27.503  21.293  5.568   1.00 11.85 ? 212 VAL   B O   1 
ATOM   4017 C  CB  . VAL   B 1 212 ? 30.715  20.959  6.368   1.00 12.48 ? 212 VAL   B CB  1 
ATOM   4018 C  CG1 . VAL   B 1 212 ? 30.653  21.876  5.154   1.00 12.01 ? 212 VAL   B CG1 1 
ATOM   4019 C  CG2 . VAL   B 1 212 ? 31.704  21.502  7.378   1.00 13.93 ? 212 VAL   B CG2 1 
ATOM   4020 N  N   . ILE   B 1 213 ? 28.189  19.138  5.515   1.00 11.42 ? 213 ILE   B N   1 
ATOM   4021 C  CA  . ILE   B 1 213 ? 27.221  18.782  4.481   1.00 11.70 ? 213 ILE   B CA  1 
ATOM   4022 C  C   . ILE   B 1 213 ? 25.808  19.123  4.969   1.00 13.92 ? 213 ILE   B C   1 
ATOM   4023 O  O   . ILE   B 1 213 ? 24.921  19.474  4.177   1.00 10.85 ? 213 ILE   B O   1 
ATOM   4024 C  CB  . ILE   B 1 213 ? 27.376  17.299  4.094   1.00 13.62 ? 213 ILE   B CB  1 
ATOM   4025 C  CG1 . ILE   B 1 213 ? 28.651  17.101  3.270   1.00 13.12 ? 213 ILE   B CG1 1 
ATOM   4026 C  CG2 . ILE   B 1 213 ? 26.174  16.729  3.348   1.00 14.79 ? 213 ILE   B CG2 1 
ATOM   4027 C  CD1 . ILE   B 1 213 ? 29.120  15.641  3.259   1.00 14.52 ? 213 ILE   B CD1 1 
ATOM   4028 N  N   . ASN   B 1 214 ? 25.596  18.894  6.272   1.00 13.53 ? 214 ASN   B N   1 
ATOM   4029 C  CA  . ASN   B 1 214 ? 24.294  19.117  6.907   1.00 17.54 ? 214 ASN   B CA  1 
ATOM   4030 C  C   . ASN   B 1 214 ? 24.081  20.548  7.396   1.00 18.19 ? 214 ASN   B C   1 
ATOM   4031 O  O   . ASN   B 1 214 ? 23.096  20.819  8.117   1.00 21.80 ? 214 ASN   B O   1 
ATOM   4032 C  CB  . ASN   B 1 214 ? 24.101  18.089  8.032   1.00 20.40 ? 214 ASN   B CB  1 
ATOM   4033 C  CG  . ASN   B 1 214 ? 23.772  16.751  7.419   1.00 25.35 ? 214 ASN   B CG  1 
ATOM   4034 O  OD1 . ASN   B 1 214 ? 22.664  16.575  6.913   1.00 31.73 ? 214 ASN   B OD1 1 
ATOM   4035 N  ND2 . ASN   B 1 214 ? 24.754  15.864  7.300   1.00 28.70 ? 214 ASN   B ND2 1 
ATOM   4036 N  N   . GLY   B 1 215 ? 24.991  21.445  7.059   1.00 16.27 ? 215 GLY   B N   1 
ATOM   4037 C  CA  . GLY   B 1 215 ? 24.859  22.863  7.332   1.00 18.09 ? 215 GLY   B CA  1 
ATOM   4038 C  C   . GLY   B 1 215 ? 25.339  23.316  8.709   1.00 19.14 ? 215 GLY   B C   1 
ATOM   4039 O  O   . GLY   B 1 215 ? 25.155  24.485  9.102   1.00 20.12 ? 215 GLY   B O   1 
ATOM   4040 N  N   . ASP   B 1 216 ? 26.053  22.452  9.430   1.00 17.82 ? 216 ASP   B N   1 
ATOM   4041 C  CA  . ASP   B 1 216 ? 26.549  22.839  10.739  1.00 20.03 ? 216 ASP   B CA  1 
ATOM   4042 C  C   . ASP   B 1 216 ? 28.038  23.142  10.597  1.00 20.41 ? 216 ASP   B C   1 
ATOM   4043 O  O   . ASP   B 1 216 ? 28.837  22.203  10.484  1.00 22.51 ? 216 ASP   B O   1 
ATOM   4044 C  CB  . ASP   B 1 216 ? 26.208  21.695  11.695  1.00 20.96 ? 216 ASP   B CB  1 
ATOM   4045 C  CG  . ASP   B 1 216 ? 26.244  22.024  13.181  1.00 26.76 ? 216 ASP   B CG  1 
ATOM   4046 O  OD1 . ASP   B 1 216 ? 26.531  23.173  13.523  1.00 25.54 ? 216 ASP   B OD1 1 
ATOM   4047 O  OD2 . ASP   B 1 216 ? 25.954  21.102  13.970  1.00 26.84 ? 216 ASP   B OD2 1 
ATOM   4048 N  N   . ARG   B 1 217 ? 28.436  24.419  10.523  1.00 19.41 ? 217 ARG   B N   1 
ATOM   4049 C  CA  . ARG   B 1 217 ? 29.770  24.725  10.042  1.00 18.80 ? 217 ARG   B CA  1 
ATOM   4050 C  C   . ARG   B 1 217 ? 30.464  25.865  10.797  1.00 19.15 ? 217 ARG   B C   1 
ATOM   4051 O  O   . ARG   B 1 217 ? 31.405  26.501  10.317  1.00 17.19 ? 217 ARG   B O   1 
ATOM   4052 C  CB  . ARG   B 1 217 ? 29.663  24.942  8.534   1.00 20.30 ? 217 ARG   B CB  1 
ATOM   4053 C  CG  . ARG   B 1 217 ? 28.705  26.047  8.137   1.00 20.07 ? 217 ARG   B CG  1 
ATOM   4054 C  CD  . ARG   B 1 217 ? 28.802  26.314  6.649   1.00 19.23 ? 217 ARG   B CD  1 
ATOM   4055 N  NE  . ARG   B 1 217 ? 27.941  27.444  6.353   1.00 17.71 ? 217 ARG   B NE  1 
ATOM   4056 C  CZ  . ARG   B 1 217 ? 26.666  27.352  6.003   1.00 18.48 ? 217 ARG   B CZ  1 
ATOM   4057 N  NH1 . ARG   B 1 217 ? 26.129  26.201  5.675   1.00 16.76 ? 217 ARG   B NH1 1 
ATOM   4058 N  NH2 . ARG   B 1 217 ? 25.926  28.452  5.944   1.00 21.42 ? 217 ARG   B NH2 1 
ATOM   4059 N  N   . TRP   B 1 218 ? 30.048  26.108  12.042  1.00 21.15 ? 218 TRP   B N   1 
ATOM   4060 C  CA  . TRP   B 1 218 ? 30.595  27.198  12.827  1.00 20.67 ? 218 TRP   B CA  1 
ATOM   4061 C  C   . TRP   B 1 218 ? 32.103  27.068  13.063  1.00 21.81 ? 218 TRP   B C   1 
ATOM   4062 O  O   . TRP   B 1 218 ? 32.819  28.061  13.202  1.00 24.22 ? 218 TRP   B O   1 
ATOM   4063 C  CB  . TRP   B 1 218 ? 29.807  27.268  14.139  1.00 21.23 ? 218 TRP   B CB  1 
ATOM   4064 C  CG  . TRP   B 1 218 ? 29.937  26.061  15.028  1.00 20.26 ? 218 TRP   B CG  1 
ATOM   4065 C  CD1 . TRP   B 1 218 ? 29.049  25.042  15.129  1.00 20.23 ? 218 TRP   B CD1 1 
ATOM   4066 C  CD2 . TRP   B 1 218 ? 31.006  25.758  15.952  1.00 21.05 ? 218 TRP   B CD2 1 
ATOM   4067 N  NE1 . TRP   B 1 218 ? 29.483  24.126  16.045  1.00 20.98 ? 218 TRP   B NE1 1 
ATOM   4068 C  CE2 . TRP   B 1 218 ? 30.678  24.539  16.567  1.00 20.66 ? 218 TRP   B CE2 1 
ATOM   4069 C  CE3 . TRP   B 1 218 ? 32.209  26.387  16.318  1.00 23.20 ? 218 TRP   B CE3 1 
ATOM   4070 C  CZ2 . TRP   B 1 218 ? 31.498  23.939  17.528  1.00 22.04 ? 218 TRP   B CZ2 1 
ATOM   4071 C  CZ3 . TRP   B 1 218 ? 33.028  25.780  17.254  1.00 24.49 ? 218 TRP   B CZ3 1 
ATOM   4072 C  CH2 . TRP   B 1 218 ? 32.675  24.569  17.840  1.00 22.22 ? 218 TRP   B CH2 1 
ATOM   4073 N  N   . PHE   B 1 219 ? 32.610  25.833  13.037  1.00 21.55 ? 219 PHE   B N   1 
ATOM   4074 C  CA  . PHE   B 1 219 ? 33.985  25.522  13.397  1.00 20.33 ? 219 PHE   B CA  1 
ATOM   4075 C  C   . PHE   B 1 219 ? 34.969  25.757  12.253  1.00 20.81 ? 219 PHE   B C   1 
ATOM   4076 O  O   . PHE   B 1 219 ? 36.168  25.684  12.493  1.00 22.58 ? 219 PHE   B O   1 
ATOM   4077 C  CB  . PHE   B 1 219 ? 34.019  24.086  13.929  1.00 19.67 ? 219 PHE   B CB  1 
ATOM   4078 C  CG  . PHE   B 1 219 ? 33.366  23.098  12.994  1.00 16.79 ? 219 PHE   B CG  1 
ATOM   4079 C  CD1 . PHE   B 1 219 ? 34.084  22.596  11.914  1.00 16.67 ? 219 PHE   B CD1 1 
ATOM   4080 C  CD2 . PHE   B 1 219 ? 32.057  22.672  13.171  1.00 15.58 ? 219 PHE   B CD2 1 
ATOM   4081 C  CE1 . PHE   B 1 219 ? 33.471  21.727  11.022  1.00 15.84 ? 219 PHE   B CE1 1 
ATOM   4082 C  CE2 . PHE   B 1 219 ? 31.452  21.829  12.264  1.00 16.26 ? 219 PHE   B CE2 1 
ATOM   4083 C  CZ  . PHE   B 1 219 ? 32.172  21.342  11.196  1.00 14.65 ? 219 PHE   B CZ  1 
ATOM   4084 N  N   . LEU   B 1 220 ? 34.490  26.069  11.038  1.00 19.85 ? 220 LEU   B N   1 
ATOM   4085 C  CA  . LEU   B 1 220 ? 35.377  26.384  9.935   1.00 20.25 ? 220 LEU   B CA  1 
ATOM   4086 C  C   . LEU   B 1 220 ? 36.042  27.725  10.229  1.00 26.57 ? 220 LEU   B C   1 
ATOM   4087 O  O   . LEU   B 1 220 ? 35.329  28.650  10.615  1.00 23.74 ? 220 LEU   B O   1 
ATOM   4088 C  CB  . LEU   B 1 220 ? 34.603  26.404  8.613   1.00 20.35 ? 220 LEU   B CB  1 
ATOM   4089 C  CG  . LEU   B 1 220 ? 33.930  25.084  8.207   1.00 19.40 ? 220 LEU   B CG  1 
ATOM   4090 C  CD1 . LEU   B 1 220 ? 33.071  25.244  6.974   1.00 18.75 ? 220 LEU   B CD1 1 
ATOM   4091 C  CD2 . LEU   B 1 220 ? 34.942  23.968  7.983   1.00 20.56 ? 220 LEU   B CD2 1 
ATOM   4092 N  N   . ASN   B 1 221 ? 37.375  27.819  10.032  1.00 32.23 ? 221 ASN   B N   1 
ATOM   4093 C  CA  . ASN   B 1 221 ? 38.146  29.041  10.286  1.00 33.01 ? 221 ASN   B CA  1 
ATOM   4094 C  C   . ASN   B 1 221 ? 38.825  29.486  9.001   1.00 34.87 ? 221 ASN   B C   1 
ATOM   4095 O  O   . ASN   B 1 221 ? 38.633  28.854  7.973   1.00 31.78 ? 221 ASN   B O   1 
ATOM   4096 C  CB  . ASN   B 1 221 ? 39.125  28.834  11.447  1.00 39.96 ? 221 ASN   B CB  1 
ATOM   4097 C  CG  . ASN   B 1 221 ? 40.211  27.800  11.193  1.00 40.46 ? 221 ASN   B CG  1 
ATOM   4098 O  OD1 . ASN   B 1 221 ? 40.615  27.532  10.056  1.00 37.83 ? 221 ASN   B OD1 1 
ATOM   4099 N  ND2 . ASN   B 1 221 ? 40.731  27.246  12.272  1.00 36.84 ? 221 ASN   B ND2 1 
ATOM   4100 N  N   . ARG   B 1 222 ? 39.643  30.564  9.056   1.00 41.46 ? 222 ARG   B N   1 
ATOM   4101 C  CA  . ARG   B 1 222 ? 40.304  31.079  7.861   1.00 46.67 ? 222 ARG   B CA  1 
ATOM   4102 C  C   . ARG   B 1 222 ? 41.783  30.687  7.883   1.00 39.08 ? 222 ARG   B C   1 
ATOM   4103 O  O   . ARG   B 1 222 ? 42.578  31.280  7.169   1.00 43.67 ? 222 ARG   B O   1 
ATOM   4104 C  CB  . ARG   B 1 222 ? 40.155  32.604  7.704   1.00 54.52 ? 222 ARG   B CB  1 
ATOM   4105 C  CG  . ARG   B 1 222 ? 41.313  33.418  8.269   1.00 58.39 ? 222 ARG   B CG  1 
ATOM   4106 C  CD  . ARG   B 1 222 ? 41.077  34.911  8.276   1.00 68.31 ? 222 ARG   B CD  1 
ATOM   4107 N  NE  . ARG   B 1 222 ? 40.118  35.323  9.298   1.00 66.22 ? 222 ARG   B NE  1 
ATOM   4108 C  CZ  . ARG   B 1 222 ? 39.170  36.236  9.130   1.00 65.88 ? 222 ARG   B CZ  1 
ATOM   4109 N  NH1 . ARG   B 1 222 ? 39.022  36.845  7.964   1.00 65.96 ? 222 ARG   B NH1 1 
ATOM   4110 N  NH2 . ARG   B 1 222 ? 38.367  36.541  10.135  1.00 70.98 ? 222 ARG   B NH2 1 
ATOM   4111 N  N   . PHE   B 1 223 ? 42.124  29.642  8.650   1.00 36.19 ? 223 PHE   B N   1 
ATOM   4112 C  CA  . PHE   B 1 223 ? 43.488  29.149  8.723   1.00 32.56 ? 223 PHE   B CA  1 
ATOM   4113 C  C   . PHE   B 1 223 ? 43.657  27.814  8.002   1.00 25.51 ? 223 PHE   B C   1 
ATOM   4114 O  O   . PHE   B 1 223 ? 42.686  27.140  7.647   1.00 20.83 ? 223 PHE   B O   1 
ATOM   4115 C  CB  . PHE   B 1 223 ? 43.897  28.917  10.173  1.00 39.97 ? 223 PHE   B CB  1 
ATOM   4116 C  CG  . PHE   B 1 223 ? 43.865  30.150  11.035  1.00 53.33 ? 223 PHE   B CG  1 
ATOM   4117 C  CD1 . PHE   B 1 223 ? 44.483  31.327  10.617  1.00 61.13 ? 223 PHE   B CD1 1 
ATOM   4118 C  CD2 . PHE   B 1 223 ? 43.251  30.118  12.282  1.00 59.14 ? 223 PHE   B CD2 1 
ATOM   4119 C  CE1 . PHE   B 1 223 ? 44.468  32.454  11.426  1.00 64.78 ? 223 PHE   B CE1 1 
ATOM   4120 C  CE2 . PHE   B 1 223 ? 43.236  31.248  13.085  1.00 63.18 ? 223 PHE   B CE2 1 
ATOM   4121 C  CZ  . PHE   B 1 223 ? 43.849  32.409  12.658  1.00 60.83 ? 223 PHE   B CZ  1 
ATOM   4122 N  N   . THR   B 1 224 ? 44.927  27.491  7.770   1.00 19.62 ? 224 THR   B N   1 
ATOM   4123 C  CA  . THR   B 1 224 ? 45.342  26.198  7.240   1.00 19.19 ? 224 THR   B CA  1 
ATOM   4124 C  C   . THR   B 1 224 ? 46.568  25.707  8.020   1.00 18.86 ? 224 THR   B C   1 
ATOM   4125 O  O   . THR   B 1 224 ? 47.065  26.389  8.904   1.00 18.78 ? 224 THR   B O   1 
ATOM   4126 C  CB  . THR   B 1 224 ? 45.633  26.292  5.752   1.00 19.77 ? 224 THR   B CB  1 
ATOM   4127 O  OG1 . THR   B 1 224 ? 45.581  24.960  5.220   1.00 20.66 ? 224 THR   B OG1 1 
ATOM   4128 C  CG2 . THR   B 1 224 ? 46.955  26.981  5.451   1.00 20.22 ? 224 THR   B CG2 1 
ATOM   4129 N  N   . THR   B 1 225 ? 47.042  24.513  7.681   1.00 17.90 ? 225 THR   B N   1 
ATOM   4130 C  CA  . THR   B 1 225 ? 48.175  23.902  8.379   1.00 19.68 ? 225 THR   B CA  1 
ATOM   4131 C  C   . THR   B 1 225 ? 48.878  23.025  7.357   1.00 19.01 ? 225 THR   B C   1 
ATOM   4132 O  O   . THR   B 1 225 ? 48.303  22.759  6.310   1.00 21.70 ? 225 THR   B O   1 
ATOM   4133 C  CB  . THR   B 1 225 ? 47.720  23.111  9.612   1.00 20.86 ? 225 THR   B CB  1 
ATOM   4134 O  OG1 . THR   B 1 225 ? 48.867  22.580  10.268  1.00 20.88 ? 225 THR   B OG1 1 
ATOM   4135 C  CG2 . THR   B 1 225 ? 46.826  21.949  9.272   1.00 22.36 ? 225 THR   B CG2 1 
ATOM   4136 N  N   . THR   B 1 226 ? 50.125  22.596  7.612   1.00 18.11 ? 226 THR   B N   1 
ATOM   4137 C  CA  . THR   B 1 226 ? 50.700  21.480  6.882   1.00 17.63 ? 226 THR   B CA  1 
ATOM   4138 C  C   . THR   B 1 226 ? 50.246  20.184  7.547   1.00 15.89 ? 226 THR   B C   1 
ATOM   4139 O  O   . THR   B 1 226 ? 49.916  20.167  8.740   1.00 15.12 ? 226 THR   B O   1 
ATOM   4140 C  CB  . THR   B 1 226 ? 52.238  21.593  6.859   1.00 18.76 ? 226 THR   B CB  1 
ATOM   4141 O  OG1 . THR   B 1 226 ? 52.749  21.501  8.192   1.00 17.35 ? 226 THR   B OG1 1 
ATOM   4142 C  CG2 . THR   B 1 226 ? 52.713  22.917  6.293   1.00 22.50 ? 226 THR   B CG2 1 
ATOM   4143 N  N   . LEU   B 1 227 ? 50.354  19.070  6.814   1.00 15.98 ? 227 LEU   B N   1 
ATOM   4144 C  CA  . LEU   B 1 227 ? 50.045  17.786  7.413   1.00 15.21 ? 227 LEU   B CA  1 
ATOM   4145 C  C   . LEU   B 1 227 ? 51.029  17.457  8.538   1.00 14.15 ? 227 LEU   B C   1 
ATOM   4146 O  O   . LEU   B 1 227 ? 50.643  16.942  9.574   1.00 13.23 ? 227 LEU   B O   1 
ATOM   4147 C  CB  . LEU   B 1 227 ? 50.104  16.740  6.307   1.00 16.88 ? 227 LEU   B CB  1 
ATOM   4148 C  CG  . LEU   B 1 227 ? 49.617  15.341  6.677   1.00 18.75 ? 227 LEU   B CG  1 
ATOM   4149 C  CD1 . LEU   B 1 227 ? 48.146  15.364  6.989   1.00 19.79 ? 227 LEU   B CD1 1 
ATOM   4150 C  CD2 . LEU   B 1 227 ? 49.890  14.382  5.520   1.00 22.24 ? 227 LEU   B CD2 1 
ATOM   4151 N  N   . ASN   B 1 228 ? 52.303  17.760  8.334   1.00 14.84 ? 228 ASN   B N   1 
ATOM   4152 C  CA  . ASN   B 1 228 ? 53.316  17.432  9.336   1.00 15.24 ? 228 ASN   B CA  1 
ATOM   4153 C  C   . ASN   B 1 228 ? 53.028  18.186  10.613  1.00 14.61 ? 228 ASN   B C   1 
ATOM   4154 O  O   . ASN   B 1 228 ? 53.015  17.648  11.713  1.00 13.96 ? 228 ASN   B O   1 
ATOM   4155 C  CB  . ASN   B 1 228 ? 54.721  17.746  8.795   1.00 15.06 ? 228 ASN   B CB  1 
ATOM   4156 C  CG  . ASN   B 1 228 ? 55.838  17.480  9.775   1.00 16.65 ? 228 ASN   B CG  1 
ATOM   4157 O  OD1 . ASN   B 1 228 ? 56.584  18.397  10.138  1.00 18.52 ? 228 ASN   B OD1 1 
ATOM   4158 N  ND2 . ASN   B 1 228 ? 55.923  16.248  10.261  1.00 16.40 ? 228 ASN   B ND2 1 
ATOM   4159 N  N   . ASP   B 1 229 ? 52.750  19.496  10.509  1.00 16.35 ? 229 ASP   B N   1 
ATOM   4160 C  CA  . ASP   B 1 229 ? 52.513  20.250  11.715  1.00 16.83 ? 229 ASP   B CA  1 
ATOM   4161 C  C   . ASP   B 1 229 ? 51.255  19.771  12.446  1.00 15.87 ? 229 ASP   B C   1 
ATOM   4162 O  O   . ASP   B 1 229 ? 51.215  19.690  13.675  1.00 16.39 ? 229 ASP   B O   1 
ATOM   4163 C  CB  . ASP   B 1 229 ? 52.355  21.750  11.438  1.00 21.06 ? 229 ASP   B CB  1 
ATOM   4164 C  CG  . ASP   B 1 229 ? 52.640  22.513  12.722  1.00 29.67 ? 229 ASP   B CG  1 
ATOM   4165 O  OD1 . ASP   B 1 229 ? 53.828  22.634  13.045  1.00 39.20 ? 229 ASP   B OD1 1 
ATOM   4166 O  OD2 . ASP   B 1 229 ? 51.690  22.847  13.464  1.00 37.19 ? 229 ASP   B OD2 1 
ATOM   4167 N  N   . PHE   B 1 230 ? 50.208  19.468  11.672  1.00 14.62 ? 230 PHE   B N   1 
ATOM   4168 C  CA  . PHE   B 1 230 ? 48.990  18.918  12.238  1.00 13.48 ? 230 PHE   B CA  1 
ATOM   4169 C  C   . PHE   B 1 230 ? 49.293  17.612  13.002  1.00 12.32 ? 230 PHE   B C   1 
ATOM   4170 O  O   . PHE   B 1 230 ? 48.847  17.408  14.127  1.00 13.17 ? 230 PHE   B O   1 
ATOM   4171 C  CB  . PHE   B 1 230 ? 47.952  18.697  11.130  1.00 15.14 ? 230 PHE   B CB  1 
ATOM   4172 C  CG  . PHE   B 1 230 ? 46.722  18.030  11.659  1.00 15.80 ? 230 PHE   B CG  1 
ATOM   4173 C  CD1 . PHE   B 1 230 ? 45.844  18.724  12.476  1.00 17.52 ? 230 PHE   B CD1 1 
ATOM   4174 C  CD2 . PHE   B 1 230 ? 46.563  16.659  11.508  1.00 19.19 ? 230 PHE   B CD2 1 
ATOM   4175 C  CE1 . PHE   B 1 230 ? 44.775  18.082  13.083  1.00 17.88 ? 230 PHE   B CE1 1 
ATOM   4176 C  CE2 . PHE   B 1 230 ? 45.483  16.018  12.096  1.00 20.14 ? 230 PHE   B CE2 1 
ATOM   4177 C  CZ  . PHE   B 1 230 ? 44.586  16.733  12.867  1.00 20.93 ? 230 PHE   B CZ  1 
ATOM   4178 N  N   . ASN   B 1 231 ? 50.032  16.711  12.372  1.00 12.04 ? 231 ASN   B N   1 
ATOM   4179 C  CA  . ASN   B 1 231 ? 50.316  15.419  12.959  1.00 12.94 ? 231 ASN   B CA  1 
ATOM   4180 C  C   . ASN   B 1 231 ? 51.058  15.580  14.278  1.00 14.65 ? 231 ASN   B C   1 
ATOM   4181 O  O   . ASN   B 1 231 ? 50.724  14.898  15.246  1.00 15.51 ? 231 ASN   B O   1 
ATOM   4182 C  CB  . ASN   B 1 231 ? 51.126  14.554  12.001  1.00 13.67 ? 231 ASN   B CB  1 
ATOM   4183 C  CG  . ASN   B 1 231 ? 50.266  13.843  11.000  1.00 14.62 ? 231 ASN   B CG  1 
ATOM   4184 O  OD1 . ASN   B 1 231 ? 49.040  13.949  11.057  1.00 14.67 ? 231 ASN   B OD1 1 
ATOM   4185 N  ND2 . ASN   B 1 231 ? 50.912  13.157  10.075  1.00 15.38 ? 231 ASN   B ND2 1 
ATOM   4186 N  N   . LEU   B 1 232 ? 51.989  16.545  14.325  1.00 14.48 ? 232 LEU   B N   1 
ATOM   4187 C  CA  . LEU   B 1 232 ? 52.766  16.756  15.531  1.00 17.25 ? 232 LEU   B CA  1 
ATOM   4188 C  C   . LEU   B 1 232 ? 51.875  17.274  16.664  1.00 18.14 ? 232 LEU   B C   1 
ATOM   4189 O  O   . LEU   B 1 232 ? 52.042  16.874  17.830  1.00 18.94 ? 232 LEU   B O   1 
ATOM   4190 C  CB  . LEU   B 1 232 ? 53.925  17.720  15.220  1.00 17.74 ? 232 LEU   B CB  1 
ATOM   4191 C  CG  . LEU   B 1 232 ? 55.047  17.160  14.348  1.00 19.79 ? 232 LEU   B CG  1 
ATOM   4192 C  CD1 . LEU   B 1 232 ? 56.100  18.227  14.059  1.00 20.16 ? 232 LEU   B CD1 1 
ATOM   4193 C  CD2 . LEU   B 1 232 ? 55.674  15.904  14.960  1.00 23.20 ? 232 LEU   B CD2 1 
ATOM   4194 N  N   . VAL   B 1 233 ? 50.927  18.162  16.341  1.00 17.65 ? 233 VAL   B N   1 
ATOM   4195 C  CA  . VAL   B 1 233 ? 50.003  18.690  17.338  1.00 18.95 ? 233 VAL   B CA  1 
ATOM   4196 C  C   . VAL   B 1 233 ? 49.010  17.606  17.775  1.00 19.45 ? 233 VAL   B C   1 
ATOM   4197 O  O   . VAL   B 1 233 ? 48.697  17.476  18.961  1.00 19.09 ? 233 VAL   B O   1 
ATOM   4198 C  CB  . VAL   B 1 233 ? 49.257  19.937  16.803  1.00 22.16 ? 233 VAL   B CB  1 
ATOM   4199 C  CG1 . VAL   B 1 233 ? 48.174  20.397  17.769  1.00 24.06 ? 233 VAL   B CG1 1 
ATOM   4200 C  CG2 . VAL   B 1 233 ? 50.207  21.085  16.509  1.00 24.88 ? 233 VAL   B CG2 1 
ATOM   4201 N  N   . ALA   B 1 234 ? 48.470  16.848  16.804  1.00 18.05 ? 234 ALA   B N   1 
ATOM   4202 C  CA  . ALA   B 1 234 ? 47.426  15.860  17.091  1.00 20.42 ? 234 ALA   B CA  1 
ATOM   4203 C  C   . ALA   B 1 234 ? 47.902  14.856  18.141  1.00 16.90 ? 234 ALA   B C   1 
ATOM   4204 O  O   . ALA   B 1 234 ? 47.167  14.501  19.068  1.00 18.10 ? 234 ALA   B O   1 
ATOM   4205 C  CB  . ALA   B 1 234 ? 47.007  15.154  15.829  1.00 23.05 ? 234 ALA   B CB  1 
ATOM   4206 N  N   . MET   B 1 235 ? 49.171  14.488  18.041  1.00 19.06 ? 235 MET   B N   1 
ATOM   4207 C  CA  . MET   B 1 235 ? 49.744  13.458  18.881  1.00 22.34 ? 235 MET   B CA  1 
ATOM   4208 C  C   . MET   B 1 235 ? 49.701  13.933  20.329  1.00 24.25 ? 235 MET   B C   1 
ATOM   4209 O  O   . MET   B 1 235 ? 49.476  13.141  21.233  1.00 20.56 ? 235 MET   B O   1 
ATOM   4210 C  CB  . MET   B 1 235 ? 51.195  13.171  18.497  1.00 31.27 ? 235 MET   B CB  1 
ATOM   4211 C  CG  . MET   B 1 235 ? 51.341  12.148  17.369  1.00 45.01 ? 235 MET   B CG  1 
ATOM   4212 S  SD  . MET   B 1 235 ? 53.058  11.622  17.080  1.00 62.23 ? 235 MET   B SD  1 
ATOM   4213 C  CE  . MET   B 1 235 ? 53.957  12.645  18.251  1.00 52.09 ? 235 MET   B CE  1 
ATOM   4214 N  N   . LYS   B 1 236 ? 49.790  15.257  20.544  1.00 22.18 ? 236 LYS   B N   1 
ATOM   4215 C  CA  . LYS   B 1 236 ? 49.736  15.792  21.901  1.00 25.53 ? 236 LYS   B CA  1 
ATOM   4216 C  C   . LYS   B 1 236 ? 48.341  15.730  22.524  1.00 22.09 ? 236 LYS   B C   1 
ATOM   4217 O  O   . LYS   B 1 236 ? 48.216  15.915  23.743  1.00 22.44 ? 236 LYS   B O   1 
ATOM   4218 C  CB  . LYS   B 1 236 ? 50.287  17.231  21.873  1.00 29.50 ? 236 LYS   B CB  1 
ATOM   4219 C  CG  . LYS   B 1 236 ? 51.759  17.317  21.498  1.00 36.13 ? 236 LYS   B CG  1 
ATOM   4220 C  CD  . LYS   B 1 236 ? 52.252  18.725  21.258  1.00 48.95 ? 236 LYS   B CD  1 
ATOM   4221 C  CE  . LYS   B 1 236 ? 53.753  18.797  21.056  1.00 57.90 ? 236 LYS   B CE  1 
ATOM   4222 N  NZ  . LYS   B 1 236 ? 54.476  18.045  22.113  1.00 65.99 ? 236 LYS   B NZ  1 
ATOM   4223 N  N   . TYR   B 1 237 ? 47.277  15.509  21.721  1.00 16.44 ? 237 TYR   B N   1 
ATOM   4224 C  CA  . TYR   B 1 237 ? 45.923  15.336  22.215  1.00 18.11 ? 237 TYR   B CA  1 
ATOM   4225 C  C   . TYR   B 1 237 ? 45.447  13.879  22.070  1.00 16.14 ? 237 TYR   B C   1 
ATOM   4226 O  O   . TYR   B 1 237 ? 44.249  13.626  22.074  1.00 18.64 ? 237 TYR   B O   1 
ATOM   4227 C  CB  . TYR   B 1 237 ? 44.982  16.288  21.465  1.00 19.17 ? 237 TYR   B CB  1 
ATOM   4228 C  CG  . TYR   B 1 237 ? 45.317  17.750  21.759  1.00 22.72 ? 237 TYR   B CG  1 
ATOM   4229 C  CD1 . TYR   B 1 237 ? 44.730  18.402  22.844  1.00 23.26 ? 237 TYR   B CD1 1 
ATOM   4230 C  CD2 . TYR   B 1 237 ? 46.299  18.437  21.049  1.00 24.70 ? 237 TYR   B CD2 1 
ATOM   4231 C  CE1 . TYR   B 1 237 ? 45.102  19.689  23.185  1.00 23.81 ? 237 TYR   B CE1 1 
ATOM   4232 C  CE2 . TYR   B 1 237 ? 46.644  19.749  21.357  1.00 25.38 ? 237 TYR   B CE2 1 
ATOM   4233 C  CZ  . TYR   B 1 237 ? 46.054  20.368  22.449  1.00 25.65 ? 237 TYR   B CZ  1 
ATOM   4234 O  OH  . TYR   B 1 237 ? 46.352  21.650  22.793  1.00 27.96 ? 237 TYR   B OH  1 
ATOM   4235 N  N   . ASN   B 1 238 ? 46.374  12.947  21.904  1.00 17.05 ? 238 ASN   B N   1 
ATOM   4236 C  CA  . ASN   B 1 238 ? 46.053  11.524  21.853  1.00 17.64 ? 238 ASN   B CA  1 
ATOM   4237 C  C   . ASN   B 1 238 ? 45.257  11.215  20.577  1.00 16.02 ? 238 ASN   B C   1 
ATOM   4238 O  O   . ASN   B 1 238 ? 44.463  10.269  20.573  1.00 15.44 ? 238 ASN   B O   1 
ATOM   4239 C  CB  . ASN   B 1 238 ? 45.262  11.080  23.086  1.00 21.42 ? 238 ASN   B CB  1 
ATOM   4240 C  CG  . ASN   B 1 238 ? 45.429  9.613   23.407  1.00 29.34 ? 238 ASN   B CG  1 
ATOM   4241 O  OD1 . ASN   B 1 238 ? 44.456  8.886   23.613  1.00 36.56 ? 238 ASN   B OD1 1 
ATOM   4242 N  ND2 . ASN   B 1 238 ? 46.674  9.170   23.483  1.00 34.19 ? 238 ASN   B ND2 1 
ATOM   4243 N  N   . TYR   B 1 239 ? 45.503  11.986  19.507  1.00 14.74 ? 239 TYR   B N   1 
ATOM   4244 C  CA  . TYR   B 1 239 ? 44.918  11.729  18.185  1.00 14.51 ? 239 TYR   B CA  1 
ATOM   4245 C  C   . TYR   B 1 239 ? 45.953  11.035  17.313  1.00 14.36 ? 239 TYR   B C   1 
ATOM   4246 O  O   . TYR   B 1 239 ? 47.153  11.316  17.408  1.00 15.30 ? 239 TYR   B O   1 
ATOM   4247 C  CB  . TYR   B 1 239 ? 44.442  13.025  17.504  1.00 13.86 ? 239 TYR   B CB  1 
ATOM   4248 C  CG  . TYR   B 1 239 ? 43.030  13.446  17.825  1.00 16.28 ? 239 TYR   B CG  1 
ATOM   4249 C  CD1 . TYR   B 1 239 ? 42.594  13.681  19.128  1.00 15.80 ? 239 TYR   B CD1 1 
ATOM   4250 C  CD2 . TYR   B 1 239 ? 42.108  13.606  16.792  1.00 15.94 ? 239 TYR   B CD2 1 
ATOM   4251 C  CE1 . TYR   B 1 239 ? 41.277  14.030  19.396  1.00 17.04 ? 239 TYR   B CE1 1 
ATOM   4252 C  CE2 . TYR   B 1 239 ? 40.816  13.995  17.047  1.00 16.52 ? 239 TYR   B CE2 1 
ATOM   4253 C  CZ  . TYR   B 1 239 ? 40.401  14.211  18.339  1.00 16.92 ? 239 TYR   B CZ  1 
ATOM   4254 O  OH  . TYR   B 1 239 ? 39.097  14.571  18.487  1.00 23.74 ? 239 TYR   B OH  1 
ATOM   4255 N  N   . GLU   B 1 240 ? 45.476  10.128  16.456  1.00 13.29 ? 240 GLU   B N   1 
ATOM   4256 C  CA  . GLU   B 1 240 ? 46.332  9.405   15.531  1.00 14.89 ? 240 GLU   B CA  1 
ATOM   4257 C  C   . GLU   B 1 240 ? 46.882  10.374  14.489  1.00 14.58 ? 240 GLU   B C   1 
ATOM   4258 O  O   . GLU   B 1 240 ? 46.185  11.299  14.068  1.00 14.59 ? 240 GLU   B O   1 
ATOM   4259 C  CB  . GLU   B 1 240 ? 45.555  8.289   14.824  1.00 18.45 ? 240 GLU   B CB  1 
ATOM   4260 C  CG  . GLU   B 1 240 ? 45.474  7.024   15.630  1.00 22.07 ? 240 GLU   B CG  1 
ATOM   4261 C  CD  . GLU   B 1 240 ? 46.833  6.380   15.868  1.00 28.29 ? 240 GLU   B CD  1 
ATOM   4262 O  OE1 . GLU   B 1 240 ? 47.237  6.238   17.050  1.00 31.41 ? 240 GLU   B OE1 1 
ATOM   4263 O  OE2 . GLU   B 1 240 ? 47.503  6.043   14.858  1.00 36.42 ? 240 GLU   B OE2 1 
ATOM   4264 N  N   . PRO   B 1 241 ? 48.121  10.197  14.008  1.00 15.58 ? 241 PRO   B N   1 
ATOM   4265 C  CA  . PRO   B 1 241 ? 48.590  10.951  12.844  1.00 14.88 ? 241 PRO   B CA  1 
ATOM   4266 C  C   . PRO   B 1 241 ? 47.846  10.505  11.591  1.00 14.23 ? 241 PRO   B C   1 
ATOM   4267 O  O   . PRO   B 1 241 ? 47.459  9.339   11.459  1.00 15.70 ? 241 PRO   B O   1 
ATOM   4268 C  CB  . PRO   B 1 241 ? 50.090  10.601  12.777  1.00 17.35 ? 241 PRO   B CB  1 
ATOM   4269 C  CG  . PRO   B 1 241 ? 50.181  9.248   13.437  1.00 18.96 ? 241 PRO   B CG  1 
ATOM   4270 C  CD  . PRO   B 1 241 ? 49.135  9.259   14.532  1.00 16.91 ? 241 PRO   B CD  1 
ATOM   4271 N  N   . LEU   B 1 242 ? 47.707  11.416  10.637  1.00 13.51 ? 242 LEU   B N   1 
ATOM   4272 C  CA  . LEU   B 1 242 ? 47.166  11.108  9.328   1.00 13.84 ? 242 LEU   B CA  1 
ATOM   4273 C  C   . LEU   B 1 242 ? 48.263  10.573  8.417   1.00 13.60 ? 242 LEU   B C   1 
ATOM   4274 O  O   . LEU   B 1 242 ? 49.395  11.056  8.458   1.00 16.22 ? 242 LEU   B O   1 
ATOM   4275 C  CB  . LEU   B 1 242 ? 46.621  12.388  8.726   1.00 14.32 ? 242 LEU   B CB  1 
ATOM   4276 C  CG  . LEU   B 1 242 ? 45.390  12.969  9.400   1.00 15.77 ? 242 LEU   B CG  1 
ATOM   4277 C  CD1 . LEU   B 1 242 ? 45.109  14.372  8.835   1.00 18.42 ? 242 LEU   B CD1 1 
ATOM   4278 C  CD2 . LEU   B 1 242 ? 44.189  12.045  9.203   1.00 16.78 ? 242 LEU   B CD2 1 
ATOM   4279 N  N   . THR   B 1 243 ? 47.887  9.583   7.619   1.00 12.44 ? 243 THR   B N   1 
ATOM   4280 C  CA  . THR   B 1 243 ? 48.681  9.040   6.538   1.00 12.42 ? 243 THR   B CA  1 
ATOM   4281 C  C   . THR   B 1 243 ? 48.312  9.685   5.186   1.00 12.87 ? 243 THR   B C   1 
ATOM   4282 O  O   . THR   B 1 243 ? 47.268  10.328  4.975   1.00 11.95 ? 243 THR   B O   1 
ATOM   4283 C  CB  . THR   B 1 243 ? 48.484  7.520   6.470   1.00 14.00 ? 243 THR   B CB  1 
ATOM   4284 O  OG1 . THR   B 1 243 ? 47.148  7.281   5.979   1.00 13.93 ? 243 THR   B OG1 1 
ATOM   4285 C  CG2 . THR   B 1 243 ? 48.723  6.813   7.780   1.00 15.50 ? 243 THR   B CG2 1 
ATOM   4286 N  N   . GLN   B 1 244 ? 49.146  9.420   4.176   1.00 14.38 ? 244 GLN   B N   1 
ATOM   4287 C  CA  . GLN   B 1 244 ? 48.817  9.874   2.841   1.00 15.42 ? 244 GLN   B CA  1 
ATOM   4288 C  C   . GLN   B 1 244 ? 47.532  9.204   2.347   1.00 12.77 ? 244 GLN   B C   1 
ATOM   4289 O  O   . GLN   B 1 244 ? 46.739  9.843   1.652   1.00 14.40 ? 244 GLN   B O   1 
ATOM   4290 C  CB  . GLN   B 1 244 ? 49.950  9.587   1.853   1.00 17.09 ? 244 GLN   B CB  1 
ATOM   4291 C  CG  . GLN   B 1 244 ? 49.849  10.377  0.553   1.00 18.37 ? 244 GLN   B CG  1 
ATOM   4292 C  CD  . GLN   B 1 244 ? 50.232  11.837  0.668   1.00 21.14 ? 244 GLN   B CD  1 
ATOM   4293 O  OE1 . GLN   B 1 244 ? 50.360  12.421  1.747   1.00 22.20 ? 244 GLN   B OE1 1 
ATOM   4294 N  NE2 . GLN   B 1 244 ? 50.463  12.457  -0.477  1.00 25.12 ? 244 GLN   B NE2 1 
ATOM   4295 N  N   . ASP   B 1 245 ? 47.320  7.929   2.678   1.00 11.58 ? 245 ASP   B N   1 
ATOM   4296 C  CA  . ASP   B 1 245 ? 46.079  7.254   2.304   1.00 13.98 ? 245 ASP   B CA  1 
ATOM   4297 C  C   . ASP   B 1 245 ? 44.859  7.962   2.924   1.00 12.88 ? 245 ASP   B C   1 
ATOM   4298 O  O   . ASP   B 1 245 ? 43.800  8.009   2.297   1.00 12.29 ? 245 ASP   B O   1 
ATOM   4299 C  CB  . ASP   B 1 245 ? 46.103  5.785   2.707   1.00 15.04 ? 245 ASP   B CB  1 
ATOM   4300 C  CG  . ASP   B 1 245 ? 47.031  4.924   1.835   1.00 18.10 ? 245 ASP   B CG  1 
ATOM   4301 O  OD1 . ASP   B 1 245 ? 47.542  5.428   0.829   1.00 18.58 ? 245 ASP   B OD1 1 
ATOM   4302 O  OD2 . ASP   B 1 245 ? 47.161  3.681   2.146   1.00 21.30 ? 245 ASP   B OD2 1 
ATOM   4303 N  N   . HIS   B 1 246 ? 44.989  8.427   4.171   1.00 12.71 ? 246 HIS   B N   1 
ATOM   4304 C  CA  . HIS   B 1 246 ? 43.888  9.094   4.852   1.00 12.71 ? 246 HIS   B CA  1 
ATOM   4305 C  C   . HIS   B 1 246 ? 43.532  10.390  4.131   1.00 12.20 ? 246 HIS   B C   1 
ATOM   4306 O  O   . HIS   B 1 246 ? 42.356  10.717  3.966   1.00 12.55 ? 246 HIS   B O   1 
ATOM   4307 C  CB  . HIS   B 1 246 ? 44.248  9.412   6.297   1.00 13.14 ? 246 HIS   B CB  1 
ATOM   4308 C  CG  . HIS   B 1 246 ? 44.350  8.240   7.219   1.00 13.48 ? 246 HIS   B CG  1 
ATOM   4309 N  ND1 . HIS   B 1 246 ? 45.084  8.270   8.395   1.00 13.55 ? 246 HIS   B ND1 1 
ATOM   4310 C  CD2 . HIS   B 1 246 ? 43.757  7.051   7.172   1.00 14.52 ? 246 HIS   B CD2 1 
ATOM   4311 C  CE1 . HIS   B 1 246 ? 44.959  7.093   8.997   1.00 14.41 ? 246 HIS   B CE1 1 
ATOM   4312 N  NE2 . HIS   B 1 246 ? 44.122  6.358   8.307   1.00 14.52 ? 246 HIS   B NE2 1 
ATOM   4313 N  N   . VAL   B 1 247 ? 44.541  11.174  3.725   1.00 12.23 ? 247 VAL   B N   1 
ATOM   4314 C  CA  . VAL   B 1 247 ? 44.265  12.393  2.998   1.00 15.81 ? 247 VAL   B CA  1 
ATOM   4315 C  C   . VAL   B 1 247 ? 43.473  12.056  1.734   1.00 14.31 ? 247 VAL   B C   1 
ATOM   4316 O  O   . VAL   B 1 247 ? 42.531  12.763  1.353   1.00 14.13 ? 247 VAL   B O   1 
ATOM   4317 C  CB  . VAL   B 1 247 ? 45.560  13.147  2.677   1.00 19.28 ? 247 VAL   B CB  1 
ATOM   4318 C  CG1 . VAL   B 1 247 ? 45.309  14.253  1.665   1.00 23.89 ? 247 VAL   B CG1 1 
ATOM   4319 C  CG2 . VAL   B 1 247 ? 46.204  13.680  3.953   1.00 20.79 ? 247 VAL   B CG2 1 
ATOM   4320 N  N   . ASP   B 1 248 ? 43.869  10.971  1.054   1.00 13.75 ? 248 ASP   B N   1 
ATOM   4321 C  CA  . ASP   B 1 248 ? 43.242  10.585  -0.210  1.00 14.34 ? 248 ASP   B CA  1 
ATOM   4322 C  C   . ASP   B 1 248 ? 41.787  10.152  -0.009  1.00 13.30 ? 248 ASP   B C   1 
ATOM   4323 O  O   . ASP   B 1 248 ? 40.926  10.482  -0.839  1.00 13.48 ? 248 ASP   B O   1 
ATOM   4324 C  CB  . ASP   B 1 248 ? 44.107  9.525   -0.901  1.00 17.49 ? 248 ASP   B CB  1 
ATOM   4325 C  CG  . ASP   B 1 248 ? 45.394  10.152  -1.462  1.00 23.88 ? 248 ASP   B CG  1 
ATOM   4326 O  OD1 . ASP   B 1 248 ? 45.429  11.404  -1.648  1.00 25.76 ? 248 ASP   B OD1 1 
ATOM   4327 O  OD2 . ASP   B 1 248 ? 46.358  9.400   -1.694  1.00 30.49 ? 248 ASP   B OD2 1 
ATOM   4328 N  N   . ILE   B 1 249 ? 41.482  9.409   1.067   1.00 11.68 ? 249 ILE   B N   1 
ATOM   4329 C  CA  . ILE   B 1 249 ? 40.112  8.932   1.255   1.00 12.91 ? 249 ILE   B CA  1 
ATOM   4330 C  C   . ILE   B 1 249 ? 39.190  10.079  1.683   1.00 13.17 ? 249 ILE   B C   1 
ATOM   4331 O  O   . ILE   B 1 249 ? 37.985  9.932   1.551   1.00 11.95 ? 249 ILE   B O   1 
ATOM   4332 C  CB  . ILE   B 1 249 ? 39.967  7.722   2.198   1.00 13.31 ? 249 ILE   B CB  1 
ATOM   4333 C  CG1 . ILE   B 1 249 ? 40.389  7.959   3.635   1.00 12.78 ? 249 ILE   B CG1 1 
ATOM   4334 C  CG2 . ILE   B 1 249 ? 40.689  6.499   1.651   1.00 14.58 ? 249 ILE   B CG2 1 
ATOM   4335 C  CD1 . ILE   B 1 249 ? 39.903  6.869   4.568   1.00 13.19 ? 249 ILE   B CD1 1 
ATOM   4336 N  N   . LEU   B 1 250 ? 39.737  11.178  2.187   1.00 12.25 ? 250 LEU   B N   1 
ATOM   4337 C  CA  . LEU   B 1 250 ? 38.945  12.384  2.443   1.00 13.12 ? 250 LEU   B CA  1 
ATOM   4338 C  C   . LEU   B 1 250 ? 38.678  13.200  1.174   1.00 14.52 ? 250 LEU   B C   1 
ATOM   4339 O  O   . LEU   B 1 250 ? 37.901  14.138  1.233   1.00 13.48 ? 250 LEU   B O   1 
ATOM   4340 C  CB  . LEU   B 1 250 ? 39.662  13.245  3.487   1.00 12.52 ? 250 LEU   B CB  1 
ATOM   4341 C  CG  . LEU   B 1 250 ? 39.666  12.684  4.908   1.00 13.50 ? 250 LEU   B CG  1 
ATOM   4342 C  CD1 . LEU   B 1 250 ? 40.688  13.379  5.791   1.00 12.95 ? 250 LEU   B CD1 1 
ATOM   4343 C  CD2 . LEU   B 1 250 ? 38.287  12.768  5.554   1.00 15.30 ? 250 LEU   B CD2 1 
ATOM   4344 N  N   . GLY   B 1 251 ? 39.308  12.850  0.038   1.00 13.46 ? 251 GLY   B N   1 
ATOM   4345 C  CA  . GLY   B 1 251 ? 39.178  13.596  -1.207  1.00 14.38 ? 251 GLY   B CA  1 
ATOM   4346 C  C   . GLY   B 1 251 ? 37.734  13.834  -1.633  1.00 13.77 ? 251 GLY   B C   1 
ATOM   4347 O  O   . GLY   B 1 251 ? 37.361  14.981  -1.896  1.00 14.13 ? 251 GLY   B O   1 
ATOM   4348 N  N   . PRO   B 1 252 ? 36.894  12.795  -1.729  1.00 14.84 ? 252 PRO   B N   1 
ATOM   4349 C  CA  . PRO   B 1 252 ? 35.496  13.006  -2.126  1.00 15.81 ? 252 PRO   B CA  1 
ATOM   4350 C  C   . PRO   B 1 252 ? 34.702  13.983  -1.244  1.00 14.62 ? 252 PRO   B C   1 
ATOM   4351 O  O   . PRO   B 1 252 ? 33.948  14.815  -1.769  1.00 14.24 ? 252 PRO   B O   1 
ATOM   4352 C  CB  . PRO   B 1 252 ? 34.903  11.601  -2.108  1.00 18.45 ? 252 PRO   B CB  1 
ATOM   4353 C  CG  . PRO   B 1 252 ? 36.075  10.710  -2.400  1.00 17.89 ? 252 PRO   B CG  1 
ATOM   4354 C  CD  . PRO   B 1 252 ? 37.238  11.359  -1.667  1.00 16.95 ? 252 PRO   B CD  1 
ATOM   4355 N  N   . LEU   B 1 253 ? 34.893  13.941  0.082   1.00 12.70 ? 253 LEU   B N   1 
ATOM   4356 C  CA  . LEU   B 1 253 ? 34.186  14.859  0.976   1.00 11.56 ? 253 LEU   B CA  1 
ATOM   4357 C  C   . LEU   B 1 253 ? 34.707  16.272  0.799   1.00 11.39 ? 253 LEU   B C   1 
ATOM   4358 O  O   . LEU   B 1 253 ? 33.964  17.245  0.889   1.00 11.81 ? 253 LEU   B O   1 
ATOM   4359 C  CB  . LEU   B 1 253 ? 34.308  14.395  2.441   1.00 12.20 ? 253 LEU   B CB  1 
ATOM   4360 C  CG  . LEU   B 1 253 ? 33.513  13.129  2.764   1.00 12.87 ? 253 LEU   B CG  1 
ATOM   4361 C  CD1 . LEU   B 1 253 ? 33.850  12.618  4.146   1.00 12.72 ? 253 LEU   B CD1 1 
ATOM   4362 C  CD2 . LEU   B 1 253 ? 32.017  13.377  2.642   1.00 14.17 ? 253 LEU   B CD2 1 
ATOM   4363 N  N   . SER   B 1 254 ? 36.011  16.378  0.560   1.00 12.93 ? 254 SER   B N   1 
ATOM   4364 C  CA  . SER   B 1 254 ? 36.651  17.655  0.351   1.00 13.21 ? 254 SER   B CA  1 
ATOM   4365 C  C   . SER   B 1 254 ? 36.097  18.303  -0.909  1.00 13.51 ? 254 SER   B C   1 
ATOM   4366 O  O   . SER   B 1 254 ? 35.796  19.485  -0.955  1.00 12.94 ? 254 SER   B O   1 
ATOM   4367 C  CB  . SER   B 1 254 ? 38.168  17.480  0.280   1.00 13.37 ? 254 SER   B CB  1 
ATOM   4368 O  OG  . SER   B 1 254 ? 38.759  18.752  0.116   1.00 16.07 ? 254 SER   B OG  1 
ATOM   4369 N  N   . ALA   B 1 255 ? 35.910  17.506  -1.938  1.00 14.32 ? 255 ALA   B N   1 
ATOM   4370 C  CA  . ALA   B 1 255 ? 35.374  18.001  -3.207  1.00 14.98 ? 255 ALA   B CA  1 
ATOM   4371 C  C   . ALA   B 1 255 ? 33.917  18.433  -3.098  1.00 14.31 ? 255 ALA   B C   1 
ATOM   4372 O  O   . ALA   B 1 255 ? 33.547  19.508  -3.583  1.00 14.04 ? 255 ALA   B O   1 
ATOM   4373 C  CB  . ALA   B 1 255 ? 35.550  16.925  -4.237  1.00 16.53 ? 255 ALA   B CB  1 
ATOM   4374 N  N   . GLN   B 1 256 ? 33.121  17.633  -2.389  1.00 13.56 ? 256 GLN   B N   1 
ATOM   4375 C  CA  . GLN   B 1 256 ? 31.690  17.836  -2.238  1.00 13.93 ? 256 GLN   B CA  1 
ATOM   4376 C  C   . GLN   B 1 256 ? 31.445  19.134  -1.473  1.00 15.00 ? 256 GLN   B C   1 
ATOM   4377 O  O   . GLN   B 1 256 ? 30.521  19.886  -1.795  1.00 16.17 ? 256 GLN   B O   1 
ATOM   4378 C  CB  . GLN   B 1 256 ? 31.090  16.626  -1.533  1.00 15.20 ? 256 GLN   B CB  1 
ATOM   4379 C  CG  . GLN   B 1 256 ? 29.584  16.715  -1.251  1.00 17.20 ? 256 GLN   B CG  1 
ATOM   4380 C  CD  . GLN   B 1 256 ? 29.076  15.511  -0.484  1.00 17.67 ? 256 GLN   B CD  1 
ATOM   4381 O  OE1 . GLN   B 1 256 ? 29.791  14.525  -0.309  1.00 17.56 ? 256 GLN   B OE1 1 
ATOM   4382 N  NE2 . GLN   B 1 256 ? 27.826  15.550  -0.034  1.00 18.09 ? 256 GLN   B NE2 1 
ATOM   4383 N  N   . THR   B 1 257 ? 32.263  19.405  -0.438  1.00 13.00 ? 257 THR   B N   1 
ATOM   4384 C  CA  . THR   B 1 257 ? 32.063  20.587  0.381   1.00 14.12 ? 257 THR   B CA  1 
ATOM   4385 C  C   . THR   B 1 257 ? 32.900  21.783  -0.066  1.00 14.50 ? 257 THR   B C   1 
ATOM   4386 O  O   . THR   B 1 257 ? 32.641  22.907  0.397   1.00 15.58 ? 257 THR   B O   1 
ATOM   4387 C  CB  . THR   B 1 257 ? 32.432  20.305  1.834   1.00 13.18 ? 257 THR   B CB  1 
ATOM   4388 O  OG1 . THR   B 1 257 ? 33.810  19.897  1.897   1.00 13.02 ? 257 THR   B OG1 1 
ATOM   4389 C  CG2 . THR   B 1 257 ? 31.507  19.261  2.407   1.00 15.17 ? 257 THR   B CG2 1 
ATOM   4390 N  N   . GLY   B 1 258 ? 33.920  21.557  -0.911  1.00 13.66 ? 258 GLY   B N   1 
ATOM   4391 C  CA  . GLY   B 1 258 ? 34.845  22.615  -1.308  1.00 14.43 ? 258 GLY   B CA  1 
ATOM   4392 C  C   . GLY   B 1 258 ? 35.775  23.076  -0.175  1.00 17.09 ? 258 GLY   B C   1 
ATOM   4393 O  O   . GLY   B 1 258 ? 36.348  24.177  -0.245  1.00 18.28 ? 258 GLY   B O   1 
ATOM   4394 N  N   . ILE   B 1 259 ? 35.904  22.236  0.873   1.00 13.62 ? 259 ILE   B N   1 
ATOM   4395 C  CA  . ILE   B 1 259 ? 36.771  22.522  2.006   1.00 14.31 ? 259 ILE   B CA  1 
ATOM   4396 C  C   . ILE   B 1 259 ? 37.998  21.633  1.859   1.00 14.10 ? 259 ILE   B C   1 
ATOM   4397 O  O   . ILE   B 1 259 ? 37.906  20.405  2.016   1.00 12.20 ? 259 ILE   B O   1 
ATOM   4398 C  CB  . ILE   B 1 259 ? 36.090  22.326  3.382   1.00 15.44 ? 259 ILE   B CB  1 
ATOM   4399 C  CG1 . ILE   B 1 259 ? 34.780  23.098  3.584   1.00 16.63 ? 259 ILE   B CG1 1 
ATOM   4400 C  CG2 . ILE   B 1 259 ? 37.070  22.614  4.507   1.00 16.38 ? 259 ILE   B CG2 1 
ATOM   4401 C  CD1 . ILE   B 1 259 ? 34.866  24.493  3.150   1.00 20.30 ? 259 ILE   B CD1 1 
ATOM   4402 N  N   . ALA   B 1 260 ? 39.168  22.274  1.649   1.00 13.88 ? 260 ALA   B N   1 
ATOM   4403 C  CA  . ALA   B 1 260 ? 40.425  21.554  1.505   1.00 14.85 ? 260 ALA   B CA  1 
ATOM   4404 C  C   . ALA   B 1 260 ? 40.689  20.719  2.755   1.00 12.97 ? 260 ALA   B C   1 
ATOM   4405 O  O   . ALA   B 1 260 ? 40.434  21.168  3.864   1.00 11.21 ? 260 ALA   B O   1 
ATOM   4406 C  CB  . ALA   B 1 260 ? 41.573  22.525  1.317   1.00 17.67 ? 260 ALA   B CB  1 
ATOM   4407 N  N   . VAL   B 1 261 ? 41.272  19.529  2.577   1.00 12.64 ? 261 VAL   B N   1 
ATOM   4408 C  CA  . VAL   B 1 261 ? 41.570  18.679  3.727   1.00 13.24 ? 261 VAL   B CA  1 
ATOM   4409 C  C   . VAL   B 1 261 ? 42.392  19.401  4.789   1.00 13.97 ? 261 VAL   B C   1 
ATOM   4410 O  O   . VAL   B 1 261 ? 42.100  19.295  5.966   1.00 13.15 ? 261 VAL   B O   1 
ATOM   4411 C  CB  . VAL   B 1 261 ? 42.271  17.390  3.273   1.00 13.88 ? 261 VAL   B CB  1 
ATOM   4412 C  CG1 . VAL   B 1 261 ? 42.795  16.596  4.461   1.00 15.00 ? 261 VAL   B CG1 1 
ATOM   4413 C  CG2 . VAL   B 1 261 ? 41.345  16.586  2.377   1.00 15.56 ? 261 VAL   B CG2 1 
ATOM   4414 N  N   . LEU   B 1 262 ? 43.417  20.173  4.395   1.00 15.56 ? 262 LEU   B N   1 
ATOM   4415 C  CA  . LEU   B 1 262 ? 44.304  20.775  5.381   1.00 15.85 ? 262 LEU   B CA  1 
ATOM   4416 C  C   . LEU   B 1 262 ? 43.623  21.962  6.067   1.00 17.13 ? 262 LEU   B C   1 
ATOM   4417 O  O   . LEU   B 1 262 ? 43.955  22.288  7.191   1.00 14.45 ? 262 LEU   B O   1 
ATOM   4418 C  CB  . LEU   B 1 262 ? 45.618  21.189  4.717   1.00 16.87 ? 262 LEU   B CB  1 
ATOM   4419 C  CG  . LEU   B 1 262 ? 46.545  20.044  4.308   1.00 18.98 ? 262 LEU   B CG  1 
ATOM   4420 C  CD1 . LEU   B 1 262 ? 47.714  20.560  3.481   1.00 20.41 ? 262 LEU   B CD1 1 
ATOM   4421 C  CD2 . LEU   B 1 262 ? 47.047  19.318  5.536   1.00 21.20 ? 262 LEU   B CD2 1 
ATOM   4422 N  N   . ASP   B 1 263 ? 42.576  22.552  5.450   1.00 16.11 ? 263 ASP   B N   1 
ATOM   4423 C  CA  . ASP   B 1 263 ? 41.804  23.563  6.157   1.00 16.60 ? 263 ASP   B CA  1 
ATOM   4424 C  C   . ASP   B 1 263 ? 40.926  22.910  7.222   1.00 15.87 ? 263 ASP   B C   1 
ATOM   4425 O  O   . ASP   B 1 263 ? 40.768  23.438  8.315   1.00 15.74 ? 263 ASP   B O   1 
ATOM   4426 C  CB  . ASP   B 1 263 ? 40.918  24.362  5.191   1.00 17.84 ? 263 ASP   B CB  1 
ATOM   4427 C  CG  . ASP   B 1 263 ? 41.690  25.151  4.136   1.00 22.54 ? 263 ASP   B CG  1 
ATOM   4428 O  OD1 . ASP   B 1 263 ? 42.945  25.234  4.229   1.00 20.74 ? 263 ASP   B OD1 1 
ATOM   4429 O  OD2 . ASP   B 1 263 ? 41.016  25.725  3.229   1.00 24.15 ? 263 ASP   B OD2 1 
ATOM   4430 N  N   . MET   B 1 264 ? 40.387  21.718  6.927   1.00 13.92 ? 264 MET   B N   1 
ATOM   4431 C  CA  . MET   B 1 264 ? 39.596  21.019  7.914   1.00 12.92 ? 264 MET   B CA  1 
ATOM   4432 C  C   . MET   B 1 264 ? 40.518  20.602  9.069   1.00 12.34 ? 264 MET   B C   1 
ATOM   4433 O  O   . MET   B 1 264 ? 40.111  20.670  10.222  1.00 15.32 ? 264 MET   B O   1 
ATOM   4434 C  CB  . MET   B 1 264 ? 38.847  19.814  7.313   1.00 12.31 ? 264 MET   B CB  1 
ATOM   4435 C  CG  . MET   B 1 264 ? 37.823  19.233  8.243   1.00 13.08 ? 264 MET   B CG  1 
ATOM   4436 S  SD  . MET   B 1 264 ? 36.493  20.454  8.560   1.00 14.45 ? 264 MET   B SD  1 
ATOM   4437 C  CE  . MET   B 1 264 ? 35.355  19.969  7.268   1.00 15.52 ? 264 MET   B CE  1 
ATOM   4438 N  N   . CYS   B 1 265 ? 41.744  20.199  8.766   1.00 13.50 ? 265 CYS   B N   1 
ATOM   4439 C  CA  . CYS   B 1 265 ? 42.731  19.873  9.789   1.00 14.27 ? 265 CYS   B CA  1 
ATOM   4440 C  C   . CYS   B 1 265 ? 42.952  21.065  10.713  1.00 15.29 ? 265 CYS   B C   1 
ATOM   4441 O  O   . CYS   B 1 265 ? 42.991  20.929  11.939  1.00 13.65 ? 265 CYS   B O   1 
ATOM   4442 C  CB  . CYS   B 1 265 ? 44.067  19.424  9.181   1.00 15.62 ? 265 CYS   B CB  1 
ATOM   4443 S  SG  . CYS   B 1 265 ? 43.960  17.800  8.381   1.00 16.97 ? 265 CYS   B SG  1 
ATOM   4444 N  N   . ALA   B 1 266 ? 43.091  22.274  10.133  1.00 16.65 ? 266 ALA   B N   1 
ATOM   4445 C  CA  . ALA   B 1 266 ? 43.293  23.474  10.930  1.00 16.34 ? 266 ALA   B CA  1 
ATOM   4446 C  C   . ALA   B 1 266 ? 42.070  23.747  11.814  1.00 16.65 ? 266 ALA   B C   1 
ATOM   4447 O  O   . ALA   B 1 266 ? 42.178  24.194  12.962  1.00 19.06 ? 266 ALA   B O   1 
ATOM   4448 C  CB  . ALA   B 1 266 ? 43.603  24.630  10.019  1.00 17.46 ? 266 ALA   B CB  1 
ATOM   4449 N  N   . SER   B 1 267 ? 40.859  23.448  11.313  1.00 15.22 ? 267 SER   B N   1 
ATOM   4450 C  CA  . SER   B 1 267 ? 39.655  23.589  12.113  1.00 15.00 ? 267 SER   B CA  1 
ATOM   4451 C  C   . SER   B 1 267 ? 39.673  22.612  13.284  1.00 16.23 ? 267 SER   B C   1 
ATOM   4452 O  O   . SER   B 1 267 ? 39.264  22.933  14.406  1.00 16.76 ? 267 SER   B O   1 
ATOM   4453 C  CB  . SER   B 1 267 ? 38.388  23.457  11.271  1.00 16.35 ? 267 SER   B CB  1 
ATOM   4454 O  OG  . SER   B 1 267 ? 38.326  24.516  10.319  1.00 19.48 ? 267 SER   B OG  1 
ATOM   4455 N  N   . LEU   B 1 268 ? 40.067  21.360  13.003  1.00 15.70 ? 268 LEU   B N   1 
ATOM   4456 C  CA  . LEU   B 1 268 ? 40.090  20.364  14.057  1.00 14.51 ? 268 LEU   B CA  1 
ATOM   4457 C  C   . LEU   B 1 268 ? 41.156  20.791  15.089  1.00 16.53 ? 268 LEU   B C   1 
ATOM   4458 O  O   . LEU   B 1 268 ? 40.944  20.706  16.299  1.00 17.87 ? 268 LEU   B O   1 
ATOM   4459 C  CB  . LEU   B 1 268 ? 40.403  18.985  13.468  1.00 14.71 ? 268 LEU   B CB  1 
ATOM   4460 C  CG  . LEU   B 1 268 ? 40.526  17.859  14.496  1.00 15.44 ? 268 LEU   B CG  1 
ATOM   4461 C  CD1 . LEU   B 1 268 ? 39.306  17.790  15.386  1.00 16.47 ? 268 LEU   B CD1 1 
ATOM   4462 C  CD2 . LEU   B 1 268 ? 40.736  16.527  13.770  1.00 17.53 ? 268 LEU   B CD2 1 
ATOM   4463 N  N   . LYS   B 1 269 ? 42.286  21.277  14.604  1.00 19.05 ? 269 LYS   B N   1 
ATOM   4464 C  CA  . LYS   B 1 269 ? 43.360  21.696  15.501  1.00 22.17 ? 269 LYS   B CA  1 
ATOM   4465 C  C   . LYS   B 1 269 ? 42.857  22.762  16.484  1.00 25.07 ? 269 LYS   B C   1 
ATOM   4466 O  O   . LYS   B 1 269 ? 43.105  22.652  17.692  1.00 22.60 ? 269 LYS   B O   1 
ATOM   4467 C  CB  . LYS   B 1 269 ? 44.568  22.115  14.666  1.00 25.85 ? 269 LYS   B CB  1 
ATOM   4468 C  CG  . LYS   B 1 269 ? 45.764  22.638  15.449  1.00 31.38 ? 269 LYS   B CG  1 
ATOM   4469 C  CD  . LYS   B 1 269 ? 46.905  23.021  14.536  1.00 37.08 ? 269 LYS   B CD  1 
ATOM   4470 C  CE  . LYS   B 1 269 ? 47.612  24.280  14.997  1.00 42.60 ? 269 LYS   B CE  1 
ATOM   4471 N  NZ  . LYS   B 1 269 ? 48.398  24.880  13.897  1.00 47.01 ? 269 LYS   B NZ  1 
ATOM   4472 N  N   . GLU   B 1 270 ? 42.050  23.737  16.014  1.00 24.64 ? 270 GLU   B N   1 
ATOM   4473 C  CA  . GLU   B 1 270 ? 41.483  24.739  16.920  1.00 23.24 ? 270 GLU   B CA  1 
ATOM   4474 C  C   . GLU   B 1 270 ? 40.527  24.119  17.921  1.00 23.56 ? 270 GLU   B C   1 
ATOM   4475 O  O   . GLU   B 1 270 ? 40.441  24.581  19.061  1.00 24.97 ? 270 GLU   B O   1 
ATOM   4476 C  CB  . GLU   B 1 270 ? 40.758  25.853  16.152  1.00 27.18 ? 270 GLU   B CB  1 
ATOM   4477 C  CG  . GLU   B 1 270 ? 41.699  26.710  15.345  1.00 36.01 ? 270 GLU   B CG  1 
ATOM   4478 C  CD  . GLU   B 1 270 ? 42.821  27.376  16.139  1.00 46.87 ? 270 GLU   B CD  1 
ATOM   4479 O  OE1 . GLU   B 1 270 ? 42.509  28.025  17.168  1.00 53.17 ? 270 GLU   B OE1 1 
ATOM   4480 O  OE2 . GLU   B 1 270 ? 44.007  27.246  15.739  1.00 49.24 ? 270 GLU   B OE2 1 
ATOM   4481 N  N   . LEU   B 1 271 ? 39.762  23.096  17.513  1.00 20.80 ? 271 LEU   B N   1 
ATOM   4482 C  CA  . LEU   B 1 271 ? 38.842  22.469  18.442  1.00 22.20 ? 271 LEU   B CA  1 
ATOM   4483 C  C   . LEU   B 1 271 ? 39.636  21.761  19.539  1.00 23.20 ? 271 LEU   B C   1 
ATOM   4484 O  O   . LEU   B 1 271 ? 39.217  21.790  20.691  1.00 25.88 ? 271 LEU   B O   1 
ATOM   4485 C  CB  . LEU   B 1 271 ? 37.933  21.478  17.707  1.00 21.81 ? 271 LEU   B CB  1 
ATOM   4486 C  CG  . LEU   B 1 271 ? 36.833  22.086  16.837  1.00 22.25 ? 271 LEU   B CG  1 
ATOM   4487 C  CD1 . LEU   B 1 271 ? 36.097  20.983  16.082  1.00 21.96 ? 271 LEU   B CD1 1 
ATOM   4488 C  CD2 . LEU   B 1 271 ? 35.847  22.898  17.680  1.00 25.94 ? 271 LEU   B CD2 1 
ATOM   4489 N  N   . LEU   B 1 272 ? 40.739  21.100  19.166  1.00 25.04 ? 272 LEU   B N   1 
ATOM   4490 C  CA  . LEU   B 1 272 ? 41.569  20.384  20.132  1.00 27.01 ? 272 LEU   B CA  1 
ATOM   4491 C  C   . LEU   B 1 272 ? 42.154  21.359  21.155  1.00 31.00 ? 272 LEU   B C   1 
ATOM   4492 O  O   . LEU   B 1 272 ? 42.208  21.047  22.351  1.00 29.36 ? 272 LEU   B O   1 
ATOM   4493 C  CB  . LEU   B 1 272 ? 42.692  19.637  19.401  1.00 25.81 ? 272 LEU   B CB  1 
ATOM   4494 C  CG  . LEU   B 1 272 ? 42.213  18.450  18.564  1.00 25.59 ? 272 LEU   B CG  1 
ATOM   4495 C  CD1 . LEU   B 1 272 ? 43.380  17.580  18.137  1.00 27.57 ? 272 LEU   B CD1 1 
ATOM   4496 C  CD2 . LEU   B 1 272 ? 41.179  17.647  19.312  1.00 28.52 ? 272 LEU   B CD2 1 
ATOM   4497 N  N   . GLN   B 1 273 ? 42.644  22.490  20.650  1.00 30.46 ? 273 GLN   B N   1 
ATOM   4498 C  CA  . GLN   B 1 273 ? 43.404  23.430  21.462  1.00 34.77 ? 273 GLN   B CA  1 
ATOM   4499 C  C   . GLN   B 1 273 ? 42.487  24.262  22.354  1.00 35.64 ? 273 GLN   B C   1 
ATOM   4500 O  O   . GLN   B 1 273 ? 42.914  24.627  23.441  1.00 35.84 ? 273 GLN   B O   1 
ATOM   4501 C  CB  . GLN   B 1 273 ? 44.283  24.325  20.592  1.00 32.13 ? 273 GLN   B CB  1 
ATOM   4502 C  CG  . GLN   B 1 273 ? 45.357  23.546  19.863  1.00 35.31 ? 273 GLN   B CG  1 
ATOM   4503 C  CD  . GLN   B 1 273 ? 46.316  24.405  19.078  1.00 39.10 ? 273 GLN   B CD  1 
ATOM   4504 O  OE1 . GLN   B 1 273 ? 45.934  25.331  18.360  1.00 40.67 ? 273 GLN   B OE1 1 
ATOM   4505 N  NE2 . GLN   B 1 273 ? 47.588  24.088  19.206  1.00 36.30 ? 273 GLN   B NE2 1 
ATOM   4506 N  N   . ASN   B 1 274 ? 41.250  24.541  21.915  1.00 34.77 ? 274 ASN   B N   1 
ATOM   4507 C  CA  . ASN   B 1 274 ? 40.374  25.492  22.591  1.00 36.28 ? 274 ASN   B CA  1 
ATOM   4508 C  C   . ASN   B 1 274 ? 39.115  24.843  23.135  1.00 37.30 ? 274 ASN   B C   1 
ATOM   4509 O  O   . ASN   B 1 274 ? 38.360  25.490  23.845  1.00 43.02 ? 274 ASN   B O   1 
ATOM   4510 C  CB  . ASN   B 1 274 ? 39.892  26.609  21.667  1.00 38.10 ? 274 ASN   B CB  1 
ATOM   4511 C  CG  . ASN   B 1 274 ? 41.035  27.421  21.119  1.00 38.35 ? 274 ASN   B CG  1 
ATOM   4512 O  OD1 . ASN   B 1 274 ? 41.269  27.444  19.919  1.00 50.17 ? 274 ASN   B OD1 1 
ATOM   4513 N  ND2 . ASN   B 1 274 ? 41.768  28.076  22.000  1.00 42.97 ? 274 ASN   B ND2 1 
ATOM   4514 N  N   . GLY   B 1 275 ? 38.858  23.595  22.772  1.00 34.32 ? 275 GLY   B N   1 
ATOM   4515 C  CA  . GLY   B 1 275 ? 37.607  22.958  23.121  1.00 32.34 ? 275 GLY   B CA  1 
ATOM   4516 C  C   . GLY   B 1 275 ? 36.426  23.474  22.310  1.00 36.35 ? 275 GLY   B C   1 
ATOM   4517 O  O   . GLY   B 1 275 ? 36.572  24.322  21.428  1.00 36.14 ? 275 GLY   B O   1 
ATOM   4518 N  N   . MET   B 1 276 ? 35.259  22.943  22.670  1.00 38.38 ? 276 MET   B N   1 
ATOM   4519 C  CA  . MET   B 1 276 ? 33.986  23.194  22.021  1.00 44.27 ? 276 MET   B CA  1 
ATOM   4520 C  C   . MET   B 1 276 ? 33.335  24.452  22.598  1.00 48.48 ? 276 MET   B C   1 
ATOM   4521 O  O   . MET   B 1 276 ? 32.375  24.960  22.026  1.00 45.42 ? 276 MET   B O   1 
ATOM   4522 C  CB  . MET   B 1 276 ? 33.044  22.015  22.292  1.00 49.95 ? 276 MET   B CB  1 
ATOM   4523 C  CG  . MET   B 1 276 ? 33.628  20.672  21.928  1.00 55.99 ? 276 MET   B CG  1 
ATOM   4524 S  SD  . MET   B 1 276 ? 33.658  20.419  20.132  1.00 60.09 ? 276 MET   B SD  1 
ATOM   4525 C  CE  . MET   B 1 276 ? 31.944  19.987  19.829  1.00 48.99 ? 276 MET   B CE  1 
ATOM   4526 N  N   . ASN   B 1 277 ? 33.813  24.885  23.777  1.00 55.79 ? 277 ASN   B N   1 
ATOM   4527 C  CA  . ASN   B 1 277 ? 33.323  26.072  24.471  1.00 54.69 ? 277 ASN   B CA  1 
ATOM   4528 C  C   . ASN   B 1 277 ? 31.795  26.109  24.514  1.00 48.43 ? 277 ASN   B C   1 
ATOM   4529 O  O   . ASN   B 1 277 ? 31.191  27.148  24.250  1.00 52.33 ? 277 ASN   B O   1 
ATOM   4530 C  CB  . ASN   B 1 277 ? 33.870  27.358  23.842  1.00 59.03 ? 277 ASN   B CB  1 
ATOM   4531 C  CG  . ASN   B 1 277 ? 35.364  27.317  23.590  1.00 70.74 ? 277 ASN   B CG  1 
ATOM   4532 O  OD1 . ASN   B 1 277 ? 35.828  27.784  22.550  1.00 78.86 ? 277 ASN   B OD1 1 
ATOM   4533 N  ND2 . ASN   B 1 277 ? 36.130  26.792  24.536  1.00 70.66 ? 277 ASN   B ND2 1 
ATOM   4534 N  N   . GLY   B 1 278 ? 31.177  24.975  24.866  1.00 45.08 ? 278 GLY   B N   1 
ATOM   4535 C  CA  . GLY   B 1 278 ? 29.743  24.917  25.090  1.00 45.95 ? 278 GLY   B CA  1 
ATOM   4536 C  C   . GLY   B 1 278 ? 28.919  24.720  23.821  1.00 48.68 ? 278 GLY   B C   1 
ATOM   4537 O  O   . GLY   B 1 278 ? 27.698  24.819  23.864  1.00 48.18 ? 278 GLY   B O   1 
ATOM   4538 N  N   . ARG   B 1 279 ? 29.566  24.436  22.683  1.00 52.96 ? 279 ARG   B N   1 
ATOM   4539 C  CA  . ARG   B 1 279 ? 28.832  24.282  21.436  1.00 46.37 ? 279 ARG   B CA  1 
ATOM   4540 C  C   . ARG   B 1 279 ? 28.790  22.806  21.081  1.00 39.25 ? 279 ARG   B C   1 
ATOM   4541 O  O   . ARG   B 1 279 ? 29.532  22.012  21.646  1.00 40.24 ? 279 ARG   B O   1 
ATOM   4542 C  CB  . ARG   B 1 279 ? 29.487  25.086  20.310  1.00 48.43 ? 279 ARG   B CB  1 
ATOM   4543 C  CG  . ARG   B 1 279 ? 29.782  26.530  20.686  1.00 49.43 ? 279 ARG   B CG  1 
ATOM   4544 C  CD  . ARG   B 1 279 ? 30.143  27.395  19.502  1.00 49.03 ? 279 ARG   B CD  1 
ATOM   4545 N  NE  . ARG   B 1 279 ? 28.992  27.594  18.630  1.00 46.16 ? 279 ARG   B NE  1 
ATOM   4546 C  CZ  . ARG   B 1 279 ? 28.907  28.529  17.690  1.00 47.83 ? 279 ARG   B CZ  1 
ATOM   4547 N  NH1 . ARG   B 1 279 ? 29.872  29.428  17.553  1.00 49.88 ? 279 ARG   B NH1 1 
ATOM   4548 N  NH2 . ARG   B 1 279 ? 27.854  28.557  16.890  1.00 41.47 ? 279 ARG   B NH2 1 
ATOM   4549 N  N   . THR   B 1 280 ? 27.964  22.475  20.089  1.00 35.57 ? 280 THR   B N   1 
ATOM   4550 C  CA  . THR   B 1 280 ? 27.803  21.101  19.654  1.00 31.14 ? 280 THR   B CA  1 
ATOM   4551 C  C   . THR   B 1 280 ? 27.973  21.013  18.133  1.00 29.28 ? 280 THR   B C   1 
ATOM   4552 O  O   . THR   B 1 280 ? 27.821  21.992  17.392  1.00 24.85 ? 280 THR   B O   1 
ATOM   4553 C  CB  . THR   B 1 280 ? 26.446  20.502  20.052  1.00 34.51 ? 280 THR   B CB  1 
ATOM   4554 O  OG1 . THR   B 1 280 ? 25.375  21.141  19.345  1.00 33.45 ? 280 THR   B OG1 1 
ATOM   4555 C  CG2 . THR   B 1 280 ? 26.204  20.565  21.545  1.00 33.54 ? 280 THR   B CG2 1 
ATOM   4556 N  N   . ILE   B 1 281 ? 28.290  19.801  17.701  1.00 23.78 ? 281 ILE   B N   1 
ATOM   4557 C  CA  . ILE   B 1 281 ? 28.430  19.499  16.291  1.00 22.87 ? 281 ILE   B CA  1 
ATOM   4558 C  C   . ILE   B 1 281 ? 27.521  18.332  16.014  1.00 22.45 ? 281 ILE   B C   1 
ATOM   4559 O  O   . ILE   B 1 281 ? 27.593  17.306  16.686  1.00 24.23 ? 281 ILE   B O   1 
ATOM   4560 C  CB  . ILE   B 1 281 ? 29.904  19.229  15.911  1.00 21.53 ? 281 ILE   B CB  1 
ATOM   4561 C  CG1 . ILE   B 1 281 ? 30.747  20.498  16.087  1.00 22.24 ? 281 ILE   B CG1 1 
ATOM   4562 C  CG2 . ILE   B 1 281 ? 29.992  18.665  14.487  1.00 22.89 ? 281 ILE   B CG2 1 
ATOM   4563 C  CD1 . ILE   B 1 281 ? 32.235  20.278  15.948  1.00 22.41 ? 281 ILE   B CD1 1 
ATOM   4564 N  N   . LEU   B 1 282 ? 26.657  18.498  15.008  1.00 22.09 ? 282 LEU   B N   1 
ATOM   4565 C  CA  . LEU   B 1 282 ? 25.636  17.506  14.722  1.00 20.84 ? 282 LEU   B CA  1 
ATOM   4566 C  C   . LEU   B 1 282 ? 24.896  17.119  16.003  1.00 23.49 ? 282 LEU   B C   1 
ATOM   4567 O  O   . LEU   B 1 282 ? 24.573  15.956  16.165  1.00 22.60 ? 282 LEU   B O   1 
ATOM   4568 C  CB  . LEU   B 1 282 ? 26.247  16.291  14.024  1.00 22.68 ? 282 LEU   B CB  1 
ATOM   4569 C  CG  . LEU   B 1 282 ? 26.531  16.490  12.532  1.00 21.25 ? 282 LEU   B CG  1 
ATOM   4570 C  CD1 . LEU   B 1 282 ? 27.505  15.455  11.973  1.00 22.95 ? 282 LEU   B CD1 1 
ATOM   4571 C  CD2 . LEU   B 1 282 ? 25.215  16.478  11.751  1.00 22.21 ? 282 LEU   B CD2 1 
ATOM   4572 N  N   . GLY   B 1 283 ? 24.666  18.095  16.892  1.00 28.79 ? 283 GLY   B N   1 
ATOM   4573 C  CA  . GLY   B 1 283 ? 23.814  17.898  18.055  1.00 31.05 ? 283 GLY   B CA  1 
ATOM   4574 C  C   . GLY   B 1 283 ? 24.540  17.228  19.218  1.00 38.13 ? 283 GLY   B C   1 
ATOM   4575 O  O   . GLY   B 1 283 ? 23.899  16.837  20.184  1.00 40.83 ? 283 GLY   B O   1 
ATOM   4576 N  N   . SER   B 1 284 ? 25.872  17.096  19.136  1.00 34.33 ? 284 SER   B N   1 
ATOM   4577 C  CA  . SER   B 1 284 ? 26.614  16.359  20.142  1.00 34.22 ? 284 SER   B CA  1 
ATOM   4578 C  C   . SER   B 1 284 ? 27.859  17.134  20.545  1.00 30.31 ? 284 SER   B C   1 
ATOM   4579 O  O   . SER   B 1 284 ? 28.519  17.756  19.709  1.00 27.08 ? 284 SER   B O   1 
ATOM   4580 C  CB  . SER   B 1 284 ? 26.954  14.986  19.656  1.00 37.15 ? 284 SER   B CB  1 
ATOM   4581 O  OG  . SER   B 1 284 ? 27.854  14.374  20.572  1.00 45.41 ? 284 SER   B OG  1 
ATOM   4582 N  N   . ALA   B 1 285 ? 28.200  17.059  21.840  1.00 28.52 ? 285 ALA   B N   1 
ATOM   4583 C  CA  . ALA   B 1 285 ? 29.394  17.707  22.356  1.00 28.23 ? 285 ALA   B CA  1 
ATOM   4584 C  C   . ALA   B 1 285 ? 30.628  16.824  22.170  1.00 26.13 ? 285 ALA   B C   1 
ATOM   4585 O  O   . ALA   B 1 285 ? 31.722  17.303  22.409  1.00 31.95 ? 285 ALA   B O   1 
ATOM   4586 C  CB  . ALA   B 1 285 ? 29.229  18.066  23.827  1.00 29.92 ? 285 ALA   B CB  1 
ATOM   4587 N  N   . LEU   B 1 286 ? 30.443  15.566  21.761  1.00 25.33 ? 286 LEU   B N   1 
ATOM   4588 C  CA  . LEU   B 1 286 ? 31.538  14.631  21.539  1.00 27.66 ? 286 LEU   B CA  1 
ATOM   4589 C  C   . LEU   B 1 286 ? 31.873  14.540  20.047  1.00 22.14 ? 286 LEU   B C   1 
ATOM   4590 O  O   . LEU   B 1 286 ? 30.962  14.425  19.248  1.00 26.07 ? 286 LEU   B O   1 
ATOM   4591 C  CB  . LEU   B 1 286 ? 31.084  13.251  22.012  1.00 30.70 ? 286 LEU   B CB  1 
ATOM   4592 C  CG  . LEU   B 1 286 ? 30.660  13.153  23.475  1.00 38.79 ? 286 LEU   B CG  1 
ATOM   4593 C  CD1 . LEU   B 1 286 ? 30.517  11.688  23.875  1.00 40.90 ? 286 LEU   B CD1 1 
ATOM   4594 C  CD2 . LEU   B 1 286 ? 31.650  13.895  24.361  1.00 36.55 ? 286 LEU   B CD2 1 
ATOM   4595 N  N   . LEU   B 1 287 ? 33.157  14.444  19.685  1.00 20.98 ? 287 LEU   B N   1 
ATOM   4596 C  CA  . LEU   B 1 287 ? 33.494  14.143  18.288  1.00 20.52 ? 287 LEU   B CA  1 
ATOM   4597 C  C   . LEU   B 1 287 ? 33.520  12.626  18.037  1.00 20.37 ? 287 LEU   B C   1 
ATOM   4598 O  O   . LEU   B 1 287 ? 34.385  11.940  18.554  1.00 23.61 ? 287 LEU   B O   1 
ATOM   4599 C  CB  . LEU   B 1 287 ? 34.850  14.774  17.968  1.00 20.51 ? 287 LEU   B CB  1 
ATOM   4600 C  CG  . LEU   B 1 287 ? 34.930  16.301  18.129  1.00 22.70 ? 287 LEU   B CG  1 
ATOM   4601 C  CD1 . LEU   B 1 287 ? 36.336  16.803  17.965  1.00 22.98 ? 287 LEU   B CD1 1 
ATOM   4602 C  CD2 . LEU   B 1 287 ? 33.983  17.017  17.161  1.00 26.14 ? 287 LEU   B CD2 1 
ATOM   4603 N  N   . GLU   B 1 288 ? 32.688  12.149  17.112  1.00 17.99 ? 288 GLU   B N   1 
ATOM   4604 C  CA  . GLU   B 1 288 ? 32.562  10.750  16.724  1.00 17.01 ? 288 GLU   B CA  1 
ATOM   4605 C  C   . GLU   B 1 288 ? 33.777  10.323  15.903  1.00 15.56 ? 288 GLU   B C   1 
ATOM   4606 O  O   . GLU   B 1 288 ? 34.197  11.089  15.028  1.00 13.38 ? 288 GLU   B O   1 
ATOM   4607 C  CB  . GLU   B 1 288 ? 31.257  10.661  15.933  1.00 19.25 ? 288 GLU   B CB  1 
ATOM   4608 C  CG  . GLU   B 1 288 ? 30.922  9.312   15.360  1.00 23.37 ? 288 GLU   B CG  1 
ATOM   4609 C  CD  . GLU   B 1 288 ? 30.777  8.167   16.352  1.00 28.17 ? 288 GLU   B CD  1 
ATOM   4610 O  OE1 . GLU   B 1 288 ? 31.468  7.113   16.160  1.00 23.88 ? 288 GLU   B OE1 1 
ATOM   4611 O  OE2 . GLU   B 1 288 ? 29.954  8.313   17.296  1.00 26.93 ? 288 GLU   B OE2 1 
ATOM   4612 N  N   . ASP   B 1 289 ? 34.359  9.138   16.199  1.00 13.51 ? 289 ASP   B N   1 
ATOM   4613 C  CA  . ASP   B 1 289 ? 35.529  8.672   15.476  1.00 12.50 ? 289 ASP   B CA  1 
ATOM   4614 C  C   . ASP   B 1 289 ? 35.334  7.283   14.853  1.00 13.11 ? 289 ASP   B C   1 
ATOM   4615 O  O   . ASP   B 1 289 ? 36.349  6.727   14.444  1.00 12.71 ? 289 ASP   B O   1 
ATOM   4616 C  CB  . ASP   B 1 289 ? 36.820  8.767   16.286  1.00 12.98 ? 289 ASP   B CB  1 
ATOM   4617 C  CG  . ASP   B 1 289 ? 37.058  7.666   17.294  1.00 14.26 ? 289 ASP   B CG  1 
ATOM   4618 O  OD1 . ASP   B 1 289 ? 36.058  6.952   17.630  1.00 14.36 ? 289 ASP   B OD1 1 
ATOM   4619 O  OD2 . ASP   B 1 289 ? 38.237  7.551   17.727  1.00 14.10 ? 289 ASP   B OD2 1 
ATOM   4620 N  N   . GLU   B 1 290 ? 34.094  6.767   14.760  1.00 13.34 ? 290 GLU   B N   1 
ATOM   4621 C  CA  . GLU   B 1 290 ? 33.845  5.449   14.198  1.00 14.33 ? 290 GLU   B CA  1 
ATOM   4622 C  C   . GLU   B 1 290 ? 32.974  5.511   12.950  1.00 14.93 ? 290 GLU   B C   1 
ATOM   4623 O  O   . GLU   B 1 290 ? 32.445  4.499   12.490  1.00 13.93 ? 290 GLU   B O   1 
ATOM   4624 C  CB  . GLU   B 1 290 ? 33.317  4.456   15.240  1.00 17.87 ? 290 GLU   B CB  1 
ATOM   4625 C  CG  . GLU   B 1 290 ? 34.315  4.114   16.351  1.00 19.46 ? 290 GLU   B CG  1 
ATOM   4626 C  CD  . GLU   B 1 290 ? 34.197  2.733   17.011  1.00 21.86 ? 290 GLU   B CD  1 
ATOM   4627 O  OE1 . GLU   B 1 290 ? 33.239  1.947   16.643  1.00 23.38 ? 290 GLU   B OE1 1 
ATOM   4628 O  OE2 . GLU   B 1 290 ? 35.076  2.388   17.862  1.00 19.60 ? 290 GLU   B OE2 1 
ATOM   4629 N  N   . PHE   B 1 291 ? 32.913  6.681   12.300  1.00 13.36 ? 291 PHE   B N   1 
ATOM   4630 C  CA  . PHE   B 1 291 ? 32.349  6.763   10.958  1.00 14.15 ? 291 PHE   B CA  1 
ATOM   4631 C  C   . PHE   B 1 291 ? 33.432  7.150   9.954   1.00 12.23 ? 291 PHE   B C   1 
ATOM   4632 O  O   . PHE   B 1 291 ? 34.021  8.215   10.088  1.00 11.47 ? 291 PHE   B O   1 
ATOM   4633 C  CB  . PHE   B 1 291 ? 31.345  7.905   10.847  1.00 18.38 ? 291 PHE   B CB  1 
ATOM   4634 C  CG  . PHE   B 1 291 ? 30.017  7.614   11.475  1.00 22.80 ? 291 PHE   B CG  1 
ATOM   4635 C  CD1 . PHE   B 1 291 ? 29.195  6.632   10.960  1.00 28.23 ? 291 PHE   B CD1 1 
ATOM   4636 C  CD2 . PHE   B 1 291 ? 29.630  8.279   12.628  1.00 27.97 ? 291 PHE   B CD2 1 
ATOM   4637 C  CE1 . PHE   B 1 291 ? 27.983  6.340   11.579  1.00 33.28 ? 291 PHE   B CE1 1 
ATOM   4638 C  CE2 . PHE   B 1 291 ? 28.407  8.014   13.228  1.00 33.75 ? 291 PHE   B CE2 1 
ATOM   4639 C  CZ  . PHE   B 1 291 ? 27.589  7.037   12.704  1.00 31.65 ? 291 PHE   B CZ  1 
ATOM   4640 N  N   . THR   B 1 292 ? 33.725  6.287   8.991   1.00 12.29 ? 292 THR   B N   1 
ATOM   4641 C  CA  . THR   B 1 292 ? 34.741  6.561   7.990   1.00 12.97 ? 292 THR   B CA  1 
ATOM   4642 C  C   . THR   B 1 292 ? 34.220  7.520   6.921   1.00 12.66 ? 292 THR   B C   1 
ATOM   4643 O  O   . THR   B 1 292 ? 33.018  7.732   6.758   1.00 12.62 ? 292 THR   B O   1 
ATOM   4644 C  CB  . THR   B 1 292 ? 35.190  5.282   7.284   1.00 14.49 ? 292 THR   B CB  1 
ATOM   4645 O  OG1 . THR   B 1 292 ? 34.085  4.786   6.520   1.00 16.58 ? 292 THR   B OG1 1 
ATOM   4646 C  CG2 . THR   B 1 292 ? 35.667  4.242   8.272   1.00 14.35 ? 292 THR   B CG2 1 
ATOM   4647 N  N   . PRO   B 1 293 ? 35.137  8.086   6.099   1.00 12.44 ? 293 PRO   B N   1 
ATOM   4648 C  CA  . PRO   B 1 293 ? 34.732  8.865   4.937   1.00 13.86 ? 293 PRO   B CA  1 
ATOM   4649 C  C   . PRO   B 1 293 ? 33.762  8.119   4.034   1.00 16.59 ? 293 PRO   B C   1 
ATOM   4650 O  O   . PRO   B 1 293 ? 32.781  8.702   3.605   1.00 19.62 ? 293 PRO   B O   1 
ATOM   4651 C  CB  . PRO   B 1 293 ? 36.065  9.180   4.261   1.00 13.55 ? 293 PRO   B CB  1 
ATOM   4652 C  CG  . PRO   B 1 293 ? 37.036  9.226   5.413   1.00 13.00 ? 293 PRO   B CG  1 
ATOM   4653 C  CD  . PRO   B 1 293 ? 36.580  8.101   6.332   1.00 13.60 ? 293 PRO   B CD  1 
ATOM   4654 N  N   . PHE   B 1 294 ? 33.974  6.805   3.842   1.00 16.42 ? 294 PHE   B N   1 
ATOM   4655 C  CA  . PHE   B 1 294 ? 33.076  5.996   3.046   1.00 21.48 ? 294 PHE   B CA  1 
ATOM   4656 C  C   . PHE   B 1 294 ? 31.721  5.837   3.727   1.00 19.28 ? 294 PHE   B C   1 
ATOM   4657 O  O   . PHE   B 1 294 ? 30.709  5.912   3.034   1.00 20.69 ? 294 PHE   B O   1 
ATOM   4658 C  CB  . PHE   B 1 294 ? 33.695  4.620   2.803   1.00 29.43 ? 294 PHE   B CB  1 
ATOM   4659 C  CG  . PHE   B 1 294 ? 34.839  4.627   1.822   1.00 39.42 ? 294 PHE   B CG  1 
ATOM   4660 C  CD1 . PHE   B 1 294 ? 34.600  4.688   0.456   1.00 49.25 ? 294 PHE   B CD1 1 
ATOM   4661 C  CD2 . PHE   B 1 294 ? 36.154  4.603   2.265   1.00 47.51 ? 294 PHE   B CD2 1 
ATOM   4662 C  CE1 . PHE   B 1 294 ? 35.654  4.690   -0.448  1.00 55.38 ? 294 PHE   B CE1 1 
ATOM   4663 C  CE2 . PHE   B 1 294 ? 37.204  4.622   1.361   1.00 46.02 ? 294 PHE   B CE2 1 
ATOM   4664 C  CZ  . PHE   B 1 294 ? 36.956  4.663   0.007   1.00 50.87 ? 294 PHE   B CZ  1 
ATOM   4665 N  N   . ASP   B 1 295 ? 31.693  5.707   5.071   1.00 16.53 ? 295 ASP   B N   1 
ATOM   4666 C  CA  . ASP   B 1 295 ? 30.426  5.636   5.794   1.00 17.53 ? 295 ASP   B CA  1 
ATOM   4667 C  C   . ASP   B 1 295 ? 29.604  6.921   5.618   1.00 18.50 ? 295 ASP   B C   1 
ATOM   4668 O  O   . ASP   B 1 295 ? 28.371  6.883   5.531   1.00 17.51 ? 295 ASP   B O   1 
ATOM   4669 C  CB  . ASP   B 1 295 ? 30.609  5.404   7.292   1.00 19.52 ? 295 ASP   B CB  1 
ATOM   4670 C  CG  . ASP   B 1 295 ? 31.098  3.995   7.559   1.00 21.80 ? 295 ASP   B CG  1 
ATOM   4671 O  OD1 . ASP   B 1 295 ? 30.484  3.071   6.968   1.00 26.62 ? 295 ASP   B OD1 1 
ATOM   4672 O  OD2 . ASP   B 1 295 ? 32.010  3.839   8.366   1.00 19.18 ? 295 ASP   B OD2 1 
ATOM   4673 N  N   . VAL   B 1 296 ? 30.296  8.063   5.620   1.00 17.32 ? 296 VAL   B N   1 
ATOM   4674 C  CA  . VAL   B 1 296 ? 29.612  9.343   5.511   1.00 18.56 ? 296 VAL   B CA  1 
ATOM   4675 C  C   . VAL   B 1 296 ? 28.974  9.456   4.137   1.00 20.64 ? 296 VAL   B C   1 
ATOM   4676 O  O   . VAL   B 1 296 ? 27.796  9.821   4.059   1.00 25.03 ? 296 VAL   B O   1 
ATOM   4677 C  CB  . VAL   B 1 296 ? 30.555  10.516  5.798   1.00 17.58 ? 296 VAL   B CB  1 
ATOM   4678 C  CG1 . VAL   B 1 296 ? 29.917  11.846  5.392   1.00 19.20 ? 296 VAL   B CG1 1 
ATOM   4679 C  CG2 . VAL   B 1 296 ? 30.932  10.496  7.247   1.00 17.99 ? 296 VAL   B CG2 1 
ATOM   4680 N  N   . VAL   B 1 297 ? 29.712  9.119   3.078   1.00 19.35 ? 297 VAL   B N   1 
ATOM   4681 C  CA  . VAL   B 1 297 ? 29.118  9.187   1.742   1.00 24.37 ? 297 VAL   B CA  1 
ATOM   4682 C  C   . VAL   B 1 297 ? 28.028  8.117   1.567   1.00 26.34 ? 297 VAL   B C   1 
ATOM   4683 O  O   . VAL   B 1 297 ? 27.023  8.425   0.918   1.00 28.63 ? 297 VAL   B O   1 
ATOM   4684 C  CB  . VAL   B 1 297 ? 30.146  9.167   0.592   1.00 24.68 ? 297 VAL   B CB  1 
ATOM   4685 C  CG1 . VAL   B 1 297 ? 31.165  10.283  0.769   1.00 24.77 ? 297 VAL   B CG1 1 
ATOM   4686 C  CG2 . VAL   B 1 297 ? 30.812  7.825   0.436   1.00 27.30 ? 297 VAL   B CG2 1 
ATOM   4687 N  N   . ARG   B 1 298 ? 28.213  6.908   2.125   1.00 29.37 ? 298 ARG   B N   1 
ATOM   4688 C  CA  . ARG   B 1 298 ? 27.197  5.843   2.156   1.00 33.39 ? 298 ARG   B CA  1 
ATOM   4689 C  C   . ARG   B 1 298 ? 25.876  6.462   2.662   1.00 36.14 ? 298 ARG   B C   1 
ATOM   4690 O  O   . ARG   B 1 298 ? 24.832  6.319   2.018   1.00 35.31 ? 298 ARG   B O   1 
ATOM   4691 C  CB  . ARG   B 1 298 ? 27.673  4.640   2.999   1.00 35.69 ? 298 ARG   B CB  1 
ATOM   4692 C  CG  . ARG   B 1 298 ? 27.761  3.264   2.338   1.00 41.47 ? 298 ARG   B CG  1 
ATOM   4693 C  CD  . ARG   B 1 298 ? 27.855  2.091   3.328   1.00 44.03 ? 298 ARG   B CD  1 
ATOM   4694 N  NE  . ARG   B 1 298 ? 26.607  1.362   3.603   1.00 44.35 ? 298 ARG   B NE  1 
ATOM   4695 C  CZ  . ARG   B 1 298 ? 26.377  0.522   4.624   1.00 40.32 ? 298 ARG   B CZ  1 
ATOM   4696 N  NH1 . ARG   B 1 298 ? 27.223  0.383   5.639   1.00 43.70 ? 298 ARG   B NH1 1 
ATOM   4697 N  NH2 . ARG   B 1 298 ? 25.251  -0.162  4.650   1.00 33.26 ? 298 ARG   B NH2 1 
ATOM   4698 N  N   . GLN   B 1 299 ? 25.915  7.258   3.747   1.00 31.88 ? 299 GLN   B N   1 
ATOM   4699 C  CA  . GLN   B 1 299 ? 24.695  7.684   4.429   1.00 31.85 ? 299 GLN   B CA  1 
ATOM   4700 C  C   . GLN   B 1 299 ? 24.119  9.010   3.930   1.00 35.96 ? 299 GLN   B C   1 
ATOM   4701 O  O   . GLN   B 1 299 ? 22.918  9.223   4.083   1.00 39.10 ? 299 GLN   B O   1 
ATOM   4702 C  CB  . GLN   B 1 299 ? 24.912  7.790   5.939   1.00 33.89 ? 299 GLN   B CB  1 
ATOM   4703 C  CG  . GLN   B 1 299 ? 24.706  6.441   6.626   1.00 38.34 ? 299 GLN   B CG  1 
ATOM   4704 C  CD  . GLN   B 1 299 ? 24.928  6.442   8.118   1.00 38.66 ? 299 GLN   B CD  1 
ATOM   4705 O  OE1 . GLN   B 1 299 ? 24.268  7.149   8.878   1.00 32.33 ? 299 GLN   B OE1 1 
ATOM   4706 N  NE2 . GLN   B 1 299 ? 25.832  5.579   8.554   1.00 45.35 ? 299 GLN   B NE2 1 
ATOM   4707 N  N   . CYS   B 1 300 ? 24.965  9.919   3.423   1.00 32.41 ? 300 CYS   B N   1 
ATOM   4708 C  CA  . CYS   B 1 300 ? 24.528  11.255  3.045   1.00 33.95 ? 300 CYS   B CA  1 
ATOM   4709 C  C   . CYS   B 1 300 ? 23.965  11.211  1.630   1.00 39.12 ? 300 CYS   B C   1 
ATOM   4710 O  O   . CYS   B 1 300 ? 22.928  11.832  1.351   1.00 35.13 ? 300 CYS   B O   1 
ATOM   4711 C  CB  . CYS   B 1 300 ? 25.665  12.267  3.094   1.00 36.06 ? 300 CYS   B CB  1 
ATOM   4712 S  SG  . CYS   B 1 300 ? 26.092  12.824  4.771   0.67 37.56 ? 300 CYS   B SG  1 
ATOM   4713 N  N   . SER   B 1 301 ? 24.655  10.426  0.784   1.00 35.76 ? 301 SER   B N   1 
ATOM   4714 C  CA  . SER   B 1 301 ? 24.474  10.403  -0.663  1.00 36.89 ? 301 SER   B CA  1 
ATOM   4715 C  C   . SER   B 1 301 ? 24.054  9.003   -1.127  1.00 35.04 ? 301 SER   B C   1 
ATOM   4716 O  O   . SER   B 1 301 ? 24.250  8.047   -0.362  1.00 33.52 ? 301 SER   B O   1 
ATOM   4717 C  CB  . SER   B 1 301 ? 25.756  10.845  -1.382  1.00 40.86 ? 301 SER   B CB  1 
ATOM   4718 O  OG  . SER   B 1 301 ? 26.058  12.226  -1.166  1.00 37.75 ? 301 SER   B OG  1 
ATOM   4719 O  OXT . SER   B 1 301 ? 23.622  8.893   -2.287  1.00 38.92 ? 301 SER   B OXT 1 
HETATM 4720 N  N1  . A1D80 C 2 .   ? 8.837   9.631   -1.015  0.95 12.39 ? 401 A1D80 A N1  1 
HETATM 4721 N  N3  . A1D80 C 2 .   ? 8.305   9.358   -3.291  0.95 12.83 ? 401 A1D80 A N3  1 
HETATM 4722 C  C4  . A1D80 C 2 .   ? 4.195   10.368  0.334   0.95 15.24 ? 401 A1D80 A C4  1 
HETATM 4723 C  C5  . A1D80 C 2 .   ? 4.020   9.009   0.370   0.95 17.28 ? 401 A1D80 A C5  1 
HETATM 4724 C  C6  . A1D80 C 2 .   ? 5.036   8.145   0.009   0.95 13.43 ? 401 A1D80 A C6  1 
HETATM 4725 C  C7  . A1D80 C 2 .   ? 7.758   10.631  -0.874  0.95 12.79 ? 401 A1D80 A C7  1 
HETATM 4726 C  C8  . A1D80 C 2 .   ? 9.513   9.249   0.139   0.95 12.45 ? 401 A1D80 A C8  1 
HETATM 4727 C  C10 . A1D80 C 2 .   ? 10.080  8.054   -2.328  0.95 11.83 ? 401 A1D80 A C10 1 
HETATM 4728 C  C13 . A1D80 C 2 .   ? 12.185  8.529   1.840   0.95 12.83 ? 401 A1D80 A C13 1 
HETATM 4729 C  C15 . A1D80 C 2 .   ? 8.989   9.478   -5.545  0.95 13.72 ? 401 A1D80 A C15 1 
HETATM 4730 C  C17 . A1D80 C 2 .   ? 8.872   7.483   -6.961  0.95 13.98 ? 401 A1D80 A C17 1 
HETATM 4731 C  C20 . A1D80 C 2 .   ? 9.737   9.235   -8.003  0.95 17.07 ? 401 A1D80 A C20 1 
HETATM 4732 C  C21 . A1D80 C 2 .   ? 10.203  8.051   -10.141 0.95 25.40 ? 401 A1D80 A C21 1 
HETATM 4733 C  C22 . A1D80 C 2 .   ? 11.616  7.469   -10.102 0.95 30.30 ? 401 A1D80 A C22 1 
HETATM 4734 C  C24 . A1D80 C 2 .   ? 13.612  6.612   -11.441 0.95 41.96 ? 401 A1D80 A C24 1 
HETATM 4735 C  C26 . A1D80 C 2 .   ? 13.682  9.198   3.088   0.95 11.73 ? 401 A1D80 A C26 1 
HETATM 4736 C  C1  . A1D80 C 2 .   ? 6.250   8.618   -0.414  0.95 13.44 ? 401 A1D80 A C1  1 
HETATM 4737 C  C2  . A1D80 C 2 .   ? 6.461   10.000  -0.439  0.95 12.97 ? 401 A1D80 A C2  1 
HETATM 4738 C  C3  . A1D80 C 2 .   ? 5.409   10.824  -0.137  0.95 15.60 ? 401 A1D80 A C3  1 
HETATM 4739 F  F1  . A1D80 C 2 .   ? 5.643   12.168  -0.169  0.95 18.29 ? 401 A1D80 A F1  1 
HETATM 4740 F  F2  . A1D80 C 2 .   ? 2.847   8.488   0.799   0.95 19.52 ? 401 A1D80 A F2  1 
HETATM 4741 F  F3  . A1D80 C 2 .   ? 4.818   6.814   0.078   0.95 12.44 ? 401 A1D80 A F3  1 
HETATM 4742 N  N2  . A1D80 C 2 .   ? 10.445  8.234   0.017   0.95 12.22 ? 401 A1D80 A N2  1 
HETATM 4743 C  C9  . A1D80 C 2 .   ? 10.821  7.657   -1.192  0.95 11.02 ? 401 A1D80 A C9  1 
HETATM 4744 C  C11 . A1D80 C 2 .   ? 9.062   9.002   -2.210  0.95 11.73 ? 401 A1D80 A C11 1 
HETATM 4745 O  O1  . A1D80 C 2 .   ? 9.285   9.779   1.197   0.95 11.94 ? 401 A1D80 A O1  1 
HETATM 4746 O  O2  . A1D80 C 2 .   ? 11.719  6.821   -1.194  0.95 11.97 ? 401 A1D80 A O2  1 
HETATM 4747 C  C12 . A1D80 C 2 .   ? 11.140  7.759   1.217   0.95 13.01 ? 401 A1D80 A C12 1 
HETATM 4748 C  C14 . A1D80 C 2 .   ? 8.447   8.718   -4.528  0.95 13.11 ? 401 A1D80 A C14 1 
HETATM 4749 C  C16 . A1D80 C 2 .   ? 9.218   8.850   -6.772  0.95 15.30 ? 401 A1D80 A C16 1 
HETATM 4750 C  C18 . A1D80 C 2 .   ? 8.283   6.747   -5.913  0.95 12.61 ? 401 A1D80 A C18 1 
HETATM 4751 C  C19 . A1D80 C 2 .   ? 8.114   7.375   -4.709  0.95 11.80 ? 401 A1D80 A C19 1 
HETATM 4752 CL CL1 . A1D80 C 2 .   ? 7.417   6.452   -3.408  0.95 13.70 ? 401 A1D80 A CL1 1 
HETATM 4753 N  N4  . A1D80 C 2 .   ? 9.705   8.160   -8.775  0.95 18.53 ? 401 A1D80 A N4  1 
HETATM 4754 N  N5  . A1D80 C 2 .   ? 9.182   7.039   -8.199  0.95 15.26 ? 401 A1D80 A N5  1 
HETATM 4755 C  C23 . A1D80 C 2 .   ? 12.192  7.179   -11.481 0.95 37.64 ? 401 A1D80 A C23 1 
HETATM 4756 C  C25 . A1D80 C 2 .   ? 13.797  5.294   -10.713 0.95 44.07 ? 401 A1D80 A C25 1 
HETATM 4757 N  N6  . A1D80 C 2 .   ? 12.617  9.614   1.221   0.95 11.00 ? 401 A1D80 A N6  1 
HETATM 4758 N  N7  . A1D80 C 2 .   ? 13.630  10.019  2.030   0.95 11.67 ? 401 A1D80 A N7  1 
HETATM 4759 N  N8  . A1D80 C 2 .   ? 12.761  8.257   2.996   0.95 12.22 ? 401 A1D80 A N8  1 
HETATM 4760 C  C27 . A1D80 C 2 .   ? 14.372  11.259  1.742   0.95 13.51 ? 401 A1D80 A C27 1 
HETATM 4761 N  N1  . A1D80 D 2 .   ? 37.308  -17.577 24.278  0.92 16.96 ? 401 A1D80 B N1  1 
HETATM 4762 N  N3  . A1D80 D 2 .   ? 37.191  -19.976 24.471  0.92 17.41 ? 401 A1D80 B N3  1 
HETATM 4763 C  C4  . A1D80 D 2 .   ? 42.105  -17.474 23.447  0.92 20.61 ? 401 A1D80 B C4  1 
HETATM 4764 C  C5  . A1D80 D 2 .   ? 41.852  -17.767 22.133  0.92 21.36 ? 401 A1D80 B C5  1 
HETATM 4765 C  C6  . A1D80 D 2 .   ? 40.565  -17.955 21.673  0.92 18.45 ? 401 A1D80 B C6  1 
HETATM 4766 C  C7  . A1D80 D 2 .   ? 38.637  -17.561 24.895  0.92 18.97 ? 401 A1D80 B C7  1 
HETATM 4767 C  C8  . A1D80 D 2 .   ? 36.783  -16.336 23.869  0.92 16.23 ? 401 A1D80 B C8  1 
HETATM 4768 C  C10 . A1D80 D 2 .   ? 35.358  -18.719 23.515  0.92 15.19 ? 401 A1D80 B C10 1 
HETATM 4769 C  C13 . A1D80 D 2 .   ? 34.365  -14.162 23.499  0.92 21.32 ? 401 A1D80 B C13 1 
HETATM 4770 C  C15 . A1D80 D 2 .   ? 36.047  -21.899 25.284  0.92 19.67 ? 401 A1D80 B C15 1 
HETATM 4771 C  C17 . A1D80 D 2 .   ? 35.118  -23.539 23.732  0.92 20.89 ? 401 A1D80 B C17 1 
HETATM 4772 C  C20 . A1D80 D 2 .   ? 34.686  -24.004 25.865  0.92 25.10 ? 401 A1D80 B C20 1 
HETATM 4773 C  C21 . A1D80 D 2 .   ? 33.382  -26.068 25.437  0.92 25.97 ? 401 A1D80 B C21 1 
HETATM 4774 C  C22 . A1D80 D 2 .   ? 31.950  -25.930 25.001  0.92 31.78 ? 401 A1D80 B C22 1 
HETATM 4775 C  C24 . A1D80 D 2 .   ? 29.849  -25.125 26.228  0.92 46.03 ? 401 A1D80 B C24 1 
HETATM 4776 C  C26 . A1D80 D 2 .   ? 33.409  -12.441 24.149  0.92 21.44 ? 401 A1D80 B C26 1 
HETATM 4777 C  C1  . A1D80 D 2 .   ? 39.507  -17.931 22.533  0.92 17.03 ? 401 A1D80 B C1  1 
HETATM 4778 C  C2  . A1D80 D 2 .   ? 39.733  -17.655 23.874  0.92 17.98 ? 401 A1D80 B C2  1 
HETATM 4779 C  C3  . A1D80 D 2 .   ? 41.025  -17.484 24.295  0.92 20.53 ? 401 A1D80 B C3  1 
HETATM 4780 F  F1  . A1D80 D 2 .   ? 41.205  -17.204 25.620  0.92 23.67 ? 401 A1D80 B F1  1 
HETATM 4781 F  F2  . A1D80 D 2 .   ? 42.859  -17.815 21.253  0.92 29.50 ? 401 A1D80 B F2  1 
HETATM 4782 F  F3  . A1D80 D 2 .   ? 40.385  -18.248 20.371  0.92 19.08 ? 401 A1D80 B F3  1 
HETATM 4783 N  N2  . A1D80 D 2 .   ? 35.582  -16.366 23.188  0.92 16.61 ? 401 A1D80 B N2  1 
HETATM 4784 C  C9  . A1D80 D 2 .   ? 34.801  -17.502 23.016  0.92 15.01 ? 401 A1D80 B C9  1 
HETATM 4785 C  C11 . A1D80 D 2 .   ? 36.619  -18.742 24.093  0.92 15.36 ? 401 A1D80 B C11 1 
HETATM 4786 O  O1  . A1D80 D 2 .   ? 37.410  -15.301 24.015  0.92 16.64 ? 401 A1D80 B O1  1 
HETATM 4787 O  O2  . A1D80 D 2 .   ? 33.710  -17.402 22.465  0.92 17.93 ? 401 A1D80 B O2  1 
HETATM 4788 C  C12 . A1D80 D 2 .   ? 35.097  -15.089 22.669  0.92 17.44 ? 401 A1D80 B C12 1 
HETATM 4789 C  C14 . A1D80 D 2 .   ? 36.522  -21.187 24.201  0.92 20.07 ? 401 A1D80 B C14 1 
HETATM 4790 C  C16 . A1D80 D 2 .   ? 35.323  -23.066 25.061  0.92 22.03 ? 401 A1D80 B C16 1 
HETATM 4791 C  C18 . A1D80 D 2 .   ? 35.648  -22.823 22.645  0.92 18.49 ? 401 A1D80 B C18 1 
HETATM 4792 C  C19 . A1D80 D 2 .   ? 36.338  -21.653 22.893  0.92 19.09 ? 401 A1D80 B C19 1 
HETATM 4793 CL CL1 . A1D80 D 2 .   ? 37.013  -20.775 21.555  0.92 20.17 ? 401 A1D80 B CL1 1 
HETATM 4794 N  N4  . A1D80 D 2 .   ? 34.182  -24.923 25.054  0.92 25.41 ? 401 A1D80 B N4  1 
HETATM 4795 N  N5  . A1D80 D 2 .   ? 34.403  -24.688 23.725  0.92 23.00 ? 401 A1D80 B N5  1 
HETATM 4796 C  C23 . A1D80 D 2 .   ? 31.228  -24.776 25.688  0.92 40.28 ? 401 A1D80 B C23 1 
HETATM 4797 C  C25 . A1D80 D 2 .   ? 28.872  -25.648 25.201  0.92 48.59 ? 401 A1D80 B C25 1 
HETATM 4798 N  N6  . A1D80 D 2 .   ? 33.975  -14.465 24.715  0.92 19.28 ? 401 A1D80 B N6  1 
HETATM 4799 N  N7  . A1D80 D 2 .   ? 33.341  -13.352 25.127  0.92 21.43 ? 401 A1D80 B N7  1 
HETATM 4800 N  N8  . A1D80 D 2 .   ? 34.062  -12.931 23.109  0.92 17.68 ? 401 A1D80 B N8  1 
HETATM 4801 C  C27 . A1D80 D 2 .   ? 32.804  -13.277 26.481  0.92 22.92 ? 401 A1D80 B C27 1 
HETATM 4802 O  O   . HOH   E 3 .   ? 17.629  11.392  -0.296  1.00 21.68 ? 501 HOH   A O   1 
HETATM 4803 O  O   . HOH   E 3 .   ? 21.017  7.958   5.806   1.00 34.11 ? 502 HOH   A O   1 
HETATM 4804 O  O   . HOH   E 3 .   ? 5.569   -7.793  -13.787 1.00 25.18 ? 503 HOH   A O   1 
HETATM 4805 O  O   . HOH   E 3 .   ? 14.269  13.640  -0.510  1.00 40.06 ? 504 HOH   A O   1 
HETATM 4806 O  O   . HOH   E 3 .   ? -2.162  6.762   -11.290 1.00 35.78 ? 505 HOH   A O   1 
HETATM 4807 O  O   . HOH   E 3 .   ? 21.830  8.053   8.507   1.00 40.89 ? 506 HOH   A O   1 
HETATM 4808 O  O   . HOH   E 3 .   ? 18.747  -1.978  45.192  1.00 27.10 ? 507 HOH   A O   1 
HETATM 4809 O  O   . HOH   E 3 .   ? 18.714  16.193  42.259  1.00 50.32 ? 508 HOH   A O   1 
HETATM 4810 O  O   . HOH   E 3 .   ? -9.862  11.112  -9.101  1.00 43.47 ? 509 HOH   A O   1 
HETATM 4811 O  O   . HOH   E 3 .   ? -3.527  -2.460  11.593  1.00 26.12 ? 510 HOH   A O   1 
HETATM 4812 O  O   . HOH   E 3 .   ? 3.833   4.275   29.625  1.00 32.94 ? 511 HOH   A O   1 
HETATM 4813 O  O   . HOH   E 3 .   ? 4.115   5.526   24.597  1.00 35.15 ? 512 HOH   A O   1 
HETATM 4814 O  O   . HOH   E 3 .   ? 17.635  -12.427 36.176  1.00 42.93 ? 513 HOH   A O   1 
HETATM 4815 O  O   . HOH   E 3 .   ? 14.421  -7.418  32.673  1.00 32.05 ? 514 HOH   A O   1 
HETATM 4816 O  O   . HOH   E 3 .   ? 3.451   10.688  27.615  1.00 36.24 ? 515 HOH   A O   1 
HETATM 4817 O  O   . HOH   E 3 .   ? 16.641  12.613  28.671  1.00 33.75 ? 516 HOH   A O   1 
HETATM 4818 O  O   . HOH   E 3 .   ? -14.677 8.767   -8.426  1.00 40.04 ? 517 HOH   A O   1 
HETATM 4819 O  O   . HOH   E 3 .   ? 14.017  -8.935  40.397  1.00 40.77 ? 518 HOH   A O   1 
HETATM 4820 O  O   . HOH   E 3 .   ? 16.176  -7.247  19.494  1.00 37.13 ? 519 HOH   A O   1 
HETATM 4821 O  O   . HOH   E 3 .   ? 18.687  8.106   -2.845  1.00 30.22 ? 520 HOH   A O   1 
HETATM 4822 O  O   . HOH   E 3 .   ? -6.656  9.180   -12.759 1.00 36.75 ? 521 HOH   A O   1 
HETATM 4823 O  O   . HOH   E 3 .   ? 11.675  5.541   -5.886  1.00 27.95 ? 522 HOH   A O   1 
HETATM 4824 O  O   . HOH   E 3 .   ? 4.587   15.393  -7.013  1.00 40.62 ? 523 HOH   A O   1 
HETATM 4825 O  O   . HOH   E 3 .   ? 3.832   -18.796 4.107   1.00 47.97 ? 524 HOH   A O   1 
HETATM 4826 O  O   . HOH   E 3 .   ? 2.438   6.943   22.414  1.00 24.32 ? 525 HOH   A O   1 
HETATM 4827 O  O   . HOH   E 3 .   ? 30.958  5.979   29.141  1.00 29.36 ? 526 HOH   A O   1 
HETATM 4828 O  O   . HOH   E 3 .   ? 11.939  13.725  26.645  1.00 28.91 ? 527 HOH   A O   1 
HETATM 4829 O  O   . HOH   E 3 .   ? 10.456  -6.291  38.806  1.00 29.83 ? 528 HOH   A O   1 
HETATM 4830 O  O   . HOH   E 3 .   ? 13.388  15.828  5.582   1.00 34.32 ? 529 HOH   A O   1 
HETATM 4831 O  O   . HOH   E 3 .   ? -9.516  1.298   4.289   1.00 43.49 ? 530 HOH   A O   1 
HETATM 4832 O  O   . HOH   E 3 .   ? 5.519   -20.340 2.651   1.00 36.68 ? 531 HOH   A O   1 
HETATM 4833 O  O   . HOH   E 3 .   ? 17.756  -18.395 6.903   1.00 42.92 ? 532 HOH   A O   1 
HETATM 4834 O  O   . HOH   E 3 .   ? 16.970  0.420   18.547  1.00 32.11 ? 533 HOH   A O   1 
HETATM 4835 O  O   . HOH   E 3 .   ? 17.194  11.433  4.529   1.00 26.20 ? 534 HOH   A O   1 
HETATM 4836 O  O   . HOH   E 3 .   ? 17.944  2.662   17.572  1.00 25.56 ? 535 HOH   A O   1 
HETATM 4837 O  O   . HOH   E 3 .   ? 19.604  -9.927  42.932  1.00 46.64 ? 536 HOH   A O   1 
HETATM 4838 O  O   . HOH   E 3 .   ? 9.094   8.718   46.714  1.00 30.18 ? 537 HOH   A O   1 
HETATM 4839 O  O   . HOH   E 3 .   ? 16.955  10.719  25.579  1.00 41.82 ? 538 HOH   A O   1 
HETATM 4840 O  O   . HOH   E 3 .   ? 19.485  3.921   3.860   1.00 24.45 ? 539 HOH   A O   1 
HETATM 4841 O  O   . HOH   E 3 .   ? 22.034  9.477   39.281  1.00 26.13 ? 540 HOH   A O   1 
HETATM 4842 O  O   . HOH   E 3 .   ? 4.731   11.747  29.948  1.00 34.25 ? 541 HOH   A O   1 
HETATM 4843 O  O   . HOH   E 3 .   ? -2.862  5.991   12.444  1.00 28.56 ? 542 HOH   A O   1 
HETATM 4844 O  O   . HOH   E 3 .   ? 11.158  4.587   -13.391 1.00 37.92 ? 543 HOH   A O   1 
HETATM 4845 O  O   . HOH   E 3 .   ? 9.863   -0.921  25.444  1.00 20.33 ? 544 HOH   A O   1 
HETATM 4846 O  O   . HOH   E 3 .   ? 9.120   -9.823  37.004  1.00 39.54 ? 545 HOH   A O   1 
HETATM 4847 O  O   . HOH   E 3 .   ? 11.181  12.629  18.025  1.00 41.09 ? 546 HOH   A O   1 
HETATM 4848 O  O   . HOH   E 3 .   ? 13.730  2.373   -5.074  1.00 26.31 ? 547 HOH   A O   1 
HETATM 4849 O  O   . HOH   E 3 .   ? 13.361  5.473   16.052  1.00 14.90 ? 548 HOH   A O   1 
HETATM 4850 O  O   . HOH   E 3 .   ? 28.936  -3.727  37.545  1.00 27.40 ? 549 HOH   A O   1 
HETATM 4851 O  O   . HOH   E 3 .   ? -10.716 1.114   -6.541  1.00 26.69 ? 550 HOH   A O   1 
HETATM 4852 O  O   . HOH   E 3 .   ? -0.102  -17.557 -7.896  1.00 28.29 ? 551 HOH   A O   1 
HETATM 4853 O  O   . HOH   E 3 .   ? 14.456  -15.164 2.272   1.00 20.34 ? 552 HOH   A O   1 
HETATM 4854 O  O   . HOH   E 3 .   ? 14.089  -5.678  18.347  1.00 19.72 ? 553 HOH   A O   1 
HETATM 4855 O  O   . HOH   E 3 .   ? 2.808   -1.134  30.350  1.00 23.78 ? 554 HOH   A O   1 
HETATM 4856 O  O   . HOH   E 3 .   ? 12.582  20.224  5.916   1.00 44.23 ? 555 HOH   A O   1 
HETATM 4857 O  O   . HOH   E 3 .   ? -2.126  -15.823 -2.220  1.00 43.37 ? 556 HOH   A O   1 
HETATM 4858 O  O   . HOH   E 3 .   ? 8.929   -13.395 15.114  1.00 27.64 ? 557 HOH   A O   1 
HETATM 4859 O  O   . HOH   E 3 .   ? 12.207  -11.362 18.586  1.00 47.11 ? 558 HOH   A O   1 
HETATM 4860 O  O   . HOH   E 3 .   ? 0.683   0.739   17.998  1.00 34.26 ? 559 HOH   A O   1 
HETATM 4861 O  O   . HOH   E 3 .   ? 0.932   20.628  0.248   1.00 38.40 ? 560 HOH   A O   1 
HETATM 4862 O  O   . HOH   E 3 .   ? 8.670   -20.067 -8.062  1.00 27.88 ? 561 HOH   A O   1 
HETATM 4863 O  O   . HOH   E 3 .   ? -8.395  -1.985  -10.649 1.00 30.68 ? 562 HOH   A O   1 
HETATM 4864 O  O   . HOH   E 3 .   ? 16.026  20.329  35.284  1.00 46.28 ? 563 HOH   A O   1 
HETATM 4865 O  O   . HOH   E 3 .   ? 22.365  -5.482  -2.694  1.00 43.88 ? 564 HOH   A O   1 
HETATM 4866 O  O   . HOH   E 3 .   ? 4.774   6.261   11.175  1.00 11.32 ? 565 HOH   A O   1 
HETATM 4867 O  O   . HOH   E 3 .   ? 9.898   -2.917  -11.356 1.00 18.87 ? 566 HOH   A O   1 
HETATM 4868 O  O   . HOH   E 3 .   ? 3.601   -17.750 11.031  1.00 41.54 ? 567 HOH   A O   1 
HETATM 4869 O  O   . HOH   E 3 .   ? 12.489  -6.820  40.485  1.00 42.48 ? 568 HOH   A O   1 
HETATM 4870 O  O   . HOH   E 3 .   ? -0.084  19.938  5.489   1.00 29.53 ? 569 HOH   A O   1 
HETATM 4871 O  O   . HOH   E 3 .   ? 17.402  2.185   25.819  1.00 12.18 ? 570 HOH   A O   1 
HETATM 4872 O  O   . HOH   E 3 .   ? 3.143   19.029  16.403  1.00 33.60 ? 571 HOH   A O   1 
HETATM 4873 O  O   . HOH   E 3 .   ? -7.701  13.927  -4.558  1.00 34.21 ? 572 HOH   A O   1 
HETATM 4874 O  O   . HOH   E 3 .   ? -8.151  -5.660  0.125   1.00 33.99 ? 573 HOH   A O   1 
HETATM 4875 O  O   . HOH   E 3 .   ? 18.141  -7.205  17.317  1.00 29.80 ? 574 HOH   A O   1 
HETATM 4876 O  O   . HOH   E 3 .   ? -4.421  -8.930  -4.458  1.00 29.99 ? 575 HOH   A O   1 
HETATM 4877 O  O   . HOH   E 3 .   ? 2.261   5.389   -11.416 1.00 32.06 ? 576 HOH   A O   1 
HETATM 4878 O  O   . HOH   E 3 .   ? 5.207   18.521  26.439  1.00 44.31 ? 577 HOH   A O   1 
HETATM 4879 O  O   . HOH   E 3 .   ? 13.174  -4.047  3.278   1.00 14.50 ? 578 HOH   A O   1 
HETATM 4880 O  O   . HOH   E 3 .   ? 23.808  6.836   53.588  1.00 35.14 ? 579 HOH   A O   1 
HETATM 4881 O  O   . HOH   E 3 .   ? 11.710  -19.369 8.226   1.00 22.99 ? 580 HOH   A O   1 
HETATM 4882 O  O   . HOH   E 3 .   ? 2.479   12.099  16.059  1.00 18.10 ? 581 HOH   A O   1 
HETATM 4883 O  O   . HOH   E 3 .   ? 2.741   -7.722  -14.678 1.00 30.12 ? 582 HOH   A O   1 
HETATM 4884 O  O   . HOH   E 3 .   ? 16.982  -6.713  42.691  1.00 46.21 ? 583 HOH   A O   1 
HETATM 4885 O  O   . HOH   E 3 .   ? 3.898   -3.133  29.010  1.00 34.53 ? 584 HOH   A O   1 
HETATM 4886 O  O   . HOH   E 3 .   ? 9.520   15.209  14.183  1.00 21.14 ? 585 HOH   A O   1 
HETATM 4887 O  O   . HOH   E 3 .   ? -1.778  -7.475  4.486   1.00 20.85 ? 586 HOH   A O   1 
HETATM 4888 O  O   . HOH   E 3 .   ? 1.637   -13.718 0.926   1.00 24.80 ? 587 HOH   A O   1 
HETATM 4889 O  O   . HOH   E 3 .   ? 2.089   -5.591  10.188  1.00 18.59 ? 588 HOH   A O   1 
HETATM 4890 O  O   . HOH   E 3 .   ? 17.032  20.743  38.333  1.00 44.68 ? 589 HOH   A O   1 
HETATM 4891 O  O   . HOH   E 3 .   ? -7.387  3.046   5.591   1.00 29.28 ? 590 HOH   A O   1 
HETATM 4892 O  O   . HOH   E 3 .   ? -1.029  14.206  8.654   1.00 20.90 ? 591 HOH   A O   1 
HETATM 4893 O  O   . HOH   E 3 .   ? 11.531  -9.633  31.397  1.00 36.61 ? 592 HOH   A O   1 
HETATM 4894 O  O   . HOH   E 3 .   ? 5.753   -20.912 -8.273  1.00 30.55 ? 593 HOH   A O   1 
HETATM 4895 O  O   . HOH   E 3 .   ? 16.363  10.272  43.100  1.00 25.54 ? 594 HOH   A O   1 
HETATM 4896 O  O   . HOH   E 3 .   ? 11.882  11.258  -0.878  1.00 24.45 ? 595 HOH   A O   1 
HETATM 4897 O  O   . HOH   E 3 .   ? 20.746  -9.048  -0.685  1.00 31.73 ? 596 HOH   A O   1 
HETATM 4898 O  O   . HOH   E 3 .   ? -4.564  12.775  -8.734  1.00 45.47 ? 597 HOH   A O   1 
HETATM 4899 O  O   . HOH   E 3 .   ? 12.631  10.064  -3.804  1.00 34.14 ? 598 HOH   A O   1 
HETATM 4900 O  O   . HOH   E 3 .   ? -4.000  7.594   4.211   1.00 15.61 ? 599 HOH   A O   1 
HETATM 4901 O  O   . HOH   E 3 .   ? -3.519  7.358   6.836   1.00 11.04 ? 600 HOH   A O   1 
HETATM 4902 O  O   . HOH   E 3 .   ? -6.971  -4.689  10.816  1.00 30.52 ? 601 HOH   A O   1 
HETATM 4903 O  O   . HOH   E 3 .   ? 4.762   14.168  30.051  1.00 31.39 ? 602 HOH   A O   1 
HETATM 4904 O  O   . HOH   E 3 .   ? -1.691  -19.432 -4.144  1.00 56.69 ? 603 HOH   A O   1 
HETATM 4905 O  O   . HOH   E 3 .   ? 10.750  13.276  43.517  1.00 36.14 ? 604 HOH   A O   1 
HETATM 4906 O  O   . HOH   E 3 .   ? 17.266  16.450  32.041  1.00 39.98 ? 605 HOH   A O   1 
HETATM 4907 O  O   . HOH   E 3 .   ? 4.054   7.726   46.439  1.00 36.85 ? 606 HOH   A O   1 
HETATM 4908 O  O   . HOH   E 3 .   ? 18.049  -13.772 8.548   1.00 18.99 ? 607 HOH   A O   1 
HETATM 4909 O  O   . HOH   E 3 .   ? 6.218   -20.118 -1.135  1.00 49.46 ? 608 HOH   A O   1 
HETATM 4910 O  O   . HOH   E 3 .   ? 6.629   -0.856  41.618  1.00 28.01 ? 609 HOH   A O   1 
HETATM 4911 O  O   . HOH   E 3 .   ? 6.868   8.920   -11.425 1.00 28.89 ? 610 HOH   A O   1 
HETATM 4912 O  O   . HOH   E 3 .   ? 29.336  -0.802  24.777  1.00 47.13 ? 611 HOH   A O   1 
HETATM 4913 O  O   . HOH   E 3 .   ? 24.003  -9.830  41.569  1.00 46.74 ? 612 HOH   A O   1 
HETATM 4914 O  O   . HOH   E 3 .   ? 0.173   -12.568 10.009  1.00 23.76 ? 613 HOH   A O   1 
HETATM 4915 O  O   . HOH   E 3 .   ? 22.893  10.239  42.020  1.00 45.32 ? 614 HOH   A O   1 
HETATM 4916 O  O   . HOH   E 3 .   ? 4.795   11.564  22.675  1.00 35.09 ? 615 HOH   A O   1 
HETATM 4917 O  O   . HOH   E 3 .   ? -4.769  14.891  -7.535  1.00 35.66 ? 616 HOH   A O   1 
HETATM 4918 O  O   . HOH   E 3 .   ? 6.153   -19.229 4.854   1.00 37.21 ? 617 HOH   A O   1 
HETATM 4919 O  O   . HOH   E 3 .   ? 16.007  14.457  2.892   1.00 26.63 ? 618 HOH   A O   1 
HETATM 4920 O  O   . HOH   E 3 .   ? -1.052  4.988   15.411  1.00 17.60 ? 619 HOH   A O   1 
HETATM 4921 O  O   . HOH   E 3 .   ? 24.701  17.901  32.421  1.00 54.12 ? 620 HOH   A O   1 
HETATM 4922 O  O   . HOH   E 3 .   ? 0.555   18.521  -2.005  1.00 41.31 ? 621 HOH   A O   1 
HETATM 4923 O  O   . HOH   E 3 .   ? -7.376  -4.467  7.127   1.00 24.73 ? 622 HOH   A O   1 
HETATM 4924 O  O   . HOH   E 3 .   ? 32.251  8.276   23.710  1.00 38.09 ? 623 HOH   A O   1 
HETATM 4925 O  O   . HOH   E 3 .   ? 6.104   11.126  -3.554  1.00 19.67 ? 624 HOH   A O   1 
HETATM 4926 O  O   . HOH   E 3 .   ? 8.010   -7.204  14.793  1.00 15.77 ? 625 HOH   A O   1 
HETATM 4927 O  O   . HOH   E 3 .   ? 18.585  -14.337 1.338   1.00 47.83 ? 626 HOH   A O   1 
HETATM 4928 O  O   . HOH   E 3 .   ? 2.717   8.792   24.476  1.00 41.37 ? 627 HOH   A O   1 
HETATM 4929 O  O   . HOH   E 3 .   ? 4.417   10.170  31.769  1.00 38.02 ? 628 HOH   A O   1 
HETATM 4930 O  O   . HOH   E 3 .   ? -1.243  2.419   16.941  1.00 28.04 ? 629 HOH   A O   1 
HETATM 4931 O  O   . HOH   E 3 .   ? -9.826  6.614   -2.216  1.00 22.29 ? 630 HOH   A O   1 
HETATM 4932 O  O   . HOH   E 3 .   ? 7.357   16.592  13.110  1.00 25.92 ? 631 HOH   A O   1 
HETATM 4933 O  O   . HOH   E 3 .   ? 9.848   2.674   47.297  1.00 38.67 ? 632 HOH   A O   1 
HETATM 4934 O  O   . HOH   E 3 .   ? 4.783   -0.488  -15.263 1.00 37.34 ? 633 HOH   A O   1 
HETATM 4935 O  O   . HOH   E 3 .   ? 17.550  -2.333  19.901  1.00 25.90 ? 634 HOH   A O   1 
HETATM 4936 O  O   . HOH   E 3 .   ? 26.069  9.959   40.484  1.00 43.68 ? 635 HOH   A O   1 
HETATM 4937 O  O   . HOH   E 3 .   ? 5.585   15.350  4.921   1.00 24.14 ? 636 HOH   A O   1 
HETATM 4938 O  O   . HOH   E 3 .   ? 11.954  15.665  43.115  1.00 31.09 ? 637 HOH   A O   1 
HETATM 4939 O  O   . HOH   E 3 .   ? 9.606   12.684  15.793  1.00 21.14 ? 638 HOH   A O   1 
HETATM 4940 O  O   . HOH   E 3 .   ? -5.605  3.211   7.354   1.00 31.64 ? 639 HOH   A O   1 
HETATM 4941 O  O   . HOH   E 3 .   ? 1.340   9.678   20.266  1.00 25.84 ? 640 HOH   A O   1 
HETATM 4942 O  O   . HOH   E 3 .   ? 1.075   0.762   36.817  1.00 30.55 ? 641 HOH   A O   1 
HETATM 4943 O  O   . HOH   E 3 .   ? 15.574  10.230  11.308  1.00 22.85 ? 642 HOH   A O   1 
HETATM 4944 O  O   . HOH   E 3 .   ? -0.451  -7.333  15.831  1.00 23.58 ? 643 HOH   A O   1 
HETATM 4945 O  O   . HOH   E 3 .   ? 27.289  -9.737  29.610  1.00 37.15 ? 644 HOH   A O   1 
HETATM 4946 O  O   . HOH   E 3 .   ? 7.667   17.266  10.245  1.00 21.11 ? 645 HOH   A O   1 
HETATM 4947 O  O   . HOH   E 3 .   ? 9.076   16.051  4.149   1.00 50.67 ? 646 HOH   A O   1 
HETATM 4948 O  O   . HOH   E 3 .   ? -6.264  5.952   3.669   1.00 18.08 ? 647 HOH   A O   1 
HETATM 4949 O  O   . HOH   E 3 .   ? 1.349   4.563   0.076   1.00 11.98 ? 648 HOH   A O   1 
HETATM 4950 O  O   . HOH   E 3 .   ? -5.358  -12.967 -14.029 1.00 42.40 ? 649 HOH   A O   1 
HETATM 4951 O  O   . HOH   E 3 .   ? 25.019  3.278   24.533  1.00 28.93 ? 650 HOH   A O   1 
HETATM 4952 O  O   . HOH   E 3 .   ? -7.317  -8.317  -9.523  1.00 27.31 ? 651 HOH   A O   1 
HETATM 4953 O  O   . HOH   E 3 .   ? 15.513  -16.061 17.955  1.00 45.84 ? 652 HOH   A O   1 
HETATM 4954 O  O   . HOH   E 3 .   ? 3.254   20.844  1.705   1.00 34.39 ? 653 HOH   A O   1 
HETATM 4955 O  O   . HOH   E 3 .   ? 15.510  9.635   22.382  1.00 29.57 ? 654 HOH   A O   1 
HETATM 4956 O  O   . HOH   E 3 .   ? 1.678   17.009  20.219  1.00 45.46 ? 655 HOH   A O   1 
HETATM 4957 O  O   . HOH   E 3 .   ? 26.504  10.670  22.618  1.00 30.55 ? 656 HOH   A O   1 
HETATM 4958 O  O   . HOH   E 3 .   ? -6.055  11.404  -7.622  1.00 29.04 ? 657 HOH   A O   1 
HETATM 4959 O  O   . HOH   E 3 .   ? 20.294  -5.921  21.699  1.00 27.14 ? 658 HOH   A O   1 
HETATM 4960 O  O   . HOH   E 3 .   ? -5.056  -8.529  7.169   1.00 29.90 ? 659 HOH   A O   1 
HETATM 4961 O  O   . HOH   E 3 .   ? 1.208   -15.624 9.024   1.00 47.54 ? 660 HOH   A O   1 
HETATM 4962 O  O   . HOH   E 3 .   ? 12.522  -6.046  21.810  1.00 23.08 ? 661 HOH   A O   1 
HETATM 4963 O  O   . HOH   E 3 .   ? 4.661   10.097  -13.009 1.00 36.43 ? 662 HOH   A O   1 
HETATM 4964 O  O   . HOH   E 3 .   ? 17.789  7.427   22.142  1.00 33.39 ? 663 HOH   A O   1 
HETATM 4965 O  O   . HOH   E 3 .   ? -3.680  4.844   8.156   1.00 12.69 ? 664 HOH   A O   1 
HETATM 4966 O  O   . HOH   E 3 .   ? 12.820  18.531  38.805  1.00 33.13 ? 665 HOH   A O   1 
HETATM 4967 O  O   . HOH   E 3 .   ? 31.231  4.375   35.941  1.00 33.37 ? 666 HOH   A O   1 
HETATM 4968 O  O   . HOH   E 3 .   ? 11.753  -1.931  42.953  1.00 22.78 ? 667 HOH   A O   1 
HETATM 4969 O  O   . HOH   E 3 .   ? 17.456  -15.591 10.573  1.00 34.37 ? 668 HOH   A O   1 
HETATM 4970 O  O   . HOH   E 3 .   ? 23.982  -9.916  2.020   1.00 14.39 ? 669 HOH   A O   1 
HETATM 4971 O  O   . HOH   E 3 .   ? -8.836  -3.311  -3.707  1.00 23.98 ? 670 HOH   A O   1 
HETATM 4972 O  O   . HOH   E 3 .   ? 16.250  -14.397 16.421  1.00 40.92 ? 671 HOH   A O   1 
HETATM 4973 O  O   . HOH   E 3 .   ? -4.057  9.405   9.743   1.00 17.10 ? 672 HOH   A O   1 
HETATM 4974 O  O   . HOH   E 3 .   ? 2.471   5.878   39.130  1.00 35.16 ? 673 HOH   A O   1 
HETATM 4975 O  O   . HOH   E 3 .   ? 6.546   20.048  28.963  1.00 46.13 ? 674 HOH   A O   1 
HETATM 4976 O  O   . HOH   E 3 .   ? -2.261  -11.673 0.703   1.00 29.33 ? 675 HOH   A O   1 
HETATM 4977 O  O   . HOH   E 3 .   ? 21.195  2.005   3.507   1.00 35.58 ? 676 HOH   A O   1 
HETATM 4978 O  O   . HOH   E 3 .   ? 10.650  -4.988  20.323  1.00 30.29 ? 677 HOH   A O   1 
HETATM 4979 O  O   . HOH   E 3 .   ? 5.225   -0.404  26.623  1.00 34.24 ? 678 HOH   A O   1 
HETATM 4980 O  O   . HOH   E 3 .   ? 19.794  12.848  27.592  1.00 29.41 ? 679 HOH   A O   1 
HETATM 4981 O  O   . HOH   E 3 .   ? -8.628  -0.632  1.468   1.00 25.10 ? 680 HOH   A O   1 
HETATM 4982 O  O   . HOH   E 3 .   ? 15.187  -7.631  -6.502  1.00 34.03 ? 681 HOH   A O   1 
HETATM 4983 O  O   . HOH   E 3 .   ? 21.307  5.890   4.493   1.00 31.54 ? 682 HOH   A O   1 
HETATM 4984 O  O   . HOH   E 3 .   ? 12.919  -4.472  42.021  1.00 25.93 ? 683 HOH   A O   1 
HETATM 4985 O  O   . HOH   E 3 .   ? 3.884   4.423   44.214  1.00 23.70 ? 684 HOH   A O   1 
HETATM 4986 O  O   . HOH   E 3 .   ? 5.875   2.447   44.775  1.00 20.07 ? 685 HOH   A O   1 
HETATM 4987 O  O   . HOH   E 3 .   ? 11.683  1.151   -13.126 1.00 42.92 ? 686 HOH   A O   1 
HETATM 4988 O  O   . HOH   E 3 .   ? 14.957  -6.301  -8.344  1.00 39.43 ? 687 HOH   A O   1 
HETATM 4989 O  O   . HOH   E 3 .   ? 8.105   3.748   29.665  1.00 13.91 ? 688 HOH   A O   1 
HETATM 4990 O  O   . HOH   E 3 .   ? 4.724   13.648  2.810   1.00 32.84 ? 689 HOH   A O   1 
HETATM 4991 O  O   . HOH   E 3 .   ? 21.823  -1.053  14.454  1.00 21.13 ? 690 HOH   A O   1 
HETATM 4992 O  O   . HOH   E 3 .   ? 17.649  9.663   6.845   1.00 26.89 ? 691 HOH   A O   1 
HETATM 4993 O  O   . HOH   E 3 .   ? -3.925  3.328   12.173  1.00 32.37 ? 692 HOH   A O   1 
HETATM 4994 O  O   . HOH   E 3 .   ? 13.591  -15.613 -4.787  1.00 32.04 ? 693 HOH   A O   1 
HETATM 4995 O  O   . HOH   E 3 .   ? 18.327  6.631   19.712  1.00 38.38 ? 694 HOH   A O   1 
HETATM 4996 O  O   . HOH   E 3 .   ? 25.006  -2.890  0.519   1.00 42.42 ? 695 HOH   A O   1 
HETATM 4997 O  O   . HOH   E 3 .   ? 0.878   -2.191  34.276  1.00 29.91 ? 696 HOH   A O   1 
HETATM 4998 O  O   . HOH   E 3 .   ? 4.122   7.109   -13.493 1.00 37.13 ? 697 HOH   A O   1 
HETATM 4999 O  O   . HOH   E 3 .   ? 7.852   13.498  -2.671  1.00 40.34 ? 698 HOH   A O   1 
HETATM 5000 O  O   . HOH   E 3 .   ? 12.520  1.136   -7.032  1.00 36.34 ? 699 HOH   A O   1 
HETATM 5001 O  O   . HOH   E 3 .   ? 4.386   -18.362 7.436   1.00 23.33 ? 700 HOH   A O   1 
HETATM 5002 O  O   . HOH   E 3 .   ? 21.009  -0.854  -2.889  1.00 32.33 ? 701 HOH   A O   1 
HETATM 5003 O  O   . HOH   E 3 .   ? 8.074   16.812  -6.366  1.00 41.91 ? 702 HOH   A O   1 
HETATM 5004 O  O   . HOH   E 3 .   ? 14.153  4.333   -6.682  1.00 43.00 ? 703 HOH   A O   1 
HETATM 5005 O  O   . HOH   E 3 .   ? 19.853  -3.810  19.983  1.00 19.65 ? 704 HOH   A O   1 
HETATM 5006 O  O   . HOH   E 3 .   ? -0.218  -12.435 4.658   1.00 36.25 ? 705 HOH   A O   1 
HETATM 5007 O  O   . HOH   E 3 .   ? -4.032  -6.692  -17.392 1.00 29.19 ? 706 HOH   A O   1 
HETATM 5008 O  O   . HOH   E 3 .   ? 24.901  -4.058  43.053  1.00 37.99 ? 707 HOH   A O   1 
HETATM 5009 O  O   . HOH   E 3 .   ? 32.177  9.305   32.317  1.00 45.93 ? 708 HOH   A O   1 
HETATM 5010 O  O   . HOH   E 3 .   ? -6.780  17.245  2.736   1.00 28.97 ? 709 HOH   A O   1 
HETATM 5011 O  O   . HOH   E 3 .   ? -6.786  -6.037  -14.202 1.00 34.36 ? 710 HOH   A O   1 
HETATM 5012 O  O   . HOH   E 3 .   ? 1.997   4.484   35.497  1.00 42.32 ? 711 HOH   A O   1 
HETATM 5013 O  O   . HOH   E 3 .   ? 14.328  9.941   44.587  1.00 32.11 ? 712 HOH   A O   1 
HETATM 5014 O  O   . HOH   E 3 .   ? -7.457  -8.409  3.365   1.00 29.04 ? 713 HOH   A O   1 
HETATM 5015 O  O   . HOH   E 3 .   ? 12.567  -8.859  19.301  1.00 40.52 ? 714 HOH   A O   1 
HETATM 5016 O  O   . HOH   E 3 .   ? 10.992  -5.813  26.411  1.00 21.28 ? 715 HOH   A O   1 
HETATM 5017 O  O   . HOH   E 3 .   ? 25.654  0.970   17.705  1.00 37.90 ? 716 HOH   A O   1 
HETATM 5018 O  O   . HOH   E 3 .   ? 16.533  4.675   -5.766  1.00 44.61 ? 717 HOH   A O   1 
HETATM 5019 O  O   . HOH   E 3 .   ? 6.560   4.237   24.658  1.00 30.65 ? 718 HOH   A O   1 
HETATM 5020 O  O   . HOH   E 3 .   ? -1.394  19.400  -3.114  1.00 43.00 ? 719 HOH   A O   1 
HETATM 5021 O  O   . HOH   E 3 .   ? 19.329  14.919  31.657  1.00 45.43 ? 720 HOH   A O   1 
HETATM 5022 O  O   . HOH   E 3 .   ? 7.630   -4.517  42.071  1.00 34.07 ? 721 HOH   A O   1 
HETATM 5023 O  O   . HOH   E 3 .   ? 20.939  0.215   44.794  1.00 49.11 ? 722 HOH   A O   1 
HETATM 5024 O  O   . HOH   E 3 .   ? 2.977   -6.229  -18.244 1.00 41.40 ? 723 HOH   A O   1 
HETATM 5025 O  O   . HOH   E 3 .   ? -12.144 3.731   0.666   1.00 33.52 ? 724 HOH   A O   1 
HETATM 5026 O  O   . HOH   E 3 .   ? -8.386  -4.330  -13.156 1.00 39.44 ? 725 HOH   A O   1 
HETATM 5027 O  O   . HOH   E 3 .   ? 16.830  -16.265 2.320   1.00 34.93 ? 726 HOH   A O   1 
HETATM 5028 O  O   . HOH   E 3 .   ? 8.921   15.971  18.319  1.00 37.42 ? 727 HOH   A O   1 
HETATM 5029 O  O   . HOH   E 3 .   ? -1.741  -10.857 10.827  1.00 45.31 ? 728 HOH   A O   1 
HETATM 5030 O  O   . HOH   E 3 .   ? 15.231  17.094  6.969   1.00 44.23 ? 729 HOH   A O   1 
HETATM 5031 O  O   . HOH   E 3 .   ? -13.588 11.275  -11.190 1.00 54.81 ? 730 HOH   A O   1 
HETATM 5032 O  O   . HOH   E 3 .   ? 23.590  -3.636  -3.161  1.00 40.07 ? 731 HOH   A O   1 
HETATM 5033 O  O   . HOH   E 3 .   ? -5.609  3.610   4.038   1.00 40.00 ? 732 HOH   A O   1 
HETATM 5034 O  O   . HOH   E 3 .   ? 7.486   0.723   25.918  1.00 30.11 ? 733 HOH   A O   1 
HETATM 5035 O  O   . HOH   E 3 .   ? 3.994   8.970   34.145  1.00 33.13 ? 734 HOH   A O   1 
HETATM 5036 O  O   . HOH   E 3 .   ? -4.236  -0.086  16.418  1.00 42.69 ? 735 HOH   A O   1 
HETATM 5037 O  O   . HOH   E 3 .   ? 6.169   15.518  1.923   1.00 43.82 ? 736 HOH   A O   1 
HETATM 5038 O  O   . HOH   E 3 .   ? 19.722  -15.734 3.814   1.00 50.46 ? 737 HOH   A O   1 
HETATM 5039 O  O   . HOH   E 3 .   ? 6.453   -2.967  27.609  1.00 38.00 ? 738 HOH   A O   1 
HETATM 5040 O  O   . HOH   E 3 .   ? -9.948  -1.326  -8.394  1.00 32.02 ? 739 HOH   A O   1 
HETATM 5041 O  O   . HOH   E 3 .   ? -6.508  -9.435  5.356   1.00 35.93 ? 740 HOH   A O   1 
HETATM 5042 O  O   . HOH   E 3 .   ? -8.429  -3.465  -6.788  1.00 45.28 ? 741 HOH   A O   1 
HETATM 5043 O  O   . HOH   E 3 .   ? 12.568  8.081   -5.515  1.00 31.85 ? 742 HOH   A O   1 
HETATM 5044 O  O   . HOH   E 3 .   ? 18.577  -13.603 -1.139  1.00 45.25 ? 743 HOH   A O   1 
HETATM 5045 O  O   . HOH   E 3 .   ? 2.186   3.791   41.853  1.00 43.14 ? 744 HOH   A O   1 
HETATM 5046 O  O   . HOH   E 3 .   ? 10.994  20.713  33.228  1.00 47.75 ? 745 HOH   A O   1 
HETATM 5047 O  O   . HOH   E 3 .   ? 2.321   -19.688 -2.669  1.00 42.60 ? 746 HOH   A O   1 
HETATM 5048 O  O   . HOH   E 3 .   ? -0.366  -6.131  11.301  1.00 29.16 ? 747 HOH   A O   1 
HETATM 5049 O  O   . HOH   E 3 .   ? 0.444   -1.796  31.473  1.00 37.88 ? 748 HOH   A O   1 
HETATM 5050 O  O   . HOH   E 3 .   ? 1.628   -17.121 7.008   1.00 49.58 ? 749 HOH   A O   1 
HETATM 5051 O  O   . HOH   E 3 .   ? 6.899   3.073   27.372  1.00 22.94 ? 750 HOH   A O   1 
HETATM 5052 O  O   . HOH   E 3 .   ? 7.763   -21.874 -0.631  1.00 51.57 ? 751 HOH   A O   1 
HETATM 5053 O  O   . HOH   E 3 .   ? 15.038  7.311   -6.194  1.00 38.22 ? 752 HOH   A O   1 
HETATM 5054 O  O   . HOH   E 3 .   ? 2.321   1.186   28.907  1.00 35.96 ? 753 HOH   A O   1 
HETATM 5055 O  O   . HOH   E 3 .   ? 7.285   -8.910  16.775  1.00 30.33 ? 754 HOH   A O   1 
HETATM 5056 O  O   . HOH   E 3 .   ? 10.837  -8.465  27.771  1.00 36.39 ? 755 HOH   A O   1 
HETATM 5057 O  O   . HOH   E 3 .   ? -4.409  6.617   10.413  1.00 30.19 ? 756 HOH   A O   1 
HETATM 5058 O  O   . HOH   E 3 .   ? 1.012   5.968   -13.313 1.00 59.91 ? 757 HOH   A O   1 
HETATM 5059 O  O   . HOH   E 3 .   ? -3.585  6.270   14.537  1.00 39.83 ? 758 HOH   A O   1 
HETATM 5060 O  O   . HOH   E 3 .   ? 1.803   -19.966 -6.988  1.00 35.87 ? 759 HOH   A O   1 
HETATM 5061 O  O   . HOH   E 3 .   ? 5.093   0.201   43.479  1.00 30.21 ? 760 HOH   A O   1 
HETATM 5062 O  O   . HOH   E 3 .   ? 8.274   21.661  33.783  1.00 46.41 ? 761 HOH   A O   1 
HETATM 5063 O  O   . HOH   E 3 .   ? -6.901  19.969  -0.243  1.00 42.89 ? 762 HOH   A O   1 
HETATM 5064 O  O   . HOH   E 3 .   ? -2.207  -9.900  4.686   1.00 34.23 ? 763 HOH   A O   1 
HETATM 5065 O  O   . HOH   E 3 .   ? 23.992  11.140  38.974  1.00 41.86 ? 764 HOH   A O   1 
HETATM 5066 O  O   . HOH   E 3 .   ? 5.699   20.578  8.607   1.00 38.38 ? 765 HOH   A O   1 
HETATM 5067 O  O   . HOH   E 3 .   ? 8.366   14.335  -0.523  1.00 33.32 ? 766 HOH   A O   1 
HETATM 5068 O  O   . HOH   E 3 .   ? 13.809  -5.651  44.110  1.00 39.66 ? 767 HOH   A O   1 
HETATM 5069 O  O   . HOH   E 3 .   ? -2.112  -18.885 -9.068  1.00 41.84 ? 768 HOH   A O   1 
HETATM 5070 O  O   . HOH   E 3 .   ? 6.629   -21.574 5.739   1.00 44.08 ? 769 HOH   A O   1 
HETATM 5071 O  O   . HOH   E 3 .   ? 13.749  -19.138 6.104   1.00 36.13 ? 770 HOH   A O   1 
HETATM 5072 O  O   . HOH   E 3 .   ? 9.796   21.358  9.927   1.00 42.24 ? 771 HOH   A O   1 
HETATM 5073 O  O   . HOH   E 3 .   ? 17.913  12.718  2.093   1.00 24.66 ? 772 HOH   A O   1 
HETATM 5074 O  O   . HOH   E 3 .   ? -4.380  21.339  2.826   1.00 34.26 ? 773 HOH   A O   1 
HETATM 5075 O  O   . HOH   E 3 .   ? -3.864  -10.852 -1.779  1.00 34.32 ? 774 HOH   A O   1 
HETATM 5076 O  O   . HOH   E 3 .   ? 7.606   19.919  10.434  1.00 27.81 ? 775 HOH   A O   1 
HETATM 5077 O  O   . HOH   E 3 .   ? 1.267   4.755   30.521  1.00 42.44 ? 776 HOH   A O   1 
HETATM 5078 O  O   . HOH   E 3 .   ? -2.043  22.554  2.481   1.00 34.90 ? 777 HOH   A O   1 
HETATM 5079 O  O   . HOH   E 3 .   ? 2.701   0.999   42.996  1.00 40.34 ? 778 HOH   A O   1 
HETATM 5080 O  O   . HOH   E 3 .   ? 15.920  15.088  29.962  1.00 47.90 ? 779 HOH   A O   1 
HETATM 5081 O  O   . HOH   E 3 .   ? 7.097   2.102   46.901  1.00 39.04 ? 780 HOH   A O   1 
HETATM 5082 O  O   . HOH   E 3 .   ? 2.799   21.148  14.730  1.00 32.21 ? 781 HOH   A O   1 
HETATM 5083 O  O   . HOH   E 3 .   ? 9.076   -3.231  27.427  1.00 39.67 ? 782 HOH   A O   1 
HETATM 5084 O  O   . HOH   E 3 .   ? 8.713   -2.363  42.760  1.00 27.71 ? 783 HOH   A O   1 
HETATM 5085 O  O   . HOH   E 3 .   ? -0.009  5.680   22.568  1.00 36.79 ? 784 HOH   A O   1 
HETATM 5086 O  O   . HOH   E 3 .   ? 11.814  -1.790  45.837  1.00 41.99 ? 785 HOH   A O   1 
HETATM 5087 O  O   . HOH   E 3 .   ? 7.065   20.192  13.310  1.00 37.41 ? 786 HOH   A O   1 
HETATM 5088 O  O   . HOH   E 3 .   ? 0.157   4.457   32.642  1.00 42.13 ? 787 HOH   A O   1 
HETATM 5089 O  O   . HOH   E 3 .   ? 7.217   22.137  6.715   1.00 36.82 ? 788 HOH   A O   1 
HETATM 5090 O  O   . HOH   F 3 .   ? 47.360  -11.318 6.345   1.00 30.16 ? 501 HOH   B O   1 
HETATM 5091 O  O   . HOH   F 3 .   ? 47.189  -26.172 31.107  1.00 36.77 ? 502 HOH   B O   1 
HETATM 5092 O  O   . HOH   F 3 .   ? 45.494  -32.880 19.311  1.00 37.41 ? 503 HOH   B O   1 
HETATM 5093 O  O   . HOH   F 3 .   ? 39.278  32.310  10.707  1.00 37.25 ? 504 HOH   B O   1 
HETATM 5094 O  O   . HOH   F 3 .   ? 30.804  2.178   15.723  1.00 30.42 ? 505 HOH   B O   1 
HETATM 5095 O  O   . HOH   F 3 .   ? 48.140  7.866   -1.024  1.00 21.94 ? 506 HOH   B O   1 
HETATM 5096 O  O   . HOH   F 3 .   ? 30.100  21.924  24.033  1.00 50.25 ? 507 HOH   B O   1 
HETATM 5097 O  O   . HOH   F 3 .   ? 41.182  19.094  23.469  1.00 36.79 ? 508 HOH   B O   1 
HETATM 5098 O  O   . HOH   F 3 .   ? 36.071  26.001  19.662  1.00 42.89 ? 509 HOH   B O   1 
HETATM 5099 O  O   . HOH   F 3 .   ? 38.182  14.302  20.793  1.00 35.09 ? 510 HOH   B O   1 
HETATM 5100 O  O   . HOH   F 3 .   ? 20.343  2.209   14.980  1.00 26.98 ? 511 HOH   B O   1 
HETATM 5101 O  O   . HOH   F 3 .   ? 20.811  -16.807 9.330   1.00 36.19 ? 512 HOH   B O   1 
HETATM 5102 O  O   . HOH   F 3 .   ? 29.749  1.219   5.419   1.00 35.47 ? 513 HOH   B O   1 
HETATM 5103 O  O   . HOH   F 3 .   ? 26.416  -11.164 20.588  1.00 28.39 ? 514 HOH   B O   1 
HETATM 5104 O  O   . HOH   F 3 .   ? 47.449  12.704  -2.441  1.00 29.70 ? 515 HOH   B O   1 
HETATM 5105 O  O   . HOH   F 3 .   ? 47.725  6.854   11.886  1.00 31.95 ? 516 HOH   B O   1 
HETATM 5106 O  O   . HOH   F 3 .   ? 56.663  20.931  10.279  1.00 33.94 ? 517 HOH   B O   1 
HETATM 5107 O  O   . HOH   F 3 .   ? 29.631  -34.294 3.643   1.00 23.51 ? 518 HOH   B O   1 
HETATM 5108 O  O   . HOH   F 3 .   ? 29.717  -21.302 19.428  1.00 21.01 ? 519 HOH   B O   1 
HETATM 5109 O  O   . HOH   F 3 .   ? 34.201  -6.300  -1.460  1.00 26.33 ? 520 HOH   B O   1 
HETATM 5110 O  O   . HOH   F 3 .   ? 35.454  -0.499  17.821  1.00 18.68 ? 521 HOH   B O   1 
HETATM 5111 O  O   . HOH   F 3 .   ? 32.228  -23.518 -5.235  1.00 24.74 ? 522 HOH   B O   1 
HETATM 5112 O  O   . HOH   F 3 .   ? 29.975  15.919  17.412  1.00 40.94 ? 523 HOH   B O   1 
HETATM 5113 O  O   . HOH   F 3 .   ? 47.212  -24.482 4.314   1.00 39.04 ? 524 HOH   B O   1 
HETATM 5114 O  O   . HOH   F 3 .   ? 32.707  -34.517 -3.107  1.00 37.53 ? 525 HOH   B O   1 
HETATM 5115 O  O   . HOH   F 3 .   ? 36.479  -26.366 27.570  1.00 36.49 ? 526 HOH   B O   1 
HETATM 5116 O  O   . HOH   F 3 .   ? 50.251  -10.619 17.036  1.00 39.93 ? 527 HOH   B O   1 
HETATM 5117 O  O   . HOH   F 3 .   ? 35.007  21.206  -4.887  1.00 28.54 ? 528 HOH   B O   1 
HETATM 5118 O  O   . HOH   F 3 .   ? 44.571  4.310   10.606  1.00 30.96 ? 529 HOH   B O   1 
HETATM 5119 O  O   . HOH   F 3 .   ? 48.141  1.605   0.927   1.00 26.16 ? 530 HOH   B O   1 
HETATM 5120 O  O   . HOH   F 3 .   ? 47.599  -33.615 11.330  1.00 24.73 ? 531 HOH   B O   1 
HETATM 5121 O  O   . HOH   F 3 .   ? 36.172  25.773  -2.302  1.00 33.10 ? 532 HOH   B O   1 
HETATM 5122 O  O   . HOH   F 3 .   ? 30.964  2.226   12.966  1.00 33.68 ? 533 HOH   B O   1 
HETATM 5123 O  O   . HOH   F 3 .   ? 39.322  25.089  1.341   1.00 27.61 ? 534 HOH   B O   1 
HETATM 5124 O  O   . HOH   F 3 .   ? 32.162  -0.344  6.703   1.00 19.78 ? 535 HOH   B O   1 
HETATM 5125 O  O   . HOH   F 3 .   ? 26.984  -17.155 25.592  1.00 32.22 ? 536 HOH   B O   1 
HETATM 5126 O  O   . HOH   F 3 .   ? 43.697  -31.706 21.094  1.00 35.21 ? 537 HOH   B O   1 
HETATM 5127 O  O   . HOH   F 3 .   ? 49.509  7.272   17.862  1.00 33.86 ? 538 HOH   B O   1 
HETATM 5128 O  O   . HOH   F 3 .   ? 49.849  14.996  1.799   1.00 30.54 ? 539 HOH   B O   1 
HETATM 5129 O  O   . HOH   F 3 .   ? 37.753  -4.944  0.146   1.00 42.01 ? 540 HOH   B O   1 
HETATM 5130 O  O   . HOH   F 3 .   ? 23.038  -8.819  -4.914  1.00 52.97 ? 541 HOH   B O   1 
HETATM 5131 O  O   . HOH   F 3 .   ? 29.981  -14.493 11.516  1.00 14.94 ? 542 HOH   B O   1 
HETATM 5132 O  O   . HOH   F 3 .   ? 23.350  -19.572 8.857   1.00 43.39 ? 543 HOH   B O   1 
HETATM 5133 O  O   . HOH   F 3 .   ? 32.213  -20.015 -5.725  1.00 28.59 ? 544 HOH   B O   1 
HETATM 5134 O  O   . HOH   F 3 .   ? 36.130  -34.481 17.876  1.00 24.72 ? 545 HOH   B O   1 
HETATM 5135 O  O   . HOH   F 3 .   ? 26.583  -9.478  22.709  1.00 26.92 ? 546 HOH   B O   1 
HETATM 5136 O  O   . HOH   F 3 .   ? 40.437  27.604  6.319   1.00 24.38 ? 547 HOH   B O   1 
HETATM 5137 O  O   . HOH   F 3 .   ? 42.812  -7.854  17.228  1.00 16.54 ? 548 HOH   B O   1 
HETATM 5138 O  O   . HOH   F 3 .   ? 25.490  -16.982 1.431   1.00 17.59 ? 549 HOH   B O   1 
HETATM 5139 O  O   . HOH   F 3 .   ? 38.555  25.839  8.023   1.00 36.88 ? 550 HOH   B O   1 
HETATM 5140 O  O   . HOH   F 3 .   ? 55.374  21.898  8.421   1.00 32.57 ? 551 HOH   B O   1 
HETATM 5141 O  O   . HOH   F 3 .   ? 20.063  -28.625 10.212  1.00 33.49 ? 552 HOH   B O   1 
HETATM 5142 O  O   . HOH   F 3 .   ? 35.749  11.381  1.351   1.00 21.20 ? 553 HOH   B O   1 
HETATM 5143 O  O   . HOH   F 3 .   ? 21.946  -27.355 7.010   1.00 34.10 ? 554 HOH   B O   1 
HETATM 5144 O  O   . HOH   F 3 .   ? 36.759  -37.482 7.591   1.00 37.94 ? 555 HOH   B O   1 
HETATM 5145 O  O   . HOH   F 3 .   ? 22.992  1.398   14.755  1.00 33.51 ? 556 HOH   B O   1 
HETATM 5146 O  O   . HOH   F 3 .   ? 41.359  11.457  -3.303  1.00 31.07 ? 557 HOH   B O   1 
HETATM 5147 O  O   . HOH   F 3 .   ? 32.793  -21.882 27.662  1.00 41.49 ? 558 HOH   B O   1 
HETATM 5148 O  O   . HOH   F 3 .   ? 35.077  14.344  21.563  1.00 31.40 ? 559 HOH   B O   1 
HETATM 5149 O  O   . HOH   F 3 .   ? 35.552  -30.922 -1.973  1.00 19.71 ? 560 HOH   B O   1 
HETATM 5150 O  O   . HOH   F 3 .   ? 40.187  -14.311 26.231  1.00 33.30 ? 561 HOH   B O   1 
HETATM 5151 O  O   . HOH   F 3 .   ? 40.616  -1.517  26.377  1.00 43.21 ? 562 HOH   B O   1 
HETATM 5152 O  O   . HOH   F 3 .   ? 41.913  11.739  22.138  1.00 29.76 ? 563 HOH   B O   1 
HETATM 5153 O  O   . HOH   F 3 .   ? 50.006  -10.608 23.737  1.00 37.82 ? 564 HOH   B O   1 
HETATM 5154 O  O   . HOH   F 3 .   ? 32.566  -21.251 25.051  1.00 35.27 ? 565 HOH   B O   1 
HETATM 5155 O  O   . HOH   F 3 .   ? 48.978  -5.780  14.027  1.00 27.89 ? 566 HOH   B O   1 
HETATM 5156 O  O   . HOH   F 3 .   ? 43.323  -1.084  4.067   1.00 36.05 ? 567 HOH   B O   1 
HETATM 5157 O  O   . HOH   F 3 .   ? 34.067  2.350   5.338   1.00 28.55 ? 568 HOH   B O   1 
HETATM 5158 O  O   . HOH   F 3 .   ? 27.537  23.855  4.676   1.00 13.29 ? 569 HOH   B O   1 
HETATM 5159 O  O   . HOH   F 3 .   ? 20.635  13.229  1.743   1.00 41.89 ? 570 HOH   B O   1 
HETATM 5160 O  O   . HOH   F 3 .   ? 22.011  -34.810 11.438  1.00 35.89 ? 571 HOH   B O   1 
HETATM 5161 O  O   . HOH   F 3 .   ? 54.244  15.586  18.757  1.00 32.73 ? 572 HOH   B O   1 
HETATM 5162 O  O   . HOH   F 3 .   ? 46.764  3.606   20.032  1.00 39.39 ? 573 HOH   B O   1 
HETATM 5163 O  O   . HOH   F 3 .   ? 47.315  -3.020  21.434  1.00 29.22 ? 574 HOH   B O   1 
HETATM 5164 O  O   . HOH   F 3 .   ? 27.623  3.046   9.336   1.00 26.61 ? 575 HOH   B O   1 
HETATM 5165 O  O   . HOH   F 3 .   ? 25.992  23.610  16.195  1.00 33.62 ? 576 HOH   B O   1 
HETATM 5166 O  O   . HOH   F 3 .   ? 49.136  9.748   18.418  1.00 31.07 ? 577 HOH   B O   1 
HETATM 5167 O  O   . HOH   F 3 .   ? 46.317  -3.992  4.634   1.00 26.26 ? 578 HOH   B O   1 
HETATM 5168 O  O   . HOH   F 3 .   ? 23.098  25.990  8.134   1.00 38.52 ? 579 HOH   B O   1 
HETATM 5169 O  O   . HOH   F 3 .   ? 37.664  25.242  14.734  1.00 19.77 ? 580 HOH   B O   1 
HETATM 5170 O  O   . HOH   F 3 .   ? 39.554  -29.713 21.511  1.00 36.79 ? 581 HOH   B O   1 
HETATM 5171 O  O   . HOH   F 3 .   ? 40.784  -0.851  23.375  1.00 37.73 ? 582 HOH   B O   1 
HETATM 5172 O  O   . HOH   F 3 .   ? 46.373  -17.141 1.987   1.00 34.42 ? 583 HOH   B O   1 
HETATM 5173 O  O   . HOH   F 3 .   ? 32.716  14.380  -4.180  1.00 24.15 ? 584 HOH   B O   1 
HETATM 5174 O  O   . HOH   F 3 .   ? 49.831  1.138   26.674  1.00 52.98 ? 585 HOH   B O   1 
HETATM 5175 O  O   . HOH   F 3 .   ? 26.432  -18.897 -4.581  1.00 26.08 ? 586 HOH   B O   1 
HETATM 5176 O  O   . HOH   F 3 .   ? 50.501  -21.725 12.339  1.00 22.49 ? 587 HOH   B O   1 
HETATM 5177 O  O   . HOH   F 3 .   ? 40.727  -39.371 9.230   1.00 31.12 ? 588 HOH   B O   1 
HETATM 5178 O  O   . HOH   F 3 .   ? 27.334  -0.415  16.036  1.00 41.53 ? 589 HOH   B O   1 
HETATM 5179 O  O   . HOH   F 3 .   ? 50.019  -10.356 13.009  1.00 30.79 ? 590 HOH   B O   1 
HETATM 5180 O  O   . HOH   F 3 .   ? 44.356  25.945  13.335  1.00 32.05 ? 591 HOH   B O   1 
HETATM 5181 O  O   . HOH   F 3 .   ? 37.535  -21.370 0.117   1.00 14.38 ? 592 HOH   B O   1 
HETATM 5182 O  O   . HOH   F 3 .   ? 43.256  -18.396 4.656   1.00 18.88 ? 593 HOH   B O   1 
HETATM 5183 O  O   . HOH   F 3 .   ? 34.658  -16.727 26.392  1.00 25.69 ? 594 HOH   B O   1 
HETATM 5184 O  O   . HOH   F 3 .   ? 24.965  20.867  16.545  1.00 29.00 ? 595 HOH   B O   1 
HETATM 5185 O  O   . HOH   F 3 .   ? 44.377  -6.872  2.279   1.00 18.38 ? 596 HOH   B O   1 
HETATM 5186 O  O   . HOH   F 3 .   ? 46.438  -3.657  9.790   1.00 36.28 ? 597 HOH   B O   1 
HETATM 5187 O  O   . HOH   F 3 .   ? 49.606  -28.060 23.911  1.00 33.89 ? 598 HOH   B O   1 
HETATM 5188 O  O   . HOH   F 3 .   ? 42.693  -5.252  27.934  1.00 46.71 ? 599 HOH   B O   1 
HETATM 5189 O  O   . HOH   F 3 .   ? 42.257  -8.967  -1.145  1.00 33.67 ? 600 HOH   B O   1 
HETATM 5190 O  O   . HOH   F 3 .   ? 42.518  14.453  -0.857  1.00 19.37 ? 601 HOH   B O   1 
HETATM 5191 O  O   . HOH   F 3 .   ? 42.938  -19.486 17.460  1.00 14.22 ? 602 HOH   B O   1 
HETATM 5192 O  O   . HOH   F 3 .   ? 33.304  -34.055 18.930  1.00 20.69 ? 603 HOH   B O   1 
HETATM 5193 O  O   . HOH   F 3 .   ? 24.656  -23.891 2.052   1.00 21.61 ? 604 HOH   B O   1 
HETATM 5194 O  O   . HOH   F 3 .   ? 42.467  -3.316  3.280   1.00 40.71 ? 605 HOH   B O   1 
HETATM 5195 O  O   . HOH   F 3 .   ? 46.328  4.627   6.311   1.00 15.89 ? 606 HOH   B O   1 
HETATM 5196 O  O   . HOH   F 3 .   ? 39.164  16.559  -3.341  1.00 27.44 ? 607 HOH   B O   1 
HETATM 5197 O  O   . HOH   F 3 .   ? 46.637  3.524   8.845   1.00 28.81 ? 608 HOH   B O   1 
HETATM 5198 O  O   . HOH   F 3 .   ? 36.768  7.770   0.236   1.00 31.72 ? 609 HOH   B O   1 
HETATM 5199 O  O   . HOH   F 3 .   ? 32.597  -33.391 10.093  1.00 13.65 ? 610 HOH   B O   1 
HETATM 5200 O  O   . HOH   F 3 .   ? 25.428  -1.216  13.798  1.00 24.81 ? 611 HOH   B O   1 
HETATM 5201 O  O   . HOH   F 3 .   ? 30.284  -28.855 15.111  1.00 13.86 ? 612 HOH   B O   1 
HETATM 5202 O  O   . HOH   F 3 .   ? 27.254  3.957   6.747   1.00 27.54 ? 613 HOH   B O   1 
HETATM 5203 O  O   . HOH   F 3 .   ? 49.373  -16.441 18.034  1.00 24.43 ? 614 HOH   B O   1 
HETATM 5204 O  O   . HOH   F 3 .   ? 39.685  -20.472 25.691  1.00 24.44 ? 615 HOH   B O   1 
HETATM 5205 O  O   . HOH   F 3 .   ? 29.153  29.679  7.574   1.00 33.63 ? 616 HOH   B O   1 
HETATM 5206 O  O   . HOH   F 3 .   ? 36.456  -5.529  4.713   1.00 17.27 ? 617 HOH   B O   1 
HETATM 5207 O  O   . HOH   F 3 .   ? 41.958  -22.046 1.193   1.00 34.04 ? 618 HOH   B O   1 
HETATM 5208 O  O   . HOH   F 3 .   ? 34.747  -18.641 -5.203  1.00 40.88 ? 619 HOH   B O   1 
HETATM 5209 O  O   . HOH   F 3 .   ? 36.256  -28.209 25.668  1.00 33.59 ? 620 HOH   B O   1 
HETATM 5210 O  O   . HOH   F 3 .   ? 41.324  -11.379 5.687   1.00 20.40 ? 621 HOH   B O   1 
HETATM 5211 O  O   . HOH   F 3 .   ? 49.179  23.862  3.859   1.00 29.03 ? 622 HOH   B O   1 
HETATM 5212 O  O   . HOH   F 3 .   ? 28.096  -12.789 -4.583  1.00 21.96 ? 623 HOH   B O   1 
HETATM 5213 O  O   . HOH   F 3 .   ? 49.234  -27.320 8.653   1.00 26.18 ? 624 HOH   B O   1 
HETATM 5214 O  O   . HOH   F 3 .   ? 32.009  -22.193 22.512  1.00 22.97 ? 625 HOH   B O   1 
HETATM 5215 O  O   . HOH   F 3 .   ? 49.711  -14.027 17.073  1.00 28.48 ? 626 HOH   B O   1 
HETATM 5216 O  O   . HOH   F 3 .   ? 25.547  -23.610 10.873  1.00 28.52 ? 627 HOH   B O   1 
HETATM 5217 O  O   . HOH   F 3 .   ? 39.802  1.360   23.060  1.00 37.33 ? 628 HOH   B O   1 
HETATM 5218 O  O   . HOH   F 3 .   ? 33.436  7.619   18.540  1.00 28.25 ? 629 HOH   B O   1 
HETATM 5219 O  O   . HOH   F 3 .   ? 33.710  -4.011  23.602  1.00 28.07 ? 630 HOH   B O   1 
HETATM 5220 O  O   . HOH   F 3 .   ? 32.583  -17.212 -5.270  1.00 33.18 ? 631 HOH   B O   1 
HETATM 5221 O  O   . HOH   F 3 .   ? 42.277  19.062  -0.079  1.00 17.62 ? 632 HOH   B O   1 
HETATM 5222 O  O   . HOH   F 3 .   ? 49.186  -13.699 14.371  1.00 21.82 ? 633 HOH   B O   1 
HETATM 5223 O  O   . HOH   F 3 .   ? 22.061  19.762  3.974   1.00 25.54 ? 634 HOH   B O   1 
HETATM 5224 O  O   . HOH   F 3 .   ? 38.725  -37.872 5.200   1.00 37.94 ? 635 HOH   B O   1 
HETATM 5225 O  O   . HOH   F 3 .   ? 31.235  21.244  -4.240  1.00 26.66 ? 636 HOH   B O   1 
HETATM 5226 O  O   . HOH   F 3 .   ? 29.494  -14.430 27.880  1.00 29.04 ? 637 HOH   B O   1 
HETATM 5227 O  O   . HOH   F 3 .   ? 41.233  -13.025 -1.361  1.00 28.08 ? 638 HOH   B O   1 
HETATM 5228 O  O   . HOH   F 3 .   ? 33.513  9.504   12.691  1.00 10.33 ? 639 HOH   B O   1 
HETATM 5229 O  O   . HOH   F 3 .   ? 49.415  10.245  21.153  1.00 37.85 ? 640 HOH   B O   1 
HETATM 5230 O  O   . HOH   F 3 .   ? 22.488  -17.958 17.760  1.00 30.91 ? 641 HOH   B O   1 
HETATM 5231 O  O   . HOH   F 3 .   ? 45.134  -33.032 5.286   1.00 23.24 ? 642 HOH   B O   1 
HETATM 5232 O  O   . HOH   F 3 .   ? 37.537  -31.100 23.946  1.00 34.33 ? 643 HOH   B O   1 
HETATM 5233 O  O   . HOH   F 3 .   ? 23.212  20.166  13.709  1.00 43.27 ? 644 HOH   B O   1 
HETATM 5234 O  O   . HOH   F 3 .   ? 24.414  -35.131 9.246   1.00 28.03 ? 645 HOH   B O   1 
HETATM 5235 O  O   . HOH   F 3 .   ? 50.294  -17.085 4.675   1.00 37.56 ? 646 HOH   B O   1 
HETATM 5236 O  O   . HOH   F 3 .   ? 30.092  -2.079  7.554   1.00 23.81 ? 647 HOH   B O   1 
HETATM 5237 O  O   . HOH   F 3 .   ? 46.399  25.853  12.009  1.00 46.97 ? 648 HOH   B O   1 
HETATM 5238 O  O   . HOH   F 3 .   ? 41.648  4.267   8.294   1.00 21.85 ? 649 HOH   B O   1 
HETATM 5239 O  O   . HOH   F 3 .   ? 39.058  5.196   8.186   1.00 16.25 ? 650 HOH   B O   1 
HETATM 5240 O  O   . HOH   F 3 .   ? 24.285  -8.333  -0.042  1.00 27.38 ? 651 HOH   B O   1 
HETATM 5241 O  O   . HOH   F 3 .   ? 26.857  26.011  12.812  1.00 35.45 ? 652 HOH   B O   1 
HETATM 5242 O  O   . HOH   F 3 .   ? 40.077  -27.082 -1.682  1.00 50.68 ? 653 HOH   B O   1 
HETATM 5243 O  O   . HOH   F 3 .   ? 43.599  -32.626 27.956  1.00 42.50 ? 654 HOH   B O   1 
HETATM 5244 O  O   . HOH   F 3 .   ? 47.695  2.232   14.685  1.00 37.06 ? 655 HOH   B O   1 
HETATM 5245 O  O   . HOH   F 3 .   ? 19.440  -16.827 6.225   1.00 36.75 ? 656 HOH   B O   1 
HETATM 5246 O  O   . HOH   F 3 .   ? 35.019  -15.169 -5.247  1.00 22.95 ? 657 HOH   B O   1 
HETATM 5247 O  O   . HOH   F 3 .   ? 51.250  19.244  3.974   1.00 20.36 ? 658 HOH   B O   1 
HETATM 5248 O  O   . HOH   F 3 .   ? 43.277  -27.485 4.276   1.00 22.30 ? 659 HOH   B O   1 
HETATM 5249 O  O   . HOH   F 3 .   ? 53.380  18.459  5.632   1.00 19.88 ? 660 HOH   B O   1 
HETATM 5250 O  O   . HOH   F 3 .   ? 44.511  20.039  1.609   1.00 15.45 ? 661 HOH   B O   1 
HETATM 5251 O  O   . HOH   F 3 .   ? 43.807  8.980   11.425  1.00 15.86 ? 662 HOH   B O   1 
HETATM 5252 O  O   . HOH   F 3 .   ? 30.313  -29.189 23.709  1.00 39.05 ? 663 HOH   B O   1 
HETATM 5253 O  O   . HOH   F 3 .   ? 43.343  13.176  -2.879  1.00 36.39 ? 664 HOH   B O   1 
HETATM 5254 O  O   . HOH   F 3 .   ? 51.493  24.679  9.285   1.00 30.01 ? 665 HOH   B O   1 
HETATM 5255 O  O   . HOH   F 3 .   ? 38.281  -29.889 26.602  1.00 33.77 ? 666 HOH   B O   1 
HETATM 5256 O  O   . HOH   F 3 .   ? 36.124  7.048   20.642  1.00 43.88 ? 667 HOH   B O   1 
HETATM 5257 O  O   . HOH   F 3 .   ? 34.852  -35.302 9.233   1.00 29.80 ? 668 HOH   B O   1 
HETATM 5258 O  O   . HOH   F 3 .   ? 36.398  1.144   6.268   1.00 36.97 ? 669 HOH   B O   1 
HETATM 5259 O  O   . HOH   F 3 .   ? 48.467  -30.113 6.130   1.00 47.12 ? 670 HOH   B O   1 
HETATM 5260 O  O   . HOH   F 3 .   ? 49.781  -18.942 20.597  1.00 37.71 ? 671 HOH   B O   1 
HETATM 5261 O  O   . HOH   F 3 .   ? 23.174  -2.904  12.685  1.00 25.90 ? 672 HOH   B O   1 
HETATM 5262 O  O   . HOH   F 3 .   ? 51.266  -23.165 9.955   1.00 46.24 ? 673 HOH   B O   1 
HETATM 5263 O  O   . HOH   F 3 .   ? 51.464  -20.925 8.680   1.00 34.86 ? 674 HOH   B O   1 
HETATM 5264 O  O   . HOH   F 3 .   ? 40.505  -17.904 -0.825  1.00 47.37 ? 675 HOH   B O   1 
HETATM 5265 O  O   . HOH   F 3 .   ? 33.190  -0.726  2.379   1.00 39.97 ? 676 HOH   B O   1 
HETATM 5266 O  O   . HOH   F 3 .   ? 27.050  -3.043  -0.841  1.00 44.51 ? 677 HOH   B O   1 
HETATM 5267 O  O   . HOH   F 3 .   ? 25.604  -15.756 -1.999  1.00 36.99 ? 678 HOH   B O   1 
HETATM 5268 O  O   . HOH   F 3 .   ? 43.384  -11.577 27.209  1.00 37.68 ? 679 HOH   B O   1 
HETATM 5269 O  O   . HOH   F 3 .   ? 40.089  -2.650  2.954   1.00 29.60 ? 680 HOH   B O   1 
HETATM 5270 O  O   . HOH   F 3 .   ? 51.388  -29.322 12.975  1.00 35.54 ? 681 HOH   B O   1 
HETATM 5271 O  O   . HOH   F 3 .   ? 30.297  10.200  19.728  1.00 40.39 ? 682 HOH   B O   1 
HETATM 5272 O  O   . HOH   F 3 .   ? 50.568  -10.634 28.345  1.00 48.93 ? 683 HOH   B O   1 
HETATM 5273 O  O   . HOH   F 3 .   ? 54.871  -30.731 18.841  1.00 44.25 ? 684 HOH   B O   1 
HETATM 5274 O  O   . HOH   F 3 .   ? 37.097  26.800  1.290   1.00 30.21 ? 685 HOH   B O   1 
HETATM 5275 O  O   . HOH   F 3 .   ? 42.988  -13.902 26.001  1.00 45.50 ? 686 HOH   B O   1 
HETATM 5276 O  O   . HOH   F 3 .   ? 44.077  -35.465 4.194   1.00 28.42 ? 687 HOH   B O   1 
HETATM 5277 O  O   . HOH   F 3 .   ? 35.709  29.073  13.910  1.00 38.67 ? 688 HOH   B O   1 
HETATM 5278 O  O   . HOH   F 3 .   ? 52.048  -22.933 19.097  1.00 31.33 ? 689 HOH   B O   1 
HETATM 5279 O  O   . HOH   F 3 .   ? 44.001  -37.151 8.156   1.00 15.55 ? 690 HOH   B O   1 
HETATM 5280 O  O   . HOH   F 3 .   ? 23.911  3.545   16.006  1.00 37.17 ? 691 HOH   B O   1 
HETATM 5281 O  O   . HOH   F 3 .   ? 34.270  9.284   0.831   1.00 39.05 ? 692 HOH   B O   1 
HETATM 5282 O  O   . HOH   F 3 .   ? 18.428  -13.837 15.666  1.00 41.86 ? 693 HOH   B O   1 
HETATM 5283 O  O   . HOH   F 3 .   ? 38.457  21.291  -1.876  1.00 36.34 ? 694 HOH   B O   1 
HETATM 5284 O  O   . HOH   F 3 .   ? 26.710  12.803  -4.299  1.00 56.54 ? 695 HOH   B O   1 
HETATM 5285 O  O   . HOH   F 3 .   ? 29.666  -22.641 22.062  1.00 34.17 ? 696 HOH   B O   1 
HETATM 5286 O  O   . HOH   F 3 .   ? 43.611  6.118   -0.378  1.00 26.42 ? 697 HOH   B O   1 
HETATM 5287 O  O   . HOH   F 3 .   ? 38.341  12.237  -4.626  1.00 41.45 ? 698 HOH   B O   1 
HETATM 5288 O  O   . HOH   F 3 .   ? 52.092  -20.651 18.688  1.00 43.62 ? 699 HOH   B O   1 
HETATM 5289 O  O   . HOH   F 3 .   ? 22.371  -12.314 -1.621  1.00 38.72 ? 700 HOH   B O   1 
HETATM 5290 O  O   . HOH   F 3 .   ? 23.053  -16.481 0.814   1.00 25.90 ? 701 HOH   B O   1 
HETATM 5291 O  O   . HOH   F 3 .   ? 41.053  -31.992 21.335  1.00 39.43 ? 702 HOH   B O   1 
HETATM 5292 O  O   . HOH   F 3 .   ? 32.962  -29.064 28.077  1.00 40.23 ? 703 HOH   B O   1 
HETATM 5293 O  O   . HOH   F 3 .   ? 27.909  28.530  11.032  1.00 49.14 ? 704 HOH   B O   1 
HETATM 5294 O  O   . HOH   F 3 .   ? 21.105  21.312  5.408   1.00 36.51 ? 705 HOH   B O   1 
HETATM 5295 O  O   . HOH   F 3 .   ? 24.469  -23.213 5.002   1.00 50.50 ? 706 HOH   B O   1 
HETATM 5296 O  O   . HOH   F 3 .   ? 49.836  -31.584 11.591  1.00 34.03 ? 707 HOH   B O   1 
HETATM 5297 O  O   . HOH   F 3 .   ? 33.726  -1.672  25.304  1.00 38.84 ? 708 HOH   B O   1 
HETATM 5298 O  O   . HOH   F 3 .   ? 24.889  23.660  21.643  1.00 42.27 ? 709 HOH   B O   1 
HETATM 5299 O  O   . HOH   F 3 .   ? 43.428  3.875   6.001   1.00 37.10 ? 710 HOH   B O   1 
HETATM 5300 O  O   . HOH   F 3 .   ? 43.898  -11.028 4.738   1.00 29.36 ? 711 HOH   B O   1 
HETATM 5301 O  O   . HOH   F 3 .   ? 37.420  -3.855  2.732   1.00 28.96 ? 712 HOH   B O   1 
HETATM 5302 O  O   . HOH   F 3 .   ? 43.781  -14.572 0.378   1.00 44.24 ? 713 HOH   B O   1 
HETATM 5303 O  O   . HOH   F 3 .   ? 21.381  -13.646 1.140   1.00 45.53 ? 714 HOH   B O   1 
HETATM 5304 O  O   . HOH   F 3 .   ? 18.201  -14.891 13.536  1.00 38.32 ? 715 HOH   B O   1 
HETATM 5305 O  O   . HOH   F 3 .   ? 37.587  26.320  5.699   1.00 32.06 ? 716 HOH   B O   1 
HETATM 5306 O  O   . HOH   F 3 .   ? 41.488  16.860  -1.360  1.00 28.38 ? 717 HOH   B O   1 
HETATM 5307 O  O   . HOH   F 3 .   ? 31.640  23.284  -3.210  1.00 32.88 ? 718 HOH   B O   1 
HETATM 5308 O  O   . HOH   F 3 .   ? 42.533  -39.267 7.272   1.00 31.65 ? 719 HOH   B O   1 
HETATM 5309 O  O   . HOH   F 3 .   ? 43.791  -17.897 2.236   1.00 33.26 ? 720 HOH   B O   1 
HETATM 5310 O  O   . HOH   F 3 .   ? 37.111  -16.395 -5.011  1.00 54.13 ? 721 HOH   B O   1 
HETATM 5311 O  O   . HOH   F 3 .   ? 27.293  -12.904 -7.128  1.00 44.65 ? 722 HOH   B O   1 
HETATM 5312 O  O   . HOH   F 3 .   ? 34.712  -25.824 -4.729  1.00 44.31 ? 723 HOH   B O   1 
HETATM 5313 O  O   . HOH   F 3 .   ? 53.803  15.984  5.236   1.00 38.57 ? 724 HOH   B O   1 
HETATM 5314 O  O   . HOH   F 3 .   ? 51.474  -17.680 19.176  1.00 33.93 ? 725 HOH   B O   1 
HETATM 5315 O  O   . HOH   F 3 .   ? 44.068  6.321   12.225  1.00 26.34 ? 726 HOH   B O   1 
HETATM 5316 O  O   . HOH   F 3 .   ? 50.620  26.563  7.114   1.00 41.12 ? 727 HOH   B O   1 
HETATM 5317 O  O   . HOH   F 3 .   ? 38.661  -39.978 7.695   1.00 49.89 ? 728 HOH   B O   1 
HETATM 5318 O  O   . HOH   F 3 .   ? 46.864  -5.836  2.825   1.00 24.16 ? 729 HOH   B O   1 
HETATM 5319 O  O   . HOH   F 3 .   ? 38.110  3.947   5.672   1.00 18.25 ? 730 HOH   B O   1 
HETATM 5320 O  O   . HOH   F 3 .   ? 41.734  20.968  -1.887  1.00 38.01 ? 731 HOH   B O   1 
HETATM 5321 O  O   . HOH   F 3 .   ? 50.200  26.288  4.918   1.00 43.34 ? 732 HOH   B O   1 
HETATM 5322 O  O   . HOH   F 3 .   ? 50.856  -4.395  15.442  1.00 40.43 ? 733 HOH   B O   1 
HETATM 5323 O  O   . HOH   F 3 .   ? 41.449  16.624  23.448  1.00 51.42 ? 734 HOH   B O   1 
HETATM 5324 O  O   . HOH   F 3 .   ? 59.012  22.080  10.031  1.00 39.79 ? 735 HOH   B O   1 
HETATM 5325 O  O   . HOH   F 3 .   ? 48.561  4.954   10.700  1.00 36.72 ? 736 HOH   B O   1 
HETATM 5326 O  O   . HOH   F 3 .   ? 25.950  -14.138 -3.589  1.00 34.05 ? 737 HOH   B O   1 
HETATM 5327 O  O   . HOH   F 3 .   ? 39.689  -22.577 -2.170  1.00 44.25 ? 738 HOH   B O   1 
HETATM 5328 O  O   . HOH   F 3 .   ? 22.192  22.763  15.962  1.00 46.44 ? 739 HOH   B O   1 
HETATM 5329 O  O   . HOH   F 3 .   ? 42.863  -25.601 2.050   1.00 37.82 ? 740 HOH   B O   1 
HETATM 5330 O  O   . HOH   F 3 .   ? 36.552  26.390  17.159  1.00 34.49 ? 741 HOH   B O   1 
HETATM 5331 O  O   . HOH   F 3 .   ? 45.381  22.551  0.752   1.00 24.94 ? 742 HOH   B O   1 
HETATM 5332 O  O   . HOH   F 3 .   ? 21.100  -18.257 1.690   1.00 47.25 ? 743 HOH   B O   1 
HETATM 5333 O  O   . HOH   F 3 .   ? 41.864  -26.828 -0.051  1.00 42.41 ? 744 HOH   B O   1 
HETATM 5334 O  O   . HOH   F 3 .   ? 46.461  18.058  1.132   1.00 35.44 ? 745 HOH   B O   1 
HETATM 5335 O  O   . HOH   F 3 .   ? 25.394  -1.181  -9.043  1.00 48.14 ? 746 HOH   B O   1 
# 
