data_7I18
# 
_entry.id   7I18 
# 
_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   7I18         pdb_00007i18 10.2210/pdb7i18/pdb 
WWPDB D_1001408188 ?            ?                   
# 
_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       2025-05-21 
_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.entry_id                        7I18 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-03 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.name_last          Weiss 
_pdbx_contact_author.name_first         Manfred 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              manfred.weiss@helmholtz-berlin.de 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2362-7047 
# 
loop_
_audit_author.pdbx_ordinal 
_audit_author.name 
1 'Barthel, T.'     
2 'Benz, L.S.'      
3 'Wollenhaupt, J.' 
4 'Weiss, M.S.'     
# 
_citation.id                        primary 
_citation.title                     
'Orthorhombic SARS-CoV-2 main protease crystals provide higher success rate in fragment screening' 
_citation.journal_abbrev            'To be published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.ordinal 
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
1  primary 'Barthel, T.'     ? 
2  primary 'Wollenhaupt, J.' ? 
3  primary 'Benz, L.S.'      ? 
4  primary 'Reincke, P.'     ? 
5  primary 'Zhang, L.'       ? 
6  primary 'Lennartz, F.'    ? 
7  primary 'Tabermann, H.'   ? 
8  primary 'Mueller, U.'     ? 
9  primary 'Meente, A.'      ? 
10 primary 'Hilgenfeld, R.'  ? 
11 primary 'Weiss, M.S.'     ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase nsp5'           33825.547 2  3.4.22.69 ? ? ? 
2 non-polymer syn 'methyl 4-fluoro-D-phenylalaninate' 197.206   1  ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                78.133    2  ?         ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                      35.453    2  ?         ? ? ? 
5 water       nat water                               18.015    96 ?         ? ? ? 
# 
_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
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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 'methyl 4-fluoro-D-phenylalaninate' R9D 
3 'DIMETHYL SULFOXIDE'                DMS 
4 'CHLORIDE ION'                      CL  
5 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 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                             ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                            ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                          ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                     ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                      ? 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                            ? 'C3 H7 N O2 S'   121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                ? 'C2 H6 O S'      78.133  
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 
R9D non-polymer         . 'methyl 4-fluoro-D-phenylalaninate' ? 'C10 H12 F N O2' 197.206 
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 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER 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 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        R9D 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   R9D 
_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 R9D 1  501 501 R9D LIG A . 
D 3 DMS 1  502 601 DMS DMS A . 
E 4 CL  1  503 1   CL  CL  A . 
F 4 CL  1  504 2   CL  CL  A . 
G 3 DMS 1  401 401 DMS DMS B . 
H 5 HOH 1  601 41  HOH HOH A . 
H 5 HOH 2  602 70  HOH HOH A . 
H 5 HOH 3  603 99  HOH HOH A . 
H 5 HOH 4  604 34  HOH HOH A . 
H 5 HOH 5  605 49  HOH HOH A . 
H 5 HOH 6  606 63  HOH HOH A . 
H 5 HOH 7  607 17  HOH HOH A . 
H 5 HOH 8  608 31  HOH HOH A . 
H 5 HOH 9  609 89  HOH HOH A . 
H 5 HOH 10 610 93  HOH HOH A . 
H 5 HOH 11 611 75  HOH HOH A . 
H 5 HOH 12 612 98  HOH HOH A . 
H 5 HOH 13 613 97  HOH HOH A . 
H 5 HOH 14 614 64  HOH HOH A . 
H 5 HOH 15 615 30  HOH HOH A . 
H 5 HOH 16 616 21  HOH HOH A . 
H 5 HOH 17 617 20  HOH HOH A . 
H 5 HOH 18 618 10  HOH HOH A . 
H 5 HOH 19 619 66  HOH HOH A . 
H 5 HOH 20 620 28  HOH HOH A . 
H 5 HOH 21 621 23  HOH HOH A . 
H 5 HOH 22 622 72  HOH HOH A . 
H 5 HOH 23 623 9   HOH HOH A . 
H 5 HOH 24 624 2   HOH HOH A . 
H 5 HOH 25 625 52  HOH HOH A . 
H 5 HOH 26 626 74  HOH HOH A . 
H 5 HOH 27 627 7   HOH HOH A . 
H 5 HOH 28 628 16  HOH HOH A . 
H 5 HOH 29 629 71  HOH HOH A . 
H 5 HOH 30 630 36  HOH HOH A . 
H 5 HOH 31 631 60  HOH HOH A . 
H 5 HOH 32 632 43  HOH HOH A . 
H 5 HOH 33 633 26  HOH HOH A . 
H 5 HOH 34 634 22  HOH HOH A . 
H 5 HOH 35 635 59  HOH HOH A . 
H 5 HOH 36 636 33  HOH HOH A . 
H 5 HOH 37 637 76  HOH HOH A . 
H 5 HOH 38 638 47  HOH HOH A . 
H 5 HOH 39 639 37  HOH HOH A . 
H 5 HOH 40 640 29  HOH HOH A . 
H 5 HOH 41 641 58  HOH HOH A . 
H 5 HOH 42 642 11  HOH HOH A . 
H 5 HOH 43 643 84  HOH HOH A . 
H 5 HOH 44 644 87  HOH HOH A . 
H 5 HOH 45 645 65  HOH HOH A . 
H 5 HOH 46 646 83  HOH HOH A . 
H 5 HOH 47 647 18  HOH HOH A . 
H 5 HOH 48 648 51  HOH HOH A . 
H 5 HOH 49 649 57  HOH HOH A . 
H 5 HOH 50 650 40  HOH HOH A . 
H 5 HOH 51 651 56  HOH HOH A . 
H 5 HOH 52 652 14  HOH HOH A . 
H 5 HOH 53 653 39  HOH HOH A . 
H 5 HOH 54 654 46  HOH HOH A . 
H 5 HOH 55 655 82  HOH HOH A . 
H 5 HOH 56 656 67  HOH HOH A . 
H 5 HOH 57 657 45  HOH HOH A . 
H 5 HOH 58 658 90  HOH HOH A . 
H 5 HOH 59 659 91  HOH HOH A . 
H 5 HOH 60 660 81  HOH HOH A . 
H 5 HOH 61 661 88  HOH HOH A . 
I 5 HOH 1  501 8   HOH HOH B . 
I 5 HOH 2  502 15  HOH HOH B . 
I 5 HOH 3  503 25  HOH HOH B . 
I 5 HOH 4  504 69  HOH HOH B . 
I 5 HOH 5  505 5   HOH HOH B . 
I 5 HOH 6  506 3   HOH HOH B . 
I 5 HOH 7  507 19  HOH HOH B . 
I 5 HOH 8  508 79  HOH HOH B . 
I 5 HOH 9  509 38  HOH HOH B . 
I 5 HOH 10 510 86  HOH HOH B . 
I 5 HOH 11 511 27  HOH HOH B . 
I 5 HOH 12 512 44  HOH HOH B . 
I 5 HOH 13 513 12  HOH HOH B . 
I 5 HOH 14 514 73  HOH HOH B . 
I 5 HOH 15 515 85  HOH HOH B . 
I 5 HOH 16 516 96  HOH HOH B . 
I 5 HOH 17 517 62  HOH HOH B . 
I 5 HOH 18 518 53  HOH HOH B . 
I 5 HOH 19 519 95  HOH HOH B . 
I 5 HOH 20 520 77  HOH HOH B . 
I 5 HOH 21 521 13  HOH HOH B . 
I 5 HOH 22 522 68  HOH HOH B . 
I 5 HOH 23 523 48  HOH HOH B . 
I 5 HOH 24 524 54  HOH HOH B . 
I 5 HOH 25 525 42  HOH HOH B . 
I 5 HOH 26 526 35  HOH HOH B . 
I 5 HOH 27 527 32  HOH HOH B . 
I 5 HOH 28 528 80  HOH HOH B . 
I 5 HOH 29 529 24  HOH HOH B . 
I 5 HOH 30 530 61  HOH HOH B . 
I 5 HOH 31 531 6   HOH HOH B . 
I 5 HOH 32 532 50  HOH HOH B . 
I 5 HOH 33 533 78  HOH HOH B . 
I 5 HOH 34 534 94  HOH HOH B . 
I 5 HOH 35 535 92  HOH HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0238 ? 1 
'data scaling'   XDS    .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7I18 
_cell.length_a           68.050 
_cell.length_b           99.280 
_cell.length_c           103.500 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I18 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          7I18 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.59 
_exptl_crystal.density_percent_sol   52.47 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pdbx_details    
;0.2 M MIB (sodium malonate, imidazole, and boric acid in the molar ratios 2:3:3) pH 7.7, 23.5 % PEG 1500, 5 % DMSO, 1 mM DTT. Crystal seeds were used to ensure reproducible crystal growth.
;
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pH              7.7 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.pdbx_collection_date   2022-12-06 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9184 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'BESSY BEAMLINE 14.1' 
_diffrn_source.pdbx_synchrotron_site       BESSY 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I18 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             45.89 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   48244 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.154 
_reflns.pdbx_netI_over_sigmaI        8.99 
_reflns.pdbx_Rrim_I_all              0.17 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     277063 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 2.00 2.12 43686 7675 1.48                 99.9  1.10  1.631               0.47               ? ? ? ? 
1 2 2.12 2.26 41989 7236 0.929                100.0 1.80  1.022               0.659              ? ? ? ? 
1 3 2.26 2.44 38909 6766 0.6459999999999999   99.9  2.62  0.711               0.828              ? ? ? ? 
1 4 2.44 2.68 35241 6225 0.41200000000000003  99.9  4.09  0.45399999999999996 0.909              ? ? ? ? 
1 5 2.68 2.99 34442 5674 0.25                 100.0 6.92  0.273               0.97               ? ? ? ? 
1 6 2.99 3.45 29314 5036 0.134                99.9  12.53 0.147               0.991              ? ? ? ? 
1 7 3.45 4.22 23669 4276 0.069                99.7  22.37 0.076               0.997              ? ? ? ? 
1 8 4.22 5.95 19442 3375 0.05                 99.8  30.29 0.055               0.998              ? ? ? ? 
1 9 5.95 ?    10371 1981 0.036000000000000004 99.1  34.82 0.04                0.9990000000000001 ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I18 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     46143 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             45.89 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_R_factor_obs                          0.21169 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20975 
_refine.ls_R_factor_R_free                       0.25461 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.4 
_refine.ls_number_reflns_R_free                  2101 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.956 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_refine.B_iso_mean                               35.174 
_refine.aniso_B[1][1]                            -1.28 
_refine.aniso_B[2][2]                            1.97 
_refine.aniso_B[3][3]                            -0.69 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_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_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.200 
_refine.pdbx_overall_ESU_R_Free                  0.177 
_refine.overall_SU_ML                            0.176 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.911 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4687 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             96 
_refine_hist.number_atoms_total               4807 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        45.89 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.013  ? 5887  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.017  ? 5222  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.494  1.641  ? 7494  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.334  1.575  ? 11359 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.506  5.000  ? 721   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       34.935 23.160 ? 269   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.538 15.000 ? 886   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       20.126 15.000 ? 25    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 710   'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 6398  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 1169  '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' ? 
r_mcbond_it                  2.460  3.616  ? 2970  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.459  3.614  ? 2963  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 3.784  5.400  ? 3525  'X-RAY DIFFRACTION' ? 
r_mcangle_other              3.784  5.401  ? 3526  'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.099  3.918  ? 2917  'X-RAY DIFFRACTION' ? 
r_scbond_other               3.098  3.919  ? 2918  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              4.881  5.775  ? 3970  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       6.997  42.067 ? 5871  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.002  42.050 ? 5860  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.997 
_refine_ls_shell.d_res_low                        2.048 
_refine_ls_shell.number_reflns_R_work             3322 
_refine_ls_shell.R_factor_R_work                  0.336 
_refine_ls_shell.percent_reflns_obs               99.74 
_refine_ls_shell.R_factor_R_free                  0.343 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             152 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7I18 
_struct.title                     
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragment D04 from the F2X-Entry Screen in orthorhombic space group
;
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I18 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SARS-CoV-2, fragment screen, main protease, 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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
_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
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I18 A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 7I18 B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              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)' 3800  ? 
1 MORE         -23   ? 
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,G,H,I 
# 
_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 SER A 46  ? LEU A 50  ? SER A 46  LEU A 50  5 ? 5  
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 ? MET A 235 ? THR A 226 MET A 235 1 ? 10 
HELX_P HELX_P8  AA8 LYS A 236 ? ASN A 238 ? LYS A 236 ASN A 238 5 ? 3  
HELX_P HELX_P9  AA9 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P10 AB1 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P11 AB2 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P12 AB3 THR A 292 ? SER A 301 ? THR A 292 SER A 301 1 ? 10 
HELX_P HELX_P13 AB4 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P14 AB5 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P15 AB6 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P16 AB7 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P17 AB8 SER B 62  ? PHE B 66  ? SER B 62  PHE B 66  5 ? 5  
HELX_P HELX_P18 AB9 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P19 AC1 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P20 AC2 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P21 AC3 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P22 AC4 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P23 AC5 THR B 292 ? GLY B 302 ? THR B 292 GLY B 302 1 ? 11 
# 
_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 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA2 3 VAL A 148 ? ASN A 151 ? VAL A 148 ASN A 151 
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 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 VAL A 157 ? GLU A 166 ? VAL A 157 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 TYR B 101 ? PHE B 103 ? TYR B 101 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 TYR B 101 ? PHE B 103 ? TYR B 101 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 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
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 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
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 GLN B 69  ? O GLN B 69  N GLN B 19  ? N GLN B 19  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
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 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA5 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA5 2 3 O CYS B 156 ? O CYS B 156 N ASP B 153 ? N ASP B 153 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N VAL B 114 ? N VAL B 114 O TYR B 126 ? O TYR B 126 
AA6 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   7I18 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    62 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NE2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HIS 
_pdbx_validate_close_contact.auth_seq_id_2    64 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
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 LYS A 5   ? ? -53.36  100.87  
2  1 ASP A 33  ? ? 43.47   -122.46 
3  1 HIS A 41  ? C -68.66  1.32    
4  1 HIS A 41  ? D -68.66  1.32    
5  1 MET A 49  ? C -28.10  -46.85  
6  1 MET A 49  ? D -28.10  -46.85  
7  1 ASN A 84  ? ? 61.52   -123.53 
8  1 ASN A 84  ? ? 61.52   -123.53 
9  1 ASN A 84  ? ? 61.52   -123.31 
10 1 ASN A 84  ? ? 61.52   -123.31 
11 1 ASP A 155 ? ? 75.08   -16.80  
12 1 GLN A 189 ? C -93.82  34.00   
13 1 GLN A 189 ? D -93.82  34.00   
14 1 ASP B 33  ? ? 52.94   -129.29 
15 1 ASN B 51  ? ? -156.63 75.23   
16 1 ASN B 84  ? ? 51.94   -125.63 
17 1 TYR B 154 ? ? 79.55   -102.43 
18 1 GLN B 189 ? ? -64.73  92.16   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLY 302 ? A GLY 302 
2 1 Y 1 A VAL 303 ? A VAL 303 
3 1 Y 1 A THR 304 ? A THR 304 
4 1 Y 1 A PHE 305 ? A PHE 305 
5 1 Y 1 A GLN 306 ? A GLN 306 
6 1 Y 1 B GLN 306 ? B GLN 306 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
DMS S    S  N N 89  
DMS O    O  N N 90  
DMS C1   C  N N 91  
DMS C2   C  N N 92  
DMS H11  H  N N 93  
DMS H12  H  N N 94  
DMS H13  H  N N 95  
DMS H21  H  N N 96  
DMS H22  H  N N 97  
DMS H23  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
R9D C4   C  Y N 301 
R9D C5   C  Y N 302 
R9D C6   C  Y N 303 
R9D C7   C  Y N 304 
R9D C8   C  Y N 305 
R9D C9   C  Y N 306 
R9D F    F  N N 307 
R9D C3   C  N N 308 
R9D C2   C  N R 309 
R9D N    N  N N 310 
R9D C1   C  N N 311 
R9D O1   O  N N 312 
R9D O    O  N N 313 
R9D C    C  N N 314 
R9D H1   H  N N 315 
R9D H2   H  N N 316 
R9D H3   H  N N 317 
R9D H4   H  N N 318 
R9D H5   H  N N 319 
R9D H6   H  N N 320 
R9D H7   H  N N 321 
R9D H8   H  N N 322 
R9D H9   H  N N 323 
R9D H11  H  N N 324 
R9D H12  H  N N 325 
R9D H13  H  N N 326 
SER N    N  N N 327 
SER CA   C  N S 328 
SER C    C  N N 329 
SER O    O  N N 330 
SER CB   C  N N 331 
SER OG   O  N N 332 
SER OXT  O  N N 333 
SER H    H  N N 334 
SER H2   H  N N 335 
SER HA   H  N N 336 
SER HB2  H  N N 337 
SER HB3  H  N N 338 
SER HG   H  N N 339 
SER HXT  H  N N 340 
THR N    N  N N 341 
THR CA   C  N S 342 
THR C    C  N N 343 
THR O    O  N N 344 
THR CB   C  N R 345 
THR OG1  O  N N 346 
THR CG2  C  N N 347 
THR OXT  O  N N 348 
THR H    H  N N 349 
THR H2   H  N N 350 
THR HA   H  N N 351 
THR HB   H  N N 352 
THR HG1  H  N N 353 
THR HG21 H  N N 354 
THR HG22 H  N N 355 
THR HG23 H  N N 356 
THR HXT  H  N N 357 
TRP N    N  N N 358 
TRP CA   C  N S 359 
TRP C    C  N N 360 
TRP O    O  N N 361 
TRP CB   C  N N 362 
TRP CG   C  Y N 363 
TRP CD1  C  Y N 364 
TRP CD2  C  Y N 365 
TRP NE1  N  Y N 366 
TRP CE2  C  Y N 367 
TRP CE3  C  Y N 368 
TRP CZ2  C  Y N 369 
TRP CZ3  C  Y N 370 
TRP CH2  C  Y N 371 
TRP OXT  O  N N 372 
TRP H    H  N N 373 
TRP H2   H  N N 374 
TRP HA   H  N N 375 
TRP HB2  H  N N 376 
TRP HB3  H  N N 377 
TRP HD1  H  N N 378 
TRP HE1  H  N N 379 
TRP HE3  H  N N 380 
TRP HZ2  H  N N 381 
TRP HZ3  H  N N 382 
TRP HH2  H  N N 383 
TRP HXT  H  N N 384 
TYR N    N  N N 385 
TYR CA   C  N S 386 
TYR C    C  N N 387 
TYR O    O  N N 388 
TYR CB   C  N N 389 
TYR CG   C  Y N 390 
TYR CD1  C  Y N 391 
TYR CD2  C  Y N 392 
TYR CE1  C  Y N 393 
TYR CE2  C  Y N 394 
TYR CZ   C  Y N 395 
TYR OH   O  N N 396 
TYR OXT  O  N N 397 
TYR H    H  N N 398 
TYR H2   H  N N 399 
TYR HA   H  N N 400 
TYR HB2  H  N N 401 
TYR HB3  H  N N 402 
TYR HD1  H  N N 403 
TYR HD2  H  N N 404 
TYR HE1  H  N N 405 
TYR HE2  H  N N 406 
TYR HH   H  N N 407 
TYR HXT  H  N N 408 
VAL N    N  N N 409 
VAL CA   C  N S 410 
VAL C    C  N N 411 
VAL O    O  N N 412 
VAL CB   C  N N 413 
VAL CG1  C  N N 414 
VAL CG2  C  N N 415 
VAL OXT  O  N N 416 
VAL H    H  N N 417 
VAL H2   H  N N 418 
VAL HA   H  N N 419 
VAL HB   H  N N 420 
VAL HG11 H  N N 421 
VAL HG12 H  N N 422 
VAL HG13 H  N N 423 
VAL HG21 H  N N 424 
VAL HG22 H  N N 425 
VAL HG23 H  N N 426 
VAL HXT  H  N N 427 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
R9D O1  C1   doub N N 286 
R9D C3  C4   sing N N 287 
R9D C3  C2   sing N N 288 
R9D N   C2   sing N N 289 
R9D C5  C4   doub Y N 290 
R9D C5  C6   sing Y N 291 
R9D C1  C2   sing N N 292 
R9D C1  O    sing N N 293 
R9D C4  C9   sing Y N 294 
R9D C6  C7   doub Y N 295 
R9D O   C    sing N N 296 
R9D C9  C8   doub Y N 297 
R9D C7  C8   sing Y N 298 
R9D C7  F    sing N N 299 
R9D C5  H1   sing N N 300 
R9D C6  H2   sing N N 301 
R9D C8  H3   sing N N 302 
R9D C9  H4   sing N N 303 
R9D C3  H5   sing N N 304 
R9D C3  H6   sing N N 305 
R9D C2  H7   sing N N 306 
R9D N   H8   sing N N 307 
R9D N   H9   sing N N 308 
R9D C   H11  sing N N 309 
R9D C   H12  sing N N 310 
R9D C   H13  sing N N 311 
SER N   CA   sing N N 312 
SER N   H    sing N N 313 
SER N   H2   sing N N 314 
SER CA  C    sing N N 315 
SER CA  CB   sing N N 316 
SER CA  HA   sing N N 317 
SER C   O    doub N N 318 
SER C   OXT  sing N N 319 
SER CB  OG   sing N N 320 
SER CB  HB2  sing N N 321 
SER CB  HB3  sing N N 322 
SER OG  HG   sing N N 323 
SER OXT HXT  sing N N 324 
THR N   CA   sing N N 325 
THR N   H    sing N N 326 
THR N   H2   sing N N 327 
THR CA  C    sing N N 328 
THR CA  CB   sing N N 329 
THR CA  HA   sing N N 330 
THR C   O    doub N N 331 
THR C   OXT  sing N N 332 
THR CB  OG1  sing N N 333 
THR CB  CG2  sing N N 334 
THR CB  HB   sing N N 335 
THR OG1 HG1  sing N N 336 
THR CG2 HG21 sing N N 337 
THR CG2 HG22 sing N N 338 
THR CG2 HG23 sing N N 339 
THR OXT HXT  sing N N 340 
TRP N   CA   sing N N 341 
TRP N   H    sing N N 342 
TRP N   H2   sing N N 343 
TRP CA  C    sing N N 344 
TRP CA  CB   sing N N 345 
TRP CA  HA   sing N N 346 
TRP C   O    doub N N 347 
TRP C   OXT  sing N N 348 
TRP CB  CG   sing N N 349 
TRP CB  HB2  sing N N 350 
TRP CB  HB3  sing N N 351 
TRP CG  CD1  doub Y N 352 
TRP CG  CD2  sing Y N 353 
TRP CD1 NE1  sing Y N 354 
TRP CD1 HD1  sing N N 355 
TRP CD2 CE2  doub Y N 356 
TRP CD2 CE3  sing Y N 357 
TRP NE1 CE2  sing Y N 358 
TRP NE1 HE1  sing N N 359 
TRP CE2 CZ2  sing Y N 360 
TRP CE3 CZ3  doub Y N 361 
TRP CE3 HE3  sing N N 362 
TRP CZ2 CH2  doub Y N 363 
TRP CZ2 HZ2  sing N N 364 
TRP CZ3 CH2  sing Y N 365 
TRP CZ3 HZ3  sing N N 366 
TRP CH2 HH2  sing N N 367 
TRP OXT HXT  sing N N 368 
TYR N   CA   sing N N 369 
TYR N   H    sing N N 370 
TYR N   H2   sing N N 371 
TYR CA  C    sing N N 372 
TYR CA  CB   sing N N 373 
TYR CA  HA   sing N N 374 
TYR C   O    doub N N 375 
TYR C   OXT  sing N N 376 
TYR CB  CG   sing N N 377 
TYR CB  HB2  sing N N 378 
TYR CB  HB3  sing N N 379 
TYR CG  CD1  doub Y N 380 
TYR CG  CD2  sing Y N 381 
TYR CD1 CE1  sing Y N 382 
TYR CD1 HD1  sing N N 383 
TYR CD2 CE2  doub Y N 384 
TYR CD2 HD2  sing N N 385 
TYR CE1 CZ   doub Y N 386 
TYR CE1 HE1  sing N N 387 
TYR CE2 CZ   sing Y N 388 
TYR CE2 HE2  sing N N 389 
TYR CZ  OH   sing N N 390 
TYR OH  HH   sing N N 391 
TYR OXT HXT  sing N N 392 
VAL N   CA   sing N N 393 
VAL N   H    sing N N 394 
VAL N   H2   sing N N 395 
VAL CA  C    sing N N 396 
VAL CA  CB   sing N N 397 
VAL CA  HA   sing N N 398 
VAL C   O    doub N N 399 
VAL C   OXT  sing N N 400 
VAL CB  CG1  sing N N 401 
VAL CB  CG2  sing N N 402 
VAL CB  HB   sing N N 403 
VAL CG1 HG11 sing N N 404 
VAL CG1 HG12 sing N N 405 
VAL CG1 HG13 sing N N 406 
VAL CG2 HG21 sing N N 407 
VAL CG2 HG22 sing N N 408 
VAL CG2 HG23 sing N N 409 
VAL OXT HXT  sing N N 410 
# 
_pdbx_audit_support.ordinal                1 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           871037 
# 
_pdbx_deposit_group.group_id            G_1002335 
_pdbx_deposit_group.group_description   
;Main Protease (SARS-CoV-2) complexed with fragments of the F2X-Entry Screen in the orthorhombic space group. PanDDA analysis of F2X-Entry Screen vs. the main protease of SARS-CoV-2, including auto-refined models with ligands placed according to PanDDA-map. The event maps are included in the mmcif and are the determining evidence for the ligands. 2Fo-Fc and Fo-Fc maps will be mostly not useful to consider here.
;
_pdbx_deposit_group.group_title         
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragments from the F2X-Entry Screen in orthorhombic space group
;
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.accession_code   7BB2 
_pdbx_initial_refinement_model.source_name      PDB 
# 
_atom_sites.entry_id                    7I18 
_atom_sites.fract_transf_matrix[1][1]   0.014695 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010073 
_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]   0.009662 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1   ? -13.672 -9.679  -12.449 1.00 45.48  ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -13.631 -9.034  -13.774 1.00 45.92  ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -12.680 -7.823  -13.736 1.00 45.12  ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -11.801 -7.776  -12.832 1.00 41.12  ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -15.040 -8.672  -14.221 1.00 52.02  ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -15.582 -7.623  -13.426 1.00 51.21  ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -12.854 -6.881  -14.673 1.00 40.40  ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -11.902 -5.797  -14.984 1.00 39.13  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -10.963 -6.240  -16.084 1.00 39.59  ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -10.918 -7.442  -16.387 1.00 41.40  ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -10.268 -5.304  -16.716 1.00 39.78  ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -9.309  -5.620  -17.799 1.00 39.02  ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -8.216  -4.553  -17.808 1.00 39.24  ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -8.513  -3.361  -17.941 1.00 39.94  ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -10.028 -5.781  -19.140 1.00 40.52  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -9.253  -6.612  -20.128 1.00 38.12  ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -9.225  -7.990  -20.016 1.00 38.20  ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -8.521  -6.012  -21.147 1.00 38.20  ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -8.506  -8.759  -20.919 1.00 37.91  ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -7.799  -6.777  -22.047 1.00 37.69  ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -7.789  -8.153  -21.929 1.00 39.09  ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? -6.976  -4.986  -17.613 1.00 36.68  ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -5.820  -4.088  -17.418 1.00 35.50  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? -4.666  -4.563  -18.286 1.00 33.79  ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? -4.487  -5.803  -18.414 1.00 32.87  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -5.405  -4.101  -15.946 1.00 37.29  ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -6.308  -3.277  -15.039 1.00 39.31  ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -5.851  -1.834  -15.068 1.00 43.66  ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -6.505  -0.990  -14.080 1.00 48.57  ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -6.345  0.332   -14.021 1.00 54.67  ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -5.524  0.931   -14.868 1.00 59.93  ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.991  1.056   -13.120 1.00 50.58  ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? -3.892  -3.604  -18.797 1.00 36.40  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? -2.481  -3.809  -19.222 1.00 37.50  ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? -1.686  -4.430  -18.074 1.00 36.20  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? -1.302  -3.707  -17.148 1.00 42.06  ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? -1.818  -2.487  -19.575 1.00 39.55  ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? -1.986  -2.092  -21.016 1.00 44.22  ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? -1.339  -3.066  -21.968 1.00 45.51  ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? -1.801  -2.823  -23.387 1.00 47.80  ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? -1.828  -1.376  -23.715 1.00 46.79  ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? -1.464  -5.728  -18.139 1.00 32.33  ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? -0.920  -6.514  -17.010 1.00 32.49  ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 0.420   -7.102  -17.447 1.00 28.62  ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 0.461   -7.838  -18.447 1.00 29.29  ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? -1.908  -7.629  -16.669 1.00 33.59  ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? -1.630  -8.298  -15.363 1.00 41.26  ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? -2.856  -9.580  -15.022 1.00 45.90  ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? -4.294  -8.566  -14.709 1.00 38.06  ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 1.479   -6.768  -16.735 1.00 28.63  ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 2.837   -7.277  -17.004 1.00 29.03  ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 3.053   -8.561  -16.189 1.00 28.78  ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.284   -8.812  -15.236 1.00 24.75  ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 3.851   -6.200  -16.677 1.00 27.68  ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 4.090   -9.332  -16.503 1.00 26.26  ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.466   -10.493 -15.660 1.00 26.57  ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 5.159   -9.979  -14.418 1.00 25.18  ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 5.791   -8.931  -14.465 1.00 25.48  ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 5.330   -11.496 -16.415 1.00 27.17  ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 4.496   -12.318 -17.356 1.00 28.81  ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 3.745   -13.384 -16.890 1.00 29.95  ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 4.404   -11.971 -18.689 1.00 28.89  ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 2.955   -14.127 -17.756 1.00 32.25  ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 3.622   -12.716 -19.557 1.00 30.26  ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 2.896   -13.792 -19.091 1.00 32.72  ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 5.023   -10.694 -13.278 1.00 24.46  ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 5.806   -10.391 -12.086 1.00 24.57  ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 7.304   -10.409 -12.459 1.00 24.81  ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 7.736   -11.344 -13.080 1.00 24.50  ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 5.486   -11.520 -11.095 1.00 25.50  ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 4.224   -12.178 -11.647 1.00 27.07  ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 4.188   -11.891 -13.131 1.00 25.20  ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 8.042   -9.365  -12.101 1.00 24.74  ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 9.376   -9.061  -12.669 1.00 23.51  ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 10.499  -9.695  -11.835 1.00 24.78  ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 11.666  -9.619  -12.268 1.00 25.52  ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 9.537   -7.587  -12.766 1.00 22.10  ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 9.397   -7.007  -11.479 1.00 22.61  ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 10.184  -10.305 -10.690 1.00 25.05  ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 11.199  -10.754 -9.702  1.00 25.63  ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 12.259  -11.672 -10.312 1.00 26.77  ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 13.439  -11.425 -10.069 1.00 24.51  ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 11.854  -12.696 -11.071 1.00 26.11  ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 12.773  -13.677 -11.707 1.00 32.04  ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 13.755  -12.967 -12.651 1.00 31.19  ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 14.847  -13.496 -12.844 1.00 33.89  ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 11.996  -14.721 -12.515 1.00 33.49  ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 11.270  -15.764 -11.675 1.00 36.20  ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 10.691  -16.897 -12.495 1.00 38.87  ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 10.079  -17.969 -11.625 1.00 42.26  ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 9.165   -17.357 -10.635 1.00 45.32  ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 13.363  -11.837 -13.240 1.00 28.21  ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 14.235  -11.054 -14.158 1.00 29.32  ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 15.085  -10.098 -13.336 1.00 26.78  ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 16.258  -9.932  -13.704 1.00 24.29  ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 13.453  -10.318 -15.263 1.00 28.53  ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 14.373  -9.499  -16.178 1.00 30.36  ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 12.637  -11.293 -16.085 1.00 28.04  ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 14.506  -9.483  -12.298 1.00 27.70  ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 15.238  -8.576  -11.380 1.00 26.83  ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 16.536  -9.244  -10.901 1.00 28.01  ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 17.550  -8.562  -10.841 1.00 29.21  ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 14.367  -8.213  -10.180 1.00 28.36  ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 13.233  -7.258  -10.517 1.00 30.21  ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? 12.298  -7.028  -9.346  1.00 27.38  ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? 12.803  -6.690  -8.294  1.00 28.78  ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? 11.079  -7.167  -9.507  1.00 27.22  ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 16.509  -10.533 -10.576 1.00 28.90  ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 17.669  -11.234 -9.997  1.00 32.70  ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 18.761  -11.474 -11.030 1.00 33.30  ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 19.791  -12.024 -10.652 1.00 33.97  ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 18.542  -11.103 -12.297 1.00 33.08  ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 19.508  -11.332 -13.403 1.00 31.84  ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 20.160  -10.022 -13.871 1.00 31.27  ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 21.105  -10.093 -14.727 1.00 25.72  ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 18.824  -11.977 -14.594 1.00 33.26  ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 18.089  -13.580 -14.230 1.00 34.85  ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 19.694  -8.871  -13.375 1.00 27.62  ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 20.094  -7.557  -13.947 1.00 28.36  ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 21.408  -7.091  -13.301 1.00 27.59  ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 21.508  -7.072  -12.076 1.00 26.89  ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 19.020  -6.472  -13.782 1.00 27.07  ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 17.718  -6.715  -14.554 1.00 27.31  ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 17.830  -7.279  -16.276 1.00 29.20  ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 18.827  -5.977  -17.002 1.00 26.79  ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 22.378  -6.700  -14.119 1.00 28.84  ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 23.711  -6.209  -13.664 1.00 29.29  ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 24.065  -4.977  -14.482 1.00 31.68  ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 23.382  -4.704  -15.499 1.00 31.73  ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 24.799  -7.295  -13.798 1.00 29.69  ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 24.482  -8.514  -12.942 1.00 29.06  ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 25.022  -7.723  -15.250 1.00 28.92  ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 25.068  -4.254  -14.002 1.00 32.19  ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 25.642  -3.059  -14.647 1.00 33.26  ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 26.895  -3.502  -15.407 1.00 35.01  ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 27.682  -4.279  -14.834 1.00 32.37  ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 25.936  -2.030  -13.562 1.00 36.70  ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 26.349  -0.684  -14.108 1.00 37.44  ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 26.657  0.244   -12.963 1.00 42.52  ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 26.049  1.300   -12.825 1.00 45.99  ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 27.621  -0.150  -12.141 1.00 40.75  ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 27.013  -3.116  -16.682 1.00 32.42  ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 28.219  -3.370  -17.514 1.00 30.46  ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 28.808  -2.016  -17.888 1.00 33.30  ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 28.068  -1.152  -18.419 1.00 32.40  ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 27.924  -4.238  -18.757 1.00 30.70  ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 29.177  -4.483  -19.587 1.00 29.68  ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 27.291  -5.567  -18.367 1.00 30.25  ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 30.096  -1.847  -17.595 1.00 33.16  ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 30.882  -0.659  -17.983 1.00 34.35  ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 32.025  -1.082  -18.924 1.00 36.16  ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 32.667  -2.143  -18.713 1.00 32.22  ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 31.371  0.108   -16.755 1.00 39.62  ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 30.263  0.340   -15.875 1.00 35.82  ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 32.019  1.420   -17.142 1.00 39.45  ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 32.250  -0.286  -19.962 1.00 37.66  ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 33.400  -0.420  -20.892 1.00 39.93  ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 33.739  0.988   -21.356 1.00 41.28  ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 32.811  1.688   -21.802 1.00 37.52  ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 33.053  -1.330  -22.063 1.00 38.19  ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 34.437  -1.649  -23.182 1.00 44.95  ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 34.997  1.406   -21.218 1.00 40.26  ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 35.375  2.808   -21.454 1.00 35.92  ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 34.607  3.700   -20.508 1.00 37.40  ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 34.561  3.382   -19.305 1.00 39.92  ? 23  GLY A O   1 
ATOM   166  N  N   . THR A 1 24  ? 33.961  4.742   -21.027 1.00 39.64  ? 24  THR A N   1 
ATOM   167  C  CA  . THR A 1 24  ? 33.109  5.667   -20.239 1.00 40.38  ? 24  THR A CA  1 
ATOM   168  C  C   . THR A 1 24  ? 31.603  5.306   -20.323 1.00 39.83  ? 24  THR A C   1 
ATOM   169  O  O   . THR A 1 24  ? 30.786  6.047   -19.760 1.00 38.01  ? 24  THR A O   1 
ATOM   170  C  CB  . THR A 1 24  ? 33.350  7.117   -20.690 1.00 42.24  ? 24  THR A CB  1 
ATOM   171  O  OG1 . THR A 1 24  ? 32.991  7.247   -22.062 1.00 46.53  ? 24  THR A OG1 1 
ATOM   172  C  CG2 . THR A 1 24  ? 34.788  7.563   -20.523 1.00 46.97  ? 24  THR A CG2 1 
ATOM   173  N  N   A THR A 1 25  ? 31.262  4.208   -21.013 0.25 38.59  ? 25  THR A N   1 
ATOM   174  N  N   B THR A 1 25  ? 31.262  4.208   -21.013 0.25 38.59  ? 25  THR A N   1 
ATOM   175  N  N   C THR A 1 25  ? 31.254  4.205   -20.996 0.25 38.47  ? 25  THR A N   1 
ATOM   176  N  N   D THR A 1 25  ? 31.254  4.205   -20.996 0.25 38.47  ? 25  THR A N   1 
ATOM   177  C  CA  A THR A 1 25  ? 29.864  3.778   -21.302 0.25 38.35  ? 25  THR A CA  1 
ATOM   178  C  CA  B THR A 1 25  ? 29.864  3.778   -21.302 0.25 38.35  ? 25  THR A CA  1 
ATOM   179  C  CA  C THR A 1 25  ? 29.846  3.818   -21.286 0.25 38.16  ? 25  THR A CA  1 
ATOM   180  C  CA  D THR A 1 25  ? 29.846  3.818   -21.286 0.25 38.16  ? 25  THR A CA  1 
ATOM   181  C  C   A THR A 1 25  ? 29.400  2.754   -20.260 0.25 36.85  ? 25  THR A C   1 
ATOM   182  C  C   B THR A 1 25  ? 29.400  2.754   -20.260 0.25 36.85  ? 25  THR A C   1 
ATOM   183  C  C   C THR A 1 25  ? 29.379  2.748   -20.294 0.25 36.74  ? 25  THR A C   1 
ATOM   184  C  C   D THR A 1 25  ? 29.379  2.748   -20.294 0.25 36.74  ? 25  THR A C   1 
ATOM   185  O  O   A THR A 1 25  ? 30.094  1.737   -20.080 0.25 35.68  ? 25  THR A O   1 
ATOM   186  O  O   B THR A 1 25  ? 30.094  1.737   -20.080 0.25 35.68  ? 25  THR A O   1 
ATOM   187  O  O   C THR A 1 25  ? 30.046  1.702   -20.184 0.25 35.35  ? 25  THR A O   1 
ATOM   188  O  O   D THR A 1 25  ? 30.046  1.702   -20.184 0.25 35.35  ? 25  THR A O   1 
ATOM   189  C  CB  A THR A 1 25  ? 29.723  3.174   -22.707 0.25 39.02  ? 25  THR A CB  1 
ATOM   190  C  CB  B THR A 1 25  ? 29.723  3.174   -22.707 0.25 39.02  ? 25  THR A CB  1 
ATOM   191  C  CB  C THR A 1 25  ? 29.679  3.363   -22.741 0.25 38.67  ? 25  THR A CB  1 
ATOM   192  C  CB  D THR A 1 25  ? 29.679  3.363   -22.741 0.25 38.67  ? 25  THR A CB  1 
ATOM   193  O  OG1 A THR A 1 25  ? 30.403  4.006   -23.646 0.25 40.45  ? 25  THR A OG1 1 
ATOM   194  O  OG1 B THR A 1 25  ? 30.403  4.006   -23.646 0.25 40.45  ? 25  THR A OG1 1 
ATOM   195  O  OG1 C THR A 1 25  ? 30.160  4.431   -23.557 0.25 40.12  ? 25  THR A OG1 1 
ATOM   196  O  OG1 D THR A 1 25  ? 30.160  4.431   -23.557 0.25 40.12  ? 25  THR A OG1 1 
ATOM   197  C  CG2 A THR A 1 25  ? 28.278  3.013   -23.126 0.25 38.45  ? 25  THR A CG2 1 
ATOM   198  C  CG2 B THR A 1 25  ? 28.278  3.013   -23.126 0.25 38.45  ? 25  THR A CG2 1 
ATOM   199  C  CG2 C THR A 1 25  ? 28.245  3.036   -23.097 0.25 38.18  ? 25  THR A CG2 1 
ATOM   200  C  CG2 D THR A 1 25  ? 28.245  3.036   -23.097 0.25 38.18  ? 25  THR A CG2 1 
ATOM   201  N  N   . THR A 1 26  ? 28.247  3.010   -19.636 1.00 36.89  ? 26  THR A N   1 
ATOM   202  C  CA  . THR A 1 26  ? 27.601  2.097   -18.673 1.00 34.69  ? 26  THR A CA  1 
ATOM   203  C  C   . THR A 1 26  ? 26.170  1.822   -19.151 1.00 31.49  ? 26  THR A C   1 
ATOM   204  O  O   . THR A 1 26  ? 25.429  2.754   -19.504 1.00 29.80  ? 26  THR A O   1 
ATOM   205  C  CB  . THR A 1 26  ? 27.609  2.678   -17.252 1.00 34.76  ? 26  THR A CB  1 
ATOM   206  O  OG1 . THR A 1 26  ? 28.959  2.807   -16.807 1.00 39.94  ? 26  THR A OG1 1 
ATOM   207  C  CG2 . THR A 1 26  ? 26.885  1.796   -16.264 1.00 37.40  ? 26  THR A CG2 1 
ATOM   208  N  N   A LEU A 1 27  ? 25.783  0.547   -19.145 0.25 30.07  ? 27  LEU A N   1 
ATOM   209  N  N   B LEU A 1 27  ? 25.783  0.547   -19.145 0.25 30.07  ? 27  LEU A N   1 
ATOM   210  N  N   C LEU A 1 27  ? 25.795  0.543   -19.164 0.25 30.63  ? 27  LEU A N   1 
ATOM   211  N  N   D LEU A 1 27  ? 25.795  0.543   -19.164 0.25 30.63  ? 27  LEU A N   1 
ATOM   212  C  CA  A LEU A 1 27  ? 24.394  0.110   -19.432 0.25 29.81  ? 27  LEU A CA  1 
ATOM   213  C  CA  B LEU A 1 27  ? 24.394  0.110   -19.432 0.25 29.81  ? 27  LEU A CA  1 
ATOM   214  C  CA  C LEU A 1 27  ? 24.414  0.089   -19.458 0.25 30.64  ? 27  LEU A CA  1 
ATOM   215  C  CA  D LEU A 1 27  ? 24.414  0.089   -19.458 0.25 30.64  ? 27  LEU A CA  1 
ATOM   216  C  C   A LEU A 1 27  ? 24.095  -1.166  -18.638 0.25 29.23  ? 27  LEU A C   1 
ATOM   217  C  C   B LEU A 1 27  ? 24.095  -1.166  -18.638 0.25 29.23  ? 27  LEU A C   1 
ATOM   218  C  C   C LEU A 1 27  ? 24.169  -1.250  -18.750 0.25 30.00  ? 27  LEU A C   1 
ATOM   219  C  C   D LEU A 1 27  ? 24.169  -1.250  -18.750 0.25 30.00  ? 27  LEU A C   1 
ATOM   220  O  O   A LEU A 1 27  ? 24.867  -1.471  -17.700 0.25 29.49  ? 27  LEU A O   1 
ATOM   221  O  O   B LEU A 1 27  ? 24.867  -1.471  -17.700 0.25 29.49  ? 27  LEU A O   1 
ATOM   222  O  O   C LEU A 1 27  ? 25.062  -1.696  -17.993 0.25 31.00  ? 27  LEU A O   1 
ATOM   223  O  O   D LEU A 1 27  ? 25.062  -1.696  -17.993 0.25 31.00  ? 27  LEU A O   1 
ATOM   224  C  CB  A LEU A 1 27  ? 24.213  -0.063  -20.945 0.25 28.80  ? 27  LEU A CB  1 
ATOM   225  C  CB  B LEU A 1 27  ? 24.213  -0.063  -20.945 0.25 28.80  ? 27  LEU A CB  1 
ATOM   226  C  CB  C LEU A 1 27  ? 24.209  0.029   -20.978 0.25 30.06  ? 27  LEU A CB  1 
ATOM   227  C  CB  D LEU A 1 27  ? 24.209  0.029   -20.978 0.25 30.06  ? 27  LEU A CB  1 
ATOM   228  C  CG  A LEU A 1 27  ? 25.350  -0.728  -21.720 0.25 28.99  ? 27  LEU A CG  1 
ATOM   229  C  CG  B LEU A 1 27  ? 25.350  -0.728  -21.720 0.25 28.99  ? 27  LEU A CG  1 
ATOM   230  C  CG  C LEU A 1 27  ? 25.298  -0.652  -21.806 0.25 30.65  ? 27  LEU A CG  1 
ATOM   231  C  CG  D LEU A 1 27  ? 25.298  -0.652  -21.806 0.25 30.65  ? 27  LEU A CG  1 
ATOM   232  C  CD1 A LEU A 1 27  ? 25.447  -2.218  -21.417 0.25 28.55  ? 27  LEU A CD1 1 
ATOM   233  C  CD1 B LEU A 1 27  ? 25.447  -2.218  -21.417 0.25 28.55  ? 27  LEU A CD1 1 
ATOM   234  C  CD1 C LEU A 1 27  ? 25.247  -2.168  -21.662 0.25 30.66  ? 27  LEU A CD1 1 
ATOM   235  C  CD1 D LEU A 1 27  ? 25.247  -2.168  -21.662 0.25 30.66  ? 27  LEU A CD1 1 
ATOM   236  C  CD2 A LEU A 1 27  ? 25.154  -0.506  -23.214 0.25 29.65  ? 27  LEU A CD2 1 
ATOM   237  C  CD2 B LEU A 1 27  ? 25.154  -0.506  -23.214 0.25 29.65  ? 27  LEU A CD2 1 
ATOM   238  C  CD2 C LEU A 1 27  ? 25.169  -0.257  -23.273 0.25 31.34  ? 27  LEU A CD2 1 
ATOM   239  C  CD2 D LEU A 1 27  ? 25.169  -0.257  -23.273 0.25 31.34  ? 27  LEU A CD2 1 
ATOM   240  N  N   . ASN A 1 28  ? 22.996  -1.846  -18.973 1.00 28.56  ? 28  ASN A N   1 
ATOM   241  C  CA  . ASN A 1 28  ? 22.534  -3.061  -18.265 1.00 28.22  ? 28  ASN A CA  1 
ATOM   242  C  C   . ASN A 1 28  ? 22.969  -4.318  -19.002 1.00 26.27  ? 28  ASN A C   1 
ATOM   243  O  O   . ASN A 1 28  ? 23.008  -4.329  -20.250 1.00 26.77  ? 28  ASN A O   1 
ATOM   244  C  CB  . ASN A 1 28  ? 21.008  -3.023  -18.105 1.00 26.61  ? 28  ASN A CB  1 
ATOM   245  C  CG  . ASN A 1 28  ? 20.568  -1.699  -17.524 1.00 27.87  ? 28  ASN A CG  1 
ATOM   246  O  OD1 . ASN A 1 28  ? 20.790  -1.463  -16.335 1.00 27.11  ? 28  ASN A OD1 1 
ATOM   247  N  ND2 . ASN A 1 28  ? 19.996  -0.824  -18.354 1.00 24.29  ? 28  ASN A ND2 1 
ATOM   248  N  N   . GLY A 1 29  ? 23.212  -5.374  -18.236 1.00 24.12  ? 29  GLY A N   1 
ATOM   249  C  CA  . GLY A 1 29  ? 23.409  -6.720  -18.787 1.00 22.79  ? 29  GLY A CA  1 
ATOM   250  C  C   . GLY A 1 29  ? 22.542  -7.735  -18.083 1.00 23.95  ? 29  GLY A C   1 
ATOM   251  O  O   . GLY A 1 29  ? 22.006  -7.460  -16.993 1.00 25.48  ? 29  GLY A O   1 
ATOM   252  N  N   . LEU A 1 30  ? 22.402  -8.891  -18.701 1.00 27.16  ? 30  LEU A N   1 
ATOM   253  C  CA  . LEU A 1 30  ? 21.508  -9.957  -18.218 1.00 30.24  ? 30  LEU A CA  1 
ATOM   254  C  C   . LEU A 1 30  ? 22.368  -11.178 -17.879 1.00 30.69  ? 30  LEU A C   1 
ATOM   255  O  O   . LEU A 1 30  ? 23.013  -11.723 -18.788 1.00 29.00  ? 30  LEU A O   1 
ATOM   256  C  CB  . LEU A 1 30  ? 20.493  -10.254 -19.313 1.00 28.20  ? 30  LEU A CB  1 
ATOM   257  C  CG  . LEU A 1 30  ? 19.532  -11.375 -18.957 1.00 29.92  ? 30  LEU A CG  1 
ATOM   258  C  CD1 . LEU A 1 30  ? 18.494  -10.893 -17.947 1.00 32.15  ? 30  LEU A CD1 1 
ATOM   259  C  CD2 . LEU A 1 30  ? 18.873  -11.910 -20.195 1.00 27.30  ? 30  LEU A CD2 1 
ATOM   260  N  N   . TRP A 1 31  ? 22.406  -11.531 -16.597 1.00 31.75  ? 31  TRP A N   1 
ATOM   261  C  CA  . TRP A 1 31  ? 23.329  -12.525 -16.002 1.00 31.86  ? 31  TRP A CA  1 
ATOM   262  C  C   . TRP A 1 31  ? 22.567  -13.830 -15.820 1.00 32.76  ? 31  TRP A C   1 
ATOM   263  O  O   . TRP A 1 31  ? 21.675  -13.897 -14.926 1.00 31.31  ? 31  TRP A O   1 
ATOM   264  C  CB  . TRP A 1 31  ? 23.909  -11.970 -14.697 1.00 36.19  ? 31  TRP A CB  1 
ATOM   265  C  CG  . TRP A 1 31  ? 24.861  -12.861 -13.962 1.00 38.70  ? 31  TRP A CG  1 
ATOM   266  C  CD1 . TRP A 1 31  ? 25.621  -13.879 -14.461 1.00 43.07  ? 31  TRP A CD1 1 
ATOM   267  C  CD2 . TRP A 1 31  ? 25.166  -12.789 -12.560 1.00 37.51  ? 31  TRP A CD2 1 
ATOM   268  N  NE1 . TRP A 1 31  ? 26.374  -14.450 -13.464 1.00 41.46  ? 31  TRP A NE1 1 
ATOM   269  C  CE2 . TRP A 1 31  ? 26.120  -13.796 -12.287 1.00 41.11  ? 31  TRP A CE2 1 
ATOM   270  C  CE3 . TRP A 1 31  ? 24.724  -11.974 -11.516 1.00 40.44  ? 31  TRP A CE3 1 
ATOM   271  C  CZ2 . TRP A 1 31  ? 26.626  -14.012 -11.008 1.00 41.29  ? 31  TRP A CZ2 1 
ATOM   272  C  CZ3 . TRP A 1 31  ? 25.229  -12.182 -10.250 1.00 39.87  ? 31  TRP A CZ3 1 
ATOM   273  C  CH2 . TRP A 1 31  ? 26.166  -13.191 -10.002 1.00 40.05  ? 31  TRP A CH2 1 
ATOM   274  N  N   . LEU A 1 32  ? 22.846  -14.788 -16.702 1.00 28.89  ? 32  LEU A N   1 
ATOM   275  C  CA  . LEU A 1 32  ? 22.240  -16.137 -16.692 1.00 32.03  ? 32  LEU A CA  1 
ATOM   276  C  C   . LEU A 1 32  ? 23.364  -17.174 -16.653 1.00 34.83  ? 32  LEU A C   1 
ATOM   277  O  O   . LEU A 1 32  ? 24.326  -17.013 -17.418 1.00 30.48  ? 32  LEU A O   1 
ATOM   278  C  CB  . LEU A 1 32  ? 21.384  -16.293 -17.942 1.00 34.40  ? 32  LEU A CB  1 
ATOM   279  C  CG  . LEU A 1 32  ? 20.291  -15.241 -18.109 1.00 33.65  ? 32  LEU A CG  1 
ATOM   280  C  CD1 . LEU A 1 32  ? 19.755  -15.272 -19.529 1.00 33.83  ? 32  LEU A CD1 1 
ATOM   281  C  CD2 . LEU A 1 32  ? 19.179  -15.467 -17.088 1.00 31.72  ? 32  LEU A CD2 1 
ATOM   282  N  N   . ASP A 1 33  ? 23.249  -18.169 -15.767 1.00 37.38  ? 33  ASP A N   1 
ATOM   283  C  CA  . ASP A 1 33  ? 24.328  -19.148 -15.460 1.00 36.42  ? 33  ASP A CA  1 
ATOM   284  C  C   . ASP A 1 33  ? 25.636  -18.334 -15.346 1.00 35.05  ? 33  ASP A C   1 
ATOM   285  O  O   . ASP A 1 33  ? 25.644  -17.355 -14.587 1.00 35.21  ? 33  ASP A O   1 
ATOM   286  C  CB  . ASP A 1 33  ? 24.276  -20.297 -16.467 1.00 37.57  ? 33  ASP A CB  1 
ATOM   287  C  CG  . ASP A 1 33  ? 22.905  -20.965 -16.588 1.00 41.91  ? 33  ASP A CG  1 
ATOM   288  O  OD1 . ASP A 1 33  ? 22.359  -21.417 -15.554 1.00 48.36  ? 33  ASP A OD1 1 
ATOM   289  O  OD2 . ASP A 1 33  ? 22.397  -21.064 -17.733 1.00 47.51  ? 33  ASP A OD2 1 
ATOM   290  N  N   . ASP A 1 34  ? 26.681  -18.614 -16.122 1.00 33.71  ? 34  ASP A N   1 
ATOM   291  C  CA  . ASP A 1 34  ? 27.975  -17.890 -15.980 1.00 34.54  ? 34  ASP A CA  1 
ATOM   292  C  C   . ASP A 1 34  ? 28.206  -16.878 -17.112 1.00 39.85  ? 34  ASP A C   1 
ATOM   293  O  O   . ASP A 1 34  ? 29.394  -16.522 -17.348 1.00 35.44  ? 34  ASP A O   1 
ATOM   294  C  CB  . ASP A 1 34  ? 29.149  -18.865 -15.945 1.00 38.62  ? 34  ASP A CB  1 
ATOM   295  C  CG  . ASP A 1 34  ? 29.308  -19.765 -17.164 1.00 39.48  ? 34  ASP A CG  1 
ATOM   296  O  OD1 . ASP A 1 34  ? 28.332  -19.933 -17.925 1.00 38.54  ? 34  ASP A OD1 1 
ATOM   297  O  OD2 . ASP A 1 34  ? 30.413  -20.344 -17.312 1.00 51.17  ? 34  ASP A OD2 1 
ATOM   298  N  N   . VAL A 1 35  ? 27.136  -16.379 -17.748 1.00 38.01  ? 35  VAL A N   1 
ATOM   299  C  CA  . VAL A 1 35  ? 27.214  -15.447 -18.917 1.00 35.81  ? 35  VAL A CA  1 
ATOM   300  C  C   . VAL A 1 35  ? 26.425  -14.163 -18.631 1.00 33.90  ? 35  VAL A C   1 
ATOM   301  O  O   . VAL A 1 35  ? 25.281  -14.235 -18.111 1.00 32.26  ? 35  VAL A O   1 
ATOM   302  C  CB  . VAL A 1 35  ? 26.718  -16.129 -20.205 1.00 36.95  ? 35  VAL A CB  1 
ATOM   303  C  CG1 . VAL A 1 35  ? 26.789  -15.191 -21.393 1.00 37.83  ? 35  VAL A CG1 1 
ATOM   304  C  CG2 . VAL A 1 35  ? 27.496  -17.407 -20.502 1.00 37.29  ? 35  VAL A CG2 1 
ATOM   305  N  N   . VAL A 1 36  ? 27.037  -13.018 -18.931 1.00 32.69  ? 36  VAL A N   1 
ATOM   306  C  CA  . VAL A 1 36  ? 26.363  -11.694 -18.925 1.00 29.57  ? 36  VAL A CA  1 
ATOM   307  C  C   . VAL A 1 36  ? 26.164  -11.305 -20.388 1.00 31.72  ? 36  VAL A C   1 
ATOM   308  O  O   . VAL A 1 36  ? 27.175  -11.228 -21.124 1.00 33.10  ? 36  VAL A O   1 
ATOM   309  C  CB  . VAL A 1 36  ? 27.139  -10.633 -18.127 1.00 32.27  ? 36  VAL A CB  1 
ATOM   310  C  CG1 . VAL A 1 36  ? 26.597  -9.225  -18.353 1.00 33.49  ? 36  VAL A CG1 1 
ATOM   311  C  CG2 . VAL A 1 36  ? 27.121  -10.955 -16.638 1.00 34.70  ? 36  VAL A CG2 1 
ATOM   312  N  N   . TYR A 1 37  ? 24.909  -11.120 -20.810 1.00 28.52  ? 37  TYR A N   1 
ATOM   313  C  CA  . TYR A 1 37  ? 24.543  -10.649 -22.167 1.00 27.87  ? 37  TYR A CA  1 
ATOM   314  C  C   . TYR A 1 37  ? 24.300  -9.143  -22.132 1.00 27.37  ? 37  TYR A C   1 
ATOM   315  O  O   . TYR A 1 37  ? 23.542  -8.689  -21.238 1.00 26.56  ? 37  TYR A O   1 
ATOM   316  C  CB  . TYR A 1 37  ? 23.294  -11.353 -22.674 1.00 28.91  ? 37  TYR A CB  1 
ATOM   317  C  CG  . TYR A 1 37  ? 23.378  -12.853 -22.644 1.00 30.79  ? 37  TYR A CG  1 
ATOM   318  C  CD1 . TYR A 1 37  ? 23.281  -13.551 -21.444 1.00 31.66  ? 37  TYR A CD1 1 
ATOM   319  C  CD2 . TYR A 1 37  ? 23.523  -13.578 -23.810 1.00 30.11  ? 37  TYR A CD2 1 
ATOM   320  C  CE1 . TYR A 1 37  ? 23.361  -14.931 -21.403 1.00 29.34  ? 37  TYR A CE1 1 
ATOM   321  C  CE2 . TYR A 1 37  ? 23.586  -14.962 -23.787 1.00 31.78  ? 37  TYR A CE2 1 
ATOM   322  C  CZ  . TYR A 1 37  ? 23.523  -15.636 -22.580 1.00 31.66  ? 37  TYR A CZ  1 
ATOM   323  O  OH  . TYR A 1 37  ? 23.582  -16.995 -22.589 1.00 34.10  ? 37  TYR A OH  1 
ATOM   324  N  N   . CYS A 1 38  ? 24.844  -8.402  -23.107 1.00 27.30  ? 38  CYS A N   1 
ATOM   325  C  CA  . CYS A 1 38  ? 24.571  -6.941  -23.253 1.00 27.27  ? 38  CYS A CA  1 
ATOM   326  C  C   . CYS A 1 38  ? 24.731  -6.502  -24.705 1.00 26.49  ? 38  CYS A C   1 
ATOM   327  O  O   . CYS A 1 38  ? 25.326  -7.207  -25.515 1.00 27.31  ? 38  CYS A O   1 
ATOM   328  C  CB  . CYS A 1 38  ? 25.442  -6.123  -22.312 1.00 28.24  ? 38  CYS A CB  1 
ATOM   329  S  SG  . CYS A 1 38  ? 27.193  -6.006  -22.786 1.00 31.26  ? 38  CYS A SG  1 
ATOM   330  N  N   . PRO A 1 39  ? 24.171  -5.333  -25.082 1.00 27.12  ? 39  PRO A N   1 
ATOM   331  C  CA  . PRO A 1 39  ? 24.354  -4.796  -26.430 1.00 26.24  ? 39  PRO A CA  1 
ATOM   332  C  C   . PRO A 1 39  ? 25.856  -4.633  -26.681 1.00 26.94  ? 39  PRO A C   1 
ATOM   333  O  O   . PRO A 1 39  ? 26.573  -4.147  -25.816 1.00 24.35  ? 39  PRO A O   1 
ATOM   334  C  CB  . PRO A 1 39  ? 23.652  -3.433  -26.416 1.00 26.31  ? 39  PRO A CB  1 
ATOM   335  C  CG  . PRO A 1 39  ? 22.693  -3.508  -25.220 1.00 25.84  ? 39  PRO A CG  1 
ATOM   336  C  CD  . PRO A 1 39  ? 23.376  -4.428  -24.231 1.00 26.24  ? 39  PRO A CD  1 
ATOM   337  N  N   . ARG A 1 40  ? 26.301  -5.038  -27.864 1.00 26.73  ? 40  ARG A N   1 
ATOM   338  C  CA  . ARG A 1 40  ? 27.728  -4.925  -28.224 1.00 26.66  ? 40  ARG A CA  1 
ATOM   339  C  C   . ARG A 1 40  ? 28.178  -3.457  -28.356 1.00 28.51  ? 40  ARG A C   1 
ATOM   340  O  O   . ARG A 1 40  ? 29.394  -3.223  -28.242 1.00 26.55  ? 40  ARG A O   1 
ATOM   341  C  CB  . ARG A 1 40  ? 28.062  -5.740  -29.470 1.00 24.39  ? 40  ARG A CB  1 
ATOM   342  C  CG  . ARG A 1 40  ? 27.449  -5.235  -30.763 1.00 25.12  ? 40  ARG A CG  1 
ATOM   343  C  CD  . ARG A 1 40  ? 27.915  -6.071  -31.942 1.00 24.60  ? 40  ARG A CD  1 
ATOM   344  N  NE  . ARG A 1 40  ? 27.303  -5.590  -33.177 1.00 26.82  ? 40  ARG A NE  1 
ATOM   345  C  CZ  . ARG A 1 40  ? 27.622  -5.989  -34.408 1.00 28.14  ? 40  ARG A CZ  1 
ATOM   346  N  NH1 . ARG A 1 40  ? 28.604  -6.861  -34.601 1.00 28.31  ? 40  ARG A NH1 1 
ATOM   347  N  NH2 . ARG A 1 40  ? 27.028  -5.431  -35.443 1.00 28.97  ? 40  ARG A NH2 1 
ATOM   348  N  N   A HIS A 1 41  ? 27.259  -2.511  -28.600 0.25 25.84  ? 41  HIS A N   1 
ATOM   349  N  N   B HIS A 1 41  ? 27.259  -2.511  -28.600 0.25 25.84  ? 41  HIS A N   1 
ATOM   350  N  N   C HIS A 1 41  ? 27.251  -2.503  -28.515 0.25 28.25  ? 41  HIS A N   1 
ATOM   351  N  N   D HIS A 1 41  ? 27.251  -2.503  -28.515 0.25 28.25  ? 41  HIS A N   1 
ATOM   352  C  CA  A HIS A 1 41  ? 27.611  -1.081  -28.830 0.25 25.74  ? 41  HIS A CA  1 
ATOM   353  C  CA  B HIS A 1 41  ? 27.611  -1.081  -28.830 0.25 25.74  ? 41  HIS A CA  1 
ATOM   354  C  CA  C HIS A 1 41  ? 27.581  -1.057  -28.658 0.25 29.85  ? 41  HIS A CA  1 
ATOM   355  C  CA  D HIS A 1 41  ? 27.581  -1.057  -28.658 0.25 29.85  ? 41  HIS A CA  1 
ATOM   356  C  C   A HIS A 1 41  ? 28.200  -0.451  -27.559 0.25 26.40  ? 41  HIS A C   1 
ATOM   357  C  C   B HIS A 1 41  ? 28.200  -0.451  -27.559 0.25 26.40  ? 41  HIS A C   1 
ATOM   358  C  C   C HIS A 1 41  ? 28.139  -0.471  -27.348 0.25 31.11  ? 41  HIS A C   1 
ATOM   359  C  C   D HIS A 1 41  ? 28.139  -0.471  -27.348 0.25 31.11  ? 41  HIS A C   1 
ATOM   360  O  O   A HIS A 1 41  ? 28.689  0.686   -27.666 0.25 26.48  ? 41  HIS A O   1 
ATOM   361  O  O   B HIS A 1 41  ? 28.689  0.686   -27.666 0.25 26.48  ? 41  HIS A O   1 
ATOM   362  O  O   C HIS A 1 41  ? 28.469  0.724   -27.361 0.25 32.13  ? 41  HIS A O   1 
ATOM   363  O  O   D HIS A 1 41  ? 28.469  0.724   -27.361 0.25 32.13  ? 41  HIS A O   1 
ATOM   364  C  CB  A HIS A 1 41  ? 26.453  -0.273  -29.451 0.25 25.43  ? 41  HIS A CB  1 
ATOM   365  C  CB  B HIS A 1 41  ? 26.453  -0.273  -29.451 0.25 25.43  ? 41  HIS A CB  1 
ATOM   366  C  CB  C HIS A 1 41  ? 26.404  -0.251  -29.243 0.25 30.61  ? 41  HIS A CB  1 
ATOM   367  C  CB  D HIS A 1 41  ? 26.404  -0.251  -29.243 0.25 30.61  ? 41  HIS A CB  1 
ATOM   368  C  CG  A HIS A 1 41  ? 25.278  0.030   -28.576 0.25 25.00  ? 41  HIS A CG  1 
ATOM   369  C  CG  B HIS A 1 41  ? 25.278  0.030   -28.576 0.25 25.00  ? 41  HIS A CG  1 
ATOM   370  C  CG  C HIS A 1 41  ? 25.208  -0.070  -28.364 0.25 31.29  ? 41  HIS A CG  1 
ATOM   371  C  CG  D HIS A 1 41  ? 25.208  -0.070  -28.364 0.25 31.29  ? 41  HIS A CG  1 
ATOM   372  N  ND1 A HIS A 1 41  ? 25.386  0.714   -27.377 0.25 24.51  ? 41  HIS A ND1 1 
ATOM   373  N  ND1 B HIS A 1 41  ? 25.386  0.714   -27.377 0.25 24.51  ? 41  HIS A ND1 1 
ATOM   374  N  ND1 C HIS A 1 41  ? 25.119  0.948   -27.430 0.25 31.57  ? 41  HIS A ND1 1 
ATOM   375  N  ND1 D HIS A 1 41  ? 25.119  0.948   -27.430 0.25 31.57  ? 41  HIS A ND1 1 
ATOM   376  C  CD2 A HIS A 1 41  ? 23.956  -0.169  -28.779 0.25 24.80  ? 41  HIS A CD2 1 
ATOM   377  C  CD2 B HIS A 1 41  ? 23.956  -0.169  -28.779 0.25 24.80  ? 41  HIS A CD2 1 
ATOM   378  C  CD2 C HIS A 1 41  ? 24.022  -0.719  -28.322 0.25 32.92  ? 41  HIS A CD2 1 
ATOM   379  C  CD2 D HIS A 1 41  ? 24.022  -0.719  -28.322 0.25 32.92  ? 41  HIS A CD2 1 
ATOM   380  C  CE1 A HIS A 1 41  ? 24.186  0.870   -26.852 0.25 25.54  ? 41  HIS A CE1 1 
ATOM   381  C  CE1 B HIS A 1 41  ? 24.186  0.870   -26.852 0.25 25.54  ? 41  HIS A CE1 1 
ATOM   382  C  CE1 C HIS A 1 41  ? 23.947  0.891   -26.825 0.25 33.07  ? 41  HIS A CE1 1 
ATOM   383  C  CE1 D HIS A 1 41  ? 23.947  0.891   -26.825 0.25 33.07  ? 41  HIS A CE1 1 
ATOM   384  N  NE2 A HIS A 1 41  ? 23.286  0.338   -27.696 0.25 25.97  ? 41  HIS A NE2 1 
ATOM   385  N  NE2 B HIS A 1 41  ? 23.286  0.338   -27.696 0.25 25.97  ? 41  HIS A NE2 1 
ATOM   386  N  NE2 C HIS A 1 41  ? 23.251  -0.124  -27.355 0.25 33.83  ? 41  HIS A NE2 1 
ATOM   387  N  NE2 D HIS A 1 41  ? 23.251  -0.124  -27.355 0.25 33.83  ? 41  HIS A NE2 1 
ATOM   388  N  N   A VAL A 1 42  ? 28.205  -1.165  -26.424 0.25 26.23  ? 42  VAL A N   1 
ATOM   389  N  N   B VAL A 1 42  ? 28.205  -1.165  -26.424 0.25 26.23  ? 42  VAL A N   1 
ATOM   390  N  N   C VAL A 1 42  ? 28.295  -1.263  -26.277 0.25 31.25  ? 42  VAL A N   1 
ATOM   391  N  N   D VAL A 1 42  ? 28.295  -1.263  -26.277 0.25 31.25  ? 42  VAL A N   1 
ATOM   392  C  CA  A VAL A 1 42  ? 28.859  -0.722  -25.154 0.25 27.39  ? 42  VAL A CA  1 
ATOM   393  C  CA  B VAL A 1 42  ? 28.859  -0.722  -25.154 0.25 27.39  ? 42  VAL A CA  1 
ATOM   394  C  CA  C VAL A 1 42  ? 29.012  -0.821  -25.040 0.25 33.06  ? 42  VAL A CA  1 
ATOM   395  C  CA  D VAL A 1 42  ? 29.012  -0.821  -25.040 0.25 33.06  ? 42  VAL A CA  1 
ATOM   396  C  C   A VAL A 1 42  ? 30.350  -0.449  -25.414 0.25 28.63  ? 42  VAL A C   1 
ATOM   397  C  C   B VAL A 1 42  ? 30.350  -0.449  -25.414 0.25 28.63  ? 42  VAL A C   1 
ATOM   398  C  C   C VAL A 1 42  ? 30.503  -0.634  -25.368 0.25 34.00  ? 42  VAL A C   1 
ATOM   399  C  C   D VAL A 1 42  ? 30.503  -0.634  -25.368 0.25 34.00  ? 42  VAL A C   1 
ATOM   400  O  O   A VAL A 1 42  ? 30.903  0.445   -24.735 0.25 27.77  ? 42  VAL A O   1 
ATOM   401  O  O   B VAL A 1 42  ? 30.903  0.445   -24.735 0.25 27.77  ? 42  VAL A O   1 
ATOM   402  O  O   C VAL A 1 42  ? 31.155  0.155   -24.655 0.25 32.92  ? 42  VAL A O   1 
ATOM   403  O  O   D VAL A 1 42  ? 31.155  0.155   -24.655 0.25 32.92  ? 42  VAL A O   1 
ATOM   404  C  CB  A VAL A 1 42  ? 28.667  -1.749  -24.018 0.25 27.05  ? 42  VAL A CB  1 
ATOM   405  C  CB  B VAL A 1 42  ? 28.667  -1.749  -24.018 0.25 27.05  ? 42  VAL A CB  1 
ATOM   406  C  CB  C VAL A 1 42  ? 28.812  -1.791  -23.855 0.25 33.14  ? 42  VAL A CB  1 
ATOM   407  C  CB  D VAL A 1 42  ? 28.812  -1.791  -23.855 0.25 33.14  ? 42  VAL A CB  1 
ATOM   408  C  CG1 A VAL A 1 42  ? 29.464  -3.028  -24.243 0.25 26.82  ? 42  VAL A CG1 1 
ATOM   409  C  CG1 B VAL A 1 42  ? 29.464  -3.028  -24.243 0.25 26.82  ? 42  VAL A CG1 1 
ATOM   410  C  CG1 C VAL A 1 42  ? 29.827  -2.929  -23.850 0.25 33.51  ? 42  VAL A CG1 1 
ATOM   411  C  CG1 D VAL A 1 42  ? 29.827  -2.929  -23.850 0.25 33.51  ? 42  VAL A CG1 1 
ATOM   412  C  CG2 A VAL A 1 42  ? 28.998  -1.141  -22.662 0.25 27.35  ? 42  VAL A CG2 1 
ATOM   413  C  CG2 B VAL A 1 42  ? 28.998  -1.141  -22.662 0.25 27.35  ? 42  VAL A CG2 1 
ATOM   414  C  CG2 C VAL A 1 42  ? 28.846  -1.051  -22.525 0.25 33.54  ? 42  VAL A CG2 1 
ATOM   415  C  CG2 D VAL A 1 42  ? 28.846  -1.051  -22.525 0.25 33.54  ? 42  VAL A CG2 1 
ATOM   416  N  N   A ILE A 1 43  ? 30.968  -1.179  -26.357 0.25 29.97  ? 43  ILE A N   1 
ATOM   417  N  N   B ILE A 1 43  ? 30.968  -1.179  -26.357 0.25 29.97  ? 43  ILE A N   1 
ATOM   418  N  N   C ILE A 1 43  ? 31.012  -1.316  -26.409 0.25 35.30  ? 43  ILE A N   1 
ATOM   419  N  N   D ILE A 1 43  ? 31.012  -1.316  -26.409 0.25 35.30  ? 43  ILE A N   1 
ATOM   420  C  CA  A ILE A 1 43  ? 32.430  -1.093  -26.668 0.25 31.34  ? 43  ILE A CA  1 
ATOM   421  C  CA  B ILE A 1 43  ? 32.430  -1.093  -26.668 0.25 31.34  ? 43  ILE A CA  1 
ATOM   422  C  CA  C ILE A 1 43  ? 32.461  -1.334  -26.786 0.25 36.84  ? 43  ILE A CA  1 
ATOM   423  C  CA  D ILE A 1 43  ? 32.461  -1.334  -26.786 0.25 36.84  ? 43  ILE A CA  1 
ATOM   424  C  C   A ILE A 1 43  ? 32.707  0.086   -27.611 0.25 33.06  ? 43  ILE A C   1 
ATOM   425  C  C   B ILE A 1 43  ? 32.707  0.086   -27.611 0.25 33.06  ? 43  ILE A C   1 
ATOM   426  C  C   C ILE A 1 43  ? 32.764  -0.210  -27.791 0.25 39.59  ? 43  ILE A C   1 
ATOM   427  C  C   D ILE A 1 43  ? 32.764  -0.210  -27.791 0.25 39.59  ? 43  ILE A C   1 
ATOM   428  O  O   A ILE A 1 43  ? 33.889  0.311   -27.910 0.25 34.72  ? 43  ILE A O   1 
ATOM   429  O  O   B ILE A 1 43  ? 33.889  0.311   -27.910 0.25 34.72  ? 43  ILE A O   1 
ATOM   430  O  O   C ILE A 1 43  ? 33.910  -0.163  -28.273 0.25 41.82  ? 43  ILE A O   1 
ATOM   431  O  O   D ILE A 1 43  ? 33.910  -0.163  -28.273 0.25 41.82  ? 43  ILE A O   1 
ATOM   432  C  CB  A ILE A 1 43  ? 32.969  -2.418  -27.247 0.25 30.02  ? 43  ILE A CB  1 
ATOM   433  C  CB  B ILE A 1 43  ? 32.969  -2.418  -27.247 0.25 30.02  ? 43  ILE A CB  1 
ATOM   434  C  CB  C ILE A 1 43  ? 32.884  -2.719  -27.323 0.25 35.29  ? 43  ILE A CB  1 
ATOM   435  C  CB  D ILE A 1 43  ? 32.884  -2.719  -27.323 0.25 35.29  ? 43  ILE A CB  1 
ATOM   436  C  CG1 A ILE A 1 43  ? 32.520  -2.661  -28.692 0.25 28.99  ? 43  ILE A CG1 1 
ATOM   437  C  CG1 B ILE A 1 43  ? 32.520  -2.661  -28.692 0.25 28.99  ? 43  ILE A CG1 1 
ATOM   438  C  CG1 C ILE A 1 43  ? 32.522  -2.930  -28.798 0.25 33.57  ? 43  ILE A CG1 1 
ATOM   439  C  CG1 D ILE A 1 43  ? 32.522  -2.930  -28.798 0.25 33.57  ? 43  ILE A CG1 1 
ATOM   440  C  CG2 A ILE A 1 43  ? 32.613  -3.580  -26.332 0.25 29.80  ? 43  ILE A CG2 1 
ATOM   441  C  CG2 B ILE A 1 43  ? 32.613  -3.580  -26.332 0.25 29.80  ? 43  ILE A CG2 1 
ATOM   442  C  CG2 C ILE A 1 43  ? 32.327  -3.829  -26.440 0.25 35.11  ? 43  ILE A CG2 1 
ATOM   443  C  CG2 D ILE A 1 43  ? 32.327  -3.829  -26.440 0.25 35.11  ? 43  ILE A CG2 1 
ATOM   444  C  CD1 A ILE A 1 43  ? 33.151  -3.866  -29.339 0.25 28.62  ? 43  ILE A CD1 1 
ATOM   445  C  CD1 B ILE A 1 43  ? 33.151  -3.866  -29.339 0.25 28.62  ? 43  ILE A CD1 1 
ATOM   446  C  CD1 C ILE A 1 43  ? 33.218  -4.107  -29.432 0.25 33.50  ? 43  ILE A CD1 1 
ATOM   447  C  CD1 D ILE A 1 43  ? 33.218  -4.107  -29.432 0.25 33.50  ? 43  ILE A CD1 1 
ATOM   448  N  N   A CYS A 1 44  ? 31.675  0.808   -28.059 0.25 34.68  ? 44  CYS A N   1 
ATOM   449  N  N   B CYS A 1 44  ? 31.675  0.808   -28.059 0.25 34.68  ? 44  CYS A N   1 
ATOM   450  N  N   C CYS A 1 44  ? 31.790  0.659   -28.085 0.25 42.77  ? 44  CYS A N   1 
ATOM   451  N  N   D CYS A 1 44  ? 31.790  0.659   -28.085 0.25 42.77  ? 44  CYS A N   1 
ATOM   452  C  CA  A CYS A 1 44  ? 31.799  1.966   -28.983 0.25 35.84  ? 44  CYS A CA  1 
ATOM   453  C  CA  B CYS A 1 44  ? 31.799  1.966   -28.983 0.25 35.84  ? 44  CYS A CA  1 
ATOM   454  C  CA  C CYS A 1 44  ? 31.923  1.823   -29.006 0.25 45.37  ? 44  CYS A CA  1 
ATOM   455  C  CA  D CYS A 1 44  ? 31.923  1.823   -29.006 0.25 45.37  ? 44  CYS A CA  1 
ATOM   456  C  C   A CYS A 1 44  ? 32.171  3.238   -28.214 0.25 37.76  ? 44  CYS A C   1 
ATOM   457  C  C   B CYS A 1 44  ? 32.171  3.238   -28.214 0.25 37.76  ? 44  CYS A C   1 
ATOM   458  C  C   C CYS A 1 44  ? 32.575  3.010   -28.286 0.25 47.61  ? 44  CYS A C   1 
ATOM   459  C  C   D CYS A 1 44  ? 32.575  3.010   -28.286 0.25 47.61  ? 44  CYS A C   1 
ATOM   460  O  O   A CYS A 1 44  ? 31.611  3.479   -27.118 0.25 34.81  ? 44  CYS A O   1 
ATOM   461  O  O   B CYS A 1 44  ? 31.611  3.479   -27.118 0.25 34.81  ? 44  CYS A O   1 
ATOM   462  O  O   C CYS A 1 44  ? 32.731  2.949   -27.049 0.25 47.65  ? 44  CYS A O   1 
ATOM   463  O  O   D CYS A 1 44  ? 32.731  2.949   -27.049 0.25 47.65  ? 44  CYS A O   1 
ATOM   464  C  CB  A CYS A 1 44  ? 30.514  2.202   -29.765 0.25 37.06  ? 44  CYS A CB  1 
ATOM   465  C  CB  B CYS A 1 44  ? 30.514  2.202   -29.765 0.25 37.06  ? 44  CYS A CB  1 
ATOM   466  C  CB  C CYS A 1 44  ? 30.568  2.264   -29.549 0.25 47.65  ? 44  CYS A CB  1 
ATOM   467  C  CB  D CYS A 1 44  ? 30.568  2.264   -29.549 0.25 47.65  ? 44  CYS A CB  1 
ATOM   468  S  SG  A CYS A 1 44  ? 30.087  0.814   -30.844 0.25 38.50  ? 44  CYS A SG  1 
ATOM   469  S  SG  B CYS A 1 44  ? 30.087  0.814   -30.844 0.25 38.50  ? 44  CYS A SG  1 
ATOM   470  S  SG  C CYS A 1 44  ? 30.064  1.393   -31.053 0.25 51.15  ? 44  CYS A SG  1 
ATOM   471  S  SG  D CYS A 1 44  ? 30.064  1.393   -31.053 0.25 51.15  ? 44  CYS A SG  1 
ATOM   472  N  N   A THR A 1 45  ? 33.095  4.010   -28.790 0.25 41.68  ? 45  THR A N   1 
ATOM   473  N  N   B THR A 1 45  ? 33.095  4.010   -28.790 0.25 41.68  ? 45  THR A N   1 
ATOM   474  N  N   C THR A 1 45  ? 32.938  4.039   -29.061 0.25 51.04  ? 45  THR A N   1 
ATOM   475  N  N   D THR A 1 45  ? 32.938  4.039   -29.061 0.25 51.04  ? 45  THR A N   1 
ATOM   476  C  CA  A THR A 1 45  ? 33.485  5.382   -28.369 0.25 44.69  ? 45  THR A CA  1 
ATOM   477  C  CA  B THR A 1 45  ? 33.485  5.382   -28.369 0.25 44.69  ? 45  THR A CA  1 
ATOM   478  C  CA  C THR A 1 45  ? 33.415  5.378   -28.610 0.25 53.31  ? 45  THR A CA  1 
ATOM   479  C  CA  D THR A 1 45  ? 33.415  5.378   -28.610 0.25 53.31  ? 45  THR A CA  1 
ATOM   480  C  C   A THR A 1 45  ? 32.739  6.379   -29.268 0.25 48.56  ? 45  THR A C   1 
ATOM   481  C  C   B THR A 1 45  ? 32.739  6.379   -29.268 0.25 48.56  ? 45  THR A C   1 
ATOM   482  C  C   C THR A 1 45  ? 32.689  6.457   -29.428 0.25 56.59  ? 45  THR A C   1 
ATOM   483  C  C   D THR A 1 45  ? 32.689  6.457   -29.428 0.25 56.59  ? 45  THR A C   1 
ATOM   484  O  O   A THR A 1 45  ? 31.855  5.930   -30.033 0.25 48.48  ? 45  THR A O   1 
ATOM   485  O  O   B THR A 1 45  ? 31.855  5.930   -30.033 0.25 48.48  ? 45  THR A O   1 
ATOM   486  O  O   C THR A 1 45  ? 31.821  6.086   -30.249 0.25 54.32  ? 45  THR A O   1 
ATOM   487  O  O   D THR A 1 45  ? 31.821  6.086   -30.249 0.25 54.32  ? 45  THR A O   1 
ATOM   488  C  CB  A THR A 1 45  ? 35.012  5.538   -28.412 0.25 43.77  ? 45  THR A CB  1 
ATOM   489  C  CB  B THR A 1 45  ? 35.012  5.538   -28.412 0.25 43.77  ? 45  THR A CB  1 
ATOM   490  C  CB  C THR A 1 45  ? 34.938  5.512   -28.749 0.25 52.53  ? 45  THR A CB  1 
ATOM   491  C  CB  D THR A 1 45  ? 34.938  5.512   -28.749 0.25 52.53  ? 45  THR A CB  1 
ATOM   492  O  OG1 A THR A 1 45  ? 35.410  5.660   -29.777 0.25 45.60  ? 45  THR A OG1 1 
ATOM   493  O  OG1 B THR A 1 45  ? 35.410  5.660   -29.777 0.25 45.60  ? 45  THR A OG1 1 
ATOM   494  O  OG1 C THR A 1 45  ? 35.243  5.663   -30.136 0.25 54.30  ? 45  THR A OG1 1 
ATOM   495  O  OG1 D THR A 1 45  ? 35.243  5.663   -30.136 0.25 54.30  ? 45  THR A OG1 1 
ATOM   496  C  CG2 A THR A 1 45  ? 35.746  4.375   -27.780 0.25 44.17  ? 45  THR A CG2 1 
ATOM   497  C  CG2 B THR A 1 45  ? 35.746  4.375   -27.780 0.25 44.17  ? 45  THR A CG2 1 
ATOM   498  C  CG2 C THR A 1 45  ? 35.701  4.330   -28.192 0.25 52.61  ? 45  THR A CG2 1 
ATOM   499  C  CG2 D THR A 1 45  ? 35.701  4.330   -28.192 0.25 52.61  ? 45  THR A CG2 1 
ATOM   500  N  N   A SER A 1 46  ? 33.095  7.666   -29.199 0.25 52.97  ? 46  SER A N   1 
ATOM   501  N  N   B SER A 1 46  ? 33.095  7.666   -29.199 0.25 52.97  ? 46  SER A N   1 
ATOM   502  N  N   C SER A 1 46  ? 33.054  7.731   -29.232 0.25 60.34  ? 46  SER A N   1 
ATOM   503  N  N   D SER A 1 46  ? 33.054  7.731   -29.232 0.25 60.34  ? 46  SER A N   1 
ATOM   504  C  CA  A SER A 1 46  ? 32.377  8.788   -29.866 0.25 55.10  ? 46  SER A CA  1 
ATOM   505  C  CA  B SER A 1 46  ? 32.377  8.788   -29.866 0.25 55.10  ? 46  SER A CA  1 
ATOM   506  C  CA  C SER A 1 46  ? 32.390  8.922   -29.831 0.25 62.18  ? 46  SER A CA  1 
ATOM   507  C  CA  D SER A 1 46  ? 32.390  8.922   -29.831 0.25 62.18  ? 46  SER A CA  1 
ATOM   508  C  C   A SER A 1 46  ? 32.406  8.645   -31.395 0.25 56.71  ? 46  SER A C   1 
ATOM   509  C  C   B SER A 1 46  ? 32.406  8.645   -31.395 0.25 56.71  ? 46  SER A C   1 
ATOM   510  C  C   C SER A 1 46  ? 32.458  8.892   -31.367 0.25 63.70  ? 46  SER A C   1 
ATOM   511  C  C   D SER A 1 46  ? 32.458  8.892   -31.367 0.25 63.70  ? 46  SER A C   1 
ATOM   512  O  O   A SER A 1 46  ? 31.343  8.848   -32.015 0.25 56.82  ? 46  SER A O   1 
ATOM   513  O  O   B SER A 1 46  ? 31.343  8.848   -32.015 0.25 56.82  ? 46  SER A O   1 
ATOM   514  O  O   C SER A 1 46  ? 31.386  9.003   -31.991 0.25 63.99  ? 46  SER A O   1 
ATOM   515  O  O   D SER A 1 46  ? 31.386  9.003   -31.991 0.25 63.99  ? 46  SER A O   1 
ATOM   516  C  CB  A SER A 1 46  ? 32.935  10.116  -29.430 0.25 56.56  ? 46  SER A CB  1 
ATOM   517  C  CB  B SER A 1 46  ? 32.935  10.116  -29.430 0.25 56.56  ? 46  SER A CB  1 
ATOM   518  C  CB  C SER A 1 46  ? 32.966  10.200  -29.273 0.25 63.46  ? 46  SER A CB  1 
ATOM   519  C  CB  D SER A 1 46  ? 32.966  10.200  -29.273 0.25 63.46  ? 46  SER A CB  1 
ATOM   520  O  OG  A SER A 1 46  ? 32.765  10.291  -28.032 0.25 58.94  ? 46  SER A OG  1 
ATOM   521  O  OG  B SER A 1 46  ? 32.765  10.291  -28.032 0.25 58.94  ? 46  SER A OG  1 
ATOM   522  O  OG  C SER A 1 46  ? 32.537  10.393  -27.934 0.25 65.55  ? 46  SER A OG  1 
ATOM   523  O  OG  D SER A 1 46  ? 32.537  10.393  -27.934 0.25 65.55  ? 46  SER A OG  1 
ATOM   524  N  N   A GLU A 1 47  ? 33.562  8.317   -31.987 0.25 58.91  ? 47  GLU A N   1 
ATOM   525  N  N   B GLU A 1 47  ? 33.562  8.317   -31.987 0.25 58.91  ? 47  GLU A N   1 
ATOM   526  N  N   C GLU A 1 47  ? 33.652  8.751   -31.959 0.25 65.81  ? 47  GLU A N   1 
ATOM   527  N  N   D GLU A 1 47  ? 33.652  8.751   -31.959 0.25 65.81  ? 47  GLU A N   1 
ATOM   528  C  CA  A GLU A 1 47  ? 33.725  8.218   -33.467 0.25 59.48  ? 47  GLU A CA  1 
ATOM   529  C  CA  B GLU A 1 47  ? 33.725  8.218   -33.467 0.25 59.48  ? 47  GLU A CA  1 
ATOM   530  C  CA  C GLU A 1 47  ? 33.845  8.807   -33.439 0.25 66.65  ? 47  GLU A CA  1 
ATOM   531  C  CA  D GLU A 1 47  ? 33.845  8.807   -33.439 0.25 66.65  ? 47  GLU A CA  1 
ATOM   532  C  C   A GLU A 1 47  ? 33.288  6.829   -33.955 0.25 56.70  ? 47  GLU A C   1 
ATOM   533  C  C   B GLU A 1 47  ? 33.288  6.829   -33.955 0.25 56.70  ? 47  GLU A C   1 
ATOM   534  C  C   C GLU A 1 47  ? 33.597  7.430   -34.078 0.25 64.26  ? 47  GLU A C   1 
ATOM   535  C  C   D GLU A 1 47  ? 33.597  7.430   -34.078 0.25 64.26  ? 47  GLU A C   1 
ATOM   536  O  O   A GLU A 1 47  ? 33.008  6.692   -35.163 0.25 61.43  ? 47  GLU A O   1 
ATOM   537  O  O   B GLU A 1 47  ? 33.008  6.692   -35.163 0.25 61.43  ? 47  GLU A O   1 
ATOM   538  O  O   C GLU A 1 47  ? 33.594  7.369   -35.322 0.25 69.06  ? 47  GLU A O   1 
ATOM   539  O  O   D GLU A 1 47  ? 33.594  7.369   -35.322 0.25 69.06  ? 47  GLU A O   1 
ATOM   540  C  CB  A GLU A 1 47  ? 35.163  8.500   -33.909 0.25 62.73  ? 47  GLU A CB  1 
ATOM   541  C  CB  B GLU A 1 47  ? 35.163  8.500   -33.909 0.25 62.73  ? 47  GLU A CB  1 
ATOM   542  C  CB  C GLU A 1 47  ? 35.240  9.315   -33.820 0.25 69.82  ? 47  GLU A CB  1 
ATOM   543  C  CB  D GLU A 1 47  ? 35.240  9.315   -33.820 0.25 69.82  ? 47  GLU A CB  1 
ATOM   544  C  CG  A GLU A 1 47  ? 35.766  9.762   -33.319 0.25 64.94  ? 47  GLU A CG  1 
ATOM   545  C  CG  B GLU A 1 47  ? 35.766  9.762   -33.319 0.25 64.94  ? 47  GLU A CG  1 
ATOM   546  C  CG  C GLU A 1 47  ? 35.442  10.806  -33.593 0.25 72.33  ? 47  GLU A CG  1 
ATOM   547  C  CG  D GLU A 1 47  ? 35.442  10.806  -33.593 0.25 72.33  ? 47  GLU A CG  1 
ATOM   548  C  CD  A GLU A 1 47  ? 36.619  9.541   -32.080 0.25 65.75  ? 47  GLU A CD  1 
ATOM   549  C  CD  B GLU A 1 47  ? 36.619  9.541   -32.080 0.25 65.75  ? 47  GLU A CD  1 
ATOM   550  C  CD  C GLU A 1 47  ? 36.043  11.170  -32.245 0.25 74.15  ? 47  GLU A CD  1 
ATOM   551  C  CD  D GLU A 1 47  ? 36.043  11.170  -32.245 0.25 74.15  ? 47  GLU A CD  1 
ATOM   552  O  OE1 A GLU A 1 47  ? 37.410  8.577   -32.073 0.25 63.99  ? 47  GLU A OE1 1 
ATOM   553  O  OE1 B GLU A 1 47  ? 37.410  8.577   -32.073 0.25 63.99  ? 47  GLU A OE1 1 
ATOM   554  O  OE1 C GLU A 1 47  ? 36.956  12.026  -32.220 0.25 73.09  ? 47  GLU A OE1 1 
ATOM   555  O  OE1 D GLU A 1 47  ? 36.956  12.026  -32.220 0.25 73.09  ? 47  GLU A OE1 1 
ATOM   556  O  OE2 A GLU A 1 47  ? 36.489  10.334  -31.127 0.25 70.03  ? 47  GLU A OE2 1 
ATOM   557  O  OE2 B GLU A 1 47  ? 36.489  10.334  -31.127 0.25 70.03  ? 47  GLU A OE2 1 
ATOM   558  O  OE2 C GLU A 1 47  ? 35.598  10.596  -31.225 0.25 77.04  ? 47  GLU A OE2 1 
ATOM   559  O  OE2 D GLU A 1 47  ? 35.598  10.596  -31.225 0.25 77.04  ? 47  GLU A OE2 1 
ATOM   560  N  N   A ASP A 1 48  ? 33.211  5.842   -33.057 0.25 52.53  ? 48  ASP A N   1 
ATOM   561  N  N   B ASP A 1 48  ? 33.211  5.842   -33.057 0.25 52.53  ? 48  ASP A N   1 
ATOM   562  N  N   C ASP A 1 48  ? 33.405  6.371   -33.283 0.25 59.23  ? 48  ASP A N   1 
ATOM   563  N  N   D ASP A 1 48  ? 33.405  6.371   -33.283 0.25 59.23  ? 48  ASP A N   1 
ATOM   564  C  CA  A ASP A 1 48  ? 32.780  4.454   -33.381 0.25 50.59  ? 48  ASP A CA  1 
ATOM   565  C  CA  B ASP A 1 48  ? 32.780  4.454   -33.381 0.25 50.59  ? 48  ASP A CA  1 
ATOM   566  C  CA  C ASP A 1 48  ? 33.002  5.024   -33.780 0.25 58.01  ? 48  ASP A CA  1 
ATOM   567  C  CA  D ASP A 1 48  ? 33.002  5.024   -33.780 0.25 58.01  ? 48  ASP A CA  1 
ATOM   568  C  C   A ASP A 1 48  ? 31.250  4.377   -33.473 0.25 49.72  ? 48  ASP A C   1 
ATOM   569  C  C   B ASP A 1 48  ? 31.250  4.377   -33.473 0.25 49.72  ? 48  ASP A C   1 
ATOM   570  C  C   C ASP A 1 48  ? 31.559  5.073   -34.294 0.25 55.80  ? 48  ASP A C   1 
ATOM   571  C  C   D ASP A 1 48  ? 31.559  5.073   -34.294 0.25 55.80  ? 48  ASP A C   1 
ATOM   572  O  O   A ASP A 1 48  ? 30.723  3.250   -33.422 0.25 50.30  ? 48  ASP A O   1 
ATOM   573  O  O   B ASP A 1 48  ? 30.723  3.250   -33.422 0.25 50.30  ? 48  ASP A O   1 
ATOM   574  O  O   C ASP A 1 48  ? 31.299  4.504   -35.374 0.25 59.72  ? 48  ASP A O   1 
ATOM   575  O  O   D ASP A 1 48  ? 31.299  4.504   -35.374 0.25 59.72  ? 48  ASP A O   1 
ATOM   576  C  CB  A ASP A 1 48  ? 33.255  3.442   -32.333 0.25 48.25  ? 48  ASP A CB  1 
ATOM   577  C  CB  B ASP A 1 48  ? 33.255  3.442   -32.333 0.25 48.25  ? 48  ASP A CB  1 
ATOM   578  C  CB  C ASP A 1 48  ? 33.069  3.951   -32.687 0.25 57.33  ? 48  ASP A CB  1 
ATOM   579  C  CB  D ASP A 1 48  ? 33.069  3.951   -32.687 0.25 57.33  ? 48  ASP A CB  1 
ATOM   580  C  CG  A ASP A 1 48  ? 34.760  3.405   -32.114 0.25 48.42  ? 48  ASP A CG  1 
ATOM   581  C  CG  B ASP A 1 48  ? 34.760  3.405   -32.114 0.25 48.42  ? 48  ASP A CG  1 
ATOM   582  C  CG  C ASP A 1 48  ? 34.453  3.373   -32.433 0.25 57.89  ? 48  ASP A CG  1 
ATOM   583  C  CG  D ASP A 1 48  ? 34.453  3.373   -32.433 0.25 57.89  ? 48  ASP A CG  1 
ATOM   584  O  OD1 A ASP A 1 48  ? 35.505  3.429   -33.120 0.25 47.84  ? 48  ASP A OD1 1 
ATOM   585  O  OD1 B ASP A 1 48  ? 35.505  3.429   -33.120 0.25 47.84  ? 48  ASP A OD1 1 
ATOM   586  O  OD1 C ASP A 1 48  ? 35.188  3.129   -33.418 0.25 56.97  ? 48  ASP A OD1 1 
ATOM   587  O  OD1 D ASP A 1 48  ? 35.188  3.129   -33.418 0.25 56.97  ? 48  ASP A OD1 1 
ATOM   588  O  OD2 A ASP A 1 48  ? 35.176  3.340   -30.935 0.25 45.66  ? 48  ASP A OD2 1 
ATOM   589  O  OD2 B ASP A 1 48  ? 35.176  3.340   -30.935 0.25 45.66  ? 48  ASP A OD2 1 
ATOM   590  O  OD2 C ASP A 1 48  ? 34.784  3.159   -31.247 0.25 57.72  ? 48  ASP A OD2 1 
ATOM   591  O  OD2 D ASP A 1 48  ? 34.784  3.159   -31.247 0.25 57.72  ? 48  ASP A OD2 1 
ATOM   592  N  N   A MET A 1 49  ? 30.547  5.508   -33.585 0.25 48.41  ? 49  MET A N   1 
ATOM   593  N  N   B MET A 1 49  ? 30.547  5.508   -33.585 0.25 48.41  ? 49  MET A N   1 
ATOM   594  N  N   C MET A 1 49  ? 30.692  5.753   -33.537 0.25 50.68  ? 49  MET A N   1 
ATOM   595  N  N   D MET A 1 49  ? 30.692  5.753   -33.537 0.25 50.68  ? 49  MET A N   1 
ATOM   596  C  CA  A MET A 1 49  ? 29.062  5.508   -33.546 0.25 50.71  ? 49  MET A CA  1 
ATOM   597  C  CA  B MET A 1 49  ? 29.062  5.508   -33.546 0.25 50.71  ? 49  MET A CA  1 
ATOM   598  C  CA  C MET A 1 49  ? 29.199  5.704   -33.553 0.25 50.49  ? 49  MET A CA  1 
ATOM   599  C  CA  D MET A 1 49  ? 29.199  5.704   -33.553 0.25 50.49  ? 49  MET A CA  1 
ATOM   600  C  C   A MET A 1 49  ? 28.488  5.378   -34.967 0.25 47.02  ? 49  MET A C   1 
ATOM   601  C  C   B MET A 1 49  ? 28.488  5.378   -34.967 0.25 47.02  ? 49  MET A C   1 
ATOM   602  C  C   C MET A 1 49  ? 28.626  5.326   -34.933 0.25 47.19  ? 49  MET A C   1 
ATOM   603  C  C   D MET A 1 49  ? 28.626  5.326   -34.933 0.25 47.19  ? 49  MET A C   1 
ATOM   604  O  O   A MET A 1 49  ? 27.436  4.719   -35.094 0.25 44.25  ? 49  MET A O   1 
ATOM   605  O  O   B MET A 1 49  ? 27.436  4.719   -35.094 0.25 44.25  ? 49  MET A O   1 
ATOM   606  O  O   C MET A 1 49  ? 27.723  4.468   -34.982 0.25 45.13  ? 49  MET A O   1 
ATOM   607  O  O   D MET A 1 49  ? 27.723  4.468   -34.982 0.25 45.13  ? 49  MET A O   1 
ATOM   608  C  CB  A MET A 1 49  ? 28.503  6.756   -32.849 0.25 55.14  ? 49  MET A CB  1 
ATOM   609  C  CB  B MET A 1 49  ? 28.503  6.756   -32.849 0.25 55.14  ? 49  MET A CB  1 
ATOM   610  C  CB  C MET A 1 49  ? 28.648  7.073   -33.130 0.25 52.01  ? 49  MET A CB  1 
ATOM   611  C  CB  D MET A 1 49  ? 28.648  7.073   -33.130 0.25 52.01  ? 49  MET A CB  1 
ATOM   612  C  CG  A MET A 1 49  ? 28.757  6.808   -31.340 0.25 58.23  ? 49  MET A CG  1 
ATOM   613  C  CG  B MET A 1 49  ? 28.757  6.808   -31.340 0.25 58.23  ? 49  MET A CG  1 
ATOM   614  C  CG  C MET A 1 49  ? 27.499  7.006   -32.139 0.25 53.03  ? 49  MET A CG  1 
ATOM   615  C  CG  D MET A 1 49  ? 27.499  7.006   -32.139 0.25 53.03  ? 49  MET A CG  1 
ATOM   616  S  SD  A MET A 1 49  ? 28.718  5.202   -30.478 0.25 73.18  ? 49  MET A SD  1 
ATOM   617  S  SD  B MET A 1 49  ? 28.718  5.202   -30.478 0.25 73.18  ? 49  MET A SD  1 
ATOM   618  S  SD  C MET A 1 49  ? 27.691  8.162   -30.757 0.25 73.18  ? 49  MET A SD  1 
ATOM   619  S  SD  D MET A 1 49  ? 27.691  8.162   -30.757 0.25 73.18  ? 49  MET A SD  1 
ATOM   620  C  CE  A MET A 1 49  ? 27.078  4.603   -30.886 0.25 64.82  ? 49  MET A CE  1 
ATOM   621  C  CE  B MET A 1 49  ? 27.078  4.603   -30.886 0.25 64.82  ? 49  MET A CE  1 
ATOM   622  C  CE  C MET A 1 49  ? 29.082  7.416   -29.911 0.25 52.40  ? 49  MET A CE  1 
ATOM   623  C  CE  D MET A 1 49  ? 29.082  7.416   -29.911 0.25 52.40  ? 49  MET A CE  1 
ATOM   624  N  N   . LEU A 1 50  ? 29.122  5.954   -36.001 1.00 44.06  ? 50  LEU A N   1 
ATOM   625  C  CA  . LEU A 1 50  ? 28.556  5.851   -37.381 1.00 40.95  ? 50  LEU A CA  1 
ATOM   626  C  C   . LEU A 1 50  ? 28.842  4.503   -38.053 1.00 31.45  ? 50  LEU A C   1 
ATOM   627  O  O   . LEU A 1 50  ? 27.923  3.948   -38.655 1.00 31.60  ? 50  LEU A O   1 
ATOM   628  C  CB  . LEU A 1 50  ? 29.069  6.995   -38.258 1.00 44.29  ? 50  LEU A CB  1 
ATOM   629  C  CG  . LEU A 1 50  ? 28.277  8.298   -38.168 1.00 48.12  ? 50  LEU A CG  1 
ATOM   630  C  CD1 . LEU A 1 50  ? 26.780  8.039   -37.980 1.00 50.69  ? 50  LEU A CD1 1 
ATOM   631  C  CD2 . LEU A 1 50  ? 28.801  9.155   -37.038 1.00 46.97  ? 50  LEU A CD2 1 
ATOM   632  N  N   . ASN A 1 51  ? 30.084  4.043   -38.032 1.00 28.91  ? 51  ASN A N   1 
ATOM   633  C  CA  . ASN A 1 51  ? 30.528  2.879   -38.829 1.00 28.86  ? 51  ASN A CA  1 
ATOM   634  C  C   . ASN A 1 51  ? 31.419  2.006   -37.959 1.00 30.49  ? 51  ASN A C   1 
ATOM   635  O  O   . ASN A 1 51  ? 32.548  1.716   -38.313 1.00 31.41  ? 51  ASN A O   1 
ATOM   636  C  CB  . ASN A 1 51  ? 31.160  3.373   -40.128 1.00 29.92  ? 51  ASN A CB  1 
ATOM   637  C  CG  . ASN A 1 51  ? 30.122  3.969   -41.057 1.00 31.01  ? 51  ASN A CG  1 
ATOM   638  O  OD1 . ASN A 1 51  ? 29.387  3.231   -41.710 1.00 32.11  ? 51  ASN A OD1 1 
ATOM   639  N  ND2 . ASN A 1 51  ? 30.032  5.290   -41.097 1.00 29.64  ? 51  ASN A ND2 1 
ATOM   640  N  N   . PRO A 1 52  ? 30.964  1.575   -36.764 1.00 31.24  ? 52  PRO A N   1 
ATOM   641  C  CA  . PRO A 1 52  ? 31.796  0.739   -35.908 1.00 32.43  ? 52  PRO A CA  1 
ATOM   642  C  C   . PRO A 1 52  ? 32.195  -0.561  -36.620 1.00 32.23  ? 52  PRO A C   1 
ATOM   643  O  O   . PRO A 1 52  ? 31.355  -1.162  -37.290 1.00 29.21  ? 52  PRO A O   1 
ATOM   644  C  CB  . PRO A 1 52  ? 30.917  0.431   -34.688 1.00 34.17  ? 52  PRO A CB  1 
ATOM   645  C  CG  . PRO A 1 52  ? 29.506  0.768   -35.128 1.00 34.84  ? 52  PRO A CG  1 
ATOM   646  C  CD  . PRO A 1 52  ? 29.647  1.838   -36.186 1.00 32.11  ? 52  PRO A CD  1 
ATOM   647  N  N   . ASN A 1 53  ? 33.469  -0.936  -36.497 1.00 27.73  ? 53  ASN A N   1 
ATOM   648  C  CA  . ASN A 1 53  ? 33.979  -2.259  -36.912 1.00 30.61  ? 53  ASN A CA  1 
ATOM   649  C  C   . ASN A 1 53  ? 34.078  -3.052  -35.619 1.00 30.89  ? 53  ASN A C   1 
ATOM   650  O  O   . ASN A 1 53  ? 35.093  -2.979  -34.946 1.00 31.92  ? 53  ASN A O   1 
ATOM   651  C  CB  . ASN A 1 53  ? 35.320  -2.120  -37.625 1.00 32.44  ? 53  ASN A CB  1 
ATOM   652  C  CG  . ASN A 1 53  ? 35.753  -3.389  -38.319 1.00 35.57  ? 53  ASN A CG  1 
ATOM   653  O  OD1 . ASN A 1 53  ? 35.608  -4.484  -37.779 1.00 33.31  ? 53  ASN A OD1 1 
ATOM   654  N  ND2 . ASN A 1 53  ? 36.333  -3.233  -39.502 1.00 37.39  ? 53  ASN A ND2 1 
ATOM   655  N  N   A TYR A 1 54  ? 33.018  -3.780  -35.275 0.25 31.06  ? 54  TYR A N   1 
ATOM   656  N  N   B TYR A 1 54  ? 33.018  -3.780  -35.275 0.25 31.06  ? 54  TYR A N   1 
ATOM   657  N  N   C TYR A 1 54  ? 33.014  -3.779  -35.280 0.25 31.20  ? 54  TYR A N   1 
ATOM   658  N  N   D TYR A 1 54  ? 33.014  -3.779  -35.280 0.25 31.20  ? 54  TYR A N   1 
ATOM   659  C  CA  A TYR A 1 54  ? 32.856  -4.420  -33.944 0.25 30.71  ? 54  TYR A CA  1 
ATOM   660  C  CA  B TYR A 1 54  ? 32.856  -4.420  -33.944 0.25 30.71  ? 54  TYR A CA  1 
ATOM   661  C  CA  C TYR A 1 54  ? 32.833  -4.417  -33.951 0.25 30.86  ? 54  TYR A CA  1 
ATOM   662  C  CA  D TYR A 1 54  ? 32.833  -4.417  -33.951 0.25 30.86  ? 54  TYR A CA  1 
ATOM   663  C  C   A TYR A 1 54  ? 33.951  -5.474  -33.745 0.25 30.54  ? 54  TYR A C   1 
ATOM   664  C  C   B TYR A 1 54  ? 33.951  -5.474  -33.745 0.25 30.54  ? 54  TYR A C   1 
ATOM   665  C  C   C TYR A 1 54  ? 33.922  -5.483  -33.744 0.25 30.73  ? 54  TYR A C   1 
ATOM   666  C  C   D TYR A 1 54  ? 33.922  -5.483  -33.744 0.25 30.73  ? 54  TYR A C   1 
ATOM   667  O  O   A TYR A 1 54  ? 34.518  -5.532  -32.640 0.25 28.56  ? 54  TYR A O   1 
ATOM   668  O  O   B TYR A 1 54  ? 34.518  -5.532  -32.640 0.25 28.56  ? 54  TYR A O   1 
ATOM   669  O  O   C TYR A 1 54  ? 34.469  -5.546  -32.629 0.25 28.66  ? 54  TYR A O   1 
ATOM   670  O  O   D TYR A 1 54  ? 34.469  -5.546  -32.629 0.25 28.66  ? 54  TYR A O   1 
ATOM   671  C  CB  A TYR A 1 54  ? 31.440  -4.970  -33.769 0.25 29.34  ? 54  TYR A CB  1 
ATOM   672  C  CB  B TYR A 1 54  ? 31.440  -4.970  -33.769 0.25 29.34  ? 54  TYR A CB  1 
ATOM   673  C  CB  C TYR A 1 54  ? 31.392  -4.915  -33.788 0.25 29.63  ? 54  TYR A CB  1 
ATOM   674  C  CB  D TYR A 1 54  ? 31.392  -4.915  -33.788 0.25 29.63  ? 54  TYR A CB  1 
ATOM   675  C  CG  A TYR A 1 54  ? 30.416  -3.905  -33.473 0.25 29.21  ? 54  TYR A CG  1 
ATOM   676  C  CG  B TYR A 1 54  ? 30.416  -3.905  -33.473 0.25 29.21  ? 54  TYR A CG  1 
ATOM   677  C  CG  C TYR A 1 54  ? 30.402  -3.827  -33.444 0.25 29.48  ? 54  TYR A CG  1 
ATOM   678  C  CG  D TYR A 1 54  ? 30.402  -3.827  -33.444 0.25 29.48  ? 54  TYR A CG  1 
ATOM   679  C  CD1 A TYR A 1 54  ? 30.407  -3.256  -32.249 0.25 29.19  ? 54  TYR A CD1 1 
ATOM   680  C  CD1 B TYR A 1 54  ? 30.407  -3.256  -32.249 0.25 29.19  ? 54  TYR A CD1 1 
ATOM   681  C  CD1 C TYR A 1 54  ? 30.374  -3.268  -32.176 0.25 29.48  ? 54  TYR A CD1 1 
ATOM   682  C  CD1 D TYR A 1 54  ? 30.374  -3.268  -32.176 0.25 29.48  ? 54  TYR A CD1 1 
ATOM   683  C  CD2 A TYR A 1 54  ? 29.471  -3.523  -34.413 0.25 28.80  ? 54  TYR A CD2 1 
ATOM   684  C  CD2 B TYR A 1 54  ? 29.471  -3.523  -34.413 0.25 28.80  ? 54  TYR A CD2 1 
ATOM   685  C  CD2 C TYR A 1 54  ? 29.499  -3.344  -34.379 0.25 29.15  ? 54  TYR A CD2 1 
ATOM   686  C  CD2 D TYR A 1 54  ? 29.499  -3.344  -34.379 0.25 29.15  ? 54  TYR A CD2 1 
ATOM   687  C  CE1 A TYR A 1 54  ? 29.481  -2.270  -31.959 0.25 28.84  ? 54  TYR A CE1 1 
ATOM   688  C  CE1 B TYR A 1 54  ? 29.481  -2.270  -31.959 0.25 28.84  ? 54  TYR A CE1 1 
ATOM   689  C  CE1 C TYR A 1 54  ? 29.477  -2.266  -31.842 0.25 29.05  ? 54  TYR A CE1 1 
ATOM   690  C  CE1 D TYR A 1 54  ? 29.477  -2.266  -31.842 0.25 29.05  ? 54  TYR A CE1 1 
ATOM   691  C  CE2 A TYR A 1 54  ? 28.538  -2.534  -34.141 0.25 28.58  ? 54  TYR A CE2 1 
ATOM   692  C  CE2 B TYR A 1 54  ? 28.538  -2.534  -34.141 0.25 28.58  ? 54  TYR A CE2 1 
ATOM   693  C  CE2 C TYR A 1 54  ? 28.596  -2.339  -34.064 0.25 28.81  ? 54  TYR A CE2 1 
ATOM   694  C  CE2 D TYR A 1 54  ? 28.596  -2.339  -34.064 0.25 28.81  ? 54  TYR A CE2 1 
ATOM   695  C  CZ  A TYR A 1 54  ? 28.540  -1.907  -32.907 0.25 28.76  ? 54  TYR A CZ  1 
ATOM   696  C  CZ  B TYR A 1 54  ? 28.540  -1.907  -32.907 0.25 28.76  ? 54  TYR A CZ  1 
ATOM   697  C  CZ  C TYR A 1 54  ? 28.581  -1.800  -32.789 0.25 29.06  ? 54  TYR A CZ  1 
ATOM   698  C  CZ  D TYR A 1 54  ? 28.581  -1.800  -32.789 0.25 29.06  ? 54  TYR A CZ  1 
ATOM   699  O  OH  A TYR A 1 54  ? 27.636  -0.925  -32.624 0.25 27.38  ? 54  TYR A OH  1 
ATOM   700  O  OH  B TYR A 1 54  ? 27.636  -0.925  -32.624 0.25 27.38  ? 54  TYR A OH  1 
ATOM   701  O  OH  C TYR A 1 54  ? 27.701  -0.804  -32.476 0.25 27.47  ? 54  TYR A OH  1 
ATOM   702  O  OH  D TYR A 1 54  ? 27.701  -0.804  -32.476 0.25 27.47  ? 54  TYR A OH  1 
ATOM   703  N  N   . GLU A 1 55  ? 34.239  -6.268  -34.779 1.00 30.83  ? 55  GLU A N   1 
ATOM   704  C  CA  . GLU A 1 55  ? 35.278  -7.330  -34.698 1.00 33.53  ? 55  GLU A CA  1 
ATOM   705  C  C   . GLU A 1 55  ? 36.636  -6.638  -34.403 1.00 31.82  ? 55  GLU A C   1 
ATOM   706  O  O   . GLU A 1 55  ? 37.375  -7.102  -33.533 1.00 30.85  ? 55  GLU A O   1 
ATOM   707  C  CB  . GLU A 1 55  ? 35.198  -8.221  -35.948 1.00 38.14  ? 55  GLU A CB  1 
ATOM   708  C  CG  . GLU A 1 55  ? 36.329  -9.245  -36.042 1.00 50.30  ? 55  GLU A CG  1 
ATOM   709  C  CD  . GLU A 1 55  ? 36.704  -9.809  -37.415 1.00 57.98  ? 55  GLU A CD  1 
ATOM   710  O  OE1 . GLU A 1 55  ? 36.557  -9.095  -38.437 1.00 58.67  ? 55  GLU A OE1 1 
ATOM   711  O  OE2 . GLU A 1 55  ? 37.196  -10.963 -37.453 1.00 63.16  ? 55  GLU A OE2 1 
ATOM   712  N  N   . ASP A 1 56  ? 36.889  -5.460  -34.966 1.00 32.67  ? 56  ASP A N   1 
ATOM   713  C  CA  . ASP A 1 56  ? 38.158  -4.712  -34.735 1.00 32.89  ? 56  ASP A CA  1 
ATOM   714  C  C   . ASP A 1 56  ? 38.229  -4.119  -33.314 1.00 32.16  ? 56  ASP A C   1 
ATOM   715  O  O   . ASP A 1 56  ? 39.277  -4.224  -32.683 1.00 29.37  ? 56  ASP A O   1 
ATOM   716  C  CB  . ASP A 1 56  ? 38.373  -3.647  -35.812 1.00 34.42  ? 56  ASP A CB  1 
ATOM   717  C  CG  . ASP A 1 56  ? 39.664  -2.882  -35.594 1.00 39.12  ? 56  ASP A CG  1 
ATOM   718  O  OD1 . ASP A 1 56  ? 40.736  -3.477  -35.842 1.00 37.22  ? 56  ASP A OD1 1 
ATOM   719  O  OD2 . ASP A 1 56  ? 39.582  -1.733  -35.122 1.00 41.46  ? 56  ASP A OD2 1 
ATOM   720  N  N   A LEU A 1 57  ? 37.138  -3.509  -32.837 0.25 31.68  ? 57  LEU A N   1 
ATOM   721  N  N   B LEU A 1 57  ? 37.138  -3.509  -32.837 0.25 31.68  ? 57  LEU A N   1 
ATOM   722  N  N   C LEU A 1 57  ? 37.142  -3.487  -32.848 0.25 31.85  ? 57  LEU A N   1 
ATOM   723  N  N   D LEU A 1 57  ? 37.142  -3.487  -32.848 0.25 31.85  ? 57  LEU A N   1 
ATOM   724  C  CA  A LEU A 1 57  ? 37.073  -2.875  -31.494 0.25 32.05  ? 57  LEU A CA  1 
ATOM   725  C  CA  B LEU A 1 57  ? 37.073  -2.875  -31.494 0.25 32.05  ? 57  LEU A CA  1 
ATOM   726  C  CA  C LEU A 1 57  ? 37.047  -2.869  -31.495 0.25 32.35  ? 57  LEU A CA  1 
ATOM   727  C  CA  D LEU A 1 57  ? 37.047  -2.869  -31.495 0.25 32.35  ? 57  LEU A CA  1 
ATOM   728  C  C   A LEU A 1 57  ? 37.141  -3.956  -30.411 0.25 32.00  ? 57  LEU A C   1 
ATOM   729  C  C   B LEU A 1 57  ? 37.141  -3.956  -30.411 0.25 32.00  ? 57  LEU A C   1 
ATOM   730  C  C   C LEU A 1 57  ? 37.147  -3.958  -30.420 0.25 32.16  ? 57  LEU A C   1 
ATOM   731  C  C   D LEU A 1 57  ? 37.147  -3.958  -30.420 0.25 32.16  ? 57  LEU A C   1 
ATOM   732  O  O   A LEU A 1 57  ? 37.757  -3.691  -29.363 0.25 33.68  ? 57  LEU A O   1 
ATOM   733  O  O   B LEU A 1 57  ? 37.757  -3.691  -29.363 0.25 33.68  ? 57  LEU A O   1 
ATOM   734  O  O   C LEU A 1 57  ? 37.779  -3.693  -29.381 0.25 33.84  ? 57  LEU A O   1 
ATOM   735  O  O   D LEU A 1 57  ? 37.779  -3.693  -29.381 0.25 33.84  ? 57  LEU A O   1 
ATOM   736  C  CB  A LEU A 1 57  ? 35.779  -2.068  -31.366 0.25 31.87  ? 57  LEU A CB  1 
ATOM   737  C  CB  B LEU A 1 57  ? 35.779  -2.068  -31.366 0.25 31.87  ? 57  LEU A CB  1 
ATOM   738  C  CB  C LEU A 1 57  ? 35.720  -2.117  -31.344 0.25 32.36  ? 57  LEU A CB  1 
ATOM   739  C  CB  D LEU A 1 57  ? 35.720  -2.117  -31.344 0.25 32.36  ? 57  LEU A CB  1 
ATOM   740  C  CG  A LEU A 1 57  ? 35.643  -0.892  -32.329 0.25 32.61  ? 57  LEU A CG  1 
ATOM   741  C  CG  B LEU A 1 57  ? 35.643  -0.892  -32.329 0.25 32.61  ? 57  LEU A CG  1 
ATOM   742  C  CG  C LEU A 1 57  ? 35.599  -0.797  -32.102 0.25 33.35  ? 57  LEU A CG  1 
ATOM   743  C  CG  D LEU A 1 57  ? 35.599  -0.797  -32.102 0.25 33.35  ? 57  LEU A CG  1 
ATOM   744  C  CD1 A LEU A 1 57  ? 34.214  -0.368  -32.334 0.25 33.11  ? 57  LEU A CD1 1 
ATOM   745  C  CD1 B LEU A 1 57  ? 34.214  -0.368  -32.334 0.25 33.11  ? 57  LEU A CD1 1 
ATOM   746  C  CD1 C LEU A 1 57  ? 34.157  -0.306  -32.076 0.25 33.95  ? 57  LEU A CD1 1 
ATOM   747  C  CD1 D LEU A 1 57  ? 34.157  -0.306  -32.076 0.25 33.95  ? 57  LEU A CD1 1 
ATOM   748  C  CD2 A LEU A 1 57  ? 36.627  0.218   -31.986 0.25 31.40  ? 57  LEU A CD2 1 
ATOM   749  C  CD2 B LEU A 1 57  ? 36.627  0.218   -31.986 0.25 31.40  ? 57  LEU A CD2 1 
ATOM   750  C  CD2 C LEU A 1 57  ? 36.533  0.261   -31.533 0.25 32.65  ? 57  LEU A CD2 1 
ATOM   751  C  CD2 D LEU A 1 57  ? 36.533  0.261   -31.533 0.25 32.65  ? 57  LEU A CD2 1 
ATOM   752  N  N   . LEU A 1 58  ? 36.527  -5.120  -30.653 1.00 31.56  ? 58  LEU A N   1 
ATOM   753  C  CA  . LEU A 1 58  ? 36.478  -6.226  -29.653 1.00 32.85  ? 58  LEU A CA  1 
ATOM   754  C  C   . LEU A 1 58  ? 37.846  -6.882  -29.463 1.00 33.69  ? 58  LEU A C   1 
ATOM   755  O  O   . LEU A 1 58  ? 38.197  -7.126  -28.303 1.00 33.79  ? 58  LEU A O   1 
ATOM   756  C  CB  . LEU A 1 58  ? 35.459  -7.303  -30.021 1.00 33.25  ? 58  LEU A CB  1 
ATOM   757  C  CG  . LEU A 1 58  ? 35.165  -8.279  -28.878 1.00 33.41  ? 58  LEU A CG  1 
ATOM   758  C  CD1 . LEU A 1 58  ? 34.618  -7.557  -27.654 1.00 36.54  ? 58  LEU A CD1 1 
ATOM   759  C  CD2 . LEU A 1 58  ? 34.209  -9.373  -29.306 1.00 32.65  ? 58  LEU A CD2 1 
ATOM   760  N  N   . ILE A 1 59  ? 38.571  -7.176  -30.543 1.00 37.01  ? 59  ILE A N   1 
ATOM   761  C  CA  . ILE A 1 59  ? 39.891  -7.882  -30.471 1.00 40.40  ? 59  ILE A CA  1 
ATOM   762  C  C   . ILE A 1 59  ? 40.897  -7.027  -29.670 1.00 37.18  ? 59  ILE A C   1 
ATOM   763  O  O   . ILE A 1 59  ? 41.854  -7.589  -29.120 1.00 41.73  ? 59  ILE A O   1 
ATOM   764  C  CB  . ILE A 1 59  ? 40.395  -8.247  -31.881 1.00 41.72  ? 59  ILE A CB  1 
ATOM   765  C  CG1 . ILE A 1 59  ? 41.457  -9.347  -31.826 1.00 42.30  ? 59  ILE A CG1 1 
ATOM   766  C  CG2 . ILE A 1 59  ? 40.888  -7.006  -32.604 1.00 41.74  ? 59  ILE A CG2 1 
ATOM   767  C  CD1 . ILE A 1 59  ? 41.852  -9.889  -33.178 1.00 43.08  ? 59  ILE A CD1 1 
ATOM   768  N  N   . ARG A 1 60  ? 40.647  -5.726  -29.541 1.00 34.27  ? 60  ARG A N   1 
ATOM   769  C  CA  . ARG A 1 60  ? 41.511  -4.765  -28.805 1.00 34.55  ? 60  ARG A CA  1 
ATOM   770  C  C   . ARG A 1 60  ? 41.256  -4.761  -27.291 1.00 36.96  ? 60  ARG A C   1 
ATOM   771  O  O   . ARG A 1 60  ? 42.050  -4.146  -26.561 1.00 36.25  ? 60  ARG A O   1 
ATOM   772  C  CB  . ARG A 1 60  ? 41.288  -3.350  -29.354 1.00 33.17  ? 60  ARG A CB  1 
ATOM   773  C  CG  . ARG A 1 60  ? 41.669  -3.214  -30.824 1.00 30.66  ? 60  ARG A CG  1 
ATOM   774  C  CD  . ARG A 1 60  ? 41.449  -1.815  -31.355 1.00 30.72  ? 60  ARG A CD  1 
ATOM   775  N  NE  . ARG A 1 60  ? 41.654  -1.821  -32.797 1.00 31.24  ? 60  ARG A NE  1 
ATOM   776  C  CZ  . ARG A 1 60  ? 42.774  -1.490  -33.423 1.00 29.35  ? 60  ARG A CZ  1 
ATOM   777  N  NH1 . ARG A 1 60  ? 43.841  -1.113  -32.741 1.00 31.25  ? 60  ARG A NH1 1 
ATOM   778  N  NH2 . ARG A 1 60  ? 42.831  -1.542  -34.738 1.00 26.71  ? 60  ARG A NH2 1 
ATOM   779  N  N   A LYS A 1 61  ? 40.191  -5.438  -26.843 0.25 36.32  ? 61  LYS A N   1 
ATOM   780  N  N   B LYS A 1 61  ? 40.191  -5.438  -26.843 0.25 36.32  ? 61  LYS A N   1 
ATOM   781  N  N   C LYS A 1 61  ? 40.178  -5.412  -26.837 0.25 36.31  ? 61  LYS A N   1 
ATOM   782  N  N   D LYS A 1 61  ? 40.178  -5.412  -26.837 0.25 36.31  ? 61  LYS A N   1 
ATOM   783  C  CA  A LYS A 1 61  ? 39.745  -5.469  -25.424 0.25 37.63  ? 61  LYS A CA  1 
ATOM   784  C  CA  B LYS A 1 61  ? 39.745  -5.469  -25.424 0.25 37.63  ? 61  LYS A CA  1 
ATOM   785  C  CA  C LYS A 1 61  ? 39.778  -5.443  -25.405 0.25 37.63  ? 61  LYS A CA  1 
ATOM   786  C  CA  D LYS A 1 61  ? 39.778  -5.443  -25.405 0.25 37.63  ? 61  LYS A CA  1 
ATOM   787  C  C   A LYS A 1 61  ? 40.281  -6.722  -24.727 0.25 37.50  ? 61  LYS A C   1 
ATOM   788  C  C   B LYS A 1 61  ? 40.281  -6.722  -24.727 0.25 37.50  ? 61  LYS A C   1 
ATOM   789  C  C   C LYS A 1 61  ? 40.307  -6.711  -24.733 0.25 37.49  ? 61  LYS A C   1 
ATOM   790  C  C   D LYS A 1 61  ? 40.307  -6.711  -24.733 0.25 37.49  ? 61  LYS A C   1 
ATOM   791  O  O   A LYS A 1 61  ? 40.295  -7.798  -25.364 0.25 34.64  ? 61  LYS A O   1 
ATOM   792  O  O   B LYS A 1 61  ? 40.295  -7.798  -25.364 0.25 34.64  ? 61  LYS A O   1 
ATOM   793  O  O   C LYS A 1 61  ? 40.332  -7.777  -25.387 0.25 34.54  ? 61  LYS A O   1 
ATOM   794  O  O   D LYS A 1 61  ? 40.332  -7.777  -25.387 0.25 34.54  ? 61  LYS A O   1 
ATOM   795  C  CB  A LYS A 1 61  ? 38.215  -5.457  -25.340 0.25 38.26  ? 61  LYS A CB  1 
ATOM   796  C  CB  B LYS A 1 61  ? 38.215  -5.457  -25.340 0.25 38.26  ? 61  LYS A CB  1 
ATOM   797  C  CB  C LYS A 1 61  ? 38.256  -5.416  -25.237 0.25 38.26  ? 61  LYS A CB  1 
ATOM   798  C  CB  D LYS A 1 61  ? 38.256  -5.416  -25.237 0.25 38.26  ? 61  LYS A CB  1 
ATOM   799  C  CG  A LYS A 1 61  ? 37.542  -4.271  -26.016 0.25 39.34  ? 61  LYS A CG  1 
ATOM   800  C  CG  B LYS A 1 61  ? 37.542  -4.271  -26.016 0.25 39.34  ? 61  LYS A CG  1 
ATOM   801  C  CG  C LYS A 1 61  ? 37.544  -4.276  -25.945 0.25 39.36  ? 61  LYS A CG  1 
ATOM   802  C  CG  D LYS A 1 61  ? 37.544  -4.276  -25.945 0.25 39.36  ? 61  LYS A CG  1 
ATOM   803  C  CD  A LYS A 1 61  ? 37.827  -2.951  -25.340 0.25 40.22  ? 61  LYS A CD  1 
ATOM   804  C  CD  B LYS A 1 61  ? 37.827  -2.951  -25.340 0.25 40.22  ? 61  LYS A CD  1 
ATOM   805  C  CD  C LYS A 1 61  ? 37.839  -2.914  -25.366 0.25 40.30  ? 61  LYS A CD  1 
ATOM   806  C  CD  D LYS A 1 61  ? 37.839  -2.914  -25.366 0.25 40.30  ? 61  LYS A CD  1 
ATOM   807  C  CE  A LYS A 1 61  ? 37.402  -1.760  -26.168 0.25 40.69  ? 61  LYS A CE  1 
ATOM   808  C  CE  B LYS A 1 61  ? 37.402  -1.760  -26.168 0.25 40.69  ? 61  LYS A CE  1 
ATOM   809  C  CE  C LYS A 1 61  ? 37.374  -1.795  -26.272 0.25 40.78  ? 61  LYS A CE  1 
ATOM   810  C  CE  D LYS A 1 61  ? 37.374  -1.795  -26.272 0.25 40.78  ? 61  LYS A CE  1 
ATOM   811  N  NZ  A LYS A 1 61  ? 37.337  -0.536  -25.339 0.25 42.12  ? 61  LYS A NZ  1 
ATOM   812  N  NZ  B LYS A 1 61  ? 37.337  -0.536  -25.339 0.25 42.12  ? 61  LYS A NZ  1 
ATOM   813  N  NZ  C LYS A 1 61  ? 37.198  -0.533  -25.522 0.25 42.20  ? 61  LYS A NZ  1 
ATOM   814  N  NZ  D LYS A 1 61  ? 37.198  -0.533  -25.522 0.25 42.20  ? 61  LYS A NZ  1 
ATOM   815  N  N   . SER A 1 62  ? 40.696  -6.574  -23.465 1.00 36.83  ? 62  SER A N   1 
ATOM   816  C  CA  . SER A 1 62  ? 40.932  -7.711  -22.543 1.00 42.61  ? 62  SER A CA  1 
ATOM   817  C  C   . SER A 1 62  ? 39.681  -7.839  -21.661 1.00 43.02  ? 62  SER A C   1 
ATOM   818  O  O   . SER A 1 62  ? 38.900  -6.842  -21.490 1.00 35.88  ? 62  SER A O   1 
ATOM   819  C  CB  . SER A 1 62  ? 42.198  -7.565  -21.722 1.00 43.46  ? 62  SER A CB  1 
ATOM   820  O  OG  . SER A 1 62  ? 42.654  -6.223  -21.682 1.00 45.26  ? 62  SER A OG  1 
ATOM   821  N  N   . ASN A 1 63  ? 39.500  -9.032  -21.114 1.00 44.97  ? 63  ASN A N   1 
ATOM   822  C  CA  . ASN A 1 63  ? 38.483  -9.316  -20.077 1.00 43.50  ? 63  ASN A CA  1 
ATOM   823  C  C   . ASN A 1 63  ? 38.403  -8.161  -19.060 1.00 45.05  ? 63  ASN A C   1 
ATOM   824  O  O   . ASN A 1 63  ? 37.278  -7.776  -18.700 1.00 45.56  ? 63  ASN A O   1 
ATOM   825  C  CB  . ASN A 1 63  ? 38.800  -10.654 -19.434 1.00 43.67  ? 63  ASN A CB  1 
ATOM   826  C  CG  . ASN A 1 63  ? 38.600  -11.817 -20.377 1.00 46.23  ? 63  ASN A CG  1 
ATOM   827  O  OD1 . ASN A 1 63  ? 37.697  -11.814 -21.224 1.00 43.54  ? 63  ASN A OD1 1 
ATOM   828  N  ND2 . ASN A 1 63  ? 39.434  -12.830 -20.213 1.00 40.12  ? 63  ASN A ND2 1 
ATOM   829  N  N   . HIS A 1 64  ? 39.525  -7.580  -18.635 1.00 45.18  ? 64  HIS A N   1 
ATOM   830  C  CA  . HIS A 1 64  ? 39.571  -6.573  -17.530 1.00 48.02  ? 64  HIS A CA  1 
ATOM   831  C  C   . HIS A 1 64  ? 39.156  -5.166  -17.975 1.00 44.18  ? 64  HIS A C   1 
ATOM   832  O  O   . HIS A 1 64  ? 39.081  -4.289  -17.088 1.00 46.59  ? 64  HIS A O   1 
ATOM   833  C  CB  . HIS A 1 64  ? 40.951  -6.542  -16.844 1.00 52.53  ? 64  HIS A CB  1 
ATOM   834  C  CG  . HIS A 1 64  ? 42.113  -6.275  -17.740 1.00 55.45  ? 64  HIS A CG  1 
ATOM   835  N  ND1 . HIS A 1 64  ? 42.868  -7.307  -18.287 1.00 63.48  ? 64  HIS A ND1 1 
ATOM   836  C  CD2 . HIS A 1 64  ? 42.677  -5.120  -18.159 1.00 57.77  ? 64  HIS A CD2 1 
ATOM   837  C  CE1 . HIS A 1 64  ? 43.852  -6.801  -19.001 1.00 59.83  ? 64  HIS A CE1 1 
ATOM   838  N  NE2 . HIS A 1 64  ? 43.755  -5.456  -18.941 1.00 60.22  ? 64  HIS A NE2 1 
ATOM   839  N  N   . ASN A 1 65  ? 38.923  -4.931  -19.268 1.00 40.33  ? 65  ASN A N   1 
ATOM   840  C  CA  . ASN A 1 65  ? 38.327  -3.658  -19.769 1.00 42.72  ? 65  ASN A CA  1 
ATOM   841  C  C   . ASN A 1 65  ? 36.817  -3.627  -19.448 1.00 39.72  ? 65  ASN A C   1 
ATOM   842  O  O   . ASN A 1 65  ? 36.221  -2.548  -19.530 1.00 37.43  ? 65  ASN A O   1 
ATOM   843  C  CB  . ASN A 1 65  ? 38.546  -3.481  -21.277 1.00 42.49  ? 65  ASN A CB  1 
ATOM   844  C  CG  . ASN A 1 65  ? 39.993  -3.273  -21.668 1.00 45.09  ? 65  ASN A CG  1 
ATOM   845  O  OD1 . ASN A 1 65  ? 40.629  -4.157  -22.238 1.00 46.27  ? 65  ASN A OD1 1 
ATOM   846  N  ND2 . ASN A 1 65  ? 40.514  -2.096  -21.379 1.00 46.77  ? 65  ASN A ND2 1 
ATOM   847  N  N   . PHE A 1 66  ? 36.220  -4.787  -19.150 1.00 40.97  ? 66  PHE A N   1 
ATOM   848  C  CA  . PHE A 1 66  ? 34.775  -4.985  -18.858 1.00 39.30  ? 66  PHE A CA  1 
ATOM   849  C  C   . PHE A 1 66  ? 34.560  -5.029  -17.339 1.00 42.50  ? 66  PHE A C   1 
ATOM   850  O  O   . PHE A 1 66  ? 34.923  -6.020  -16.714 1.00 39.22  ? 66  PHE A O   1 
ATOM   851  C  CB  . PHE A 1 66  ? 34.267  -6.260  -19.540 1.00 39.73  ? 66  PHE A CB  1 
ATOM   852  C  CG  . PHE A 1 66  ? 34.333  -6.200  -21.049 1.00 43.29  ? 66  PHE A CG  1 
ATOM   853  C  CD1 . PHE A 1 66  ? 33.533  -5.310  -21.750 1.00 47.43  ? 66  PHE A CD1 1 
ATOM   854  C  CD2 . PHE A 1 66  ? 35.208  -6.998  -21.768 1.00 43.76  ? 66  PHE A CD2 1 
ATOM   855  C  CE1 . PHE A 1 66  ? 33.609  -5.220  -23.134 1.00 51.71  ? 66  PHE A CE1 1 
ATOM   856  C  CE2 . PHE A 1 66  ? 35.278  -6.917  -23.152 1.00 44.75  ? 66  PHE A CE2 1 
ATOM   857  C  CZ  . PHE A 1 66  ? 34.477  -6.030  -23.834 1.00 48.16  ? 66  PHE A CZ  1 
ATOM   858  N  N   . LEU A 1 67  ? 33.955  -3.983  -16.784 1.00 42.56  ? 67  LEU A N   1 
ATOM   859  C  CA  . LEU A 1 67  ? 33.597  -3.854  -15.347 1.00 46.99  ? 67  LEU A CA  1 
ATOM   860  C  C   . LEU A 1 67  ? 32.118  -4.246  -15.164 1.00 41.77  ? 67  LEU A C   1 
ATOM   861  O  O   . LEU A 1 67  ? 31.226  -3.517  -15.622 1.00 40.15  ? 67  LEU A O   1 
ATOM   862  C  CB  . LEU A 1 67  ? 33.938  -2.418  -14.931 1.00 51.46  ? 67  LEU A CB  1 
ATOM   863  C  CG  . LEU A 1 67  ? 35.331  -1.977  -15.407 1.00 66.58  ? 67  LEU A CG  1 
ATOM   864  C  CD1 . LEU A 1 67  ? 35.446  -0.471  -15.604 1.00 67.54  ? 67  LEU A CD1 1 
ATOM   865  C  CD2 . LEU A 1 67  ? 36.422  -2.484  -14.464 1.00 69.95  ? 67  LEU A CD2 1 
ATOM   866  N  N   . VAL A 1 68  ? 31.886  -5.435  -14.611 1.00 39.47  ? 68  VAL A N   1 
ATOM   867  C  CA  . VAL A 1 68  ? 30.546  -6.021  -14.345 1.00 38.29  ? 68  VAL A CA  1 
ATOM   868  C  C   . VAL A 1 68  ? 30.302  -6.008  -12.831 1.00 42.59  ? 68  VAL A C   1 
ATOM   869  O  O   . VAL A 1 68  ? 31.106  -6.619  -12.085 1.00 35.52  ? 68  VAL A O   1 
ATOM   870  C  CB  . VAL A 1 68  ? 30.424  -7.441  -14.906 1.00 39.23  ? 68  VAL A CB  1 
ATOM   871  C  CG1 . VAL A 1 68  ? 29.037  -8.009  -14.640 1.00 37.86  ? 68  VAL A CG1 1 
ATOM   872  C  CG2 . VAL A 1 68  ? 30.787  -7.504  -16.392 1.00 38.88  ? 68  VAL A CG2 1 
ATOM   873  N  N   . GLN A 1 69  ? 29.199  -5.371  -12.428 1.00 39.28  ? 69  GLN A N   1 
ATOM   874  C  CA  . GLN A 1 69  ? 28.800  -5.130  -11.025 1.00 40.53  ? 69  GLN A CA  1 
ATOM   875  C  C   . GLN A 1 69  ? 27.393  -5.717  -10.818 1.00 40.24  ? 69  GLN A C   1 
ATOM   876  O  O   . GLN A 1 69  ? 26.445  -5.286  -11.498 1.00 36.76  ? 69  GLN A O   1 
ATOM   877  C  CB  . GLN A 1 69  ? 28.893  -3.629  -10.775 1.00 45.72  ? 69  GLN A CB  1 
ATOM   878  C  CG  . GLN A 1 69  ? 29.094  -3.259  -9.318  1.00 54.72  ? 69  GLN A CG  1 
ATOM   879  C  CD  . GLN A 1 69  ? 29.364  -1.782  -9.177  1.00 56.71  ? 69  GLN A CD  1 
ATOM   880  O  OE1 . GLN A 1 69  ? 30.255  -1.242  -9.831  1.00 53.79  ? 69  GLN A OE1 1 
ATOM   881  N  NE2 . GLN A 1 69  ? 28.584  -1.125  -8.331  1.00 57.99  ? 69  GLN A NE2 1 
ATOM   882  N  N   . ALA A 1 70  ? 27.271  -6.734  -9.972  1.00 39.88  ? 70  ALA A N   1 
ATOM   883  C  CA  . ALA A 1 70  ? 25.986  -7.294  -9.496  1.00 40.18  ? 70  ALA A CA  1 
ATOM   884  C  C   . ALA A 1 70  ? 25.720  -6.713  -8.108  1.00 43.67  ? 70  ALA A C   1 
ATOM   885  O  O   . ALA A 1 70  ? 26.426  -7.108  -7.161  1.00 42.95  ? 70  ALA A O   1 
ATOM   886  C  CB  . ALA A 1 70  ? 26.053  -8.796  -9.487  1.00 39.61  ? 70  ALA A CB  1 
ATOM   887  N  N   . GLY A 1 71  ? 24.795  -5.755  -8.004  1.00 42.62  ? 71  GLY A N   1 
ATOM   888  C  CA  . GLY A 1 71  ? 24.642  -4.924  -6.799  1.00 47.08  ? 71  GLY A CA  1 
ATOM   889  C  C   . GLY A 1 71  ? 25.978  -4.314  -6.419  1.00 52.62  ? 71  GLY A C   1 
ATOM   890  O  O   . GLY A 1 71  ? 26.511  -3.543  -7.235  1.00 56.94  ? 71  GLY A O   1 
ATOM   891  N  N   . ASN A 1 72  ? 26.528  -4.688  -5.258  1.00 58.96  ? 72  ASN A N   1 
ATOM   892  C  CA  . ASN A 1 72  ? 27.823  -4.175  -4.732  1.00 60.62  ? 72  ASN A CA  1 
ATOM   893  C  C   . ASN A 1 72  ? 28.997  -5.048  -5.188  1.00 55.77  ? 72  ASN A C   1 
ATOM   894  O  O   . ASN A 1 72  ? 30.124  -4.559  -5.148  1.00 57.02  ? 72  ASN A O   1 
ATOM   895  C  CB  . ASN A 1 72  ? 27.814  -4.069  -3.205  1.00 67.40  ? 72  ASN A CB  1 
ATOM   896  C  CG  . ASN A 1 72  ? 27.612  -2.643  -2.745  1.00 70.99  ? 72  ASN A CG  1 
ATOM   897  O  OD1 . ASN A 1 72  ? 27.054  -1.828  -3.482  1.00 67.83  ? 72  ASN A OD1 1 
ATOM   898  N  ND2 . ASN A 1 72  ? 28.074  -2.334  -1.543  1.00 70.26  ? 72  ASN A ND2 1 
ATOM   899  N  N   . VAL A 1 73  ? 28.744  -6.289  -5.593  1.00 54.60  ? 73  VAL A N   1 
ATOM   900  C  CA  . VAL A 1 73  ? 29.793  -7.274  -5.998  1.00 54.07  ? 73  VAL A CA  1 
ATOM   901  C  C   . VAL A 1 73  ? 30.332  -6.876  -7.379  1.00 56.08  ? 73  VAL A C   1 
ATOM   902  O  O   . VAL A 1 73  ? 29.511  -6.564  -8.262  1.00 51.87  ? 73  VAL A O   1 
ATOM   903  C  CB  . VAL A 1 73  ? 29.215  -8.706  -6.033  1.00 52.59  ? 73  VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 73  ? 30.242  -9.738  -6.482  1.00 52.58  ? 73  VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 73  ? 28.592  -9.105  -4.701  1.00 53.73  ? 73  VAL A CG2 1 
ATOM   906  N  N   . GLN A 1 74  ? 31.650  -6.926  -7.586  1.00 52.04  ? 74  GLN A N   1 
ATOM   907  C  CA  . GLN A 1 74  ? 32.239  -6.917  -8.949  1.00 52.70  ? 74  GLN A CA  1 
ATOM   908  C  C   . GLN A 1 74  ? 32.367  -8.367  -9.399  1.00 48.10  ? 74  GLN A C   1 
ATOM   909  O  O   . GLN A 1 74  ? 32.942  -9.134  -8.643  1.00 48.61  ? 74  GLN A O   1 
ATOM   910  C  CB  . GLN A 1 74  ? 33.593  -6.218  -8.962  1.00 57.80  ? 74  GLN A CB  1 
ATOM   911  C  CG  . GLN A 1 74  ? 33.485  -4.705  -8.891  1.00 63.94  ? 74  GLN A CG  1 
ATOM   912  C  CD  . GLN A 1 74  ? 34.850  -4.067  -8.930  1.00 71.33  ? 74  GLN A CD  1 
ATOM   913  O  OE1 . GLN A 1 74  ? 35.804  -4.632  -9.472  1.00 70.69  ? 74  GLN A OE1 1 
ATOM   914  N  NE2 . GLN A 1 74  ? 34.951  -2.882  -8.341  1.00 76.02  ? 74  GLN A NE2 1 
ATOM   915  N  N   . LEU A 1 75  ? 31.819  -8.735  -10.557 1.00 44.92  ? 75  LEU A N   1 
ATOM   916  C  CA  . LEU A 1 75  ? 32.045  -10.081 -11.156 1.00 46.89  ? 75  LEU A CA  1 
ATOM   917  C  C   . LEU A 1 75  ? 33.345  -10.032 -11.965 1.00 47.91  ? 75  LEU A C   1 
ATOM   918  O  O   . LEU A 1 75  ? 33.664  -8.967  -12.541 1.00 50.13  ? 75  LEU A O   1 
ATOM   919  C  CB  . LEU A 1 75  ? 30.865  -10.503 -12.041 1.00 46.59  ? 75  LEU A CB  1 
ATOM   920  C  CG  . LEU A 1 75  ? 29.546  -10.760 -11.314 1.00 51.33  ? 75  LEU A CG  1 
ATOM   921  C  CD1 . LEU A 1 75  ? 28.426  -11.023 -12.305 1.00 47.12  ? 75  LEU A CD1 1 
ATOM   922  C  CD2 . LEU A 1 75  ? 29.677  -11.926 -10.340 1.00 53.73  ? 75  LEU A CD2 1 
ATOM   923  N  N   . ARG A 1 76  ? 34.069  -11.147 -11.990 1.00 46.30  ? 76  ARG A N   1 
ATOM   924  C  CA  . ARG A 1 76  ? 35.351  -11.282 -12.720 1.00 50.64  ? 76  ARG A CA  1 
ATOM   925  C  C   . ARG A 1 76  ? 35.018  -11.818 -14.112 1.00 44.01  ? 76  ARG A C   1 
ATOM   926  O  O   . ARG A 1 76  ? 34.496  -12.953 -14.214 1.00 38.95  ? 76  ARG A O   1 
ATOM   927  C  CB  . ARG A 1 76  ? 36.324  -12.174 -11.941 1.00 54.70  ? 76  ARG A CB  1 
ATOM   928  C  CG  . ARG A 1 76  ? 37.742  -12.199 -12.501 1.00 64.92  ? 76  ARG A CG  1 
ATOM   929  C  CD  . ARG A 1 76  ? 38.745  -12.878 -11.578 1.00 66.53  ? 76  ARG A CD  1 
ATOM   930  N  NE  . ARG A 1 76  ? 39.829  -13.561 -12.289 1.00 74.20  ? 76  ARG A NE  1 
ATOM   931  C  CZ  . ARG A 1 76  ? 39.757  -14.829 -12.775 1.00 79.95  ? 76  ARG A CZ  1 
ATOM   932  N  NH1 . ARG A 1 76  ? 38.629  -15.603 -12.657 1.00 86.76  ? 76  ARG A NH1 1 
ATOM   933  N  NH2 . ARG A 1 76  ? 40.821  -15.331 -13.392 1.00 75.35  ? 76  ARG A NH2 1 
ATOM   934  N  N   . VAL A 1 77  ? 35.243  -11.000 -15.139 1.00 41.74  ? 77  VAL A N   1 
ATOM   935  C  CA  . VAL A 1 77  ? 35.047  -11.422 -16.553 1.00 42.52  ? 77  VAL A CA  1 
ATOM   936  C  C   . VAL A 1 77  ? 36.242  -12.307 -16.918 1.00 40.65  ? 77  VAL A C   1 
ATOM   937  O  O   . VAL A 1 77  ? 37.362  -11.831 -16.793 1.00 35.57  ? 77  VAL A O   1 
ATOM   938  C  CB  . VAL A 1 77  ? 34.907  -10.207 -17.489 1.00 45.07  ? 77  VAL A CB  1 
ATOM   939  C  CG1 . VAL A 1 77  ? 34.962  -10.616 -18.955 1.00 43.25  ? 77  VAL A CG1 1 
ATOM   940  C  CG2 . VAL A 1 77  ? 33.650  -9.400  -17.177 1.00 45.39  ? 77  VAL A CG2 1 
ATOM   941  N  N   . ILE A 1 78  ? 35.993  -13.546 -17.341 1.00 45.61  ? 78  ILE A N   1 
ATOM   942  C  CA  . ILE A 1 78  ? 37.044  -14.551 -17.689 1.00 46.76  ? 78  ILE A CA  1 
ATOM   943  C  C   . ILE A 1 78  ? 37.014  -14.838 -19.200 1.00 46.06  ? 78  ILE A C   1 
ATOM   944  O  O   . ILE A 1 78  ? 37.791  -15.681 -19.637 1.00 41.03  ? 78  ILE A O   1 
ATOM   945  C  CB  . ILE A 1 78  ? 36.883  -15.838 -16.844 1.00 48.65  ? 78  ILE A CB  1 
ATOM   946  C  CG1 . ILE A 1 78  ? 35.611  -16.631 -17.169 1.00 51.57  ? 78  ILE A CG1 1 
ATOM   947  C  CG2 . ILE A 1 78  ? 36.964  -15.514 -15.358 1.00 49.63  ? 78  ILE A CG2 1 
ATOM   948  C  CD1 . ILE A 1 78  ? 35.527  -17.980 -16.470 1.00 52.85  ? 78  ILE A CD1 1 
ATOM   949  N  N   . GLY A 1 79  ? 36.158  -14.163 -19.975 1.00 42.97  ? 79  GLY A N   1 
ATOM   950  C  CA  . GLY A 1 79  ? 35.926  -14.493 -21.401 1.00 42.72  ? 79  GLY A CA  1 
ATOM   951  C  C   . GLY A 1 79  ? 34.971  -13.508 -22.066 1.00 43.80  ? 79  GLY A C   1 
ATOM   952  O  O   . GLY A 1 79  ? 34.070  -13.003 -21.367 1.00 36.30  ? 79  GLY A O   1 
ATOM   953  N  N   . HIS A 1 80  ? 35.188  -13.200 -23.349 1.00 43.98  ? 80  HIS A N   1 
ATOM   954  C  CA  . HIS A 1 80  ? 34.339  -12.284 -24.159 1.00 42.93  ? 80  HIS A CA  1 
ATOM   955  C  C   . HIS A 1 80  ? 34.215  -12.838 -25.583 1.00 44.11  ? 80  HIS A C   1 
ATOM   956  O  O   . HIS A 1 80  ? 35.240  -13.213 -26.154 1.00 40.43  ? 80  HIS A O   1 
ATOM   957  C  CB  . HIS A 1 80  ? 34.874  -10.847 -24.090 1.00 42.80  ? 80  HIS A CB  1 
ATOM   958  C  CG  . HIS A 1 80  ? 36.235  -10.639 -24.669 1.00 48.85  ? 80  HIS A CG  1 
ATOM   959  N  ND1 . HIS A 1 80  ? 37.357  -10.450 -23.882 1.00 51.05  ? 80  HIS A ND1 1 
ATOM   960  C  CD2 . HIS A 1 80  ? 36.653  -10.530 -25.951 1.00 52.63  ? 80  HIS A CD2 1 
ATOM   961  C  CE1 . HIS A 1 80  ? 38.409  -10.253 -24.656 1.00 54.79  ? 80  HIS A CE1 1 
ATOM   962  N  NE2 . HIS A 1 80  ? 38.003  -10.298 -25.931 1.00 52.38  ? 80  HIS A NE2 1 
ATOM   963  N  N   . SER A 1 81  ? 32.987  -12.930 -26.102 1.00 41.93  ? 81  SER A N   1 
ATOM   964  C  CA  . SER A 1 81  ? 32.662  -13.327 -27.495 1.00 37.30  ? 81  SER A CA  1 
ATOM   965  C  C   . SER A 1 81  ? 31.465  -12.511 -27.983 1.00 37.13  ? 81  SER A C   1 
ATOM   966  O  O   . SER A 1 81  ? 30.669  -12.045 -27.169 1.00 38.16  ? 81  SER A O   1 
ATOM   967  C  CB  . SER A 1 81  ? 32.386  -14.804 -27.588 1.00 37.82  ? 81  SER A CB  1 
ATOM   968  O  OG  . SER A 1 81  ? 31.013  -15.085 -27.403 1.00 39.26  ? 81  SER A OG  1 
ATOM   969  N  N   . MET A 1 82  ? 31.319  -12.375 -29.282 1.00 34.75  ? 82  MET A N   1 
ATOM   970  C  CA  . MET A 1 82  ? 30.207  -11.618 -29.887 1.00 36.21  ? 82  MET A CA  1 
ATOM   971  C  C   . MET A 1 82  ? 29.293  -12.623 -30.576 1.00 35.32  ? 82  MET A C   1 
ATOM   972  O  O   . MET A 1 82  ? 29.814  -13.542 -31.230 1.00 30.53  ? 82  MET A O   1 
ATOM   973  C  CB  . MET A 1 82  ? 30.790  -10.650 -30.913 1.00 38.68  ? 82  MET A CB  1 
ATOM   974  C  CG  . MET A 1 82  ? 29.812  -9.673  -31.467 1.00 42.10  ? 82  MET A CG  1 
ATOM   975  S  SD  . MET A 1 82  ? 30.726  -8.199  -31.970 1.00 39.90  ? 82  MET A SD  1 
ATOM   976  C  CE  . MET A 1 82  ? 31.692  -8.878  -33.327 1.00 38.51  ? 82  MET A CE  1 
ATOM   977  N  N   . GLN A 1 83  ? 27.980  -12.489 -30.430 1.00 33.73  ? 83  GLN A N   1 
ATOM   978  C  CA  . GLN A 1 83  ? 27.040  -13.236 -31.295 1.00 31.37  ? 83  GLN A CA  1 
ATOM   979  C  C   . GLN A 1 83  ? 26.061  -12.221 -31.862 1.00 31.97  ? 83  GLN A C   1 
ATOM   980  O  O   . GLN A 1 83  ? 25.238  -11.678 -31.081 1.00 28.78  ? 83  GLN A O   1 
ATOM   981  C  CB  . GLN A 1 83  ? 26.326  -14.349 -30.530 1.00 34.04  ? 83  GLN A CB  1 
ATOM   982  C  CG  . GLN A 1 83  ? 25.246  -15.053 -31.350 1.00 31.06  ? 83  GLN A CG  1 
ATOM   983  C  CD  . GLN A 1 83  ? 24.490  -16.002 -30.462 1.00 31.56  ? 83  GLN A CD  1 
ATOM   984  O  OE1 . GLN A 1 83  ? 24.693  -16.031 -29.252 1.00 32.50  ? 83  GLN A OE1 1 
ATOM   985  N  NE2 . GLN A 1 83  ? 23.635  -16.809 -31.058 1.00 32.61  ? 83  GLN A NE2 1 
ATOM   986  N  N   . ASN A 1 84  ? 26.209  -11.941 -33.154 1.00 29.46  ? 84  ASN A N   1 
ATOM   987  C  CA  . ASN A 1 84  ? 25.378  -10.961 -33.881 1.00 27.34  ? 84  ASN A CA  1 
ATOM   988  C  C   . ASN A 1 84  ? 25.662  -9.638  -33.163 1.00 26.75  ? 84  ASN A C   1 
ATOM   989  O  O   . ASN A 1 84  ? 26.823  -9.281  -33.063 1.00 26.28  ? 84  ASN A O   1 
ATOM   990  C  CB  . ASN A 1 84  ? 23.947  -11.492 -33.991 1.00 26.54  ? 84  ASN A CB  1 
ATOM   991  C  CG  . ASN A 1 84  ? 23.902  -12.811 -34.729 1.00 28.12  ? 84  ASN A CG  1 
ATOM   992  O  OD1 . ASN A 1 84  ? 24.350  -12.878 -35.868 1.00 28.73  ? 84  ASN A OD1 1 
ATOM   993  N  ND2 . ASN A 1 84  ? 23.344  -13.847 -34.114 1.00 25.66  ? 84  ASN A ND2 1 
ATOM   994  N  N   A CYS A 1 85  ? 24.628  -8.957  -32.654 0.25 26.15  ? 85  CYS A N   1 
ATOM   995  N  N   B CYS A 1 85  ? 24.628  -8.957  -32.654 0.25 26.15  ? 85  CYS A N   1 
ATOM   996  N  N   C CYS A 1 85  ? 24.627  -8.963  -32.652 0.25 26.34  ? 85  CYS A N   1 
ATOM   997  N  N   D CYS A 1 85  ? 24.627  -8.963  -32.652 0.25 26.34  ? 85  CYS A N   1 
ATOM   998  C  CA  A CYS A 1 85  ? 24.732  -7.606  -32.034 0.25 26.25  ? 85  CYS A CA  1 
ATOM   999  C  CA  B CYS A 1 85  ? 24.732  -7.606  -32.034 0.25 26.25  ? 85  CYS A CA  1 
ATOM   1000 C  CA  C CYS A 1 85  ? 24.728  -7.610  -32.038 0.25 26.57  ? 85  CYS A CA  1 
ATOM   1001 C  CA  D CYS A 1 85  ? 24.728  -7.610  -32.038 0.25 26.57  ? 85  CYS A CA  1 
ATOM   1002 C  C   A CYS A 1 85  ? 24.793  -7.700  -30.502 0.25 27.24  ? 85  CYS A C   1 
ATOM   1003 C  C   B CYS A 1 85  ? 24.793  -7.700  -30.502 0.25 27.24  ? 85  CYS A C   1 
ATOM   1004 C  C   C CYS A 1 85  ? 24.782  -7.702  -30.504 0.25 27.45  ? 85  CYS A C   1 
ATOM   1005 C  C   D CYS A 1 85  ? 24.782  -7.702  -30.504 0.25 27.45  ? 85  CYS A C   1 
ATOM   1006 O  O   A CYS A 1 85  ? 24.702  -6.645  -29.835 0.25 25.80  ? 85  CYS A O   1 
ATOM   1007 O  O   B CYS A 1 85  ? 24.702  -6.645  -29.835 0.25 25.80  ? 85  CYS A O   1 
ATOM   1008 O  O   C CYS A 1 85  ? 24.688  -6.648  -29.839 0.25 26.04  ? 85  CYS A O   1 
ATOM   1009 O  O   D CYS A 1 85  ? 24.688  -6.648  -29.839 0.25 26.04  ? 85  CYS A O   1 
ATOM   1010 C  CB  A CYS A 1 85  ? 23.572  -6.727  -32.477 0.25 26.28  ? 85  CYS A CB  1 
ATOM   1011 C  CB  B CYS A 1 85  ? 23.572  -6.727  -32.477 0.25 26.28  ? 85  CYS A CB  1 
ATOM   1012 C  CB  C CYS A 1 85  ? 23.577  -6.733  -32.510 0.25 26.80  ? 85  CYS A CB  1 
ATOM   1013 C  CB  D CYS A 1 85  ? 23.577  -6.733  -32.510 0.25 26.80  ? 85  CYS A CB  1 
ATOM   1014 S  SG  A CYS A 1 85  ? 23.480  -6.556  -34.277 0.25 25.58  ? 85  CYS A SG  1 
ATOM   1015 S  SG  B CYS A 1 85  ? 23.480  -6.556  -34.277 0.25 25.58  ? 85  CYS A SG  1 
ATOM   1016 S  SG  C CYS A 1 85  ? 23.640  -6.421  -34.292 0.25 26.56  ? 85  CYS A SG  1 
ATOM   1017 S  SG  D CYS A 1 85  ? 23.640  -6.421  -34.292 0.25 26.56  ? 85  CYS A SG  1 
ATOM   1018 N  N   . VAL A 1 86  ? 24.964  -8.910  -29.960 1.00 27.82  ? 86  VAL A N   1 
ATOM   1019 C  CA  . VAL A 1 86  ? 25.030  -9.119  -28.489 1.00 29.68  ? 86  VAL A CA  1 
ATOM   1020 C  C   . VAL A 1 86  ? 26.445  -9.564  -28.095 1.00 29.58  ? 86  VAL A C   1 
ATOM   1021 O  O   . VAL A 1 86  ? 27.011  -10.482 -28.722 1.00 30.78  ? 86  VAL A O   1 
ATOM   1022 C  CB  . VAL A 1 86  ? 23.916  -10.077 -28.039 1.00 30.70  ? 86  VAL A CB  1 
ATOM   1023 C  CG1 . VAL A 1 86  ? 24.280  -10.849 -26.789 1.00 31.71  ? 86  VAL A CG1 1 
ATOM   1024 C  CG2 . VAL A 1 86  ? 22.613  -9.305  -27.843 1.00 31.22  ? 86  VAL A CG2 1 
ATOM   1025 N  N   . LEU A 1 87  ? 26.984  -8.894  -27.084 1.00 28.36  ? 87  LEU A N   1 
ATOM   1026 C  CA  . LEU A 1 87  ? 28.240  -9.290  -26.406 1.00 30.01  ? 87  LEU A CA  1 
ATOM   1027 C  C   . LEU A 1 87  ? 27.904  -10.289 -25.288 1.00 31.97  ? 87  LEU A C   1 
ATOM   1028 O  O   . LEU A 1 87  ? 26.859  -10.112 -24.598 1.00 27.83  ? 87  LEU A O   1 
ATOM   1029 C  CB  . LEU A 1 87  ? 28.847  -7.995  -25.880 1.00 33.61  ? 87  LEU A CB  1 
ATOM   1030 C  CG  . LEU A 1 87  ? 30.167  -8.106  -25.136 1.00 38.65  ? 87  LEU A CG  1 
ATOM   1031 C  CD1 . LEU A 1 87  ? 31.276  -8.587  -26.059 1.00 42.05  ? 87  LEU A CD1 1 
ATOM   1032 C  CD2 . LEU A 1 87  ? 30.523  -6.750  -24.540 1.00 42.26  ? 87  LEU A CD2 1 
ATOM   1033 N  N   . LYS A 1 88  ? 28.695  -11.353 -25.179 1.00 31.63  ? 88  LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 88  ? 28.592  -12.377 -24.119 1.00 33.37  ? 88  LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 88  ? 29.887  -12.332 -23.324 1.00 35.82  ? 88  LYS A C   1 
ATOM   1036 O  O   . LYS A 1 88  ? 30.931  -12.679 -23.894 1.00 36.60  ? 88  LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 88  ? 28.344  -13.762 -24.712 1.00 32.72  ? 88  LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 88  ? 27.108  -13.808 -25.591 1.00 38.01  ? 88  LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 88  ? 26.578  -15.188 -25.866 1.00 38.07  ? 88  LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 88  ? 27.195  -15.771 -27.109 1.00 41.00  ? 88  LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 88  ? 26.365  -16.870 -27.643 1.00 46.10  ? 88  LYS A NZ  1 
ATOM   1042 N  N   . LEU A 1 89  ? 29.808  -11.837 -22.091 1.00 36.57  ? 89  LEU A N   1 
ATOM   1043 C  CA  . LEU A 1 89  ? 30.922  -11.821 -21.119 1.00 36.81  ? 89  LEU A CA  1 
ATOM   1044 C  C   . LEU A 1 89  ? 30.779  -13.055 -20.233 1.00 41.42  ? 89  LEU A C   1 
ATOM   1045 O  O   . LEU A 1 89  ? 29.743  -13.163 -19.498 1.00 40.55  ? 89  LEU A O   1 
ATOM   1046 C  CB  . LEU A 1 89  ? 30.854  -10.533 -20.310 1.00 36.65  ? 89  LEU A CB  1 
ATOM   1047 C  CG  . LEU A 1 89  ? 30.762  -9.259  -21.137 1.00 33.68  ? 89  LEU A CG  1 
ATOM   1048 C  CD1 . LEU A 1 89  ? 30.747  -8.042  -20.233 1.00 31.47  ? 89  LEU A CD1 1 
ATOM   1049 C  CD2 . LEU A 1 89  ? 31.920  -9.184  -22.119 1.00 36.64  ? 89  LEU A CD2 1 
ATOM   1050 N  N   . LYS A 1 90  ? 31.740  -13.975 -20.346 1.00 41.62  ? 90  LYS A N   1 
ATOM   1051 C  CA  . LYS A 1 90  ? 31.847  -15.157 -19.455 1.00 44.12  ? 90  LYS A CA  1 
ATOM   1052 C  C   . LYS A 1 90  ? 32.391  -14.638 -18.130 1.00 43.78  ? 90  LYS A C   1 
ATOM   1053 O  O   . LYS A 1 90  ? 33.296  -13.746 -18.160 1.00 38.46  ? 90  LYS A O   1 
ATOM   1054 C  CB  . LYS A 1 90  ? 32.711  -16.243 -20.092 1.00 49.41  ? 90  LYS A CB  1 
ATOM   1055 C  CG  . LYS A 1 90  ? 32.633  -17.622 -19.453 1.00 54.19  ? 90  LYS A CG  1 
ATOM   1056 C  CD  . LYS A 1 90  ? 33.691  -18.541 -20.043 1.00 63.13  ? 90  LYS A CD  1 
ATOM   1057 C  CE  . LYS A 1 90  ? 33.901  -19.847 -19.304 1.00 67.41  ? 90  LYS A CE  1 
ATOM   1058 N  NZ  . LYS A 1 90  ? 35.147  -20.514 -19.756 1.00 70.48  ? 90  LYS A NZ  1 
ATOM   1059 N  N   . VAL A 1 91  ? 31.786  -15.088 -17.027 1.00 42.03  ? 91  VAL A N   1 
ATOM   1060 C  CA  . VAL A 1 91  ? 32.193  -14.701 -15.651 1.00 42.22  ? 91  VAL A CA  1 
ATOM   1061 C  C   . VAL A 1 91  ? 32.481  -15.984 -14.865 1.00 43.09  ? 91  VAL A C   1 
ATOM   1062 O  O   . VAL A 1 91  ? 32.110  -17.078 -15.353 1.00 41.59  ? 91  VAL A O   1 
ATOM   1063 C  CB  . VAL A 1 91  ? 31.146  -13.793 -14.974 1.00 45.28  ? 91  VAL A CB  1 
ATOM   1064 C  CG1 . VAL A 1 91  ? 31.205  -12.387 -15.549 1.00 50.48  ? 91  VAL A CG1 1 
ATOM   1065 C  CG2 . VAL A 1 91  ? 29.729  -14.343 -15.050 1.00 45.42  ? 91  VAL A CG2 1 
ATOM   1066 N  N   . ASP A 1 92  ? 33.150  -15.849 -13.718 1.00 44.81  ? 92  ASP A N   1 
ATOM   1067 C  CA  . ASP A 1 92  ? 33.668  -16.992 -12.908 1.00 53.52  ? 92  ASP A CA  1 
ATOM   1068 C  C   . ASP A 1 92  ? 32.632  -17.458 -11.869 1.00 52.31  ? 92  ASP A C   1 
ATOM   1069 O  O   . ASP A 1 92  ? 32.894  -18.488 -11.252 1.00 54.94  ? 92  ASP A O   1 
ATOM   1070 C  CB  . ASP A 1 92  ? 35.005  -16.655 -12.241 1.00 53.09  ? 92  ASP A CB  1 
ATOM   1071 C  CG  . ASP A 1 92  ? 34.946  -15.511 -11.242 1.00 58.28  ? 92  ASP A CG  1 
ATOM   1072 O  OD1 . ASP A 1 92  ? 33.965  -14.718 -11.279 1.00 59.68  ? 92  ASP A OD1 1 
ATOM   1073 O  OD2 . ASP A 1 92  ? 35.881  -15.418 -10.427 1.00 60.82  ? 92  ASP A OD2 1 
ATOM   1074 N  N   . THR A 1 93  ? 31.518  -16.731 -11.695 1.00 48.24  ? 93  THR A N   1 
ATOM   1075 C  CA  . THR A 1 93  ? 30.358  -17.078 -10.831 1.00 41.12  ? 93  THR A CA  1 
ATOM   1076 C  C   . THR A 1 93  ? 29.111  -17.300 -11.694 1.00 40.00  ? 93  THR A C   1 
ATOM   1077 O  O   . THR A 1 93  ? 28.780  -16.401 -12.467 1.00 35.63  ? 93  THR A O   1 
ATOM   1078 C  CB  . THR A 1 93  ? 30.015  -15.929 -9.876  1.00 44.59  ? 93  THR A CB  1 
ATOM   1079 O  OG1 . THR A 1 93  ? 31.205  -15.468 -9.242  1.00 45.06  ? 93  THR A OG1 1 
ATOM   1080 C  CG2 . THR A 1 93  ? 28.999  -16.322 -8.824  1.00 45.54  ? 93  THR A CG2 1 
ATOM   1081 N  N   . ALA A 1 94  ? 28.431  -18.434 -11.561 1.00 37.24  ? 94  ALA A N   1 
ATOM   1082 C  CA  . ALA A 1 94  ? 27.064  -18.633 -12.089 1.00 40.29  ? 94  ALA A CA  1 
ATOM   1083 C  C   . ALA A 1 94  ? 26.107  -17.838 -11.197 1.00 40.75  ? 94  ALA A C   1 
ATOM   1084 O  O   . ALA A 1 94  ? 26.366  -17.766 -9.988  1.00 42.14  ? 94  ALA A O   1 
ATOM   1085 C  CB  . ALA A 1 94  ? 26.686  -20.093 -12.134 1.00 41.82  ? 94  ALA A CB  1 
ATOM   1086 N  N   . ASN A 1 95  ? 25.084  -17.217 -11.781 1.00 39.38  ? 95  ASN A N   1 
ATOM   1087 C  CA  . ASN A 1 95  ? 24.094  -16.402 -11.030 1.00 37.00  ? 95  ASN A CA  1 
ATOM   1088 C  C   . ASN A 1 95  ? 23.291  -17.370 -10.173 1.00 32.97  ? 95  ASN A C   1 
ATOM   1089 O  O   . ASN A 1 95  ? 22.620  -18.250 -10.718 1.00 34.98  ? 95  ASN A O   1 
ATOM   1090 C  CB  . ASN A 1 95  ? 23.199  -15.597 -11.983 1.00 38.65  ? 95  ASN A CB  1 
ATOM   1091 C  CG  . ASN A 1 95  ? 22.210  -14.686 -11.281 1.00 37.22  ? 95  ASN A CG  1 
ATOM   1092 O  OD1 . ASN A 1 95  ? 22.282  -14.501 -10.061 1.00 34.09  ? 95  ASN A OD1 1 
ATOM   1093 N  ND2 . ASN A 1 95  ? 21.288  -14.121 -12.049 1.00 33.34  ? 95  ASN A ND2 1 
ATOM   1094 N  N   . PRO A 1 96  ? 23.311  -17.252 -8.824  1.00 35.54  ? 96  PRO A N   1 
ATOM   1095 C  CA  . PRO A 1 96  ? 22.521  -18.158 -7.987  1.00 36.79  ? 96  PRO A CA  1 
ATOM   1096 C  C   . PRO A 1 96  ? 21.012  -17.906 -8.157  1.00 37.19  ? 96  PRO A C   1 
ATOM   1097 O  O   . PRO A 1 96  ? 20.256  -18.785 -7.881  1.00 35.31  ? 96  PRO A O   1 
ATOM   1098 C  CB  . PRO A 1 96  ? 23.050  -17.925 -6.561  1.00 37.59  ? 96  PRO A CB  1 
ATOM   1099 C  CG  . PRO A 1 96  ? 23.729  -16.552 -6.595  1.00 37.99  ? 96  PRO A CG  1 
ATOM   1100 C  CD  . PRO A 1 96  ? 24.082  -16.267 -8.041  1.00 37.16  ? 96  PRO A CD  1 
ATOM   1101 N  N   . LYS A 1 97  ? 20.629  -16.763 -8.732  1.00 38.65  ? 97  LYS A N   1 
ATOM   1102 C  CA  . LYS A 1 97  ? 19.215  -16.371 -8.966  1.00 41.02  ? 97  LYS A CA  1 
ATOM   1103 C  C   . LYS A 1 97  ? 18.736  -16.754 -10.376 1.00 38.09  ? 97  LYS A C   1 
ATOM   1104 O  O   . LYS A 1 97  ? 17.613  -16.364 -10.733 1.00 33.47  ? 97  LYS A O   1 
ATOM   1105 C  CB  . LYS A 1 97  ? 19.098  -14.861 -8.750  1.00 41.70  ? 97  LYS A CB  1 
ATOM   1106 C  CG  . LYS A 1 97  ? 19.563  -14.411 -7.378  1.00 43.36  ? 97  LYS A CG  1 
ATOM   1107 C  CD  . LYS A 1 97  ? 19.147  -13.010 -7.030  1.00 45.29  ? 97  LYS A CD  1 
ATOM   1108 C  CE  . LYS A 1 97  ? 19.315  -12.725 -5.556  1.00 50.51  ? 97  LYS A CE  1 
ATOM   1109 N  NZ  . LYS A 1 97  ? 18.961  -11.328 -5.237  1.00 58.59  ? 97  LYS A NZ  1 
ATOM   1110 N  N   . THR A 1 98  ? 19.534  -17.479 -11.165 1.00 36.04  ? 98  THR A N   1 
ATOM   1111 C  CA  . THR A 1 98  ? 19.147  -17.865 -12.547 1.00 32.95  ? 98  THR A CA  1 
ATOM   1112 C  C   . THR A 1 98  ? 17.830  -18.615 -12.469 1.00 33.51  ? 98  THR A C   1 
ATOM   1113 O  O   . THR A 1 98  ? 17.763  -19.626 -11.804 1.00 39.47  ? 98  THR A O   1 
ATOM   1114 C  CB  . THR A 1 98  ? 20.214  -18.698 -13.270 1.00 31.35  ? 98  THR A CB  1 
ATOM   1115 O  OG1 . THR A 1 98  ? 21.422  -17.937 -13.266 1.00 31.59  ? 98  THR A OG1 1 
ATOM   1116 C  CG2 . THR A 1 98  ? 19.835  -19.040 -14.695 1.00 31.07  ? 98  THR A CG2 1 
ATOM   1117 N  N   . PRO A 1 99  ? 16.756  -18.152 -13.144 1.00 33.61  ? 99  PRO A N   1 
ATOM   1118 C  CA  . PRO A 1 99  ? 15.519  -18.919 -13.233 1.00 33.57  ? 99  PRO A CA  1 
ATOM   1119 C  C   . PRO A 1 99  ? 15.564  -19.969 -14.348 1.00 34.68  ? 99  PRO A C   1 
ATOM   1120 O  O   . PRO A 1 99  ? 16.453  -19.933 -15.145 1.00 33.30  ? 99  PRO A O   1 
ATOM   1121 C  CB  . PRO A 1 99  ? 14.486  -17.846 -13.608 1.00 34.83  ? 99  PRO A CB  1 
ATOM   1122 C  CG  . PRO A 1 99  ? 15.287  -16.858 -14.449 1.00 32.81  ? 99  PRO A CG  1 
ATOM   1123 C  CD  . PRO A 1 99  ? 16.678  -16.865 -13.857 1.00 32.44  ? 99  PRO A CD  1 
ATOM   1124 N  N   . LYS A 1 100 ? 14.576  -20.852 -14.398 1.00 36.08  ? 100 LYS A N   1 
ATOM   1125 C  CA  . LYS A 1 100 ? 14.281  -21.600 -15.634 1.00 39.71  ? 100 LYS A CA  1 
ATOM   1126 C  C   . LYS A 1 100 ? 14.057  -20.542 -16.721 1.00 41.31  ? 100 LYS A C   1 
ATOM   1127 O  O   . LYS A 1 100 ? 13.281  -19.579 -16.482 1.00 36.26  ? 100 LYS A O   1 
ATOM   1128 C  CB  . LYS A 1 100 ? 13.066  -22.510 -15.452 1.00 48.01  ? 100 LYS A CB  1 
ATOM   1129 C  CG  . LYS A 1 100 ? 13.197  -23.547 -14.345 1.00 57.19  ? 100 LYS A CG  1 
ATOM   1130 C  CD  . LYS A 1 100 ? 11.958  -24.390 -14.188 1.00 62.95  ? 100 LYS A CD  1 
ATOM   1131 C  CE  . LYS A 1 100 ? 12.239  -25.765 -13.621 1.00 69.45  ? 100 LYS A CE  1 
ATOM   1132 N  NZ  . LYS A 1 100 ? 11.119  -26.691 -13.918 1.00 72.92  ? 100 LYS A NZ  1 
ATOM   1133 N  N   . TYR A 1 101 ? 14.769  -20.645 -17.841 1.00 40.94  ? 101 TYR A N   1 
ATOM   1134 C  CA  . TYR A 1 101 ? 14.674  -19.646 -18.937 1.00 37.71  ? 101 TYR A CA  1 
ATOM   1135 C  C   . TYR A 1 101 ? 14.898  -20.307 -20.285 1.00 35.47  ? 101 TYR A C   1 
ATOM   1136 O  O   . TYR A 1 101 ? 15.375  -21.421 -20.378 1.00 33.15  ? 101 TYR A O   1 
ATOM   1137 C  CB  . TYR A 1 101 ? 15.651  -18.484 -18.748 1.00 36.04  ? 101 TYR A CB  1 
ATOM   1138 C  CG  . TYR A 1 101 ? 17.095  -18.798 -19.043 1.00 38.21  ? 101 TYR A CG  1 
ATOM   1139 C  CD1 . TYR A 1 101 ? 17.623  -18.631 -20.315 1.00 38.23  ? 101 TYR A CD1 1 
ATOM   1140 C  CD2 . TYR A 1 101 ? 17.942  -19.253 -18.048 1.00 36.40  ? 101 TYR A CD2 1 
ATOM   1141 C  CE1 . TYR A 1 101 ? 18.942  -18.943 -20.601 1.00 35.58  ? 101 TYR A CE1 1 
ATOM   1142 C  CE2 . TYR A 1 101 ? 19.267  -19.560 -18.312 1.00 37.77  ? 101 TYR A CE2 1 
ATOM   1143 C  CZ  . TYR A 1 101 ? 19.771  -19.394 -19.590 1.00 39.65  ? 101 TYR A CZ  1 
ATOM   1144 O  OH  . TYR A 1 101 ? 21.082  -19.683 -19.832 1.00 39.40  ? 101 TYR A OH  1 
ATOM   1145 N  N   . LYS A 1 102 ? 14.509  -19.576 -21.317 1.00 37.14  ? 102 LYS A N   1 
ATOM   1146 C  CA  . LYS A 1 102 ? 14.771  -19.898 -22.726 1.00 35.89  ? 102 LYS A CA  1 
ATOM   1147 C  C   . LYS A 1 102 ? 14.791  -18.574 -23.474 1.00 32.54  ? 102 LYS A C   1 
ATOM   1148 O  O   . LYS A 1 102 ? 14.247  -17.580 -22.947 1.00 29.72  ? 102 LYS A O   1 
ATOM   1149 C  CB  . LYS A 1 102 ? 13.684  -20.831 -23.263 1.00 38.53  ? 102 LYS A CB  1 
ATOM   1150 C  CG  . LYS A 1 102 ? 12.292  -20.216 -23.249 1.00 43.65  ? 102 LYS A CG  1 
ATOM   1151 C  CD  . LYS A 1 102 ? 11.289  -20.946 -24.083 1.00 46.74  ? 102 LYS A CD  1 
ATOM   1152 C  CE  . LYS A 1 102 ? 10.807  -22.218 -23.435 1.00 48.71  ? 102 LYS A CE  1 
ATOM   1153 N  NZ  . LYS A 1 102 ? 9.794   -22.862 -24.296 1.00 53.62  ? 102 LYS A NZ  1 
ATOM   1154 N  N   . PHE A 1 103 ? 15.342  -18.594 -24.677 1.00 31.00  ? 103 PHE A N   1 
ATOM   1155 C  CA  . PHE A 1 103 ? 15.370  -17.450 -25.609 1.00 30.89  ? 103 PHE A CA  1 
ATOM   1156 C  C   . PHE A 1 103 ? 14.414  -17.755 -26.740 1.00 31.92  ? 103 PHE A C   1 
ATOM   1157 O  O   . PHE A 1 103 ? 14.477  -18.867 -27.267 1.00 31.64  ? 103 PHE A O   1 
ATOM   1158 C  CB  . PHE A 1 103 ? 16.763  -17.210 -26.175 1.00 29.54  ? 103 PHE A CB  1 
ATOM   1159 C  CG  . PHE A 1 103 ? 17.807  -16.854 -25.156 1.00 28.13  ? 103 PHE A CG  1 
ATOM   1160 C  CD1 . PHE A 1 103 ? 17.452  -16.372 -23.901 1.00 30.03  ? 103 PHE A CD1 1 
ATOM   1161 C  CD2 . PHE A 1 103 ? 19.153  -16.960 -25.470 1.00 28.29  ? 103 PHE A CD2 1 
ATOM   1162 C  CE1 . PHE A 1 103 ? 18.420  -16.045 -22.967 1.00 25.90  ? 103 PHE A CE1 1 
ATOM   1163 C  CE2 . PHE A 1 103 ? 20.119  -16.618 -24.537 1.00 27.92  ? 103 PHE A CE2 1 
ATOM   1164 C  CZ  . PHE A 1 103 ? 19.749  -16.162 -23.288 1.00 28.76  ? 103 PHE A CZ  1 
ATOM   1165 N  N   . VAL A 1 104 ? 13.533  -16.811 -27.043 1.00 29.72  ? 104 VAL A N   1 
ATOM   1166 C  CA  . VAL A 1 104 ? 12.516  -16.974 -28.113 1.00 32.47  ? 104 VAL A CA  1 
ATOM   1167 C  C   . VAL A 1 104 ? 12.526  -15.680 -28.911 1.00 30.62  ? 104 VAL A C   1 
ATOM   1168 O  O   . VAL A 1 104 ? 12.519  -14.615 -28.273 1.00 30.94  ? 104 VAL A O   1 
ATOM   1169 C  CB  . VAL A 1 104 ? 11.102  -17.280 -27.582 1.00 35.94  ? 104 VAL A CB  1 
ATOM   1170 C  CG1 . VAL A 1 104 ? 10.919  -18.736 -27.208 1.00 41.64  ? 104 VAL A CG1 1 
ATOM   1171 C  CG2 . VAL A 1 104 ? 10.747  -16.412 -26.403 1.00 41.63  ? 104 VAL A CG2 1 
ATOM   1172 N  N   . ARG A 1 105 ? 12.554  -15.802 -30.236 1.00 29.22  ? 105 ARG A N   1 
ATOM   1173 C  CA  . ARG A 1 105 ? 12.303  -14.695 -31.189 1.00 28.41  ? 105 ARG A CA  1 
ATOM   1174 C  C   . ARG A 1 105 ? 10.814  -14.680 -31.475 1.00 27.41  ? 105 ARG A C   1 
ATOM   1175 O  O   . ARG A 1 105 ? 10.294  -15.717 -31.891 1.00 33.32  ? 105 ARG A O   1 
ATOM   1176 C  CB  . ARG A 1 105 ? 13.083  -14.857 -32.492 1.00 27.51  ? 105 ARG A CB  1 
ATOM   1177 C  CG  . ARG A 1 105 ? 13.044  -13.608 -33.363 1.00 28.15  ? 105 ARG A CG  1 
ATOM   1178 C  CD  . ARG A 1 105 ? 13.775  -13.817 -34.672 1.00 27.47  ? 105 ARG A CD  1 
ATOM   1179 N  NE  . ARG A 1 105 ? 13.754  -12.634 -35.521 1.00 26.90  ? 105 ARG A NE  1 
ATOM   1180 C  CZ  . ARG A 1 105 ? 14.549  -11.580 -35.395 1.00 27.48  ? 105 ARG A CZ  1 
ATOM   1181 N  NH1 . ARG A 1 105 ? 15.437  -11.504 -34.421 1.00 28.25  ? 105 ARG A NH1 1 
ATOM   1182 N  NH2 . ARG A 1 105 ? 14.447  -10.593 -36.255 1.00 28.73  ? 105 ARG A NH2 1 
ATOM   1183 N  N   . ILE A 1 106 ? 10.178  -13.540 -31.245 1.00 25.99  ? 106 ILE A N   1 
ATOM   1184 C  CA  . ILE A 1 106 ? 8.704   -13.364 -31.363 1.00 25.72  ? 106 ILE A CA  1 
ATOM   1185 C  C   . ILE A 1 106 ? 8.383   -12.734 -32.715 1.00 24.63  ? 106 ILE A C   1 
ATOM   1186 O  O   . ILE A 1 106 ? 9.299   -12.218 -33.360 1.00 26.86  ? 106 ILE A O   1 
ATOM   1187 C  CB  . ILE A 1 106 ? 8.175   -12.518 -30.201 1.00 25.77  ? 106 ILE A CB  1 
ATOM   1188 C  CG1 . ILE A 1 106 ? 8.815   -11.124 -30.164 1.00 26.62  ? 106 ILE A CG1 1 
ATOM   1189 C  CG2 . ILE A 1 106 ? 8.364   -13.284 -28.908 1.00 26.94  ? 106 ILE A CG2 1 
ATOM   1190 C  CD1 . ILE A 1 106 ? 8.084   -10.138 -29.288 1.00 28.49  ? 106 ILE A CD1 1 
ATOM   1191 N  N   . GLN A 1 107 ? 7.126   -12.784 -33.118 1.00 27.76  ? 107 GLN A N   1 
ATOM   1192 C  CA  . GLN A 1 107 ? 6.609   -12.190 -34.375 1.00 29.32  ? 107 GLN A CA  1 
ATOM   1193 C  C   . GLN A 1 107 ? 5.878   -10.892 -34.056 1.00 29.47  ? 107 GLN A C   1 
ATOM   1194 O  O   . GLN A 1 107 ? 5.425   -10.682 -32.927 1.00 27.96  ? 107 GLN A O   1 
ATOM   1195 C  CB  . GLN A 1 107 ? 5.666   -13.193 -35.039 1.00 31.08  ? 107 GLN A CB  1 
ATOM   1196 C  CG  . GLN A 1 107 ? 6.342   -14.531 -35.309 1.00 31.72  ? 107 GLN A CG  1 
ATOM   1197 C  CD  . GLN A 1 107 ? 7.363   -14.353 -36.398 1.00 35.87  ? 107 GLN A CD  1 
ATOM   1198 O  OE1 . GLN A 1 107 ? 7.109   -13.669 -37.387 1.00 35.44  ? 107 GLN A OE1 1 
ATOM   1199 N  NE2 . GLN A 1 107 ? 8.546   -14.910 -36.200 1.00 38.37  ? 107 GLN A NE2 1 
ATOM   1200 N  N   . PRO A 1 108 ? 5.757   -9.988  -35.055 1.00 30.18  ? 108 PRO A N   1 
ATOM   1201 C  CA  . PRO A 1 108 ? 4.931   -8.793  -34.920 1.00 28.94  ? 108 PRO A CA  1 
ATOM   1202 C  C   . PRO A 1 108 ? 3.578   -9.162  -34.300 1.00 28.74  ? 108 PRO A C   1 
ATOM   1203 O  O   . PRO A 1 108 ? 2.976   -10.177 -34.671 1.00 26.75  ? 108 PRO A O   1 
ATOM   1204 C  CB  . PRO A 1 108 ? 4.734   -8.294  -36.356 1.00 29.88  ? 108 PRO A CB  1 
ATOM   1205 C  CG  . PRO A 1 108 ? 5.943   -8.833  -37.103 1.00 33.16  ? 108 PRO A CG  1 
ATOM   1206 C  CD  . PRO A 1 108 ? 6.368   -10.105 -36.389 1.00 30.61  ? 108 PRO A CD  1 
ATOM   1207 N  N   . GLY A 1 109 ? 3.139   -8.356  -33.345 1.00 27.83  ? 109 GLY A N   1 
ATOM   1208 C  CA  . GLY A 1 109 ? 1.836   -8.545  -32.696 1.00 27.95  ? 109 GLY A CA  1 
ATOM   1209 C  C   . GLY A 1 109 ? 1.955   -9.241  -31.362 1.00 26.00  ? 109 GLY A C   1 
ATOM   1210 O  O   . GLY A 1 109 ? 1.047   -9.066  -30.549 1.00 26.92  ? 109 GLY A O   1 
ATOM   1211 N  N   . GLN A 1 110 ? 3.026   -9.999  -31.146 1.00 24.80  ? 110 GLN A N   1 
ATOM   1212 C  CA  . GLN A 1 110 ? 3.280   -10.642 -29.840 1.00 25.74  ? 110 GLN A CA  1 
ATOM   1213 C  C   . GLN A 1 110 ? 3.451   -9.519  -28.809 1.00 25.66  ? 110 GLN A C   1 
ATOM   1214 O  O   . GLN A 1 110 ? 3.972   -8.432  -29.140 1.00 26.09  ? 110 GLN A O   1 
ATOM   1215 C  CB  . GLN A 1 110 ? 4.507   -11.557 -29.931 1.00 25.28  ? 110 GLN A CB  1 
ATOM   1216 C  CG  . GLN A 1 110 ? 4.729   -12.426 -28.705 1.00 25.45  ? 110 GLN A CG  1 
ATOM   1217 C  CD  . GLN A 1 110 ? 3.525   -13.275 -28.365 1.00 27.58  ? 110 GLN A CD  1 
ATOM   1218 O  OE1 . GLN A 1 110 ? 2.662   -12.887 -27.564 1.00 26.24  ? 110 GLN A OE1 1 
ATOM   1219 N  NE2 . GLN A 1 110 ? 3.461   -14.447 -28.984 1.00 26.48  ? 110 GLN A NE2 1 
ATOM   1220 N  N   . THR A 1 111 ? 3.038   -9.788  -27.591 1.00 24.72  ? 111 THR A N   1 
ATOM   1221 C  CA  . THR A 1 111 ? 3.242   -8.912  -26.426 1.00 23.96  ? 111 THR A CA  1 
ATOM   1222 C  C   . THR A 1 111 ? 4.318   -9.506  -25.525 1.00 25.74  ? 111 THR A C   1 
ATOM   1223 O  O   . THR A 1 111 ? 4.593   -10.731 -25.612 1.00 25.15  ? 111 THR A O   1 
ATOM   1224 C  CB  . THR A 1 111 ? 1.929   -8.766  -25.655 1.00 23.49  ? 111 THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 111 ? 1.445   -10.075 -25.310 1.00 22.27  ? 111 THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 111 ? 0.938   -7.973  -26.468 1.00 22.97  ? 111 THR A CG2 1 
ATOM   1227 N  N   . PHE A 1 112 ? 4.884   -8.666  -24.662 1.00 26.58  ? 112 PHE A N   1 
ATOM   1228 C  CA  . PHE A 1 112 ? 5.840   -9.077  -23.606 1.00 26.07  ? 112 PHE A CA  1 
ATOM   1229 C  C   . PHE A 1 112 ? 5.906   -7.982  -22.542 1.00 25.46  ? 112 PHE A C   1 
ATOM   1230 O  O   . PHE A 1 112 ? 5.509   -6.829  -22.829 1.00 23.51  ? 112 PHE A O   1 
ATOM   1231 C  CB  . PHE A 1 112 ? 7.223   -9.370  -24.200 1.00 26.62  ? 112 PHE A CB  1 
ATOM   1232 C  CG  . PHE A 1 112 ? 7.791   -8.284  -25.080 1.00 26.76  ? 112 PHE A CG  1 
ATOM   1233 C  CD1 . PHE A 1 112 ? 7.475   -8.221  -26.433 1.00 29.04  ? 112 PHE A CD1 1 
ATOM   1234 C  CD2 . PHE A 1 112 ? 8.634   -7.320  -24.557 1.00 26.66  ? 112 PHE A CD2 1 
ATOM   1235 C  CE1 . PHE A 1 112 ? 8.012   -7.228  -27.243 1.00 31.38  ? 112 PHE A CE1 1 
ATOM   1236 C  CE2 . PHE A 1 112 ? 9.169   -6.331  -25.367 1.00 28.51  ? 112 PHE A CE2 1 
ATOM   1237 C  CZ  . PHE A 1 112 ? 8.860   -6.279  -26.707 1.00 28.75  ? 112 PHE A CZ  1 
ATOM   1238 N  N   . SER A 1 113 ? 6.437   -8.337  -21.366 1.00 25.93  ? 113 SER A N   1 
ATOM   1239 C  CA  . SER A 1 113 ? 6.757   -7.386  -20.270 1.00 25.64  ? 113 SER A CA  1 
ATOM   1240 C  C   . SER A 1 113 ? 8.150   -6.799  -20.496 1.00 26.58  ? 113 SER A C   1 
ATOM   1241 O  O   . SER A 1 113 ? 9.054   -7.513  -20.946 1.00 27.16  ? 113 SER A O   1 
ATOM   1242 C  CB  . SER A 1 113 ? 6.613   -8.053  -18.933 1.00 25.96  ? 113 SER A CB  1 
ATOM   1243 O  OG  . SER A 1 113 ? 5.300   -8.587  -18.781 1.00 23.07  ? 113 SER A OG  1 
ATOM   1244 N  N   . VAL A 1 114 ? 8.332   -5.520  -20.191 1.00 27.85  ? 114 VAL A N   1 
ATOM   1245 C  CA  . VAL A 1 114 ? 9.679   -4.898  -20.172 1.00 24.04  ? 114 VAL A CA  1 
ATOM   1246 C  C   . VAL A 1 114 ? 10.033  -4.506  -18.732 1.00 24.77  ? 114 VAL A C   1 
ATOM   1247 O  O   . VAL A 1 114 ? 9.237   -3.834  -18.083 1.00 22.23  ? 114 VAL A O   1 
ATOM   1248 C  CB  . VAL A 1 114 ? 9.729   -3.693  -21.122 1.00 24.65  ? 114 VAL A CB  1 
ATOM   1249 C  CG1 . VAL A 1 114 ? 11.028  -2.923  -20.963 1.00 23.15  ? 114 VAL A CG1 1 
ATOM   1250 C  CG2 . VAL A 1 114 ? 9.516   -4.133  -22.562 1.00 25.53  ? 114 VAL A CG2 1 
ATOM   1251 N  N   . LEU A 1 115 ? 11.221  -4.890  -18.277 1.00 23.25  ? 115 LEU A N   1 
ATOM   1252 C  CA  . LEU A 1 115 ? 11.786  -4.436  -16.985 1.00 24.92  ? 115 LEU A CA  1 
ATOM   1253 C  C   . LEU A 1 115 ? 12.771  -3.303  -17.292 1.00 23.89  ? 115 LEU A C   1 
ATOM   1254 O  O   . LEU A 1 115 ? 13.938  -3.575  -17.651 1.00 22.78  ? 115 LEU A O   1 
ATOM   1255 C  CB  . LEU A 1 115 ? 12.475  -5.597  -16.263 1.00 24.97  ? 115 LEU A CB  1 
ATOM   1256 C  CG  . LEU A 1 115 ? 13.041  -5.205  -14.899 1.00 25.41  ? 115 LEU A CG  1 
ATOM   1257 C  CD1 . LEU A 1 115 ? 11.915  -4.737  -14.004 1.00 25.51  ? 115 LEU A CD1 1 
ATOM   1258 C  CD2 . LEU A 1 115 ? 13.799  -6.344  -14.250 1.00 26.09  ? 115 LEU A CD2 1 
ATOM   1259 N  N   . ALA A 1 116 ? 12.297  -2.061  -17.266 1.00 22.76  ? 116 ALA A N   1 
ATOM   1260 C  CA  . ALA A 1 116 ? 13.171  -0.905  -17.550 1.00 23.86  ? 116 ALA A CA  1 
ATOM   1261 C  C   . ALA A 1 116 ? 14.192  -0.804  -16.404 1.00 23.56  ? 116 ALA A C   1 
ATOM   1262 O  O   . ALA A 1 116 ? 13.772  -0.829  -15.261 1.00 21.11  ? 116 ALA A O   1 
ATOM   1263 C  CB  . ALA A 1 116 ? 12.371  0.354   -17.718 1.00 23.50  ? 116 ALA A CB  1 
ATOM   1264 N  N   . CYS A 1 117 ? 15.487  -0.723  -16.726 1.00 24.84  ? 117 CYS A N   1 
ATOM   1265 C  CA  . CYS A 1 117 ? 16.600  -0.709  -15.747 1.00 26.55  ? 117 CYS A CA  1 
ATOM   1266 C  C   . CYS A 1 117 ? 17.603  0.401   -16.061 1.00 29.11  ? 117 CYS A C   1 
ATOM   1267 O  O   . CYS A 1 117 ? 17.839  0.720   -17.259 1.00 27.16  ? 117 CYS A O   1 
ATOM   1268 C  CB  . CYS A 1 117 ? 17.333  -2.038  -15.745 1.00 28.62  ? 117 CYS A CB  1 
ATOM   1269 S  SG  . CYS A 1 117 ? 16.298  -3.414  -15.191 1.00 30.64  ? 117 CYS A SG  1 
ATOM   1270 N  N   . TYR A 1 118 ? 18.190  0.964   -15.012 1.00 30.27  ? 118 TYR A N   1 
ATOM   1271 C  CA  . TYR A 1 118 ? 19.275  1.968   -15.119 1.00 31.36  ? 118 TYR A CA  1 
ATOM   1272 C  C   . TYR A 1 118 ? 20.368  1.565   -14.134 1.00 32.76  ? 118 TYR A C   1 
ATOM   1273 O  O   . TYR A 1 118 ? 20.015  1.277   -12.955 1.00 31.36  ? 118 TYR A O   1 
ATOM   1274 C  CB  . TYR A 1 118 ? 18.696  3.360   -14.888 1.00 31.43  ? 118 TYR A CB  1 
ATOM   1275 C  CG  . TYR A 1 118 ? 17.623  3.712   -15.884 1.00 30.81  ? 118 TYR A CG  1 
ATOM   1276 C  CD1 . TYR A 1 118 ? 17.938  4.249   -17.120 1.00 29.66  ? 118 TYR A CD1 1 
ATOM   1277 C  CD2 . TYR A 1 118 ? 16.294  3.457   -15.611 1.00 30.91  ? 118 TYR A CD2 1 
ATOM   1278 C  CE1 . TYR A 1 118 ? 16.955  4.536   -18.056 1.00 32.21  ? 118 TYR A CE1 1 
ATOM   1279 C  CE2 . TYR A 1 118 ? 15.296  3.746   -16.530 1.00 32.41  ? 118 TYR A CE2 1 
ATOM   1280 C  CZ  . TYR A 1 118 ? 15.625  4.282   -17.763 1.00 32.29  ? 118 TYR A CZ  1 
ATOM   1281 O  OH  . TYR A 1 118 ? 14.644  4.566   -18.674 1.00 30.62  ? 118 TYR A OH  1 
ATOM   1282 N  N   . ASN A 1 119 ? 21.611  1.447   -14.619 1.00 30.24  ? 119 ASN A N   1 
ATOM   1283 C  CA  . ASN A 1 119 ? 22.791  1.099   -13.784 1.00 31.01  ? 119 ASN A CA  1 
ATOM   1284 C  C   . ASN A 1 119 ? 22.583  -0.270  -13.136 1.00 31.52  ? 119 ASN A C   1 
ATOM   1285 O  O   . ASN A 1 119 ? 23.026  -0.446  -11.995 1.00 33.69  ? 119 ASN A O   1 
ATOM   1286 C  CB  . ASN A 1 119 ? 23.031  2.152   -12.711 1.00 31.69  ? 119 ASN A CB  1 
ATOM   1287 C  CG  . ASN A 1 119 ? 23.354  3.489   -13.340 1.00 34.21  ? 119 ASN A CG  1 
ATOM   1288 O  OD1 . ASN A 1 119 ? 22.606  4.442   -13.191 1.00 40.40  ? 119 ASN A OD1 1 
ATOM   1289 N  ND2 . ASN A 1 119 ? 24.467  3.563   -14.045 1.00 34.38  ? 119 ASN A ND2 1 
ATOM   1290 N  N   . GLY A 1 120 ? 21.951  -1.208  -13.848 1.00 28.31  ? 120 GLY A N   1 
ATOM   1291 C  CA  . GLY A 1 120 ? 21.696  -2.575  -13.359 1.00 30.06  ? 120 GLY A CA  1 
ATOM   1292 C  C   . GLY A 1 120 ? 20.615  -2.639  -12.281 1.00 30.12  ? 120 GLY A C   1 
ATOM   1293 O  O   . GLY A 1 120 ? 20.435  -3.716  -11.742 1.00 32.36  ? 120 GLY A O   1 
ATOM   1294 N  N   . SER A 1 121 ? 19.875  -1.557  -12.033 1.00 30.09  ? 121 SER A N   1 
ATOM   1295 C  CA  . SER A 1 121 ? 18.765  -1.506  -11.044 1.00 31.50  ? 121 SER A CA  1 
ATOM   1296 C  C   . SER A 1 121 ? 17.417  -1.287  -11.734 1.00 30.20  ? 121 SER A C   1 
ATOM   1297 O  O   . SER A 1 121 ? 17.245  -0.372  -12.526 1.00 24.52  ? 121 SER A O   1 
ATOM   1298 C  CB  . SER A 1 121 ? 19.025  -0.432  -10.045 1.00 31.13  ? 121 SER A CB  1 
ATOM   1299 O  OG  . SER A 1 121 ? 20.232  -0.693  -9.348  1.00 36.37  ? 121 SER A OG  1 
ATOM   1300 N  N   . PRO A 1 122 ? 16.388  -2.078  -11.384 1.00 34.43  ? 122 PRO A N   1 
ATOM   1301 C  CA  . PRO A 1 122 ? 15.083  -1.986  -12.036 1.00 36.80  ? 122 PRO A CA  1 
ATOM   1302 C  C   . PRO A 1 122 ? 14.364  -0.686  -11.659 1.00 33.11  ? 122 PRO A C   1 
ATOM   1303 O  O   . PRO A 1 122 ? 14.395  -0.307  -10.512 1.00 33.65  ? 122 PRO A O   1 
ATOM   1304 C  CB  . PRO A 1 122 ? 14.278  -3.174  -11.506 1.00 37.98  ? 122 PRO A CB  1 
ATOM   1305 C  CG  . PRO A 1 122 ? 15.225  -3.934  -10.592 1.00 40.63  ? 122 PRO A CG  1 
ATOM   1306 C  CD  . PRO A 1 122 ? 16.392  -3.031  -10.269 1.00 38.87  ? 122 PRO A CD  1 
ATOM   1307 N  N   . SER A 1 123 ? 13.748  -0.040  -12.640 1.00 31.53  ? 123 SER A N   1 
ATOM   1308 C  CA  . SER A 1 123 ? 12.978  1.220   -12.473 1.00 32.65  ? 123 SER A CA  1 
ATOM   1309 C  C   . SER A 1 123 ? 11.469  0.927   -12.536 1.00 32.89  ? 123 SER A C   1 
ATOM   1310 O  O   . SER A 1 123 ? 10.711  1.507   -11.754 1.00 29.60  ? 123 SER A O   1 
ATOM   1311 C  CB  . SER A 1 123 ? 13.393  2.225   -13.508 1.00 35.24  ? 123 SER A CB  1 
ATOM   1312 O  OG  . SER A 1 123 ? 12.731  3.471   -13.319 1.00 42.78  ? 123 SER A OG  1 
ATOM   1313 N  N   . GLY A 1 124 ? 11.032  0.056   -13.438 1.00 29.78  ? 124 GLY A N   1 
ATOM   1314 C  CA  . GLY A 1 124 ? 9.589   -0.210  -13.600 1.00 32.31  ? 124 GLY A CA  1 
ATOM   1315 C  C   . GLY A 1 124 ? 9.330   -1.377  -14.523 1.00 27.92  ? 124 GLY A C   1 
ATOM   1316 O  O   . GLY A 1 124 ? 10.252  -1.764  -15.274 1.00 26.05  ? 124 GLY A O   1 
ATOM   1317 N  N   . VAL A 1 125 ? 8.116   -1.908  -14.482 1.00 27.11  ? 125 VAL A N   1 
ATOM   1318 C  CA  . VAL A 1 125 ? 7.700   -3.001  -15.399 1.00 26.55  ? 125 VAL A CA  1 
ATOM   1319 C  C   . VAL A 1 125 ? 6.461   -2.546  -16.158 1.00 27.08  ? 125 VAL A C   1 
ATOM   1320 O  O   . VAL A 1 125 ? 5.553   -1.991  -15.504 1.00 24.53  ? 125 VAL A O   1 
ATOM   1321 C  CB  . VAL A 1 125 ? 7.488   -4.333  -14.647 1.00 28.41  ? 125 VAL A CB  1 
ATOM   1322 C  CG1 . VAL A 1 125 ? 6.371   -4.268  -13.646 1.00 31.46  ? 125 VAL A CG1 1 
ATOM   1323 C  CG2 . VAL A 1 125 ? 7.265   -5.502  -15.588 1.00 29.29  ? 125 VAL A CG2 1 
ATOM   1324 N  N   . TYR A 1 126 ? 6.414   -2.790  -17.477 1.00 25.06  ? 126 TYR A N   1 
ATOM   1325 C  CA  . TYR A 1 126 ? 5.216   -2.499  -18.309 1.00 24.99  ? 126 TYR A CA  1 
ATOM   1326 C  C   . TYR A 1 126 ? 5.126   -3.449  -19.493 1.00 24.14  ? 126 TYR A C   1 
ATOM   1327 O  O   . TYR A 1 126 ? 6.117   -4.128  -19.858 1.00 22.41  ? 126 TYR A O   1 
ATOM   1328 C  CB  . TYR A 1 126 ? 5.240   -1.036  -18.782 1.00 26.05  ? 126 TYR A CB  1 
ATOM   1329 C  CG  . TYR A 1 126 ? 6.498   -0.630  -19.508 1.00 25.39  ? 126 TYR A CG  1 
ATOM   1330 C  CD1 . TYR A 1 126 ? 6.670   -0.893  -20.857 1.00 23.73  ? 126 TYR A CD1 1 
ATOM   1331 C  CD2 . TYR A 1 126 ? 7.528   0.017   -18.838 1.00 27.56  ? 126 TYR A CD2 1 
ATOM   1332 C  CE1 . TYR A 1 126 ? 7.832   -0.539  -21.521 1.00 25.55  ? 126 TYR A CE1 1 
ATOM   1333 C  CE2 . TYR A 1 126 ? 8.682   0.404   -19.497 1.00 26.50  ? 126 TYR A CE2 1 
ATOM   1334 C  CZ  . TYR A 1 126 ? 8.836   0.128   -20.845 1.00 26.40  ? 126 TYR A CZ  1 
ATOM   1335 O  OH  . TYR A 1 126 ? 9.980   0.527   -21.471 1.00 27.45  ? 126 TYR A OH  1 
ATOM   1336 N  N   . GLN A 1 127 ? 3.953   -3.433  -20.115 1.00 25.48  ? 127 GLN A N   1 
ATOM   1337 C  CA  . GLN A 1 127 ? 3.607   -4.243  -21.304 1.00 28.87  ? 127 GLN A CA  1 
ATOM   1338 C  C   . GLN A 1 127 ? 3.866   -3.473  -22.593 1.00 28.07  ? 127 GLN A C   1 
ATOM   1339 O  O   . GLN A 1 127 ? 3.582   -2.254  -22.670 1.00 29.83  ? 127 GLN A O   1 
ATOM   1340 C  CB  . GLN A 1 127 ? 2.129   -4.624  -21.330 1.00 30.83  ? 127 GLN A CB  1 
ATOM   1341 C  CG  . GLN A 1 127 ? 1.812   -5.799  -20.434 1.00 31.73  ? 127 GLN A CG  1 
ATOM   1342 C  CD  . GLN A 1 127 ? 2.549   -7.047  -20.852 1.00 32.14  ? 127 GLN A CD  1 
ATOM   1343 O  OE1 . GLN A 1 127 ? 3.543   -7.440  -20.251 1.00 33.91  ? 127 GLN A OE1 1 
ATOM   1344 N  NE2 . GLN A 1 127 ? 2.023   -7.713  -21.858 1.00 29.94  ? 127 GLN A NE2 1 
ATOM   1345 N  N   A CYS A 1 128 ? 4.418   -4.190  -23.581 0.35 27.89  ? 128 CYS A N   1 
ATOM   1346 N  N   B CYS A 1 128 ? 4.356   -4.169  -23.615 0.15 28.46  ? 128 CYS A N   1 
ATOM   1347 N  N   C CYS A 1 128 ? 4.418   -4.190  -23.581 0.35 27.89  ? 128 CYS A N   1 
ATOM   1348 N  N   D CYS A 1 128 ? 4.356   -4.169  -23.615 0.15 28.46  ? 128 CYS A N   1 
ATOM   1349 C  CA  A CYS A 1 128 ? 4.673   -3.748  -24.977 0.35 26.71  ? 128 CYS A CA  1 
ATOM   1350 C  CA  B CYS A 1 128 ? 4.455   -3.625  -24.989 0.15 28.03  ? 128 CYS A CA  1 
ATOM   1351 C  CA  C CYS A 1 128 ? 4.673   -3.748  -24.977 0.35 26.70  ? 128 CYS A CA  1 
ATOM   1352 C  CA  D CYS A 1 128 ? 4.455   -3.625  -24.989 0.15 28.03  ? 128 CYS A CA  1 
ATOM   1353 C  C   A CYS A 1 128 ? 4.193   -4.818  -25.960 0.35 26.69  ? 128 CYS A C   1 
ATOM   1354 C  C   B CYS A 1 128 ? 4.391   -4.769  -26.001 0.15 27.50  ? 128 CYS A C   1 
ATOM   1355 C  C   C CYS A 1 128 ? 4.193   -4.818  -25.960 0.35 26.69  ? 128 CYS A C   1 
ATOM   1356 C  C   D CYS A 1 128 ? 4.391   -4.769  -26.001 0.15 27.50  ? 128 CYS A C   1 
ATOM   1357 O  O   A CYS A 1 128 ? 4.046   -5.986  -25.537 0.35 25.48  ? 128 CYS A O   1 
ATOM   1358 O  O   B CYS A 1 128 ? 4.704   -5.924  -25.640 0.15 26.67  ? 128 CYS A O   1 
ATOM   1359 O  O   C CYS A 1 128 ? 4.046   -5.987  -25.537 0.35 25.48  ? 128 CYS A O   1 
ATOM   1360 O  O   D CYS A 1 128 ? 4.704   -5.924  -25.640 0.15 26.67  ? 128 CYS A O   1 
ATOM   1361 C  CB  A CYS A 1 128 ? 6.157   -3.558  -25.248 0.35 27.02  ? 128 CYS A CB  1 
ATOM   1362 C  CB  B CYS A 1 128 ? 5.719   -2.795  -25.167 0.15 28.64  ? 128 CYS A CB  1 
ATOM   1363 C  CB  C CYS A 1 128 ? 6.158   -3.558  -25.248 0.35 27.01  ? 128 CYS A CB  1 
ATOM   1364 C  CB  D CYS A 1 128 ? 5.719   -2.795  -25.167 0.15 28.64  ? 128 CYS A CB  1 
ATOM   1365 S  SG  A CYS A 1 128 ? 6.821   -2.002  -24.611 0.35 28.73  ? 128 CYS A SG  1 
ATOM   1366 S  SG  B CYS A 1 128 ? 7.238   -3.759  -24.975 0.15 30.61  ? 128 CYS A SG  1 
ATOM   1367 S  SG  C CYS A 1 128 ? 6.821   -2.003  -24.611 0.35 28.73  ? 128 CYS A SG  1 
ATOM   1368 S  SG  D CYS A 1 128 ? 7.238   -3.759  -24.975 0.15 30.61  ? 128 CYS A SG  1 
ATOM   1369 N  N   . ALA A 1 129 ? 3.989   -4.425  -27.221 1.00 27.01  ? 129 ALA A N   1 
ATOM   1370 C  CA  . ALA A 1 129 ? 3.834   -5.349  -28.358 1.00 27.52  ? 129 ALA A CA  1 
ATOM   1371 C  C   . ALA A 1 129 ? 4.950   -5.065  -29.361 1.00 26.81  ? 129 ALA A C   1 
ATOM   1372 O  O   . ALA A 1 129 ? 5.412   -3.926  -29.467 1.00 29.46  ? 129 ALA A O   1 
ATOM   1373 C  CB  . ALA A 1 129 ? 2.492   -5.129  -28.982 1.00 27.42  ? 129 ALA A CB  1 
ATOM   1374 N  N   . MET A 1 130 ? 5.389   -6.080  -30.076 1.00 26.09  ? 130 MET A N   1 
ATOM   1375 C  CA  . MET A 1 130 ? 6.236   -5.905  -31.279 1.00 25.68  ? 130 MET A CA  1 
ATOM   1376 C  C   . MET A 1 130 ? 5.315   -5.344  -32.381 1.00 27.72  ? 130 MET A C   1 
ATOM   1377 O  O   . MET A 1 130 ? 4.396   -6.069  -32.819 1.00 27.09  ? 130 MET A O   1 
ATOM   1378 C  CB  . MET A 1 130 ? 6.839   -7.258  -31.668 1.00 27.42  ? 130 MET A CB  1 
ATOM   1379 C  CG  . MET A 1 130 ? 7.776   -7.235  -32.859 1.00 28.21  ? 130 MET A CG  1 
ATOM   1380 S  SD  . MET A 1 130 ? 9.100   -6.044  -32.649 1.00 28.78  ? 130 MET A SD  1 
ATOM   1381 C  CE  . MET A 1 130 ? 10.011  -6.774  -31.282 1.00 25.60  ? 130 MET A CE  1 
ATOM   1382 N  N   . ARG A 1 131 ? 5.486   -4.075  -32.762 1.00 24.98  ? 131 ARG A N   1 
ATOM   1383 C  CA  . ARG A 1 131 ? 4.677   -3.447  -33.831 1.00 26.07  ? 131 ARG A CA  1 
ATOM   1384 C  C   . ARG A 1 131 ? 4.928   -4.163  -35.159 1.00 25.99  ? 131 ARG A C   1 
ATOM   1385 O  O   . ARG A 1 131 ? 5.975   -4.771  -35.371 1.00 25.80  ? 131 ARG A O   1 
ATOM   1386 C  CB  . ARG A 1 131 ? 5.014   -1.961  -33.976 1.00 27.08  ? 131 ARG A CB  1 
ATOM   1387 C  CG  . ARG A 1 131 ? 4.785   -1.118  -32.730 1.00 28.91  ? 131 ARG A CG  1 
ATOM   1388 C  CD  . ARG A 1 131 ? 3.439   -1.274  -32.078 1.00 27.90  ? 131 ARG A CD  1 
ATOM   1389 N  NE  . ARG A 1 131 ? 2.358   -1.011  -33.011 1.00 28.77  ? 131 ARG A NE  1 
ATOM   1390 C  CZ  . ARG A 1 131 ? 1.058   -1.128  -32.717 1.00 30.27  ? 131 ARG A CZ  1 
ATOM   1391 N  NH1 . ARG A 1 131 ? 0.656   -1.429  -31.488 1.00 24.87  ? 131 ARG A NH1 1 
ATOM   1392 N  NH2 . ARG A 1 131 ? 0.167   -0.933  -33.673 1.00 30.78  ? 131 ARG A NH2 1 
ATOM   1393 N  N   . PRO A 1 132 ? 3.956   -4.130  -36.092 1.00 25.24  ? 132 PRO A N   1 
ATOM   1394 C  CA  . PRO A 1 132 ? 4.162   -4.645  -37.442 1.00 24.52  ? 132 PRO A CA  1 
ATOM   1395 C  C   . PRO A 1 132 ? 5.432   -4.098  -38.097 1.00 24.89  ? 132 PRO A C   1 
ATOM   1396 O  O   . PRO A 1 132 ? 5.986   -4.800  -38.884 1.00 25.54  ? 132 PRO A O   1 
ATOM   1397 C  CB  . PRO A 1 132 ? 2.903   -4.170  -38.178 1.00 24.16  ? 132 PRO A CB  1 
ATOM   1398 C  CG  . PRO A 1 132 ? 1.848   -4.202  -37.092 1.00 23.19  ? 132 PRO A CG  1 
ATOM   1399 C  CD  . PRO A 1 132 ? 2.576   -3.688  -35.865 1.00 23.80  ? 132 PRO A CD  1 
ATOM   1400 N  N   . ASN A 1 133 ? 5.857   -2.881  -37.746 1.00 25.76  ? 133 ASN A N   1 
ATOM   1401 C  CA  . ASN A 1 133 ? 7.079   -2.263  -38.321 1.00 27.32  ? 133 ASN A CA  1 
ATOM   1402 C  C   . ASN A 1 133 ? 8.307   -2.633  -37.479 1.00 28.91  ? 133 ASN A C   1 
ATOM   1403 O  O   . ASN A 1 133 ? 9.341   -2.009  -37.694 1.00 26.85  ? 133 ASN A O   1 
ATOM   1404 C  CB  . ASN A 1 133 ? 6.947   -0.745  -38.469 1.00 28.95  ? 133 ASN A CB  1 
ATOM   1405 C  CG  . ASN A 1 133 ? 6.896   0.016   -37.158 1.00 28.14  ? 133 ASN A CG  1 
ATOM   1406 O  OD1 . ASN A 1 133 ? 7.053   -0.554  -36.079 1.00 30.18  ? 133 ASN A OD1 1 
ATOM   1407 N  ND2 . ASN A 1 133 ? 6.671   1.311   -37.254 1.00 25.15  ? 133 ASN A ND2 1 
ATOM   1408 N  N   . PHE A 1 134 ? 8.201   -3.615  -36.569 1.00 28.98  ? 134 PHE A N   1 
ATOM   1409 C  CA  . PHE A 1 134 ? 9.344   -4.219  -35.841 1.00 28.30  ? 134 PHE A CA  1 
ATOM   1410 C  C   . PHE A 1 134 ? 9.963   -3.219  -34.865 1.00 29.03  ? 134 PHE A C   1 
ATOM   1411 O  O   . PHE A 1 134 ? 11.164  -3.381  -34.513 1.00 31.25  ? 134 PHE A O   1 
ATOM   1412 C  CB  . PHE A 1 134 ? 10.425  -4.704  -36.808 1.00 28.47  ? 134 PHE A CB  1 
ATOM   1413 C  CG  . PHE A 1 134 ? 9.938   -5.827  -37.669 1.00 31.12  ? 134 PHE A CG  1 
ATOM   1414 C  CD1 . PHE A 1 134 ? 9.890   -7.119  -37.167 1.00 36.77  ? 134 PHE A CD1 1 
ATOM   1415 C  CD2 . PHE A 1 134 ? 9.498   -5.587  -38.959 1.00 35.94  ? 134 PHE A CD2 1 
ATOM   1416 C  CE1 . PHE A 1 134 ? 9.409   -8.163  -37.948 1.00 38.20  ? 134 PHE A CE1 1 
ATOM   1417 C  CE2 . PHE A 1 134 ? 9.029   -6.630  -39.744 1.00 37.11  ? 134 PHE A CE2 1 
ATOM   1418 C  CZ  . PHE A 1 134 ? 8.984   -7.913  -39.234 1.00 36.49  ? 134 PHE A CZ  1 
ATOM   1419 N  N   . THR A 1 135 ? 9.190   -2.225  -34.436 1.00 27.65  ? 135 THR A N   1 
ATOM   1420 C  CA  . THR A 1 135 ? 9.566   -1.351  -33.307 1.00 27.26  ? 135 THR A CA  1 
ATOM   1421 C  C   . THR A 1 135 ? 8.679   -1.690  -32.117 1.00 27.35  ? 135 THR A C   1 
ATOM   1422 O  O   . THR A 1 135 ? 7.691   -2.442  -32.297 1.00 26.93  ? 135 THR A O   1 
ATOM   1423 C  CB  . THR A 1 135 ? 9.480   0.124   -33.709 1.00 29.73  ? 135 THR A CB  1 
ATOM   1424 O  OG1 . THR A 1 135 ? 8.121   0.464   -34.001 1.00 28.51  ? 135 THR A OG1 1 
ATOM   1425 C  CG2 . THR A 1 135 ? 10.338  0.429   -34.919 1.00 30.53  ? 135 THR A CG2 1 
ATOM   1426 N  N   . ILE A 1 136 ? 9.018   -1.129  -30.956 1.00 24.43  ? 136 ILE A N   1 
ATOM   1427 C  CA  . ILE A 1 136 ? 8.164   -1.156  -29.739 1.00 25.47  ? 136 ILE A CA  1 
ATOM   1428 C  C   . ILE A 1 136 ? 8.025   0.288   -29.243 1.00 25.99  ? 136 ILE A C   1 
ATOM   1429 O  O   . ILE A 1 136 ? 8.957   1.102   -29.479 1.00 25.86  ? 136 ILE A O   1 
ATOM   1430 C  CB  . ILE A 1 136 ? 8.731   -2.138  -28.692 1.00 26.31  ? 136 ILE A CB  1 
ATOM   1431 C  CG1 . ILE A 1 136 ? 9.903   -1.550  -27.905 1.00 26.22  ? 136 ILE A CG1 1 
ATOM   1432 C  CG2 . ILE A 1 136 ? 9.112   -3.449  -29.371 1.00 25.89  ? 136 ILE A CG2 1 
ATOM   1433 C  CD1 . ILE A 1 136 ? 10.404  -2.441  -26.803 1.00 27.42  ? 136 ILE A CD1 1 
ATOM   1434 N  N   . LYS A 1 137 ? 6.866   0.613   -28.676 1.00 29.36  ? 137 LYS A N   1 
ATOM   1435 C  CA  . LYS A 1 137 ? 6.568   1.949   -28.087 1.00 30.72  ? 137 LYS A CA  1 
ATOM   1436 C  C   . LYS A 1 137 ? 6.824   1.809   -26.589 1.00 30.20  ? 137 LYS A C   1 
ATOM   1437 O  O   . LYS A 1 137 ? 5.942   1.380   -25.847 1.00 27.10  ? 137 LYS A O   1 
ATOM   1438 C  CB  . LYS A 1 137 ? 5.149   2.408   -28.437 1.00 36.94  ? 137 LYS A CB  1 
ATOM   1439 C  CG  . LYS A 1 137 ? 4.840   2.416   -29.930 1.00 40.91  ? 137 LYS A CG  1 
ATOM   1440 C  CD  . LYS A 1 137 ? 3.414   2.849   -30.252 1.00 45.53  ? 137 LYS A CD  1 
ATOM   1441 C  CE  . LYS A 1 137 ? 3.226   3.030   -31.741 1.00 53.31  ? 137 LYS A CE  1 
ATOM   1442 N  NZ  . LYS A 1 137 ? 1.797   3.196   -32.095 1.00 58.59  ? 137 LYS A NZ  1 
ATOM   1443 N  N   . GLY A 1 138 ? 8.074   2.013   -26.202 1.00 27.27  ? 138 GLY A N   1 
ATOM   1444 C  CA  . GLY A 1 138 ? 8.523   1.764   -24.833 1.00 27.20  ? 138 GLY A CA  1 
ATOM   1445 C  C   . GLY A 1 138 ? 8.644   3.054   -24.077 1.00 25.26  ? 138 GLY A C   1 
ATOM   1446 O  O   . GLY A 1 138 ? 8.191   4.088   -24.575 1.00 24.40  ? 138 GLY A O   1 
ATOM   1447 N  N   . SER A 1 139 ? 9.247   2.962   -22.908 1.00 24.49  ? 139 SER A N   1 
ATOM   1448 C  CA  . SER A 1 139 ? 9.599   4.106   -22.044 1.00 25.91  ? 139 SER A CA  1 
ATOM   1449 C  C   . SER A 1 139 ? 11.019  3.838   -21.551 1.00 25.59  ? 139 SER A C   1 
ATOM   1450 O  O   . SER A 1 139 ? 11.205  2.947   -20.736 1.00 25.28  ? 139 SER A O   1 
ATOM   1451 C  CB  . SER A 1 139 ? 8.587   4.282   -20.927 1.00 25.27  ? 139 SER A CB  1 
ATOM   1452 O  OG  . SER A 1 139 ? 9.072   5.246   -20.013 1.00 26.55  ? 139 SER A OG  1 
ATOM   1453 N  N   . PHE A 1 140 ? 11.964  4.543   -22.152 1.00 27.60  ? 140 PHE A N   1 
ATOM   1454 C  CA  . PHE A 1 140 ? 13.409  4.259   -22.138 1.00 29.54  ? 140 PHE A CA  1 
ATOM   1455 C  C   . PHE A 1 140 ? 14.164  5.589   -22.180 1.00 31.77  ? 140 PHE A C   1 
ATOM   1456 O  O   . PHE A 1 140 ? 14.006  6.374   -23.144 1.00 33.13  ? 140 PHE A O   1 
ATOM   1457 C  CB  . PHE A 1 140 ? 13.789  3.429   -23.360 1.00 28.05  ? 140 PHE A CB  1 
ATOM   1458 C  CG  . PHE A 1 140 ? 13.367  1.985   -23.334 1.00 28.65  ? 140 PHE A CG  1 
ATOM   1459 C  CD1 . PHE A 1 140 ? 13.713  1.165   -22.273 1.00 31.91  ? 140 PHE A CD1 1 
ATOM   1460 C  CD2 . PHE A 1 140 ? 12.681  1.423   -24.397 1.00 29.44  ? 140 PHE A CD2 1 
ATOM   1461 C  CE1 . PHE A 1 140 ? 13.394  -0.183  -22.271 1.00 31.02  ? 140 PHE A CE1 1 
ATOM   1462 C  CE2 . PHE A 1 140 ? 12.368  0.070   -24.397 1.00 30.16  ? 140 PHE A CE2 1 
ATOM   1463 C  CZ  . PHE A 1 140 ? 12.739  -0.734  -23.348 1.00 30.22  ? 140 PHE A CZ  1 
ATOM   1464 N  N   . LEU A 1 141 ? 14.966  5.830   -21.153 1.00 33.05  ? 141 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 141 ? 15.843  7.014   -21.065 1.00 36.03  ? 141 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 141 ? 17.281  6.570   -21.350 1.00 37.08  ? 141 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 141 ? 17.536  5.345   -21.488 1.00 35.84  ? 141 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 141 ? 15.675  7.628   -19.676 1.00 38.51  ? 141 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 141 ? 14.260  8.083   -19.325 1.00 39.87  ? 141 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 141 ? 14.192  8.568   -17.880 1.00 43.66  ? 141 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 141 ? 13.780  9.178   -20.263 1.00 41.63  ? 141 LEU A CD2 1 
ATOM   1472 N  N   . ASN A 1 142 ? 18.194  7.527   -21.490 1.00 39.76  ? 142 ASN A N   1 
ATOM   1473 C  CA  . ASN A 1 142 ? 19.639  7.220   -21.612 1.00 41.16  ? 142 ASN A CA  1 
ATOM   1474 C  C   . ASN A 1 142 ? 20.006  6.285   -20.451 1.00 37.52  ? 142 ASN A C   1 
ATOM   1475 O  O   . ASN A 1 142 ? 19.535  6.510   -19.307 1.00 34.42  ? 142 ASN A O   1 
ATOM   1476 C  CB  . ASN A 1 142 ? 20.482  8.496   -21.705 1.00 48.35  ? 142 ASN A CB  1 
ATOM   1477 C  CG  . ASN A 1 142 ? 20.330  9.213   -23.039 1.00 58.78  ? 142 ASN A CG  1 
ATOM   1478 O  OD1 . ASN A 1 142 ? 19.811  8.666   -24.021 1.00 60.13  ? 142 ASN A OD1 1 
ATOM   1479 N  ND2 . ASN A 1 142 ? 20.801  10.448  -23.098 1.00 63.31  ? 142 ASN A ND2 1 
ATOM   1480 N  N   . GLY A 1 143 ? 20.737  5.217   -20.757 1.00 33.10  ? 143 GLY A N   1 
ATOM   1481 C  CA  . GLY A 1 143 ? 21.234  4.263   -19.753 1.00 32.07  ? 143 GLY A CA  1 
ATOM   1482 C  C   . GLY A 1 143 ? 20.346  3.037   -19.658 1.00 30.31  ? 143 GLY A C   1 
ATOM   1483 O  O   . GLY A 1 143 ? 20.708  2.123   -18.904 1.00 26.41  ? 143 GLY A O   1 
ATOM   1484 N  N   . SER A 1 144 ? 19.241  2.984   -20.415 1.00 28.97  ? 144 SER A N   1 
ATOM   1485 C  CA  . SER A 1 144 ? 18.281  1.851   -20.358 1.00 27.05  ? 144 SER A CA  1 
ATOM   1486 C  C   . SER A 1 144 ? 18.671  0.693   -21.272 1.00 26.53  ? 144 SER A C   1 
ATOM   1487 O  O   . SER A 1 144 ? 18.050  -0.373  -21.161 1.00 25.59  ? 144 SER A O   1 
ATOM   1488 C  CB  . SER A 1 144 ? 16.855  2.275   -20.672 1.00 27.97  ? 144 SER A CB  1 
ATOM   1489 O  OG  . SER A 1 144 ? 16.790  2.966   -21.896 1.00 28.78  ? 144 SER A OG  1 
ATOM   1490 N  N   A CYS A 1 145 ? 19.657  0.897   -22.156 0.25 26.04  ? 145 CYS A N   1 
ATOM   1491 N  N   B CYS A 1 145 ? 19.657  0.897   -22.156 0.25 26.04  ? 145 CYS A N   1 
ATOM   1492 N  N   C CYS A 1 145 ? 19.631  0.897   -22.182 0.25 26.90  ? 145 CYS A N   1 
ATOM   1493 N  N   D CYS A 1 145 ? 19.631  0.897   -22.182 0.25 26.90  ? 145 CYS A N   1 
ATOM   1494 C  CA  A CYS A 1 145 ? 20.172  -0.143  -23.088 0.25 25.35  ? 145 CYS A CA  1 
ATOM   1495 C  CA  B CYS A 1 145 ? 20.172  -0.143  -23.088 0.25 25.35  ? 145 CYS A CA  1 
ATOM   1496 C  CA  C CYS A 1 145 ? 20.095  -0.162  -23.118 0.25 26.67  ? 145 CYS A CA  1 
ATOM   1497 C  CA  D CYS A 1 145 ? 20.095  -0.162  -23.118 0.25 26.67  ? 145 CYS A CA  1 
ATOM   1498 C  C   A CYS A 1 145 ? 20.524  -1.403  -22.292 0.25 24.81  ? 145 CYS A C   1 
ATOM   1499 C  C   B CYS A 1 145 ? 20.524  -1.403  -22.292 0.25 24.81  ? 145 CYS A C   1 
ATOM   1500 C  C   C CYS A 1 145 ? 20.513  -1.394  -22.311 0.25 25.54  ? 145 CYS A C   1 
ATOM   1501 C  C   D CYS A 1 145 ? 20.513  -1.394  -22.311 0.25 25.54  ? 145 CYS A C   1 
ATOM   1502 O  O   A CYS A 1 145 ? 21.083  -1.264  -21.188 0.25 24.70  ? 145 CYS A O   1 
ATOM   1503 O  O   B CYS A 1 145 ? 21.083  -1.264  -21.188 0.25 24.70  ? 145 CYS A O   1 
ATOM   1504 O  O   C CYS A 1 145 ? 21.100  -1.226  -21.227 0.25 25.49  ? 145 CYS A O   1 
ATOM   1505 O  O   D CYS A 1 145 ? 21.100  -1.226  -21.227 0.25 25.49  ? 145 CYS A O   1 
ATOM   1506 C  CB  A CYS A 1 145 ? 21.380  0.363   -23.865 0.25 25.47  ? 145 CYS A CB  1 
ATOM   1507 C  CB  B CYS A 1 145 ? 21.380  0.363   -23.865 0.25 25.47  ? 145 CYS A CB  1 
ATOM   1508 C  CB  C CYS A 1 145 ? 21.228  0.320   -24.013 0.25 27.65  ? 145 CYS A CB  1 
ATOM   1509 C  CB  D CYS A 1 145 ? 21.228  0.320   -24.013 0.25 27.65  ? 145 CYS A CB  1 
ATOM   1510 S  SG  A CYS A 1 145 ? 21.002  1.820   -24.875 0.25 24.68  ? 145 CYS A SG  1 
ATOM   1511 S  SG  B CYS A 1 145 ? 21.002  1.820   -24.875 0.25 24.68  ? 145 CYS A SG  1 
ATOM   1512 S  SG  C CYS A 1 145 ? 20.632  1.326   -25.394 0.25 28.54  ? 145 CYS A SG  1 
ATOM   1513 S  SG  D CYS A 1 145 ? 20.632  1.326   -25.394 0.25 28.54  ? 145 CYS A SG  1 
ATOM   1514 N  N   . GLY A 1 146 ? 20.164  -2.581  -22.809 1.00 24.62  ? 146 GLY A N   1 
ATOM   1515 C  CA  . GLY A 1 146 ? 20.377  -3.852  -22.097 1.00 25.86  ? 146 GLY A CA  1 
ATOM   1516 C  C   . GLY A 1 146 ? 19.176  -4.255  -21.241 1.00 24.29  ? 146 GLY A C   1 
ATOM   1517 O  O   . GLY A 1 146 ? 19.164  -5.429  -20.815 1.00 22.56  ? 146 GLY A O   1 
ATOM   1518 N  N   . SER A 1 147 ? 18.202  -3.358  -21.001 1.00 23.89  ? 147 SER A N   1 
ATOM   1519 C  CA  . SER A 1 147 ? 16.862  -3.714  -20.449 1.00 22.21  ? 147 SER A CA  1 
ATOM   1520 C  C   . SER A 1 147 ? 16.257  -4.778  -21.370 1.00 21.42  ? 147 SER A C   1 
ATOM   1521 O  O   . SER A 1 147 ? 16.514  -4.714  -22.550 1.00 21.49  ? 147 SER A O   1 
ATOM   1522 C  CB  . SER A 1 147 ? 15.939  -2.528  -20.321 1.00 22.70  ? 147 SER A CB  1 
ATOM   1523 O  OG  . SER A 1 147 ? 16.404  -1.592  -19.362 1.00 23.04  ? 147 SER A OG  1 
ATOM   1524 N  N   . VAL A 1 148 ? 15.504  -5.733  -20.839 1.00 20.74  ? 148 VAL A N   1 
ATOM   1525 C  CA  . VAL A 1 148 ? 14.988  -6.887  -21.612 1.00 20.84  ? 148 VAL A CA  1 
ATOM   1526 C  C   . VAL A 1 148 ? 13.475  -6.956  -21.524 1.00 21.57  ? 148 VAL A C   1 
ATOM   1527 O  O   . VAL A 1 148 ? 12.871  -6.380  -20.589 1.00 22.51  ? 148 VAL A O   1 
ATOM   1528 C  CB  . VAL A 1 148 ? 15.616  -8.211  -21.164 1.00 22.24  ? 148 VAL A CB  1 
ATOM   1529 C  CG1 . VAL A 1 148 ? 17.113  -8.178  -21.381 1.00 22.55  ? 148 VAL A CG1 1 
ATOM   1530 C  CG2 . VAL A 1 148 ? 15.278  -8.559  -19.730 1.00 22.80  ? 148 VAL A CG2 1 
ATOM   1531 N  N   . GLY A 1 149 ? 12.901  -7.630  -22.514 1.00 21.33  ? 149 GLY A N   1 
ATOM   1532 C  CA  . GLY A 1 149 ? 11.482  -7.987  -22.550 1.00 21.18  ? 149 GLY A CA  1 
ATOM   1533 C  C   . GLY A 1 149 ? 11.331  -9.482  -22.419 1.00 23.57  ? 149 GLY A C   1 
ATOM   1534 O  O   . GLY A 1 149 ? 12.193  -10.234 -22.956 1.00 22.64  ? 149 GLY A O   1 
ATOM   1535 N  N   . PHE A 1 150 ? 10.255  -9.925  -21.776 1.00 24.44  ? 150 PHE A N   1 
ATOM   1536 C  CA  . PHE A 1 150 ? 10.101  -11.348 -21.430 1.00 25.28  ? 150 PHE A CA  1 
ATOM   1537 C  C   . PHE A 1 150 ? 8.625   -11.683 -21.283 1.00 27.46  ? 150 PHE A C   1 
ATOM   1538 O  O   . PHE A 1 150 ? 7.820   -10.770 -21.059 1.00 25.46  ? 150 PHE A O   1 
ATOM   1539 C  CB  . PHE A 1 150 ? 10.887  -11.653 -20.154 1.00 25.92  ? 150 PHE A CB  1 
ATOM   1540 C  CG  . PHE A 1 150 ? 10.465  -10.800 -18.983 1.00 26.67  ? 150 PHE A CG  1 
ATOM   1541 C  CD1 . PHE A 1 150 ? 10.957  -9.512  -18.826 1.00 29.05  ? 150 PHE A CD1 1 
ATOM   1542 C  CD2 . PHE A 1 150 ? 9.560   -11.275 -18.051 1.00 27.09  ? 150 PHE A CD2 1 
ATOM   1543 C  CE1 . PHE A 1 150 ? 10.535  -8.710  -17.769 1.00 30.03  ? 150 PHE A CE1 1 
ATOM   1544 C  CE2 . PHE A 1 150 ? 9.129   -10.472 -17.004 1.00 28.08  ? 150 PHE A CE2 1 
ATOM   1545 C  CZ  . PHE A 1 150 ? 9.619   -9.195  -16.859 1.00 28.92  ? 150 PHE A CZ  1 
ATOM   1546 N  N   . ASN A 1 151 ? 8.315   -12.978 -21.424 1.00 29.85  ? 151 ASN A N   1 
ATOM   1547 C  CA  . ASN A 1 151 ? 7.071   -13.606 -20.927 1.00 31.02  ? 151 ASN A CA  1 
ATOM   1548 C  C   . ASN A 1 151 ? 7.449   -14.631 -19.854 1.00 33.89  ? 151 ASN A C   1 
ATOM   1549 O  O   . ASN A 1 151 ? 8.628   -15.096 -19.800 1.00 32.36  ? 151 ASN A O   1 
ATOM   1550 C  CB  . ASN A 1 151 ? 6.229   -14.197 -22.051 1.00 29.77  ? 151 ASN A CB  1 
ATOM   1551 C  CG  . ASN A 1 151 ? 5.659   -13.112 -22.942 1.00 31.58  ? 151 ASN A CG  1 
ATOM   1552 O  OD1 . ASN A 1 151 ? 4.706   -12.439 -22.568 1.00 34.36  ? 151 ASN A OD1 1 
ATOM   1553 N  ND2 . ASN A 1 151 ? 6.246   -12.919 -24.115 1.00 30.70  ? 151 ASN A ND2 1 
ATOM   1554 N  N   . ILE A 1 152 ? 6.501   -14.909 -18.968 1.00 34.81  ? 152 ILE A N   1 
ATOM   1555 C  CA  . ILE A 1 152 ? 6.644   -15.999 -17.970 1.00 38.18  ? 152 ILE A CA  1 
ATOM   1556 C  C   . ILE A 1 152 ? 5.358   -16.813 -18.009 1.00 43.24  ? 152 ILE A C   1 
ATOM   1557 O  O   . ILE A 1 152 ? 4.566   -16.720 -17.061 1.00 44.11  ? 152 ILE A O   1 
ATOM   1558 C  CB  . ILE A 1 152 ? 6.925   -15.475 -16.552 1.00 37.03  ? 152 ILE A CB  1 
ATOM   1559 C  CG1 . ILE A 1 152 ? 8.012   -14.397 -16.517 1.00 35.84  ? 152 ILE A CG1 1 
ATOM   1560 C  CG2 . ILE A 1 152 ? 7.248   -16.656 -15.636 1.00 37.74  ? 152 ILE A CG2 1 
ATOM   1561 C  CD1 . ILE A 1 152 ? 8.430   -13.974 -15.107 1.00 33.67  ? 152 ILE A CD1 1 
ATOM   1562 N  N   . ASP A 1 153 ? 5.158   -17.575 -19.072 1.00 48.66  ? 153 ASP A N   1 
ATOM   1563 C  CA  . ASP A 1 153 ? 4.125   -18.635 -19.073 1.00 59.66  ? 153 ASP A CA  1 
ATOM   1564 C  C   . ASP A 1 153 ? 4.770   -19.823 -18.343 1.00 61.29  ? 153 ASP A C   1 
ATOM   1565 O  O   . ASP A 1 153 ? 5.906   -20.179 -18.712 1.00 58.15  ? 153 ASP A O   1 
ATOM   1566 C  CB  . ASP A 1 153 ? 3.586   -18.822 -20.497 1.00 60.46  ? 153 ASP A CB  1 
ATOM   1567 C  CG  . ASP A 1 153 ? 3.028   -17.532 -21.100 1.00 58.79  ? 153 ASP A CG  1 
ATOM   1568 O  OD1 . ASP A 1 153 ? 2.282   -16.820 -20.393 1.00 58.64  ? 153 ASP A OD1 1 
ATOM   1569 O  OD2 . ASP A 1 153 ? 3.359   -17.228 -22.264 1.00 49.68  ? 153 ASP A OD2 1 
ATOM   1570 N  N   . TYR A 1 154 ? 4.137   -20.262 -17.241 1.00 69.72  ? 154 TYR A N   1 
ATOM   1571 C  CA  . TYR A 1 154 ? 4.312   -21.564 -16.535 1.00 75.72  ? 154 TYR A CA  1 
ATOM   1572 C  C   . TYR A 1 154 ? 5.718   -21.717 -15.929 1.00 71.86  ? 154 TYR A C   1 
ATOM   1573 O  O   . TYR A 1 154 ? 6.370   -22.747 -16.175 1.00 82.92  ? 154 TYR A O   1 
ATOM   1574 C  CB  . TYR A 1 154 ? 3.974   -22.718 -17.488 1.00 85.16  ? 154 TYR A CB  1 
ATOM   1575 C  CG  . TYR A 1 154 ? 2.831   -22.434 -18.434 1.00 92.60  ? 154 TYR A CG  1 
ATOM   1576 C  CD1 . TYR A 1 154 ? 1.544   -22.215 -17.963 1.00 95.82  ? 154 TYR A CD1 1 
ATOM   1577 C  CD2 . TYR A 1 154 ? 3.036   -22.371 -19.805 1.00 95.26  ? 154 TYR A CD2 1 
ATOM   1578 C  CE1 . TYR A 1 154 ? 0.493   -21.944 -18.829 1.00 96.87  ? 154 TYR A CE1 1 
ATOM   1579 C  CE2 . TYR A 1 154 ? 1.996   -22.105 -20.684 1.00 95.36  ? 154 TYR A CE2 1 
ATOM   1580 C  CZ  . TYR A 1 154 ? 0.720   -21.889 -20.196 1.00 94.85  ? 154 TYR A CZ  1 
ATOM   1581 O  OH  . TYR A 1 154 ? -0.294  -21.627 -21.072 1.00 90.93  ? 154 TYR A OH  1 
ATOM   1582 N  N   . ASP A 1 155 ? 6.168   -20.749 -15.130 1.00 65.55  ? 155 ASP A N   1 
ATOM   1583 C  CA  . ASP A 1 155 ? 7.413   -20.838 -14.309 1.00 66.04  ? 155 ASP A CA  1 
ATOM   1584 C  C   . ASP A 1 155 ? 8.698   -20.689 -15.142 1.00 61.04  ? 155 ASP A C   1 
ATOM   1585 O  O   . ASP A 1 155 ? 9.762   -20.467 -14.511 1.00 55.97  ? 155 ASP A O   1 
ATOM   1586 C  CB  . ASP A 1 155 ? 7.510   -22.164 -13.545 1.00 73.75  ? 155 ASP A CB  1 
ATOM   1587 C  CG  . ASP A 1 155 ? 7.588   -22.012 -12.030 1.00 82.10  ? 155 ASP A CG  1 
ATOM   1588 O  OD1 . ASP A 1 155 ? 7.776   -20.871 -11.549 1.00 83.95  ? 155 ASP A OD1 1 
ATOM   1589 O  OD2 . ASP A 1 155 ? 7.465   -23.041 -11.339 1.00 87.22  ? 155 ASP A OD2 1 
ATOM   1590 N  N   . CYS A 1 156 ? 8.645   -20.840 -16.474 1.00 49.70  ? 156 CYS A N   1 
ATOM   1591 C  CA  . CYS A 1 156 ? 9.818   -20.636 -17.369 1.00 43.24  ? 156 CYS A CA  1 
ATOM   1592 C  C   . CYS A 1 156 ? 9.843   -19.189 -17.891 1.00 35.72  ? 156 CYS A C   1 
ATOM   1593 O  O   . CYS A 1 156 ? 8.825   -18.732 -18.436 1.00 35.60  ? 156 CYS A O   1 
ATOM   1594 C  CB  . CYS A 1 156 ? 9.797   -21.613 -18.537 1.00 41.36  ? 156 CYS A CB  1 
ATOM   1595 S  SG  . CYS A 1 156 ? 11.215  -21.402 -19.648 1.00 45.21  ? 156 CYS A SG  1 
ATOM   1596 N  N   . VAL A 1 157 ? 10.975  -18.500 -17.771 1.00 33.56  ? 157 VAL A N   1 
ATOM   1597 C  CA  . VAL A 1 157 ? 11.132  -17.105 -18.269 1.00 32.94  ? 157 VAL A CA  1 
ATOM   1598 C  C   . VAL A 1 157 ? 11.581  -17.139 -19.732 1.00 32.26  ? 157 VAL A C   1 
ATOM   1599 O  O   . VAL A 1 157 ? 12.738  -17.517 -19.963 1.00 30.81  ? 157 VAL A O   1 
ATOM   1600 C  CB  . VAL A 1 157 ? 12.138  -16.310 -17.427 1.00 33.14  ? 157 VAL A CB  1 
ATOM   1601 C  CG1 . VAL A 1 157 ? 12.419  -14.958 -18.070 1.00 34.89  ? 157 VAL A CG1 1 
ATOM   1602 C  CG2 . VAL A 1 157 ? 11.660  -16.136 -15.991 1.00 33.91  ? 157 VAL A CG2 1 
ATOM   1603 N  N   . SER A 1 158 ? 10.726  -16.702 -20.666 1.00 28.55  ? 158 SER A N   1 
ATOM   1604 C  CA  . SER A 1 158 ? 11.069  -16.617 -22.105 1.00 29.98  ? 158 SER A CA  1 
ATOM   1605 C  C   . SER A 1 158 ? 11.560  -15.186 -22.417 1.00 30.93  ? 158 SER A C   1 
ATOM   1606 O  O   . SER A 1 158 ? 10.728  -14.223 -22.418 1.00 28.16  ? 158 SER A O   1 
ATOM   1607 C  CB  . SER A 1 158 ? 9.933   -17.092 -22.981 1.00 32.77  ? 158 SER A CB  1 
ATOM   1608 O  OG  . SER A 1 158 ? 8.756   -16.326 -22.769 1.00 41.37  ? 158 SER A OG  1 
ATOM   1609 N  N   . PHE A 1 159 ? 12.882  -15.031 -22.589 1.00 26.37  ? 159 PHE A N   1 
ATOM   1610 C  CA  . PHE A 1 159 ? 13.525  -13.762 -22.968 1.00 26.39  ? 159 PHE A CA  1 
ATOM   1611 C  C   . PHE A 1 159 ? 13.361  -13.566 -24.473 1.00 27.37  ? 159 PHE A C   1 
ATOM   1612 O  O   . PHE A 1 159 ? 13.855  -14.413 -25.259 1.00 28.00  ? 159 PHE A O   1 
ATOM   1613 C  CB  . PHE A 1 159 ? 14.992  -13.757 -22.558 1.00 29.29  ? 159 PHE A CB  1 
ATOM   1614 C  CG  . PHE A 1 159 ? 15.204  -13.732 -21.071 1.00 29.48  ? 159 PHE A CG  1 
ATOM   1615 C  CD1 . PHE A 1 159 ? 14.974  -12.574 -20.348 1.00 28.97  ? 159 PHE A CD1 1 
ATOM   1616 C  CD2 . PHE A 1 159 ? 15.614  -14.872 -20.402 1.00 28.95  ? 159 PHE A CD2 1 
ATOM   1617 C  CE1 . PHE A 1 159 ? 15.175  -12.560 -18.977 1.00 28.71  ? 159 PHE A CE1 1 
ATOM   1618 C  CE2 . PHE A 1 159 ? 15.814  -14.852 -19.036 1.00 28.56  ? 159 PHE A CE2 1 
ATOM   1619 C  CZ  . PHE A 1 159 ? 15.596  -13.693 -18.331 1.00 29.45  ? 159 PHE A CZ  1 
ATOM   1620 N  N   . CYS A 1 160 ? 12.738  -12.458 -24.877 1.00 25.45  ? 160 CYS A N   1 
ATOM   1621 C  CA  . CYS A 1 160 ? 12.411  -12.244 -26.301 1.00 25.34  ? 160 CYS A CA  1 
ATOM   1622 C  C   . CYS A 1 160 ? 12.962  -10.928 -26.830 1.00 24.59  ? 160 CYS A C   1 
ATOM   1623 O  O   . CYS A 1 160 ? 12.920  -10.789 -28.057 1.00 24.59  ? 160 CYS A O   1 
ATOM   1624 C  CB  . CYS A 1 160 ? 10.916  -12.352 -26.553 1.00 27.29  ? 160 CYS A CB  1 
ATOM   1625 S  SG  . CYS A 1 160 ? 9.936   -11.111 -25.684 1.00 30.34  ? 160 CYS A SG  1 
ATOM   1626 N  N   . TYR A 1 161 ? 13.447  -10.018 -25.972 1.00 24.08  ? 161 TYR A N   1 
ATOM   1627 C  CA  . TYR A 1 161 ? 13.883  -8.671  -26.422 1.00 23.74  ? 161 TYR A CA  1 
ATOM   1628 C  C   . TYR A 1 161 ? 14.982  -8.115  -25.514 1.00 23.43  ? 161 TYR A C   1 
ATOM   1629 O  O   . TYR A 1 161 ? 14.887  -8.287  -24.278 1.00 22.73  ? 161 TYR A O   1 
ATOM   1630 C  CB  . TYR A 1 161 ? 12.680  -7.732  -26.507 1.00 23.62  ? 161 TYR A CB  1 
ATOM   1631 C  CG  . TYR A 1 161 ? 13.005  -6.304  -26.887 1.00 23.75  ? 161 TYR A CG  1 
ATOM   1632 C  CD1 . TYR A 1 161 ? 13.314  -5.350  -25.934 1.00 24.23  ? 161 TYR A CD1 1 
ATOM   1633 C  CD2 . TYR A 1 161 ? 13.030  -5.904  -28.213 1.00 24.92  ? 161 TYR A CD2 1 
ATOM   1634 C  CE1 . TYR A 1 161 ? 13.602  -4.032  -26.277 1.00 22.41  ? 161 TYR A CE1 1 
ATOM   1635 C  CE2 . TYR A 1 161 ? 13.335  -4.601  -28.576 1.00 24.16  ? 161 TYR A CE2 1 
ATOM   1636 C  CZ  . TYR A 1 161 ? 13.616  -3.660  -27.611 1.00 23.93  ? 161 TYR A CZ  1 
ATOM   1637 O  OH  . TYR A 1 161 ? 13.891  -2.385  -28.028 1.00 24.33  ? 161 TYR A OH  1 
ATOM   1638 N  N   . MET A 1 162 ? 15.991  -7.458  -26.117 1.00 22.48  ? 162 MET A N   1 
ATOM   1639 C  CA  . MET A 1 162 ? 17.020  -6.637  -25.424 1.00 23.27  ? 162 MET A CA  1 
ATOM   1640 C  C   . MET A 1 162 ? 17.051  -5.262  -26.094 1.00 21.94  ? 162 MET A C   1 
ATOM   1641 O  O   . MET A 1 162 ? 17.071  -5.208  -27.321 1.00 22.84  ? 162 MET A O   1 
ATOM   1642 C  CB  . MET A 1 162 ? 18.412  -7.283  -25.488 1.00 26.11  ? 162 MET A CB  1 
ATOM   1643 C  CG  . MET A 1 162 ? 19.498  -6.430  -24.826 1.00 29.22  ? 162 MET A CG  1 
ATOM   1644 S  SD  . MET A 1 162 ? 21.069  -7.298  -24.568 1.00 32.38  ? 162 MET A SD  1 
ATOM   1645 C  CE  . MET A 1 162 ? 20.721  -8.050  -22.978 1.00 30.63  ? 162 MET A CE  1 
ATOM   1646 N  N   . HIS A 1 163 ? 17.031  -4.185  -25.319 1.00 21.19  ? 163 HIS A N   1 
ATOM   1647 C  CA  . HIS A 1 163 ? 16.879  -2.812  -25.861 1.00 23.31  ? 163 HIS A CA  1 
ATOM   1648 C  C   . HIS A 1 163 ? 18.248  -2.298  -26.321 1.00 25.23  ? 163 HIS A C   1 
ATOM   1649 O  O   . HIS A 1 163 ? 19.233  -2.388  -25.537 1.00 25.64  ? 163 HIS A O   1 
ATOM   1650 C  CB  . HIS A 1 163 ? 16.210  -1.913  -24.831 1.00 23.44  ? 163 HIS A CB  1 
ATOM   1651 C  CG  . HIS A 1 163 ? 16.041  -0.523  -25.318 1.00 24.96  ? 163 HIS A CG  1 
ATOM   1652 N  ND1 . HIS A 1 163 ? 15.342  -0.242  -26.468 1.00 24.66  ? 163 HIS A ND1 1 
ATOM   1653 C  CD2 . HIS A 1 163 ? 16.506  0.654   -24.836 1.00 25.69  ? 163 HIS A CD2 1 
ATOM   1654 C  CE1 . HIS A 1 163 ? 15.367  1.072   -26.668 1.00 26.31  ? 163 HIS A CE1 1 
ATOM   1655 N  NE2 . HIS A 1 163 ? 16.077  1.640   -25.688 1.00 27.76  ? 163 HIS A NE2 1 
ATOM   1656 N  N   A HIS A 1 164 ? 18.325  -1.802  -27.560 0.25 24.24  ? 164 HIS A N   1 
ATOM   1657 N  N   B HIS A 1 164 ? 18.325  -1.802  -27.560 0.25 24.24  ? 164 HIS A N   1 
ATOM   1658 N  N   C HIS A 1 164 ? 18.318  -1.750  -27.542 0.25 24.94  ? 164 HIS A N   1 
ATOM   1659 N  N   D HIS A 1 164 ? 18.318  -1.750  -27.542 0.25 24.94  ? 164 HIS A N   1 
ATOM   1660 C  CA  A HIS A 1 164 ? 19.573  -1.259  -28.162 0.25 24.84  ? 164 HIS A CA  1 
ATOM   1661 C  CA  B HIS A 1 164 ? 19.573  -1.259  -28.162 0.25 24.84  ? 164 HIS A CA  1 
ATOM   1662 C  CA  C HIS A 1 164 ? 19.569  -1.217  -28.152 0.25 25.90  ? 164 HIS A CA  1 
ATOM   1663 C  CA  D HIS A 1 164 ? 19.569  -1.217  -28.152 0.25 25.90  ? 164 HIS A CA  1 
ATOM   1664 C  C   A HIS A 1 164 ? 19.478  0.258   -28.373 0.25 25.66  ? 164 HIS A C   1 
ATOM   1665 C  C   B HIS A 1 164 ? 19.478  0.258   -28.373 0.25 25.66  ? 164 HIS A C   1 
ATOM   1666 C  C   C HIS A 1 164 ? 19.491  0.293   -28.412 0.25 26.74  ? 164 HIS A C   1 
ATOM   1667 C  C   D HIS A 1 164 ? 19.491  0.293   -28.412 0.25 26.74  ? 164 HIS A C   1 
ATOM   1668 O  O   A HIS A 1 164 ? 20.486  0.934   -28.094 0.25 26.18  ? 164 HIS A O   1 
ATOM   1669 O  O   B HIS A 1 164 ? 20.486  0.934   -28.094 0.25 26.18  ? 164 HIS A O   1 
ATOM   1670 O  O   C HIS A 1 164 ? 20.498  0.974   -28.135 0.25 27.14  ? 164 HIS A O   1 
ATOM   1671 O  O   D HIS A 1 164 ? 20.498  0.974   -28.135 0.25 27.14  ? 164 HIS A O   1 
ATOM   1672 C  CB  A HIS A 1 164 ? 19.928  -2.005  -29.456 0.25 23.54  ? 164 HIS A CB  1 
ATOM   1673 C  CB  B HIS A 1 164 ? 19.928  -2.005  -29.456 0.25 23.54  ? 164 HIS A CB  1 
ATOM   1674 C  CB  C HIS A 1 164 ? 19.917  -1.975  -29.439 0.25 24.93  ? 164 HIS A CB  1 
ATOM   1675 C  CB  D HIS A 1 164 ? 19.917  -1.975  -29.439 0.25 24.93  ? 164 HIS A CB  1 
ATOM   1676 C  CG  A HIS A 1 164 ? 20.425  -3.396  -29.234 0.25 23.13  ? 164 HIS A CG  1 
ATOM   1677 C  CG  B HIS A 1 164 ? 20.425  -3.396  -29.234 0.25 23.13  ? 164 HIS A CG  1 
ATOM   1678 C  CG  C HIS A 1 164 ? 20.571  -3.293  -29.199 0.25 24.84  ? 164 HIS A CG  1 
ATOM   1679 C  CG  D HIS A 1 164 ? 20.571  -3.293  -29.199 0.25 24.84  ? 164 HIS A CG  1 
ATOM   1680 N  ND1 A HIS A 1 164 ? 21.723  -3.777  -29.524 0.25 22.65  ? 164 HIS A ND1 1 
ATOM   1681 N  ND1 B HIS A 1 164 ? 21.723  -3.777  -29.524 0.25 22.65  ? 164 HIS A ND1 1 
ATOM   1682 N  ND1 C HIS A 1 164 ? 21.818  -3.600  -29.709 0.25 24.67  ? 164 HIS A ND1 1 
ATOM   1683 N  ND1 D HIS A 1 164 ? 21.818  -3.600  -29.709 0.25 24.67  ? 164 HIS A ND1 1 
ATOM   1684 C  CD2 A HIS A 1 164 ? 19.805  -4.497  -28.757 0.25 22.72  ? 164 HIS A CD2 1 
ATOM   1685 C  CD2 B HIS A 1 164 ? 19.805  -4.497  -28.757 0.25 22.72  ? 164 HIS A CD2 1 
ATOM   1686 C  CD2 C HIS A 1 164 ? 20.166  -4.377  -28.505 0.25 24.63  ? 164 HIS A CD2 1 
ATOM   1687 C  CD2 D HIS A 1 164 ? 20.166  -4.377  -28.505 0.25 24.63  ? 164 HIS A CD2 1 
ATOM   1688 C  CE1 A HIS A 1 164 ? 21.872  -5.055  -29.250 0.25 22.35  ? 164 HIS A CE1 1 
ATOM   1689 C  CE1 B HIS A 1 164 ? 21.872  -5.055  -29.250 0.25 22.35  ? 164 HIS A CE1 1 
ATOM   1690 C  CE1 C HIS A 1 164 ? 22.141  -4.824  -29.359 0.25 24.26  ? 164 HIS A CE1 1 
ATOM   1691 C  CE1 D HIS A 1 164 ? 22.141  -4.824  -29.359 0.25 24.26  ? 164 HIS A CE1 1 
ATOM   1692 N  NE2 A HIS A 1 164 ? 20.710  -5.521  -28.775 0.25 22.81  ? 164 HIS A NE2 1 
ATOM   1693 N  NE2 B HIS A 1 164 ? 20.710  -5.521  -28.775 0.25 22.81  ? 164 HIS A NE2 1 
ATOM   1694 N  NE2 C HIS A 1 164 ? 21.146  -5.323  -28.619 0.25 25.19  ? 164 HIS A NE2 1 
ATOM   1695 N  NE2 D HIS A 1 164 ? 21.146  -5.323  -28.619 0.25 25.19  ? 164 HIS A NE2 1 
ATOM   1696 N  N   A MET A 1 165 ? 18.358  0.801   -28.864 0.25 26.91  ? 165 MET A N   1 
ATOM   1697 N  N   B MET A 1 165 ? 18.358  0.801   -28.864 0.25 26.91  ? 165 MET A N   1 
ATOM   1698 N  N   C MET A 1 165 ? 18.395  0.818   -28.968 0.25 28.03  ? 165 MET A N   1 
ATOM   1699 N  N   D MET A 1 165 ? 18.395  0.818   -28.968 0.25 28.03  ? 165 MET A N   1 
ATOM   1700 C  CA  A MET A 1 165 ? 18.352  2.226   -29.301 0.25 28.28  ? 165 MET A CA  1 
ATOM   1701 C  CA  B MET A 1 165 ? 18.352  2.226   -29.301 0.25 28.28  ? 165 MET A CA  1 
ATOM   1702 C  CA  C MET A 1 165 ? 18.380  2.244   -29.396 0.25 29.37  ? 165 MET A CA  1 
ATOM   1703 C  CA  D MET A 1 165 ? 18.380  2.244   -29.396 0.25 29.37  ? 165 MET A CA  1 
ATOM   1704 C  C   A MET A 1 165 ? 16.937  2.793   -29.482 0.25 27.65  ? 165 MET A C   1 
ATOM   1705 C  C   B MET A 1 165 ? 16.937  2.793   -29.482 0.25 27.65  ? 165 MET A C   1 
ATOM   1706 C  C   C MET A 1 165 ? 16.954  2.794   -29.528 0.25 28.31  ? 165 MET A C   1 
ATOM   1707 C  C   D MET A 1 165 ? 16.954  2.794   -29.528 0.25 28.31  ? 165 MET A C   1 
ATOM   1708 O  O   A MET A 1 165 ? 15.965  2.008   -29.564 0.25 27.38  ? 165 MET A O   1 
ATOM   1709 O  O   B MET A 1 165 ? 15.965  2.008   -29.564 0.25 27.38  ? 165 MET A O   1 
ATOM   1710 O  O   C MET A 1 165 ? 15.989  1.999   -29.598 0.25 28.07  ? 165 MET A O   1 
ATOM   1711 O  O   D MET A 1 165 ? 15.989  1.999   -29.598 0.25 28.07  ? 165 MET A O   1 
ATOM   1712 C  CB  A MET A 1 165 ? 19.117  2.356   -30.620 0.25 29.50  ? 165 MET A CB  1 
ATOM   1713 C  CB  B MET A 1 165 ? 19.117  2.356   -30.620 0.25 29.50  ? 165 MET A CB  1 
ATOM   1714 C  CB  C MET A 1 165 ? 19.124  2.402   -30.727 0.25 30.93  ? 165 MET A CB  1 
ATOM   1715 C  CB  D MET A 1 165 ? 19.124  2.402   -30.727 0.25 30.93  ? 165 MET A CB  1 
ATOM   1716 C  CG  A MET A 1 165 ? 18.404  1.716   -31.784 0.25 30.51  ? 165 MET A CG  1 
ATOM   1717 C  CG  B MET A 1 165 ? 18.404  1.716   -31.784 0.25 30.51  ? 165 MET A CG  1 
ATOM   1718 C  CG  C MET A 1 165 ? 18.318  1.994   -31.937 0.25 32.44  ? 165 MET A CG  1 
ATOM   1719 C  CG  D MET A 1 165 ? 18.318  1.994   -31.937 0.25 32.44  ? 165 MET A CG  1 
ATOM   1720 S  SD  A MET A 1 165 ? 19.531  1.156   -33.083 0.25 34.48  ? 165 MET A SD  1 
ATOM   1721 S  SD  B MET A 1 165 ? 19.531  1.156   -33.083 0.25 34.48  ? 165 MET A SD  1 
ATOM   1722 S  SD  C MET A 1 165 ? 19.363  1.377   -33.285 0.25 36.43  ? 165 MET A SD  1 
ATOM   1723 S  SD  D MET A 1 165 ? 19.363  1.377   -33.285 0.25 36.43  ? 165 MET A SD  1 
ATOM   1724 C  CE  A MET A 1 165 ? 18.385  1.074   -34.457 0.25 34.94  ? 165 MET A CE  1 
ATOM   1725 C  CE  B MET A 1 165 ? 18.385  1.074   -34.457 0.25 34.94  ? 165 MET A CE  1 
ATOM   1726 C  CE  C MET A 1 165 ? 18.173  1.375   -34.625 0.25 37.51  ? 165 MET A CE  1 
ATOM   1727 C  CE  D MET A 1 165 ? 18.173  1.375   -34.625 0.25 37.51  ? 165 MET A CE  1 
ATOM   1728 N  N   . GLU A 1 166 ? 16.860  4.127   -29.571 1.00 26.93  ? 166 GLU A N   1 
ATOM   1729 C  CA  . GLU A 1 166 ? 15.607  4.879   -29.821 1.00 29.72  ? 166 GLU A CA  1 
ATOM   1730 C  C   . GLU A 1 166 ? 15.723  5.461   -31.228 1.00 30.81  ? 166 GLU A C   1 
ATOM   1731 O  O   . GLU A 1 166 ? 16.784  6.030   -31.546 1.00 29.12  ? 166 GLU A O   1 
ATOM   1732 C  CB  . GLU A 1 166 ? 15.424  6.015   -28.817 1.00 29.16  ? 166 GLU A CB  1 
ATOM   1733 C  CG  . GLU A 1 166 ? 14.097  6.756   -28.986 1.00 30.22  ? 166 GLU A CG  1 
ATOM   1734 C  CD  . GLU A 1 166 ? 13.732  7.626   -27.795 1.00 30.66  ? 166 GLU A CD  1 
ATOM   1735 O  OE1 . GLU A 1 166 ? 13.633  7.099   -26.671 1.00 31.35  ? 166 GLU A OE1 1 
ATOM   1736 O  OE2 . GLU A 1 166 ? 13.552  8.829   -27.981 1.00 31.13  ? 166 GLU A OE2 1 
ATOM   1737 N  N   . LEU A 1 167 ? 14.703  5.287   -32.061 1.00 30.67  ? 167 LEU A N   1 
ATOM   1738 C  CA  . LEU A 1 167 ? 14.716  5.856   -33.429 1.00 31.70  ? 167 LEU A CA  1 
ATOM   1739 C  C   . LEU A 1 167 ? 14.216  7.290   -33.370 1.00 33.32  ? 167 LEU A C   1 
ATOM   1740 O  O   . LEU A 1 167 ? 13.661  7.711   -32.366 1.00 30.35  ? 167 LEU A O   1 
ATOM   1741 C  CB  . LEU A 1 167 ? 13.861  4.974   -34.340 1.00 32.44  ? 167 LEU A CB  1 
ATOM   1742 C  CG  . LEU A 1 167 ? 14.419  3.566   -34.525 1.00 31.98  ? 167 LEU A CG  1 
ATOM   1743 C  CD1 . LEU A 1 167 ? 13.335  2.618   -34.996 1.00 36.17  ? 167 LEU A CD1 1 
ATOM   1744 C  CD2 . LEU A 1 167 ? 15.581  3.571   -35.495 1.00 33.10  ? 167 LEU A CD2 1 
ATOM   1745 N  N   . PRO A 1 168 ? 14.407  8.095   -34.436 1.00 38.93  ? 168 PRO A N   1 
ATOM   1746 C  CA  . PRO A 1 168 ? 14.050  9.514   -34.389 1.00 39.18  ? 168 PRO A CA  1 
ATOM   1747 C  C   . PRO A 1 168 ? 12.574  9.800   -34.098 1.00 38.98  ? 168 PRO A C   1 
ATOM   1748 O  O   . PRO A 1 168 ? 12.309  10.868  -33.596 1.00 42.77  ? 168 PRO A O   1 
ATOM   1749 C  CB  . PRO A 1 168 ? 14.445  10.030  -35.781 1.00 45.19  ? 168 PRO A CB  1 
ATOM   1750 C  CG  . PRO A 1 168 ? 15.539  9.057   -36.226 1.00 45.13  ? 168 PRO A CG  1 
ATOM   1751 C  CD  . PRO A 1 168 ? 15.077  7.714   -35.693 1.00 42.83  ? 168 PRO A CD  1 
ATOM   1752 N  N   . THR A 1 169 ? 11.653  8.879   -34.392 1.00 37.18  ? 169 THR A N   1 
ATOM   1753 C  CA  . THR A 1 169 ? 10.217  9.086   -34.072 1.00 34.65  ? 169 THR A CA  1 
ATOM   1754 C  C   . THR A 1 169 ? 9.943   8.801   -32.596 1.00 32.26  ? 169 THR A C   1 
ATOM   1755 O  O   . THR A 1 169 ? 8.797   8.941   -32.215 1.00 31.59  ? 169 THR A O   1 
ATOM   1756 C  CB  . THR A 1 169 ? 9.278   8.287   -34.983 1.00 36.92  ? 169 THR A CB  1 
ATOM   1757 O  OG1 . THR A 1 169 ? 9.604   6.900   -34.950 1.00 38.67  ? 169 THR A OG1 1 
ATOM   1758 C  CG2 . THR A 1 169 ? 9.321   8.779   -36.415 1.00 36.63  ? 169 THR A CG2 1 
ATOM   1759 N  N   . GLY A 1 170 ? 10.942  8.474   -31.779 1.00 30.59  ? 170 GLY A N   1 
ATOM   1760 C  CA  . GLY A 1 170 ? 10.723  8.225   -30.341 1.00 30.29  ? 170 GLY A CA  1 
ATOM   1761 C  C   . GLY A 1 170 ? 10.236  6.806   -30.039 1.00 31.68  ? 170 GLY A C   1 
ATOM   1762 O  O   . GLY A 1 170 ? 9.785   6.592   -28.898 1.00 34.31  ? 170 GLY A O   1 
ATOM   1763 N  N   . VAL A 1 171 ? 10.332  5.870   -30.996 1.00 28.29  ? 171 VAL A N   1 
ATOM   1764 C  CA  . VAL A 1 171 ? 10.050  4.417   -30.800 1.00 29.25  ? 171 VAL A CA  1 
ATOM   1765 C  C   . VAL A 1 171 ? 11.391  3.681   -30.676 1.00 28.09  ? 171 VAL A C   1 
ATOM   1766 O  O   . VAL A 1 171 ? 12.434  4.273   -30.960 1.00 25.94  ? 171 VAL A O   1 
ATOM   1767 C  CB  . VAL A 1 171 ? 9.169   3.829   -31.925 1.00 31.02  ? 171 VAL A CB  1 
ATOM   1768 C  CG1 . VAL A 1 171 ? 7.822   4.538   -31.980 1.00 32.78  ? 171 VAL A CG1 1 
ATOM   1769 C  CG2 . VAL A 1 171 ? 9.840   3.849   -33.295 1.00 31.10  ? 171 VAL A CG2 1 
ATOM   1770 N  N   . HIS A 1 172 ? 11.351  2.407   -30.308 1.00 26.57  ? 172 HIS A N   1 
ATOM   1771 C  CA  . HIS A 1 172 ? 12.533  1.669   -29.802 1.00 25.96  ? 172 HIS A CA  1 
ATOM   1772 C  C   . HIS A 1 172 ? 12.804  0.444   -30.668 1.00 25.43  ? 172 HIS A C   1 
ATOM   1773 O  O   . HIS A 1 172 ? 11.837  -0.171  -31.194 1.00 23.46  ? 172 HIS A O   1 
ATOM   1774 C  CB  . HIS A 1 172 ? 12.321  1.380   -28.315 1.00 25.20  ? 172 HIS A CB  1 
ATOM   1775 C  CG  . HIS A 1 172 ? 12.059  2.643   -27.558 1.00 23.92  ? 172 HIS A CG  1 
ATOM   1776 N  ND1 . HIS A 1 172 ? 10.828  2.946   -27.066 1.00 21.85  ? 172 HIS A ND1 1 
ATOM   1777 C  CD2 . HIS A 1 172 ? 12.840  3.710   -27.285 1.00 21.67  ? 172 HIS A CD2 1 
ATOM   1778 C  CE1 . HIS A 1 172 ? 10.864  4.124   -26.482 1.00 21.82  ? 172 HIS A CE1 1 
ATOM   1779 N  NE2 . HIS A 1 172 ? 12.077  4.610   -26.601 1.00 20.76  ? 172 HIS A NE2 1 
ATOM   1780 N  N   . ALA A 1 173 ? 14.089  0.151   -30.850 1.00 24.03  ? 173 ALA A N   1 
ATOM   1781 C  CA  . ALA A 1 173 ? 14.571  -0.985  -31.651 1.00 23.17  ? 173 ALA A CA  1 
ATOM   1782 C  C   . ALA A 1 173 ? 15.575  -1.792  -30.836 1.00 22.85  ? 173 ALA A C   1 
ATOM   1783 O  O   . ALA A 1 173 ? 16.302  -1.233  -30.002 1.00 23.25  ? 173 ALA A O   1 
ATOM   1784 C  CB  . ALA A 1 173 ? 15.142  -0.477  -32.946 1.00 22.69  ? 173 ALA A CB  1 
ATOM   1785 N  N   . GLY A 1 174 ? 15.578  -3.097  -31.054 1.00 25.17  ? 174 GLY A N   1 
ATOM   1786 C  CA  . GLY A 1 174 ? 16.429  -4.022  -30.301 1.00 24.23  ? 174 GLY A CA  1 
ATOM   1787 C  C   . GLY A 1 174 ? 16.482  -5.379  -30.956 1.00 24.60  ? 174 GLY A C   1 
ATOM   1788 O  O   . GLY A 1 174 ? 15.975  -5.528  -32.094 1.00 22.62  ? 174 GLY A O   1 
ATOM   1789 N  N   . THR A 1 175 ? 16.999  -6.360  -30.213 1.00 24.12  ? 175 THR A N   1 
ATOM   1790 C  CA  . THR A 1 175 ? 17.350  -7.702  -30.736 1.00 23.26  ? 175 THR A CA  1 
ATOM   1791 C  C   . THR A 1 175 ? 16.672  -8.783  -29.911 1.00 23.09  ? 175 THR A C   1 
ATOM   1792 O  O   . THR A 1 175 ? 16.176  -8.501  -28.828 1.00 24.36  ? 175 THR A O   1 
ATOM   1793 C  CB  . THR A 1 175 ? 18.864  -7.951  -30.708 1.00 23.49  ? 175 THR A CB  1 
ATOM   1794 O  OG1 . THR A 1 175 ? 19.321  -7.945  -29.359 1.00 23.53  ? 175 THR A OG1 1 
ATOM   1795 C  CG2 . THR A 1 175 ? 19.624  -6.900  -31.474 1.00 24.50  ? 175 THR A CG2 1 
ATOM   1796 N  N   . ASP A 1 176 ? 16.669  -9.988  -30.438 1.00 22.11  ? 176 ASP A N   1 
ATOM   1797 C  CA  . ASP A 1 176 ? 16.406  -11.193 -29.629 1.00 23.23  ? 176 ASP A CA  1 
ATOM   1798 C  C   . ASP A 1 176 ? 17.667  -11.392 -28.785 1.00 24.67  ? 176 ASP A C   1 
ATOM   1799 O  O   . ASP A 1 176 ? 18.657  -10.577 -28.938 1.00 23.73  ? 176 ASP A O   1 
ATOM   1800 C  CB  . ASP A 1 176 ? 15.981  -12.379 -30.500 1.00 23.94  ? 176 ASP A CB  1 
ATOM   1801 C  CG  . ASP A 1 176 ? 17.014  -12.820 -31.538 1.00 26.26  ? 176 ASP A CG  1 
ATOM   1802 O  OD1 . ASP A 1 176 ? 18.231  -12.616 -31.311 1.00 27.29  ? 176 ASP A OD1 1 
ATOM   1803 O  OD2 . ASP A 1 176 ? 16.594  -13.308 -32.592 1.00 26.38  ? 176 ASP A OD2 1 
ATOM   1804 N  N   . LEU A 1 177 ? 17.650  -12.412 -27.929 1.00 25.49  ? 177 LEU A N   1 
ATOM   1805 C  CA  . LEU A 1 177 ? 18.790  -12.706 -27.026 1.00 25.82  ? 177 LEU A CA  1 
ATOM   1806 C  C   . LEU A 1 177 ? 19.878  -13.491 -27.760 1.00 25.76  ? 177 LEU A C   1 
ATOM   1807 O  O   . LEU A 1 177 ? 20.895  -13.742 -27.114 1.00 29.52  ? 177 LEU A O   1 
ATOM   1808 C  CB  . LEU A 1 177 ? 18.285  -13.419 -25.771 1.00 25.21  ? 177 LEU A CB  1 
ATOM   1809 C  CG  . LEU A 1 177 ? 17.959  -12.467 -24.621 1.00 27.14  ? 177 LEU A CG  1 
ATOM   1810 C  CD1 . LEU A 1 177 ? 19.221  -11.836 -24.058 1.00 30.04  ? 177 LEU A CD1 1 
ATOM   1811 C  CD2 . LEU A 1 177 ? 17.021  -11.367 -25.099 1.00 28.27  ? 177 LEU A CD2 1 
ATOM   1812 N  N   . GLU A 1 178 ? 19.706  -13.785 -29.057 1.00 27.83  ? 178 GLU A N   1 
ATOM   1813 C  CA  . GLU A 1 178 ? 20.790  -14.266 -29.960 1.00 29.88  ? 178 GLU A CA  1 
ATOM   1814 C  C   . GLU A 1 178 ? 21.416  -13.093 -30.718 1.00 29.17  ? 178 GLU A C   1 
ATOM   1815 O  O   . GLU A 1 178 ? 22.288  -13.358 -31.572 1.00 28.26  ? 178 GLU A O   1 
ATOM   1816 C  CB  . GLU A 1 178 ? 20.269  -15.291 -30.967 1.00 33.44  ? 178 GLU A CB  1 
ATOM   1817 C  CG  . GLU A 1 178 ? 19.791  -16.546 -30.289 1.00 40.85  ? 178 GLU A CG  1 
ATOM   1818 C  CD  . GLU A 1 178 ? 19.212  -17.604 -31.204 1.00 43.19  ? 178 GLU A CD  1 
ATOM   1819 O  OE1 . GLU A 1 178 ? 18.402  -17.262 -32.084 1.00 48.96  ? 178 GLU A OE1 1 
ATOM   1820 O  OE2 . GLU A 1 178 ? 19.561  -18.765 -31.001 1.00 48.97  ? 178 GLU A OE2 1 
ATOM   1821 N  N   . GLY A 1 179 ? 20.971  -11.862 -30.457 1.00 27.32  ? 179 GLY A N   1 
ATOM   1822 C  CA  . GLY A 1 179 ? 21.615  -10.657 -31.006 1.00 26.64  ? 179 GLY A CA  1 
ATOM   1823 C  C   . GLY A 1 179 ? 21.141  -10.294 -32.403 1.00 26.77  ? 179 GLY A C   1 
ATOM   1824 O  O   . GLY A 1 179 ? 21.751  -9.392  -32.994 1.00 26.67  ? 179 GLY A O   1 
ATOM   1825 N  N   . ASN A 1 180 ? 20.099  -10.929 -32.945 1.00 29.58  ? 180 ASN A N   1 
ATOM   1826 C  CA  . ASN A 1 180 ? 19.544  -10.535 -34.278 1.00 28.47  ? 180 ASN A CA  1 
ATOM   1827 C  C   . ASN A 1 180 ? 18.490  -9.441  -34.087 1.00 30.69  ? 180 ASN A C   1 
ATOM   1828 O  O   . ASN A 1 180 ? 17.533  -9.657  -33.302 1.00 26.81  ? 180 ASN A O   1 
ATOM   1829 C  CB  . ASN A 1 180 ? 18.974  -11.726 -35.039 1.00 30.62  ? 180 ASN A CB  1 
ATOM   1830 C  CG  . ASN A 1 180 ? 20.062  -12.732 -35.348 1.00 33.18  ? 180 ASN A CG  1 
ATOM   1831 O  OD1 . ASN A 1 180 ? 20.031  -13.845 -34.838 1.00 37.15  ? 180 ASN A OD1 1 
ATOM   1832 N  ND2 . ASN A 1 180 ? 21.060  -12.313 -36.107 1.00 33.14  ? 180 ASN A ND2 1 
ATOM   1833 N  N   . PHE A 1 181 ? 18.663  -8.300  -34.755 1.00 28.81  ? 181 PHE A N   1 
ATOM   1834 C  CA  . PHE A 1 181 ? 17.692  -7.182  -34.705 1.00 27.88  ? 181 PHE A CA  1 
ATOM   1835 C  C   . PHE A 1 181 ? 16.311  -7.697  -35.117 1.00 27.66  ? 181 PHE A C   1 
ATOM   1836 O  O   . PHE A 1 181 ? 16.199  -8.613  -35.964 1.00 26.13  ? 181 PHE A O   1 
ATOM   1837 C  CB  . PHE A 1 181 ? 18.109  -5.978  -35.561 1.00 26.92  ? 181 PHE A CB  1 
ATOM   1838 C  CG  . PHE A 1 181 ? 18.801  -4.918  -34.750 1.00 26.20  ? 181 PHE A CG  1 
ATOM   1839 C  CD1 . PHE A 1 181 ? 20.170  -4.978  -34.544 1.00 27.53  ? 181 PHE A CD1 1 
ATOM   1840 C  CD2 . PHE A 1 181 ? 18.074  -3.949  -34.077 1.00 25.12  ? 181 PHE A CD2 1 
ATOM   1841 C  CE1 . PHE A 1 181 ? 20.805  -4.046  -33.738 1.00 26.25  ? 181 PHE A CE1 1 
ATOM   1842 C  CE2 . PHE A 1 181 ? 18.708  -3.025  -33.260 1.00 23.99  ? 181 PHE A CE2 1 
ATOM   1843 C  CZ  . PHE A 1 181 ? 20.071  -3.068  -33.105 1.00 26.44  ? 181 PHE A CZ  1 
ATOM   1844 N  N   . TYR A 1 182 ? 15.288  -7.121  -34.490 1.00 22.79  ? 182 TYR A N   1 
ATOM   1845 C  CA  . TYR A 1 182 ? 13.919  -7.087  -35.039 1.00 23.14  ? 182 TYR A CA  1 
ATOM   1846 C  C   . TYR A 1 182 ? 13.904  -5.978  -36.092 1.00 21.70  ? 182 TYR A C   1 
ATOM   1847 O  O   . TYR A 1 182 ? 14.287  -4.829  -35.806 1.00 25.22  ? 182 TYR A O   1 
ATOM   1848 C  CB  . TYR A 1 182 ? 12.875  -6.922  -33.930 1.00 22.73  ? 182 TYR A CB  1 
ATOM   1849 C  CG  . TYR A 1 182 ? 12.742  -8.097  -32.993 1.00 23.83  ? 182 TYR A CG  1 
ATOM   1850 C  CD1 . TYR A 1 182 ? 12.021  -9.235  -33.354 1.00 23.80  ? 182 TYR A CD1 1 
ATOM   1851 C  CD2 . TYR A 1 182 ? 13.339  -8.081  -31.739 1.00 24.92  ? 182 TYR A CD2 1 
ATOM   1852 C  CE1 . TYR A 1 182 ? 11.879  -10.304 -32.485 1.00 23.21  ? 182 TYR A CE1 1 
ATOM   1853 C  CE2 . TYR A 1 182 ? 13.204  -9.150  -30.859 1.00 24.32  ? 182 TYR A CE2 1 
ATOM   1854 C  CZ  . TYR A 1 182 ? 12.476  -10.272 -31.233 1.00 24.92  ? 182 TYR A CZ  1 
ATOM   1855 O  OH  . TYR A 1 182 ? 12.357  -11.325 -30.357 1.00 23.99  ? 182 TYR A OH  1 
ATOM   1856 N  N   . GLY A 1 183 ? 13.458  -6.323  -37.289 1.00 22.42  ? 183 GLY A N   1 
ATOM   1857 C  CA  . GLY A 1 183 ? 13.289  -5.380  -38.398 1.00 24.08  ? 183 GLY A CA  1 
ATOM   1858 C  C   . GLY A 1 183 ? 14.613  -5.111  -39.105 1.00 28.13  ? 183 GLY A C   1 
ATOM   1859 O  O   . GLY A 1 183 ? 15.598  -5.821  -38.926 1.00 26.96  ? 183 GLY A O   1 
ATOM   1860 N  N   . PRO A 1 184 ? 14.655  -4.077  -39.967 1.00 30.25  ? 184 PRO A N   1 
ATOM   1861 C  CA  . PRO A 1 184 ? 15.827  -3.835  -40.801 1.00 31.11  ? 184 PRO A CA  1 
ATOM   1862 C  C   . PRO A 1 184 ? 16.883  -2.966  -40.099 1.00 30.87  ? 184 PRO A C   1 
ATOM   1863 O  O   . PRO A 1 184 ? 17.700  -2.434  -40.741 1.00 38.46  ? 184 PRO A O   1 
ATOM   1864 C  CB  . PRO A 1 184 ? 15.173  -3.159  -42.020 1.00 30.22  ? 184 PRO A CB  1 
ATOM   1865 C  CG  . PRO A 1 184 ? 14.040  -2.343  -41.417 1.00 32.08  ? 184 PRO A CG  1 
ATOM   1866 C  CD  . PRO A 1 184 ? 13.541  -3.157  -40.243 1.00 31.16  ? 184 PRO A CD  1 
ATOM   1867 N  N   . PHE A 1 185 ? 16.863  -2.867  -38.782 1.00 31.34  ? 185 PHE A N   1 
ATOM   1868 C  CA  . PHE A 1 185 ? 17.707  -1.901  -38.046 1.00 28.75  ? 185 PHE A CA  1 
ATOM   1869 C  C   . PHE A 1 185 ? 19.109  -2.478  -37.829 1.00 27.40  ? 185 PHE A C   1 
ATOM   1870 O  O   . PHE A 1 185 ? 19.273  -3.707  -37.844 1.00 26.40  ? 185 PHE A O   1 
ATOM   1871 C  CB  . PHE A 1 185 ? 16.974  -1.477  -36.776 1.00 27.94  ? 185 PHE A CB  1 
ATOM   1872 C  CG  . PHE A 1 185 ? 15.601  -0.964  -37.087 1.00 28.65  ? 185 PHE A CG  1 
ATOM   1873 C  CD1 . PHE A 1 185 ? 15.444  0.208   -37.817 1.00 28.66  ? 185 PHE A CD1 1 
ATOM   1874 C  CD2 . PHE A 1 185 ? 14.470  -1.666  -36.691 1.00 29.38  ? 185 PHE A CD2 1 
ATOM   1875 C  CE1 . PHE A 1 185 ? 14.179  0.689   -38.117 1.00 27.71  ? 185 PHE A CE1 1 
ATOM   1876 C  CE2 . PHE A 1 185 ? 13.206  -1.197  -37.009 1.00 27.70  ? 185 PHE A CE2 1 
ATOM   1877 C  CZ  . PHE A 1 185 ? 13.064  -0.017  -37.719 1.00 28.71  ? 185 PHE A CZ  1 
ATOM   1878 N  N   . VAL A 1 186 ? 20.087  -1.579  -37.671 1.00 26.88  ? 186 VAL A N   1 
ATOM   1879 C  CA  . VAL A 1 186 ? 21.521  -1.895  -37.383 1.00 27.91  ? 186 VAL A CA  1 
ATOM   1880 C  C   . VAL A 1 186 ? 21.995  -1.044  -36.195 1.00 26.84  ? 186 VAL A C   1 
ATOM   1881 O  O   . VAL A 1 186 ? 21.488  0.095   -36.006 1.00 25.92  ? 186 VAL A O   1 
ATOM   1882 C  CB  . VAL A 1 186 ? 22.439  -1.631  -38.597 1.00 29.23  ? 186 VAL A CB  1 
ATOM   1883 C  CG1 . VAL A 1 186 ? 22.140  -2.540  -39.785 1.00 27.69  ? 186 VAL A CG1 1 
ATOM   1884 C  CG2 . VAL A 1 186 ? 22.406  -0.171  -39.006 1.00 29.43  ? 186 VAL A CG2 1 
ATOM   1885 N  N   A ASP A 1 187 ? 22.959  -1.560  -35.424 0.25 26.14  ? 187 ASP A N   1 
ATOM   1886 N  N   B ASP A 1 187 ? 22.959  -1.560  -35.424 0.25 26.14  ? 187 ASP A N   1 
ATOM   1887 N  N   C ASP A 1 187 ? 22.969  -1.572  -35.443 0.25 26.47  ? 187 ASP A N   1 
ATOM   1888 N  N   D ASP A 1 187 ? 22.969  -1.572  -35.443 0.25 26.47  ? 187 ASP A N   1 
ATOM   1889 C  CA  A ASP A 1 187 ? 23.518  -0.866  -34.232 0.25 26.21  ? 187 ASP A CA  1 
ATOM   1890 C  CA  B ASP A 1 187 ? 23.518  -0.866  -34.232 0.25 26.21  ? 187 ASP A CA  1 
ATOM   1891 C  CA  C ASP A 1 187 ? 23.568  -0.917  -34.249 0.25 26.74  ? 187 ASP A CA  1 
ATOM   1892 C  CA  D ASP A 1 187 ? 23.568  -0.917  -34.249 0.25 26.74  ? 187 ASP A CA  1 
ATOM   1893 C  C   A ASP A 1 187 ? 24.605  0.114   -34.696 0.25 26.64  ? 187 ASP A C   1 
ATOM   1894 C  C   B ASP A 1 187 ? 24.605  0.114   -34.696 0.25 26.64  ? 187 ASP A C   1 
ATOM   1895 C  C   C ASP A 1 187 ? 24.682  0.029   -34.718 0.25 27.33  ? 187 ASP A C   1 
ATOM   1896 C  C   D ASP A 1 187 ? 24.682  0.029   -34.718 0.25 27.33  ? 187 ASP A C   1 
ATOM   1897 O  O   A ASP A 1 187 ? 25.770  -0.047  -34.294 0.25 26.22  ? 187 ASP A O   1 
ATOM   1898 O  O   B ASP A 1 187 ? 25.770  -0.047  -34.294 0.25 26.22  ? 187 ASP A O   1 
ATOM   1899 O  O   C ASP A 1 187 ? 25.856  -0.217  -34.393 0.25 26.66  ? 187 ASP A O   1 
ATOM   1900 O  O   D ASP A 1 187 ? 25.856  -0.217  -34.393 0.25 26.66  ? 187 ASP A O   1 
ATOM   1901 C  CB  A ASP A 1 187 ? 23.964  -1.860  -33.153 0.25 25.40  ? 187 ASP A CB  1 
ATOM   1902 C  CB  B ASP A 1 187 ? 23.964  -1.860  -33.153 0.25 25.40  ? 187 ASP A CB  1 
ATOM   1903 C  CB  C ASP A 1 187 ? 24.013  -1.943  -33.201 0.25 26.00  ? 187 ASP A CB  1 
ATOM   1904 C  CB  D ASP A 1 187 ? 24.013  -1.943  -33.201 0.25 26.00  ? 187 ASP A CB  1 
ATOM   1905 C  CG  A ASP A 1 187 ? 24.942  -2.936  -33.591 0.25 25.28  ? 187 ASP A CG  1 
ATOM   1906 C  CG  B ASP A 1 187 ? 24.942  -2.936  -33.591 0.25 25.28  ? 187 ASP A CG  1 
ATOM   1907 C  CG  C ASP A 1 187 ? 24.902  -3.067  -33.704 0.25 26.11  ? 187 ASP A CG  1 
ATOM   1908 C  CG  D ASP A 1 187 ? 24.902  -3.067  -33.704 0.25 26.11  ? 187 ASP A CG  1 
ATOM   1909 O  OD1 A ASP A 1 187 ? 25.112  -3.141  -34.812 0.25 26.36  ? 187 ASP A OD1 1 
ATOM   1910 O  OD1 B ASP A 1 187 ? 25.112  -3.141  -34.812 0.25 26.36  ? 187 ASP A OD1 1 
ATOM   1911 O  OD1 C ASP A 1 187 ? 25.208  -3.102  -34.914 0.25 27.00  ? 187 ASP A OD1 1 
ATOM   1912 O  OD1 D ASP A 1 187 ? 25.208  -3.102  -34.914 0.25 27.00  ? 187 ASP A OD1 1 
ATOM   1913 O  OD2 A ASP A 1 187 ? 25.518  -3.570  -32.700 0.25 25.58  ? 187 ASP A OD2 1 
ATOM   1914 O  OD2 B ASP A 1 187 ? 25.518  -3.570  -32.700 0.25 25.58  ? 187 ASP A OD2 1 
ATOM   1915 O  OD2 C ASP A 1 187 ? 25.274  -3.909  -32.877 0.25 26.66  ? 187 ASP A OD2 1 
ATOM   1916 O  OD2 D ASP A 1 187 ? 25.274  -3.909  -32.877 0.25 26.66  ? 187 ASP A OD2 1 
ATOM   1917 N  N   A ARG A 1 188 ? 24.200  1.089   -35.517 0.25 26.97  ? 188 ARG A N   1 
ATOM   1918 N  N   B ARG A 1 188 ? 24.200  1.089   -35.517 0.25 26.97  ? 188 ARG A N   1 
ATOM   1919 N  N   C ARG A 1 188 ? 24.285  1.058   -35.471 0.25 27.90  ? 188 ARG A N   1 
ATOM   1920 N  N   D ARG A 1 188 ? 24.285  1.058   -35.471 0.25 27.90  ? 188 ARG A N   1 
ATOM   1921 C  CA  A ARG A 1 188 ? 24.996  2.248   -36.006 0.25 28.59  ? 188 ARG A CA  1 
ATOM   1922 C  CA  B ARG A 1 188 ? 24.996  2.248   -36.006 0.25 28.59  ? 188 ARG A CA  1 
ATOM   1923 C  CA  C ARG A 1 188 ? 25.093  2.221   -35.927 0.25 29.93  ? 188 ARG A CA  1 
ATOM   1924 C  CA  D ARG A 1 188 ? 25.093  2.221   -35.927 0.25 29.93  ? 188 ARG A CA  1 
ATOM   1925 C  C   A ARG A 1 188 ? 24.116  3.505   -35.950 0.25 28.90  ? 188 ARG A C   1 
ATOM   1926 C  C   B ARG A 1 188 ? 24.116  3.505   -35.950 0.25 28.90  ? 188 ARG A C   1 
ATOM   1927 C  C   C ARG A 1 188 ? 24.166  3.442   -35.937 0.25 30.30  ? 188 ARG A C   1 
ATOM   1928 C  C   D ARG A 1 188 ? 24.166  3.442   -35.937 0.25 30.30  ? 188 ARG A C   1 
ATOM   1929 O  O   A ARG A 1 188 ? 22.902  3.393   -36.280 0.25 27.60  ? 188 ARG A O   1 
ATOM   1930 O  O   B ARG A 1 188 ? 22.902  3.393   -36.280 0.25 27.60  ? 188 ARG A O   1 
ATOM   1931 O  O   C ARG A 1 188 ? 22.960  3.269   -36.292 0.25 29.20  ? 188 ARG A O   1 
ATOM   1932 O  O   D ARG A 1 188 ? 22.960  3.269   -36.292 0.25 29.20  ? 188 ARG A O   1 
ATOM   1933 C  CB  A ARG A 1 188 ? 25.403  2.092   -37.478 0.25 28.40  ? 188 ARG A CB  1 
ATOM   1934 C  CB  B ARG A 1 188 ? 25.403  2.092   -37.478 0.25 28.40  ? 188 ARG A CB  1 
ATOM   1935 C  CB  C ARG A 1 188 ? 25.605  2.066   -37.367 0.25 30.38  ? 188 ARG A CB  1 
ATOM   1936 C  CB  D ARG A 1 188 ? 25.605  2.066   -37.367 0.25 30.38  ? 188 ARG A CB  1 
ATOM   1937 C  CG  A ARG A 1 188 ? 26.249  0.872   -37.815 0.25 29.18  ? 188 ARG A CG  1 
ATOM   1938 C  CG  B ARG A 1 188 ? 26.249  0.872   -37.815 0.25 29.18  ? 188 ARG A CG  1 
ATOM   1939 C  CG  C ARG A 1 188 ? 26.216  0.717   -37.719 0.25 31.65  ? 188 ARG A CG  1 
ATOM   1940 C  CG  D ARG A 1 188 ? 26.216  0.717   -37.719 0.25 31.65  ? 188 ARG A CG  1 
ATOM   1941 C  CD  A ARG A 1 188 ? 26.263  0.564   -39.311 0.25 28.33  ? 188 ARG A CD  1 
ATOM   1942 C  CD  B ARG A 1 188 ? 26.263  0.564   -39.311 0.25 28.33  ? 188 ARG A CD  1 
ATOM   1943 C  CD  C ARG A 1 188 ? 26.392  0.481   -39.220 0.25 31.28  ? 188 ARG A CD  1 
ATOM   1944 C  CD  D ARG A 1 188 ? 26.392  0.481   -39.220 0.25 31.28  ? 188 ARG A CD  1 
ATOM   1945 N  NE  A ARG A 1 188 ? 26.492  1.752   -40.130 0.25 28.79  ? 188 ARG A NE  1 
ATOM   1946 N  NE  B ARG A 1 188 ? 26.492  1.752   -40.130 0.25 28.79  ? 188 ARG A NE  1 
ATOM   1947 N  NE  C ARG A 1 188 ? 26.607  1.691   -40.013 0.25 32.10  ? 188 ARG A NE  1 
ATOM   1948 N  NE  D ARG A 1 188 ? 26.607  1.691   -40.013 0.25 32.10  ? 188 ARG A NE  1 
ATOM   1949 C  CZ  A ARG A 1 188 ? 26.232  1.855   -41.436 0.25 28.42  ? 188 ARG A CZ  1 
ATOM   1950 C  CZ  B ARG A 1 188 ? 26.232  1.855   -41.436 0.25 28.42  ? 188 ARG A CZ  1 
ATOM   1951 C  CZ  C ARG A 1 188 ? 26.154  1.892   -41.254 0.25 32.43  ? 188 ARG A CZ  1 
ATOM   1952 C  CZ  D ARG A 1 188 ? 26.154  1.892   -41.254 0.25 32.43  ? 188 ARG A CZ  1 
ATOM   1953 N  NH1 A ARG A 1 188 ? 25.722  0.835   -42.105 0.25 28.39  ? 188 ARG A NH1 1 
ATOM   1954 N  NH1 B ARG A 1 188 ? 25.722  0.835   -42.105 0.25 28.39  ? 188 ARG A NH1 1 
ATOM   1955 N  NH1 C ARG A 1 188 ? 25.425  0.973   -41.868 0.25 32.83  ? 188 ARG A NH1 1 
ATOM   1956 N  NH1 D ARG A 1 188 ? 25.425  0.973   -41.868 0.25 32.83  ? 188 ARG A NH1 1 
ATOM   1957 N  NH2 A ARG A 1 188 ? 26.478  2.989   -42.071 0.25 28.00  ? 188 ARG A NH2 1 
ATOM   1958 N  NH2 B ARG A 1 188 ? 26.478  2.989   -42.071 0.25 28.00  ? 188 ARG A NH2 1 
ATOM   1959 N  NH2 C ARG A 1 188 ? 26.415  3.029   -41.879 0.25 32.11  ? 188 ARG A NH2 1 
ATOM   1960 N  NH2 D ARG A 1 188 ? 26.415  3.029   -41.879 0.25 32.11  ? 188 ARG A NH2 1 
ATOM   1961 N  N   A GLN A 1 189 ? 24.710  4.670   -35.658 0.25 31.80  ? 189 GLN A N   1 
ATOM   1962 N  N   B GLN A 1 189 ? 24.710  4.670   -35.658 0.25 31.80  ? 189 GLN A N   1 
ATOM   1963 N  N   C GLN A 1 189 ? 24.699  4.639   -35.667 0.25 33.04  ? 189 GLN A N   1 
ATOM   1964 N  N   D GLN A 1 189 ? 24.699  4.639   -35.667 0.25 33.04  ? 189 GLN A N   1 
ATOM   1965 C  CA  A GLN A 1 189 ? 23.969  5.957   -35.547 0.25 34.62  ? 189 GLN A CA  1 
ATOM   1966 C  CA  B GLN A 1 189 ? 23.969  5.957   -35.547 0.25 34.62  ? 189 GLN A CA  1 
ATOM   1967 C  CA  C GLN A 1 189 ? 23.864  5.865   -35.558 0.25 35.72  ? 189 GLN A CA  1 
ATOM   1968 C  CA  D GLN A 1 189 ? 23.864  5.865   -35.558 0.25 35.72  ? 189 GLN A CA  1 
ATOM   1969 C  C   A GLN A 1 189 ? 23.780  6.608   -36.926 0.25 35.82  ? 189 GLN A C   1 
ATOM   1970 C  C   B GLN A 1 189 ? 23.780  6.608   -36.926 0.25 35.82  ? 189 GLN A C   1 
ATOM   1971 C  C   C GLN A 1 189 ? 23.819  6.592   -36.911 0.25 36.63  ? 189 GLN A C   1 
ATOM   1972 C  C   D GLN A 1 189 ? 23.819  6.592   -36.911 0.25 36.63  ? 189 GLN A C   1 
ATOM   1973 O  O   A GLN A 1 189 ? 23.540  7.830   -36.955 0.25 37.08  ? 189 GLN A O   1 
ATOM   1974 O  O   B GLN A 1 189 ? 23.540  7.830   -36.955 0.25 37.08  ? 189 GLN A O   1 
ATOM   1975 O  O   C GLN A 1 189 ? 23.739  7.835   -36.906 0.25 38.22  ? 189 GLN A O   1 
ATOM   1976 O  O   D GLN A 1 189 ? 23.739  7.835   -36.906 0.25 38.22  ? 189 GLN A O   1 
ATOM   1977 C  CB  A GLN A 1 189 ? 24.674  6.895   -34.566 0.25 36.94  ? 189 GLN A CB  1 
ATOM   1978 C  CB  B GLN A 1 189 ? 24.674  6.895   -34.566 0.25 36.94  ? 189 GLN A CB  1 
ATOM   1979 C  CB  C GLN A 1 189 ? 24.367  6.681   -34.368 0.25 38.52  ? 189 GLN A CB  1 
ATOM   1980 C  CB  D GLN A 1 189 ? 24.367  6.681   -34.368 0.25 38.52  ? 189 GLN A CB  1 
ATOM   1981 C  CG  A GLN A 1 189 ? 24.523  6.447   -33.115 0.25 39.94  ? 189 GLN A CG  1 
ATOM   1982 C  CG  B GLN A 1 189 ? 24.523  6.447   -33.115 0.25 39.94  ? 189 GLN A CG  1 
ATOM   1983 C  CG  C GLN A 1 189 ? 24.184  5.927   -33.049 0.25 40.49  ? 189 GLN A CG  1 
ATOM   1984 C  CG  D GLN A 1 189 ? 24.184  5.927   -33.049 0.25 40.49  ? 189 GLN A CG  1 
ATOM   1985 C  CD  A GLN A 1 189 ? 24.447  7.591   -32.131 0.25 41.80  ? 189 GLN A CD  1 
ATOM   1986 C  CD  B GLN A 1 189 ? 24.447  7.591   -32.131 0.25 41.80  ? 189 GLN A CD  1 
ATOM   1987 C  CD  C GLN A 1 189 ? 23.043  6.448   -32.197 0.25 42.09  ? 189 GLN A CD  1 
ATOM   1988 C  CD  D GLN A 1 189 ? 23.043  6.448   -32.197 0.25 42.09  ? 189 GLN A CD  1 
ATOM   1989 O  OE1 A GLN A 1 189 ? 25.044  8.648   -32.324 0.25 43.39  ? 189 GLN A OE1 1 
ATOM   1990 O  OE1 B GLN A 1 189 ? 25.044  8.648   -32.324 0.25 43.39  ? 189 GLN A OE1 1 
ATOM   1991 O  OE1 C GLN A 1 189 ? 22.822  7.660   -32.068 0.25 44.95  ? 189 GLN A OE1 1 
ATOM   1992 O  OE1 D GLN A 1 189 ? 22.822  7.660   -32.068 0.25 44.95  ? 189 GLN A OE1 1 
ATOM   1993 N  NE2 A GLN A 1 189 ? 23.711  7.379   -31.049 0.25 43.49  ? 189 GLN A NE2 1 
ATOM   1994 N  NE2 B GLN A 1 189 ? 23.711  7.379   -31.049 0.25 43.49  ? 189 GLN A NE2 1 
ATOM   1995 N  NE2 C GLN A 1 189 ? 22.308  5.526   -31.593 0.25 41.35  ? 189 GLN A NE2 1 
ATOM   1996 N  NE2 D GLN A 1 189 ? 22.308  5.526   -31.593 0.25 41.35  ? 189 GLN A NE2 1 
ATOM   1997 N  N   . THR A 1 190 ? 23.842  5.823   -38.011 1.00 35.46  ? 190 THR A N   1 
ATOM   1998 C  CA  . THR A 1 190 ? 23.467  6.255   -39.385 1.00 38.27  ? 190 THR A CA  1 
ATOM   1999 C  C   . THR A 1 190 ? 21.953  6.481   -39.380 1.00 37.55  ? 190 THR A C   1 
ATOM   2000 O  O   . THR A 1 190 ? 21.255  5.771   -38.620 1.00 33.99  ? 190 THR A O   1 
ATOM   2001 C  CB  . THR A 1 190 ? 23.853  5.176   -40.422 1.00 38.14  ? 190 THR A CB  1 
ATOM   2002 O  OG1 . THR A 1 190 ? 24.023  5.747   -41.722 1.00 38.35  ? 190 THR A OG1 1 
ATOM   2003 C  CG2 . THR A 1 190 ? 22.850  4.046   -40.508 1.00 35.14  ? 190 THR A CG2 1 
ATOM   2004 N  N   . ALA A 1 191 ? 21.463  7.420   -40.182 1.00 40.46  ? 191 ALA A N   1 
ATOM   2005 C  CA  . ALA A 1 191 ? 20.016  7.729   -40.301 1.00 41.78  ? 191 ALA A CA  1 
ATOM   2006 C  C   . ALA A 1 191 ? 19.228  6.443   -40.592 1.00 39.20  ? 191 ALA A C   1 
ATOM   2007 O  O   . ALA A 1 191 ? 19.538  5.750   -41.584 1.00 37.09  ? 191 ALA A O   1 
ATOM   2008 C  CB  . ALA A 1 191 ? 19.782  8.767   -41.371 1.00 44.78  ? 191 ALA A CB  1 
ATOM   2009 N  N   . GLN A 1 192 ? 18.246  6.150   -39.738 1.00 38.38  ? 192 GLN A N   1 
ATOM   2010 C  CA  . GLN A 1 192 ? 17.314  4.994   -39.825 1.00 37.51  ? 192 GLN A CA  1 
ATOM   2011 C  C   . GLN A 1 192 ? 15.921  5.491   -39.432 1.00 37.88  ? 192 GLN A C   1 
ATOM   2012 O  O   . GLN A 1 192 ? 15.832  6.347   -38.516 1.00 39.48  ? 192 GLN A O   1 
ATOM   2013 C  CB  . GLN A 1 192 ? 17.718  3.890   -38.842 1.00 35.39  ? 192 GLN A CB  1 
ATOM   2014 C  CG  . GLN A 1 192 ? 18.946  3.119   -39.247 1.00 33.93  ? 192 GLN A CG  1 
ATOM   2015 C  CD  . GLN A 1 192 ? 19.395  2.136   -38.196 1.00 32.61  ? 192 GLN A CD  1 
ATOM   2016 O  OE1 . GLN A 1 192 ? 19.012  0.973   -38.224 1.00 31.53  ? 192 GLN A OE1 1 
ATOM   2017 N  NE2 . GLN A 1 192 ? 20.254  2.584   -37.290 1.00 30.65  ? 192 GLN A NE2 1 
ATOM   2018 N  N   . ALA A 1 193 ? 14.872  4.973   -40.066 1.00 37.45  ? 193 ALA A N   1 
ATOM   2019 C  CA  . ALA A 1 193 ? 13.478  5.261   -39.651 1.00 40.99  ? 193 ALA A CA  1 
ATOM   2020 C  C   . ALA A 1 193 ? 12.621  4.015   -39.835 1.00 36.71  ? 193 ALA A C   1 
ATOM   2021 O  O   . ALA A 1 193 ? 12.846  3.255   -40.790 1.00 33.84  ? 193 ALA A O   1 
ATOM   2022 C  CB  . ALA A 1 193 ? 12.918  6.453   -40.382 1.00 39.46  ? 193 ALA A CB  1 
ATOM   2023 N  N   . ALA A 1 194 ? 11.714  3.799   -38.887 1.00 40.55  ? 194 ALA A N   1 
ATOM   2024 C  CA  . ALA A 1 194 ? 10.714  2.713   -38.913 1.00 40.48  ? 194 ALA A CA  1 
ATOM   2025 C  C   . ALA A 1 194 ? 9.848   2.909   -40.148 1.00 41.73  ? 194 ALA A C   1 
ATOM   2026 O  O   . ALA A 1 194 ? 9.628   4.089   -40.504 1.00 42.90  ? 194 ALA A O   1 
ATOM   2027 C  CB  . ALA A 1 194 ? 9.891   2.768   -37.659 1.00 43.62  ? 194 ALA A CB  1 
ATOM   2028 N  N   . GLY A 1 195 ? 9.435   1.817   -40.794 1.00 44.39  ? 195 GLY A N   1 
ATOM   2029 C  CA  . GLY A 1 195 ? 8.328   1.821   -41.768 1.00 43.80  ? 195 GLY A CA  1 
ATOM   2030 C  C   . GLY A 1 195 ? 7.059   2.372   -41.128 1.00 43.31  ? 195 GLY A C   1 
ATOM   2031 O  O   . GLY A 1 195 ? 6.995   2.437   -39.864 1.00 36.91  ? 195 GLY A O   1 
ATOM   2032 N  N   . THR A 1 196 ? 6.090   2.786   -41.950 1.00 40.34  ? 196 THR A N   1 
ATOM   2033 C  CA  . THR A 1 196 ? 4.769   3.292   -41.492 1.00 40.29  ? 196 THR A CA  1 
ATOM   2034 C  C   . THR A 1 196 ? 4.177   2.199   -40.606 1.00 36.59  ? 196 THR A C   1 
ATOM   2035 O  O   . THR A 1 196 ? 4.258   1.031   -40.986 1.00 37.98  ? 196 THR A O   1 
ATOM   2036 C  CB  . THR A 1 196 ? 3.847   3.637   -42.669 1.00 43.73  ? 196 THR A CB  1 
ATOM   2037 O  OG1 . THR A 1 196 ? 3.906   2.519   -43.556 1.00 51.82  ? 196 THR A OG1 1 
ATOM   2038 C  CG2 . THR A 1 196 ? 4.247   4.902   -43.399 1.00 42.97  ? 196 THR A CG2 1 
ATOM   2039 N  N   . ASP A 1 197 ? 3.665   2.549   -39.437 1.00 33.92  ? 197 ASP A N   1 
ATOM   2040 C  CA  . ASP A 1 197 ? 3.122   1.511   -38.534 1.00 37.28  ? 197 ASP A CA  1 
ATOM   2041 C  C   . ASP A 1 197 ? 1.672   1.257   -38.932 1.00 39.86  ? 197 ASP A C   1 
ATOM   2042 O  O   . ASP A 1 197 ? 1.063   2.155   -39.566 1.00 41.07  ? 197 ASP A O   1 
ATOM   2043 C  CB  . ASP A 1 197 ? 3.233   1.863   -37.053 1.00 35.07  ? 197 ASP A CB  1 
ATOM   2044 C  CG  . ASP A 1 197 ? 3.217   0.604   -36.203 1.00 34.97  ? 197 ASP A CG  1 
ATOM   2045 O  OD1 . ASP A 1 197 ? 3.558   -0.508  -36.771 1.00 29.17  ? 197 ASP A OD1 1 
ATOM   2046 O  OD2 . ASP A 1 197 ? 2.824   0.722   -35.029 1.00 34.02  ? 197 ASP A OD2 1 
ATOM   2047 N  N   . THR A 1 198 ? 1.183   0.063   -38.594 1.00 33.18  ? 198 THR A N   1 
ATOM   2048 C  CA  . THR A 1 198 ? -0.210  -0.375  -38.817 1.00 32.68  ? 198 THR A CA  1 
ATOM   2049 C  C   . THR A 1 198 ? -0.783  -0.912  -37.496 1.00 28.80  ? 198 THR A C   1 
ATOM   2050 O  O   . THR A 1 198 ? 0.007   -1.233  -36.577 1.00 28.71  ? 198 THR A O   1 
ATOM   2051 C  CB  . THR A 1 198 ? -0.184  -1.362  -39.976 1.00 34.09  ? 198 THR A CB  1 
ATOM   2052 O  OG1 . THR A 1 198 ? 0.770   -2.344  -39.575 1.00 34.72  ? 198 THR A OG1 1 
ATOM   2053 C  CG2 . THR A 1 198 ? 0.249   -0.723  -41.276 1.00 35.20  ? 198 THR A CG2 1 
ATOM   2054 N  N   . THR A 1 199 ? -2.106  -0.987  -37.402 1.00 27.10  ? 199 THR A N   1 
ATOM   2055 C  CA  . THR A 1 199 ? -2.846  -1.518  -36.239 1.00 24.34  ? 199 THR A CA  1 
ATOM   2056 C  C   . THR A 1 199 ? -2.895  -3.038  -36.351 1.00 24.56  ? 199 THR A C   1 
ATOM   2057 O  O   . THR A 1 199 ? -3.114  -3.534  -37.466 1.00 25.84  ? 199 THR A O   1 
ATOM   2058 C  CB  . THR A 1 199 ? -4.228  -0.869  -36.134 1.00 27.99  ? 199 THR A CB  1 
ATOM   2059 O  OG1 . THR A 1 199 ? -3.996  0.536   -36.140 1.00 28.64  ? 199 THR A OG1 1 
ATOM   2060 C  CG2 . THR A 1 199 ? -4.978  -1.272  -34.886 1.00 28.10  ? 199 THR A CG2 1 
ATOM   2061 N  N   . ILE A 1 200 ? -2.685  -3.732  -35.222 1.00 24.22  ? 200 ILE A N   1 
ATOM   2062 C  CA  . ILE A 1 200 ? -2.623  -5.218  -35.133 1.00 25.28  ? 200 ILE A CA  1 
ATOM   2063 C  C   . ILE A 1 200 ? -4.055  -5.731  -35.012 1.00 27.16  ? 200 ILE A C   1 
ATOM   2064 O  O   . ILE A 1 200 ? -4.609  -5.776  -33.868 1.00 27.94  ? 200 ILE A O   1 
ATOM   2065 C  CB  . ILE A 1 200 ? -1.734  -5.709  -33.974 1.00 25.41  ? 200 ILE A CB  1 
ATOM   2066 C  CG1 . ILE A 1 200 ? -0.337  -5.083  -34.003 1.00 27.45  ? 200 ILE A CG1 1 
ATOM   2067 C  CG2 . ILE A 1 200 ? -1.664  -7.230  -33.962 1.00 24.94  ? 200 ILE A CG2 1 
ATOM   2068 C  CD1 . ILE A 1 200 ? 0.267   -4.934  -32.623 1.00 28.19  ? 200 ILE A CD1 1 
ATOM   2069 N  N   . THR A 1 201 ? -4.627  -6.074  -36.166 1.00 27.07  ? 201 THR A N   1 
ATOM   2070 C  CA  . THR A 1 201 ? -6.083  -6.303  -36.355 1.00 26.27  ? 201 THR A CA  1 
ATOM   2071 C  C   . THR A 1 201 ? -6.500  -7.444  -35.420 1.00 24.21  ? 201 THR A C   1 
ATOM   2072 O  O   . THR A 1 201 ? -7.469  -7.268  -34.656 1.00 26.44  ? 201 THR A O   1 
ATOM   2073 C  CB  . THR A 1 201 ? -6.387  -6.573  -37.836 1.00 24.82  ? 201 THR A CB  1 
ATOM   2074 O  OG1 . THR A 1 201 ? -5.873  -5.478  -38.597 1.00 25.20  ? 201 THR A OG1 1 
ATOM   2075 C  CG2 . THR A 1 201 ? -7.864  -6.761  -38.107 1.00 27.15  ? 201 THR A CG2 1 
ATOM   2076 N  N   . VAL A 1 202 ? -5.795  -8.572  -35.479 1.00 24.06  ? 202 VAL A N   1 
ATOM   2077 C  CA  . VAL A 1 202 ? -6.138  -9.773  -34.675 1.00 24.92  ? 202 VAL A CA  1 
ATOM   2078 C  C   . VAL A 1 202 ? -6.215  -9.388  -33.191 1.00 28.21  ? 202 VAL A C   1 
ATOM   2079 O  O   . VAL A 1 202 ? -7.120  -9.899  -32.504 1.00 25.46  ? 202 VAL A O   1 
ATOM   2080 C  CB  . VAL A 1 202 ? -5.172  -10.936 -34.919 1.00 24.20  ? 202 VAL A CB  1 
ATOM   2081 C  CG1 . VAL A 1 202 ? -3.730  -10.611 -34.547 1.00 25.84  ? 202 VAL A CG1 1 
ATOM   2082 C  CG2 . VAL A 1 202 ? -5.623  -12.175 -34.167 1.00 24.39  ? 202 VAL A CG2 1 
ATOM   2083 N  N   . ASN A 1 203 ? -5.322  -8.506  -32.713 1.00 29.28  ? 203 ASN A N   1 
ATOM   2084 C  CA  . ASN A 1 203 ? -5.311  -8.075  -31.280 1.00 27.36  ? 203 ASN A CA  1 
ATOM   2085 C  C   . ASN A 1 203 ? -6.539  -7.203  -30.990 1.00 26.00  ? 203 ASN A C   1 
ATOM   2086 O  O   . ASN A 1 203 ? -7.124  -7.323  -29.889 1.00 23.62  ? 203 ASN A O   1 
ATOM   2087 C  CB  . ASN A 1 203 ? -4.034  -7.331  -30.892 1.00 27.24  ? 203 ASN A CB  1 
ATOM   2088 C  CG  . ASN A 1 203 ? -2.802  -8.203  -30.794 1.00 26.94  ? 203 ASN A CG  1 
ATOM   2089 O  OD1 . ASN A 1 203 ? -2.890  -9.424  -30.960 1.00 26.80  ? 203 ASN A OD1 1 
ATOM   2090 N  ND2 . ASN A 1 203 ? -1.655  -7.576  -30.510 1.00 26.57  ? 203 ASN A ND2 1 
ATOM   2091 N  N   . VAL A 1 204 ? -6.914  -6.328  -31.916 1.00 27.27  ? 204 VAL A N   1 
ATOM   2092 C  CA  . VAL A 1 204 ? -8.120  -5.469  -31.733 1.00 28.84  ? 204 VAL A CA  1 
ATOM   2093 C  C   . VAL A 1 204 ? -9.351  -6.375  -31.560 1.00 27.31  ? 204 VAL A C   1 
ATOM   2094 O  O   . VAL A 1 204 ? -10.159 -6.131  -30.655 1.00 27.73  ? 204 VAL A O   1 
ATOM   2095 C  CB  . VAL A 1 204 ? -8.285  -4.460  -32.881 1.00 29.11  ? 204 VAL A CB  1 
ATOM   2096 C  CG1 . VAL A 1 204 ? -9.604  -3.712  -32.755 1.00 29.25  ? 204 VAL A CG1 1 
ATOM   2097 C  CG2 . VAL A 1 204 ? -7.125  -3.466  -32.930 1.00 27.49  ? 204 VAL A CG2 1 
ATOM   2098 N  N   . LEU A 1 205 ? -9.469  -7.405  -32.381 1.00 27.23  ? 205 LEU A N   1 
ATOM   2099 C  CA  . LEU A 1 205 ? -10.610 -8.347  -32.303 1.00 28.36  ? 205 LEU A CA  1 
ATOM   2100 C  C   . LEU A 1 205 ? -10.602 -9.036  -30.944 1.00 27.78  ? 205 LEU A C   1 
ATOM   2101 O  O   . LEU A 1 205 ? -11.697 -9.158  -30.342 1.00 26.34  ? 205 LEU A O   1 
ATOM   2102 C  CB  . LEU A 1 205 ? -10.550 -9.351  -33.454 1.00 26.26  ? 205 LEU A CB  1 
ATOM   2103 C  CG  . LEU A 1 205 ? -10.849 -8.744  -34.825 1.00 27.44  ? 205 LEU A CG  1 
ATOM   2104 C  CD1 . LEU A 1 205 ? -10.486 -9.724  -35.926 1.00 26.51  ? 205 LEU A CD1 1 
ATOM   2105 C  CD2 . LEU A 1 205 ? -12.311 -8.316  -34.945 1.00 27.32  ? 205 LEU A CD2 1 
ATOM   2106 N  N   . ALA A 1 206 ? -9.430  -9.471  -30.477 1.00 28.04  ? 206 ALA A N   1 
ATOM   2107 C  CA  . ALA A 1 206 ? -9.283  -10.204 -29.195 1.00 28.10  ? 206 ALA A CA  1 
ATOM   2108 C  C   . ALA A 1 206 ? -9.798  -9.320  -28.061 1.00 28.55  ? 206 ALA A C   1 
ATOM   2109 O  O   . ALA A 1 206 ? -10.514 -9.801  -27.171 1.00 30.20  ? 206 ALA A O   1 
ATOM   2110 C  CB  . ALA A 1 206 ? -7.845  -10.613 -28.978 1.00 30.33  ? 206 ALA A CB  1 
ATOM   2111 N  N   . TRP A 1 207 ? -9.493  -8.040  -28.149 1.00 27.44  ? 207 TRP A N   1 
ATOM   2112 C  CA  . TRP A 1 207 ? -9.882  -7.037  -27.141 1.00 28.69  ? 207 TRP A CA  1 
ATOM   2113 C  C   . TRP A 1 207 ? -11.396 -6.802  -27.166 1.00 29.57  ? 207 TRP A C   1 
ATOM   2114 O  O   . TRP A 1 207 ? -11.969 -6.626  -26.088 1.00 29.74  ? 207 TRP A O   1 
ATOM   2115 C  CB  . TRP A 1 207 ? -9.060  -5.785  -27.441 1.00 28.68  ? 207 TRP A CB  1 
ATOM   2116 C  CG  . TRP A 1 207 ? -9.343  -4.614  -26.579 1.00 28.26  ? 207 TRP A CG  1 
ATOM   2117 C  CD1 . TRP A 1 207 ? -8.953  -4.404  -25.287 1.00 31.45  ? 207 TRP A CD1 1 
ATOM   2118 C  CD2 . TRP A 1 207 ? -10.054 -3.445  -26.996 1.00 30.44  ? 207 TRP A CD2 1 
ATOM   2119 N  NE1 . TRP A 1 207 ? -9.371  -3.169  -24.872 1.00 30.41  ? 207 TRP A NE1 1 
ATOM   2120 C  CE2 . TRP A 1 207 ? -10.048 -2.558  -25.899 1.00 31.67  ? 207 TRP A CE2 1 
ATOM   2121 C  CE3 . TRP A 1 207 ? -10.678 -3.067  -28.188 1.00 30.02  ? 207 TRP A CE3 1 
ATOM   2122 C  CZ2 . TRP A 1 207 ? -10.667 -1.314  -25.964 1.00 31.02  ? 207 TRP A CZ2 1 
ATOM   2123 C  CZ3 . TRP A 1 207 ? -11.272 -1.830  -28.249 1.00 31.84  ? 207 TRP A CZ3 1 
ATOM   2124 C  CH2 . TRP A 1 207 ? -11.256 -0.967  -27.154 1.00 31.67  ? 207 TRP A CH2 1 
ATOM   2125 N  N   . LEU A 1 208 ? -12.028 -6.787  -28.345 1.00 30.99  ? 208 LEU A N   1 
ATOM   2126 C  CA  . LEU A 1 208 ? -13.511 -6.669  -28.443 1.00 27.83  ? 208 LEU A CA  1 
ATOM   2127 C  C   . LEU A 1 208 ? -14.139 -7.917  -27.810 1.00 29.01  ? 208 LEU A C   1 
ATOM   2128 O  O   . LEU A 1 208 ? -15.106 -7.748  -27.065 1.00 30.25  ? 208 LEU A O   1 
ATOM   2129 C  CB  . LEU A 1 208 ? -13.960 -6.490  -29.892 1.00 26.82  ? 208 LEU A CB  1 
ATOM   2130 C  CG  . LEU A 1 208 ? -13.532 -5.190  -30.561 1.00 26.65  ? 208 LEU A CG  1 
ATOM   2131 C  CD1 . LEU A 1 208 ? -13.968 -5.175  -32.002 1.00 26.11  ? 208 LEU A CD1 1 
ATOM   2132 C  CD2 . LEU A 1 208 ? -14.046 -3.963  -29.830 1.00 31.03  ? 208 LEU A CD2 1 
ATOM   2133 N  N   . TYR A 1 209 ? -13.577 -9.110  -28.024 1.00 29.89  ? 209 TYR A N   1 
ATOM   2134 C  CA  . TYR A 1 209 ? -14.016 -10.357 -27.337 1.00 31.40  ? 209 TYR A CA  1 
ATOM   2135 C  C   . TYR A 1 209 ? -13.882 -10.203 -25.815 1.00 34.17  ? 209 TYR A C   1 
ATOM   2136 O  O   . TYR A 1 209 ? -14.808 -10.601 -25.088 1.00 38.14  ? 209 TYR A O   1 
ATOM   2137 C  CB  . TYR A 1 209 ? -13.248 -11.584 -27.843 1.00 30.58  ? 209 TYR A CB  1 
ATOM   2138 C  CG  . TYR A 1 209 ? -13.790 -12.186 -29.119 1.00 28.54  ? 209 TYR A CG  1 
ATOM   2139 C  CD1 . TYR A 1 209 ? -15.052 -12.763 -29.164 1.00 29.46  ? 209 TYR A CD1 1 
ATOM   2140 C  CD2 . TYR A 1 209 ? -13.051 -12.181 -30.289 1.00 29.51  ? 209 TYR A CD2 1 
ATOM   2141 C  CE1 . TYR A 1 209 ? -15.562 -13.319 -30.325 1.00 29.50  ? 209 TYR A CE1 1 
ATOM   2142 C  CE2 . TYR A 1 209 ? -13.550 -12.725 -31.465 1.00 29.48  ? 209 TYR A CE2 1 
ATOM   2143 C  CZ  . TYR A 1 209 ? -14.811 -13.304 -31.490 1.00 30.68  ? 209 TYR A CZ  1 
ATOM   2144 O  OH  . TYR A 1 209 ? -15.312 -13.847 -32.652 1.00 29.57  ? 209 TYR A OH  1 
ATOM   2145 N  N   . ALA A 1 210 ? -12.782 -9.619  -25.338 1.00 32.35  ? 210 ALA A N   1 
ATOM   2146 C  CA  . ALA A 1 210 ? -12.582 -9.262  -23.916 1.00 31.16  ? 210 ALA A CA  1 
ATOM   2147 C  C   . ALA A 1 210 ? -13.715 -8.342  -23.443 1.00 32.42  ? 210 ALA A C   1 
ATOM   2148 O  O   . ALA A 1 210 ? -14.213 -8.546  -22.326 1.00 30.99  ? 210 ALA A O   1 
ATOM   2149 C  CB  . ALA A 1 210 ? -11.242 -8.601  -23.708 1.00 31.59  ? 210 ALA A CB  1 
ATOM   2150 N  N   . ALA A 1 211 ? -14.066 -7.317  -24.219 1.00 31.85  ? 211 ALA A N   1 
ATOM   2151 C  CA  . ALA A 1 211 ? -15.150 -6.379  -23.859 1.00 32.97  ? 211 ALA A CA  1 
ATOM   2152 C  C   . ALA A 1 211 ? -16.442 -7.183  -23.666 1.00 31.60  ? 211 ALA A C   1 
ATOM   2153 O  O   . ALA A 1 211 ? -17.063 -6.994  -22.635 1.00 29.18  ? 211 ALA A O   1 
ATOM   2154 C  CB  . ALA A 1 211 ? -15.294 -5.264  -24.879 1.00 35.16  ? 211 ALA A CB  1 
ATOM   2155 N  N   . VAL A 1 212 ? -16.753 -8.118  -24.572 1.00 32.09  ? 212 VAL A N   1 
ATOM   2156 C  CA  . VAL A 1 212 ? -17.987 -8.951  -24.519 1.00 33.59  ? 212 VAL A CA  1 
ATOM   2157 C  C   . VAL A 1 212 ? -17.930 -9.872  -23.295 1.00 35.83  ? 212 VAL A C   1 
ATOM   2158 O  O   . VAL A 1 212 ? -18.935 -9.973  -22.575 1.00 34.94  ? 212 VAL A O   1 
ATOM   2159 C  CB  . VAL A 1 212 ? -18.219 -9.733  -25.823 1.00 34.16  ? 212 VAL A CB  1 
ATOM   2160 C  CG1 . VAL A 1 212 ? -19.231 -10.854 -25.638 1.00 33.74  ? 212 VAL A CG1 1 
ATOM   2161 C  CG2 . VAL A 1 212 ? -18.662 -8.795  -26.944 1.00 32.92  ? 212 VAL A CG2 1 
ATOM   2162 N  N   . ILE A 1 213 ? -16.793 -10.507 -23.039 1.00 33.97  ? 213 ILE A N   1 
ATOM   2163 C  CA  . ILE A 1 213 ? -16.624 -11.354 -21.830 1.00 33.15  ? 213 ILE A CA  1 
ATOM   2164 C  C   . ILE A 1 213 ? -16.930 -10.518 -20.583 1.00 34.10  ? 213 ILE A C   1 
ATOM   2165 O  O   . ILE A 1 213 ? -17.558 -11.067 -19.669 1.00 35.38  ? 213 ILE A O   1 
ATOM   2166 C  CB  . ILE A 1 213 ? -15.221 -11.977 -21.801 1.00 34.83  ? 213 ILE A CB  1 
ATOM   2167 C  CG1 . ILE A 1 213 ? -15.135 -13.121 -22.820 1.00 34.48  ? 213 ILE A CG1 1 
ATOM   2168 C  CG2 . ILE A 1 213 ? -14.871 -12.411 -20.381 1.00 35.77  ? 213 ILE A CG2 1 
ATOM   2169 C  CD1 . ILE A 1 213 ? -13.732 -13.595 -23.151 1.00 36.32  ? 213 ILE A CD1 1 
ATOM   2170 N  N   . ASN A 1 214 ? -16.533 -9.244  -20.559 1.00 33.10  ? 214 ASN A N   1 
ATOM   2171 C  CA  . ASN A 1 214 ? -16.728 -8.337  -19.398 1.00 41.97  ? 214 ASN A CA  1 
ATOM   2172 C  C   . ASN A 1 214 ? -18.125 -7.676  -19.427 1.00 40.52  ? 214 ASN A C   1 
ATOM   2173 O  O   . ASN A 1 214 ? -18.389 -6.820  -18.560 1.00 39.36  ? 214 ASN A O   1 
ATOM   2174 C  CB  . ASN A 1 214 ? -15.579 -7.327  -19.313 1.00 46.91  ? 214 ASN A CB  1 
ATOM   2175 C  CG  . ASN A 1 214 ? -14.354 -7.889  -18.611 1.00 54.59  ? 214 ASN A CG  1 
ATOM   2176 O  OD1 . ASN A 1 214 ? -13.722 -8.841  -19.080 1.00 56.51  ? 214 ASN A OD1 1 
ATOM   2177 N  ND2 . ASN A 1 214 ? -14.018 -7.313  -17.467 1.00 55.41  ? 214 ASN A ND2 1 
ATOM   2178 N  N   . GLY A 1 215 ? -18.981 -8.021  -20.391 1.00 36.04  ? 215 GLY A N   1 
ATOM   2179 C  CA  . GLY A 1 215 ? -20.423 -7.707  -20.354 1.00 38.75  ? 215 GLY A CA  1 
ATOM   2180 C  C   . GLY A 1 215 ? -20.881 -6.531  -21.224 1.00 42.37  ? 215 GLY A C   1 
ATOM   2181 O  O   . GLY A 1 215 ? -22.044 -6.111  -21.077 1.00 41.45  ? 215 GLY A O   1 
ATOM   2182 N  N   A ASP A 1 216 ? -19.988 -6.000  -22.073 0.26 40.82  ? 216 ASP A N   1 
ATOM   2183 N  N   B ASP A 1 216 ? -20.026 -6.038  -22.127 0.24 40.48  ? 216 ASP A N   1 
ATOM   2184 N  N   C ASP A 1 216 ? -19.988 -6.000  -22.073 0.26 40.82  ? 216 ASP A N   1 
ATOM   2185 N  N   D ASP A 1 216 ? -20.026 -6.038  -22.127 0.24 40.48  ? 216 ASP A N   1 
ATOM   2186 C  CA  A ASP A 1 216 ? -20.286 -4.925  -23.062 0.26 41.23  ? 216 ASP A CA  1 
ATOM   2187 C  CA  B ASP A 1 216 ? -20.342 -4.893  -23.026 0.24 40.66  ? 216 ASP A CA  1 
ATOM   2188 C  CA  C ASP A 1 216 ? -20.286 -4.925  -23.062 0.26 41.23  ? 216 ASP A CA  1 
ATOM   2189 C  CA  D ASP A 1 216 ? -20.342 -4.893  -23.026 0.24 40.66  ? 216 ASP A CA  1 
ATOM   2190 C  C   A ASP A 1 216 ? -20.771 -5.569  -24.367 0.26 40.38  ? 216 ASP A C   1 
ATOM   2191 C  C   B ASP A 1 216 ? -20.697 -5.435  -24.419 0.24 39.97  ? 216 ASP A C   1 
ATOM   2192 C  C   C ASP A 1 216 ? -20.771 -5.569  -24.367 0.26 40.38  ? 216 ASP A C   1 
ATOM   2193 C  C   D ASP A 1 216 ? -20.697 -5.435  -24.419 0.24 39.97  ? 216 ASP A C   1 
ATOM   2194 O  O   A ASP A 1 216 ? -20.087 -6.496  -24.850 0.26 40.93  ? 216 ASP A O   1 
ATOM   2195 O  O   B ASP A 1 216 ? -19.853 -6.146  -25.009 0.24 40.02  ? 216 ASP A O   1 
ATOM   2196 O  O   C ASP A 1 216 ? -20.087 -6.496  -24.850 0.26 40.93  ? 216 ASP A O   1 
ATOM   2197 O  O   D ASP A 1 216 ? -19.853 -6.146  -25.009 0.24 40.02  ? 216 ASP A O   1 
ATOM   2198 C  CB  A ASP A 1 216 ? -19.055 -4.068  -23.380 0.26 42.64  ? 216 ASP A CB  1 
ATOM   2199 C  CB  B ASP A 1 216 ? -19.181 -3.894  -23.060 0.24 41.65  ? 216 ASP A CB  1 
ATOM   2200 C  CB  C ASP A 1 216 ? -19.055 -4.068  -23.380 0.26 42.64  ? 216 ASP A CB  1 
ATOM   2201 C  CB  D ASP A 1 216 ? -19.181 -3.894  -23.060 0.24 41.65  ? 216 ASP A CB  1 
ATOM   2202 C  CG  A ASP A 1 216 ? -18.436 -3.320  -22.207 0.26 43.88  ? 216 ASP A CG  1 
ATOM   2203 C  CG  B ASP A 1 216 ? -19.616 -2.437  -23.054 0.24 42.49  ? 216 ASP A CG  1 
ATOM   2204 C  CG  C ASP A 1 216 ? -18.436 -3.320  -22.207 0.26 43.88  ? 216 ASP A CG  1 
ATOM   2205 C  CG  D ASP A 1 216 ? -19.616 -2.437  -23.054 0.24 42.49  ? 216 ASP A CG  1 
ATOM   2206 O  OD1 A ASP A 1 216 ? -19.179 -2.986  -21.252 0.26 44.03  ? 216 ASP A OD1 1 
ATOM   2207 O  OD1 B ASP A 1 216 ? -20.836 -2.192  -22.979 0.24 43.17  ? 216 ASP A OD1 1 
ATOM   2208 O  OD1 C ASP A 1 216 ? -19.179 -2.986  -21.252 0.26 44.03  ? 216 ASP A OD1 1 
ATOM   2209 O  OD1 D ASP A 1 216 ? -20.836 -2.192  -22.979 0.24 43.17  ? 216 ASP A OD1 1 
ATOM   2210 O  OD2 A ASP A 1 216 ? -17.203 -3.062  -22.271 0.26 44.64  ? 216 ASP A OD2 1 
ATOM   2211 O  OD2 B ASP A 1 216 ? -18.726 -1.556  -23.111 0.24 42.67  ? 216 ASP A OD2 1 
ATOM   2212 O  OD2 C ASP A 1 216 ? -17.203 -3.062  -22.271 0.26 44.64  ? 216 ASP A OD2 1 
ATOM   2213 O  OD2 D ASP A 1 216 ? -18.726 -1.556  -23.111 0.24 42.67  ? 216 ASP A OD2 1 
ATOM   2214 N  N   . ARG A 1 217 ? -21.888 -5.099  -24.928 1.00 37.94  ? 217 ARG A N   1 
ATOM   2215 C  CA  . ARG A 1 217 ? -22.386 -5.598  -26.248 1.00 36.62  ? 217 ARG A CA  1 
ATOM   2216 C  C   . ARG A 1 217 ? -22.816 -4.472  -27.185 1.00 32.86  ? 217 ARG A C   1 
ATOM   2217 O  O   . ARG A 1 217 ? -23.341 -4.809  -28.292 1.00 28.94  ? 217 ARG A O   1 
ATOM   2218 C  CB  . ARG A 1 217 ? -23.551 -6.574  -26.071 1.00 38.28  ? 217 ARG A CB  1 
ATOM   2219 C  CG  . ARG A 1 217 ? -23.113 -7.903  -25.475 1.00 41.34  ? 217 ARG A CG  1 
ATOM   2220 C  CD  . ARG A 1 217 ? -24.245 -8.870  -25.310 1.00 42.38  ? 217 ARG A CD  1 
ATOM   2221 N  NE  . ARG A 1 217 ? -24.867 -9.150  -26.600 1.00 45.99  ? 217 ARG A NE  1 
ATOM   2222 C  CZ  . ARG A 1 217 ? -24.636 -10.219 -27.368 1.00 43.83  ? 217 ARG A CZ  1 
ATOM   2223 N  NH1 . ARG A 1 217 ? -23.788 -11.156 -26.986 1.00 40.95  ? 217 ARG A NH1 1 
ATOM   2224 N  NH2 . ARG A 1 217 ? -25.275 -10.354 -28.520 1.00 43.87  ? 217 ARG A NH2 1 
ATOM   2225 N  N   . TRP A 1 218 ? -22.595 -3.206  -26.821 1.00 31.97  ? 218 TRP A N   1 
ATOM   2226 C  CA  . TRP A 1 218 ? -23.246 -2.081  -27.541 1.00 32.07  ? 218 TRP A CA  1 
ATOM   2227 C  C   . TRP A 1 218 ? -22.752 -1.979  -28.998 1.00 31.65  ? 218 TRP A C   1 
ATOM   2228 O  O   . TRP A 1 218 ? -23.482 -1.415  -29.811 1.00 30.78  ? 218 TRP A O   1 
ATOM   2229 C  CB  . TRP A 1 218 ? -23.071 -0.765  -26.787 1.00 32.95  ? 218 TRP A CB  1 
ATOM   2230 C  CG  . TRP A 1 218 ? -21.663 -0.288  -26.680 1.00 34.69  ? 218 TRP A CG  1 
ATOM   2231 C  CD1 . TRP A 1 218 ? -20.858 -0.395  -25.584 1.00 33.38  ? 218 TRP A CD1 1 
ATOM   2232 C  CD2 . TRP A 1 218 ? -20.918 0.437   -27.671 1.00 35.43  ? 218 TRP A CD2 1 
ATOM   2233 N  NE1 . TRP A 1 218 ? -19.657 0.204   -25.835 1.00 36.06  ? 218 TRP A NE1 1 
ATOM   2234 C  CE2 . TRP A 1 218 ? -19.656 0.709   -27.108 1.00 34.86  ? 218 TRP A CE2 1 
ATOM   2235 C  CE3 . TRP A 1 218 ? -21.180 0.874   -28.977 1.00 38.63  ? 218 TRP A CE3 1 
ATOM   2236 C  CZ2 . TRP A 1 218 ? -18.662 1.390   -27.809 1.00 37.28  ? 218 TRP A CZ2 1 
ATOM   2237 C  CZ3 . TRP A 1 218 ? -20.198 1.555   -29.668 1.00 38.09  ? 218 TRP A CZ3 1 
ATOM   2238 C  CH2 . TRP A 1 218 ? -18.953 1.802   -29.090 1.00 36.33  ? 218 TRP A CH2 1 
ATOM   2239 N  N   . PHE A 1 219 ? -21.556 -2.476  -29.318 1.00 30.49  ? 219 PHE A N   1 
ATOM   2240 C  CA  . PHE A 1 219 ? -20.875 -2.248  -30.618 1.00 29.56  ? 219 PHE A CA  1 
ATOM   2241 C  C   . PHE A 1 219 ? -21.136 -3.429  -31.539 1.00 30.41  ? 219 PHE A C   1 
ATOM   2242 O  O   . PHE A 1 219 ? -20.701 -3.370  -32.688 1.00 33.61  ? 219 PHE A O   1 
ATOM   2243 C  CB  . PHE A 1 219 ? -19.363 -2.104  -30.431 1.00 32.20  ? 219 PHE A CB  1 
ATOM   2244 C  CG  . PHE A 1 219 ? -18.763 -3.129  -29.500 1.00 27.95  ? 219 PHE A CG  1 
ATOM   2245 C  CD1 . PHE A 1 219 ? -18.429 -4.398  -29.948 1.00 28.12  ? 219 PHE A CD1 1 
ATOM   2246 C  CD2 . PHE A 1 219 ? -18.591 -2.835  -28.163 1.00 28.33  ? 219 PHE A CD2 1 
ATOM   2247 C  CE1 . PHE A 1 219 ? -17.896 -5.341  -29.080 1.00 29.07  ? 219 PHE A CE1 1 
ATOM   2248 C  CE2 . PHE A 1 219 ? -18.063 -3.779  -27.296 1.00 31.27  ? 219 PHE A CE2 1 
ATOM   2249 C  CZ  . PHE A 1 219 ? -17.708 -5.031  -27.757 1.00 29.60  ? 219 PHE A CZ  1 
ATOM   2250 N  N   . LEU A 1 220 ? -21.782 -4.491  -31.063 1.00 28.74  ? 220 LEU A N   1 
ATOM   2251 C  CA  . LEU A 1 220 ? -22.112 -5.619  -31.968 1.00 31.98  ? 220 LEU A CA  1 
ATOM   2252 C  C   . LEU A 1 220 ? -23.196 -5.181  -32.974 1.00 33.15  ? 220 LEU A C   1 
ATOM   2253 O  O   . LEU A 1 220 ? -23.867 -4.145  -32.743 1.00 31.20  ? 220 LEU A O   1 
ATOM   2254 C  CB  . LEU A 1 220 ? -22.564 -6.827  -31.143 1.00 34.79  ? 220 LEU A CB  1 
ATOM   2255 C  CG  . LEU A 1 220 ? -21.538 -7.410  -30.174 1.00 35.78  ? 220 LEU A CG  1 
ATOM   2256 C  CD1 . LEU A 1 220 ? -22.171 -8.500  -29.333 1.00 37.65  ? 220 LEU A CD1 1 
ATOM   2257 C  CD2 . LEU A 1 220 ? -20.317 -7.945  -30.902 1.00 37.73  ? 220 LEU A CD2 1 
ATOM   2258 N  N   . ASN A 1 221 ? -23.347 -5.921  -34.071 1.00 30.74  ? 221 ASN A N   1 
ATOM   2259 C  CA  . ASN A 1 221 ? -24.360 -5.629  -35.107 1.00 30.55  ? 221 ASN A CA  1 
ATOM   2260 C  C   . ASN A 1 221 ? -24.866 -6.952  -35.663 1.00 33.62  ? 221 ASN A C   1 
ATOM   2261 O  O   . ASN A 1 221 ? -24.315 -8.021  -35.319 1.00 33.45  ? 221 ASN A O   1 
ATOM   2262 C  CB  . ASN A 1 221 ? -23.851 -4.681  -36.196 1.00 30.77  ? 221 ASN A CB  1 
ATOM   2263 C  CG  . ASN A 1 221 ? -22.769 -5.269  -37.084 1.00 32.24  ? 221 ASN A CG  1 
ATOM   2264 O  OD1 . ASN A 1 221 ? -22.625 -6.489  -37.198 1.00 33.89  ? 221 ASN A OD1 1 
ATOM   2265 N  ND2 . ASN A 1 221 ? -22.012 -4.399  -37.732 1.00 30.63  ? 221 ASN A ND2 1 
ATOM   2266 N  N   . ARG A 1 222 ? -25.880 -6.868  -36.516 1.00 36.60  ? 222 ARG A N   1 
ATOM   2267 C  CA  . ARG A 1 222 ? -26.587 -8.058  -37.025 1.00 40.83  ? 222 ARG A CA  1 
ATOM   2268 C  C   . ARG A 1 222 ? -25.923 -8.493  -38.319 1.00 35.91  ? 222 ARG A C   1 
ATOM   2269 O  O   . ARG A 1 222 ? -26.391 -9.464  -38.894 1.00 39.47  ? 222 ARG A O   1 
ATOM   2270 C  CB  . ARG A 1 222 ? -28.065 -7.728  -37.238 1.00 49.02  ? 222 ARG A CB  1 
ATOM   2271 C  CG  . ARG A 1 222 ? -28.313 -6.619  -38.251 1.00 56.88  ? 222 ARG A CG  1 
ATOM   2272 C  CD  . ARG A 1 222 ? -29.758 -6.644  -38.706 1.00 66.34  ? 222 ARG A CD  1 
ATOM   2273 N  NE  . ARG A 1 222 ? -30.023 -5.713  -39.789 1.00 71.14  ? 222 ARG A NE  1 
ATOM   2274 C  CZ  . ARG A 1 222 ? -29.967 -6.004  -41.088 1.00 79.15  ? 222 ARG A CZ  1 
ATOM   2275 N  NH1 . ARG A 1 222 ? -29.644 -7.224  -41.496 1.00 85.79  ? 222 ARG A NH1 1 
ATOM   2276 N  NH2 . ARG A 1 222 ? -30.236 -5.061  -41.980 1.00 74.59  ? 222 ARG A NH2 1 
ATOM   2277 N  N   . PHE A 1 223 ? -24.892 -7.777  -38.764 1.00 37.14  ? 223 PHE A N   1 
ATOM   2278 C  CA  . PHE A 1 223 ? -24.180 -8.070  -40.031 1.00 38.39  ? 223 PHE A CA  1 
ATOM   2279 C  C   . PHE A 1 223 ? -23.042 -9.053  -39.803 1.00 36.51  ? 223 PHE A C   1 
ATOM   2280 O  O   . PHE A 1 223 ? -22.645 -9.342  -38.651 1.00 34.76  ? 223 PHE A O   1 
ATOM   2281 C  CB  . PHE A 1 223 ? -23.636 -6.797  -40.677 1.00 41.54  ? 223 PHE A CB  1 
ATOM   2282 C  CG  . PHE A 1 223 ? -24.733 -5.842  -41.039 1.00 41.98  ? 223 PHE A CG  1 
ATOM   2283 C  CD1 . PHE A 1 223 ? -25.727 -6.234  -41.917 1.00 46.00  ? 223 PHE A CD1 1 
ATOM   2284 C  CD2 . PHE A 1 223 ? -24.806 -4.584  -40.466 1.00 45.61  ? 223 PHE A CD2 1 
ATOM   2285 C  CE1 . PHE A 1 223 ? -26.764 -5.372  -42.239 1.00 50.84  ? 223 PHE A CE1 1 
ATOM   2286 C  CE2 . PHE A 1 223 ? -25.850 -3.728  -40.779 1.00 50.87  ? 223 PHE A CE2 1 
ATOM   2287 C  CZ  . PHE A 1 223 ? -26.822 -4.119  -41.676 1.00 52.63  ? 223 PHE A CZ  1 
ATOM   2288 N  N   . THR A 1 224 ? -22.562 -9.557  -40.934 1.00 35.89  ? 224 THR A N   1 
ATOM   2289 C  CA  . THR A 1 224 ? -21.330 -10.358 -41.065 1.00 37.40  ? 224 THR A CA  1 
ATOM   2290 C  C   . THR A 1 224 ? -20.569 -9.803  -42.269 1.00 36.75  ? 224 THR A C   1 
ATOM   2291 O  O   . THR A 1 224 ? -21.030 -8.791  -42.858 1.00 37.47  ? 224 THR A O   1 
ATOM   2292 C  CB  . THR A 1 224 ? -21.637 -11.855 -41.175 1.00 38.65  ? 224 THR A CB  1 
ATOM   2293 O  OG1 . THR A 1 224 ? -20.380 -12.533 -41.132 1.00 38.56  ? 224 THR A OG1 1 
ATOM   2294 C  CG2 . THR A 1 224 ? -22.388 -12.236 -42.433 1.00 37.68  ? 224 THR A CG2 1 
ATOM   2295 N  N   . THR A 1 225 ? -19.443 -10.430 -42.597 1.00 35.04  ? 225 THR A N   1 
ATOM   2296 C  CA  . THR A 1 225 ? -18.544 -10.025 -43.703 1.00 32.35  ? 225 THR A CA  1 
ATOM   2297 C  C   . THR A 1 225 ? -17.771 -11.256 -44.157 1.00 28.13  ? 225 THR A C   1 
ATOM   2298 O  O   . THR A 1 225 ? -17.595 -12.140 -43.331 1.00 30.31  ? 225 THR A O   1 
ATOM   2299 C  CB  . THR A 1 225 ? -17.595 -8.903  -43.270 1.00 32.80  ? 225 THR A CB  1 
ATOM   2300 O  OG1 . THR A 1 225 ? -16.837 -8.511  -44.425 1.00 31.83  ? 225 THR A OG1 1 
ATOM   2301 C  CG2 . THR A 1 225 ? -16.686 -9.332  -42.132 1.00 31.56  ? 225 THR A CG2 1 
ATOM   2302 N  N   . THR A 1 226 ? -17.345 -11.283 -45.418 1.00 28.44  ? 226 THR A N   1 
ATOM   2303 C  CA  . THR A 1 226 ? -16.305 -12.209 -45.921 1.00 29.68  ? 226 THR A CA  1 
ATOM   2304 C  C   . THR A 1 226 ? -14.964 -11.705 -45.375 1.00 29.01  ? 226 THR A C   1 
ATOM   2305 O  O   . THR A 1 226 ? -14.841 -10.477 -45.077 1.00 25.59  ? 226 THR A O   1 
ATOM   2306 C  CB  . THR A 1 226 ? -16.300 -12.324 -47.457 1.00 31.24  ? 226 THR A CB  1 
ATOM   2307 O  OG1 . THR A 1 226 ? -15.877 -11.090 -48.033 1.00 30.50  ? 226 THR A OG1 1 
ATOM   2308 C  CG2 . THR A 1 226 ? -17.646 -12.717 -48.042 1.00 31.36  ? 226 THR A CG2 1 
ATOM   2309 N  N   . LEU A 1 227 ? -13.999 -12.613 -45.265 1.00 30.84  ? 227 LEU A N   1 
ATOM   2310 C  CA  . LEU A 1 227 ? -12.620 -12.290 -44.836 1.00 30.55  ? 227 LEU A CA  1 
ATOM   2311 C  C   . LEU A 1 227 ? -12.072 -11.265 -45.820 1.00 30.44  ? 227 LEU A C   1 
ATOM   2312 O  O   . LEU A 1 227 ? -11.504 -10.260 -45.364 1.00 32.95  ? 227 LEU A O   1 
ATOM   2313 C  CB  . LEU A 1 227 ? -11.773 -13.563 -44.801 1.00 32.89  ? 227 LEU A CB  1 
ATOM   2314 C  CG  . LEU A 1 227 ? -10.343 -13.380 -44.295 1.00 34.77  ? 227 LEU A CG  1 
ATOM   2315 C  CD1 . LEU A 1 227 ? -10.319 -12.640 -42.960 1.00 32.43  ? 227 LEU A CD1 1 
ATOM   2316 C  CD2 . LEU A 1 227 ? -9.637  -14.723 -44.175 1.00 33.65  ? 227 LEU A CD2 1 
ATOM   2317 N  N   . ASN A 1 228 ? -12.272 -11.498 -47.116 1.00 28.64  ? 228 ASN A N   1 
ATOM   2318 C  CA  . ASN A 1 228 ? -11.724 -10.615 -48.174 1.00 31.08  ? 228 ASN A CA  1 
ATOM   2319 C  C   . ASN A 1 228 ? -12.297 -9.195  -48.069 1.00 29.11  ? 228 ASN A C   1 
ATOM   2320 O  O   . ASN A 1 228 ? -11.492 -8.250  -48.101 1.00 29.35  ? 228 ASN A O   1 
ATOM   2321 C  CB  . ASN A 1 228 ? -11.971 -11.127 -49.586 1.00 35.20  ? 228 ASN A CB  1 
ATOM   2322 C  CG  . ASN A 1 228 ? -10.918 -10.555 -50.499 1.00 41.29  ? 228 ASN A CG  1 
ATOM   2323 O  OD1 . ASN A 1 228 ? -9.745  -10.894 -50.350 1.00 46.36  ? 228 ASN A OD1 1 
ATOM   2324 N  ND2 . ASN A 1 228 ? -11.307 -9.623  -51.359 1.00 44.34  ? 228 ASN A ND2 1 
ATOM   2325 N  N   . ASP A 1 229 ? -13.625 -9.041  -47.967 1.00 29.57  ? 229 ASP A N   1 
ATOM   2326 C  CA  . ASP A 1 229 ? -14.261 -7.700  -47.853 1.00 30.71  ? 229 ASP A CA  1 
ATOM   2327 C  C   . ASP A 1 229 ? -13.770 -7.021  -46.565 1.00 29.71  ? 229 ASP A C   1 
ATOM   2328 O  O   . ASP A 1 229 ? -13.627 -5.790  -46.551 1.00 26.96  ? 229 ASP A O   1 
ATOM   2329 C  CB  . ASP A 1 229 ? -15.791 -7.773  -47.889 1.00 31.23  ? 229 ASP A CB  1 
ATOM   2330 C  CG  . ASP A 1 229 ? -16.370 -8.025  -49.270 1.00 31.07  ? 229 ASP A CG  1 
ATOM   2331 O  OD1 . ASP A 1 229 ? -15.608 -7.910  -50.234 1.00 28.12  ? 229 ASP A OD1 1 
ATOM   2332 O  OD2 . ASP A 1 229 ? -17.590 -8.298  -49.354 1.00 29.59  ? 229 ASP A OD2 1 
ATOM   2333 N  N   . PHE A 1 230 ? -13.591 -7.780  -45.490 1.00 29.44  ? 230 PHE A N   1 
ATOM   2334 C  CA  . PHE A 1 230 ? -13.091 -7.201  -44.222 1.00 31.72  ? 230 PHE A CA  1 
ATOM   2335 C  C   . PHE A 1 230 ? -11.709 -6.577  -44.466 1.00 32.64  ? 230 PHE A C   1 
ATOM   2336 O  O   . PHE A 1 230 ? -11.499 -5.401  -44.087 1.00 35.85  ? 230 PHE A O   1 
ATOM   2337 C  CB  . PHE A 1 230 ? -13.044 -8.236  -43.103 1.00 32.48  ? 230 PHE A CB  1 
ATOM   2338 C  CG  . PHE A 1 230 ? -12.358 -7.660  -41.901 1.00 32.83  ? 230 PHE A CG  1 
ATOM   2339 C  CD1 . PHE A 1 230 ? -13.015 -6.750  -41.090 1.00 32.51  ? 230 PHE A CD1 1 
ATOM   2340 C  CD2 . PHE A 1 230 ? -11.028 -7.956  -41.649 1.00 32.91  ? 230 PHE A CD2 1 
ATOM   2341 C  CE1 . PHE A 1 230 ? -12.366 -6.199  -40.002 1.00 34.75  ? 230 PHE A CE1 1 
ATOM   2342 C  CE2 . PHE A 1 230 ? -10.381 -7.395  -40.566 1.00 32.31  ? 230 PHE A CE2 1 
ATOM   2343 C  CZ  . PHE A 1 230 ? -11.044 -6.504  -39.762 1.00 35.87  ? 230 PHE A CZ  1 
ATOM   2344 N  N   . ASN A 1 231 ? -10.807 -7.322  -45.116 1.00 30.31  ? 231 ASN A N   1 
ATOM   2345 C  CA  . ASN A 1 231 ? -9.401  -6.886  -45.368 1.00 30.99  ? 231 ASN A CA  1 
ATOM   2346 C  C   . ASN A 1 231 ? -9.389  -5.684  -46.316 1.00 29.91  ? 231 ASN A C   1 
ATOM   2347 O  O   . ASN A 1 231 ? -8.554  -4.788  -46.125 1.00 27.47  ? 231 ASN A O   1 
ATOM   2348 C  CB  . ASN A 1 231 ? -8.532  -8.043  -45.869 1.00 30.71  ? 231 ASN A CB  1 
ATOM   2349 C  CG  . ASN A 1 231 ? -8.109  -8.978  -44.753 1.00 34.05  ? 231 ASN A CG  1 
ATOM   2350 O  OD1 . ASN A 1 231 ? -7.797  -8.533  -43.658 1.00 39.58  ? 231 ASN A OD1 1 
ATOM   2351 N  ND2 . ASN A 1 231 ? -8.101  -10.277 -45.005 1.00 31.45  ? 231 ASN A ND2 1 
ATOM   2352 N  N   . LEU A 1 232 ? -10.282 -5.641  -47.308 1.00 29.12  ? 232 LEU A N   1 
ATOM   2353 C  CA  . LEU A 1 232 ? -10.358 -4.485  -48.245 1.00 28.31  ? 232 LEU A CA  1 
ATOM   2354 C  C   . LEU A 1 232 ? -10.759 -3.234  -47.461 1.00 27.58  ? 232 LEU A C   1 
ATOM   2355 O  O   . LEU A 1 232 ? -10.193 -2.174  -47.742 1.00 28.68  ? 232 LEU A O   1 
ATOM   2356 C  CB  . LEU A 1 232 ? -11.345 -4.782  -49.383 1.00 30.29  ? 232 LEU A CB  1 
ATOM   2357 C  CG  . LEU A 1 232 ? -10.863 -5.810  -50.408 1.00 30.94  ? 232 LEU A CG  1 
ATOM   2358 C  CD1 . LEU A 1 232 ? -12.025 -6.263  -51.299 1.00 30.97  ? 232 LEU A CD1 1 
ATOM   2359 C  CD2 . LEU A 1 232 ? -9.702  -5.248  -51.245 1.00 29.78  ? 232 LEU A CD2 1 
ATOM   2360 N  N   . VAL A 1 233 ? -11.665 -3.345  -46.481 1.00 27.13  ? 233 VAL A N   1 
ATOM   2361 C  CA  . VAL A 1 233 ? -12.067 -2.170  -45.649 1.00 29.49  ? 233 VAL A CA  1 
ATOM   2362 C  C   . VAL A 1 233 ? -10.932 -1.826  -44.672 1.00 29.48  ? 233 VAL A C   1 
ATOM   2363 O  O   . VAL A 1 233 ? -10.528 -0.643  -44.621 1.00 28.42  ? 233 VAL A O   1 
ATOM   2364 C  CB  . VAL A 1 233 ? -13.378 -2.411  -44.876 1.00 30.45  ? 233 VAL A CB  1 
ATOM   2365 C  CG1 . VAL A 1 233 ? -13.693 -1.238  -43.949 1.00 29.91  ? 233 VAL A CG1 1 
ATOM   2366 C  CG2 . VAL A 1 233 ? -14.549 -2.685  -45.810 1.00 33.37  ? 233 VAL A CG2 1 
ATOM   2367 N  N   . ALA A 1 234 ? -10.489 -2.803  -43.879 1.00 31.76  ? 234 ALA A N   1 
ATOM   2368 C  CA  . ALA A 1 234 ? -9.568  -2.584  -42.733 1.00 35.41  ? 234 ALA A CA  1 
ATOM   2369 C  C   . ALA A 1 234 ? -8.286  -1.889  -43.214 1.00 35.68  ? 234 ALA A C   1 
ATOM   2370 O  O   . ALA A 1 234 ? -7.783  -0.959  -42.541 1.00 41.22  ? 234 ALA A O   1 
ATOM   2371 C  CB  . ALA A 1 234 ? -9.248  -3.888  -42.057 1.00 35.80  ? 234 ALA A CB  1 
ATOM   2372 N  N   . MET A 1 235 ? -7.775  -2.289  -44.365 1.00 37.13  ? 235 MET A N   1 
ATOM   2373 C  CA  . MET A 1 235 ? -6.488  -1.738  -44.847 1.00 40.01  ? 235 MET A CA  1 
ATOM   2374 C  C   . MET A 1 235 ? -6.645  -0.269  -45.244 1.00 33.40  ? 235 MET A C   1 
ATOM   2375 O  O   . MET A 1 235 ? -5.643  0.431   -45.213 1.00 29.61  ? 235 MET A O   1 
ATOM   2376 C  CB  . MET A 1 235 ? -5.933  -2.612  -45.968 1.00 47.11  ? 235 MET A CB  1 
ATOM   2377 C  CG  . MET A 1 235 ? -5.531  -3.965  -45.376 1.00 56.75  ? 235 MET A CG  1 
ATOM   2378 S  SD  . MET A 1 235 ? -5.164  -5.246  -46.568 1.00 69.10  ? 235 MET A SD  1 
ATOM   2379 C  CE  . MET A 1 235 ? -3.763  -4.472  -47.379 1.00 61.05  ? 235 MET A CE  1 
ATOM   2380 N  N   . LYS A 1 236 ? -7.864  0.219   -45.461 1.00 31.57  ? 236 LYS A N   1 
ATOM   2381 C  CA  . LYS A 1 236 ? -8.096  1.659   -45.743 1.00 31.76  ? 236 LYS A CA  1 
ATOM   2382 C  C   . LYS A 1 236 ? -7.956  2.463   -44.449 1.00 30.38  ? 236 LYS A C   1 
ATOM   2383 O  O   . LYS A 1 236 ? -7.938  3.696   -44.558 1.00 29.30  ? 236 LYS A O   1 
ATOM   2384 C  CB  . LYS A 1 236 ? -9.463  1.876   -46.404 1.00 33.89  ? 236 LYS A CB  1 
ATOM   2385 C  CG  . LYS A 1 236 ? -9.652  1.074   -47.688 1.00 36.58  ? 236 LYS A CG  1 
ATOM   2386 C  CD  . LYS A 1 236 ? -11.000 1.254   -48.361 1.00 37.73  ? 236 LYS A CD  1 
ATOM   2387 C  CE  . LYS A 1 236 ? -11.079 0.488   -49.668 1.00 38.91  ? 236 LYS A CE  1 
ATOM   2388 N  NZ  . LYS A 1 236 ? -12.416 0.615   -50.283 1.00 43.58  ? 236 LYS A NZ  1 
ATOM   2389 N  N   . TYR A 1 237 ? -7.902  1.796   -43.285 1.00 29.15  ? 237 TYR A N   1 
ATOM   2390 C  CA  . TYR A 1 237 ? -7.607  2.432   -41.968 1.00 33.65  ? 237 TYR A CA  1 
ATOM   2391 C  C   . TYR A 1 237 ? -6.198  2.085   -41.456 1.00 30.89  ? 237 TYR A C   1 
ATOM   2392 O  O   . TYR A 1 237 ? -5.950  2.239   -40.247 1.00 29.73  ? 237 TYR A O   1 
ATOM   2393 C  CB  . TYR A 1 237 ? -8.682  2.044   -40.946 1.00 31.79  ? 237 TYR A CB  1 
ATOM   2394 C  CG  . TYR A 1 237 ? -10.101 2.420   -41.324 1.00 33.31  ? 237 TYR A CG  1 
ATOM   2395 C  CD1 . TYR A 1 237 ? -10.914 1.565   -42.054 1.00 33.29  ? 237 TYR A CD1 1 
ATOM   2396 C  CD2 . TYR A 1 237 ? -10.654 3.625   -40.918 1.00 34.09  ? 237 TYR A CD2 1 
ATOM   2397 C  CE1 . TYR A 1 237 ? -12.227 1.889   -42.372 1.00 34.16  ? 237 TYR A CE1 1 
ATOM   2398 C  CE2 . TYR A 1 237 ? -11.965 3.967   -41.223 1.00 35.38  ? 237 TYR A CE2 1 
ATOM   2399 C  CZ  . TYR A 1 237 ? -12.759 3.101   -41.958 1.00 36.59  ? 237 TYR A CZ  1 
ATOM   2400 O  OH  . TYR A 1 237 ? -14.054 3.449   -42.246 1.00 36.19  ? 237 TYR A OH  1 
ATOM   2401 N  N   . ASN A 1 238 ? -5.292  1.618   -42.316 1.00 32.23  ? 238 ASN A N   1 
ATOM   2402 C  CA  . ASN A 1 238 ? -3.920  1.195   -41.913 1.00 33.73  ? 238 ASN A CA  1 
ATOM   2403 C  C   . ASN A 1 238 ? -3.970  0.029   -40.917 1.00 33.21  ? 238 ASN A C   1 
ATOM   2404 O  O   . ASN A 1 238 ? -3.077  -0.056  -40.054 1.00 31.43  ? 238 ASN A O   1 
ATOM   2405 C  CB  . ASN A 1 238 ? -3.128  2.347   -41.283 1.00 38.49  ? 238 ASN A CB  1 
ATOM   2406 C  CG  . ASN A 1 238 ? -2.108  2.929   -42.231 1.00 45.60  ? 238 ASN A CG  1 
ATOM   2407 O  OD1 . ASN A 1 238 ? -2.267  2.827   -43.445 1.00 53.98  ? 238 ASN A OD1 1 
ATOM   2408 N  ND2 . ASN A 1 238 ? -1.055  3.522   -41.692 1.00 48.54  ? 238 ASN A ND2 1 
ATOM   2409 N  N   . TYR A 1 239 ? -4.946  -0.862  -41.039 1.00 28.91  ? 239 TYR A N   1 
ATOM   2410 C  CA  . TYR A 1 239 ? -5.013  -2.123  -40.257 1.00 28.49  ? 239 TYR A CA  1 
ATOM   2411 C  C   . TYR A 1 239 ? -4.237  -3.216  -40.989 1.00 30.66  ? 239 TYR A C   1 
ATOM   2412 O  O   . TYR A 1 239 ? -4.340  -3.288  -42.224 1.00 32.19  ? 239 TYR A O   1 
ATOM   2413 C  CB  . TYR A 1 239 ? -6.474  -2.529  -40.047 1.00 28.17  ? 239 TYR A CB  1 
ATOM   2414 C  CG  . TYR A 1 239 ? -7.051  -1.925  -38.802 1.00 28.14  ? 239 TYR A CG  1 
ATOM   2415 C  CD1 . TYR A 1 239 ? -7.106  -0.548  -38.620 1.00 29.04  ? 239 TYR A CD1 1 
ATOM   2416 C  CD2 . TYR A 1 239 ? -7.472  -2.744  -37.774 1.00 26.47  ? 239 TYR A CD2 1 
ATOM   2417 C  CE1 . TYR A 1 239 ? -7.582  -0.006  -37.434 1.00 29.92  ? 239 TYR A CE1 1 
ATOM   2418 C  CE2 . TYR A 1 239 ? -7.942  -2.222  -36.595 1.00 26.75  ? 239 TYR A CE2 1 
ATOM   2419 C  CZ  . TYR A 1 239 ? -7.996  -0.856  -36.426 1.00 25.88  ? 239 TYR A CZ  1 
ATOM   2420 O  OH  . TYR A 1 239 ? -8.471  -0.413  -35.241 1.00 28.47  ? 239 TYR A OH  1 
ATOM   2421 N  N   . GLU A 1 240 ? -3.535  -4.067  -40.244 1.00 30.66  ? 240 GLU A N   1 
ATOM   2422 C  CA  . GLU A 1 240 ? -2.881  -5.276  -40.790 1.00 31.85  ? 240 GLU A CA  1 
ATOM   2423 C  C   . GLU A 1 240 ? -3.942  -6.161  -41.426 1.00 33.58  ? 240 GLU A C   1 
ATOM   2424 O  O   . GLU A 1 240 ? -5.075  -6.214  -40.936 1.00 30.94  ? 240 GLU A O   1 
ATOM   2425 C  CB  . GLU A 1 240 ? -2.145  -6.078  -39.711 1.00 32.66  ? 240 GLU A CB  1 
ATOM   2426 C  CG  . GLU A 1 240 ? -0.858  -5.423  -39.272 1.00 36.69  ? 240 GLU A CG  1 
ATOM   2427 C  CD  . GLU A 1 240 ? 0.207   -5.482  -40.349 1.00 39.40  ? 240 GLU A CD  1 
ATOM   2428 O  OE1 . GLU A 1 240 ? 0.623   -6.609  -40.663 1.00 42.64  ? 240 GLU A OE1 1 
ATOM   2429 O  OE2 . GLU A 1 240 ? 0.574   -4.407  -40.900 1.00 40.08  ? 240 GLU A OE2 1 
ATOM   2430 N  N   . PRO A 1 241 ? -3.590  -6.869  -42.527 1.00 31.55  ? 241 PRO A N   1 
ATOM   2431 C  CA  . PRO A 1 241 ? -4.447  -7.910  -43.075 1.00 32.16  ? 241 PRO A CA  1 
ATOM   2432 C  C   . PRO A 1 241 ? -4.714  -8.931  -41.972 1.00 29.57  ? 241 PRO A C   1 
ATOM   2433 O  O   . PRO A 1 241 ? -3.830  -9.170  -41.147 1.00 29.48  ? 241 PRO A O   1 
ATOM   2434 C  CB  . PRO A 1 241 ? -3.643  -8.532  -44.235 1.00 31.55  ? 241 PRO A CB  1 
ATOM   2435 C  CG  . PRO A 1 241 ? -2.634  -7.456  -44.611 1.00 31.75  ? 241 PRO A CG  1 
ATOM   2436 C  CD  . PRO A 1 241 ? -2.364  -6.697  -43.325 1.00 32.68  ? 241 PRO A CD  1 
ATOM   2437 N  N   . LEU A 1 242 ? -5.934  -9.441  -41.947 1.00 26.19  ? 242 LEU A N   1 
ATOM   2438 C  CA  . LEU A 1 242 ? -6.324  -10.594 -41.107 1.00 28.35  ? 242 LEU A CA  1 
ATOM   2439 C  C   . LEU A 1 242 ? -6.243  -11.849 -41.969 1.00 29.88  ? 242 LEU A C   1 
ATOM   2440 O  O   . LEU A 1 242 ? -6.801  -11.833 -43.081 1.00 31.52  ? 242 LEU A O   1 
ATOM   2441 C  CB  . LEU A 1 242 ? -7.743  -10.402 -40.576 1.00 29.38  ? 242 LEU A CB  1 
ATOM   2442 C  CG  . LEU A 1 242 ? -8.087  -11.284 -39.379 1.00 32.17  ? 242 LEU A CG  1 
ATOM   2443 C  CD1 . LEU A 1 242 ? -7.510  -10.701 -38.084 1.00 30.37  ? 242 LEU A CD1 1 
ATOM   2444 C  CD2 . LEU A 1 242 ? -9.596  -11.478 -39.270 1.00 35.58  ? 242 LEU A CD2 1 
ATOM   2445 N  N   . THR A 1 243 ? -5.562  -12.870 -41.471 1.00 29.90  ? 243 THR A N   1 
ATOM   2446 C  CA  . THR A 1 243 ? -5.287  -14.148 -42.169 1.00 31.10  ? 243 THR A CA  1 
ATOM   2447 C  C   . THR A 1 243 ? -6.143  -15.257 -41.562 1.00 32.23  ? 243 THR A C   1 
ATOM   2448 O  O   . THR A 1 243 ? -6.671  -15.092 -40.420 1.00 31.92  ? 243 THR A O   1 
ATOM   2449 C  CB  . THR A 1 243 ? -3.808  -14.522 -42.044 1.00 32.79  ? 243 THR A CB  1 
ATOM   2450 O  OG1 . THR A 1 243 ? -3.569  -14.921 -40.692 1.00 31.01  ? 243 THR A OG1 1 
ATOM   2451 C  CG2 . THR A 1 243 ? -2.866  -13.400 -42.429 1.00 33.22  ? 243 THR A CG2 1 
ATOM   2452 N  N   . GLN A 1 244 ? -6.245  -16.374 -42.273 1.00 32.07  ? 244 GLN A N   1 
ATOM   2453 C  CA  . GLN A 1 244 ? -6.989  -17.551 -41.775 1.00 32.60  ? 244 GLN A CA  1 
ATOM   2454 C  C   . GLN A 1 244 ? -6.335  -18.012 -40.467 1.00 32.33  ? 244 GLN A C   1 
ATOM   2455 O  O   . GLN A 1 244 ? -7.063  -18.486 -39.586 1.00 35.94  ? 244 GLN A O   1 
ATOM   2456 C  CB  . GLN A 1 244 ? -7.064  -18.641 -42.847 1.00 33.40  ? 244 GLN A CB  1 
ATOM   2457 C  CG  . GLN A 1 244 ? -7.934  -19.820 -42.416 1.00 34.67  ? 244 GLN A CG  1 
ATOM   2458 C  CD  . GLN A 1 244 ? -9.306  -19.315 -42.037 1.00 34.49  ? 244 GLN A CD  1 
ATOM   2459 O  OE1 . GLN A 1 244 ? -9.898  -18.515 -42.751 1.00 39.00  ? 244 GLN A OE1 1 
ATOM   2460 N  NE2 . GLN A 1 244 ? -9.788  -19.700 -40.870 1.00 35.09  ? 244 GLN A NE2 1 
ATOM   2461 N  N   . ASP A 1 245 ? -5.013  -17.845 -40.323 1.00 33.73  ? 245 ASP A N   1 
ATOM   2462 C  CA  . ASP A 1 245 ? -4.314  -18.154 -39.052 1.00 33.71  ? 245 ASP A CA  1 
ATOM   2463 C  C   . ASP A 1 245 ? -4.934  -17.330 -37.935 1.00 31.05  ? 245 ASP A C   1 
ATOM   2464 O  O   . ASP A 1 245 ? -5.270  -17.933 -36.907 1.00 27.84  ? 245 ASP A O   1 
ATOM   2465 C  CB  . ASP A 1 245 ? -2.807  -17.908 -39.114 1.00 37.89  ? 245 ASP A CB  1 
ATOM   2466 C  CG  . ASP A 1 245 ? -2.061  -19.116 -39.643 1.00 38.23  ? 245 ASP A CG  1 
ATOM   2467 O  OD1 . ASP A 1 245 ? -2.720  -20.006 -40.169 1.00 41.34  ? 245 ASP A OD1 1 
ATOM   2468 O  OD2 . ASP A 1 245 ? -0.846  -19.171 -39.480 1.00 41.22  ? 245 ASP A OD2 1 
ATOM   2469 N  N   . HIS A 1 246 ? -5.056  -16.014 -38.137 1.00 29.45  ? 246 HIS A N   1 
ATOM   2470 C  CA  . HIS A 1 246 ? -5.680  -15.068 -37.175 1.00 29.70  ? 246 HIS A CA  1 
ATOM   2471 C  C   . HIS A 1 246 ? -7.124  -15.510 -36.874 1.00 31.08  ? 246 HIS A C   1 
ATOM   2472 O  O   . HIS A 1 246 ? -7.556  -15.425 -35.708 1.00 30.17  ? 246 HIS A O   1 
ATOM   2473 C  CB  . HIS A 1 246 ? -5.653  -13.633 -37.723 1.00 30.88  ? 246 HIS A CB  1 
ATOM   2474 C  CG  . HIS A 1 246 ? -4.278  -13.086 -37.932 1.00 28.51  ? 246 HIS A CG  1 
ATOM   2475 N  ND1 . HIS A 1 246 ? -4.001  -12.138 -38.888 1.00 26.91  ? 246 HIS A ND1 1 
ATOM   2476 C  CD2 . HIS A 1 246 ? -3.108  -13.353 -37.301 1.00 27.87  ? 246 HIS A CD2 1 
ATOM   2477 C  CE1 . HIS A 1 246 ? -2.709  -11.856 -38.844 1.00 27.05  ? 246 HIS A CE1 1 
ATOM   2478 N  NE2 . HIS A 1 246 ? -2.152  -12.570 -37.855 1.00 25.27  ? 246 HIS A NE2 1 
ATOM   2479 N  N   . VAL A 1 247 ? -7.872  -15.944 -37.890 1.00 32.50  ? 247 VAL A N   1 
ATOM   2480 C  CA  . VAL A 1 247 ? -9.268  -16.425 -37.672 1.00 32.89  ? 247 VAL A CA  1 
ATOM   2481 C  C   . VAL A 1 247 ? -9.212  -17.670 -36.769 1.00 34.32  ? 247 VAL A C   1 
ATOM   2482 O  O   . VAL A 1 247 ? -9.949  -17.700 -35.764 1.00 33.36  ? 247 VAL A O   1 
ATOM   2483 C  CB  . VAL A 1 247 ? -10.022 -16.671 -38.996 1.00 34.18  ? 247 VAL A CB  1 
ATOM   2484 C  CG1 . VAL A 1 247 ? -11.403 -17.289 -38.769 1.00 31.25  ? 247 VAL A CG1 1 
ATOM   2485 C  CG2 . VAL A 1 247 ? -10.155 -15.384 -39.803 1.00 30.95  ? 247 VAL A CG2 1 
ATOM   2486 N  N   . ASP A 1 248 ? -8.337  -18.632 -37.073 1.00 37.69  ? 248 ASP A N   1 
ATOM   2487 C  CA  . ASP A 1 248 ? -8.193  -19.889 -36.284 1.00 36.98  ? 248 ASP A CA  1 
ATOM   2488 C  C   . ASP A 1 248 ? -7.896  -19.535 -34.826 1.00 37.75  ? 248 ASP A C   1 
ATOM   2489 O  O   . ASP A 1 248 ? -8.580  -20.050 -33.915 1.00 38.70  ? 248 ASP A O   1 
ATOM   2490 C  CB  . ASP A 1 248 ? -7.101  -20.794 -36.871 1.00 38.33  ? 248 ASP A CB  1 
ATOM   2491 C  CG  . ASP A 1 248 ? -7.486  -21.390 -38.212 1.00 40.17  ? 248 ASP A CG  1 
ATOM   2492 O  OD1 . ASP A 1 248 ? -8.675  -21.306 -38.566 1.00 39.82  ? 248 ASP A OD1 1 
ATOM   2493 O  OD2 . ASP A 1 248 ? -6.593  -21.911 -38.900 1.00 41.75  ? 248 ASP A OD2 1 
ATOM   2494 N  N   . ILE A 1 249 ? -6.917  -18.654 -34.615 1.00 39.88  ? 249 ILE A N   1 
ATOM   2495 C  CA  . ILE A 1 249 ? -6.414  -18.284 -33.262 1.00 41.60  ? 249 ILE A CA  1 
ATOM   2496 C  C   . ILE A 1 249 ? -7.582  -17.757 -32.419 1.00 37.84  ? 249 ILE A C   1 
ATOM   2497 O  O   . ILE A 1 249 ? -7.572  -18.018 -31.219 1.00 35.59  ? 249 ILE A O   1 
ATOM   2498 C  CB  . ILE A 1 249 ? -5.242  -17.281 -33.374 1.00 48.49  ? 249 ILE A CB  1 
ATOM   2499 C  CG1 . ILE A 1 249 ? -3.969  -17.976 -33.886 1.00 51.52  ? 249 ILE A CG1 1 
ATOM   2500 C  CG2 . ILE A 1 249 ? -5.003  -16.566 -32.050 1.00 46.66  ? 249 ILE A CG2 1 
ATOM   2501 C  CD1 . ILE A 1 249 ? -2.814  -17.041 -34.239 1.00 50.08  ? 249 ILE A CD1 1 
ATOM   2502 N  N   . LEU A 1 250 ? -8.552  -17.046 -33.019 1.00 38.30  ? 250 LEU A N   1 
ATOM   2503 C  CA  . LEU A 1 250 ? -9.720  -16.445 -32.291 1.00 34.13  ? 250 LEU A CA  1 
ATOM   2504 C  C   . LEU A 1 250 ? -10.825 -17.484 -32.025 1.00 32.60  ? 250 LEU A C   1 
ATOM   2505 O  O   . LEU A 1 250 ? -11.749 -17.138 -31.263 1.00 37.25  ? 250 LEU A O   1 
ATOM   2506 C  CB  . LEU A 1 250 ? -10.265 -15.254 -33.089 1.00 31.76  ? 250 LEU A CB  1 
ATOM   2507 C  CG  . LEU A 1 250 ? -9.341  -14.043 -33.173 1.00 35.74  ? 250 LEU A CG  1 
ATOM   2508 C  CD1 . LEU A 1 250 ? -9.758  -13.100 -34.299 1.00 37.98  ? 250 LEU A CD1 1 
ATOM   2509 C  CD2 . LEU A 1 250 ? -9.286  -13.296 -31.846 1.00 35.48  ? 250 LEU A CD2 1 
ATOM   2510 N  N   . GLY A 1 251 ? -10.741 -18.704 -32.576 1.00 32.26  ? 251 GLY A N   1 
ATOM   2511 C  CA  . GLY A 1 251 ? -11.773 -19.760 -32.433 1.00 34.01  ? 251 GLY A CA  1 
ATOM   2512 C  C   . GLY A 1 251 ? -12.229 -19.974 -30.983 1.00 37.47  ? 251 GLY A C   1 
ATOM   2513 O  O   . GLY A 1 251 ? -13.421 -20.010 -30.691 1.00 39.81  ? 251 GLY A O   1 
ATOM   2514 N  N   . PRO A 1 252 ? -11.315 -20.213 -30.019 1.00 42.82  ? 252 PRO A N   1 
ATOM   2515 C  CA  . PRO A 1 252 ? -11.692 -20.274 -28.597 1.00 42.23  ? 252 PRO A CA  1 
ATOM   2516 C  C   . PRO A 1 252 ? -12.463 -19.062 -28.044 1.00 36.40  ? 252 PRO A C   1 
ATOM   2517 O  O   . PRO A 1 252 ? -13.392 -19.289 -27.340 1.00 36.06  ? 252 PRO A O   1 
ATOM   2518 C  CB  . PRO A 1 252 ? -10.343 -20.419 -27.875 1.00 39.88  ? 252 PRO A CB  1 
ATOM   2519 C  CG  . PRO A 1 252 ? -9.475  -21.123 -28.886 1.00 38.65  ? 252 PRO A CG  1 
ATOM   2520 C  CD  . PRO A 1 252 ? -9.907  -20.579 -30.237 1.00 39.83  ? 252 PRO A CD  1 
ATOM   2521 N  N   . LEU A 1 253 ? -12.096 -17.821 -28.373 1.00 35.19  ? 253 LEU A N   1 
ATOM   2522 C  CA  . LEU A 1 253 ? -12.839 -16.640 -27.849 1.00 34.44  ? 253 LEU A CA  1 
ATOM   2523 C  C   . LEU A 1 253 ? -14.216 -16.557 -28.535 1.00 33.86  ? 253 LEU A C   1 
ATOM   2524 O  O   . LEU A 1 253 ? -15.182 -16.095 -27.893 1.00 34.99  ? 253 LEU A O   1 
ATOM   2525 C  CB  . LEU A 1 253 ? -12.021 -15.366 -28.064 1.00 34.11  ? 253 LEU A CB  1 
ATOM   2526 C  CG  . LEU A 1 253 ? -10.803 -15.190 -27.154 1.00 34.68  ? 253 LEU A CG  1 
ATOM   2527 C  CD1 . LEU A 1 253 ? -9.897  -14.118 -27.711 1.00 32.02  ? 253 LEU A CD1 1 
ATOM   2528 C  CD2 . LEU A 1 253 ? -11.224 -14.836 -25.723 1.00 36.35  ? 253 LEU A CD2 1 
ATOM   2529 N  N   . SER A 1 254 ? -14.289 -16.958 -29.805 1.00 34.46  ? 254 SER A N   1 
ATOM   2530 C  CA  . SER A 1 254 ? -15.541 -17.098 -30.592 1.00 37.83  ? 254 SER A CA  1 
ATOM   2531 C  C   . SER A 1 254 ? -16.501 -18.065 -29.870 1.00 39.55  ? 254 SER A C   1 
ATOM   2532 O  O   . SER A 1 254 ? -17.694 -17.741 -29.719 1.00 41.32  ? 254 SER A O   1 
ATOM   2533 C  CB  . SER A 1 254 ? -15.221 -17.573 -31.981 1.00 35.37  ? 254 SER A CB  1 
ATOM   2534 O  OG  . SER A 1 254 ? -16.376 -17.559 -32.797 1.00 39.44  ? 254 SER A OG  1 
ATOM   2535 N  N   . ALA A 1 255 ? -15.986 -19.214 -29.432 1.00 41.52  ? 255 ALA A N   1 
ATOM   2536 C  CA  . ALA A 1 255 ? -16.739 -20.301 -28.763 1.00 41.08  ? 255 ALA A CA  1 
ATOM   2537 C  C   . ALA A 1 255 ? -17.243 -19.827 -27.399 1.00 39.92  ? 255 ALA A C   1 
ATOM   2538 O  O   . ALA A 1 255 ? -18.398 -20.045 -27.091 1.00 44.92  ? 255 ALA A O   1 
ATOM   2539 C  CB  . ALA A 1 255 ? -15.852 -21.516 -28.626 1.00 41.90  ? 255 ALA A CB  1 
ATOM   2540 N  N   . GLN A 1 256 ? -16.397 -19.176 -26.610 1.00 45.58  ? 256 GLN A N   1 
ATOM   2541 C  CA  . GLN A 1 256 ? -16.766 -18.702 -25.255 1.00 48.44  ? 256 GLN A CA  1 
ATOM   2542 C  C   . GLN A 1 256 ? -17.891 -17.656 -25.344 1.00 47.72  ? 256 GLN A C   1 
ATOM   2543 O  O   . GLN A 1 256 ? -18.769 -17.679 -24.480 1.00 46.03  ? 256 GLN A O   1 
ATOM   2544 C  CB  . GLN A 1 256 ? -15.530 -18.152 -24.542 1.00 52.41  ? 256 GLN A CB  1 
ATOM   2545 C  CG  . GLN A 1 256 ? -15.679 -18.133 -23.031 1.00 52.87  ? 256 GLN A CG  1 
ATOM   2546 C  CD  . GLN A 1 256 ? -14.585 -17.307 -22.416 1.00 56.28  ? 256 GLN A CD  1 
ATOM   2547 O  OE1 . GLN A 1 256 ? -13.420 -17.407 -22.799 1.00 62.32  ? 256 GLN A OE1 1 
ATOM   2548 N  NE2 . GLN A 1 256 ? -14.965 -16.454 -21.478 1.00 55.24  ? 256 GLN A NE2 1 
ATOM   2549 N  N   . THR A 1 257 ? -17.879 -16.764 -26.338 1.00 40.66  ? 257 THR A N   1 
ATOM   2550 C  CA  . THR A 1 257 ? -18.867 -15.657 -26.440 1.00 38.38  ? 257 THR A CA  1 
ATOM   2551 C  C   . THR A 1 257 ? -20.021 -16.038 -27.380 1.00 38.73  ? 257 THR A C   1 
ATOM   2552 O  O   . THR A 1 257 ? -21.040 -15.354 -27.334 1.00 39.73  ? 257 THR A O   1 
ATOM   2553 C  CB  . THR A 1 257 ? -18.209 -14.349 -26.891 1.00 37.43  ? 257 THR A CB  1 
ATOM   2554 O  OG1 . THR A 1 257 ? -17.709 -14.541 -28.218 1.00 32.23  ? 257 THR A OG1 1 
ATOM   2555 C  CG2 . THR A 1 257 ? -17.109 -13.923 -25.946 1.00 38.14  ? 257 THR A CG2 1 
ATOM   2556 N  N   . GLY A 1 258 ? -19.872 -17.080 -28.201 1.00 37.73  ? 258 GLY A N   1 
ATOM   2557 C  CA  . GLY A 1 258 ? -20.871 -17.452 -29.219 1.00 37.38  ? 258 GLY A CA  1 
ATOM   2558 C  C   . GLY A 1 258 ? -21.000 -16.424 -30.339 1.00 38.71  ? 258 GLY A C   1 
ATOM   2559 O  O   . GLY A 1 258 ? -21.983 -16.508 -31.079 1.00 39.62  ? 258 GLY A O   1 
ATOM   2560 N  N   . ILE A 1 259 ? -20.036 -15.515 -30.505 1.00 35.47  ? 259 ILE A N   1 
ATOM   2561 C  CA  . ILE A 1 259 ? -19.972 -14.583 -31.672 1.00 34.79  ? 259 ILE A CA  1 
ATOM   2562 C  C   . ILE A 1 259 ? -18.900 -15.073 -32.659 1.00 31.83  ? 259 ILE A C   1 
ATOM   2563 O  O   . ILE A 1 259 ? -17.713 -15.127 -32.273 1.00 34.42  ? 259 ILE A O   1 
ATOM   2564 C  CB  . ILE A 1 259 ? -19.691 -13.150 -31.200 1.00 33.69  ? 259 ILE A CB  1 
ATOM   2565 C  CG1 . ILE A 1 259 ? -20.793 -12.629 -30.273 1.00 35.50  ? 259 ILE A CG1 1 
ATOM   2566 C  CG2 . ILE A 1 259 ? -19.474 -12.239 -32.399 1.00 36.11  ? 259 ILE A CG2 1 
ATOM   2567 C  CD1 . ILE A 1 259 ? -20.372 -11.438 -29.411 1.00 36.88  ? 259 ILE A CD1 1 
ATOM   2568 N  N   . ALA A 1 260 ? -19.303 -15.435 -33.875 1.00 31.59  ? 260 ALA A N   1 
ATOM   2569 C  CA  . ALA A 1 260 ? -18.429 -15.920 -34.971 1.00 32.19  ? 260 ALA A CA  1 
ATOM   2570 C  C   . ALA A 1 260 ? -17.327 -14.886 -35.231 1.00 31.49  ? 260 ALA A C   1 
ATOM   2571 O  O   . ALA A 1 260 ? -17.599 -13.681 -35.096 1.00 29.16  ? 260 ALA A O   1 
ATOM   2572 C  CB  . ALA A 1 260 ? -19.245 -16.152 -36.226 1.00 33.00  ? 260 ALA A CB  1 
ATOM   2573 N  N   . VAL A 1 261 ? -16.131 -15.324 -35.626 1.00 32.80  ? 261 VAL A N   1 
ATOM   2574 C  CA  . VAL A 1 261 ? -14.991 -14.390 -35.866 1.00 32.08  ? 261 VAL A CA  1 
ATOM   2575 C  C   . VAL A 1 261 ? -15.414 -13.330 -36.895 1.00 33.47  ? 261 VAL A C   1 
ATOM   2576 O  O   . VAL A 1 261 ? -15.264 -12.117 -36.615 1.00 31.38  ? 261 VAL A O   1 
ATOM   2577 C  CB  . VAL A 1 261 ? -13.723 -15.151 -36.287 1.00 35.06  ? 261 VAL A CB  1 
ATOM   2578 C  CG1 . VAL A 1 261 ? -12.637 -14.210 -36.783 1.00 34.04  ? 261 VAL A CG1 1 
ATOM   2579 C  CG2 . VAL A 1 261 ? -13.201 -16.035 -35.157 1.00 35.86  ? 261 VAL A CG2 1 
ATOM   2580 N  N   . LEU A 1 262 ? -15.996 -13.742 -38.023 1.00 33.57  ? 262 LEU A N   1 
ATOM   2581 C  CA  . LEU A 1 262 ? -16.387 -12.778 -39.085 1.00 30.37  ? 262 LEU A CA  1 
ATOM   2582 C  C   . LEU A 1 262 ? -17.554 -11.890 -38.644 1.00 30.58  ? 262 LEU A C   1 
ATOM   2583 O  O   . LEU A 1 262 ? -17.654 -10.784 -39.199 1.00 32.93  ? 262 LEU A O   1 
ATOM   2584 C  CB  . LEU A 1 262 ? -16.727 -13.543 -40.360 1.00 32.76  ? 262 LEU A CB  1 
ATOM   2585 C  CG  . LEU A 1 262 ? -15.554 -14.242 -41.033 1.00 34.97  ? 262 LEU A CG  1 
ATOM   2586 C  CD1 . LEU A 1 262 ? -16.042 -15.047 -42.235 1.00 36.08  ? 262 LEU A CD1 1 
ATOM   2587 C  CD2 . LEU A 1 262 ? -14.479 -13.246 -41.458 1.00 34.98  ? 262 LEU A CD2 1 
ATOM   2588 N  N   . ASP A 1 263 ? -18.389 -12.297 -37.674 1.00 28.84  ? 263 ASP A N   1 
ATOM   2589 C  CA  . ASP A 1 263 ? -19.412 -11.381 -37.107 1.00 30.55  ? 263 ASP A CA  1 
ATOM   2590 C  C   . ASP A 1 263 ? -18.668 -10.270 -36.359 1.00 27.61  ? 263 ASP A C   1 
ATOM   2591 O  O   . ASP A 1 263 ? -19.023 -9.089  -36.500 1.00 26.28  ? 263 ASP A O   1 
ATOM   2592 C  CB  . ASP A 1 263 ? -20.462 -12.106 -36.246 1.00 35.96  ? 263 ASP A CB  1 
ATOM   2593 C  CG  . ASP A 1 263 ? -21.450 -12.945 -37.054 1.00 40.11  ? 263 ASP A CG  1 
ATOM   2594 O  OD1 . ASP A 1 263 ? -21.475 -12.799 -38.291 1.00 45.98  ? 263 ASP A OD1 1 
ATOM   2595 O  OD2 . ASP A 1 263 ? -22.175 -13.763 -36.449 1.00 45.45  ? 263 ASP A OD2 1 
ATOM   2596 N  N   . MET A 1 264 ? -17.680 -10.629 -35.549 1.00 30.31  ? 264 MET A N   1 
ATOM   2597 C  CA  . MET A 1 264 ? -16.903 -9.615  -34.803 1.00 30.00  ? 264 MET A CA  1 
ATOM   2598 C  C   . MET A 1 264 ? -16.166 -8.724  -35.815 1.00 30.24  ? 264 MET A C   1 
ATOM   2599 O  O   . MET A 1 264 ? -15.967 -7.540  -35.498 1.00 29.00  ? 264 MET A O   1 
ATOM   2600 C  CB  . MET A 1 264 ? -15.926 -10.255 -33.815 1.00 29.72  ? 264 MET A CB  1 
ATOM   2601 C  CG  . MET A 1 264 ? -15.336 -9.254  -32.851 1.00 30.03  ? 264 MET A CG  1 
ATOM   2602 S  SD  . MET A 1 264 ? -16.547 -8.487  -31.718 1.00 29.94  ? 264 MET A SD  1 
ATOM   2603 C  CE  . MET A 1 264 ? -16.699 -9.748  -30.453 1.00 30.91  ? 264 MET A CE  1 
ATOM   2604 N  N   . CYS A 1 265 ? -15.760 -9.254  -36.976 1.00 29.09  ? 265 CYS A N   1 
ATOM   2605 C  CA  . CYS A 1 265 ? -15.076 -8.451  -38.026 1.00 27.83  ? 265 CYS A CA  1 
ATOM   2606 C  C   . CYS A 1 265 ? -16.025 -7.348  -38.515 1.00 29.71  ? 265 CYS A C   1 
ATOM   2607 O  O   . CYS A 1 265 ? -15.568 -6.168  -38.683 1.00 26.21  ? 265 CYS A O   1 
ATOM   2608 C  CB  . CYS A 1 265 ? -14.561 -9.335  -39.150 1.00 27.21  ? 265 CYS A CB  1 
ATOM   2609 S  SG  . CYS A 1 265 ? -13.140 -10.347 -38.656 1.00 26.82  ? 265 CYS A SG  1 
ATOM   2610 N  N   . ALA A 1 266 ? -17.320 -7.684  -38.655 1.00 28.50  ? 266 ALA A N   1 
ATOM   2611 C  CA  . ALA A 1 266 ? -18.374 -6.727  -39.054 1.00 29.33  ? 266 ALA A CA  1 
ATOM   2612 C  C   . ALA A 1 266 ? -18.494 -5.631  -37.983 1.00 30.34  ? 266 ALA A C   1 
ATOM   2613 O  O   . ALA A 1 266 ? -18.582 -4.444  -38.335 1.00 28.81  ? 266 ALA A O   1 
ATOM   2614 C  CB  . ALA A 1 266 ? -19.682 -7.447  -39.273 1.00 32.07  ? 266 ALA A CB  1 
ATOM   2615 N  N   . SER A 1 267 ? -18.451 -6.000  -36.705 1.00 31.63  ? 267 SER A N   1 
ATOM   2616 C  CA  . SER A 1 267 ? -18.501 -5.021  -35.590 1.00 31.40  ? 267 SER A CA  1 
ATOM   2617 C  C   . SER A 1 267 ? -17.320 -4.062  -35.717 1.00 28.75  ? 267 SER A C   1 
ATOM   2618 O  O   . SER A 1 267 ? -17.510 -2.849  -35.627 1.00 29.47  ? 267 SER A O   1 
ATOM   2619 C  CB  . SER A 1 267 ? -18.530 -5.694  -34.239 1.00 34.49  ? 267 SER A CB  1 
ATOM   2620 O  OG  . SER A 1 267 ? -18.561 -4.702  -33.218 1.00 39.19  ? 267 SER A OG  1 
ATOM   2621 N  N   . LEU A 1 268 ? -16.120 -4.589  -35.929 1.00 32.20  ? 268 LEU A N   1 
ATOM   2622 C  CA  . LEU A 1 268 ? -14.912 -3.740  -36.094 1.00 28.54  ? 268 LEU A CA  1 
ATOM   2623 C  C   . LEU A 1 268 ? -15.097 -2.797  -37.294 1.00 27.69  ? 268 LEU A C   1 
ATOM   2624 O  O   . LEU A 1 268 ? -14.761 -1.595  -37.154 1.00 27.29  ? 268 LEU A O   1 
ATOM   2625 C  CB  . LEU A 1 268 ? -13.675 -4.631  -36.218 1.00 27.57  ? 268 LEU A CB  1 
ATOM   2626 C  CG  . LEU A 1 268 ? -12.360 -3.881  -36.421 1.00 27.65  ? 268 LEU A CG  1 
ATOM   2627 C  CD1 . LEU A 1 268 ? -12.249 -2.657  -35.520 1.00 27.37  ? 268 LEU A CD1 1 
ATOM   2628 C  CD2 . LEU A 1 268 ? -11.182 -4.811  -36.190 1.00 28.20  ? 268 LEU A CD2 1 
ATOM   2629 N  N   . LYS A 1 269 ? -15.585 -3.288  -38.438 1.00 28.49  ? 269 LYS A N   1 
ATOM   2630 C  CA  . LYS A 1 269 ? -15.751 -2.442  -39.646 1.00 29.05  ? 269 LYS A CA  1 
ATOM   2631 C  C   . LYS A 1 269 ? -16.597 -1.219  -39.313 1.00 29.62  ? 269 LYS A C   1 
ATOM   2632 O  O   . LYS A 1 269 ? -16.217 -0.075  -39.701 1.00 27.33  ? 269 LYS A O   1 
ATOM   2633 C  CB  . LYS A 1 269 ? -16.415 -3.197  -40.791 1.00 35.91  ? 269 LYS A CB  1 
ATOM   2634 C  CG  . LYS A 1 269 ? -15.477 -4.129  -41.530 1.00 43.10  ? 269 LYS A CG  1 
ATOM   2635 C  CD  . LYS A 1 269 ? -16.201 -5.216  -42.319 1.00 48.40  ? 269 LYS A CD  1 
ATOM   2636 C  CE  . LYS A 1 269 ? -16.988 -4.677  -43.494 1.00 46.72  ? 269 LYS A CE  1 
ATOM   2637 N  NZ  . LYS A 1 269 ? -17.388 -5.794  -44.378 1.00 47.10  ? 269 LYS A NZ  1 
ATOM   2638 N  N   . GLU A 1 270 ? -17.715 -1.461  -38.624 1.00 30.97  ? 270 GLU A N   1 
ATOM   2639 C  CA  . GLU A 1 270 ? -18.675 -0.405  -38.202 1.00 32.33  ? 270 GLU A CA  1 
ATOM   2640 C  C   . GLU A 1 270 ? -17.981 0.542   -37.215 1.00 29.88  ? 270 GLU A C   1 
ATOM   2641 O  O   . GLU A 1 270 ? -18.097 1.754   -37.392 1.00 29.44  ? 270 GLU A O   1 
ATOM   2642 C  CB  . GLU A 1 270 ? -19.934 -1.058  -37.621 1.00 31.71  ? 270 GLU A CB  1 
ATOM   2643 C  CG  . GLU A 1 270 ? -20.896 -0.057  -37.012 1.00 36.74  ? 270 GLU A CG  1 
ATOM   2644 C  CD  . GLU A 1 270 ? -22.308 -0.612  -36.870 1.00 36.28  ? 270 GLU A CD  1 
ATOM   2645 O  OE1 . GLU A 1 270 ? -22.989 -0.763  -37.898 1.00 37.09  ? 270 GLU A OE1 1 
ATOM   2646 O  OE2 . GLU A 1 270 ? -22.686 -0.957  -35.753 1.00 41.09  ? 270 GLU A OE2 1 
ATOM   2647 N  N   . LEU A 1 271 ? -17.244 0.012   -36.236 1.00 29.58  ? 271 LEU A N   1 
ATOM   2648 C  CA  . LEU A 1 271 ? -16.518 0.845   -35.238 1.00 29.86  ? 271 LEU A CA  1 
ATOM   2649 C  C   . LEU A 1 271 ? -15.565 1.785   -35.963 1.00 29.07  ? 271 LEU A C   1 
ATOM   2650 O  O   . LEU A 1 271 ? -15.477 2.938   -35.553 1.00 30.44  ? 271 LEU A O   1 
ATOM   2651 C  CB  . LEU A 1 271 ? -15.755 -0.049  -34.259 1.00 30.72  ? 271 LEU A CB  1 
ATOM   2652 C  CG  . LEU A 1 271 ? -16.562 -0.511  -33.049 1.00 29.12  ? 271 LEU A CG  1 
ATOM   2653 C  CD1 . LEU A 1 271 ? -15.851 -1.632  -32.293 1.00 27.18  ? 271 LEU A CD1 1 
ATOM   2654 C  CD2 . LEU A 1 271 ? -16.839 0.668   -32.141 1.00 30.99  ? 271 LEU A CD2 1 
ATOM   2655 N  N   . LEU A 1 272 ? -14.903 1.301   -37.016 1.00 30.43  ? 272 LEU A N   1 
ATOM   2656 C  CA  . LEU A 1 272 ? -13.918 2.100   -37.789 1.00 29.54  ? 272 LEU A CA  1 
ATOM   2657 C  C   . LEU A 1 272 ? -14.663 3.218   -38.498 1.00 30.12  ? 272 LEU A C   1 
ATOM   2658 O  O   . LEU A 1 272 ? -14.099 4.318   -38.613 1.00 27.55  ? 272 LEU A O   1 
ATOM   2659 C  CB  . LEU A 1 272 ? -13.160 1.198   -38.767 1.00 28.83  ? 272 LEU A CB  1 
ATOM   2660 C  CG  . LEU A 1 272 ? -12.103 0.343   -38.078 1.00 29.74  ? 272 LEU A CG  1 
ATOM   2661 C  CD1 . LEU A 1 272 ? -11.530 -0.724  -38.983 1.00 30.31  ? 272 LEU A CD1 1 
ATOM   2662 C  CD2 . LEU A 1 272 ? -11.003 1.236   -37.543 1.00 31.87  ? 272 LEU A CD2 1 
ATOM   2663 N  N   . GLN A 1 273 ? -15.873 2.916   -38.966 1.00 28.22  ? 273 GLN A N   1 
ATOM   2664 C  CA  . GLN A 1 273 ? -16.732 3.834   -39.752 1.00 28.67  ? 273 GLN A CA  1 
ATOM   2665 C  C   . GLN A 1 273 ? -17.339 4.916   -38.847 1.00 29.07  ? 273 GLN A C   1 
ATOM   2666 O  O   . GLN A 1 273 ? -17.464 6.073   -39.297 1.00 28.41  ? 273 GLN A O   1 
ATOM   2667 C  CB  . GLN A 1 273 ? -17.809 2.987   -40.432 1.00 29.99  ? 273 GLN A CB  1 
ATOM   2668 C  CG  . GLN A 1 273 ? -18.957 3.775   -41.029 1.00 31.57  ? 273 GLN A CG  1 
ATOM   2669 C  CD  . GLN A 1 273 ? -20.031 2.794   -41.439 1.00 33.60  ? 273 GLN A CD  1 
ATOM   2670 O  OE1 . GLN A 1 273 ? -19.910 2.106   -42.447 1.00 36.75  ? 273 GLN A OE1 1 
ATOM   2671 N  NE2 . GLN A 1 273 ? -21.044 2.649   -40.606 1.00 30.05  ? 273 GLN A NE2 1 
ATOM   2672 N  N   . ASN A 1 274 ? -17.699 4.555   -37.617 1.00 30.63  ? 274 ASN A N   1 
ATOM   2673 C  CA  . ASN A 1 274 ? -18.590 5.349   -36.735 1.00 32.98  ? 274 ASN A CA  1 
ATOM   2674 C  C   . ASN A 1 274 ? -17.791 6.034   -35.620 1.00 34.10  ? 274 ASN A C   1 
ATOM   2675 O  O   . ASN A 1 274 ? -18.249 7.077   -35.149 1.00 34.21  ? 274 ASN A O   1 
ATOM   2676 C  CB  . ASN A 1 274 ? -19.686 4.458   -36.135 1.00 32.30  ? 274 ASN A CB  1 
ATOM   2677 C  CG  . ASN A 1 274 ? -20.678 3.954   -37.165 1.00 33.31  ? 274 ASN A CG  1 
ATOM   2678 O  OD1 . ASN A 1 274 ? -20.644 4.376   -38.320 1.00 28.83  ? 274 ASN A OD1 1 
ATOM   2679 N  ND2 . ASN A 1 274 ? -21.569 3.061   -36.747 1.00 30.50  ? 274 ASN A ND2 1 
ATOM   2680 N  N   . GLY A 1 275 ? -16.670 5.468   -35.183 1.00 33.66  ? 275 GLY A N   1 
ATOM   2681 C  CA  . GLY A 1 275 ? -16.077 5.831   -33.877 1.00 36.61  ? 275 GLY A CA  1 
ATOM   2682 C  C   . GLY A 1 275 ? -16.948 5.312   -32.738 1.00 36.52  ? 275 GLY A C   1 
ATOM   2683 O  O   . GLY A 1 275 ? -17.760 4.399   -32.979 1.00 35.07  ? 275 GLY A O   1 
ATOM   2684 N  N   . MET A 1 276 ? -16.798 5.844   -31.532 1.00 36.24  ? 276 MET A N   1 
ATOM   2685 C  CA  . MET A 1 276 ? -17.449 5.260   -30.328 1.00 40.72  ? 276 MET A CA  1 
ATOM   2686 C  C   . MET A 1 276 ? -18.662 6.079   -29.896 1.00 45.10  ? 276 MET A C   1 
ATOM   2687 O  O   . MET A 1 276 ? -19.447 5.562   -29.056 1.00 48.28  ? 276 MET A O   1 
ATOM   2688 C  CB  . MET A 1 276 ? -16.445 5.157   -29.180 1.00 40.42  ? 276 MET A CB  1 
ATOM   2689 C  CG  . MET A 1 276 ? -15.417 4.090   -29.469 1.00 41.08  ? 276 MET A CG  1 
ATOM   2690 S  SD  . MET A 1 276 ? -14.563 3.574   -28.002 1.00 48.03  ? 276 MET A SD  1 
ATOM   2691 C  CE  . MET A 1 276 ? -13.279 2.605   -28.792 1.00 43.09  ? 276 MET A CE  1 
ATOM   2692 N  N   . ASN A 1 277 ? -18.829 7.281   -30.452 1.00 47.42  ? 277 ASN A N   1 
ATOM   2693 C  CA  . ASN A 1 277 ? -20.025 8.114   -30.182 1.00 50.65  ? 277 ASN A CA  1 
ATOM   2694 C  C   . ASN A 1 277 ? -20.037 8.397   -28.676 1.00 47.36  ? 277 ASN A C   1 
ATOM   2695 O  O   . ASN A 1 277 ? -20.991 7.989   -28.002 1.00 41.55  ? 277 ASN A O   1 
ATOM   2696 C  CB  . ASN A 1 277 ? -21.277 7.384   -30.671 1.00 57.29  ? 277 ASN A CB  1 
ATOM   2697 C  CG  . ASN A 1 277 ? -22.483 8.284   -30.834 1.00 68.37  ? 277 ASN A CG  1 
ATOM   2698 O  OD1 . ASN A 1 277 ? -22.351 9.507   -30.913 1.00 73.35  ? 277 ASN A OD1 1 
ATOM   2699 N  ND2 . ASN A 1 277 ? -23.660 7.677   -30.909 1.00 67.57  ? 277 ASN A ND2 1 
ATOM   2700 N  N   . GLY A 1 278 ? -18.950 8.986   -28.171 1.00 44.16  ? 278 GLY A N   1 
ATOM   2701 C  CA  . GLY A 1 278 ? -18.784 9.352   -26.756 1.00 41.85  ? 278 GLY A CA  1 
ATOM   2702 C  C   . GLY A 1 278 ? -18.803 8.149   -25.824 1.00 41.23  ? 278 GLY A C   1 
ATOM   2703 O  O   . GLY A 1 278 ? -18.878 8.372   -24.621 1.00 42.65  ? 278 GLY A O   1 
ATOM   2704 N  N   . ARG A 1 279 ? -18.713 6.914   -26.320 1.00 40.11  ? 279 ARG A N   1 
ATOM   2705 C  CA  . ARG A 1 279 ? -18.623 5.718   -25.442 1.00 42.12  ? 279 ARG A CA  1 
ATOM   2706 C  C   . ARG A 1 279 ? -17.151 5.322   -25.297 1.00 39.45  ? 279 ARG A C   1 
ATOM   2707 O  O   . ARG A 1 279 ? -16.300 5.985   -25.902 1.00 40.08  ? 279 ARG A O   1 
ATOM   2708 C  CB  . ARG A 1 279 ? -19.488 4.568   -25.961 1.00 45.26  ? 279 ARG A CB  1 
ATOM   2709 C  CG  . ARG A 1 279 ? -20.973 4.799   -25.728 1.00 51.94  ? 279 ARG A CG  1 
ATOM   2710 C  CD  . ARG A 1 279 ? -21.830 3.715   -26.323 1.00 54.20  ? 279 ARG A CD  1 
ATOM   2711 N  NE  . ARG A 1 279 ? -22.022 4.008   -27.728 1.00 59.92  ? 279 ARG A NE  1 
ATOM   2712 C  CZ  . ARG A 1 279 ? -23.156 3.825   -28.393 1.00 65.90  ? 279 ARG A CZ  1 
ATOM   2713 N  NH1 . ARG A 1 279 ? -24.226 3.352   -27.771 1.00 68.21  ? 279 ARG A NH1 1 
ATOM   2714 N  NH2 . ARG A 1 279 ? -23.216 4.132   -29.679 1.00 65.32  ? 279 ARG A NH2 1 
ATOM   2715 N  N   . THR A 1 280 ? -16.886 4.344   -24.432 1.00 38.65  ? 280 THR A N   1 
ATOM   2716 C  CA  . THR A 1 280 ? -15.554 3.758   -24.150 1.00 39.72  ? 280 THR A CA  1 
ATOM   2717 C  C   . THR A 1 280 ? -15.738 2.243   -24.115 1.00 36.58  ? 280 THR A C   1 
ATOM   2718 O  O   . THR A 1 280 ? -16.850 1.810   -23.843 1.00 38.60  ? 280 THR A O   1 
ATOM   2719 C  CB  . THR A 1 280 ? -14.940 4.313   -22.853 1.00 40.20  ? 280 THR A CB  1 
ATOM   2720 O  OG1 . THR A 1 280 ? -15.755 3.905   -21.758 1.00 37.97  ? 280 THR A OG1 1 
ATOM   2721 C  CG2 . THR A 1 280 ? -14.812 5.822   -22.831 1.00 39.45  ? 280 THR A CG2 1 
ATOM   2722 N  N   . ILE A 1 281 ? -14.708 1.501   -24.502 1.00 38.14  ? 281 ILE A N   1 
ATOM   2723 C  CA  . ILE A 1 281 ? -14.618 0.021   -24.367 1.00 34.96  ? 281 ILE A CA  1 
ATOM   2724 C  C   . ILE A 1 281 ? -13.446 -0.272  -23.442 1.00 33.35  ? 281 ILE A C   1 
ATOM   2725 O  O   . ILE A 1 281 ? -12.339 0.243   -23.710 1.00 31.92  ? 281 ILE A O   1 
ATOM   2726 C  CB  . ILE A 1 281 ? -14.443 -0.653  -25.738 1.00 34.27  ? 281 ILE A CB  1 
ATOM   2727 C  CG1 . ILE A 1 281 ? -15.624 -0.346  -26.653 1.00 31.64  ? 281 ILE A CG1 1 
ATOM   2728 C  CG2 . ILE A 1 281 ? -14.235 -2.148  -25.573 1.00 36.90  ? 281 ILE A CG2 1 
ATOM   2729 C  CD1 . ILE A 1 281 ? -15.413 -0.778  -28.062 1.00 31.88  ? 281 ILE A CD1 1 
ATOM   2730 N  N   . LEU A 1 282 ? -13.711 -1.021  -22.376 1.00 35.59  ? 282 LEU A N   1 
ATOM   2731 C  CA  . LEU A 1 282 ? -12.742 -1.334  -21.303 1.00 35.20  ? 282 LEU A CA  1 
ATOM   2732 C  C   . LEU A 1 282 ? -11.909 -0.089  -20.971 1.00 36.74  ? 282 LEU A C   1 
ATOM   2733 O  O   . LEU A 1 282 ? -10.678 -0.187  -20.913 1.00 36.18  ? 282 LEU A O   1 
ATOM   2734 C  CB  . LEU A 1 282 ? -11.900 -2.504  -21.813 1.00 34.39  ? 282 LEU A CB  1 
ATOM   2735 C  CG  . LEU A 1 282 ? -12.713 -3.743  -22.194 1.00 33.67  ? 282 LEU A CG  1 
ATOM   2736 C  CD1 . LEU A 1 282 ? -11.849 -4.763  -22.906 1.00 31.65  ? 282 LEU A CD1 1 
ATOM   2737 C  CD2 . LEU A 1 282 ? -13.345 -4.374  -20.964 1.00 34.74  ? 282 LEU A CD2 1 
ATOM   2738 N  N   . GLY A 1 283 ? -12.554 1.068   -20.822 1.00 40.09  ? 283 GLY A N   1 
ATOM   2739 C  CA  . GLY A 1 283 ? -11.891 2.302   -20.357 1.00 39.51  ? 283 GLY A CA  1 
ATOM   2740 C  C   . GLY A 1 283 ? -11.059 2.990   -21.426 1.00 41.55  ? 283 GLY A C   1 
ATOM   2741 O  O   . GLY A 1 283 ? -10.414 3.984   -21.092 1.00 42.10  ? 283 GLY A O   1 
ATOM   2742 N  N   . SER A 1 284 ? -11.077 2.523   -22.677 1.00 40.28  ? 284 SER A N   1 
ATOM   2743 C  CA  . SER A 1 284 ? -10.416 3.223   -23.810 1.00 36.42  ? 284 SER A CA  1 
ATOM   2744 C  C   . SER A 1 284 ? -11.455 3.856   -24.736 1.00 35.07  ? 284 SER A C   1 
ATOM   2745 O  O   . SER A 1 284 ? -12.491 3.208   -24.988 1.00 36.32  ? 284 SER A O   1 
ATOM   2746 C  CB  . SER A 1 284 ? -9.515  2.311   -24.566 1.00 35.63  ? 284 SER A CB  1 
ATOM   2747 O  OG  . SER A 1 284 ? -8.701  3.071   -25.454 1.00 41.35  ? 284 SER A OG  1 
ATOM   2748 N  N   . ALA A 1 285 ? -11.166 5.059   -25.246 1.00 34.74  ? 285 ALA A N   1 
ATOM   2749 C  CA  . ALA A 1 285 ? -11.913 5.716   -26.347 1.00 34.14  ? 285 ALA A CA  1 
ATOM   2750 C  C   . ALA A 1 285 ? -11.232 5.451   -27.698 1.00 35.47  ? 285 ALA A C   1 
ATOM   2751 O  O   . ALA A 1 285 ? -11.733 5.984   -28.703 1.00 36.14  ? 285 ALA A O   1 
ATOM   2752 C  CB  . ALA A 1 285 ? -12.034 7.198   -26.076 1.00 35.53  ? 285 ALA A CB  1 
ATOM   2753 N  N   . LEU A 1 286 ? -10.133 4.681   -27.720 1.00 35.02  ? 286 LEU A N   1 
ATOM   2754 C  CA  . LEU A 1 286 ? -9.487  4.160   -28.962 1.00 35.01  ? 286 LEU A CA  1 
ATOM   2755 C  C   . LEU A 1 286 ? -9.617  2.637   -29.013 1.00 32.31  ? 286 LEU A C   1 
ATOM   2756 O  O   . LEU A 1 286 ? -9.791  2.018   -27.947 1.00 31.07  ? 286 LEU A O   1 
ATOM   2757 C  CB  . LEU A 1 286 ? -8.001  4.514   -28.960 1.00 40.52  ? 286 LEU A CB  1 
ATOM   2758 C  CG  . LEU A 1 286 ? -7.664  5.979   -29.181 1.00 43.70  ? 286 LEU A CG  1 
ATOM   2759 C  CD1 . LEU A 1 286 ? -6.170  6.122   -29.355 1.00 43.74  ? 286 LEU A CD1 1 
ATOM   2760 C  CD2 . LEU A 1 286 ? -8.416  6.560   -30.376 1.00 46.02  ? 286 LEU A CD2 1 
ATOM   2761 N  N   . LEU A 1 287 ? -9.422  2.044   -30.190 1.00 29.58  ? 287 LEU A N   1 
ATOM   2762 C  CA  . LEU A 1 287 ? -9.378  0.566   -30.346 1.00 30.71  ? 287 LEU A CA  1 
ATOM   2763 C  C   . LEU A 1 287 ? -7.985  0.036   -29.955 1.00 31.09  ? 287 LEU A C   1 
ATOM   2764 O  O   . LEU A 1 287 ? -7.007  0.338   -30.642 1.00 33.60  ? 287 LEU A O   1 
ATOM   2765 C  CB  . LEU A 1 287 ? -9.762  0.217   -31.786 1.00 30.60  ? 287 LEU A CB  1 
ATOM   2766 C  CG  . LEU A 1 287 ? -11.127 0.768   -32.224 1.00 30.71  ? 287 LEU A CG  1 
ATOM   2767 C  CD1 . LEU A 1 287 ? -11.392 0.505   -33.698 1.00 31.44  ? 287 LEU A CD1 1 
ATOM   2768 C  CD2 . LEU A 1 287 ? -12.244 0.189   -31.372 1.00 31.34  ? 287 LEU A CD2 1 
ATOM   2769 N  N   . GLU A 1 288 ? -7.913  -0.760  -28.895 1.00 32.39  ? 288 GLU A N   1 
ATOM   2770 C  CA  . GLU A 1 288 ? -6.642  -1.239  -28.291 1.00 33.70  ? 288 GLU A CA  1 
ATOM   2771 C  C   . GLU A 1 288 ? -6.120  -2.432  -29.088 1.00 29.54  ? 288 GLU A C   1 
ATOM   2772 O  O   . GLU A 1 288 ? -6.910  -3.352  -29.349 1.00 29.16  ? 288 GLU A O   1 
ATOM   2773 C  CB  . GLU A 1 288 ? -6.856  -1.618  -26.826 1.00 37.80  ? 288 GLU A CB  1 
ATOM   2774 C  CG  . GLU A 1 288 ? -6.822  -0.417  -25.906 1.00 49.55  ? 288 GLU A CG  1 
ATOM   2775 C  CD  . GLU A 1 288 ? -5.507  0.345   -25.983 1.00 53.79  ? 288 GLU A CD  1 
ATOM   2776 O  OE1 . GLU A 1 288 ? -4.433  -0.330  -25.986 1.00 55.65  ? 288 GLU A OE1 1 
ATOM   2777 O  OE2 . GLU A 1 288 ? -5.574  1.597   -26.101 1.00 53.48  ? 288 GLU A OE2 1 
ATOM   2778 N  N   . ASP A 1 289 ? -4.822  -2.451  -29.381 1.00 28.53  ? 289 ASP A N   1 
ATOM   2779 C  CA  . ASP A 1 289 ? -4.197  -3.520  -30.210 1.00 29.17  ? 289 ASP A CA  1 
ATOM   2780 C  C   . ASP A 1 289 ? -2.969  -4.156  -29.532 1.00 26.55  ? 289 ASP A C   1 
ATOM   2781 O  O   . ASP A 1 289 ? -2.245  -4.882  -30.254 1.00 24.41  ? 289 ASP A O   1 
ATOM   2782 C  CB  . ASP A 1 289 ? -3.873  -2.992  -31.618 1.00 28.51  ? 289 ASP A CB  1 
ATOM   2783 C  CG  . ASP A 1 289 ? -2.628  -2.120  -31.726 1.00 28.00  ? 289 ASP A CG  1 
ATOM   2784 O  OD1 . ASP A 1 289 ? -2.166  -1.583  -30.694 1.00 24.00  ? 289 ASP A OD1 1 
ATOM   2785 O  OD2 . ASP A 1 289 ? -2.156  -1.961  -32.850 1.00 24.31  ? 289 ASP A OD2 1 
ATOM   2786 N  N   . GLU A 1 290 ? -2.731  -3.935  -28.229 1.00 24.86  ? 290 GLU A N   1 
ATOM   2787 C  CA  . GLU A 1 290 ? -1.544  -4.518  -27.544 1.00 26.10  ? 290 GLU A CA  1 
ATOM   2788 C  C   . GLU A 1 290 ? -1.972  -5.611  -26.550 1.00 27.01  ? 290 GLU A C   1 
ATOM   2789 O  O   . GLU A 1 290 ? -1.196  -5.907  -25.637 1.00 29.95  ? 290 GLU A O   1 
ATOM   2790 C  CB  . GLU A 1 290 ? -0.653  -3.412  -26.968 1.00 26.55  ? 290 GLU A CB  1 
ATOM   2791 C  CG  . GLU A 1 290 ? -0.085  -2.520  -28.064 1.00 27.22  ? 290 GLU A CG  1 
ATOM   2792 C  CD  . GLU A 1 290 ? 1.258   -1.824  -27.828 1.00 29.42  ? 290 GLU A CD  1 
ATOM   2793 O  OE1 . GLU A 1 290 ? 1.751   -1.832  -26.684 1.00 26.43  ? 290 GLU A OE1 1 
ATOM   2794 O  OE2 . GLU A 1 290 ? 1.826   -1.276  -28.818 1.00 29.12  ? 290 GLU A OE2 1 
ATOM   2795 N  N   . PHE A 1 291 ? -3.117  -6.260  -26.774 1.00 27.45  ? 291 PHE A N   1 
ATOM   2796 C  CA  . PHE A 1 291 ? -3.529  -7.532  -26.116 1.00 27.87  ? 291 PHE A CA  1 
ATOM   2797 C  C   . PHE A 1 291 ? -3.714  -8.611  -27.184 1.00 27.58  ? 291 PHE A C   1 
ATOM   2798 O  O   . PHE A 1 291 ? -4.553  -8.413  -28.056 1.00 29.38  ? 291 PHE A O   1 
ATOM   2799 C  CB  . PHE A 1 291 ? -4.855  -7.394  -25.366 1.00 28.59  ? 291 PHE A CB  1 
ATOM   2800 C  CG  . PHE A 1 291 ? -4.879  -6.359  -24.273 1.00 30.02  ? 291 PHE A CG  1 
ATOM   2801 C  CD1 . PHE A 1 291 ? -5.290  -5.064  -24.539 1.00 31.57  ? 291 PHE A CD1 1 
ATOM   2802 C  CD2 . PHE A 1 291 ? -4.514  -6.682  -22.975 1.00 30.62  ? 291 PHE A CD2 1 
ATOM   2803 C  CE1 . PHE A 1 291 ? -5.325  -4.106  -23.534 1.00 32.86  ? 291 PHE A CE1 1 
ATOM   2804 C  CE2 . PHE A 1 291 ? -4.552  -5.724  -21.967 1.00 34.24  ? 291 PHE A CE2 1 
ATOM   2805 C  CZ  . PHE A 1 291 ? -4.948  -4.434  -22.250 1.00 34.77  ? 291 PHE A CZ  1 
ATOM   2806 N  N   . THR A 1 292 ? -2.989  -9.721  -27.087 1.00 28.91  ? 292 THR A N   1 
ATOM   2807 C  CA  . THR A 1 292 ? -3.145  -10.906 -27.972 1.00 29.85  ? 292 THR A CA  1 
ATOM   2808 C  C   . THR A 1 292 ? -4.332  -11.765 -27.515 1.00 31.40  ? 292 THR A C   1 
ATOM   2809 O  O   . THR A 1 292 ? -4.808  -11.645 -26.383 1.00 28.50  ? 292 THR A O   1 
ATOM   2810 C  CB  . THR A 1 292 ? -1.872  -11.748 -27.997 1.00 27.36  ? 292 THR A CB  1 
ATOM   2811 O  OG1 . THR A 1 292 ? -1.758  -12.371 -26.729 1.00 27.05  ? 292 THR A OG1 1 
ATOM   2812 C  CG2 . THR A 1 292 ? -0.624  -10.942 -28.274 1.00 30.79  ? 292 THR A CG2 1 
ATOM   2813 N  N   . PRO A 1 293 ? -4.876  -12.627 -28.408 1.00 30.01  ? 293 PRO A N   1 
ATOM   2814 C  CA  . PRO A 1 293 ? -5.846  -13.650 -28.011 1.00 30.13  ? 293 PRO A CA  1 
ATOM   2815 C  C   . PRO A 1 293 ? -5.405  -14.441 -26.777 1.00 30.28  ? 293 PRO A C   1 
ATOM   2816 O  O   . PRO A 1 293 ? -6.240  -14.754 -25.962 1.00 29.88  ? 293 PRO A O   1 
ATOM   2817 C  CB  . PRO A 1 293 ? -5.891  -14.542 -29.251 1.00 28.84  ? 293 PRO A CB  1 
ATOM   2818 C  CG  . PRO A 1 293 ? -5.741  -13.529 -30.380 1.00 31.05  ? 293 PRO A CG  1 
ATOM   2819 C  CD  . PRO A 1 293 ? -4.691  -12.572 -29.869 1.00 30.07  ? 293 PRO A CD  1 
ATOM   2820 N  N   . PHE A 1 294 ? -4.119  -14.775 -26.690 1.00 29.95  ? 294 PHE A N   1 
ATOM   2821 C  CA  . PHE A 1 294 ? -3.579  -15.553 -25.554 1.00 31.93  ? 294 PHE A CA  1 
ATOM   2822 C  C   . PHE A 1 294 ? -3.688  -14.697 -24.283 1.00 30.73  ? 294 PHE A C   1 
ATOM   2823 O  O   . PHE A 1 294 ? -4.201  -15.200 -23.296 1.00 29.28  ? 294 PHE A O   1 
ATOM   2824 C  CB  . PHE A 1 294 ? -2.177  -16.065 -25.856 1.00 35.55  ? 294 PHE A CB  1 
ATOM   2825 C  CG  . PHE A 1 294 ? -1.563  -16.881 -24.737 1.00 44.21  ? 294 PHE A CG  1 
ATOM   2826 C  CD1 . PHE A 1 294 ? -1.037  -16.264 -23.605 1.00 48.20  ? 294 PHE A CD1 1 
ATOM   2827 C  CD2 . PHE A 1 294 ? -1.469  -18.263 -24.824 1.00 48.48  ? 294 PHE A CD2 1 
ATOM   2828 C  CE1 . PHE A 1 294 ? -0.463  -17.007 -22.580 1.00 51.50  ? 294 PHE A CE1 1 
ATOM   2829 C  CE2 . PHE A 1 294 ? -0.877  -19.004 -23.809 1.00 52.40  ? 294 PHE A CE2 1 
ATOM   2830 C  CZ  . PHE A 1 294 ? -0.382  -18.378 -22.687 1.00 53.01  ? 294 PHE A CZ  1 
ATOM   2831 N  N   . ASP A 1 295 ? -3.282  -13.428 -24.332 1.00 30.57  ? 295 ASP A N   1 
ATOM   2832 C  CA  . ASP A 1 295 ? -3.390  -12.469 -23.198 1.00 30.09  ? 295 ASP A CA  1 
ATOM   2833 C  C   . ASP A 1 295 ? -4.842  -12.399 -22.692 1.00 32.67  ? 295 ASP A C   1 
ATOM   2834 O  O   . ASP A 1 295 ? -5.022  -12.362 -21.458 1.00 30.86  ? 295 ASP A O   1 
ATOM   2835 C  CB  . ASP A 1 295 ? -2.967  -11.061 -23.615 1.00 29.67  ? 295 ASP A CB  1 
ATOM   2836 C  CG  . ASP A 1 295 ? -1.497  -10.879 -23.929 1.00 28.06  ? 295 ASP A CG  1 
ATOM   2837 O  OD1 . ASP A 1 295 ? -0.720  -11.778 -23.603 1.00 27.57  ? 295 ASP A OD1 1 
ATOM   2838 O  OD2 . ASP A 1 295 ? -1.151  -9.821  -24.515 1.00 27.07  ? 295 ASP A OD2 1 
ATOM   2839 N  N   . VAL A 1 296 ? -5.838  -12.350 -23.592 1.00 32.39  ? 296 VAL A N   1 
ATOM   2840 C  CA  . VAL A 1 296 ? -7.270  -12.139 -23.212 1.00 31.32  ? 296 VAL A CA  1 
ATOM   2841 C  C   . VAL A 1 296 ? -7.724  -13.369 -22.430 1.00 33.36  ? 296 VAL A C   1 
ATOM   2842 O  O   . VAL A 1 296 ? -8.310  -13.197 -21.342 1.00 33.78  ? 296 VAL A O   1 
ATOM   2843 C  CB  . VAL A 1 296 ? -8.177  -11.839 -24.424 1.00 31.48  ? 296 VAL A CB  1 
ATOM   2844 C  CG1 . VAL A 1 296 ? -9.658  -11.944 -24.111 1.00 30.42  ? 296 VAL A CG1 1 
ATOM   2845 C  CG2 . VAL A 1 296 ? -7.899  -10.458 -24.988 1.00 32.72  ? 296 VAL A CG2 1 
ATOM   2846 N  N   . VAL A 1 297 ? -7.426  -14.566 -22.931 1.00 34.68  ? 297 VAL A N   1 
ATOM   2847 C  CA  . VAL A 1 297 ? -7.758  -15.842 -22.234 1.00 35.41  ? 297 VAL A CA  1 
ATOM   2848 C  C   . VAL A 1 297 ? -7.006  -15.943 -20.898 1.00 37.86  ? 297 VAL A C   1 
ATOM   2849 O  O   . VAL A 1 297 ? -7.636  -16.354 -19.906 1.00 38.47  ? 297 VAL A O   1 
ATOM   2850 C  CB  . VAL A 1 297 ? -7.488  -17.056 -23.132 1.00 38.11  ? 297 VAL A CB  1 
ATOM   2851 C  CG1 . VAL A 1 297 ? -7.641  -18.353 -22.358 1.00 39.38  ? 297 VAL A CG1 1 
ATOM   2852 C  CG2 . VAL A 1 297 ? -8.389  -17.052 -24.356 1.00 35.94  ? 297 VAL A CG2 1 
ATOM   2853 N  N   . ARG A 1 298 ? -5.719  -15.586 -20.833 1.00 39.09  ? 298 ARG A N   1 
ATOM   2854 C  CA  . ARG A 1 298 ? -4.942  -15.609 -19.553 1.00 38.54  ? 298 ARG A CA  1 
ATOM   2855 C  C   . ARG A 1 298 ? -5.669  -14.720 -18.533 1.00 39.19  ? 298 ARG A C   1 
ATOM   2856 O  O   . ARG A 1 298 ? -5.877  -15.151 -17.392 1.00 38.88  ? 298 ARG A O   1 
ATOM   2857 C  CB  . ARG A 1 298 ? -3.484  -15.190 -19.795 1.00 40.18  ? 298 ARG A CB  1 
ATOM   2858 C  CG  . ARG A 1 298 ? -2.634  -14.869 -18.563 1.00 47.65  ? 298 ARG A CG  1 
ATOM   2859 C  CD  . ARG A 1 298 ? -1.402  -14.020 -18.931 1.00 52.26  ? 298 ARG A CD  1 
ATOM   2860 N  NE  . ARG A 1 298 ? -0.707  -13.323 -17.835 1.00 50.63  ? 298 ARG A NE  1 
ATOM   2861 C  CZ  . ARG A 1 298 ? -0.181  -12.079 -17.883 1.00 47.62  ? 298 ARG A CZ  1 
ATOM   2862 N  NH1 . ARG A 1 298 ? -0.270  -11.322 -18.965 1.00 38.76  ? 298 ARG A NH1 1 
ATOM   2863 N  NH2 . ARG A 1 298 ? 0.437   -11.589 -16.814 1.00 49.29  ? 298 ARG A NH2 1 
ATOM   2864 N  N   . GLN A 1 299 ? -6.050  -13.507 -18.927 1.00 38.28  ? 299 GLN A N   1 
ATOM   2865 C  CA  . GLN A 1 299 ? -6.503  -12.479 -17.958 1.00 39.89  ? 299 GLN A CA  1 
ATOM   2866 C  C   . GLN A 1 299 ? -7.990  -12.701 -17.622 1.00 39.84  ? 299 GLN A C   1 
ATOM   2867 O  O   . GLN A 1 299 ? -8.343  -12.465 -16.458 1.00 42.86  ? 299 GLN A O   1 
ATOM   2868 C  CB  . GLN A 1 299 ? -6.191  -11.066 -18.468 1.00 37.34  ? 299 GLN A CB  1 
ATOM   2869 C  CG  . GLN A 1 299 ? -6.611  -10.011 -17.460 1.00 36.14  ? 299 GLN A CG  1 
ATOM   2870 C  CD  . GLN A 1 299 ? -6.329  -8.571  -17.788 1.00 33.79  ? 299 GLN A CD  1 
ATOM   2871 O  OE1 . GLN A 1 299 ? -6.846  -7.688  -17.124 1.00 34.72  ? 299 GLN A OE1 1 
ATOM   2872 N  NE2 . GLN A 1 299 ? -5.550  -8.304  -18.820 1.00 36.10  ? 299 GLN A NE2 1 
ATOM   2873 N  N   . CYS A 1 300 ? -8.821  -13.160 -18.568 1.00 41.50  ? 300 CYS A N   1 
ATOM   2874 C  CA  . CYS A 1 300 ? -10.309 -13.279 -18.420 1.00 43.65  ? 300 CYS A CA  1 
ATOM   2875 C  C   . CYS A 1 300 ? -10.716 -14.636 -17.824 1.00 51.49  ? 300 CYS A C   1 
ATOM   2876 O  O   . CYS A 1 300 ? -11.832 -14.735 -17.287 1.00 60.79  ? 300 CYS A O   1 
ATOM   2877 C  CB  . CYS A 1 300 ? -11.017 -13.069 -19.753 1.00 41.06  ? 300 CYS A CB  1 
ATOM   2878 S  SG  . CYS A 1 300 ? -10.944 -11.340 -20.282 1.00 41.87  ? 300 CYS A SG  1 
ATOM   2879 N  N   . SER A 1 301 ? -9.847  -15.641 -17.922 1.00 55.44  ? 301 SER A N   1 
ATOM   2880 C  CA  . SER A 1 301 ? -10.053 -17.016 -17.399 1.00 57.52  ? 301 SER A CA  1 
ATOM   2881 C  C   . SER A 1 301 ? -8.753  -17.488 -16.738 1.00 53.43  ? 301 SER A C   1 
ATOM   2882 O  O   . SER A 1 301 ? -8.854  -18.260 -15.807 1.00 54.62  ? 301 SER A O   1 
ATOM   2883 C  CB  . SER A 1 301 ? -10.485 -17.963 -18.498 1.00 58.59  ? 301 SER A CB  1 
ATOM   2884 O  OG  . SER A 1 301 ? -9.368  -18.374 -19.287 1.00 63.74  ? 301 SER A OG  1 
ATOM   2885 N  N   . SER B 1 1   ? 12.963  8.470   -24.401 1.00 36.05  ? 1   SER B N   1 
ATOM   2886 C  CA  . SER B 1 1   ? 11.565  8.960   -24.271 1.00 34.06  ? 1   SER B CA  1 
ATOM   2887 C  C   . SER B 1 1   ? 10.569  7.801   -24.405 1.00 32.06  ? 1   SER B C   1 
ATOM   2888 O  O   . SER B 1 1   ? 10.970  6.621   -24.405 1.00 31.50  ? 1   SER B O   1 
ATOM   2889 C  CB  . SER B 1 1   ? 11.289  10.079  -25.251 1.00 35.77  ? 1   SER B CB  1 
ATOM   2890 O  OG  . SER B 1 1   ? 11.417  9.629   -26.580 1.00 35.59  ? 1   SER B OG  1 
ATOM   2891 N  N   . GLY B 1 2   ? 9.287   8.141   -24.420 1.00 32.57  ? 2   GLY B N   1 
ATOM   2892 C  CA  . GLY B 1 2   ? 8.174   7.201   -24.267 1.00 32.07  ? 2   GLY B CA  1 
ATOM   2893 C  C   . GLY B 1 2   ? 7.522   7.425   -22.912 1.00 35.14  ? 2   GLY B C   1 
ATOM   2894 O  O   . GLY B 1 2   ? 8.203   7.902   -21.981 1.00 33.43  ? 2   GLY B O   1 
ATOM   2895 N  N   . PHE B 1 3   ? 6.255   7.060   -22.783 1.00 32.60  ? 3   PHE B N   1 
ATOM   2896 C  CA  . PHE B 1 3   ? 5.523   7.185   -21.509 1.00 32.81  ? 3   PHE B CA  1 
ATOM   2897 C  C   . PHE B 1 3   ? 4.492   6.066   -21.409 1.00 32.02  ? 3   PHE B C   1 
ATOM   2898 O  O   . PHE B 1 3   ? 3.595   5.983   -22.234 1.00 34.49  ? 3   PHE B O   1 
ATOM   2899 C  CB  . PHE B 1 3   ? 4.869   8.561   -21.375 1.00 33.39  ? 3   PHE B CB  1 
ATOM   2900 C  CG  . PHE B 1 3   ? 4.531   8.864   -19.944 1.00 31.68  ? 3   PHE B CG  1 
ATOM   2901 C  CD1 . PHE B 1 3   ? 5.537   9.139   -19.038 1.00 30.00  ? 3   PHE B CD1 1 
ATOM   2902 C  CD2 . PHE B 1 3   ? 3.231   8.752   -19.494 1.00 30.18  ? 3   PHE B CD2 1 
ATOM   2903 C  CE1 . PHE B 1 3   ? 5.238   9.388   -17.709 1.00 31.81  ? 3   PHE B CE1 1 
ATOM   2904 C  CE2 . PHE B 1 3   ? 2.927   8.991   -18.169 1.00 31.85  ? 3   PHE B CE2 1 
ATOM   2905 C  CZ  . PHE B 1 3   ? 3.933   9.306   -17.275 1.00 34.06  ? 3   PHE B CZ  1 
ATOM   2906 N  N   . ARG B 1 4   ? 4.637   5.229   -20.395 1.00 29.95  ? 4   ARG B N   1 
ATOM   2907 C  CA  . ARG B 1 4   ? 3.817   4.017   -20.219 1.00 30.39  ? 4   ARG B CA  1 
ATOM   2908 C  C   . ARG B 1 4   ? 3.294   3.971   -18.788 1.00 29.88  ? 4   ARG B C   1 
ATOM   2909 O  O   . ARG B 1 4   ? 3.942   4.525   -17.882 1.00 28.71  ? 4   ARG B O   1 
ATOM   2910 C  CB  . ARG B 1 4   ? 4.681   2.792   -20.510 1.00 31.32  ? 4   ARG B CB  1 
ATOM   2911 C  CG  . ARG B 1 4   ? 4.835   2.519   -21.991 1.00 35.29  ? 4   ARG B CG  1 
ATOM   2912 C  CD  . ARG B 1 4   ? 3.773   1.521   -22.421 1.00 36.52  ? 4   ARG B CD  1 
ATOM   2913 N  NE  . ARG B 1 4   ? 3.959   1.186   -23.826 1.00 40.68  ? 4   ARG B NE  1 
ATOM   2914 C  CZ  . ARG B 1 4   ? 3.121   0.461   -24.549 1.00 42.64  ? 4   ARG B CZ  1 
ATOM   2915 N  NH1 . ARG B 1 4   ? 2.031   -0.044  -23.989 1.00 46.94  ? 4   ARG B NH1 1 
ATOM   2916 N  NH2 . ARG B 1 4   ? 3.383   0.220   -25.822 1.00 36.36  ? 4   ARG B NH2 1 
ATOM   2917 N  N   . LYS B 1 5   ? 2.154   3.322   -18.621 1.00 30.27  ? 5   LYS B N   1 
ATOM   2918 C  CA  . LYS B 1 5   ? 1.628   2.889   -17.314 1.00 32.71  ? 5   LYS B CA  1 
ATOM   2919 C  C   . LYS B 1 5   ? 2.588   1.844   -16.751 1.00 31.87  ? 5   LYS B C   1 
ATOM   2920 O  O   . LYS B 1 5   ? 2.716   0.751   -17.339 1.00 27.27  ? 5   LYS B O   1 
ATOM   2921 C  CB  . LYS B 1 5   ? 0.224   2.315   -17.469 1.00 34.96  ? 5   LYS B CB  1 
ATOM   2922 C  CG  . LYS B 1 5   ? -0.473  2.059   -16.148 1.00 39.53  ? 5   LYS B CG  1 
ATOM   2923 C  CD  . LYS B 1 5   ? -1.905  2.447   -16.196 1.00 43.48  ? 5   LYS B CD  1 
ATOM   2924 C  CE  . LYS B 1 5   ? -2.065  3.951   -16.122 1.00 48.58  ? 5   LYS B CE  1 
ATOM   2925 N  NZ  . LYS B 1 5   ? -3.493  4.326   -16.165 1.00 52.58  ? 5   LYS B NZ  1 
ATOM   2926 N  N   . MET B 1 6   ? 3.256   2.184   -15.658 1.00 30.72  ? 6   MET B N   1 
ATOM   2927 C  CA  . MET B 1 6   ? 4.467   1.443   -15.244 1.00 29.93  ? 6   MET B CA  1 
ATOM   2928 C  C   . MET B 1 6   ? 4.284   1.036   -13.790 1.00 26.76  ? 6   MET B C   1 
ATOM   2929 O  O   . MET B 1 6   ? 4.049   1.912   -12.985 1.00 24.61  ? 6   MET B O   1 
ATOM   2930 C  CB  . MET B 1 6   ? 5.686   2.345   -15.435 1.00 32.18  ? 6   MET B CB  1 
ATOM   2931 C  CG  . MET B 1 6   ? 6.996   1.693   -15.165 1.00 36.00  ? 6   MET B CG  1 
ATOM   2932 S  SD  . MET B 1 6   ? 8.340   2.880   -15.432 1.00 40.12  ? 6   MET B SD  1 
ATOM   2933 C  CE  . MET B 1 6   ? 8.487   2.832   -17.215 1.00 39.49  ? 6   MET B CE  1 
ATOM   2934 N  N   . ALA B 1 7   ? 4.372   -0.252  -13.488 1.00 25.08  ? 7   ALA B N   1 
ATOM   2935 C  CA  . ALA B 1 7   ? 4.268   -0.774  -12.111 1.00 24.09  ? 7   ALA B CA  1 
ATOM   2936 C  C   . ALA B 1 7   ? 5.657   -0.702  -11.490 1.00 25.37  ? 7   ALA B C   1 
ATOM   2937 O  O   . ALA B 1 7   ? 6.628   -0.660  -12.244 1.00 27.07  ? 7   ALA B O   1 
ATOM   2938 C  CB  . ALA B 1 7   ? 3.728   -2.178  -12.145 1.00 24.11  ? 7   ALA B CB  1 
ATOM   2939 N  N   . PHE B 1 8   ? 5.771   -0.711  -10.168 1.00 26.50  ? 8   PHE B N   1 
ATOM   2940 C  CA  . PHE B 1 8   ? 7.077   -0.950  -9.513  1.00 24.40  ? 8   PHE B CA  1 
ATOM   2941 C  C   . PHE B 1 8   ? 7.498   -2.383  -9.815  1.00 24.71  ? 8   PHE B C   1 
ATOM   2942 O  O   . PHE B 1 8   ? 6.662   -3.261  -10.023 1.00 23.04  ? 8   PHE B O   1 
ATOM   2943 C  CB  . PHE B 1 8   ? 6.988   -0.755  -8.007  1.00 27.02  ? 8   PHE B CB  1 
ATOM   2944 C  CG  . PHE B 1 8   ? 6.826   0.678   -7.595  1.00 26.72  ? 8   PHE B CG  1 
ATOM   2945 C  CD1 . PHE B 1 8   ? 7.929   1.508   -7.497  1.00 28.82  ? 8   PHE B CD1 1 
ATOM   2946 C  CD2 . PHE B 1 8   ? 5.574   1.194   -7.336  1.00 29.47  ? 8   PHE B CD2 1 
ATOM   2947 C  CE1 . PHE B 1 8   ? 7.779   2.832   -7.119  1.00 30.82  ? 8   PHE B CE1 1 
ATOM   2948 C  CE2 . PHE B 1 8   ? 5.419   2.525   -6.975  1.00 30.75  ? 8   PHE B CE2 1 
ATOM   2949 C  CZ  . PHE B 1 8   ? 6.518   3.332   -6.852  1.00 31.05  ? 8   PHE B CZ  1 
ATOM   2950 N  N   . PRO B 1 9   ? 8.811   -2.674  -9.797  1.00 25.85  ? 9   PRO B N   1 
ATOM   2951 C  CA  . PRO B 1 9   ? 9.287   -4.052  -9.911  1.00 26.61  ? 9   PRO B CA  1 
ATOM   2952 C  C   . PRO B 1 9   ? 8.682   -4.782  -8.699  1.00 28.97  ? 9   PRO B C   1 
ATOM   2953 O  O   . PRO B 1 9   ? 8.658   -4.168  -7.641  1.00 31.52  ? 9   PRO B O   1 
ATOM   2954 C  CB  . PRO B 1 9   ? 10.812  -3.959  -9.778  1.00 26.92  ? 9   PRO B CB  1 
ATOM   2955 C  CG  . PRO B 1 9   ? 11.121  -2.466  -9.918  1.00 27.93  ? 9   PRO B CG  1 
ATOM   2956 C  CD  . PRO B 1 9   ? 9.878   -1.726  -9.469  1.00 26.69  ? 9   PRO B CD  1 
ATOM   2957 N  N   . SER B 1 10  ? 8.203   -6.012  -8.874  1.00 26.62  ? 10  SER B N   1 
ATOM   2958 C  CA  . SER B 1 10  ? 7.376   -6.748  -7.876  1.00 28.75  ? 10  SER B CA  1 
ATOM   2959 C  C   . SER B 1 10  ? 8.172   -7.820  -7.109  1.00 27.80  ? 10  SER B C   1 
ATOM   2960 O  O   . SER B 1 10  ? 7.591   -8.432  -6.204  1.00 26.03  ? 10  SER B O   1 
ATOM   2961 C  CB  . SER B 1 10  ? 6.172   -7.353  -8.546  1.00 28.07  ? 10  SER B CB  1 
ATOM   2962 O  OG  . SER B 1 10  ? 6.546   -8.212  -9.616  1.00 28.03  ? 10  SER B OG  1 
ATOM   2963 N  N   . GLY B 1 11  ? 9.451   -8.041  -7.425  1.00 29.28  ? 11  GLY B N   1 
ATOM   2964 C  CA  . GLY B 1 11  ? 10.282  -9.103  -6.819  1.00 29.24  ? 11  GLY B CA  1 
ATOM   2965 C  C   . GLY B 1 11  ? 10.198  -9.124  -5.295  1.00 30.18  ? 11  GLY B C   1 
ATOM   2966 O  O   . GLY B 1 11  ? 9.957   -10.197 -4.723  1.00 34.75  ? 11  GLY B O   1 
ATOM   2967 N  N   . LYS B 1 12  ? 10.415  -7.989  -4.643  1.00 29.40  ? 12  LYS B N   1 
ATOM   2968 C  CA  . LYS B 1 12  ? 10.419  -7.897  -3.157  1.00 29.49  ? 12  LYS B CA  1 
ATOM   2969 C  C   . LYS B 1 12  ? 9.094   -8.423  -2.601  1.00 28.98  ? 12  LYS B C   1 
ATOM   2970 O  O   . LYS B 1 12  ? 9.102   -8.981  -1.520  1.00 30.50  ? 12  LYS B O   1 
ATOM   2971 C  CB  . LYS B 1 12  ? 10.671  -6.459  -2.707  1.00 31.79  ? 12  LYS B CB  1 
ATOM   2972 C  CG  . LYS B 1 12  ? 12.120  -5.997  -2.827  1.00 34.37  ? 12  LYS B CG  1 
ATOM   2973 C  CD  . LYS B 1 12  ? 12.303  -4.521  -2.451  1.00 40.60  ? 12  LYS B CD  1 
ATOM   2974 C  CE  . LYS B 1 12  ? 13.743  -4.105  -2.184  1.00 43.08  ? 12  LYS B CE  1 
ATOM   2975 N  NZ  . LYS B 1 12  ? 14.670  -4.721  -3.155  1.00 47.25  ? 12  LYS B NZ  1 
ATOM   2976 N  N   . VAL B 1 13  ? 7.993   -8.270  -3.334  1.00 28.04  ? 13  VAL B N   1 
ATOM   2977 C  CA  . VAL B 1 13  ? 6.643   -8.645  -2.848  1.00 28.35  ? 13  VAL B CA  1 
ATOM   2978 C  C   . VAL B 1 13  ? 6.340   -10.103 -3.219  1.00 28.66  ? 13  VAL B C   1 
ATOM   2979 O  O   . VAL B 1 13  ? 5.704   -10.770 -2.385  1.00 26.14  ? 13  VAL B O   1 
ATOM   2980 C  CB  . VAL B 1 13  ? 5.582   -7.662  -3.359  1.00 27.39  ? 13  VAL B CB  1 
ATOM   2981 C  CG1 . VAL B 1 13  ? 4.193   -8.074  -2.888  1.00 29.16  ? 13  VAL B CG1 1 
ATOM   2982 C  CG2 . VAL B 1 13  ? 5.920   -6.245  -2.916  1.00 28.12  ? 13  VAL B CG2 1 
ATOM   2983 N  N   . GLU B 1 14  ? 6.784   -10.580 -4.391  1.00 26.95  ? 14  GLU B N   1 
ATOM   2984 C  CA  . GLU B 1 14  ? 6.601   -11.987 -4.855  1.00 28.87  ? 14  GLU B CA  1 
ATOM   2985 C  C   . GLU B 1 14  ? 7.098   -12.963 -3.771  1.00 30.45  ? 14  GLU B C   1 
ATOM   2986 O  O   . GLU B 1 14  ? 6.396   -13.957 -3.496  1.00 30.19  ? 14  GLU B O   1 
ATOM   2987 C  CB  . GLU B 1 14  ? 7.351   -12.227 -6.171  1.00 29.87  ? 14  GLU B CB  1 
ATOM   2988 C  CG  . GLU B 1 14  ? 6.723   -11.531 -7.361  1.00 29.43  ? 14  GLU B CG  1 
ATOM   2989 C  CD  . GLU B 1 14  ? 7.609   -11.555 -8.590  1.00 29.68  ? 14  GLU B CD  1 
ATOM   2990 O  OE1 . GLU B 1 14  ? 8.019   -12.662 -8.966  1.00 27.67  ? 14  GLU B OE1 1 
ATOM   2991 O  OE2 . GLU B 1 14  ? 7.879   -10.469 -9.172  1.00 28.16  ? 14  GLU B OE2 1 
ATOM   2992 N  N   . GLY B 1 15  ? 8.244   -12.673 -3.151  1.00 29.94  ? 15  GLY B N   1 
ATOM   2993 C  CA  . GLY B 1 15  ? 8.821   -13.489 -2.065  1.00 31.78  ? 15  GLY B CA  1 
ATOM   2994 C  C   . GLY B 1 15  ? 8.026   -13.437 -0.760  1.00 32.03  ? 15  GLY B C   1 
ATOM   2995 O  O   . GLY B 1 15  ? 8.468   -14.064 0.200   1.00 29.48  ? 15  GLY B O   1 
ATOM   2996 N  N   . CYS B 1 16  ? 6.885   -12.743 -0.703  1.00 30.69  ? 16  CYS B N   1 
ATOM   2997 C  CA  . CYS B 1 16  ? 6.053   -12.664 0.526   1.00 30.11  ? 16  CYS B CA  1 
ATOM   2998 C  C   . CYS B 1 16  ? 4.700   -13.348 0.356   1.00 26.71  ? 16  CYS B C   1 
ATOM   2999 O  O   . CYS B 1 16  ? 3.946   -13.422 1.336   1.00 26.85  ? 16  CYS B O   1 
ATOM   3000 C  CB  . CYS B 1 16  ? 5.807   -11.214 0.908   1.00 28.72  ? 16  CYS B CB  1 
ATOM   3001 S  SG  . CYS B 1 16  ? 7.333   -10.339 1.315   1.00 31.54  ? 16  CYS B SG  1 
ATOM   3002 N  N   . MET B 1 17  ? 4.360   -13.809 -0.837  1.00 28.79  ? 17  MET B N   1 
ATOM   3003 C  CA  . MET B 1 17  ? 2.986   -14.296 -1.099  1.00 26.94  ? 17  MET B CA  1 
ATOM   3004 C  C   . MET B 1 17  ? 2.920   -15.777 -0.741  1.00 28.79  ? 17  MET B C   1 
ATOM   3005 O  O   . MET B 1 17  ? 3.810   -16.515 -1.131  1.00 29.28  ? 17  MET B O   1 
ATOM   3006 C  CB  . MET B 1 17  ? 2.594   -14.112 -2.565  1.00 29.45  ? 17  MET B CB  1 
ATOM   3007 C  CG  . MET B 1 17  ? 2.646   -12.682 -3.032  1.00 27.09  ? 17  MET B CG  1 
ATOM   3008 S  SD  . MET B 1 17  ? 1.746   -11.554 -1.942  1.00 26.40  ? 17  MET B SD  1 
ATOM   3009 C  CE  . MET B 1 17  ? 0.085   -12.239 -2.003  1.00 24.44  ? 17  MET B CE  1 
ATOM   3010 N  N   . VAL B 1 18  ? 1.872   -16.169 -0.035  1.00 29.78  ? 18  VAL B N   1 
ATOM   3011 C  CA  . VAL B 1 18  ? 1.606   -17.578 0.337   1.00 30.11  ? 18  VAL B CA  1 
ATOM   3012 C  C   . VAL B 1 18  ? 0.155   -17.900 0.021   1.00 29.61  ? 18  VAL B C   1 
ATOM   3013 O  O   . VAL B 1 18  ? -0.658  -16.982 -0.225  1.00 29.82  ? 18  VAL B O   1 
ATOM   3014 C  CB  . VAL B 1 18  ? 1.955   -17.841 1.820   1.00 30.24  ? 18  VAL B CB  1 
ATOM   3015 C  CG1 . VAL B 1 18  ? 3.429   -17.596 2.077   1.00 30.19  ? 18  VAL B CG1 1 
ATOM   3016 C  CG2 . VAL B 1 18  ? 1.103   -17.024 2.779   1.00 31.04  ? 18  VAL B CG2 1 
ATOM   3017 N  N   . GLN B 1 19  ? -0.157  -19.187 0.086   1.00 36.69  ? 19  GLN B N   1 
ATOM   3018 C  CA  . GLN B 1 19  ? -1.531  -19.717 -0.018  1.00 35.73  ? 19  GLN B CA  1 
ATOM   3019 C  C   . GLN B 1 19  ? -2.080  -19.912 1.389   1.00 35.40  ? 19  GLN B C   1 
ATOM   3020 O  O   . GLN B 1 19  ? -1.345  -20.439 2.248   1.00 35.89  ? 19  GLN B O   1 
ATOM   3021 C  CB  . GLN B 1 19  ? -1.524  -21.037 -0.774  1.00 41.39  ? 19  GLN B CB  1 
ATOM   3022 C  CG  . GLN B 1 19  ? -2.921  -21.600 -0.952  1.00 44.67  ? 19  GLN B CG  1 
ATOM   3023 C  CD  . GLN B 1 19  ? -2.879  -22.875 -1.745  1.00 47.59  ? 19  GLN B CD  1 
ATOM   3024 O  OE1 . GLN B 1 19  ? -3.553  -23.005 -2.770  1.00 53.04  ? 19  GLN B OE1 1 
ATOM   3025 N  NE2 . GLN B 1 19  ? -2.065  -23.810 -1.278  1.00 45.94  ? 19  GLN B NE2 1 
ATOM   3026 N  N   . VAL B 1 20  ? -3.326  -19.498 1.603   1.00 36.30  ? 20  VAL B N   1 
ATOM   3027 C  CA  . VAL B 1 20  ? -4.049  -19.673 2.892   1.00 37.99  ? 20  VAL B CA  1 
ATOM   3028 C  C   . VAL B 1 20  ? -5.355  -20.406 2.582   1.00 39.38  ? 20  VAL B C   1 
ATOM   3029 O  O   . VAL B 1 20  ? -6.110  -19.949 1.710   1.00 40.59  ? 20  VAL B O   1 
ATOM   3030 C  CB  . VAL B 1 20  ? -4.296  -18.321 3.589   1.00 39.24  ? 20  VAL B CB  1 
ATOM   3031 C  CG1 . VAL B 1 20  ? -5.113  -18.469 4.862   1.00 39.29  ? 20  VAL B CG1 1 
ATOM   3032 C  CG2 . VAL B 1 20  ? -2.991  -17.594 3.877   1.00 39.56  ? 20  VAL B CG2 1 
ATOM   3033 N  N   . THR B 1 21  ? -5.586  -21.521 3.268   1.00 43.45  ? 21  THR B N   1 
ATOM   3034 C  CA  . THR B 1 21  ? -6.824  -22.324 3.165   1.00 41.51  ? 21  THR B CA  1 
ATOM   3035 C  C   . THR B 1 21  ? -7.414  -22.502 4.566   1.00 43.65  ? 21  THR B C   1 
ATOM   3036 O  O   . THR B 1 21  ? -6.665  -22.824 5.506   1.00 42.85  ? 21  THR B O   1 
ATOM   3037 C  CB  . THR B 1 21  ? -6.567  -23.677 2.498   1.00 40.88  ? 21  THR B CB  1 
ATOM   3038 O  OG1 . THR B 1 21  ? -5.976  -23.459 1.220   1.00 33.98  ? 21  THR B OG1 1 
ATOM   3039 C  CG2 . THR B 1 21  ? -7.837  -24.488 2.363   1.00 42.05  ? 21  THR B CG2 1 
ATOM   3040 N  N   . CYS B 1 22  ? -8.711  -22.264 4.670   1.00 40.59  ? 22  CYS B N   1 
ATOM   3041 C  CA  . CYS B 1 22  ? -9.540  -22.485 5.870   1.00 44.24  ? 22  CYS B CA  1 
ATOM   3042 C  C   . CYS B 1 22  ? -10.861 -23.071 5.380   1.00 46.79  ? 22  CYS B C   1 
ATOM   3043 O  O   . CYS B 1 22  ? -11.569 -22.377 4.630   1.00 46.66  ? 22  CYS B O   1 
ATOM   3044 C  CB  . CYS B 1 22  ? -9.756  -21.181 6.624   1.00 45.38  ? 22  CYS B CB  1 
ATOM   3045 S  SG  . CYS B 1 22  ? -10.627 -21.387 8.196   1.00 46.73  ? 22  CYS B SG  1 
ATOM   3046 N  N   . GLY B 1 23  ? -11.133 -24.328 5.726   1.00 49.89  ? 23  GLY B N   1 
ATOM   3047 C  CA  . GLY B 1 23  ? -12.278 -25.086 5.190   1.00 47.24  ? 23  GLY B CA  1 
ATOM   3048 C  C   . GLY B 1 23  ? -12.125 -25.279 3.697   1.00 41.69  ? 23  GLY B C   1 
ATOM   3049 O  O   . GLY B 1 23  ? -11.080 -25.772 3.266   1.00 45.66  ? 23  GLY B O   1 
ATOM   3050 N  N   . THR B 1 24  ? -13.114 -24.853 2.925   1.00 46.81  ? 24  THR B N   1 
ATOM   3051 C  CA  . THR B 1 24  ? -13.117 -25.008 1.451   1.00 49.15  ? 24  THR B CA  1 
ATOM   3052 C  C   . THR B 1 24  ? -12.582 -23.730 0.784   1.00 46.34  ? 24  THR B C   1 
ATOM   3053 O  O   . THR B 1 24  ? -12.503 -23.728 -0.460  1.00 47.29  ? 24  THR B O   1 
ATOM   3054 C  CB  . THR B 1 24  ? -14.519 -25.364 0.930   1.00 49.94  ? 24  THR B CB  1 
ATOM   3055 O  OG1 . THR B 1 24  ? -15.434 -24.368 1.389   1.00 50.64  ? 24  THR B OG1 1 
ATOM   3056 C  CG2 . THR B 1 24  ? -14.982 -26.740 1.352   1.00 50.56  ? 24  THR B CG2 1 
ATOM   3057 N  N   . THR B 1 25  ? -12.265 -22.674 1.538   1.00 44.51  ? 25  THR B N   1 
ATOM   3058 C  CA  . THR B 1 25  ? -11.843 -21.373 0.945   1.00 44.13  ? 25  THR B CA  1 
ATOM   3059 C  C   . THR B 1 25  ? -10.322 -21.335 0.861   1.00 43.95  ? 25  THR B C   1 
ATOM   3060 O  O   . THR B 1 25  ? -9.679  -21.398 1.921   1.00 43.55  ? 25  THR B O   1 
ATOM   3061 C  CB  . THR B 1 25  ? -12.357 -20.157 1.720   1.00 47.02  ? 25  THR B CB  1 
ATOM   3062 O  OG1 . THR B 1 25  ? -13.759 -20.324 1.884   1.00 47.42  ? 25  THR B OG1 1 
ATOM   3063 C  CG2 . THR B 1 25  ? -12.092 -18.842 1.019   1.00 46.03  ? 25  THR B CG2 1 
ATOM   3064 N  N   . THR B 1 26  ? -9.774  -21.246 -0.354  1.00 38.29  ? 26  THR B N   1 
ATOM   3065 C  CA  . THR B 1 26  ? -8.366  -20.847 -0.561  1.00 40.16  ? 26  THR B CA  1 
ATOM   3066 C  C   . THR B 1 26  ? -8.320  -19.401 -1.075  1.00 40.22  ? 26  THR B C   1 
ATOM   3067 O  O   . THR B 1 26  ? -9.190  -19.004 -1.877  1.00 38.01  ? 26  THR B O   1 
ATOM   3068 C  CB  . THR B 1 26  ? -7.644  -21.828 -1.482  1.00 42.17  ? 26  THR B CB  1 
ATOM   3069 O  OG1 . THR B 1 26  ? -7.542  -23.048 -0.749  1.00 43.57  ? 26  THR B OG1 1 
ATOM   3070 C  CG2 . THR B 1 26  ? -6.260  -21.364 -1.869  1.00 44.97  ? 26  THR B CG2 1 
ATOM   3071 N  N   . LEU B 1 27  ? -7.342  -18.637 -0.591  1.00 37.33  ? 27  LEU B N   1 
ATOM   3072 C  CA  . LEU B 1 27  ? -6.983  -17.310 -1.140  1.00 33.98  ? 27  LEU B CA  1 
ATOM   3073 C  C   . LEU B 1 27  ? -5.528  -17.043 -0.759  1.00 34.52  ? 27  LEU B C   1 
ATOM   3074 O  O   . LEU B 1 27  ? -4.819  -18.027 -0.360  1.00 32.43  ? 27  LEU B O   1 
ATOM   3075 C  CB  . LEU B 1 27  ? -7.960  -16.249 -0.621  1.00 33.62  ? 27  LEU B CB  1 
ATOM   3076 C  CG  . LEU B 1 27  ? -8.307  -16.325 0.865   1.00 33.55  ? 27  LEU B CG  1 
ATOM   3077 C  CD1 . LEU B 1 27  ? -7.131  -15.945 1.758   1.00 32.10  ? 27  LEU B CD1 1 
ATOM   3078 C  CD2 . LEU B 1 27  ? -9.507  -15.452 1.155   1.00 34.66  ? 27  LEU B CD2 1 
ATOM   3079 N  N   . ASN B 1 28  ? -5.084  -15.791 -0.915  1.00 29.02  ? 28  ASN B N   1 
ATOM   3080 C  CA  . ASN B 1 28  ? -3.657  -15.412 -0.777  1.00 27.07  ? 28  ASN B CA  1 
ATOM   3081 C  C   . ASN B 1 28  ? -3.418  -14.773 0.585   1.00 26.42  ? 28  ASN B C   1 
ATOM   3082 O  O   . ASN B 1 28  ? -4.313  -14.080 1.090   1.00 27.46  ? 28  ASN B O   1 
ATOM   3083 C  CB  . ASN B 1 28  ? -3.232  -14.469 -1.904  1.00 26.51  ? 28  ASN B CB  1 
ATOM   3084 C  CG  . ASN B 1 28  ? -3.540  -15.065 -3.253  1.00 26.06  ? 28  ASN B CG  1 
ATOM   3085 O  OD1 . ASN B 1 28  ? -2.761  -15.859 -3.747  1.00 26.34  ? 28  ASN B OD1 1 
ATOM   3086 N  ND2 . ASN B 1 28  ? -4.686  -14.729 -3.821  1.00 27.84  ? 28  ASN B ND2 1 
ATOM   3087 N  N   . GLY B 1 29  ? -2.213  -14.967 1.103   1.00 26.02  ? 29  GLY B N   1 
ATOM   3088 C  CA  . GLY B 1 29  ? -1.712  -14.294 2.301   1.00 28.07  ? 29  GLY B CA  1 
ATOM   3089 C  C   . GLY B 1 29  ? -0.404  -13.585 2.019   1.00 28.17  ? 29  GLY B C   1 
ATOM   3090 O  O   . GLY B 1 29  ? 0.304   -13.983 1.058   1.00 25.97  ? 29  GLY B O   1 
ATOM   3091 N  N   . LEU B 1 30  ? -0.103  -12.586 2.848   1.00 25.63  ? 30  LEU B N   1 
ATOM   3092 C  CA  . LEU B 1 30  ? 1.167   -11.839 2.831   1.00 27.32  ? 30  LEU B CA  1 
ATOM   3093 C  C   . LEU B 1 30  ? 2.005   -12.262 4.055   1.00 29.13  ? 30  LEU B C   1 
ATOM   3094 O  O   . LEU B 1 30  ? 1.587   -12.012 5.205   1.00 27.13  ? 30  LEU B O   1 
ATOM   3095 C  CB  . LEU B 1 30  ? 0.817   -10.346 2.838   1.00 26.16  ? 30  LEU B CB  1 
ATOM   3096 C  CG  . LEU B 1 30  ? 2.012   -9.401  2.757   1.00 25.13  ? 30  LEU B CG  1 
ATOM   3097 C  CD1 . LEU B 1 30  ? 2.740   -9.543  1.419   1.00 26.93  ? 30  LEU B CD1 1 
ATOM   3098 C  CD2 . LEU B 1 30  ? 1.568   -7.973  2.983   1.00 27.05  ? 30  LEU B CD2 1 
ATOM   3099 N  N   . TRP B 1 31  ? 3.159   -12.884 3.821   1.00 29.65  ? 31  TRP B N   1 
ATOM   3100 C  CA  . TRP B 1 31  ? 4.065   -13.412 4.879   1.00 29.94  ? 31  TRP B CA  1 
ATOM   3101 C  C   . TRP B 1 31  ? 5.211   -12.425 5.151   1.00 28.39  ? 31  TRP B C   1 
ATOM   3102 O  O   . TRP B 1 31  ? 6.111   -12.322 4.312   1.00 28.76  ? 31  TRP B O   1 
ATOM   3103 C  CB  . TRP B 1 31  ? 4.589   -14.775 4.442   1.00 30.39  ? 31  TRP B CB  1 
ATOM   3104 C  CG  . TRP B 1 31  ? 5.458   -15.458 5.449   1.00 33.33  ? 31  TRP B CG  1 
ATOM   3105 C  CD1 . TRP B 1 31  ? 5.516   -15.234 6.795   1.00 35.63  ? 31  TRP B CD1 1 
ATOM   3106 C  CD2 . TRP B 1 31  ? 6.379   -16.521 5.178   1.00 34.12  ? 31  TRP B CD2 1 
ATOM   3107 N  NE1 . TRP B 1 31  ? 6.411   -16.084 7.383   1.00 35.65  ? 31  TRP B NE1 1 
ATOM   3108 C  CE2 . TRP B 1 31  ? 6.947   -16.895 6.417   1.00 38.73  ? 31  TRP B CE2 1 
ATOM   3109 C  CE3 . TRP B 1 31  ? 6.752   -17.205 4.017   1.00 34.64  ? 31  TRP B CE3 1 
ATOM   3110 C  CZ2 . TRP B 1 31  ? 7.907   -17.900 6.515   1.00 37.09  ? 31  TRP B CZ2 1 
ATOM   3111 C  CZ3 . TRP B 1 31  ? 7.687   -18.209 4.121   1.00 36.82  ? 31  TRP B CZ3 1 
ATOM   3112 C  CH2 . TRP B 1 31  ? 8.256   -18.546 5.355   1.00 37.04  ? 31  TRP B CH2 1 
ATOM   3113 N  N   . LEU B 1 32  ? 5.175   -11.720 6.275   1.00 28.48  ? 32  LEU B N   1 
ATOM   3114 C  CA  . LEU B 1 32  ? 6.235   -10.754 6.685   1.00 29.93  ? 32  LEU B CA  1 
ATOM   3115 C  C   . LEU B 1 32  ? 6.663   -11.061 8.122   1.00 30.85  ? 32  LEU B C   1 
ATOM   3116 O  O   . LEU B 1 32  ? 5.781   -11.132 9.006   1.00 31.17  ? 32  LEU B O   1 
ATOM   3117 C  CB  . LEU B 1 32  ? 5.707   -9.322  6.592   1.00 29.39  ? 32  LEU B CB  1 
ATOM   3118 C  CG  . LEU B 1 32  ? 5.223   -8.887  5.207   1.00 31.63  ? 32  LEU B CG  1 
ATOM   3119 C  CD1 . LEU B 1 32  ? 4.362   -7.640  5.310   1.00 28.70  ? 32  LEU B CD1 1 
ATOM   3120 C  CD2 . LEU B 1 32  ? 6.398   -8.659  4.285   1.00 31.82  ? 32  LEU B CD2 1 
ATOM   3121 N  N   . ASP B 1 33  ? 7.972   -11.162 8.358   1.00 32.42  ? 33  ASP B N   1 
ATOM   3122 C  CA  . ASP B 1 33  ? 8.494   -11.601 9.671   1.00 31.58  ? 33  ASP B CA  1 
ATOM   3123 C  C   . ASP B 1 33  ? 7.774   -12.926 9.952   1.00 30.40  ? 33  ASP B C   1 
ATOM   3124 O  O   . ASP B 1 33  ? 7.727   -13.758 9.030   1.00 28.01  ? 33  ASP B O   1 
ATOM   3125 C  CB  . ASP B 1 33  ? 8.305   -10.479 10.697  1.00 32.57  ? 33  ASP B CB  1 
ATOM   3126 C  CG  . ASP B 1 33  ? 8.937   -9.166  10.270  1.00 33.05  ? 33  ASP B CG  1 
ATOM   3127 O  OD1 . ASP B 1 33  ? 10.177  -9.120  10.182  1.00 36.49  ? 33  ASP B OD1 1 
ATOM   3128 O  OD2 . ASP B 1 33  ? 8.181   -8.214  9.991   1.00 34.18  ? 33  ASP B OD2 1 
ATOM   3129 N  N   . ASP B 1 34  ? 7.163   -13.108 11.121  1.00 32.54  ? 34  ASP B N   1 
ATOM   3130 C  CA  . ASP B 1 34  ? 6.555   -14.416 11.501  1.00 35.13  ? 34  ASP B CA  1 
ATOM   3131 C  C   . ASP B 1 34  ? 5.025   -14.313 11.478  1.00 33.29  ? 34  ASP B C   1 
ATOM   3132 O  O   . ASP B 1 34  ? 4.367   -15.082 12.206  1.00 35.22  ? 34  ASP B O   1 
ATOM   3133 C  CB  . ASP B 1 34  ? 7.103   -14.906 12.849  1.00 36.82  ? 34  ASP B CB  1 
ATOM   3134 C  CG  . ASP B 1 34  ? 6.790   -13.991 14.025  1.00 37.12  ? 34  ASP B CG  1 
ATOM   3135 O  OD1 . ASP B 1 34  ? 6.493   -12.815 13.784  1.00 34.79  ? 34  ASP B OD1 1 
ATOM   3136 O  OD2 . ASP B 1 34  ? 6.820   -14.469 15.165  1.00 41.40  ? 34  ASP B OD2 1 
ATOM   3137 N  N   . VAL B 1 35  ? 4.453   -13.443 10.642  1.00 31.18  ? 35  VAL B N   1 
ATOM   3138 C  CA  . VAL B 1 35  ? 2.967   -13.298 10.549  1.00 29.51  ? 35  VAL B CA  1 
ATOM   3139 C  C   . VAL B 1 35  ? 2.529   -13.416 9.092   1.00 30.71  ? 35  VAL B C   1 
ATOM   3140 O  O   . VAL B 1 35  ? 3.199   -12.830 8.218   1.00 30.74  ? 35  VAL B O   1 
ATOM   3141 C  CB  . VAL B 1 35  ? 2.513   -11.962 11.158  1.00 29.94  ? 35  VAL B CB  1 
ATOM   3142 C  CG1 . VAL B 1 35  ? 1.019   -11.756 11.008  1.00 28.54  ? 35  VAL B CG1 1 
ATOM   3143 C  CG2 . VAL B 1 35  ? 2.934   -11.856 12.613  1.00 31.92  ? 35  VAL B CG2 1 
ATOM   3144 N  N   . VAL B 1 36  ? 1.427   -14.131 8.860   1.00 29.46  ? 36  VAL B N   1 
ATOM   3145 C  CA  . VAL B 1 36  ? 0.700   -14.143 7.567   1.00 31.39  ? 36  VAL B CA  1 
ATOM   3146 C  C   . VAL B 1 36  ? -0.576  -13.313 7.716   1.00 31.10  ? 36  VAL B C   1 
ATOM   3147 O  O   . VAL B 1 36  ? -1.357  -13.612 8.633   1.00 32.62  ? 36  VAL B O   1 
ATOM   3148 C  CB  . VAL B 1 36  ? 0.419   -15.582 7.109   1.00 31.05  ? 36  VAL B CB  1 
ATOM   3149 C  CG1 . VAL B 1 36  ? -0.386  -15.599 5.822   1.00 30.24  ? 36  VAL B CG1 1 
ATOM   3150 C  CG2 . VAL B 1 36  ? 1.731   -16.330 6.952   1.00 30.61  ? 36  VAL B CG2 1 
ATOM   3151 N  N   . TYR B 1 37  ? -0.763  -12.322 6.836   1.00 29.40  ? 37  TYR B N   1 
ATOM   3152 C  CA  . TYR B 1 37  ? -1.941  -11.422 6.786   1.00 27.51  ? 37  TYR B CA  1 
ATOM   3153 C  C   . TYR B 1 37  ? -2.843  -11.875 5.643   1.00 26.91  ? 37  TYR B C   1 
ATOM   3154 O  O   . TYR B 1 37  ? -2.343  -12.087 4.516   1.00 26.21  ? 37  TYR B O   1 
ATOM   3155 C  CB  . TYR B 1 37  ? -1.498  -9.970  6.582   1.00 28.33  ? 37  TYR B CB  1 
ATOM   3156 C  CG  . TYR B 1 37  ? -0.532  -9.485  7.626   1.00 26.86  ? 37  TYR B CG  1 
ATOM   3157 C  CD1 . TYR B 1 37  ? 0.803   -9.826  7.552   1.00 28.17  ? 37  TYR B CD1 1 
ATOM   3158 C  CD2 . TYR B 1 37  ? -0.943  -8.694  8.693   1.00 27.50  ? 37  TYR B CD2 1 
ATOM   3159 C  CE1 . TYR B 1 37  ? 1.717   -9.375  8.492   1.00 31.34  ? 37  TYR B CE1 1 
ATOM   3160 C  CE2 . TYR B 1 37  ? -0.046  -8.242  9.653   1.00 27.79  ? 37  TYR B CE2 1 
ATOM   3161 C  CZ  . TYR B 1 37  ? 1.291   -8.599  9.559   1.00 29.26  ? 37  TYR B CZ  1 
ATOM   3162 O  OH  . TYR B 1 37  ? 2.213   -8.215  10.488  1.00 31.62  ? 37  TYR B OH  1 
ATOM   3163 N  N   . CYS B 1 38  ? -4.141  -12.005 5.892   1.00 26.08  ? 38  CYS B N   1 
ATOM   3164 C  CA  . CYS B 1 38  ? -5.122  -12.287 4.819   1.00 27.35  ? 38  CYS B CA  1 
ATOM   3165 C  C   . CYS B 1 38  ? -6.464  -11.687 5.210   1.00 27.50  ? 38  CYS B C   1 
ATOM   3166 O  O   . CYS B 1 38  ? -6.619  -11.154 6.304   1.00 27.36  ? 38  CYS B O   1 
ATOM   3167 C  CB  . CYS B 1 38  ? -5.233  -13.789 4.524   1.00 31.33  ? 38  CYS B CB  1 
ATOM   3168 S  SG  . CYS B 1 38  ? -5.978  -14.775 5.858   1.00 33.70  ? 38  CYS B SG  1 
ATOM   3169 N  N   . PRO B 1 39  ? -7.448  -11.662 4.287   1.00 27.49  ? 39  PRO B N   1 
ATOM   3170 C  CA  . PRO B 1 39  ? -8.775  -11.177 4.614   1.00 27.61  ? 39  PRO B CA  1 
ATOM   3171 C  C   . PRO B 1 39  ? -9.414  -12.108 5.654   1.00 30.62  ? 39  PRO B C   1 
ATOM   3172 O  O   . PRO B 1 39  ? -9.266  -13.313 5.499   1.00 28.28  ? 39  PRO B O   1 
ATOM   3173 C  CB  . PRO B 1 39  ? -9.496  -11.244 3.266   1.00 28.48  ? 39  PRO B CB  1 
ATOM   3174 C  CG  . PRO B 1 39  ? -8.399  -11.159 2.253   1.00 27.46  ? 39  PRO B CG  1 
ATOM   3175 C  CD  . PRO B 1 39  ? -7.324  -12.027 2.866   1.00 27.31  ? 39  PRO B CD  1 
ATOM   3176 N  N   . ARG B 1 40  ? -10.095 -11.538 6.657   1.00 29.50  ? 40  ARG B N   1 
ATOM   3177 C  CA  . ARG B 1 40  ? -10.748 -12.326 7.730   1.00 30.36  ? 40  ARG B CA  1 
ATOM   3178 C  C   . ARG B 1 40  ? -11.851 -13.183 7.104   1.00 33.96  ? 40  ARG B C   1 
ATOM   3179 O  O   . ARG B 1 40  ? -12.106 -14.279 7.652   1.00 36.92  ? 40  ARG B O   1 
ATOM   3180 C  CB  . ARG B 1 40  ? -11.257 -11.423 8.862   1.00 31.06  ? 40  ARG B CB  1 
ATOM   3181 C  CG  . ARG B 1 40  ? -12.416 -10.507 8.502   1.00 32.05  ? 40  ARG B CG  1 
ATOM   3182 C  CD  . ARG B 1 40  ? -12.929 -9.796  9.741   1.00 30.14  ? 40  ARG B CD  1 
ATOM   3183 N  NE  . ARG B 1 40  ? -13.993 -8.888  9.387   1.00 31.38  ? 40  ARG B NE  1 
ATOM   3184 C  CZ  . ARG B 1 40  ? -14.672 -8.138  10.237  1.00 34.43  ? 40  ARG B CZ  1 
ATOM   3185 N  NH1 . ARG B 1 40  ? -14.392 -8.158  11.529  1.00 35.05  ? 40  ARG B NH1 1 
ATOM   3186 N  NH2 . ARG B 1 40  ? -15.622 -7.345  9.785   1.00 31.41  ? 40  ARG B NH2 1 
ATOM   3187 N  N   . HIS B 1 41  ? -12.435 -12.762 5.977   1.00 30.76  ? 41  HIS B N   1 
ATOM   3188 C  CA  . HIS B 1 41  ? -13.558 -13.492 5.335   1.00 33.36  ? 41  HIS B CA  1 
ATOM   3189 C  C   . HIS B 1 41  ? -13.132 -14.871 4.825   1.00 31.66  ? 41  HIS B C   1 
ATOM   3190 O  O   . HIS B 1 41  ? -14.013 -15.592 4.413   1.00 35.38  ? 41  HIS B O   1 
ATOM   3191 C  CB  . HIS B 1 41  ? -14.297 -12.655 4.272   1.00 35.17  ? 41  HIS B CB  1 
ATOM   3192 C  CG  . HIS B 1 41  ? -13.620 -12.488 2.953   1.00 34.07  ? 41  HIS B CG  1 
ATOM   3193 N  ND1 . HIS B 1 41  ? -13.253 -13.557 2.151   1.00 35.79  ? 41  HIS B ND1 1 
ATOM   3194 C  CD2 . HIS B 1 41  ? -13.310 -11.369 2.261   1.00 36.75  ? 41  HIS B CD2 1 
ATOM   3195 C  CE1 . HIS B 1 41  ? -12.716 -13.109 1.031   1.00 35.61  ? 41  HIS B CE1 1 
ATOM   3196 N  NE2 . HIS B 1 41  ? -12.743 -11.762 1.073   1.00 37.75  ? 41  HIS B NE2 1 
ATOM   3197 N  N   . VAL B 1 42  ? -11.864 -15.258 4.903   1.00 37.01  ? 42  VAL B N   1 
ATOM   3198 C  CA  . VAL B 1 42  ? -11.421 -16.656 4.608   1.00 37.65  ? 42  VAL B CA  1 
ATOM   3199 C  C   . VAL B 1 42  ? -12.134 -17.645 5.558   1.00 45.13  ? 42  VAL B C   1 
ATOM   3200 O  O   . VAL B 1 42  ? -12.296 -18.822 5.148   1.00 43.83  ? 42  VAL B O   1 
ATOM   3201 C  CB  . VAL B 1 42  ? -9.892  -16.794 4.711   1.00 38.83  ? 42  VAL B CB  1 
ATOM   3202 C  CG1 . VAL B 1 42  ? -9.379  -16.633 6.144   1.00 37.06  ? 42  VAL B CG1 1 
ATOM   3203 C  CG2 . VAL B 1 42  ? -9.391  -18.096 4.103   1.00 39.28  ? 42  VAL B CG2 1 
ATOM   3204 N  N   . ILE B 1 43  ? -12.511 -17.216 6.778   1.00 42.86  ? 43  ILE B N   1 
ATOM   3205 C  CA  . ILE B 1 43  ? -13.067 -18.120 7.836   1.00 44.48  ? 43  ILE B CA  1 
ATOM   3206 C  C   . ILE B 1 43  ? -14.547 -18.413 7.570   1.00 46.05  ? 43  ILE B C   1 
ATOM   3207 O  O   . ILE B 1 43  ? -15.071 -19.283 8.252   1.00 50.35  ? 43  ILE B O   1 
ATOM   3208 C  CB  . ILE B 1 43  ? -12.868 -17.570 9.266   1.00 41.61  ? 43  ILE B CB  1 
ATOM   3209 C  CG1 . ILE B 1 43  ? -13.759 -16.359 9.550   1.00 44.14  ? 43  ILE B CG1 1 
ATOM   3210 C  CG2 . ILE B 1 43  ? -11.400 -17.297 9.525   1.00 40.86  ? 43  ILE B CG2 1 
ATOM   3211 C  CD1 . ILE B 1 43  ? -13.571 -15.762 10.924  1.00 46.28  ? 43  ILE B CD1 1 
ATOM   3212 N  N   . CYS B 1 44  ? -15.183 -17.721 6.624   1.00 48.30  ? 44  CYS B N   1 
ATOM   3213 C  CA  . CYS B 1 44  ? -16.639 -17.800 6.338   1.00 49.95  ? 44  CYS B CA  1 
ATOM   3214 C  C   . CYS B 1 44  ? -16.956 -18.890 5.313   1.00 54.48  ? 44  CYS B C   1 
ATOM   3215 O  O   . CYS B 1 44  ? -16.131 -19.109 4.430   1.00 56.86  ? 44  CYS B O   1 
ATOM   3216 C  CB  . CYS B 1 44  ? -17.144 -16.469 5.808   1.00 46.88  ? 44  CYS B CB  1 
ATOM   3217 S  SG  . CYS B 1 44  ? -17.011 -15.176 7.060   1.00 51.42  ? 44  CYS B SG  1 
ATOM   3218 N  N   . THR B 1 45  ? -18.114 -19.545 5.468   1.00 61.54  ? 45  THR B N   1 
ATOM   3219 C  CA  . THR B 1 45  ? -18.816 -20.340 4.423   1.00 64.69  ? 45  THR B CA  1 
ATOM   3220 C  C   . THR B 1 45  ? -19.852 -19.433 3.762   1.00 72.34  ? 45  THR B C   1 
ATOM   3221 O  O   . THR B 1 45  ? -20.185 -18.404 4.389   1.00 70.50  ? 45  THR B O   1 
ATOM   3222 C  CB  . THR B 1 45  ? -19.549 -21.551 5.010   1.00 60.81  ? 45  THR B CB  1 
ATOM   3223 O  OG1 . THR B 1 45  ? -20.639 -21.011 5.756   1.00 59.58  ? 45  THR B OG1 1 
ATOM   3224 C  CG2 . THR B 1 45  ? -18.676 -22.412 5.895   1.00 61.37  ? 45  THR B CG2 1 
ATOM   3225 N  N   . SER B 1 46  ? -20.350 -19.824 2.580   1.00 83.09  ? 46  SER B N   1 
ATOM   3226 C  CA  . SER B 1 46  ? -21.407 -19.124 1.798   1.00 84.93  ? 46  SER B CA  1 
ATOM   3227 C  C   . SER B 1 46  ? -22.475 -18.601 2.759   1.00 85.60  ? 46  SER B C   1 
ATOM   3228 O  O   . SER B 1 46  ? -22.815 -17.400 2.676   1.00 93.50  ? 46  SER B O   1 
ATOM   3229 C  CB  . SER B 1 46  ? -22.042 -20.028 0.765   1.00 86.56  ? 46  SER B CB  1 
ATOM   3230 O  OG  . SER B 1 46  ? -21.206 -21.132 0.456   1.00 95.13  ? 46  SER B OG  1 
ATOM   3231 N  N   . GLU B 1 47  ? -22.961 -19.486 3.638   1.00 81.34  ? 47  GLU B N   1 
ATOM   3232 C  CA  . GLU B 1 47  ? -24.071 -19.219 4.590   1.00 80.57  ? 47  GLU B CA  1 
ATOM   3233 C  C   . GLU B 1 47  ? -23.650 -18.122 5.573   1.00 75.33  ? 47  GLU B C   1 
ATOM   3234 O  O   . GLU B 1 47  ? -24.438 -17.176 5.796   1.00 66.50  ? 47  GLU B O   1 
ATOM   3235 C  CB  . GLU B 1 47  ? -24.428 -20.487 5.359   1.00 85.95  ? 47  GLU B CB  1 
ATOM   3236 C  CG  . GLU B 1 47  ? -24.767 -21.666 4.470   1.00 98.30  ? 47  GLU B CG  1 
ATOM   3237 C  CD  . GLU B 1 47  ? -25.467 -22.798 5.204   1.00 107.67 ? 47  GLU B CD  1 
ATOM   3238 O  OE1 . GLU B 1 47  ? -25.514 -22.746 6.453   1.00 114.23 ? 47  GLU B OE1 1 
ATOM   3239 O  OE2 . GLU B 1 47  ? -25.972 -23.723 4.528   1.00 117.42 ? 47  GLU B OE2 1 
ATOM   3240 N  N   . ASP B 1 48  ? -22.451 -18.256 6.140   1.00 69.93  ? 48  ASP B N   1 
ATOM   3241 C  CA  . ASP B 1 48  ? -21.871 -17.273 7.092   1.00 68.90  ? 48  ASP B CA  1 
ATOM   3242 C  C   . ASP B 1 48  ? -21.888 -15.882 6.442   1.00 68.59  ? 48  ASP B C   1 
ATOM   3243 O  O   . ASP B 1 48  ? -22.233 -14.914 7.145   1.00 62.37  ? 48  ASP B O   1 
ATOM   3244 C  CB  . ASP B 1 48  ? -20.452 -17.673 7.515   1.00 67.43  ? 48  ASP B CB  1 
ATOM   3245 C  CG  . ASP B 1 48  ? -20.373 -18.869 8.453   1.00 62.33  ? 48  ASP B CG  1 
ATOM   3246 O  OD1 . ASP B 1 48  ? -21.102 -18.872 9.464   1.00 60.03  ? 48  ASP B OD1 1 
ATOM   3247 O  OD2 . ASP B 1 48  ? -19.575 -19.784 8.171   1.00 60.37  ? 48  ASP B OD2 1 
ATOM   3248 N  N   . MET B 1 49  ? -21.573 -15.792 5.141   1.00 73.11  ? 49  MET B N   1 
ATOM   3249 C  CA  . MET B 1 49  ? -21.199 -14.515 4.465   1.00 70.22  ? 49  MET B CA  1 
ATOM   3250 C  C   . MET B 1 49  ? -22.390 -13.549 4.395   1.00 69.16  ? 49  MET B C   1 
ATOM   3251 O  O   . MET B 1 49  ? -22.131 -12.336 4.222   1.00 61.75  ? 49  MET B O   1 
ATOM   3252 C  CB  . MET B 1 49  ? -20.636 -14.735 3.055   1.00 70.99  ? 49  MET B CB  1 
ATOM   3253 C  CG  . MET B 1 49  ? -19.113 -14.915 3.020   1.00 78.52  ? 49  MET B CG  1 
ATOM   3254 S  SD  . MET B 1 49  ? -18.146 -13.535 3.759   1.00 81.71  ? 49  MET B SD  1 
ATOM   3255 C  CE  . MET B 1 49  ? -17.600 -12.642 2.299   1.00 76.16  ? 49  MET B CE  1 
ATOM   3256 N  N   . LEU B 1 50  ? -23.632 -14.026 4.546   1.00 64.12  ? 50  LEU B N   1 
ATOM   3257 C  CA  . LEU B 1 50  ? -24.831 -13.147 4.447   1.00 63.37  ? 50  LEU B CA  1 
ATOM   3258 C  C   . LEU B 1 50  ? -24.891 -12.219 5.669   1.00 56.98  ? 50  LEU B C   1 
ATOM   3259 O  O   . LEU B 1 50  ? -25.282 -11.057 5.499   1.00 61.45  ? 50  LEU B O   1 
ATOM   3260 C  CB  . LEU B 1 50  ? -26.102 -13.991 4.290   1.00 68.82  ? 50  LEU B CB  1 
ATOM   3261 C  CG  . LEU B 1 50  ? -26.364 -14.525 2.879   1.00 78.12  ? 50  LEU B CG  1 
ATOM   3262 C  CD1 . LEU B 1 50  ? -25.287 -15.518 2.454   1.00 80.15  ? 50  LEU B CD1 1 
ATOM   3263 C  CD2 . LEU B 1 50  ? -27.745 -15.169 2.784   1.00 79.81  ? 50  LEU B CD2 1 
ATOM   3264 N  N   . ASN B 1 51  ? -24.491 -12.696 6.848   1.00 56.35  ? 51  ASN B N   1 
ATOM   3265 C  CA  . ASN B 1 51  ? -24.522 -11.918 8.118   1.00 56.75  ? 51  ASN B CA  1 
ATOM   3266 C  C   . ASN B 1 51  ? -23.501 -12.514 9.086   1.00 52.45  ? 51  ASN B C   1 
ATOM   3267 O  O   . ASN B 1 51  ? -23.847 -13.214 10.027  1.00 48.99  ? 51  ASN B O   1 
ATOM   3268 C  CB  . ASN B 1 51  ? -25.927 -11.887 8.717   1.00 59.85  ? 51  ASN B CB  1 
ATOM   3269 C  CG  . ASN B 1 51  ? -26.053 -10.882 9.841   1.00 62.96  ? 51  ASN B CG  1 
ATOM   3270 O  OD1 . ASN B 1 51  ? -25.992 -11.251 11.009  1.00 66.01  ? 51  ASN B OD1 1 
ATOM   3271 N  ND2 . ASN B 1 51  ? -26.211 -9.612  9.499   1.00 62.14  ? 51  ASN B ND2 1 
ATOM   3272 N  N   . PRO B 1 52  ? -22.196 -12.267 8.875   1.00 52.60  ? 52  PRO B N   1 
ATOM   3273 C  CA  . PRO B 1 52  ? -21.152 -13.011 9.575   1.00 52.00  ? 52  PRO B CA  1 
ATOM   3274 C  C   . PRO B 1 52  ? -20.882 -12.411 10.958  1.00 47.31  ? 52  PRO B C   1 
ATOM   3275 O  O   . PRO B 1 52  ? -20.872 -11.214 11.073  1.00 46.29  ? 52  PRO B O   1 
ATOM   3276 C  CB  . PRO B 1 52  ? -19.953 -12.822 8.640   1.00 55.02  ? 52  PRO B CB  1 
ATOM   3277 C  CG  . PRO B 1 52  ? -20.153 -11.420 8.088   1.00 56.40  ? 52  PRO B CG  1 
ATOM   3278 C  CD  . PRO B 1 52  ? -21.653 -11.240 7.975   1.00 56.75  ? 52  PRO B CD  1 
ATOM   3279 N  N   . ASN B 1 53  ? -20.700 -13.260 11.965  1.00 51.20  ? 53  ASN B N   1 
ATOM   3280 C  CA  . ASN B 1 53  ? -20.226 -12.857 13.316  1.00 55.15  ? 53  ASN B CA  1 
ATOM   3281 C  C   . ASN B 1 53  ? -18.771 -13.322 13.435  1.00 53.81  ? 53  ASN B C   1 
ATOM   3282 O  O   . ASN B 1 53  ? -18.544 -14.528 13.718  1.00 44.88  ? 53  ASN B O   1 
ATOM   3283 C  CB  . ASN B 1 53  ? -21.111 -13.428 14.430  1.00 62.43  ? 53  ASN B CB  1 
ATOM   3284 C  CG  . ASN B 1 53  ? -20.707 -12.942 15.809  1.00 66.07  ? 53  ASN B CG  1 
ATOM   3285 O  OD1 . ASN B 1 53  ? -19.563 -12.538 16.037  1.00 61.53  ? 53  ASN B OD1 1 
ATOM   3286 N  ND2 . ASN B 1 53  ? -21.639 -12.990 16.744  1.00 69.79  ? 53  ASN B ND2 1 
ATOM   3287 N  N   . TYR B 1 54  ? -17.822 -12.418 13.163  1.00 52.04  ? 54  TYR B N   1 
ATOM   3288 C  CA  . TYR B 1 54  ? -16.401 -12.782 12.907  1.00 48.47  ? 54  TYR B CA  1 
ATOM   3289 C  C   . TYR B 1 54  ? -15.763 -13.226 14.233  1.00 47.62  ? 54  TYR B C   1 
ATOM   3290 O  O   . TYR B 1 54  ? -15.102 -14.309 14.228  1.00 42.81  ? 54  TYR B O   1 
ATOM   3291 C  CB  . TYR B 1 54  ? -15.661 -11.658 12.172  1.00 44.35  ? 54  TYR B CB  1 
ATOM   3292 C  CG  . TYR B 1 54  ? -15.909 -11.586 10.682  1.00 39.92  ? 54  TYR B CG  1 
ATOM   3293 C  CD1 . TYR B 1 54  ? -15.336 -12.500 9.814   1.00 40.01  ? 54  TYR B CD1 1 
ATOM   3294 C  CD2 . TYR B 1 54  ? -16.733 -10.618 10.132  1.00 38.25  ? 54  TYR B CD2 1 
ATOM   3295 C  CE1 . TYR B 1 54  ? -15.563 -12.448 8.446   1.00 38.76  ? 54  TYR B CE1 1 
ATOM   3296 C  CE2 . TYR B 1 54  ? -16.971 -10.551 8.769   1.00 39.33  ? 54  TYR B CE2 1 
ATOM   3297 C  CZ  . TYR B 1 54  ? -16.367 -11.459 7.914   1.00 39.44  ? 54  TYR B CZ  1 
ATOM   3298 O  OH  . TYR B 1 54  ? -16.589 -11.404 6.560   1.00 37.65  ? 54  TYR B OH  1 
ATOM   3299 N  N   . GLU B 1 55  ? -15.978 -12.457 15.314  1.00 49.15  ? 55  GLU B N   1 
ATOM   3300 C  CA  . GLU B 1 55  ? -15.613 -12.841 16.711  1.00 52.04  ? 55  GLU B CA  1 
ATOM   3301 C  C   . GLU B 1 55  ? -15.979 -14.316 16.878  1.00 53.94  ? 55  GLU B C   1 
ATOM   3302 O  O   . GLU B 1 55  ? -15.061 -15.166 17.046  1.00 49.96  ? 55  GLU B O   1 
ATOM   3303 C  CB  . GLU B 1 55  ? -16.378 -12.031 17.768  1.00 57.75  ? 55  GLU B CB  1 
ATOM   3304 C  CG  . GLU B 1 55  ? -16.050 -10.539 17.785  1.00 65.71  ? 55  GLU B CG  1 
ATOM   3305 C  CD  . GLU B 1 55  ? -16.895 -9.656  18.699  1.00 61.47  ? 55  GLU B CD  1 
ATOM   3306 O  OE1 . GLU B 1 55  ? -18.092 -9.967  18.898  1.00 66.12  ? 55  GLU B OE1 1 
ATOM   3307 O  OE2 . GLU B 1 55  ? -16.351 -8.655  19.207  1.00 51.47  ? 55  GLU B OE2 1 
ATOM   3308 N  N   . ASP B 1 56  ? -17.276 -14.605 16.719  1.00 57.26  ? 56  ASP B N   1 
ATOM   3309 C  CA  . ASP B 1 56  ? -17.889 -15.921 17.024  1.00 60.34  ? 56  ASP B CA  1 
ATOM   3310 C  C   . ASP B 1 56  ? -17.304 -16.979 16.084  1.00 60.55  ? 56  ASP B C   1 
ATOM   3311 O  O   . ASP B 1 56  ? -16.902 -18.048 16.573  1.00 62.23  ? 56  ASP B O   1 
ATOM   3312 C  CB  . ASP B 1 56  ? -19.419 -15.852 16.975  1.00 66.12  ? 56  ASP B CB  1 
ATOM   3313 C  CG  . ASP B 1 56  ? -20.064 -16.861 17.906  1.00 70.07  ? 56  ASP B CG  1 
ATOM   3314 O  OD1 . ASP B 1 56  ? -19.733 -16.824 19.115  1.00 71.05  ? 56  ASP B OD1 1 
ATOM   3315 O  OD2 . ASP B 1 56  ? -20.848 -17.700 17.413  1.00 69.49  ? 56  ASP B OD2 1 
ATOM   3316 N  N   . LEU B 1 57  ? -17.228 -16.696 14.786  1.00 55.01  ? 57  LEU B N   1 
ATOM   3317 C  CA  . LEU B 1 57  ? -16.669 -17.670 13.815  1.00 58.95  ? 57  LEU B CA  1 
ATOM   3318 C  C   . LEU B 1 57  ? -15.204 -17.969 14.150  1.00 55.95  ? 57  LEU B C   1 
ATOM   3319 O  O   . LEU B 1 57  ? -14.785 -19.106 13.889  1.00 56.22  ? 57  LEU B O   1 
ATOM   3320 C  CB  . LEU B 1 57  ? -16.812 -17.131 12.387  1.00 61.98  ? 57  LEU B CB  1 
ATOM   3321 C  CG  . LEU B 1 57  ? -18.218 -17.226 11.800  1.00 64.76  ? 57  LEU B CG  1 
ATOM   3322 C  CD1 . LEU B 1 57  ? -18.358 -16.348 10.567  1.00 62.73  ? 57  LEU B CD1 1 
ATOM   3323 C  CD2 . LEU B 1 57  ? -18.571 -18.677 11.488  1.00 65.47  ? 57  LEU B CD2 1 
ATOM   3324 N  N   . LEU B 1 58  ? -14.458 -16.993 14.681  1.00 55.29  ? 58  LEU B N   1 
ATOM   3325 C  CA  . LEU B 1 58  ? -12.979 -17.084 14.808  1.00 59.06  ? 58  LEU B CA  1 
ATOM   3326 C  C   . LEU B 1 58  ? -12.609 -17.948 16.022  1.00 63.59  ? 58  LEU B C   1 
ATOM   3327 O  O   . LEU B 1 58  ? -11.735 -18.844 15.873  1.00 54.98  ? 58  LEU B O   1 
ATOM   3328 C  CB  . LEU B 1 58  ? -12.374 -15.679 14.921  1.00 55.61  ? 58  LEU B CB  1 
ATOM   3329 C  CG  . LEU B 1 58  ? -10.858 -15.653 15.129  1.00 57.32  ? 58  LEU B CG  1 
ATOM   3330 C  CD1 . LEU B 1 58  ? -10.132 -16.384 14.004  1.00 56.64  ? 58  LEU B CD1 1 
ATOM   3331 C  CD2 . LEU B 1 58  ? -10.340 -14.228 15.271  1.00 56.46  ? 58  LEU B CD2 1 
ATOM   3332 N  N   . ILE B 1 59  ? -13.212 -17.663 17.183  1.00 69.24  ? 59  ILE B N   1 
ATOM   3333 C  CA  . ILE B 1 59  ? -13.005 -18.434 18.451  1.00 74.89  ? 59  ILE B CA  1 
ATOM   3334 C  C   . ILE B 1 59  ? -13.271 -19.918 18.163  1.00 70.46  ? 59  ILE B C   1 
ATOM   3335 O  O   . ILE B 1 59  ? -12.470 -20.747 18.608  1.00 73.32  ? 59  ILE B O   1 
ATOM   3336 C  CB  . ILE B 1 59  ? -13.860 -17.888 19.620  1.00 74.49  ? 59  ILE B CB  1 
ATOM   3337 C  CG1 . ILE B 1 59  ? -15.358 -17.896 19.301  1.00 77.97  ? 59  ILE B CG1 1 
ATOM   3338 C  CG2 . ILE B 1 59  ? -13.385 -16.501 20.039  1.00 71.40  ? 59  ILE B CG2 1 
ATOM   3339 C  CD1 . ILE B 1 59  ? -16.085 -19.167 19.695  1.00 78.84  ? 59  ILE B CD1 1 
ATOM   3340 N  N   . ARG B 1 60  ? -14.305 -20.236 17.382  1.00 70.26  ? 60  ARG B N   1 
ATOM   3341 C  CA  . ARG B 1 60  ? -14.651 -21.633 17.006  1.00 75.49  ? 60  ARG B CA  1 
ATOM   3342 C  C   . ARG B 1 60  ? -13.469 -22.307 16.300  1.00 72.63  ? 60  ARG B C   1 
ATOM   3343 O  O   . ARG B 1 60  ? -13.426 -23.536 16.305  1.00 71.59  ? 60  ARG B O   1 
ATOM   3344 C  CB  . ARG B 1 60  ? -15.855 -21.692 16.063  1.00 87.17  ? 60  ARG B CB  1 
ATOM   3345 C  CG  . ARG B 1 60  ? -17.193 -21.326 16.688  1.00 95.54  ? 60  ARG B CG  1 
ATOM   3346 C  CD  . ARG B 1 60  ? -18.206 -21.120 15.579  1.00 103.58 ? 60  ARG B CD  1 
ATOM   3347 N  NE  . ARG B 1 60  ? -19.572 -20.992 16.053  1.00 111.95 ? 60  ARG B NE  1 
ATOM   3348 C  CZ  . ARG B 1 60  ? -20.627 -20.841 15.262  1.00 113.79 ? 60  ARG B CZ  1 
ATOM   3349 N  NH1 . ARG B 1 60  ? -20.468 -20.804 13.947  1.00 114.52 ? 60  ARG B NH1 1 
ATOM   3350 N  NH2 . ARG B 1 60  ? -21.835 -20.725 15.790  1.00 112.85 ? 60  ARG B NH2 1 
ATOM   3351 N  N   . LYS B 1 61  ? -12.574 -21.544 15.666  1.00 76.12  ? 61  LYS B N   1 
ATOM   3352 C  CA  . LYS B 1 61  ? -11.445 -22.098 14.865  1.00 70.06  ? 61  LYS B CA  1 
ATOM   3353 C  C   . LYS B 1 61  ? -10.251 -22.359 15.783  1.00 61.09  ? 61  LYS B C   1 
ATOM   3354 O  O   . LYS B 1 61  ? -10.205 -21.784 16.897  1.00 63.39  ? 61  LYS B O   1 
ATOM   3355 C  CB  . LYS B 1 61  ? -11.028 -21.143 13.740  1.00 72.20  ? 61  LYS B CB  1 
ATOM   3356 C  CG  . LYS B 1 61  ? -12.141 -20.727 12.787  1.00 67.69  ? 61  LYS B CG  1 
ATOM   3357 C  CD  . LYS B 1 61  ? -12.425 -21.739 11.712  1.00 66.08  ? 61  LYS B CD  1 
ATOM   3358 C  CE  . LYS B 1 61  ? -13.876 -21.720 11.271  1.00 65.88  ? 61  LYS B CE  1 
ATOM   3359 N  NZ  . LYS B 1 61  ? -14.071 -22.530 10.048  1.00 64.32  ? 61  LYS B NZ  1 
ATOM   3360 N  N   . SER B 1 62  ? -9.310  -23.172 15.315  1.00 51.97  ? 62  SER B N   1 
ATOM   3361 C  CA  . SER B 1 62  ? -7.967  -23.298 15.933  1.00 55.53  ? 62  SER B CA  1 
ATOM   3362 C  C   . SER B 1 62  ? -6.862  -23.197 14.876  1.00 50.43  ? 62  SER B C   1 
ATOM   3363 O  O   . SER B 1 62  ? -7.147  -23.385 13.675  1.00 47.29  ? 62  SER B O   1 
ATOM   3364 C  CB  . SER B 1 62  ? -7.846  -24.581 16.705  1.00 61.42  ? 62  SER B CB  1 
ATOM   3365 O  OG  . SER B 1 62  ? -7.690  -25.679 15.820  1.00 60.51  ? 62  SER B OG  1 
ATOM   3366 N  N   . ASN B 1 63  ? -5.632  -22.977 15.346  1.00 48.55  ? 63  ASN B N   1 
ATOM   3367 C  CA  . ASN B 1 63  ? -4.406  -22.793 14.527  1.00 47.27  ? 63  ASN B CA  1 
ATOM   3368 C  C   . ASN B 1 63  ? -4.360  -23.812 13.368  1.00 51.90  ? 63  ASN B C   1 
ATOM   3369 O  O   . ASN B 1 63  ? -4.105  -23.391 12.215  1.00 49.15  ? 63  ASN B O   1 
ATOM   3370 C  CB  . ASN B 1 63  ? -3.164  -22.853 15.419  1.00 43.81  ? 63  ASN B CB  1 
ATOM   3371 C  CG  . ASN B 1 63  ? -3.075  -21.705 16.409  1.00 49.22  ? 63  ASN B CG  1 
ATOM   3372 O  OD1 . ASN B 1 63  ? -3.734  -20.672 16.251  1.00 46.22  ? 63  ASN B OD1 1 
ATOM   3373 N  ND2 . ASN B 1 63  ? -2.266  -21.876 17.448  1.00 46.82  ? 63  ASN B ND2 1 
ATOM   3374 N  N   . HIS B 1 64  ? -4.628  -25.093 13.648  1.00 49.20  ? 64  HIS B N   1 
ATOM   3375 C  CA  . HIS B 1 64  ? -4.510  -26.249 12.711  1.00 52.83  ? 64  HIS B CA  1 
ATOM   3376 C  C   . HIS B 1 64  ? -5.643  -26.222 11.663  1.00 51.64  ? 64  HIS B C   1 
ATOM   3377 O  O   . HIS B 1 64  ? -5.516  -26.942 10.660  1.00 52.31  ? 64  HIS B O   1 
ATOM   3378 C  CB  . HIS B 1 64  ? -4.440  -27.548 13.535  1.00 67.13  ? 64  HIS B CB  1 
ATOM   3379 C  CG  . HIS B 1 64  ? -5.182  -27.440 14.833  1.00 82.78  ? 64  HIS B CG  1 
ATOM   3380 N  ND1 . HIS B 1 64  ? -4.606  -26.891 15.981  1.00 83.05  ? 64  HIS B ND1 1 
ATOM   3381 C  CD2 . HIS B 1 64  ? -6.462  -27.739 15.160  1.00 92.09  ? 64  HIS B CD2 1 
ATOM   3382 C  CE1 . HIS B 1 64  ? -5.497  -26.879 16.955  1.00 91.16  ? 64  HIS B CE1 1 
ATOM   3383 N  NE2 . HIS B 1 64  ? -6.640  -27.405 16.481  1.00 96.84  ? 64  HIS B NE2 1 
ATOM   3384 N  N   . ASN B 1 65  ? -6.682  -25.393 11.855  1.00 50.38  ? 65  ASN B N   1 
ATOM   3385 C  CA  . ASN B 1 65  ? -7.745  -25.096 10.854  1.00 54.06  ? 65  ASN B CA  1 
ATOM   3386 C  C   . ASN B 1 65  ? -7.256  -24.141 9.761   1.00 54.59  ? 65  ASN B C   1 
ATOM   3387 O  O   . ASN B 1 65  ? -8.091  -23.759 8.919   1.00 54.25  ? 65  ASN B O   1 
ATOM   3388 C  CB  . ASN B 1 65  ? -8.958  -24.404 11.470  1.00 60.45  ? 65  ASN B CB  1 
ATOM   3389 C  CG  . ASN B 1 65  ? -9.682  -25.288 12.455  1.00 69.12  ? 65  ASN B CG  1 
ATOM   3390 O  OD1 . ASN B 1 65  ? -9.254  -25.441 13.597  1.00 81.62  ? 65  ASN B OD1 1 
ATOM   3391 N  ND2 . ASN B 1 65  ? -10.779 -25.875 12.012  1.00 72.63  ? 65  ASN B ND2 1 
ATOM   3392 N  N   . PHE B 1 66  ? -5.990  -23.723 9.786   1.00 46.69  ? 66  PHE B N   1 
ATOM   3393 C  CA  . PHE B 1 66  ? -5.436  -22.763 8.799   1.00 47.49  ? 66  PHE B CA  1 
ATOM   3394 C  C   . PHE B 1 66  ? -4.237  -23.406 8.114   1.00 41.43  ? 66  PHE B C   1 
ATOM   3395 O  O   . PHE B 1 66  ? -3.189  -23.491 8.754   1.00 44.77  ? 66  PHE B O   1 
ATOM   3396 C  CB  . PHE B 1 66  ? -5.029  -21.443 9.465   1.00 48.92  ? 66  PHE B CB  1 
ATOM   3397 C  CG  . PHE B 1 66  ? -6.162  -20.650 10.062  1.00 47.40  ? 66  PHE B CG  1 
ATOM   3398 C  CD1 . PHE B 1 66  ? -7.005  -19.903 9.257   1.00 47.67  ? 66  PHE B CD1 1 
ATOM   3399 C  CD2 . PHE B 1 66  ? -6.380  -20.642 11.431  1.00 46.98  ? 66  PHE B CD2 1 
ATOM   3400 C  CE1 . PHE B 1 66  ? -8.043  -19.168 9.809   1.00 46.50  ? 66  PHE B CE1 1 
ATOM   3401 C  CE2 . PHE B 1 66  ? -7.415  -19.901 11.981  1.00 44.74  ? 66  PHE B CE2 1 
ATOM   3402 C  CZ  . PHE B 1 66  ? -8.240  -19.164 11.171  1.00 46.18  ? 66  PHE B CZ  1 
ATOM   3403 N  N   . LEU B 1 67  ? -4.406  -23.823 6.863   1.00 39.44  ? 67  LEU B N   1 
ATOM   3404 C  CA  . LEU B 1 67  ? -3.348  -24.433 6.016   1.00 46.03  ? 67  LEU B CA  1 
ATOM   3405 C  C   . LEU B 1 67  ? -2.646  -23.316 5.230   1.00 45.29  ? 67  LEU B C   1 
ATOM   3406 O  O   . LEU B 1 67  ? -3.279  -22.738 4.325   1.00 47.24  ? 67  LEU B O   1 
ATOM   3407 C  CB  . LEU B 1 67  ? -4.002  -25.468 5.100   1.00 50.09  ? 67  LEU B CB  1 
ATOM   3408 C  CG  . LEU B 1 67  ? -4.826  -26.504 5.861   1.00 57.60  ? 67  LEU B CG  1 
ATOM   3409 C  CD1 . LEU B 1 67  ? -5.982  -27.045 5.031   1.00 61.34  ? 67  LEU B CD1 1 
ATOM   3410 C  CD2 . LEU B 1 67  ? -3.922  -27.622 6.352   1.00 59.42  ? 67  LEU B CD2 1 
ATOM   3411 N  N   . VAL B 1 68  ? -1.410  -23.008 5.626   1.00 39.93  ? 68  VAL B N   1 
ATOM   3412 C  CA  . VAL B 1 68  ? -0.550  -21.944 5.049   1.00 40.37  ? 68  VAL B CA  1 
ATOM   3413 C  C   . VAL B 1 68  ? 0.589   -22.648 4.312   1.00 41.26  ? 68  VAL B C   1 
ATOM   3414 O  O   . VAL B 1 68  ? 1.386   -23.358 4.967   1.00 40.98  ? 68  VAL B O   1 
ATOM   3415 C  CB  . VAL B 1 68  ? -0.022  -20.966 6.113   1.00 39.39  ? 68  VAL B CB  1 
ATOM   3416 C  CG1 . VAL B 1 68  ? 0.809   -19.846 5.496   1.00 42.33  ? 68  VAL B CG1 1 
ATOM   3417 C  CG2 . VAL B 1 68  ? -1.142  -20.384 6.946   1.00 40.28  ? 68  VAL B CG2 1 
ATOM   3418 N  N   . GLN B 1 69  ? 0.626   -22.460 2.996   1.00 39.66  ? 69  GLN B N   1 
ATOM   3419 C  CA  . GLN B 1 69  ? 1.622   -23.066 2.087   1.00 45.00  ? 69  GLN B CA  1 
ATOM   3420 C  C   . GLN B 1 69  ? 2.439   -21.935 1.437   1.00 40.44  ? 69  GLN B C   1 
ATOM   3421 O  O   . GLN B 1 69  ? 1.817   -21.029 0.862   1.00 35.15  ? 69  GLN B O   1 
ATOM   3422 C  CB  . GLN B 1 69  ? 0.866   -23.963 1.113   1.00 46.50  ? 69  GLN B CB  1 
ATOM   3423 C  CG  . GLN B 1 69  ? 1.703   -25.127 0.602   1.00 60.97  ? 69  GLN B CG  1 
ATOM   3424 C  CD  . GLN B 1 69  ? 0.894   -26.201 -0.093  1.00 65.61  ? 69  GLN B CD  1 
ATOM   3425 O  OE1 . GLN B 1 69  ? -0.226  -26.528 0.299   1.00 61.53  ? 69  GLN B OE1 1 
ATOM   3426 N  NE2 . GLN B 1 69  ? 1.463   -26.760 -1.151  1.00 79.87  ? 69  GLN B NE2 1 
ATOM   3427 N  N   . ALA B 1 70  ? 3.766   -21.958 1.613   1.00 35.30  ? 70  ALA B N   1 
ATOM   3428 C  CA  . ALA B 1 70  ? 4.759   -21.145 0.878   1.00 38.99  ? 70  ALA B CA  1 
ATOM   3429 C  C   . ALA B 1 70  ? 5.489   -22.041 -0.132  1.00 43.32  ? 70  ALA B C   1 
ATOM   3430 O  O   . ALA B 1 70  ? 6.309   -22.876 0.295   1.00 49.14  ? 70  ALA B O   1 
ATOM   3431 C  CB  . ALA B 1 70  ? 5.718   -20.484 1.844   1.00 35.43  ? 70  ALA B CB  1 
ATOM   3432 N  N   . GLY B 1 71  ? 5.211   -21.881 -1.428  1.00 49.73  ? 71  GLY B N   1 
ATOM   3433 C  CA  . GLY B 1 71  ? 5.605   -22.858 -2.462  1.00 55.54  ? 71  GLY B CA  1 
ATOM   3434 C  C   . GLY B 1 71  ? 5.075   -24.244 -2.126  1.00 60.91  ? 71  GLY B C   1 
ATOM   3435 O  O   . GLY B 1 71  ? 3.838   -24.390 -2.007  1.00 59.14  ? 71  GLY B O   1 
ATOM   3436 N  N   . ASN B 1 72  ? 5.972   -25.218 -1.936  1.00 67.88  ? 72  ASN B N   1 
ATOM   3437 C  CA  . ASN B 1 72  ? 5.638   -26.643 -1.649  1.00 73.95  ? 72  ASN B CA  1 
ATOM   3438 C  C   . ASN B 1 72  ? 6.032   -26.955 -0.197  1.00 70.10  ? 72  ASN B C   1 
ATOM   3439 O  O   . ASN B 1 72  ? 6.498   -28.066 0.065   1.00 78.77  ? 72  ASN B O   1 
ATOM   3440 C  CB  . ASN B 1 72  ? 6.324   -27.570 -2.663  1.00 81.93  ? 72  ASN B CB  1 
ATOM   3441 C  CG  . ASN B 1 72  ? 5.449   -28.692 -3.188  1.00 91.38  ? 72  ASN B CG  1 
ATOM   3442 O  OD1 . ASN B 1 72  ? 4.235   -28.531 -3.319  1.00 96.77  ? 72  ASN B OD1 1 
ATOM   3443 N  ND2 . ASN B 1 72  ? 6.060   -29.821 -3.531  1.00 91.13  ? 72  ASN B ND2 1 
ATOM   3444 N  N   . VAL B 1 73  ? 5.841   -25.995 0.708   1.00 65.40  ? 73  VAL B N   1 
ATOM   3445 C  CA  . VAL B 1 73  ? 6.273   -26.046 2.135   1.00 62.72  ? 73  VAL B CA  1 
ATOM   3446 C  C   . VAL B 1 73  ? 5.107   -25.555 2.999   1.00 61.37  ? 73  VAL B C   1 
ATOM   3447 O  O   . VAL B 1 73  ? 4.725   -24.382 2.848   1.00 61.01  ? 73  VAL B O   1 
ATOM   3448 C  CB  . VAL B 1 73  ? 7.523   -25.168 2.342   1.00 62.52  ? 73  VAL B CB  1 
ATOM   3449 C  CG1 . VAL B 1 73  ? 7.782   -24.852 3.810   1.00 61.61  ? 73  VAL B CG1 1 
ATOM   3450 C  CG2 . VAL B 1 73  ? 8.747   -25.778 1.685   1.00 60.70  ? 73  VAL B CG2 1 
ATOM   3451 N  N   . GLN B 1 74  ? 4.570   -26.403 3.877   1.00 62.07  ? 74  GLN B N   1 
ATOM   3452 C  CA  . GLN B 1 74  ? 3.567   -25.986 4.893   1.00 60.31  ? 74  GLN B CA  1 
ATOM   3453 C  C   . GLN B 1 74  ? 4.311   -25.137 5.932   1.00 56.42  ? 74  GLN B C   1 
ATOM   3454 O  O   . GLN B 1 74  ? 5.453   -25.516 6.281   1.00 58.02  ? 74  GLN B O   1 
ATOM   3455 C  CB  . GLN B 1 74  ? 2.857   -27.195 5.514   1.00 66.49  ? 74  GLN B CB  1 
ATOM   3456 C  CG  . GLN B 1 74  ? 2.162   -28.110 4.507   1.00 74.70  ? 74  GLN B CG  1 
ATOM   3457 C  CD  . GLN B 1 74  ? 0.951   -27.495 3.844   1.00 84.18  ? 74  GLN B CD  1 
ATOM   3458 O  OE1 . GLN B 1 74  ? 0.938   -27.254 2.638   1.00 90.08  ? 74  GLN B OE1 1 
ATOM   3459 N  NE2 . GLN B 1 74  ? -0.088  -27.243 4.626   1.00 92.43  ? 74  GLN B NE2 1 
ATOM   3460 N  N   . LEU B 1 75  ? 3.754   -23.977 6.304   1.00 49.45  ? 75  LEU B N   1 
ATOM   3461 C  CA  . LEU B 1 75  ? 4.148   -23.208 7.517   1.00 47.26  ? 75  LEU B CA  1 
ATOM   3462 C  C   . LEU B 1 75  ? 3.264   -23.680 8.670   1.00 47.56  ? 75  LEU B C   1 
ATOM   3463 O  O   . LEU B 1 75  ? 2.071   -23.929 8.423   1.00 48.05  ? 75  LEU B O   1 
ATOM   3464 C  CB  . LEU B 1 75  ? 3.956   -21.697 7.331   1.00 47.35  ? 75  LEU B CB  1 
ATOM   3465 C  CG  . LEU B 1 75  ? 4.621   -21.049 6.120   1.00 47.12  ? 75  LEU B CG  1 
ATOM   3466 C  CD1 . LEU B 1 75  ? 4.448   -19.537 6.164   1.00 48.38  ? 75  LEU B CD1 1 
ATOM   3467 C  CD2 . LEU B 1 75  ? 6.095   -21.407 6.031   1.00 47.12  ? 75  LEU B CD2 1 
ATOM   3468 N  N   . ARG B 1 76  ? 3.832   -23.758 9.875   1.00 48.03  ? 76  ARG B N   1 
ATOM   3469 C  CA  . ARG B 1 76  ? 3.119   -24.101 11.128  1.00 46.15  ? 76  ARG B CA  1 
ATOM   3470 C  C   . ARG B 1 76  ? 2.557   -22.806 11.733  1.00 42.86  ? 76  ARG B C   1 
ATOM   3471 O  O   . ARG B 1 76  ? 3.360   -21.896 12.084  1.00 38.24  ? 76  ARG B O   1 
ATOM   3472 C  CB  . ARG B 1 76  ? 4.066   -24.824 12.092  1.00 54.90  ? 76  ARG B CB  1 
ATOM   3473 C  CG  . ARG B 1 76  ? 3.375   -25.402 13.322  1.00 63.06  ? 76  ARG B CG  1 
ATOM   3474 C  CD  . ARG B 1 76  ? 4.315   -26.184 14.223  1.00 70.84  ? 76  ARG B CD  1 
ATOM   3475 N  NE  . ARG B 1 76  ? 4.663   -27.472 13.615  1.00 80.94  ? 76  ARG B NE  1 
ATOM   3476 C  CZ  . ARG B 1 76  ? 3.904   -28.577 13.633  1.00 85.53  ? 76  ARG B CZ  1 
ATOM   3477 N  NH1 . ARG B 1 76  ? 2.721   -28.578 14.234  1.00 87.41  ? 76  ARG B NH1 1 
ATOM   3478 N  NH2 . ARG B 1 76  ? 4.326   -29.681 13.024  1.00 82.24  ? 76  ARG B NH2 1 
ATOM   3479 N  N   . VAL B 1 77  ? 1.232   -22.727 11.837  1.00 37.82  ? 77  VAL B N   1 
ATOM   3480 C  CA  . VAL B 1 77  ? 0.505   -21.605 12.498  1.00 40.12  ? 77  VAL B CA  1 
ATOM   3481 C  C   . VAL B 1 77  ? 0.442   -21.922 13.990  1.00 42.53  ? 77  VAL B C   1 
ATOM   3482 O  O   . VAL B 1 77  ? -0.134  -22.980 14.329  1.00 44.29  ? 77  VAL B O   1 
ATOM   3483 C  CB  . VAL B 1 77  ? -0.918  -21.418 11.944  1.00 38.99  ? 77  VAL B CB  1 
ATOM   3484 C  CG1 . VAL B 1 77  ? -1.626  -20.258 12.616  1.00 40.26  ? 77  VAL B CG1 1 
ATOM   3485 C  CG2 . VAL B 1 77  ? -0.946  -21.272 10.432  1.00 40.34  ? 77  VAL B CG2 1 
ATOM   3486 N  N   . ILE B 1 78  ? 0.989   -21.024 14.814  1.00 40.91  ? 78  ILE B N   1 
ATOM   3487 C  CA  . ILE B 1 78  ? 1.094   -21.138 16.302  1.00 41.86  ? 78  ILE B CA  1 
ATOM   3488 C  C   . ILE B 1 78  ? 0.204   -20.083 16.974  1.00 40.44  ? 78  ILE B C   1 
ATOM   3489 O  O   . ILE B 1 78  ? 0.248   -19.974 18.198  1.00 41.31  ? 78  ILE B O   1 
ATOM   3490 C  CB  . ILE B 1 78  ? 2.565   -20.985 16.748  1.00 40.93  ? 78  ILE B CB  1 
ATOM   3491 C  CG1 . ILE B 1 78  ? 3.100   -19.582 16.445  1.00 43.11  ? 78  ILE B CG1 1 
ATOM   3492 C  CG2 . ILE B 1 78  ? 3.439   -22.063 16.124  1.00 41.60  ? 78  ILE B CG2 1 
ATOM   3493 C  CD1 . ILE B 1 78  ? 4.472   -19.300 17.003  1.00 44.20  ? 78  ILE B CD1 1 
ATOM   3494 N  N   . GLY B 1 79  ? -0.541  -19.287 16.210  1.00 42.31  ? 79  GLY B N   1 
ATOM   3495 C  CA  . GLY B 1 79  ? -1.375  -18.205 16.765  1.00 41.55  ? 79  GLY B CA  1 
ATOM   3496 C  C   . GLY B 1 79  ? -2.241  -17.577 15.691  1.00 44.03  ? 79  GLY B C   1 
ATOM   3497 O  O   . GLY B 1 79  ? -1.805  -17.514 14.521  1.00 43.51  ? 79  GLY B O   1 
ATOM   3498 N  N   . HIS B 1 80  ? -3.439  -17.141 16.061  1.00 43.43  ? 80  HIS B N   1 
ATOM   3499 C  CA  . HIS B 1 80  ? -4.385  -16.466 15.145  1.00 46.63  ? 80  HIS B CA  1 
ATOM   3500 C  C   . HIS B 1 80  ? -5.068  -15.341 15.909  1.00 45.11  ? 80  HIS B C   1 
ATOM   3501 O  O   . HIS B 1 80  ? -5.436  -15.534 17.071  1.00 46.04  ? 80  HIS B O   1 
ATOM   3502 C  CB  . HIS B 1 80  ? -5.371  -17.458 14.516  1.00 48.66  ? 80  HIS B CB  1 
ATOM   3503 C  CG  . HIS B 1 80  ? -6.236  -18.183 15.491  1.00 54.23  ? 80  HIS B CG  1 
ATOM   3504 N  ND1 . HIS B 1 80  ? -5.821  -19.329 16.154  1.00 54.06  ? 80  HIS B ND1 1 
ATOM   3505 C  CD2 . HIS B 1 80  ? -7.508  -17.965 15.880  1.00 58.21  ? 80  HIS B CD2 1 
ATOM   3506 C  CE1 . HIS B 1 80  ? -6.800  -19.764 16.926  1.00 57.36  ? 80  HIS B CE1 1 
ATOM   3507 N  NE2 . HIS B 1 80  ? -7.843  -18.950 16.773  1.00 57.37  ? 80  HIS B NE2 1 
ATOM   3508 N  N   . SER B 1 81  ? -5.180  -14.188 15.275  1.00 37.95  ? 81  SER B N   1 
ATOM   3509 C  CA  . SER B 1 81  ? -5.953  -13.044 15.793  1.00 36.13  ? 81  SER B CA  1 
ATOM   3510 C  C   . SER B 1 81  ? -6.435  -12.217 14.618  1.00 38.68  ? 81  SER B C   1 
ATOM   3511 O  O   . SER B 1 81  ? -5.998  -12.445 13.485  1.00 38.30  ? 81  SER B O   1 
ATOM   3512 C  CB  . SER B 1 81  ? -5.152  -12.195 16.722  1.00 36.01  ? 81  SER B CB  1 
ATOM   3513 O  OG  . SER B 1 81  ? -4.106  -11.562 16.021  1.00 38.55  ? 81  SER B OG  1 
ATOM   3514 N  N   . MET B 1 82  ? -7.322  -11.289 14.916  1.00 40.57  ? 82  MET B N   1 
ATOM   3515 C  CA  . MET B 1 82  ? -7.986  -10.453 13.912  1.00 42.59  ? 82  MET B CA  1 
ATOM   3516 C  C   . MET B 1 82  ? -7.716  -8.995  14.286  1.00 38.66  ? 82  MET B C   1 
ATOM   3517 O  O   . MET B 1 82  ? -7.742  -8.656  15.475  1.00 37.77  ? 82  MET B O   1 
ATOM   3518 C  CB  . MET B 1 82  ? -9.472  -10.816 13.903  1.00 45.46  ? 82  MET B CB  1 
ATOM   3519 C  CG  . MET B 1 82  ? -10.355 -9.867  13.148  1.00 47.02  ? 82  MET B CG  1 
ATOM   3520 S  SD  . MET B 1 82  ? -12.081 -10.409 13.224  1.00 56.51  ? 82  MET B SD  1 
ATOM   3521 C  CE  . MET B 1 82  ? -11.887 -12.160 12.897  1.00 48.26  ? 82  MET B CE  1 
ATOM   3522 N  N   . GLN B 1 83  ? -7.375  -8.190  13.293  1.00 35.79  ? 83  GLN B N   1 
ATOM   3523 C  CA  . GLN B 1 83  ? -7.304  -6.723  13.414  1.00 34.70  ? 83  GLN B CA  1 
ATOM   3524 C  C   . GLN B 1 83  ? -8.233  -6.139  12.352  1.00 33.91  ? 83  GLN B C   1 
ATOM   3525 O  O   . GLN B 1 83  ? -7.949  -6.286  11.147  1.00 31.66  ? 83  GLN B O   1 
ATOM   3526 C  CB  . GLN B 1 83  ? -5.867  -6.243  13.281  1.00 35.21  ? 83  GLN B CB  1 
ATOM   3527 C  CG  . GLN B 1 83  ? -5.776  -4.738  13.412  1.00 35.23  ? 83  GLN B CG  1 
ATOM   3528 C  CD  . GLN B 1 83  ? -4.372  -4.241  13.221  1.00 38.00  ? 83  GLN B CD  1 
ATOM   3529 O  OE1 . GLN B 1 83  ? -3.480  -4.979  12.814  1.00 39.61  ? 83  GLN B OE1 1 
ATOM   3530 N  NE2 . GLN B 1 83  ? -4.178  -2.971  13.522  1.00 40.10  ? 83  GLN B NE2 1 
ATOM   3531 N  N   . ASN B 1 84  ? -9.352  -5.565  12.793  1.00 34.04  ? 84  ASN B N   1 
ATOM   3532 C  CA  . ASN B 1 84  ? -10.392 -5.048  11.881  1.00 31.50  ? 84  ASN B CA  1 
ATOM   3533 C  C   . ASN B 1 84  ? -10.739 -6.175  10.906  1.00 29.65  ? 84  ASN B C   1 
ATOM   3534 O  O   . ASN B 1 84  ? -10.970 -7.310  11.389  1.00 26.88  ? 84  ASN B O   1 
ATOM   3535 C  CB  . ASN B 1 84  ? -9.881  -3.766  11.235  1.00 30.94  ? 84  ASN B CB  1 
ATOM   3536 C  CG  . ASN B 1 84  ? -9.547  -2.733  12.279  1.00 31.66  ? 84  ASN B CG  1 
ATOM   3537 O  OD1 . ASN B 1 84  ? -10.380 -2.422  13.127  1.00 30.23  ? 84  ASN B OD1 1 
ATOM   3538 N  ND2 . ASN B 1 84  ? -8.353  -2.174  12.197  1.00 29.61  ? 84  ASN B ND2 1 
ATOM   3539 N  N   . CYS B 1 85  ? -10.663 -5.931  9.589   1.00 27.44  ? 85  CYS B N   1 
ATOM   3540 C  CA  . CYS B 1 85  ? -11.060 -6.937  8.574   1.00 27.86  ? 85  CYS B CA  1 
ATOM   3541 C  C   . CYS B 1 85  ? -9.885  -7.801  8.106   1.00 27.55  ? 85  CYS B C   1 
ATOM   3542 O  O   . CYS B 1 85  ? -10.059 -8.547  7.134   1.00 27.83  ? 85  CYS B O   1 
ATOM   3543 C  CB  . CYS B 1 85  ? -11.739 -6.275  7.390   1.00 28.16  ? 85  CYS B CB  1 
ATOM   3544 S  SG  . CYS B 1 85  ? -13.185 -5.323  7.899   1.00 28.66  ? 85  CYS B SG  1 
ATOM   3545 N  N   . VAL B 1 86  ? -8.747  -7.759  8.782   1.00 26.73  ? 86  VAL B N   1 
ATOM   3546 C  CA  . VAL B 1 86  ? -7.590  -8.612  8.413   1.00 28.18  ? 86  VAL B CA  1 
ATOM   3547 C  C   . VAL B 1 86  ? -7.348  -9.668  9.494   1.00 29.27  ? 86  VAL B C   1 
ATOM   3548 O  O   . VAL B 1 86  ? -7.330  -9.321  10.684  1.00 32.93  ? 86  VAL B O   1 
ATOM   3549 C  CB  . VAL B 1 86  ? -6.364  -7.729  8.155   1.00 28.72  ? 86  VAL B CB  1 
ATOM   3550 C  CG1 . VAL B 1 86  ? -5.075  -8.485  8.373   1.00 32.60  ? 86  VAL B CG1 1 
ATOM   3551 C  CG2 . VAL B 1 86  ? -6.416  -7.170  6.743   1.00 29.90  ? 86  VAL B CG2 1 
ATOM   3552 N  N   . LEU B 1 87  ? -7.142  -10.910 9.069   1.00 29.20  ? 87  LEU B N   1 
ATOM   3553 C  CA  . LEU B 1 87  ? -6.698  -12.033 9.928   1.00 32.70  ? 87  LEU B CA  1 
ATOM   3554 C  C   . LEU B 1 87  ? -5.164  -12.036 9.987   1.00 31.74  ? 87  LEU B C   1 
ATOM   3555 O  O   . LEU B 1 87  ? -4.546  -11.835 8.936   1.00 29.43  ? 87  LEU B O   1 
ATOM   3556 C  CB  . LEU B 1 87  ? -7.270  -13.319 9.322   1.00 34.78  ? 87  LEU B CB  1 
ATOM   3557 C  CG  . LEU B 1 87  ? -7.095  -14.587 10.141  1.00 39.15  ? 87  LEU B CG  1 
ATOM   3558 C  CD1 . LEU B 1 87  ? -7.829  -14.484 11.478  1.00 40.99  ? 87  LEU B CD1 1 
ATOM   3559 C  CD2 . LEU B 1 87  ? -7.612  -15.779 9.353   1.00 42.25  ? 87  LEU B CD2 1 
ATOM   3560 N  N   . LYS B 1 88  ? -4.584  -12.165 11.184  1.00 30.83  ? 88  LYS B N   1 
ATOM   3561 C  CA  . LYS B 1 88  ? -3.122  -12.260 11.409  1.00 33.37  ? 88  LYS B CA  1 
ATOM   3562 C  C   . LYS B 1 88  ? -2.812  -13.659 11.940  1.00 34.17  ? 88  LYS B C   1 
ATOM   3563 O  O   . LYS B 1 88  ? -3.239  -13.982 13.064  1.00 39.37  ? 88  LYS B O   1 
ATOM   3564 C  CB  . LYS B 1 88  ? -2.658  -11.149 12.345  1.00 32.47  ? 88  LYS B CB  1 
ATOM   3565 C  CG  . LYS B 1 88  ? -2.943  -9.744  11.824  1.00 35.73  ? 88  LYS B CG  1 
ATOM   3566 C  CD  . LYS B 1 88  ? -2.214  -8.646  12.575  1.00 37.66  ? 88  LYS B CD  1 
ATOM   3567 C  CE  . LYS B 1 88  ? -2.491  -8.641  14.054  1.00 42.27  ? 88  LYS B CE  1 
ATOM   3568 N  NZ  . LYS B 1 88  ? -1.895  -7.448  14.706  1.00 46.46  ? 88  LYS B NZ  1 
ATOM   3569 N  N   . LEU B 1 89  ? -2.190  -14.489 11.109  1.00 32.26  ? 89  LEU B N   1 
ATOM   3570 C  CA  . LEU B 1 89  ? -1.805  -15.871 11.471  1.00 32.13  ? 89  LEU B CA  1 
ATOM   3571 C  C   . LEU B 1 89  ? -0.320  -15.869 11.804  1.00 32.83  ? 89  LEU B C   1 
ATOM   3572 O  O   . LEU B 1 89  ? 0.505   -15.753 10.879  1.00 30.28  ? 89  LEU B O   1 
ATOM   3573 C  CB  . LEU B 1 89  ? -2.141  -16.824 10.323  1.00 34.17  ? 89  LEU B CB  1 
ATOM   3574 C  CG  . LEU B 1 89  ? -3.625  -16.906 9.965   1.00 36.21  ? 89  LEU B CG  1 
ATOM   3575 C  CD1 . LEU B 1 89  ? -3.865  -17.906 8.843   1.00 38.32  ? 89  LEU B CD1 1 
ATOM   3576 C  CD2 . LEU B 1 89  ? -4.467  -17.270 11.177  1.00 37.09  ? 89  LEU B CD2 1 
ATOM   3577 N  N   . LYS B 1 90  ? -0.002  -15.919 13.097  1.00 34.83  ? 90  LYS B N   1 
ATOM   3578 C  CA  . LYS B 1 90  ? 1.384   -16.052 13.599  1.00 37.76  ? 90  LYS B CA  1 
ATOM   3579 C  C   . LYS B 1 90  ? 1.889   -17.448 13.231  1.00 36.58  ? 90  LYS B C   1 
ATOM   3580 O  O   . LYS B 1 90  ? 1.142   -18.414 13.455  1.00 34.01  ? 90  LYS B O   1 
ATOM   3581 C  CB  . LYS B 1 90  ? 1.441   -15.822 15.110  1.00 44.49  ? 90  LYS B CB  1 
ATOM   3582 C  CG  . LYS B 1 90  ? 2.856   -15.859 15.658  1.00 53.48  ? 90  LYS B CG  1 
ATOM   3583 C  CD  . LYS B 1 90  ? 3.039   -15.127 16.965  1.00 61.75  ? 90  LYS B CD  1 
ATOM   3584 C  CE  . LYS B 1 90  ? 4.486   -15.127 17.415  1.00 68.94  ? 90  LYS B CE  1 
ATOM   3585 N  NZ  . LYS B 1 90  ? 4.691   -14.323 18.640  1.00 73.27  ? 90  LYS B NZ  1 
ATOM   3586 N  N   . VAL B 1 91  ? 3.091   -17.537 12.656  1.00 35.57  ? 91  VAL B N   1 
ATOM   3587 C  CA  . VAL B 1 91  ? 3.677   -18.811 12.144  1.00 36.29  ? 91  VAL B CA  1 
ATOM   3588 C  C   . VAL B 1 91  ? 4.997   -19.044 12.874  1.00 35.70  ? 91  VAL B C   1 
ATOM   3589 O  O   . VAL B 1 91  ? 5.535   -18.070 13.437  1.00 33.36  ? 91  VAL B O   1 
ATOM   3590 C  CB  . VAL B 1 91  ? 3.846   -18.789 10.610  1.00 38.28  ? 91  VAL B CB  1 
ATOM   3591 C  CG1 . VAL B 1 91  ? 2.501   -18.860 9.919   1.00 37.78  ? 91  VAL B CG1 1 
ATOM   3592 C  CG2 . VAL B 1 91  ? 4.641   -17.581 10.111  1.00 40.64  ? 91  VAL B CG2 1 
ATOM   3593 N  N   . ASP B 1 92  ? 5.514   -20.271 12.861  1.00 37.75  ? 92  ASP B N   1 
ATOM   3594 C  CA  . ASP B 1 92  ? 6.701   -20.638 13.684  1.00 42.10  ? 92  ASP B CA  1 
ATOM   3595 C  C   . ASP B 1 92  ? 7.984   -20.107 13.036  1.00 46.96  ? 92  ASP B C   1 
ATOM   3596 O  O   . ASP B 1 92  ? 9.031   -20.200 13.687  1.00 52.86  ? 92  ASP B O   1 
ATOM   3597 C  CB  . ASP B 1 92  ? 6.800   -22.151 13.918  1.00 45.86  ? 92  ASP B CB  1 
ATOM   3598 C  CG  . ASP B 1 92  ? 7.158   -22.983 12.692  1.00 50.20  ? 92  ASP B CG  1 
ATOM   3599 O  OD1 . ASP B 1 92  ? 7.327   -22.403 11.598  1.00 53.69  ? 92  ASP B OD1 1 
ATOM   3600 O  OD2 . ASP B 1 92  ? 7.256   -24.221 12.835  1.00 59.84  ? 92  ASP B OD2 1 
ATOM   3601 N  N   . THR B 1 93  ? 7.925   -19.602 11.798  1.00 46.29  ? 93  THR B N   1 
ATOM   3602 C  CA  . THR B 1 93  ? 9.124   -19.241 10.996  1.00 41.36  ? 93  THR B CA  1 
ATOM   3603 C  C   . THR B 1 93  ? 8.970   -17.848 10.378  1.00 40.53  ? 93  THR B C   1 
ATOM   3604 O  O   . THR B 1 93  ? 7.934   -17.577 9.753   1.00 38.15  ? 93  THR B O   1 
ATOM   3605 C  CB  . THR B 1 93  ? 9.376   -20.289 9.915   1.00 43.84  ? 93  THR B CB  1 
ATOM   3606 O  OG1 . THR B 1 93  ? 9.587   -21.488 10.654  1.00 49.46  ? 93  THR B OG1 1 
ATOM   3607 C  CG2 . THR B 1 93  ? 10.570  -19.966 9.045   1.00 48.42  ? 93  THR B CG2 1 
ATOM   3608 N  N   . ALA B 1 94  ? 9.988   -17.006 10.553  1.00 37.70  ? 94  ALA B N   1 
ATOM   3609 C  CA  . ALA B 1 94  ? 10.085  -15.670 9.944   1.00 37.96  ? 94  ALA B CA  1 
ATOM   3610 C  C   . ALA B 1 94  ? 10.388  -15.841 8.455   1.00 41.40  ? 94  ALA B C   1 
ATOM   3611 O  O   . ALA B 1 94  ? 11.108  -16.800 8.083   1.00 39.30  ? 94  ALA B O   1 
ATOM   3612 C  CB  . ALA B 1 94  ? 11.131  -14.841 10.649  1.00 39.01  ? 94  ALA B CB  1 
ATOM   3613 N  N   . ASN B 1 95  ? 9.818   -14.970 7.620   1.00 40.84  ? 95  ASN B N   1 
ATOM   3614 C  CA  . ASN B 1 95  ? 10.065  -15.007 6.159   1.00 36.25  ? 95  ASN B CA  1 
ATOM   3615 C  C   . ASN B 1 95  ? 11.514  -14.580 5.934   1.00 34.67  ? 95  ASN B C   1 
ATOM   3616 O  O   . ASN B 1 95  ? 11.850  -13.426 6.173   1.00 33.68  ? 95  ASN B O   1 
ATOM   3617 C  CB  . ASN B 1 95  ? 9.045   -14.157 5.398   1.00 37.58  ? 95  ASN B CB  1 
ATOM   3618 C  CG  . ASN B 1 95  ? 9.179   -14.318 3.902   1.00 34.64  ? 95  ASN B CG  1 
ATOM   3619 O  OD1 . ASN B 1 95  ? 10.093  -14.999 3.450   1.00 31.47  ? 95  ASN B OD1 1 
ATOM   3620 N  ND2 . ASN B 1 95  ? 8.288   -13.692 3.145   1.00 31.78  ? 95  ASN B ND2 1 
ATOM   3621 N  N   . PRO B 1 96  ? 12.421  -15.475 5.468   1.00 31.32  ? 96  PRO B N   1 
ATOM   3622 C  CA  . PRO B 1 96  ? 13.804  -15.072 5.248   1.00 33.55  ? 96  PRO B CA  1 
ATOM   3623 C  C   . PRO B 1 96  ? 13.856  -14.089 4.062   1.00 36.35  ? 96  PRO B C   1 
ATOM   3624 O  O   . PRO B 1 96  ? 14.842  -13.420 3.894   1.00 35.82  ? 96  PRO B O   1 
ATOM   3625 C  CB  . PRO B 1 96  ? 14.506  -16.404 4.945   1.00 35.24  ? 96  PRO B CB  1 
ATOM   3626 C  CG  . PRO B 1 96  ? 13.408  -17.247 4.304   1.00 33.72  ? 96  PRO B CG  1 
ATOM   3627 C  CD  . PRO B 1 96  ? 12.155  -16.866 5.059   1.00 30.84  ? 96  PRO B CD  1 
ATOM   3628 N  N   . LYS B 1 97  ? 12.790  -14.014 3.265   1.00 35.88  ? 97  LYS B N   1 
ATOM   3629 C  CA  . LYS B 1 97  ? 12.692  -13.057 2.138   1.00 36.80  ? 97  LYS B CA  1 
ATOM   3630 C  C   . LYS B 1 97  ? 11.990  -11.757 2.572   1.00 35.94  ? 97  LYS B C   1 
ATOM   3631 O  O   . LYS B 1 97  ? 11.765  -10.907 1.699   1.00 38.37  ? 97  LYS B O   1 
ATOM   3632 C  CB  . LYS B 1 97  ? 11.971  -13.744 0.975   1.00 38.76  ? 97  LYS B CB  1 
ATOM   3633 C  CG  . LYS B 1 97  ? 12.597  -15.058 0.527   1.00 43.14  ? 97  LYS B CG  1 
ATOM   3634 C  CD  . LYS B 1 97  ? 12.428  -15.329 -0.954  1.00 48.34  ? 97  LYS B CD  1 
ATOM   3635 C  CE  . LYS B 1 97  ? 12.689  -16.767 -1.342  1.00 51.53  ? 97  LYS B CE  1 
ATOM   3636 N  NZ  . LYS B 1 97  ? 11.534  -17.621 -0.978  1.00 53.50  ? 97  LYS B NZ  1 
ATOM   3637 N  N   . THR B 1 98  ? 11.667  -11.566 3.852   1.00 32.58  ? 98  THR B N   1 
ATOM   3638 C  CA  . THR B 1 98  ? 11.012  -10.321 4.333   1.00 32.27  ? 98  THR B CA  1 
ATOM   3639 C  C   . THR B 1 98  ? 11.840  -9.123  3.867   1.00 32.52  ? 98  THR B C   1 
ATOM   3640 O  O   . THR B 1 98  ? 13.023  -9.008  4.208   1.00 32.95  ? 98  THR B O   1 
ATOM   3641 C  CB  . THR B 1 98  ? 10.834  -10.306 5.859   1.00 32.10  ? 98  THR B CB  1 
ATOM   3642 O  OG1 . THR B 1 98  ? 10.025  -11.430 6.190   1.00 32.84  ? 98  THR B OG1 1 
ATOM   3643 C  CG2 . THR B 1 98  ? 10.181  -9.036  6.370   1.00 31.14  ? 98  THR B CG2 1 
ATOM   3644 N  N   . PRO B 1 99  ? 11.272  -8.194  3.067   1.00 28.10  ? 99  PRO B N   1 
ATOM   3645 C  CA  . PRO B 1 99  ? 11.976  -6.950  2.745   1.00 28.98  ? 99  PRO B CA  1 
ATOM   3646 C  C   . PRO B 1 99  ? 11.807  -5.871  3.816   1.00 30.01  ? 99  PRO B C   1 
ATOM   3647 O  O   . PRO B 1 99  ? 10.971  -6.018  4.670   1.00 28.78  ? 99  PRO B O   1 
ATOM   3648 C  CB  . PRO B 1 99  ? 11.266  -6.519  1.459   1.00 30.76  ? 99  PRO B CB  1 
ATOM   3649 C  CG  . PRO B 1 99  ? 9.827   -6.944  1.716   1.00 30.19  ? 99  PRO B CG  1 
ATOM   3650 C  CD  . PRO B 1 99  ? 9.965   -8.293  2.400   1.00 29.52  ? 99  PRO B CD  1 
ATOM   3651 N  N   . LYS B 1 100 ? 12.605  -4.809  3.742   1.00 30.24  ? 100 LYS B N   1 
ATOM   3652 C  CA  . LYS B 1 100 ? 12.360  -3.552  4.490   1.00 33.24  ? 100 LYS B CA  1 
ATOM   3653 C  C   . LYS B 1 100 ? 10.965  -3.056  4.072   1.00 32.87  ? 100 LYS B C   1 
ATOM   3654 O  O   . LYS B 1 100 ? 10.736  -2.909  2.847   1.00 29.51  ? 100 LYS B O   1 
ATOM   3655 C  CB  . LYS B 1 100 ? 13.493  -2.556  4.197   1.00 39.18  ? 100 LYS B CB  1 
ATOM   3656 C  CG  . LYS B 1 100 ? 13.391  -1.211  4.909   1.00 49.59  ? 100 LYS B CG  1 
ATOM   3657 C  CD  . LYS B 1 100 ? 14.484  -0.222  4.515   1.00 58.07  ? 100 LYS B CD  1 
ATOM   3658 C  CE  . LYS B 1 100 ? 14.440  1.078   5.294   1.00 62.80  ? 100 LYS B CE  1 
ATOM   3659 N  NZ  . LYS B 1 100 ? 15.008  0.909   6.655   1.00 68.72  ? 100 LYS B NZ  1 
ATOM   3660 N  N   . TYR B 1 101 ? 10.038  -2.881  5.019   1.00 28.32  ? 101 TYR B N   1 
ATOM   3661 C  CA  . TYR B 1 101 ? 8.622   -2.576  4.694   1.00 28.95  ? 101 TYR B CA  1 
ATOM   3662 C  C   . TYR B 1 101 ? 7.978   -1.731  5.796   1.00 30.94  ? 101 TYR B C   1 
ATOM   3663 O  O   . TYR B 1 101 ? 8.439   -1.741  6.963   1.00 28.28  ? 101 TYR B O   1 
ATOM   3664 C  CB  . TYR B 1 101 ? 7.850   -3.875  4.427   1.00 26.71  ? 101 TYR B CB  1 
ATOM   3665 C  CG  . TYR B 1 101 ? 7.383   -4.578  5.674   1.00 27.71  ? 101 TYR B CG  1 
ATOM   3666 C  CD1 . TYR B 1 101 ? 6.196   -4.214  6.289   1.00 25.92  ? 101 TYR B CD1 1 
ATOM   3667 C  CD2 . TYR B 1 101 ? 8.142   -5.576  6.271   1.00 28.68  ? 101 TYR B CD2 1 
ATOM   3668 C  CE1 . TYR B 1 101 ? 5.763   -4.843  7.442   1.00 27.63  ? 101 TYR B CE1 1 
ATOM   3669 C  CE2 . TYR B 1 101 ? 7.734   -6.196  7.445   1.00 28.30  ? 101 TYR B CE2 1 
ATOM   3670 C  CZ  . TYR B 1 101 ? 6.533   -5.832  8.029   1.00 28.21  ? 101 TYR B CZ  1 
ATOM   3671 O  OH  . TYR B 1 101 ? 6.122   -6.423  9.192   1.00 31.96  ? 101 TYR B OH  1 
ATOM   3672 N  N   . LYS B 1 102 ? 6.964   -0.964  5.398   1.00 30.45  ? 102 LYS B N   1 
ATOM   3673 C  CA  . LYS B 1 102 ? 5.971   -0.336  6.300   1.00 33.51  ? 102 LYS B CA  1 
ATOM   3674 C  C   . LYS B 1 102 ? 4.570   -0.679  5.783   1.00 31.30  ? 102 LYS B C   1 
ATOM   3675 O  O   . LYS B 1 102 ? 4.410   -0.955  4.566   1.00 27.57  ? 102 LYS B O   1 
ATOM   3676 C  CB  . LYS B 1 102 ? 6.021   1.198   6.327   1.00 38.16  ? 102 LYS B CB  1 
ATOM   3677 C  CG  . LYS B 1 102 ? 7.372   1.869   6.174   1.00 48.11  ? 102 LYS B CG  1 
ATOM   3678 C  CD  . LYS B 1 102 ? 7.261   3.390   6.056   1.00 48.39  ? 102 LYS B CD  1 
ATOM   3679 C  CE  . LYS B 1 102 ? 8.572   4.024   5.633   1.00 56.71  ? 102 LYS B CE  1 
ATOM   3680 N  NZ  . LYS B 1 102 ? 8.427   5.451   5.259   1.00 60.80  ? 102 LYS B NZ  1 
ATOM   3681 N  N   . PHE B 1 103 ? 3.584   -0.573  6.669   1.00 28.30  ? 103 PHE B N   1 
ATOM   3682 C  CA  . PHE B 1 103 ? 2.141   -0.491  6.335   1.00 27.12  ? 103 PHE B CA  1 
ATOM   3683 C  C   . PHE B 1 103 ? 1.749   0.984   6.244   1.00 26.60  ? 103 PHE B C   1 
ATOM   3684 O  O   . PHE B 1 103 ? 1.964   1.754   7.186   1.00 26.93  ? 103 PHE B O   1 
ATOM   3685 C  CB  . PHE B 1 103 ? 1.308   -1.212  7.393   1.00 28.04  ? 103 PHE B CB  1 
ATOM   3686 C  CG  . PHE B 1 103 ? 1.454   -2.714  7.425   1.00 27.53  ? 103 PHE B CG  1 
ATOM   3687 C  CD1 . PHE B 1 103 ? 2.096   -3.404  6.408   1.00 26.45  ? 103 PHE B CD1 1 
ATOM   3688 C  CD2 . PHE B 1 103 ? 0.905   -3.444  8.470   1.00 28.81  ? 103 PHE B CD2 1 
ATOM   3689 C  CE1 . PHE B 1 103 ? 2.214   -4.786  6.449   1.00 27.82  ? 103 PHE B CE1 1 
ATOM   3690 C  CE2 . PHE B 1 103 ? 1.002   -4.833  8.491   1.00 28.87  ? 103 PHE B CE2 1 
ATOM   3691 C  CZ  . PHE B 1 103 ? 1.643   -5.502  7.476   1.00 28.17  ? 103 PHE B CZ  1 
ATOM   3692 N  N   . VAL B 1 104 ? 1.199   1.391   5.113   1.00 25.54  ? 104 VAL B N   1 
ATOM   3693 C  CA  . VAL B 1 104 ? 0.838   2.809   4.866   1.00 28.70  ? 104 VAL B CA  1 
ATOM   3694 C  C   . VAL B 1 104 ? -0.608  2.835   4.400   1.00 30.01  ? 104 VAL B C   1 
ATOM   3695 O  O   . VAL B 1 104 ? -1.046  1.848   3.756   1.00 32.24  ? 104 VAL B O   1 
ATOM   3696 C  CB  . VAL B 1 104 ? 1.823   3.436   3.863   1.00 34.11  ? 104 VAL B CB  1 
ATOM   3697 C  CG1 . VAL B 1 104 ? 1.287   4.700   3.227   1.00 39.69  ? 104 VAL B CG1 1 
ATOM   3698 C  CG2 . VAL B 1 104 ? 3.166   3.701   4.537   1.00 32.71  ? 104 VAL B CG2 1 
ATOM   3699 N  N   . ARG B 1 105 ? -1.344  3.880   4.775   1.00 27.82  ? 105 ARG B N   1 
ATOM   3700 C  CA  . ARG B 1 105 ? -2.724  4.098   4.282   1.00 29.82  ? 105 ARG B CA  1 
ATOM   3701 C  C   . ARG B 1 105 ? -2.618  5.233   3.270   1.00 30.49  ? 105 ARG B C   1 
ATOM   3702 O  O   . ARG B 1 105 ? -1.989  6.236   3.613   1.00 35.07  ? 105 ARG B O   1 
ATOM   3703 C  CB  . ARG B 1 105 ? -3.715  4.382   5.419   1.00 30.67  ? 105 ARG B CB  1 
ATOM   3704 C  CG  . ARG B 1 105 ? -5.151  4.522   4.922   1.00 30.36  ? 105 ARG B CG  1 
ATOM   3705 C  CD  . ARG B 1 105 ? -6.208  4.587   6.001   1.00 29.06  ? 105 ARG B CD  1 
ATOM   3706 N  NE  . ARG B 1 105 ? -7.528  4.714   5.423   1.00 27.40  ? 105 ARG B NE  1 
ATOM   3707 C  CZ  . ARG B 1 105 ? -8.347  3.705   5.100   1.00 30.08  ? 105 ARG B CZ  1 
ATOM   3708 N  NH1 . ARG B 1 105 ? -8.006  2.446   5.308   1.00 27.53  ? 105 ARG B NH1 1 
ATOM   3709 N  NH2 . ARG B 1 105 ? -9.532  3.957   4.572   1.00 30.56  ? 105 ARG B NH2 1 
ATOM   3710 N  N   . ILE B 1 106 ? -3.131  5.051   2.055   1.00 30.33  ? 106 ILE B N   1 
ATOM   3711 C  CA  . ILE B 1 106 ? -3.007  6.084   0.985   1.00 30.99  ? 106 ILE B CA  1 
ATOM   3712 C  C   . ILE B 1 106 ? -4.296  6.903   0.893   1.00 30.52  ? 106 ILE B C   1 
ATOM   3713 O  O   . ILE B 1 106 ? -5.318  6.450   1.402   1.00 26.97  ? 106 ILE B O   1 
ATOM   3714 C  CB  . ILE B 1 106 ? -2.640  5.453   -0.368  1.00 33.08  ? 106 ILE B CB  1 
ATOM   3715 C  CG1 . ILE B 1 106 ? -3.689  4.431   -0.814  1.00 32.99  ? 106 ILE B CG1 1 
ATOM   3716 C  CG2 . ILE B 1 106 ? -1.235  4.884   -0.302  1.00 31.53  ? 106 ILE B CG2 1 
ATOM   3717 C  CD1 . ILE B 1 106 ? -3.432  3.876   -2.184  1.00 35.66  ? 106 ILE B CD1 1 
ATOM   3718 N  N   . GLN B 1 107 ? -4.185  8.070   0.263   1.00 32.45  ? 107 GLN B N   1 
ATOM   3719 C  CA  . GLN B 1 107 ? -5.268  9.039   -0.036  1.00 35.98  ? 107 GLN B CA  1 
ATOM   3720 C  C   . GLN B 1 107 ? -5.833  8.739   -1.420  1.00 33.29  ? 107 GLN B C   1 
ATOM   3721 O  O   . GLN B 1 107 ? -5.106  8.268   -2.290  1.00 31.23  ? 107 GLN B O   1 
ATOM   3722 C  CB  . GLN B 1 107 ? -4.696  10.460  -0.037  1.00 38.52  ? 107 GLN B CB  1 
ATOM   3723 C  CG  . GLN B 1 107 ? -4.126  10.903  1.306   1.00 46.13  ? 107 GLN B CG  1 
ATOM   3724 C  CD  . GLN B 1 107 ? -5.168  10.742  2.380   1.00 49.52  ? 107 GLN B CD  1 
ATOM   3725 O  OE1 . GLN B 1 107 ? -6.341  11.061  2.186   1.00 53.93  ? 107 GLN B OE1 1 
ATOM   3726 N  NE2 . GLN B 1 107 ? -4.747  10.217  3.519   1.00 60.75  ? 107 GLN B NE2 1 
ATOM   3727 N  N   . PRO B 1 108 ? -7.133  9.007   -1.662  1.00 33.20  ? 108 PRO B N   1 
ATOM   3728 C  CA  . PRO B 1 108 ? -7.698  8.969   -3.011  1.00 36.39  ? 108 PRO B CA  1 
ATOM   3729 C  C   . PRO B 1 108 ? -6.876  9.828   -3.978  1.00 32.20  ? 108 PRO B C   1 
ATOM   3730 O  O   . PRO B 1 108 ? -6.484  10.890  -3.579  1.00 32.69  ? 108 PRO B O   1 
ATOM   3731 C  CB  . PRO B 1 108 ? -9.098  9.594   -2.865  1.00 38.00  ? 108 PRO B CB  1 
ATOM   3732 C  CG  . PRO B 1 108 ? -9.442  9.416   -1.413  1.00 36.67  ? 108 PRO B CG  1 
ATOM   3733 C  CD  . PRO B 1 108 ? -8.124  9.418   -0.662  1.00 33.43  ? 108 PRO B CD  1 
ATOM   3734 N  N   . GLY B 1 109 ? -6.668  9.358   -5.208  1.00 30.87  ? 109 GLY B N   1 
ATOM   3735 C  CA  . GLY B 1 109 ? -5.808  10.013  -6.206  1.00 28.34  ? 109 GLY B CA  1 
ATOM   3736 C  C   . GLY B 1 109 ? -4.389  9.477   -6.171  1.00 30.25  ? 109 GLY B C   1 
ATOM   3737 O  O   . GLY B 1 109 ? -3.660  9.702   -7.168  1.00 31.56  ? 109 GLY B O   1 
ATOM   3738 N  N   . GLN B 1 110 ? -3.976  8.805   -5.086  1.00 29.84  ? 110 GLN B N   1 
ATOM   3739 C  CA  . GLN B 1 110 ? -2.604  8.207   -5.003  1.00 32.08  ? 110 GLN B CA  1 
ATOM   3740 C  C   . GLN B 1 110 ? -2.615  6.890   -5.785  1.00 28.34  ? 110 GLN B C   1 
ATOM   3741 O  O   . GLN B 1 110 ? -3.675  6.259   -5.873  1.00 27.26  ? 110 GLN B O   1 
ATOM   3742 C  CB  . GLN B 1 110 ? -2.104  8.064   -3.560  1.00 36.55  ? 110 GLN B CB  1 
ATOM   3743 C  CG  . GLN B 1 110 ? -1.685  9.403   -2.955  1.00 44.87  ? 110 GLN B CG  1 
ATOM   3744 C  CD  . GLN B 1 110 ? -1.203  9.342   -1.517  1.00 55.83  ? 110 GLN B CD  1 
ATOM   3745 O  OE1 . GLN B 1 110 ? -1.601  8.489   -0.717  1.00 58.14  ? 110 GLN B OE1 1 
ATOM   3746 N  NE2 . GLN B 1 110 ? -0.340  10.283  -1.153  1.00 65.83  ? 110 GLN B NE2 1 
ATOM   3747 N  N   . THR B 1 111 ? -1.485  6.531   -6.393  1.00 27.06  ? 111 THR B N   1 
ATOM   3748 C  CA  . THR B 1 111 ? -1.372  5.326   -7.253  1.00 26.03  ? 111 THR B CA  1 
ATOM   3749 C  C   . THR B 1 111 ? -0.557  4.259   -6.517  1.00 25.39  ? 111 THR B C   1 
ATOM   3750 O  O   . THR B 1 111 ? 0.101   4.561   -5.520  1.00 24.27  ? 111 THR B O   1 
ATOM   3751 C  CB  . THR B 1 111 ? -0.768  5.653   -8.617  1.00 25.44  ? 111 THR B CB  1 
ATOM   3752 O  OG1 . THR B 1 111 ? 0.477   6.318   -8.401  1.00 28.04  ? 111 THR B OG1 1 
ATOM   3753 C  CG2 . THR B 1 111 ? -1.691  6.499   -9.453  1.00 26.49  ? 111 THR B CG2 1 
ATOM   3754 N  N   . PHE B 1 112 ? -0.615  3.033   -7.002  1.00 25.29  ? 112 PHE B N   1 
ATOM   3755 C  CA  . PHE B 1 112 ? 0.157   1.916   -6.422  1.00 25.45  ? 112 PHE B CA  1 
ATOM   3756 C  C   . PHE B 1 112 ? 0.106   0.755   -7.399  1.00 23.63  ? 112 PHE B C   1 
ATOM   3757 O  O   . PHE B 1 112 ? -0.710  0.766   -8.329  1.00 21.49  ? 112 PHE B O   1 
ATOM   3758 C  CB  . PHE B 1 112 ? -0.388  1.509   -5.055  1.00 25.05  ? 112 PHE B CB  1 
ATOM   3759 C  CG  . PHE B 1 112 ? -1.843  1.103   -5.038  1.00 27.20  ? 112 PHE B CG  1 
ATOM   3760 C  CD1 . PHE B 1 112 ? -2.848  2.045   -4.895  1.00 28.07  ? 112 PHE B CD1 1 
ATOM   3761 C  CD2 . PHE B 1 112 ? -2.205  -0.229  -5.108  1.00 27.27  ? 112 PHE B CD2 1 
ATOM   3762 C  CE1 . PHE B 1 112 ? -4.181  1.661   -4.822  1.00 29.05  ? 112 PHE B CE1 1 
ATOM   3763 C  CE2 . PHE B 1 112 ? -3.533  -0.611  -5.049  1.00 28.73  ? 112 PHE B CE2 1 
ATOM   3764 C  CZ  . PHE B 1 112 ? -4.521  0.332   -4.910  1.00 29.85  ? 112 PHE B CZ  1 
ATOM   3765 N  N   . SER B 1 113 ? 0.984   -0.197  -7.160  1.00 23.19  ? 113 SER B N   1 
ATOM   3766 C  CA  . SER B 1 113 ? 1.134   -1.428  -7.962  1.00 24.29  ? 113 SER B CA  1 
ATOM   3767 C  C   . SER B 1 113 ? 0.391   -2.550  -7.265  1.00 24.44  ? 113 SER B C   1 
ATOM   3768 O  O   . SER B 1 113 ? 0.512   -2.661  -6.053  1.00 24.13  ? 113 SER B O   1 
ATOM   3769 C  CB  . SER B 1 113 ? 2.579   -1.782  -8.128  1.00 25.58  ? 113 SER B CB  1 
ATOM   3770 O  OG  . SER B 1 113 ? 3.237   -0.781  -8.871  1.00 30.89  ? 113 SER B OG  1 
ATOM   3771 N  N   . VAL B 1 114 ? -0.336  -3.353  -8.029  1.00 26.42  ? 114 VAL B N   1 
ATOM   3772 C  CA  . VAL B 1 114 ? -1.063  -4.547  -7.530  1.00 26.97  ? 114 VAL B CA  1 
ATOM   3773 C  C   . VAL B 1 114 ? -0.337  -5.776  -8.079  1.00 28.81  ? 114 VAL B C   1 
ATOM   3774 O  O   . VAL B 1 114 ? -0.175  -5.869  -9.328  1.00 26.82  ? 114 VAL B O   1 
ATOM   3775 C  CB  . VAL B 1 114 ? -2.527  -4.510  -7.996  1.00 29.49  ? 114 VAL B CB  1 
ATOM   3776 C  CG1 . VAL B 1 114 ? -3.241  -5.821  -7.720  1.00 29.90  ? 114 VAL B CG1 1 
ATOM   3777 C  CG2 . VAL B 1 114 ? -3.279  -3.337  -7.380  1.00 31.00  ? 114 VAL B CG2 1 
ATOM   3778 N  N   . LEU B 1 115 ? 0.028   -6.703  -7.201  1.00 26.70  ? 115 LEU B N   1 
ATOM   3779 C  CA  . LEU B 1 115 ? 0.486   -8.042  -7.620  1.00 24.50  ? 115 LEU B CA  1 
ATOM   3780 C  C   . LEU B 1 115 ? -0.693  -9.018  -7.508  1.00 26.41  ? 115 LEU B C   1 
ATOM   3781 O  O   . LEU B 1 115 ? -0.920  -9.608  -6.426  1.00 23.28  ? 115 LEU B O   1 
ATOM   3782 C  CB  . LEU B 1 115 ? 1.673   -8.428  -6.743  1.00 26.09  ? 115 LEU B CB  1 
ATOM   3783 C  CG  . LEU B 1 115 ? 2.363   -9.718  -7.144  1.00 24.53  ? 115 LEU B CG  1 
ATOM   3784 C  CD1 . LEU B 1 115 ? 2.922   -9.596  -8.538  1.00 23.78  ? 115 LEU B CD1 1 
ATOM   3785 C  CD2 . LEU B 1 115 ? 3.447   -10.070 -6.151  1.00 24.82  ? 115 LEU B CD2 1 
ATOM   3786 N  N   . ALA B 1 116 ? -1.447  -9.180  -8.594  1.00 27.53  ? 116 ALA B N   1 
ATOM   3787 C  CA  . ALA B 1 116 ? -2.549  -10.159 -8.655  1.00 29.21  ? 116 ALA B CA  1 
ATOM   3788 C  C   . ALA B 1 116 ? -1.937  -11.545 -8.464  1.00 31.35  ? 116 ALA B C   1 
ATOM   3789 O  O   . ALA B 1 116 ? -0.943  -11.840 -9.164  1.00 33.25  ? 116 ALA B O   1 
ATOM   3790 C  CB  . ALA B 1 116 ? -3.289  -10.045 -9.956  1.00 30.14  ? 116 ALA B CB  1 
ATOM   3791 N  N   . CYS B 1 117 ? -2.453  -12.317 -7.505  1.00 32.30  ? 117 CYS B N   1 
ATOM   3792 C  CA  . CYS B 1 117 ? -2.021  -13.711 -7.206  1.00 33.38  ? 117 CYS B CA  1 
ATOM   3793 C  C   . CYS B 1 117 ? -3.216  -14.661 -7.129  1.00 32.70  ? 117 CYS B C   1 
ATOM   3794 O  O   . CYS B 1 117 ? -4.334  -14.204 -6.870  1.00 31.79  ? 117 CYS B O   1 
ATOM   3795 C  CB  . CYS B 1 117 ? -1.315  -13.806 -5.865  1.00 34.35  ? 117 CYS B CB  1 
ATOM   3796 S  SG  . CYS B 1 117 ? 0.028   -12.622 -5.699  1.00 36.32  ? 117 CYS B SG  1 
ATOM   3797 N  N   . TYR B 1 118 ? -2.958  -15.947 -7.348  1.00 33.25  ? 118 TYR B N   1 
ATOM   3798 C  CA  . TYR B 1 118 ? -3.946  -17.060 -7.287  1.00 34.58  ? 118 TYR B CA  1 
ATOM   3799 C  C   . TYR B 1 118 ? -3.223  -18.240 -6.625  1.00 36.09  ? 118 TYR B C   1 
ATOM   3800 O  O   . TYR B 1 118 ? -2.070  -18.552 -7.065  1.00 33.54  ? 118 TYR B O   1 
ATOM   3801 C  CB  . TYR B 1 118 ? -4.497  -17.367 -8.687  1.00 33.63  ? 118 TYR B CB  1 
ATOM   3802 C  CG  . TYR B 1 118 ? -5.210  -16.193 -9.301  1.00 34.17  ? 118 TYR B CG  1 
ATOM   3803 C  CD1 . TYR B 1 118 ? -4.520  -15.238 -10.042 1.00 35.50  ? 118 TYR B CD1 1 
ATOM   3804 C  CD2 . TYR B 1 118 ? -6.565  -15.974 -9.067  1.00 34.21  ? 118 TYR B CD2 1 
ATOM   3805 C  CE1 . TYR B 1 118 ? -5.158  -14.124 -10.580 1.00 31.61  ? 118 TYR B CE1 1 
ATOM   3806 C  CE2 . TYR B 1 118 ? -7.211  -14.861 -9.583  1.00 33.06  ? 118 TYR B CE2 1 
ATOM   3807 C  CZ  . TYR B 1 118 ? -6.505  -13.939 -10.344 1.00 31.06  ? 118 TYR B CZ  1 
ATOM   3808 O  OH  . TYR B 1 118 ? -7.148  -12.859 -10.843 1.00 32.28  ? 118 TYR B OH  1 
ATOM   3809 N  N   . ASN B 1 119 ? -3.785  -18.776 -5.532  1.00 36.53  ? 119 ASN B N   1 
ATOM   3810 C  CA  . ASN B 1 119 ? -3.218  -19.948 -4.803  1.00 39.49  ? 119 ASN B CA  1 
ATOM   3811 C  C   . ASN B 1 119 ? -1.801  -19.602 -4.315  1.00 37.89  ? 119 ASN B C   1 
ATOM   3812 O  O   . ASN B 1 119 ? -0.919  -20.472 -4.354  1.00 32.01  ? 119 ASN B O   1 
ATOM   3813 C  CB  . ASN B 1 119 ? -3.192  -21.210 -5.683  1.00 43.68  ? 119 ASN B CB  1 
ATOM   3814 C  CG  . ASN B 1 119 ? -4.565  -21.618 -6.177  1.00 46.32  ? 119 ASN B CG  1 
ATOM   3815 O  OD1 . ASN B 1 119 ? -4.795  -21.729 -7.379  1.00 57.01  ? 119 ASN B OD1 1 
ATOM   3816 N  ND2 . ASN B 1 119 ? -5.495  -21.817 -5.258  1.00 52.68  ? 119 ASN B ND2 1 
ATOM   3817 N  N   . GLY B 1 120 ? -1.568  -18.347 -3.930  1.00 35.87  ? 120 GLY B N   1 
ATOM   3818 C  CA  . GLY B 1 120 ? -0.267  -17.894 -3.414  1.00 33.58  ? 120 GLY B CA  1 
ATOM   3819 C  C   . GLY B 1 120 ? 0.768   -17.749 -4.523  1.00 32.61  ? 120 GLY B C   1 
ATOM   3820 O  O   . GLY B 1 120 ? 1.924   -17.479 -4.197  1.00 36.27  ? 120 GLY B O   1 
ATOM   3821 N  N   . SER B 1 121 ? 0.389   -17.876 -5.791  1.00 32.63  ? 121 SER B N   1 
ATOM   3822 C  CA  . SER B 1 121 ? 1.323   -17.702 -6.931  1.00 39.25  ? 121 SER B CA  1 
ATOM   3823 C  C   . SER B 1 121 ? 1.127   -16.346 -7.621  1.00 35.13  ? 121 SER B C   1 
ATOM   3824 O  O   . SER B 1 121 ? 0.055   -16.035 -8.133  1.00 31.45  ? 121 SER B O   1 
ATOM   3825 C  CB  . SER B 1 121 ? 1.218   -18.826 -7.900  1.00 42.38  ? 121 SER B CB  1 
ATOM   3826 O  OG  . SER B 1 121 ? 2.406   -18.882 -8.663  1.00 48.14  ? 121 SER B OG  1 
ATOM   3827 N  N   . PRO B 1 122 ? 2.157   -15.473 -7.637  1.00 34.26  ? 122 PRO B N   1 
ATOM   3828 C  CA  . PRO B 1 122 ? 2.058   -14.215 -8.379  1.00 34.10  ? 122 PRO B CA  1 
ATOM   3829 C  C   . PRO B 1 122 ? 1.754   -14.470 -9.862  1.00 34.87  ? 122 PRO B C   1 
ATOM   3830 O  O   . PRO B 1 122 ? 2.370   -15.310 -10.488 1.00 34.74  ? 122 PRO B O   1 
ATOM   3831 C  CB  . PRO B 1 122 ? 3.406   -13.544 -8.122  1.00 33.41  ? 122 PRO B CB  1 
ATOM   3832 C  CG  . PRO B 1 122 ? 3.828   -14.105 -6.774  1.00 35.41  ? 122 PRO B CG  1 
ATOM   3833 C  CD  . PRO B 1 122 ? 3.388   -15.559 -6.831  1.00 34.21  ? 122 PRO B CD  1 
ATOM   3834 N  N   . SER B 1 123 ? 0.783   -13.733 -10.383 1.00 32.04  ? 123 SER B N   1 
ATOM   3835 C  CA  . SER B 1 123 ? 0.192   -13.957 -11.717 1.00 32.14  ? 123 SER B CA  1 
ATOM   3836 C  C   . SER B 1 123 ? 0.463   -12.772 -12.658 1.00 29.31  ? 123 SER B C   1 
ATOM   3837 O  O   . SER B 1 123 ? 0.732   -13.013 -13.832 1.00 29.46  ? 123 SER B O   1 
ATOM   3838 C  CB  . SER B 1 123 ? -1.270  -14.212 -11.551 1.00 35.25  ? 123 SER B CB  1 
ATOM   3839 O  OG  . SER B 1 123 ? -1.804  -14.688 -12.764 1.00 42.89  ? 123 SER B OG  1 
ATOM   3840 N  N   . GLY B 1 124 ? 0.334   -11.539 -12.170 1.00 26.34  ? 124 GLY B N   1 
ATOM   3841 C  CA  . GLY B 1 124 ? 0.562   -10.331 -12.966 1.00 24.76  ? 124 GLY B CA  1 
ATOM   3842 C  C   . GLY B 1 124 ? 0.704   -9.120  -12.084 1.00 25.20  ? 124 GLY B C   1 
ATOM   3843 O  O   . GLY B 1 124 ? 0.357   -9.187  -10.894 1.00 26.20  ? 124 GLY B O   1 
ATOM   3844 N  N   A VAL B 1 125 ? 1.243   -8.038  -12.654 0.20 25.41  ? 125 VAL B N   1 
ATOM   3845 N  N   B VAL B 1 125 ? 1.213   -8.024  -12.648 0.30 24.63  ? 125 VAL B N   1 
ATOM   3846 N  N   C VAL B 1 125 ? 1.243   -8.038  -12.654 0.20 25.41  ? 125 VAL B N   1 
ATOM   3847 N  N   D VAL B 1 125 ? 1.213   -8.024  -12.648 0.30 24.63  ? 125 VAL B N   1 
ATOM   3848 C  CA  A VAL B 1 125 ? 1.433   -6.721  -11.980 0.20 26.19  ? 125 VAL B CA  1 
ATOM   3849 C  CA  B VAL B 1 125 ? 1.400   -6.731  -11.930 0.30 25.28  ? 125 VAL B CA  1 
ATOM   3850 C  CA  C VAL B 1 125 ? 1.433   -6.721  -11.980 0.20 26.19  ? 125 VAL B CA  1 
ATOM   3851 C  CA  D VAL B 1 125 ? 1.400   -6.731  -11.930 0.30 25.28  ? 125 VAL B CA  1 
ATOM   3852 C  C   A VAL B 1 125 ? 0.780   -5.639  -12.843 0.20 25.59  ? 125 VAL B C   1 
ATOM   3853 C  C   B VAL B 1 125 ? 0.872   -5.595  -12.812 0.30 24.83  ? 125 VAL B C   1 
ATOM   3854 C  C   C VAL B 1 125 ? 0.780   -5.639  -12.843 0.20 25.59  ? 125 VAL B C   1 
ATOM   3855 C  C   D VAL B 1 125 ? 0.872   -5.595  -12.812 0.30 24.83  ? 125 VAL B C   1 
ATOM   3856 O  O   A VAL B 1 125 ? 0.868   -5.735  -14.083 0.20 24.47  ? 125 VAL B O   1 
ATOM   3857 O  O   B VAL B 1 125 ? 1.133   -5.614  -14.031 0.30 22.98  ? 125 VAL B O   1 
ATOM   3858 O  O   C VAL B 1 125 ? 0.868   -5.735  -14.083 0.20 24.47  ? 125 VAL B O   1 
ATOM   3859 O  O   D VAL B 1 125 ? 1.133   -5.614  -14.031 0.30 22.98  ? 125 VAL B O   1 
ATOM   3860 C  CB  A VAL B 1 125 ? 2.921   -6.409  -11.740 0.20 27.31  ? 125 VAL B CB  1 
ATOM   3861 C  CB  B VAL B 1 125 ? 2.871   -6.520  -11.525 0.30 25.96  ? 125 VAL B CB  1 
ATOM   3862 C  CB  C VAL B 1 125 ? 2.921   -6.409  -11.740 0.20 27.31  ? 125 VAL B CB  1 
ATOM   3863 C  CB  D VAL B 1 125 ? 2.871   -6.520  -11.525 0.30 25.96  ? 125 VAL B CB  1 
ATOM   3864 C  CG1 A VAL B 1 125 ? 3.111   -5.530  -10.513 0.20 27.53  ? 125 VAL B CG1 1 
ATOM   3865 C  CG1 B VAL B 1 125 ? 3.767   -6.285  -12.732 0.30 25.49  ? 125 VAL B CG1 1 
ATOM   3866 C  CG1 C VAL B 1 125 ? 3.111   -5.530  -10.513 0.20 27.53  ? 125 VAL B CG1 1 
ATOM   3867 C  CG1 D VAL B 1 125 ? 3.767   -6.285  -12.732 0.30 25.49  ? 125 VAL B CG1 1 
ATOM   3868 C  CG2 A VAL B 1 125 ? 3.756   -7.673  -11.627 0.20 27.86  ? 125 VAL B CG2 1 
ATOM   3869 C  CG2 B VAL B 1 125 ? 3.015   -5.394  -10.512 0.30 26.15  ? 125 VAL B CG2 1 
ATOM   3870 C  CG2 C VAL B 1 125 ? 3.756   -7.673  -11.627 0.20 27.86  ? 125 VAL B CG2 1 
ATOM   3871 C  CG2 D VAL B 1 125 ? 3.015   -5.394  -10.512 0.30 26.15  ? 125 VAL B CG2 1 
ATOM   3872 N  N   . TYR B 1 126 ? 0.142   -4.655  -12.206 1.00 26.14  ? 126 TYR B N   1 
ATOM   3873 C  CA  . TYR B 1 126 ? -0.434  -3.487  -12.907 1.00 24.70  ? 126 TYR B CA  1 
ATOM   3874 C  C   . TYR B 1 126 ? -0.533  -2.330  -11.929 1.00 25.91  ? 126 TYR B C   1 
ATOM   3875 O  O   . TYR B 1 126 ? -0.597  -2.557  -10.696 1.00 24.12  ? 126 TYR B O   1 
ATOM   3876 C  CB  . TYR B 1 126 ? -1.796  -3.794  -13.525 1.00 25.76  ? 126 TYR B CB  1 
ATOM   3877 C  CG  . TYR B 1 126 ? -2.832  -4.413  -12.622 1.00 28.10  ? 126 TYR B CG  1 
ATOM   3878 C  CD1 . TYR B 1 126 ? -2.931  -5.790  -12.507 1.00 28.42  ? 126 TYR B CD1 1 
ATOM   3879 C  CD2 . TYR B 1 126 ? -3.715  -3.633  -11.880 1.00 28.04  ? 126 TYR B CD2 1 
ATOM   3880 C  CE1 . TYR B 1 126 ? -3.895  -6.374  -11.693 1.00 31.26  ? 126 TYR B CE1 1 
ATOM   3881 C  CE2 . TYR B 1 126 ? -4.661  -4.204  -11.049 1.00 29.67  ? 126 TYR B CE2 1 
ATOM   3882 C  CZ  . TYR B 1 126 ? -4.766  -5.584  -10.969 1.00 30.13  ? 126 TYR B CZ  1 
ATOM   3883 O  OH  . TYR B 1 126 ? -5.723  -6.164  -10.183 1.00 35.51  ? 126 TYR B OH  1 
ATOM   3884 N  N   . GLN B 1 127 ? -0.526  -1.136  -12.509 1.00 24.58  ? 127 GLN B N   1 
ATOM   3885 C  CA  . GLN B 1 127 ? -0.649  0.158   -11.802 1.00 27.80  ? 127 GLN B CA  1 
ATOM   3886 C  C   . GLN B 1 127 ? -2.160  0.461   -11.687 1.00 30.55  ? 127 GLN B C   1 
ATOM   3887 O  O   . GLN B 1 127 ? -2.929  0.166   -12.620 1.00 30.44  ? 127 GLN B O   1 
ATOM   3888 C  CB  . GLN B 1 127 ? 0.194   1.149   -12.603 1.00 27.59  ? 127 GLN B CB  1 
ATOM   3889 C  CG  . GLN B 1 127 ? 0.642   2.408   -11.889 1.00 30.49  ? 127 GLN B CG  1 
ATOM   3890 C  CD  . GLN B 1 127 ? 1.515   2.221   -10.678 1.00 28.92  ? 127 GLN B CD  1 
ATOM   3891 O  OE1 . GLN B 1 127 ? 1.893   1.111   -10.294 1.00 29.58  ? 127 GLN B OE1 1 
ATOM   3892 N  NE2 . GLN B 1 127 ? 1.798   3.341   -10.037 1.00 30.02  ? 127 GLN B NE2 1 
ATOM   3893 N  N   A CYS B 1 128 ? -2.565  0.977   -10.516 0.25 29.76  ? 128 CYS B N   1 
ATOM   3894 N  N   B CYS B 1 128 ? -2.585  1.048   -10.573 0.25 30.88  ? 128 CYS B N   1 
ATOM   3895 N  N   C CYS B 1 128 ? -2.565  0.977   -10.516 0.25 29.76  ? 128 CYS B N   1 
ATOM   3896 N  N   D CYS B 1 128 ? -2.585  1.048   -10.573 0.25 30.88  ? 128 CYS B N   1 
ATOM   3897 C  CA  A CYS B 1 128 ? -3.945  1.406   -10.155 0.25 29.23  ? 128 CYS B CA  1 
ATOM   3898 C  CA  B CYS B 1 128 ? -3.968  1.557   -10.425 0.25 30.80  ? 128 CYS B CA  1 
ATOM   3899 C  CA  C CYS B 1 128 ? -3.945  1.406   -10.155 0.25 29.23  ? 128 CYS B CA  1 
ATOM   3900 C  CA  D CYS B 1 128 ? -3.968  1.557   -10.425 0.25 30.80  ? 128 CYS B CA  1 
ATOM   3901 C  C   A CYS B 1 128 ? -3.900  2.781   -9.478  0.25 29.74  ? 128 CYS B C   1 
ATOM   3902 C  C   B CYS B 1 128 ? -3.997  2.665   -9.374  0.25 30.56  ? 128 CYS B C   1 
ATOM   3903 C  C   C CYS B 1 128 ? -3.900  2.781   -9.478  0.25 29.74  ? 128 CYS B C   1 
ATOM   3904 C  C   D CYS B 1 128 ? -3.997  2.665   -9.374  0.25 30.56  ? 128 CYS B C   1 
ATOM   3905 O  O   A CYS B 1 128 ? -2.813  3.158   -8.996  0.25 28.90  ? 128 CYS B O   1 
ATOM   3906 O  O   B CYS B 1 128 ? -3.076  2.737   -8.536  0.25 29.18  ? 128 CYS B O   1 
ATOM   3907 O  O   C CYS B 1 128 ? -2.813  3.158   -8.996  0.25 28.90  ? 128 CYS B O   1 
ATOM   3908 O  O   D CYS B 1 128 ? -3.076  2.737   -8.536  0.25 29.18  ? 128 CYS B O   1 
ATOM   3909 C  CB  A CYS B 1 128 ? -4.594  0.440   -9.169  0.25 29.08  ? 128 CYS B CB  1 
ATOM   3910 C  CB  B CYS B 1 128 ? -4.933  0.434   -10.072 0.25 32.42  ? 128 CYS B CB  1 
ATOM   3911 C  CB  C CYS B 1 128 ? -4.594  0.440   -9.169  0.25 29.08  ? 128 CYS B CB  1 
ATOM   3912 C  CB  D CYS B 1 128 ? -4.933  0.434   -10.072 0.25 32.42  ? 128 CYS B CB  1 
ATOM   3913 S  SG  A CYS B 1 128 ? -5.286  -1.054  -9.924  0.25 28.42  ? 128 CYS B SG  1 
ATOM   3914 S  SG  B CYS B 1 128 ? -4.665  -0.231  -8.413  0.25 33.65  ? 128 CYS B SG  1 
ATOM   3915 S  SG  C CYS B 1 128 ? -5.286  -1.054  -9.924  0.25 28.42  ? 128 CYS B SG  1 
ATOM   3916 S  SG  D CYS B 1 128 ? -4.665  -0.231  -8.413  0.25 33.65  ? 128 CYS B SG  1 
ATOM   3917 N  N   . ALA B 1 129 ? -5.030  3.501   -9.452  1.00 30.01  ? 129 ALA B N   1 
ATOM   3918 C  CA  . ALA B 1 129 ? -5.247  4.637   -8.537  1.00 29.96  ? 129 ALA B CA  1 
ATOM   3919 C  C   . ALA B 1 129 ? -6.388  4.232   -7.598  1.00 27.37  ? 129 ALA B C   1 
ATOM   3920 O  O   . ALA B 1 129 ? -7.323  3.531   -8.037  1.00 29.34  ? 129 ALA B O   1 
ATOM   3921 C  CB  . ALA B 1 129 ? -5.567  5.899   -9.291  1.00 31.00  ? 129 ALA B CB  1 
ATOM   3922 N  N   . MET B 1 130 ? -6.256  4.602   -6.334  1.00 27.24  ? 130 MET B N   1 
ATOM   3923 C  CA  . MET B 1 130 ? -7.391  4.714   -5.391  1.00 28.18  ? 130 MET B CA  1 
ATOM   3924 C  C   . MET B 1 130 ? -8.307  5.814   -5.950  1.00 27.97  ? 130 MET B C   1 
ATOM   3925 O  O   . MET B 1 130 ? -7.867  6.991   -6.027  1.00 27.45  ? 130 MET B O   1 
ATOM   3926 C  CB  . MET B 1 130 ? -6.862  5.088   -4.004  1.00 29.55  ? 130 MET B CB  1 
ATOM   3927 C  CG  . MET B 1 130 ? -7.918  5.179   -2.935  1.00 30.68  ? 130 MET B CG  1 
ATOM   3928 S  SD  . MET B 1 130 ? -8.794  3.616   -2.734  1.00 33.97  ? 130 MET B SD  1 
ATOM   3929 C  CE  . MET B 1 130 ? -7.502  2.524   -2.156  1.00 32.37  ? 130 MET B CE  1 
ATOM   3930 N  N   . ARG B 1 131 ? -9.492  5.444   -6.417  1.00 27.37  ? 131 ARG B N   1 
ATOM   3931 C  CA  . ARG B 1 131 ? -10.435 6.400   -7.041  1.00 30.18  ? 131 ARG B CA  1 
ATOM   3932 C  C   . ARG B 1 131 ? -10.940 7.333   -5.941  1.00 31.12  ? 131 ARG B C   1 
ATOM   3933 O  O   . ARG B 1 131 ? -10.884 6.987   -4.760  1.00 25.40  ? 131 ARG B O   1 
ATOM   3934 C  CB  . ARG B 1 131 ? -11.597 5.665   -7.712  1.00 31.69  ? 131 ARG B CB  1 
ATOM   3935 C  CG  . ARG B 1 131 ? -11.195 4.671   -8.795  1.00 33.64  ? 131 ARG B CG  1 
ATOM   3936 C  CD  . ARG B 1 131 ? -10.497 5.287   -9.990  1.00 33.96  ? 131 ARG B CD  1 
ATOM   3937 N  NE  . ARG B 1 131 ? -11.039 6.572   -10.407 1.00 31.34  ? 131 ARG B NE  1 
ATOM   3938 C  CZ  . ARG B 1 131 ? -10.408 7.419   -11.210 1.00 31.08  ? 131 ARG B CZ  1 
ATOM   3939 N  NH1 . ARG B 1 131 ? -9.219  7.100   -11.698 1.00 28.96  ? 131 ARG B NH1 1 
ATOM   3940 N  NH2 . ARG B 1 131 ? -10.952 8.591   -11.492 1.00 30.01  ? 131 ARG B NH2 1 
ATOM   3941 N  N   . PRO B 1 132 ? -11.404 8.556   -6.287  1.00 34.37  ? 132 PRO B N   1 
ATOM   3942 C  CA  . PRO B 1 132 ? -12.070 9.426   -5.315  1.00 33.57  ? 132 PRO B CA  1 
ATOM   3943 C  C   . PRO B 1 132 ? -13.217 8.726   -4.570  1.00 30.19  ? 132 PRO B C   1 
ATOM   3944 O  O   . PRO B 1 132 ? -13.386 9.027   -3.440  1.00 31.36  ? 132 PRO B O   1 
ATOM   3945 C  CB  . PRO B 1 132 ? -12.552 10.600  -6.180  1.00 32.76  ? 132 PRO B CB  1 
ATOM   3946 C  CG  . PRO B 1 132 ? -11.500 10.665  -7.276  1.00 31.72  ? 132 PRO B CG  1 
ATOM   3947 C  CD  . PRO B 1 132 ? -11.209 9.216   -7.593  1.00 31.81  ? 132 PRO B CD  1 
ATOM   3948 N  N   . ASN B 1 133 ? -13.905 7.770   -5.187  1.00 29.67  ? 133 ASN B N   1 
ATOM   3949 C  CA  . ASN B 1 133 ? -15.020 7.019   -4.538  1.00 29.93  ? 133 ASN B CA  1 
ATOM   3950 C  C   . ASN B 1 133 ? -14.487 5.810   -3.755  1.00 30.25  ? 133 ASN B C   1 
ATOM   3951 O  O   . ASN B 1 133 ? -15.310 4.980   -3.353  1.00 30.53  ? 133 ASN B O   1 
ATOM   3952 C  CB  . ASN B 1 133 ? -16.089 6.563   -5.539  1.00 27.59  ? 133 ASN B CB  1 
ATOM   3953 C  CG  . ASN B 1 133 ? -15.652 5.440   -6.462  1.00 31.87  ? 133 ASN B CG  1 
ATOM   3954 O  OD1 . ASN B 1 133 ? -14.490 5.005   -6.443  1.00 28.00  ? 133 ASN B OD1 1 
ATOM   3955 N  ND2 . ASN B 1 133 ? -16.570 4.990   -7.317  1.00 27.70  ? 133 ASN B ND2 1 
ATOM   3956 N  N   . PHE B 1 134 ? -13.169 5.643   -3.646  1.00 28.30  ? 134 PHE B N   1 
ATOM   3957 C  CA  . PHE B 1 134 ? -12.487 4.638   -2.785  1.00 28.36  ? 134 PHE B CA  1 
ATOM   3958 C  C   . PHE B 1 134 ? -12.584 3.235   -3.367  1.00 28.30  ? 134 PHE B C   1 
ATOM   3959 O  O   . PHE B 1 134 ? -12.330 2.267   -2.630  1.00 35.63  ? 134 PHE B O   1 
ATOM   3960 C  CB  . PHE B 1 134 ? -13.021 4.633   -1.347  1.00 27.73  ? 134 PHE B CB  1 
ATOM   3961 C  CG  . PHE B 1 134 ? -12.593 5.822   -0.534  1.00 28.12  ? 134 PHE B CG  1 
ATOM   3962 C  CD1 . PHE B 1 134 ? -11.272 5.958   -0.120  1.00 31.92  ? 134 PHE B CD1 1 
ATOM   3963 C  CD2 . PHE B 1 134 ? -13.497 6.835   -0.235  1.00 29.91  ? 134 PHE B CD2 1 
ATOM   3964 C  CE1 . PHE B 1 134 ? -10.872 7.058   0.635   1.00 32.00  ? 134 PHE B CE1 1 
ATOM   3965 C  CE2 . PHE B 1 134 ? -13.099 7.939   0.501   1.00 30.59  ? 134 PHE B CE2 1 
ATOM   3966 C  CZ  . PHE B 1 134 ? -11.786 8.054   0.928   1.00 33.12  ? 134 PHE B CZ  1 
ATOM   3967 N  N   . THR B 1 135 ? -12.880 3.109   -4.654  1.00 28.87  ? 135 THR B N   1 
ATOM   3968 C  CA  . THR B 1 135 ? -12.759 1.820   -5.384  1.00 29.14  ? 135 THR B CA  1 
ATOM   3969 C  C   . THR B 1 135 ? -11.447 1.857   -6.166  1.00 28.16  ? 135 THR B C   1 
ATOM   3970 O  O   . THR B 1 135 ? -10.869 2.947   -6.266  1.00 27.83  ? 135 THR B O   1 
ATOM   3971 C  CB  . THR B 1 135 ? -13.966 1.581   -6.301  1.00 30.07  ? 135 THR B CB  1 
ATOM   3972 O  OG1 . THR B 1 135 ? -13.900 2.576   -7.323  1.00 29.87  ? 135 THR B OG1 1 
ATOM   3973 C  CG2 . THR B 1 135 ? -15.283 1.665   -5.563  1.00 31.62  ? 135 THR B CG2 1 
ATOM   3974 N  N   . ILE B 1 136 ? -10.981 0.705   -6.641  1.00 28.91  ? 136 ILE B N   1 
ATOM   3975 C  CA  . ILE B 1 136 ? -9.893  0.622   -7.654  1.00 32.66  ? 136 ILE B CA  1 
ATOM   3976 C  C   . ILE B 1 136 ? -10.456 -0.127  -8.872  1.00 34.13  ? 136 ILE B C   1 
ATOM   3977 O  O   . ILE B 1 136 ? -11.302 -1.046  -8.690  1.00 34.31  ? 136 ILE B O   1 
ATOM   3978 C  CB  . ILE B 1 136 ? -8.595  0.009   -7.082  1.00 33.21  ? 136 ILE B CB  1 
ATOM   3979 C  CG1 . ILE B 1 136 ? -8.667  -1.504  -6.903  1.00 33.25  ? 136 ILE B CG1 1 
ATOM   3980 C  CG2 . ILE B 1 136 ? -8.188  0.690   -5.777  1.00 33.13  ? 136 ILE B CG2 1 
ATOM   3981 C  CD1 . ILE B 1 136 ? -7.313  -2.132  -6.703  1.00 34.80  ? 136 ILE B CD1 1 
ATOM   3982 N  N   . LYS B 1 137 ? -10.048 0.278   -10.074 1.00 30.86  ? 137 LYS B N   1 
ATOM   3983 C  CA  . LYS B 1 137 ? -10.425 -0.429  -11.320 1.00 35.76  ? 137 LYS B CA  1 
ATOM   3984 C  C   . LYS B 1 137 ? -9.381  -1.503  -11.581 1.00 34.78  ? 137 LYS B C   1 
ATOM   3985 O  O   . LYS B 1 137 ? -8.411  -1.238  -12.317 1.00 36.92  ? 137 LYS B O   1 
ATOM   3986 C  CB  . LYS B 1 137 ? -10.566 0.573   -12.460 1.00 40.67  ? 137 LYS B CB  1 
ATOM   3987 C  CG  . LYS B 1 137 ? -11.619 1.628   -12.178 1.00 43.90  ? 137 LYS B CG  1 
ATOM   3988 C  CD  . LYS B 1 137 ? -12.050 2.364   -13.406 1.00 51.10  ? 137 LYS B CD  1 
ATOM   3989 C  CE  . LYS B 1 137 ? -13.112 3.392   -13.103 1.00 58.32  ? 137 LYS B CE  1 
ATOM   3990 N  NZ  . LYS B 1 137 ? -13.639 3.984   -14.352 1.00 63.31  ? 137 LYS B NZ  1 
ATOM   3991 N  N   . GLY B 1 138 ? -9.551  -2.652  -10.934 1.00 35.26  ? 138 GLY B N   1 
ATOM   3992 C  CA  . GLY B 1 138 ? -8.561  -3.739  -10.961 1.00 37.12  ? 138 GLY B CA  1 
ATOM   3993 C  C   . GLY B 1 138 ? -8.909  -4.737  -12.042 1.00 37.74  ? 138 GLY B C   1 
ATOM   3994 O  O   . GLY B 1 138 ? -9.885  -4.507  -12.789 1.00 37.32  ? 138 GLY B O   1 
ATOM   3995 N  N   . SER B 1 139 ? -8.144  -5.820  -12.116 1.00 34.53  ? 139 SER B N   1 
ATOM   3996 C  CA  . SER B 1 139 ? -8.469  -7.001  -12.945 1.00 31.74  ? 139 SER B CA  1 
ATOM   3997 C  C   . SER B 1 139 ? -8.278  -8.196  -12.035 1.00 32.01  ? 139 SER B C   1 
ATOM   3998 O  O   . SER B 1 139 ? -7.117  -8.517  -11.730 1.00 31.27  ? 139 SER B O   1 
ATOM   3999 C  CB  . SER B 1 139 ? -7.628  -7.084  -14.175 1.00 33.97  ? 139 SER B CB  1 
ATOM   4000 O  OG  . SER B 1 139 ? -7.915  -8.279  -14.883 1.00 35.25  ? 139 SER B OG  1 
ATOM   4001 N  N   . PHE B 1 140 ? -9.383  -8.723  -11.513 1.00 31.54  ? 140 PHE B N   1 
ATOM   4002 C  CA  . PHE B 1 140 ? -9.364  -9.765  -10.461 1.00 34.87  ? 140 PHE B CA  1 
ATOM   4003 C  C   . PHE B 1 140 ? -10.387 -10.842 -10.795 1.00 37.93  ? 140 PHE B C   1 
ATOM   4004 O  O   . PHE B 1 140 ? -11.554 -10.490 -11.072 1.00 36.93  ? 140 PHE B O   1 
ATOM   4005 C  CB  . PHE B 1 140 ? -9.706  -9.181  -9.091  1.00 32.56  ? 140 PHE B CB  1 
ATOM   4006 C  CG  . PHE B 1 140 ? -8.640  -8.302  -8.490  1.00 32.24  ? 140 PHE B CG  1 
ATOM   4007 C  CD1 . PHE B 1 140 ? -7.385  -8.814  -8.201  1.00 32.06  ? 140 PHE B CD1 1 
ATOM   4008 C  CD2 . PHE B 1 140 ? -8.905  -6.970  -8.184  1.00 32.31  ? 140 PHE B CD2 1 
ATOM   4009 C  CE1 . PHE B 1 140 ? -6.413  -8.016  -7.622  1.00 30.03  ? 140 PHE B CE1 1 
ATOM   4010 C  CE2 . PHE B 1 140 ? -7.936  -6.169  -7.593  1.00 31.19  ? 140 PHE B CE2 1 
ATOM   4011 C  CZ  . PHE B 1 140 ? -6.698  -6.702  -7.305  1.00 34.23  ? 140 PHE B CZ  1 
ATOM   4012 N  N   . LEU B 1 141 ? -9.948  -12.099 -10.747 1.00 37.38  ? 141 LEU B N   1 
ATOM   4013 C  CA  . LEU B 1 141 ? -10.831 -13.289 -10.821 1.00 40.90  ? 141 LEU B CA  1 
ATOM   4014 C  C   . LEU B 1 141 ? -10.896 -13.965 -9.446  1.00 45.08  ? 141 LEU B C   1 
ATOM   4015 O  O   . LEU B 1 141 ? -10.125 -13.594 -8.563  1.00 43.71  ? 141 LEU B O   1 
ATOM   4016 C  CB  . LEU B 1 141 ? -10.290 -14.248 -11.883 1.00 39.12  ? 141 LEU B CB  1 
ATOM   4017 C  CG  . LEU B 1 141 ? -10.119 -13.641 -13.276 1.00 40.82  ? 141 LEU B CG  1 
ATOM   4018 C  CD1 . LEU B 1 141 ? -9.589  -14.700 -14.238 1.00 42.96  ? 141 LEU B CD1 1 
ATOM   4019 C  CD2 . LEU B 1 141 ? -11.417 -13.026 -13.800 1.00 38.13  ? 141 LEU B CD2 1 
ATOM   4020 N  N   . ASN B 1 142 ? -11.780 -14.952 -9.305  1.00 47.82  ? 142 ASN B N   1 
ATOM   4021 C  CA  . ASN B 1 142 ? -11.960 -15.754 -8.068  1.00 49.62  ? 142 ASN B CA  1 
ATOM   4022 C  C   . ASN B 1 142 ? -10.608 -16.337 -7.642  1.00 43.72  ? 142 ASN B C   1 
ATOM   4023 O  O   . ASN B 1 142 ? -9.883  -16.882 -8.501  1.00 41.89  ? 142 ASN B O   1 
ATOM   4024 C  CB  . ASN B 1 142 ? -13.043 -16.819 -8.257  1.00 52.71  ? 142 ASN B CB  1 
ATOM   4025 C  CG  . ASN B 1 142 ? -14.410 -16.215 -8.510  1.00 59.68  ? 142 ASN B CG  1 
ATOM   4026 O  OD1 . ASN B 1 142 ? -14.734 -15.135 -8.003  1.00 65.18  ? 142 ASN B OD1 1 
ATOM   4027 N  ND2 . ASN B 1 142 ? -15.227 -16.911 -9.282  1.00 60.11  ? 142 ASN B ND2 1 
ATOM   4028 N  N   . GLY B 1 143 ? -10.285 -16.207 -6.356  1.00 40.51  ? 143 GLY B N   1 
ATOM   4029 C  CA  . GLY B 1 143 ? -8.999  -16.640 -5.778  1.00 38.31  ? 143 GLY B CA  1 
ATOM   4030 C  C   . GLY B 1 143 ? -7.986  -15.507 -5.748  1.00 35.34  ? 143 GLY B C   1 
ATOM   4031 O  O   . GLY B 1 143 ? -6.872  -15.754 -5.278  1.00 34.82  ? 143 GLY B O   1 
ATOM   4032 N  N   . SER B 1 144 ? -8.349  -14.304 -6.219  1.00 32.47  ? 144 SER B N   1 
ATOM   4033 C  CA  . SER B 1 144 ? -7.469  -13.101 -6.191  1.00 31.98  ? 144 SER B CA  1 
ATOM   4034 C  C   . SER B 1 144 ? -7.427  -12.466 -4.793  1.00 31.08  ? 144 SER B C   1 
ATOM   4035 O  O   . SER B 1 144 ? -6.516  -11.666 -4.540  1.00 28.28  ? 144 SER B O   1 
ATOM   4036 C  CB  . SER B 1 144 ? -7.854  -12.075 -7.231  1.00 30.51  ? 144 SER B CB  1 
ATOM   4037 O  OG  . SER B 1 144 ? -9.144  -11.561 -6.990  1.00 32.62  ? 144 SER B OG  1 
ATOM   4038 N  N   . CYS B 1 145 ? -8.379  -12.786 -3.912  1.00 30.98  ? 145 CYS B N   1 
ATOM   4039 C  CA  . CYS B 1 145 ? -8.481  -12.149 -2.582  1.00 28.25  ? 145 CYS B CA  1 
ATOM   4040 C  C   . CYS B 1 145 ? -7.159  -12.342 -1.847  1.00 27.28  ? 145 CYS B C   1 
ATOM   4041 O  O   . CYS B 1 145 ? -6.538  -13.446 -1.960  1.00 27.81  ? 145 CYS B O   1 
ATOM   4042 C  CB  . CYS B 1 145 ? -9.656  -12.699 -1.785  1.00 32.02  ? 145 CYS B CB  1 
ATOM   4043 S  SG  . CYS B 1 145 ? -11.237 -12.054 -2.369  1.00 34.64  ? 145 CYS B SG  1 
ATOM   4044 N  N   . GLY B 1 146 ? -6.739  -11.302 -1.126  1.00 25.60  ? 146 GLY B N   1 
ATOM   4045 C  CA  . GLY B 1 146 ? -5.452  -11.289 -0.409  1.00 25.00  ? 146 GLY B CA  1 
ATOM   4046 C  C   . GLY B 1 146 ? -4.298  -10.829 -1.289  1.00 25.74  ? 146 GLY B C   1 
ATOM   4047 O  O   . GLY B 1 146 ? -3.195  -10.602 -0.741  1.00 24.32  ? 146 GLY B O   1 
ATOM   4048 N  N   . SER B 1 147 ? -4.496  -10.681 -2.604  1.00 25.30  ? 147 SER B N   1 
ATOM   4049 C  CA  . SER B 1 147 ? -3.525  -9.949  -3.464  1.00 25.21  ? 147 SER B CA  1 
ATOM   4050 C  C   . SER B 1 147 ? -3.282  -8.581  -2.801  1.00 26.13  ? 147 SER B C   1 
ATOM   4051 O  O   . SER B 1 147 ? -4.241  -8.041  -2.198  1.00 23.93  ? 147 SER B O   1 
ATOM   4052 C  CB  . SER B 1 147 ? -4.028  -9.806  -4.876  1.00 24.89  ? 147 SER B CB  1 
ATOM   4053 O  OG  . SER B 1 147 ? -4.115  -11.064 -5.541  1.00 25.99  ? 147 SER B OG  1 
ATOM   4054 N  N   . VAL B 1 148 ? -2.093  -7.989  -2.943  1.00 27.95  ? 148 VAL B N   1 
ATOM   4055 C  CA  . VAL B 1 148 ? -1.753  -6.698  -2.272  1.00 28.09  ? 148 VAL B CA  1 
ATOM   4056 C  C   . VAL B 1 148 ? -1.283  -5.622  -3.255  1.00 26.85  ? 148 VAL B C   1 
ATOM   4057 O  O   . VAL B 1 148 ? -0.848  -5.929  -4.386  1.00 28.18  ? 148 VAL B O   1 
ATOM   4058 C  CB  . VAL B 1 148 ? -0.717  -6.892  -1.158  1.00 30.59  ? 148 VAL B CB  1 
ATOM   4059 C  CG1 . VAL B 1 148 ? -1.259  -7.804  -0.065  1.00 30.82  ? 148 VAL B CG1 1 
ATOM   4060 C  CG2 . VAL B 1 148 ? 0.609   -7.388  -1.690  1.00 29.29  ? 148 VAL B CG2 1 
ATOM   4061 N  N   . GLY B 1 149 ? -1.382  -4.385  -2.786  1.00 25.53  ? 149 GLY B N   1 
ATOM   4062 C  CA  . GLY B 1 149 ? -0.972  -3.169  -3.501  1.00 26.31  ? 149 GLY B CA  1 
ATOM   4063 C  C   . GLY B 1 149 ? 0.119   -2.487  -2.712  1.00 28.16  ? 149 GLY B C   1 
ATOM   4064 O  O   . GLY B 1 149 ? 0.072   -2.548  -1.461  1.00 24.31  ? 149 GLY B O   1 
ATOM   4065 N  N   . PHE B 1 150 ? 1.090   -1.895  -3.397  1.00 24.79  ? 150 PHE B N   1 
ATOM   4066 C  CA  . PHE B 1 150 ? 2.305   -1.372  -2.740  1.00 26.01  ? 150 PHE B CA  1 
ATOM   4067 C  C   . PHE B 1 150 ? 2.936   -0.273  -3.591  1.00 26.09  ? 150 PHE B C   1 
ATOM   4068 O  O   . PHE B 1 150 ? 2.672   -0.194  -4.810  1.00 24.08  ? 150 PHE B O   1 
ATOM   4069 C  CB  . PHE B 1 150 ? 3.321   -2.493  -2.520  1.00 24.32  ? 150 PHE B CB  1 
ATOM   4070 C  CG  . PHE B 1 150 ? 3.865   -3.104  -3.788  1.00 23.64  ? 150 PHE B CG  1 
ATOM   4071 C  CD1 . PHE B 1 150 ? 3.184   -4.115  -4.450  1.00 25.81  ? 150 PHE B CD1 1 
ATOM   4072 C  CD2 . PHE B 1 150 ? 5.070   -2.689  -4.310  1.00 25.42  ? 150 PHE B CD2 1 
ATOM   4073 C  CE1 . PHE B 1 150 ? 3.668   -4.655  -5.632  1.00 26.76  ? 150 PHE B CE1 1 
ATOM   4074 C  CE2 . PHE B 1 150 ? 5.568   -3.245  -5.482  1.00 26.30  ? 150 PHE B CE2 1 
ATOM   4075 C  CZ  . PHE B 1 150 ? 4.867   -4.227  -6.143  1.00 26.04  ? 150 PHE B CZ  1 
ATOM   4076 N  N   . ASN B 1 151 ? 3.783   0.504   -2.931  1.00 25.49  ? 151 ASN B N   1 
ATOM   4077 C  CA  . ASN B 1 151 ? 4.738   1.457   -3.534  1.00 28.91  ? 151 ASN B CA  1 
ATOM   4078 C  C   . ASN B 1 151 ? 6.114   1.021   -3.047  1.00 31.16  ? 151 ASN B C   1 
ATOM   4079 O  O   . ASN B 1 151 ? 6.182   0.277   -2.058  1.00 30.90  ? 151 ASN B O   1 
ATOM   4080 C  CB  . ASN B 1 151 ? 4.403   2.899   -3.136  1.00 28.90  ? 151 ASN B CB  1 
ATOM   4081 C  CG  . ASN B 1 151 ? 3.171   3.375   -3.867  1.00 33.29  ? 151 ASN B CG  1 
ATOM   4082 O  OD1 . ASN B 1 151 ? 3.203   3.535   -5.082  1.00 33.29  ? 151 ASN B OD1 1 
ATOM   4083 N  ND2 . ASN B 1 151 ? 2.062   3.520   -3.169  1.00 31.34  ? 151 ASN B ND2 1 
ATOM   4084 N  N   . ILE B 1 152 ? 7.154   1.460   -3.722  1.00 32.04  ? 152 ILE B N   1 
ATOM   4085 C  CA  . ILE B 1 152 ? 8.540   1.367   -3.209  1.00 34.96  ? 152 ILE B CA  1 
ATOM   4086 C  C   . ILE B 1 152 ? 9.122   2.775   -3.125  1.00 40.67  ? 152 ILE B C   1 
ATOM   4087 O  O   . ILE B 1 152 ? 9.031   3.507   -4.120  1.00 41.81  ? 152 ILE B O   1 
ATOM   4088 C  CB  . ILE B 1 152 ? 9.355   0.454   -4.116  1.00 33.85  ? 152 ILE B CB  1 
ATOM   4089 C  CG1 . ILE B 1 152 ? 8.628   -0.878  -4.310  1.00 34.46  ? 152 ILE B CG1 1 
ATOM   4090 C  CG2 . ILE B 1 152 ? 10.759  0.321   -3.557  1.00 35.52  ? 152 ILE B CG2 1 
ATOM   4091 C  CD1 . ILE B 1 152 ? 9.433   -1.942  -5.003  1.00 35.90  ? 152 ILE B CD1 1 
ATOM   4092 N  N   . ASP B 1 153 ? 9.684   3.115   -1.967  1.00 48.30  ? 153 ASP B N   1 
ATOM   4093 C  CA  . ASP B 1 153 ? 10.447  4.363   -1.717  1.00 52.37  ? 153 ASP B CA  1 
ATOM   4094 C  C   . ASP B 1 153 ? 11.864  3.965   -1.322  1.00 59.25  ? 153 ASP B C   1 
ATOM   4095 O  O   . ASP B 1 153 ? 12.056  3.658   -0.129  1.00 68.58  ? 153 ASP B O   1 
ATOM   4096 C  CB  . ASP B 1 153 ? 9.764   5.184   -0.628  1.00 55.88  ? 153 ASP B CB  1 
ATOM   4097 C  CG  . ASP B 1 153 ? 8.401   5.682   -1.066  1.00 62.44  ? 153 ASP B CG  1 
ATOM   4098 O  OD1 . ASP B 1 153 ? 8.366   6.734   -1.735  1.00 71.91  ? 153 ASP B OD1 1 
ATOM   4099 O  OD2 . ASP B 1 153 ? 7.389   5.001   -0.760  1.00 62.07  ? 153 ASP B OD2 1 
ATOM   4100 N  N   . TYR B 1 154 ? 12.784  3.924   -2.292  1.00 57.18  ? 154 TYR B N   1 
ATOM   4101 C  CA  . TYR B 1 154 ? 14.211  3.518   -2.146  1.00 65.52  ? 154 TYR B CA  1 
ATOM   4102 C  C   . TYR B 1 154 ? 14.305  1.990   -2.120  1.00 62.96  ? 154 TYR B C   1 
ATOM   4103 O  O   . TYR B 1 154 ? 14.228  1.393   -3.210  1.00 58.61  ? 154 TYR B O   1 
ATOM   4104 C  CB  . TYR B 1 154 ? 14.866  4.230   -0.956  1.00 73.72  ? 154 TYR B CB  1 
ATOM   4105 C  CG  . TYR B 1 154 ? 14.865  5.726   -1.129  1.00 84.13  ? 154 TYR B CG  1 
ATOM   4106 C  CD1 . TYR B 1 154 ? 15.824  6.352   -1.915  1.00 87.48  ? 154 TYR B CD1 1 
ATOM   4107 C  CD2 . TYR B 1 154 ? 13.854  6.508   -0.582  1.00 88.91  ? 154 TYR B CD2 1 
ATOM   4108 C  CE1 . TYR B 1 154 ? 15.805  7.725   -2.113  1.00 93.94  ? 154 TYR B CE1 1 
ATOM   4109 C  CE2 . TYR B 1 154 ? 13.823  7.881   -0.764  1.00 92.85  ? 154 TYR B CE2 1 
ATOM   4110 C  CZ  . TYR B 1 154 ? 14.803  8.488   -1.534  1.00 96.41  ? 154 TYR B CZ  1 
ATOM   4111 O  OH  . TYR B 1 154 ? 14.770  9.838   -1.718  1.00 98.56  ? 154 TYR B OH  1 
ATOM   4112 N  N   . ASP B 1 155 ? 14.482  1.379   -0.944  1.00 60.74  ? 155 ASP B N   1 
ATOM   4113 C  CA  . ASP B 1 155 ? 14.511  -0.104  -0.789  1.00 61.30  ? 155 ASP B CA  1 
ATOM   4114 C  C   . ASP B 1 155 ? 13.349  -0.559  0.115   1.00 55.21  ? 155 ASP B C   1 
ATOM   4115 O  O   . ASP B 1 155 ? 13.187  -1.786  0.312   1.00 55.55  ? 155 ASP B O   1 
ATOM   4116 C  CB  . ASP B 1 155 ? 15.870  -0.564  -0.257  1.00 60.30  ? 155 ASP B CB  1 
ATOM   4117 C  CG  . ASP B 1 155 ? 16.198  0.021   1.104   1.00 67.23  ? 155 ASP B CG  1 
ATOM   4118 O  OD1 . ASP B 1 155 ? 15.717  1.145   1.407   1.00 70.35  ? 155 ASP B OD1 1 
ATOM   4119 O  OD2 . ASP B 1 155 ? 16.917  -0.651  1.856   1.00 75.01  ? 155 ASP B OD2 1 
ATOM   4120 N  N   . CYS B 1 156 ? 12.558  0.388   0.627   1.00 44.53  ? 156 CYS B N   1 
ATOM   4121 C  CA  . CYS B 1 156 ? 11.436  0.131   1.567   1.00 39.37  ? 156 CYS B CA  1 
ATOM   4122 C  C   . CYS B 1 156 ? 10.156  -0.061  0.754   1.00 37.31  ? 156 CYS B C   1 
ATOM   4123 O  O   . CYS B 1 156 ? 9.798   0.860   -0.022  1.00 35.51  ? 156 CYS B O   1 
ATOM   4124 C  CB  . CYS B 1 156 ? 11.290  1.262   2.577   1.00 35.82  ? 156 CYS B CB  1 
ATOM   4125 S  SG  . CYS B 1 156 ? 9.900   1.061   3.727   1.00 41.55  ? 156 CYS B SG  1 
ATOM   4126 N  N   . VAL B 1 157 ? 9.522   -1.225  0.894   1.00 32.29  ? 157 VAL B N   1 
ATOM   4127 C  CA  . VAL B 1 157 ? 8.161   -1.489  0.346   1.00 33.25  ? 157 VAL B CA  1 
ATOM   4128 C  C   . VAL B 1 157 ? 7.109   -0.943  1.313   1.00 31.66  ? 157 VAL B C   1 
ATOM   4129 O  O   . VAL B 1 157 ? 7.068   -1.398  2.453   1.00 36.10  ? 157 VAL B O   1 
ATOM   4130 C  CB  . VAL B 1 157 ? 7.929   -2.983  0.085   1.00 29.70  ? 157 VAL B CB  1 
ATOM   4131 C  CG1 . VAL B 1 157 ? 6.551   -3.207  -0.520  1.00 30.96  ? 157 VAL B CG1 1 
ATOM   4132 C  CG2 . VAL B 1 157 ? 9.018   -3.543  -0.804  1.00 29.18  ? 157 VAL B CG2 1 
ATOM   4133 N  N   . SER B 1 158 ? 6.270   -0.028  0.849   1.00 28.41  ? 158 SER B N   1 
ATOM   4134 C  CA  . SER B 1 158 ? 5.085   0.486   1.580   1.00 29.73  ? 158 SER B CA  1 
ATOM   4135 C  C   . SER B 1 158 ? 3.842   -0.269  1.103   1.00 26.74  ? 158 SER B C   1 
ATOM   4136 O  O   . SER B 1 158 ? 3.418   -0.000  -0.019  1.00 26.00  ? 158 SER B O   1 
ATOM   4137 C  CB  . SER B 1 158 ? 4.946   1.978   1.386   1.00 28.68  ? 158 SER B CB  1 
ATOM   4138 O  OG  . SER B 1 158 ? 5.960   2.644   2.127   1.00 33.21  ? 158 SER B OG  1 
ATOM   4139 N  N   . PHE B 1 159 ? 3.304   -1.211  1.890   1.00 24.98  ? 159 PHE B N   1 
ATOM   4140 C  CA  . PHE B 1 159 ? 2.049   -1.941  1.549   1.00 25.54  ? 159 PHE B CA  1 
ATOM   4141 C  C   . PHE B 1 159 ? 0.834   -1.103  1.949   1.00 27.57  ? 159 PHE B C   1 
ATOM   4142 O  O   . PHE B 1 159 ? 0.812   -0.637  3.126   1.00 28.25  ? 159 PHE B O   1 
ATOM   4143 C  CB  . PHE B 1 159 ? 1.994   -3.285  2.259   1.00 25.69  ? 159 PHE B CB  1 
ATOM   4144 C  CG  . PHE B 1 159 ? 3.082   -4.251  1.873   1.00 25.47  ? 159 PHE B CG  1 
ATOM   4145 C  CD1 . PHE B 1 159 ? 2.940   -5.056  0.751   1.00 25.99  ? 159 PHE B CD1 1 
ATOM   4146 C  CD2 . PHE B 1 159 ? 4.190   -4.434  2.688   1.00 26.53  ? 159 PHE B CD2 1 
ATOM   4147 C  CE1 . PHE B 1 159 ? 3.894   -6.004  0.422   1.00 25.46  ? 159 PHE B CE1 1 
ATOM   4148 C  CE2 . PHE B 1 159 ? 5.138   -5.399  2.370   1.00 28.08  ? 159 PHE B CE2 1 
ATOM   4149 C  CZ  . PHE B 1 159 ? 5.003   -6.163  1.224   1.00 25.79  ? 159 PHE B CZ  1 
ATOM   4150 N  N   . CYS B 1 160 ? -0.106  -0.885  1.011   1.00 26.09  ? 160 CYS B N   1 
ATOM   4151 C  CA  . CYS B 1 160 ? -1.229  0.085   1.146   1.00 26.37  ? 160 CYS B CA  1 
ATOM   4152 C  C   . CYS B 1 160 ? -2.597  -0.566  0.880   1.00 26.62  ? 160 CYS B C   1 
ATOM   4153 O  O   . CYS B 1 160 ? -3.610  0.071   1.233   1.00 27.65  ? 160 CYS B O   1 
ATOM   4154 C  CB  . CYS B 1 160 ? -1.020  1.299   0.239   1.00 25.72  ? 160 CYS B CB  1 
ATOM   4155 S  SG  . CYS B 1 160 ? -0.899  0.909   -1.528  1.00 25.95  ? 160 CYS B SG  1 
ATOM   4156 N  N   . TYR B 1 161 ? -2.654  -1.778  0.311   1.00 24.44  ? 161 TYR B N   1 
ATOM   4157 C  CA  . TYR B 1 161 ? -3.912  -2.378  -0.196  1.00 23.90  ? 161 TYR B CA  1 
ATOM   4158 C  C   . TYR B 1 161 ? -3.893  -3.901  -0.051  1.00 22.99  ? 161 TYR B C   1 
ATOM   4159 O  O   . TYR B 1 161 ? -2.893  -4.546  -0.401  1.00 24.36  ? 161 TYR B O   1 
ATOM   4160 C  CB  . TYR B 1 161 ? -4.159  -2.016  -1.664  1.00 24.33  ? 161 TYR B CB  1 
ATOM   4161 C  CG  . TYR B 1 161 ? -5.489  -2.497  -2.207  1.00 25.71  ? 161 TYR B CG  1 
ATOM   4162 C  CD1 . TYR B 1 161 ? -6.666  -1.807  -1.948  1.00 25.73  ? 161 TYR B CD1 1 
ATOM   4163 C  CD2 . TYR B 1 161 ? -5.588  -3.678  -2.936  1.00 24.10  ? 161 TYR B CD2 1 
ATOM   4164 C  CE1 . TYR B 1 161 ? -7.888  -2.262  -2.421  1.00 25.80  ? 161 TYR B CE1 1 
ATOM   4165 C  CE2 . TYR B 1 161 ? -6.796  -4.144  -3.417  1.00 23.56  ? 161 TYR B CE2 1 
ATOM   4166 C  CZ  . TYR B 1 161 ? -7.957  -3.440  -3.161  1.00 26.64  ? 161 TYR B CZ  1 
ATOM   4167 O  OH  . TYR B 1 161 ? -9.159  -3.908  -3.636  1.00 24.72  ? 161 TYR B OH  1 
ATOM   4168 N  N   . MET B 1 162 ? -5.008  -4.452  0.413   1.00 22.49  ? 162 MET B N   1 
ATOM   4169 C  CA  . MET B 1 162 ? -5.300  -5.899  0.328   1.00 25.60  ? 162 MET B CA  1 
ATOM   4170 C  C   . MET B 1 162 ? -6.688  -6.078  -0.285  1.00 25.93  ? 162 MET B C   1 
ATOM   4171 O  O   . MET B 1 162 ? -7.637  -5.413  0.142   1.00 25.25  ? 162 MET B O   1 
ATOM   4172 C  CB  . MET B 1 162 ? -5.228  -6.593  1.687   1.00 25.91  ? 162 MET B CB  1 
ATOM   4173 C  CG  . MET B 1 162 ? -5.520  -8.070  1.593   1.00 29.47  ? 162 MET B CG  1 
ATOM   4174 S  SD  . MET B 1 162 ? -5.203  -8.997  3.118   1.00 33.78  ? 162 MET B SD  1 
ATOM   4175 C  CE  . MET B 1 162 ? -3.515  -9.511  2.787   1.00 32.93  ? 162 MET B CE  1 
ATOM   4176 N  N   . HIS B 1 163 ? -6.771  -6.957  -1.277  1.00 25.93  ? 163 HIS B N   1 
ATOM   4177 C  CA  . HIS B 1 163 ? -7.996  -7.191  -2.064  1.00 25.61  ? 163 HIS B CA  1 
ATOM   4178 C  C   . HIS B 1 163 ? -8.978  -8.051  -1.258  1.00 26.92  ? 163 HIS B C   1 
ATOM   4179 O  O   . HIS B 1 163 ? -8.591  -9.171  -0.824  1.00 28.98  ? 163 HIS B O   1 
ATOM   4180 C  CB  . HIS B 1 163 ? -7.651  -7.806  -3.428  1.00 25.62  ? 163 HIS B CB  1 
ATOM   4181 C  CG  . HIS B 1 163 ? -8.864  -7.946  -4.289  1.00 26.89  ? 163 HIS B CG  1 
ATOM   4182 N  ND1 . HIS B 1 163 ? -9.732  -6.892  -4.499  1.00 28.07  ? 163 HIS B ND1 1 
ATOM   4183 C  CD2 . HIS B 1 163 ? -9.397  -9.011  -4.924  1.00 31.06  ? 163 HIS B CD2 1 
ATOM   4184 C  CE1 . HIS B 1 163 ? -10.739 -7.298  -5.253  1.00 28.70  ? 163 HIS B CE1 1 
ATOM   4185 N  NE2 . HIS B 1 163 ? -10.543 -8.592  -5.545  1.00 30.03  ? 163 HIS B NE2 1 
ATOM   4186 N  N   . HIS B 1 164 ? -10.214 -7.567  -1.109  1.00 28.76  ? 164 HIS B N   1 
ATOM   4187 C  CA  . HIS B 1 164 ? -11.327 -8.265  -0.410  1.00 29.50  ? 164 HIS B CA  1 
ATOM   4188 C  C   . HIS B 1 164 ? -12.456 -8.660  -1.383  1.00 30.77  ? 164 HIS B C   1 
ATOM   4189 O  O   . HIS B 1 164 ? -12.884 -9.803  -1.265  1.00 31.63  ? 164 HIS B O   1 
ATOM   4190 C  CB  . HIS B 1 164 ? -11.853 -7.409  0.751   1.00 32.04  ? 164 HIS B CB  1 
ATOM   4191 C  CG  . HIS B 1 164 ? -10.920 -7.360  1.912   1.00 33.75  ? 164 HIS B CG  1 
ATOM   4192 N  ND1 . HIS B 1 164 ? -11.178 -8.023  3.098   1.00 35.86  ? 164 HIS B ND1 1 
ATOM   4193 C  CD2 . HIS B 1 164 ? -9.704  -6.786  2.049   1.00 36.34  ? 164 HIS B CD2 1 
ATOM   4194 C  CE1 . HIS B 1 164 ? -10.177 -7.824  3.931   1.00 35.80  ? 164 HIS B CE1 1 
ATOM   4195 N  NE2 . HIS B 1 164 ? -9.247  -7.071  3.306   1.00 34.08  ? 164 HIS B NE2 1 
ATOM   4196 N  N   . MET B 1 165 ? -12.943 -7.779  -2.281  1.00 29.94  ? 165 MET B N   1 
ATOM   4197 C  CA  . MET B 1 165 ? -14.225 -8.035  -2.997  1.00 33.45  ? 165 MET B CA  1 
ATOM   4198 C  C   . MET B 1 165 ? -14.354 -7.277  -4.328  1.00 34.76  ? 165 MET B C   1 
ATOM   4199 O  O   . MET B 1 165 ? -13.686 -6.226  -4.538  1.00 31.82  ? 165 MET B O   1 
ATOM   4200 C  CB  . MET B 1 165 ? -15.414 -7.657  -2.095  1.00 35.56  ? 165 MET B CB  1 
ATOM   4201 C  CG  . MET B 1 165 ? -15.554 -6.151  -1.835  1.00 40.53  ? 165 MET B CG  1 
ATOM   4202 S  SD  . MET B 1 165 ? -16.750 -5.658  -0.515  1.00 47.88  ? 165 MET B SD  1 
ATOM   4203 C  CE  . MET B 1 165 ? -16.626 -7.124  0.509   1.00 49.81  ? 165 MET B CE  1 
ATOM   4204 N  N   . GLU B 1 166 ? -15.274 -7.756  -5.164  1.00 35.25  ? 166 GLU B N   1 
ATOM   4205 C  CA  . GLU B 1 166 ? -15.694 -7.078  -6.421  1.00 38.16  ? 166 GLU B CA  1 
ATOM   4206 C  C   . GLU B 1 166 ? -17.117 -6.529  -6.230  1.00 37.96  ? 166 GLU B C   1 
ATOM   4207 O  O   . GLU B 1 166 ? -17.967 -7.278  -5.750  1.00 36.69  ? 166 GLU B O   1 
ATOM   4208 C  CB  . GLU B 1 166 ? -15.623 -8.051  -7.599  1.00 36.46  ? 166 GLU B CB  1 
ATOM   4209 C  CG  . GLU B 1 166 ? -16.052 -7.405  -8.901  1.00 38.36  ? 166 GLU B CG  1 
ATOM   4210 C  CD  . GLU B 1 166 ? -15.649 -8.150  -10.161 1.00 40.64  ? 166 GLU B CD  1 
ATOM   4211 O  OE1 . GLU B 1 166 ? -14.436 -8.297  -10.416 1.00 39.32  ? 166 GLU B OE1 1 
ATOM   4212 O  OE2 . GLU B 1 166 ? -16.553 -8.586  -10.887 1.00 50.23  ? 166 GLU B OE2 1 
ATOM   4213 N  N   . LEU B 1 167 ? -17.356 -5.263  -6.560  1.00 37.44  ? 167 LEU B N   1 
ATOM   4214 C  CA  . LEU B 1 167 ? -18.702 -4.632  -6.498  1.00 36.96  ? 167 LEU B CA  1 
ATOM   4215 C  C   . LEU B 1 167 ? -19.452 -4.952  -7.787  1.00 40.65  ? 167 LEU B C   1 
ATOM   4216 O  O   . LEU B 1 167 ? -18.842 -5.364  -8.774  1.00 41.46  ? 167 LEU B O   1 
ATOM   4217 C  CB  . LEU B 1 167 ? -18.534 -3.122  -6.296  1.00 36.40  ? 167 LEU B CB  1 
ATOM   4218 C  CG  . LEU B 1 167 ? -17.850 -2.732  -4.985  1.00 37.77  ? 167 LEU B CG  1 
ATOM   4219 C  CD1 . LEU B 1 167 ? -17.439 -1.270  -4.995  1.00 38.32  ? 167 LEU B CD1 1 
ATOM   4220 C  CD2 . LEU B 1 167 ? -18.754 -3.045  -3.805  1.00 38.33  ? 167 LEU B CD2 1 
ATOM   4221 N  N   . PRO B 1 168 ? -20.795 -4.779  -7.826  1.00 45.73  ? 168 PRO B N   1 
ATOM   4222 C  CA  . PRO B 1 168 ? -21.598 -5.254  -8.957  1.00 44.96  ? 168 PRO B CA  1 
ATOM   4223 C  C   . PRO B 1 168 ? -21.154 -4.635  -10.292 1.00 45.52  ? 168 PRO B C   1 
ATOM   4224 O  O   . PRO B 1 168 ? -21.200 -5.318  -11.280 1.00 51.14  ? 168 PRO B O   1 
ATOM   4225 C  CB  . PRO B 1 168 ? -23.038 -4.856  -8.582  1.00 45.51  ? 168 PRO B CB  1 
ATOM   4226 C  CG  . PRO B 1 168 ? -23.001 -4.726  -7.079  1.00 47.98  ? 168 PRO B CG  1 
ATOM   4227 C  CD  . PRO B 1 168 ? -21.624 -4.162  -6.779  1.00 47.38  ? 168 PRO B CD  1 
ATOM   4228 N  N   . THR B 1 169 ? -20.664 -3.397  -10.276 1.00 44.12  ? 169 THR B N   1 
ATOM   4229 C  CA  . THR B 1 169 ? -20.247 -2.652  -11.493 1.00 44.83  ? 169 THR B CA  1 
ATOM   4230 C  C   . THR B 1 169 ? -18.868 -3.109  -12.009 1.00 43.45  ? 169 THR B C   1 
ATOM   4231 O  O   . THR B 1 169 ? -18.384 -2.471  -12.955 1.00 40.98  ? 169 THR B O   1 
ATOM   4232 C  CB  . THR B 1 169 ? -20.230 -1.149  -11.210 1.00 45.07  ? 169 THR B CB  1 
ATOM   4233 O  OG1 . THR B 1 169 ? -19.383 -0.991  -10.075 1.00 45.61  ? 169 THR B OG1 1 
ATOM   4234 C  CG2 . THR B 1 169 ? -21.609 -0.587  -10.936 1.00 48.47  ? 169 THR B CG2 1 
ATOM   4235 N  N   . GLY B 1 170 ? -18.234 -4.132  -11.418 1.00 39.83  ? 170 GLY B N   1 
ATOM   4236 C  CA  . GLY B 1 170 ? -16.955 -4.685  -11.914 1.00 36.23  ? 170 GLY B CA  1 
ATOM   4237 C  C   . GLY B 1 170 ? -15.716 -3.997  -11.328 1.00 39.55  ? 170 GLY B C   1 
ATOM   4238 O  O   . GLY B 1 170 ? -14.598 -4.426  -11.688 1.00 39.71  ? 170 GLY B O   1 
ATOM   4239 N  N   . VAL B 1 171 ? -15.876 -3.000  -10.444 1.00 33.28  ? 171 VAL B N   1 
ATOM   4240 C  CA  . VAL B 1 171 ? -14.753 -2.327  -9.723  1.00 32.26  ? 171 VAL B CA  1 
ATOM   4241 C  C   . VAL B 1 171 ? -14.489 -3.046  -8.387  1.00 32.52  ? 171 VAL B C   1 
ATOM   4242 O  O   . VAL B 1 171 ? -15.261 -3.963  -8.042  1.00 29.67  ? 171 VAL B O   1 
ATOM   4243 C  CB  . VAL B 1 171 ? -15.038 -0.825  -9.527  1.00 36.14  ? 171 VAL B CB  1 
ATOM   4244 C  CG1 . VAL B 1 171 ? -15.189 -0.108  -10.875 1.00 38.71  ? 171 VAL B CG1 1 
ATOM   4245 C  CG2 . VAL B 1 171 ? -16.239 -0.577  -8.629  1.00 35.46  ? 171 VAL B CG2 1 
ATOM   4246 N  N   . HIS B 1 172 ? -13.418 -2.668  -7.676  1.00 30.44  ? 172 HIS B N   1 
ATOM   4247 C  CA  . HIS B 1 172 ? -12.797 -3.496  -6.602  1.00 29.58  ? 172 HIS B CA  1 
ATOM   4248 C  C   . HIS B 1 172 ? -12.657 -2.693  -5.302  1.00 26.79  ? 172 HIS B C   1 
ATOM   4249 O  O   . HIS B 1 172 ? -12.399 -1.475  -5.351  1.00 26.35  ? 172 HIS B O   1 
ATOM   4250 C  CB  . HIS B 1 172 ? -11.493 -4.117  -7.112  1.00 30.05  ? 172 HIS B CB  1 
ATOM   4251 C  CG  . HIS B 1 172 ? -11.728 -5.021  -8.275  1.00 35.34  ? 172 HIS B CG  1 
ATOM   4252 N  ND1 . HIS B 1 172 ? -11.468 -4.628  -9.581  1.00 33.25  ? 172 HIS B ND1 1 
ATOM   4253 C  CD2 . HIS B 1 172 ? -12.269 -6.263  -8.347  1.00 34.66  ? 172 HIS B CD2 1 
ATOM   4254 C  CE1 . HIS B 1 172 ? -11.809 -5.602  -10.396 1.00 32.80  ? 172 HIS B CE1 1 
ATOM   4255 N  NE2 . HIS B 1 172 ? -12.285 -6.618  -9.668  1.00 34.75  ? 172 HIS B NE2 1 
ATOM   4256 N  N   . ALA B 1 173 ? -12.865 -3.368  -4.174  1.00 26.37  ? 173 ALA B N   1 
ATOM   4257 C  CA  . ALA B 1 173 ? -12.799 -2.808  -2.812  1.00 24.84  ? 173 ALA B CA  1 
ATOM   4258 C  C   . ALA B 1 173 ? -11.914 -3.709  -1.949  1.00 24.94  ? 173 ALA B C   1 
ATOM   4259 O  O   . ALA B 1 173 ? -11.970 -4.963  -2.103  1.00 24.24  ? 173 ALA B O   1 
ATOM   4260 C  CB  . ALA B 1 173 ? -14.196 -2.705  -2.238  1.00 28.27  ? 173 ALA B CB  1 
ATOM   4261 N  N   . GLY B 1 174 ? -11.141 -3.082  -1.067  1.00 24.49  ? 174 GLY B N   1 
ATOM   4262 C  CA  . GLY B 1 174 ? -10.227 -3.763  -0.133  1.00 24.15  ? 174 GLY B CA  1 
ATOM   4263 C  C   . GLY B 1 174 ? -9.814  -2.846  1.003   1.00 23.42  ? 174 GLY B C   1 
ATOM   4264 O  O   . GLY B 1 174 ? -10.431 -1.785  1.181   1.00 22.37  ? 174 GLY B O   1 
ATOM   4265 N  N   . THR B 1 175 ? -8.830  -3.268  1.791   1.00 23.27  ? 175 THR B N   1 
ATOM   4266 C  CA  . THR B 1 175 ? -8.451  -2.593  3.049   1.00 24.28  ? 175 THR B CA  1 
ATOM   4267 C  C   . THR B 1 175 ? -6.990  -2.183  2.968   1.00 25.06  ? 175 THR B C   1 
ATOM   4268 O  O   . THR B 1 175 ? -6.288  -2.681  2.081   1.00 26.61  ? 175 THR B O   1 
ATOM   4269 C  CB  . THR B 1 175 ? -8.650  -3.522  4.253   1.00 27.20  ? 175 THR B CB  1 
ATOM   4270 O  OG1 . THR B 1 175 ? -7.758  -4.638  4.146   1.00 25.58  ? 175 THR B OG1 1 
ATOM   4271 C  CG2 . THR B 1 175 ? -10.079 -3.990  4.364   1.00 27.64  ? 175 THR B CG2 1 
ATOM   4272 N  N   . ASP B 1 176 ? -6.558  -1.332  3.885   1.00 24.78  ? 176 ASP B N   1 
ATOM   4273 C  CA  . ASP B 1 176 ? -5.126  -1.218  4.210   1.00 23.77  ? 176 ASP B CA  1 
ATOM   4274 C  C   . ASP B 1 176 ? -4.732  -2.521  4.918   1.00 23.30  ? 176 ASP B C   1 
ATOM   4275 O  O   . ASP B 1 176 ? -5.610  -3.390  5.146   1.00 22.62  ? 176 ASP B O   1 
ATOM   4276 C  CB  . ASP B 1 176 ? -4.846  0.059   4.985   1.00 24.84  ? 176 ASP B CB  1 
ATOM   4277 C  CG  . ASP B 1 176 ? -5.485  0.117   6.349   1.00 25.79  ? 176 ASP B CG  1 
ATOM   4278 O  OD1 . ASP B 1 176 ? -5.741  -0.956  6.956   1.00 25.77  ? 176 ASP B OD1 1 
ATOM   4279 O  OD2 . ASP B 1 176 ? -5.737  1.227   6.773   1.00 25.72  ? 176 ASP B OD2 1 
ATOM   4280 N  N   . LEU B 1 177 ? -3.456  -2.641  5.279   1.00 24.90  ? 177 LEU B N   1 
ATOM   4281 C  CA  . LEU B 1 177 ? -2.890  -3.887  5.861   1.00 24.52  ? 177 LEU B CA  1 
ATOM   4282 C  C   . LEU B 1 177 ? -3.178  -3.949  7.360   1.00 28.07  ? 177 LEU B C   1 
ATOM   4283 O  O   . LEU B 1 177 ? -2.841  -4.978  7.955   1.00 28.11  ? 177 LEU B O   1 
ATOM   4284 C  CB  . LEU B 1 177 ? -1.394  -3.961  5.553   1.00 23.25  ? 177 LEU B CB  1 
ATOM   4285 C  CG  . LEU B 1 177 ? -1.036  -4.756  4.303   1.00 24.63  ? 177 LEU B CG  1 
ATOM   4286 C  CD1 . LEU B 1 177 ? -1.422  -6.231  4.455   1.00 25.29  ? 177 LEU B CD1 1 
ATOM   4287 C  CD2 . LEU B 1 177 ? -1.679  -4.146  3.066   1.00 22.69  ? 177 LEU B CD2 1 
ATOM   4288 N  N   . GLU B 1 178 ? -3.809  -2.917  7.929   1.00 28.15  ? 178 GLU B N   1 
ATOM   4289 C  CA  . GLU B 1 178 ? -4.341  -2.942  9.316   1.00 30.86  ? 178 GLU B CA  1 
ATOM   4290 C  C   . GLU B 1 178 ? -5.836  -3.279  9.264   1.00 29.51  ? 178 GLU B C   1 
ATOM   4291 O  O   . GLU B 1 178 ? -6.482  -3.191  10.307  1.00 32.44  ? 178 GLU B O   1 
ATOM   4292 C  CB  . GLU B 1 178 ? -4.138  -1.592  10.010  1.00 31.06  ? 178 GLU B CB  1 
ATOM   4293 C  CG  . GLU B 1 178 ? -2.688  -1.201  10.214  1.00 34.44  ? 178 GLU B CG  1 
ATOM   4294 C  CD  . GLU B 1 178 ? -2.539  0.244   10.668  1.00 40.03  ? 178 GLU B CD  1 
ATOM   4295 O  OE1 . GLU B 1 178 ? -3.349  1.082   10.258  1.00 53.19  ? 178 GLU B OE1 1 
ATOM   4296 O  OE2 . GLU B 1 178 ? -1.622  0.533   11.424  1.00 46.31  ? 178 GLU B OE2 1 
ATOM   4297 N  N   . GLY B 1 179 ? -6.363  -3.607  8.079   1.00 28.29  ? 179 GLY B N   1 
ATOM   4298 C  CA  . GLY B 1 179 ? -7.734  -4.133  7.889   1.00 28.35  ? 179 GLY B CA  1 
ATOM   4299 C  C   . GLY B 1 179 ? -8.838  -3.081  7.866   1.00 26.76  ? 179 GLY B C   1 
ATOM   4300 O  O   . GLY B 1 179 ? -10.018 -3.473  7.966   1.00 30.63  ? 179 GLY B O   1 
ATOM   4301 N  N   . ASN B 1 180 ? -8.506  -1.802  7.719   1.00 26.74  ? 180 ASN B N   1 
ATOM   4302 C  CA  . ASN B 1 180 ? -9.498  -0.713  7.550   1.00 26.94  ? 180 ASN B CA  1 
ATOM   4303 C  C   . ASN B 1 180 ? -9.871  -0.606  6.073   1.00 27.56  ? 180 ASN B C   1 
ATOM   4304 O  O   . ASN B 1 180 ? -8.949  -0.372  5.252   1.00 25.59  ? 180 ASN B O   1 
ATOM   4305 C  CB  . ASN B 1 180 ? -8.944  0.644   7.973   1.00 29.33  ? 180 ASN B CB  1 
ATOM   4306 C  CG  . ASN B 1 180 ? -8.306  0.657   9.343   1.00 33.59  ? 180 ASN B CG  1 
ATOM   4307 O  OD1 . ASN B 1 180 ? -7.103  0.917   9.463   1.00 41.86  ? 180 ASN B OD1 1 
ATOM   4308 N  ND2 . ASN B 1 180 ? -9.096  0.401   10.368  1.00 26.14  ? 180 ASN B ND2 1 
ATOM   4309 N  N   . PHE B 1 181 ? -11.150 -0.741  5.735   1.00 25.38  ? 181 PHE B N   1 
ATOM   4310 C  CA  . PHE B 1 181 ? -11.639 -0.572  4.342   1.00 28.01  ? 181 PHE B CA  1 
ATOM   4311 C  C   . PHE B 1 181 ? -11.278 0.829   3.849   1.00 28.57  ? 181 PHE B C   1 
ATOM   4312 O  O   . PHE B 1 181 ? -11.262 1.806   4.647   1.00 27.46  ? 181 PHE B O   1 
ATOM   4313 C  CB  . PHE B 1 181 ? -13.150 -0.818  4.194   1.00 27.04  ? 181 PHE B CB  1 
ATOM   4314 C  CG  . PHE B 1 181 ? -13.457 -2.211  3.720   1.00 26.09  ? 181 PHE B CG  1 
ATOM   4315 C  CD1 . PHE B 1 181 ? -13.404 -2.533  2.375   1.00 28.26  ? 181 PHE B CD1 1 
ATOM   4316 C  CD2 . PHE B 1 181 ? -13.737 -3.214  4.632   1.00 25.64  ? 181 PHE B CD2 1 
ATOM   4317 C  CE1 . PHE B 1 181 ? -13.597 -3.844  1.958   1.00 26.91  ? 181 PHE B CE1 1 
ATOM   4318 C  CE2 . PHE B 1 181 ? -13.939 -4.517  4.214   1.00 26.32  ? 181 PHE B CE2 1 
ATOM   4319 C  CZ  . PHE B 1 181 ? -13.885 -4.824  2.878   1.00 28.56  ? 181 PHE B CZ  1 
ATOM   4320 N  N   . TYR B 1 182 ? -10.966 0.913   2.556   1.00 28.48  ? 182 TYR B N   1 
ATOM   4321 C  CA  . TYR B 1 182 ? -11.061 2.158   1.767   1.00 28.11  ? 182 TYR B CA  1 
ATOM   4322 C  C   . TYR B 1 182 ? -12.503 2.207   1.262   1.00 27.82  ? 182 TYR B C   1 
ATOM   4323 O  O   . TYR B 1 182 ? -12.945 1.239   0.587   1.00 27.67  ? 182 TYR B O   1 
ATOM   4324 C  CB  . TYR B 1 182 ? -10.067 2.190   0.604   1.00 27.76  ? 182 TYR B CB  1 
ATOM   4325 C  CG  . TYR B 1 182 ? -8.604  2.213   0.987   1.00 28.19  ? 182 TYR B CG  1 
ATOM   4326 C  CD1 . TYR B 1 182 ? -7.958  3.402   1.282   1.00 27.03  ? 182 TYR B CD1 1 
ATOM   4327 C  CD2 . TYR B 1 182 ? -7.850  1.048   1.014   1.00 25.87  ? 182 TYR B CD2 1 
ATOM   4328 C  CE1 . TYR B 1 182 ? -6.610  3.432   1.601   1.00 27.71  ? 182 TYR B CE1 1 
ATOM   4329 C  CE2 . TYR B 1 182 ? -6.505  1.065   1.339   1.00 24.76  ? 182 TYR B CE2 1 
ATOM   4330 C  CZ  . TYR B 1 182 ? -5.880  2.259   1.653   1.00 26.02  ? 182 TYR B CZ  1 
ATOM   4331 O  OH  . TYR B 1 182 ? -4.543  2.306   1.958   1.00 24.25  ? 182 TYR B OH  1 
ATOM   4332 N  N   . GLY B 1 183 ? -13.220 3.259   1.643   1.00 27.40  ? 183 GLY B N   1 
ATOM   4333 C  CA  . GLY B 1 183 ? -14.599 3.519   1.197   1.00 29.77  ? 183 GLY B CA  1 
ATOM   4334 C  C   . GLY B 1 183 ? -15.640 2.925   2.134   1.00 29.43  ? 183 GLY B C   1 
ATOM   4335 O  O   . GLY B 1 183 ? -15.329 2.122   3.020   1.00 28.60  ? 183 GLY B O   1 
ATOM   4336 N  N   . PRO B 1 184 ? -16.925 3.258   1.907   1.00 31.22  ? 184 PRO B N   1 
ATOM   4337 C  CA  . PRO B 1 184 ? -17.990 2.878   2.835   1.00 31.03  ? 184 PRO B CA  1 
ATOM   4338 C  C   . PRO B 1 184 ? -18.500 1.447   2.592   1.00 32.14  ? 184 PRO B C   1 
ATOM   4339 O  O   . PRO B 1 184 ? -19.685 1.271   2.357   1.00 28.65  ? 184 PRO B O   1 
ATOM   4340 C  CB  . PRO B 1 184 ? -19.044 3.967   2.550   1.00 30.54  ? 184 PRO B CB  1 
ATOM   4341 C  CG  . PRO B 1 184 ? -18.879 4.291   1.075   1.00 28.95  ? 184 PRO B CG  1 
ATOM   4342 C  CD  . PRO B 1 184 ? -17.407 4.081   0.783   1.00 29.22  ? 184 PRO B CD  1 
ATOM   4343 N  N   . PHE B 1 185 ? -17.597 0.465   2.678   1.00 30.24  ? 185 PHE B N   1 
ATOM   4344 C  CA  . PHE B 1 185 ? -17.831 -0.957  2.311   1.00 29.60  ? 185 PHE B CA  1 
ATOM   4345 C  C   . PHE B 1 185 ? -17.676 -1.820  3.558   1.00 28.87  ? 185 PHE B C   1 
ATOM   4346 O  O   . PHE B 1 185 ? -16.971 -1.416  4.464   1.00 28.34  ? 185 PHE B O   1 
ATOM   4347 C  CB  . PHE B 1 185 ? -16.920 -1.383  1.146   1.00 31.06  ? 185 PHE B CB  1 
ATOM   4348 C  CG  . PHE B 1 185 ? -17.081 -0.476  -0.053  1.00 30.44  ? 185 PHE B CG  1 
ATOM   4349 C  CD1 . PHE B 1 185 ? -18.306 -0.373  -0.693  1.00 29.71  ? 185 PHE B CD1 1 
ATOM   4350 C  CD2 . PHE B 1 185 ? -16.052 0.340   -0.478  1.00 29.91  ? 185 PHE B CD2 1 
ATOM   4351 C  CE1 . PHE B 1 185 ? -18.491 0.521   -1.737  1.00 34.67  ? 185 PHE B CE1 1 
ATOM   4352 C  CE2 . PHE B 1 185 ? -16.223 1.194   -1.560  1.00 32.24  ? 185 PHE B CE2 1 
ATOM   4353 C  CZ  . PHE B 1 185 ? -17.443 1.294   -2.182  1.00 32.15  ? 185 PHE B CZ  1 
ATOM   4354 N  N   . VAL B 1 186 ? -18.302 -2.994  3.553   1.00 28.14  ? 186 VAL B N   1 
ATOM   4355 C  CA  . VAL B 1 186 ? -18.196 -4.008  4.637   1.00 29.95  ? 186 VAL B CA  1 
ATOM   4356 C  C   . VAL B 1 186 ? -17.968 -5.385  4.007   1.00 30.85  ? 186 VAL B C   1 
ATOM   4357 O  O   . VAL B 1 186 ? -18.448 -5.624  2.876   1.00 31.73  ? 186 VAL B O   1 
ATOM   4358 C  CB  . VAL B 1 186 ? -19.464 -3.980  5.502   1.00 32.89  ? 186 VAL B CB  1 
ATOM   4359 C  CG1 . VAL B 1 186 ? -19.744 -2.590  6.026   1.00 34.04  ? 186 VAL B CG1 1 
ATOM   4360 C  CG2 . VAL B 1 186 ? -20.668 -4.501  4.734   1.00 33.79  ? 186 VAL B CG2 1 
ATOM   4361 N  N   . ASP B 1 187 ? -17.261 -6.277  4.703   1.00 32.51  ? 187 ASP B N   1 
ATOM   4362 C  CA  . ASP B 1 187 ? -17.014 -7.654  4.198   1.00 32.51  ? 187 ASP B CA  1 
ATOM   4363 C  C   . ASP B 1 187 ? -18.214 -8.536  4.571   1.00 36.01  ? 187 ASP B C   1 
ATOM   4364 O  O   . ASP B 1 187 ? -18.097 -9.396  5.472   1.00 40.61  ? 187 ASP B O   1 
ATOM   4365 C  CB  . ASP B 1 187 ? -15.687 -8.215  4.693   1.00 30.66  ? 187 ASP B CB  1 
ATOM   4366 C  CG  . ASP B 1 187 ? -15.426 -8.039  6.180   1.00 30.56  ? 187 ASP B CG  1 
ATOM   4367 O  OD1 . ASP B 1 187 ? -16.260 -7.403  6.872   1.00 31.23  ? 187 ASP B OD1 1 
ATOM   4368 O  OD2 . ASP B 1 187 ? -14.373 -8.515  6.624   1.00 32.81  ? 187 ASP B OD2 1 
ATOM   4369 N  N   . ARG B 1 188 ? -19.321 -8.363  3.866   1.00 44.33  ? 188 ARG B N   1 
ATOM   4370 C  CA  . ARG B 1 188 ? -20.466 -9.307  3.917   1.00 54.79  ? 188 ARG B CA  1 
ATOM   4371 C  C   . ARG B 1 188 ? -21.135 -9.344  2.542   1.00 56.51  ? 188 ARG B C   1 
ATOM   4372 O  O   . ARG B 1 188 ? -21.109 -8.306  1.837   1.00 47.58  ? 188 ARG B O   1 
ATOM   4373 C  CB  . ARG B 1 188 ? -21.439 -8.909  5.030   1.00 58.83  ? 188 ARG B CB  1 
ATOM   4374 C  CG  . ARG B 1 188 ? -22.423 -7.811  4.652   1.00 66.00  ? 188 ARG B CG  1 
ATOM   4375 C  CD  . ARG B 1 188 ? -23.283 -7.381  5.827   1.00 71.34  ? 188 ARG B CD  1 
ATOM   4376 N  NE  . ARG B 1 188 ? -22.420 -7.143  6.974   1.00 79.57  ? 188 ARG B NE  1 
ATOM   4377 C  CZ  . ARG B 1 188 ? -22.767 -7.293  8.242   1.00 86.20  ? 188 ARG B CZ  1 
ATOM   4378 N  NH1 . ARG B 1 188 ? -23.992 -7.673  8.572   1.00 99.67  ? 188 ARG B NH1 1 
ATOM   4379 N  NH2 . ARG B 1 188 ? -21.870 -7.072  9.182   1.00 84.61  ? 188 ARG B NH2 1 
ATOM   4380 N  N   . GLN B 1 189 ? -21.687 -10.503 2.179   1.00 63.79  ? 189 GLN B N   1 
ATOM   4381 C  CA  . GLN B 1 189 ? -22.637 -10.626 1.047   1.00 69.51  ? 189 GLN B CA  1 
ATOM   4382 C  C   . GLN B 1 189 ? -23.886 -9.824  1.427   1.00 67.40  ? 189 GLN B C   1 
ATOM   4383 O  O   . GLN B 1 189 ? -24.739 -10.361 2.156   1.00 71.92  ? 189 GLN B O   1 
ATOM   4384 C  CB  . GLN B 1 189 ? -22.936 -12.092 0.713   1.00 72.34  ? 189 GLN B CB  1 
ATOM   4385 C  CG  . GLN B 1 189 ? -23.802 -12.249 -0.526  1.00 77.07  ? 189 GLN B CG  1 
ATOM   4386 C  CD  . GLN B 1 189 ? -23.345 -11.316 -1.623  1.00 82.23  ? 189 GLN B CD  1 
ATOM   4387 O  OE1 . GLN B 1 189 ? -24.000 -10.320 -1.929  1.00 88.46  ? 189 GLN B OE1 1 
ATOM   4388 N  NE2 . GLN B 1 189 ? -22.173 -11.591 -2.180  1.00 81.89  ? 189 GLN B NE2 1 
ATOM   4389 N  N   . THR B 1 190 ? -23.912 -8.549  1.030   1.00 62.07  ? 190 THR B N   1 
ATOM   4390 C  CA  . THR B 1 190 ? -25.066 -7.620  1.141   1.00 56.32  ? 190 THR B CA  1 
ATOM   4391 C  C   . THR B 1 190 ? -25.008 -6.682  -0.069  1.00 55.32  ? 190 THR B C   1 
ATOM   4392 O  O   . THR B 1 190 ? -24.054 -6.813  -0.869  1.00 59.27  ? 190 THR B O   1 
ATOM   4393 C  CB  . THR B 1 190 ? -25.104 -6.904  2.504   1.00 58.20  ? 190 THR B CB  1 
ATOM   4394 O  OG1 . THR B 1 190 ? -26.470 -6.632  2.806   1.00 57.94  ? 190 THR B OG1 1 
ATOM   4395 C  CG2 . THR B 1 190 ? -24.336 -5.597  2.570   1.00 55.73  ? 190 THR B CG2 1 
ATOM   4396 N  N   . ALA B 1 191 ? -26.006 -5.802  -0.210  1.00 52.87  ? 191 ALA B N   1 
ATOM   4397 C  CA  . ALA B 1 191 ? -26.157 -4.871  -1.355  1.00 50.89  ? 191 ALA B CA  1 
ATOM   4398 C  C   . ALA B 1 191 ? -25.214 -3.689  -1.137  1.00 44.87  ? 191 ALA B C   1 
ATOM   4399 O  O   . ALA B 1 191 ? -25.373 -2.998  -0.106  1.00 47.19  ? 191 ALA B O   1 
ATOM   4400 C  CB  . ALA B 1 191 ? -27.592 -4.412  -1.478  1.00 51.71  ? 191 ALA B CB  1 
ATOM   4401 N  N   . GLN B 1 192 ? -24.236 -3.503  -2.028  1.00 41.18  ? 192 GLN B N   1 
ATOM   4402 C  CA  . GLN B 1 192 ? -23.233 -2.406  -1.937  1.00 37.26  ? 192 GLN B CA  1 
ATOM   4403 C  C   . GLN B 1 192 ? -22.931 -1.905  -3.345  1.00 37.95  ? 192 GLN B C   1 
ATOM   4404 O  O   . GLN B 1 192 ? -22.863 -2.727  -4.264  1.00 38.44  ? 192 GLN B O   1 
ATOM   4405 C  CB  . GLN B 1 192 ? -21.949 -2.874  -1.251  1.00 35.87  ? 192 GLN B CB  1 
ATOM   4406 C  CG  . GLN B 1 192 ? -22.158 -3.759  -0.035  1.00 34.32  ? 192 GLN B CG  1 
ATOM   4407 C  CD  . GLN B 1 192 ? -20.873 -3.954  0.733   1.00 34.22  ? 192 GLN B CD  1 
ATOM   4408 O  OE1 . GLN B 1 192 ? -20.273 -2.990  1.178   1.00 33.30  ? 192 GLN B OE1 1 
ATOM   4409 N  NE2 . GLN B 1 192 ? -20.431 -5.194  0.879   1.00 31.50  ? 192 GLN B NE2 1 
ATOM   4410 N  N   . ALA B 1 193 ? -22.801 -0.592  -3.513  1.00 38.10  ? 193 ALA B N   1 
ATOM   4411 C  CA  . ALA B 1 193 ? -22.546 0.037   -4.826  1.00 39.04  ? 193 ALA B CA  1 
ATOM   4412 C  C   . ALA B 1 193 ? -21.413 1.048   -4.672  1.00 39.92  ? 193 ALA B C   1 
ATOM   4413 O  O   . ALA B 1 193 ? -21.264 1.638   -3.587  1.00 39.23  ? 193 ALA B O   1 
ATOM   4414 C  CB  . ALA B 1 193 ? -23.799 0.690   -5.366  1.00 36.18  ? 193 ALA B CB  1 
ATOM   4415 N  N   . ALA B 1 194 ? -20.640 1.224   -5.735  1.00 42.42  ? 194 ALA B N   1 
ATOM   4416 C  CA  . ALA B 1 194 ? -19.682 2.341   -5.883  1.00 48.30  ? 194 ALA B CA  1 
ATOM   4417 C  C   . ALA B 1 194 ? -20.460 3.665   -5.961  1.00 46.51  ? 194 ALA B C   1 
ATOM   4418 O  O   . ALA B 1 194 ? -21.346 3.780   -6.826  1.00 46.95  ? 194 ALA B O   1 
ATOM   4419 C  CB  . ALA B 1 194 ? -18.845 2.115   -7.120  1.00 49.06  ? 194 ALA B CB  1 
ATOM   4420 N  N   . GLY B 1 195 ? -20.159 4.612   -5.073  1.00 45.20  ? 195 GLY B N   1 
ATOM   4421 C  CA  . GLY B 1 195 ? -20.509 6.033   -5.252  1.00 45.08  ? 195 GLY B CA  1 
ATOM   4422 C  C   . GLY B 1 195 ? -20.131 6.506   -6.645  1.00 46.25  ? 195 GLY B C   1 
ATOM   4423 O  O   . GLY B 1 195 ? -19.259 5.886   -7.292  1.00 44.83  ? 195 GLY B O   1 
ATOM   4424 N  N   . THR B 1 196 ? -20.792 7.546   -7.139  1.00 45.73  ? 196 THR B N   1 
ATOM   4425 C  CA  . THR B 1 196 ? -20.472 8.128   -8.460  1.00 45.56  ? 196 THR B CA  1 
ATOM   4426 C  C   . THR B 1 196 ? -19.030 8.652   -8.345  1.00 42.51  ? 196 THR B C   1 
ATOM   4427 O  O   . THR B 1 196 ? -18.680 9.280   -7.341  1.00 40.51  ? 196 THR B O   1 
ATOM   4428 C  CB  . THR B 1 196 ? -21.584 9.092   -8.891  1.00 47.31  ? 196 THR B CB  1 
ATOM   4429 O  OG1 . THR B 1 196 ? -21.609 10.141  -7.934  1.00 48.48  ? 196 THR B OG1 1 
ATOM   4430 C  CG2 . THR B 1 196 ? -22.952 8.444   -8.949  1.00 48.49  ? 196 THR B CG2 1 
ATOM   4431 N  N   . ASP B 1 197 ? -18.184 8.294   -9.300  1.00 44.91  ? 197 ASP B N   1 
ATOM   4432 C  CA  . ASP B 1 197 ? -16.735 8.592   -9.253  1.00 39.07  ? 197 ASP B CA  1 
ATOM   4433 C  C   . ASP B 1 197 ? -16.481 9.978   -9.826  1.00 38.24  ? 197 ASP B C   1 
ATOM   4434 O  O   . ASP B 1 197 ? -17.351 10.525  -10.503 1.00 41.73  ? 197 ASP B O   1 
ATOM   4435 C  CB  . ASP B 1 197 ? -15.951 7.534   -10.010 1.00 37.62  ? 197 ASP B CB  1 
ATOM   4436 C  CG  . ASP B 1 197 ? -14.505 7.443   -9.563  1.00 34.61  ? 197 ASP B CG  1 
ATOM   4437 O  OD1 . ASP B 1 197 ? -14.166 7.980   -8.470  1.00 34.07  ? 197 ASP B OD1 1 
ATOM   4438 O  OD2 . ASP B 1 197 ? -13.758 6.789   -10.281 1.00 33.37  ? 197 ASP B OD2 1 
ATOM   4439 N  N   . THR B 1 198 ? -15.324 10.539  -9.537  1.00 37.22  ? 198 THR B N   1 
ATOM   4440 C  CA  . THR B 1 198 ? -14.913 11.836  -10.106 1.00 39.99  ? 198 THR B CA  1 
ATOM   4441 C  C   . THR B 1 198 ? -13.531 11.658  -10.698 1.00 36.88  ? 198 THR B C   1 
ATOM   4442 O  O   . THR B 1 198 ? -12.895 10.639  -10.393 1.00 35.02  ? 198 THR B O   1 
ATOM   4443 C  CB  . THR B 1 198 ? -14.950 12.946  -9.059  1.00 44.52  ? 198 THR B CB  1 
ATOM   4444 O  OG1 . THR B 1 198 ? -14.369 12.410  -7.871  1.00 43.27  ? 198 THR B OG1 1 
ATOM   4445 C  CG2 . THR B 1 198 ? -16.358 13.442  -8.810  1.00 47.29  ? 198 THR B CG2 1 
ATOM   4446 N  N   . THR B 1 199 ? -13.107 12.626  -11.501 1.00 32.91  ? 199 THR B N   1 
ATOM   4447 C  CA  . THR B 1 199 ? -11.802 12.605  -12.199 1.00 31.25  ? 199 THR B CA  1 
ATOM   4448 C  C   . THR B 1 199 ? -10.759 13.295  -11.331 1.00 28.89  ? 199 THR B C   1 
ATOM   4449 O  O   . THR B 1 199 ? -11.071 14.372  -10.712 1.00 33.63  ? 199 THR B O   1 
ATOM   4450 C  CB  . THR B 1 199 ? -11.925 13.205  -13.602 1.00 31.83  ? 199 THR B CB  1 
ATOM   4451 O  OG1 . THR B 1 199 ? -12.886 12.375  -14.245 1.00 34.15  ? 199 THR B OG1 1 
ATOM   4452 C  CG2 . THR B 1 199 ? -10.619 13.168  -14.356 1.00 32.06  ? 199 THR B CG2 1 
ATOM   4453 N  N   . ILE B 1 200 ? -9.557  12.722  -11.296 1.00 26.70  ? 200 ILE B N   1 
ATOM   4454 C  CA  . ILE B 1 200 ? -8.457  13.222  -10.423 1.00 26.35  ? 200 ILE B CA  1 
ATOM   4455 C  C   . ILE B 1 200 ? -7.710  14.332  -11.171 1.00 26.77  ? 200 ILE B C   1 
ATOM   4456 O  O   . ILE B 1 200 ? -6.722  14.069  -11.881 1.00 26.25  ? 200 ILE B O   1 
ATOM   4457 C  CB  . ILE B 1 200 ? -7.534  12.100  -9.908  1.00 26.56  ? 200 ILE B CB  1 
ATOM   4458 C  CG1 . ILE B 1 200 ? -8.317  10.869  -9.437  1.00 26.00  ? 200 ILE B CG1 1 
ATOM   4459 C  CG2 . ILE B 1 200 ? -6.643  12.653  -8.811  1.00 25.71  ? 200 ILE B CG2 1 
ATOM   4460 C  CD1 . ILE B 1 200 ? -7.542  9.566   -9.555  1.00 26.55  ? 200 ILE B CD1 1 
ATOM   4461 N  N   . THR B 1 201 ? -8.122  15.575  -10.907 1.00 31.04  ? 201 THR B N   1 
ATOM   4462 C  CA  . THR B 1 201 ? -7.668  16.795  -11.610 1.00 28.42  ? 201 THR B CA  1 
ATOM   4463 C  C   . THR B 1 201 ? -6.144  16.870  -11.596 1.00 30.67  ? 201 THR B C   1 
ATOM   4464 O  O   . THR B 1 201 ? -5.545  17.054  -12.682 1.00 30.77  ? 201 THR B O   1 
ATOM   4465 C  CB  . THR B 1 201 ? -8.340  18.019  -10.992 1.00 28.98  ? 201 THR B CB  1 
ATOM   4466 O  OG1 . THR B 1 201 ? -9.733  17.746  -11.068 1.00 28.46  ? 201 THR B OG1 1 
ATOM   4467 C  CG2 . THR B 1 201 ? -8.004  19.301  -11.713 1.00 30.55  ? 201 THR B CG2 1 
ATOM   4468 N  N   . VAL B 1 202 ? -5.517  16.753  -10.428 1.00 27.88  ? 202 VAL B N   1 
ATOM   4469 C  CA  . VAL B 1 202 ? -4.049  16.977  -10.330 1.00 29.17  ? 202 VAL B CA  1 
ATOM   4470 C  C   . VAL B 1 202 ? -3.290  15.930  -11.174 1.00 27.17  ? 202 VAL B C   1 
ATOM   4471 O  O   . VAL B 1 202 ? -2.237  16.272  -11.729 1.00 26.17  ? 202 VAL B O   1 
ATOM   4472 C  CB  . VAL B 1 202 ? -3.586  17.026  -8.866  1.00 30.28  ? 202 VAL B CB  1 
ATOM   4473 C  CG1 . VAL B 1 202 ? -3.729  15.682  -8.160  1.00 33.29  ? 202 VAL B CG1 1 
ATOM   4474 C  CG2 . VAL B 1 202 ? -2.162  17.550  -8.786  1.00 31.21  ? 202 VAL B CG2 1 
ATOM   4475 N  N   . ASN B 1 203 ? -3.823  14.712  -11.288 1.00 27.16  ? 203 ASN B N   1 
ATOM   4476 C  CA  . ASN B 1 203 ? -3.224  13.607  -12.079 1.00 26.24  ? 203 ASN B CA  1 
ATOM   4477 C  C   . ASN B 1 203 ? -3.358  13.885  -13.580 1.00 24.87  ? 203 ASN B C   1 
ATOM   4478 O  O   . ASN B 1 203 ? -2.410  13.638  -14.322 1.00 24.63  ? 203 ASN B O   1 
ATOM   4479 C  CB  . ASN B 1 203 ? -3.839  12.253  -11.710 1.00 25.74  ? 203 ASN B CB  1 
ATOM   4480 C  CG  . ASN B 1 203 ? -3.441  11.780  -10.326 1.00 26.40  ? 203 ASN B CG  1 
ATOM   4481 O  OD1 . ASN B 1 203 ? -2.718  12.473  -9.609  1.00 26.73  ? 203 ASN B OD1 1 
ATOM   4482 N  ND2 . ASN B 1 203 ? -3.902  10.596  -9.952  1.00 25.17  ? 203 ASN B ND2 1 
ATOM   4483 N  N   . VAL B 1 204 ? -4.510  14.365  -14.022 1.00 27.26  ? 204 VAL B N   1 
ATOM   4484 C  CA  . VAL B 1 204 ? -4.718  14.750  -15.443 1.00 27.50  ? 204 VAL B CA  1 
ATOM   4485 C  C   . VAL B 1 204 ? -3.661  15.800  -15.800 1.00 27.43  ? 204 VAL B C   1 
ATOM   4486 O  O   . VAL B 1 204 ? -3.028  15.683  -16.861 1.00 26.78  ? 204 VAL B O   1 
ATOM   4487 C  CB  . VAL B 1 204 ? -6.146  15.262  -15.720 1.00 27.52  ? 204 VAL B CB  1 
ATOM   4488 C  CG1 . VAL B 1 204 ? -6.286  15.754  -17.165 1.00 27.09  ? 204 VAL B CG1 1 
ATOM   4489 C  CG2 . VAL B 1 204 ? -7.178  14.199  -15.453 1.00 27.15  ? 204 VAL B CG2 1 
ATOM   4490 N  N   . LEU B 1 205 ? -3.472  16.798  -14.943 1.00 28.48  ? 205 LEU B N   1 
ATOM   4491 C  CA  . LEU B 1 205 ? -2.480  17.866  -15.201 1.00 31.69  ? 205 LEU B CA  1 
ATOM   4492 C  C   . LEU B 1 205 ? -1.076  17.263  -15.221 1.00 30.35  ? 205 LEU B C   1 
ATOM   4493 O  O   . LEU B 1 205 ? -0.309  17.668  -16.089 1.00 30.08  ? 205 LEU B O   1 
ATOM   4494 C  CB  . LEU B 1 205 ? -2.626  18.971  -14.149 1.00 35.33  ? 205 LEU B CB  1 
ATOM   4495 C  CG  . LEU B 1 205 ? -3.920  19.773  -14.296 1.00 37.65  ? 205 LEU B CG  1 
ATOM   4496 C  CD1 . LEU B 1 205 ? -4.192  20.624  -13.063 1.00 42.97  ? 205 LEU B CD1 1 
ATOM   4497 C  CD2 . LEU B 1 205 ? -3.872  20.637  -15.538 1.00 37.67  ? 205 LEU B CD2 1 
ATOM   4498 N  N   . ALA B 1 206 ? -0.766  16.306  -14.342 1.00 27.60  ? 206 ALA B N   1 
ATOM   4499 C  CA  . ALA B 1 206 ? 0.551   15.636  -14.333 1.00 28.43  ? 206 ALA B CA  1 
ATOM   4500 C  C   . ALA B 1 206 ? 0.773   14.976  -15.696 1.00 29.11  ? 206 ALA B C   1 
ATOM   4501 O  O   . ALA B 1 206 ? 1.896   15.093  -16.245 1.00 26.69  ? 206 ALA B O   1 
ATOM   4502 C  CB  . ALA B 1 206 ? 0.644   14.632  -13.217 1.00 28.67  ? 206 ALA B CB  1 
ATOM   4503 N  N   . TRP B 1 207 ? -0.267  14.343  -16.236 1.00 26.82  ? 207 TRP B N   1 
ATOM   4504 C  CA  . TRP B 1 207 ? -0.176  13.558  -17.499 1.00 30.16  ? 207 TRP B CA  1 
ATOM   4505 C  C   . TRP B 1 207 ? -0.029  14.500  -18.705 1.00 31.69  ? 207 TRP B C   1 
ATOM   4506 O  O   . TRP B 1 207 ? 0.710   14.134  -19.651 1.00 29.70  ? 207 TRP B O   1 
ATOM   4507 C  CB  . TRP B 1 207 ? -1.369  12.605  -17.613 1.00 28.37  ? 207 TRP B CB  1 
ATOM   4508 C  CG  . TRP B 1 207 ? -1.605  11.911  -18.924 1.00 28.40  ? 207 TRP B CG  1 
ATOM   4509 C  CD1 . TRP B 1 207 ? -1.045  10.749  -19.389 1.00 28.07  ? 207 TRP B CD1 1 
ATOM   4510 C  CD2 . TRP B 1 207 ? -2.639  12.246  -19.856 1.00 28.29  ? 207 TRP B CD2 1 
ATOM   4511 N  NE1 . TRP B 1 207 ? -1.604  10.394  -20.593 1.00 29.89  ? 207 TRP B NE1 1 
ATOM   4512 C  CE2 . TRP B 1 207 ? -2.586  11.295  -20.901 1.00 27.54  ? 207 TRP B CE2 1 
ATOM   4513 C  CE3 . TRP B 1 207 ? -3.562  13.291  -19.929 1.00 29.30  ? 207 TRP B CE3 1 
ATOM   4514 C  CZ2 . TRP B 1 207 ? -3.434  11.357  -21.998 1.00 29.68  ? 207 TRP B CZ2 1 
ATOM   4515 C  CZ3 . TRP B 1 207 ? -4.395  13.358  -21.025 1.00 31.28  ? 207 TRP B CZ3 1 
ATOM   4516 C  CH2 . TRP B 1 207 ? -4.335  12.399  -22.044 1.00 31.08  ? 207 TRP B CH2 1 
ATOM   4517 N  N   . LEU B 1 208 ? -0.688  15.658  -18.683 1.00 32.73  ? 208 LEU B N   1 
ATOM   4518 C  CA  . LEU B 1 208 ? -0.441  16.745  -19.671 1.00 33.95  ? 208 LEU B CA  1 
ATOM   4519 C  C   . LEU B 1 208 ? 1.032   17.169  -19.623 1.00 29.60  ? 208 LEU B C   1 
ATOM   4520 O  O   . LEU B 1 208 ? 1.610   17.375  -20.681 1.00 28.93  ? 208 LEU B O   1 
ATOM   4521 C  CB  . LEU B 1 208 ? -1.375  17.930  -19.397 1.00 34.26  ? 208 LEU B CB  1 
ATOM   4522 C  CG  . LEU B 1 208 ? -2.847  17.649  -19.676 1.00 34.43  ? 208 LEU B CG  1 
ATOM   4523 C  CD1 . LEU B 1 208 ? -3.673  18.922  -19.568 1.00 38.29  ? 208 LEU B CD1 1 
ATOM   4524 C  CD2 . LEU B 1 208 ? -3.024  17.037  -21.051 1.00 32.83  ? 208 LEU B CD2 1 
ATOM   4525 N  N   . TYR B 1 209 ? 1.641   17.259  -18.449 1.00 30.95  ? 209 TYR B N   1 
ATOM   4526 C  CA  . TYR B 1 209 ? 3.078   17.599  -18.337 1.00 33.69  ? 209 TYR B CA  1 
ATOM   4527 C  C   . TYR B 1 209 ? 3.916   16.476  -18.977 1.00 36.86  ? 209 TYR B C   1 
ATOM   4528 O  O   . TYR B 1 209 ? 4.891   16.814  -19.692 1.00 34.42  ? 209 TYR B O   1 
ATOM   4529 C  CB  . TYR B 1 209 ? 3.482   17.879  -16.893 1.00 36.29  ? 209 TYR B CB  1 
ATOM   4530 C  CG  . TYR B 1 209 ? 3.165   19.273  -16.416 1.00 40.64  ? 209 TYR B CG  1 
ATOM   4531 C  CD1 . TYR B 1 209 ? 3.841   20.384  -16.900 1.00 42.52  ? 209 TYR B CD1 1 
ATOM   4532 C  CD2 . TYR B 1 209 ? 2.189   19.475  -15.458 1.00 40.28  ? 209 TYR B CD2 1 
ATOM   4533 C  CE1 . TYR B 1 209 ? 3.532   21.664  -16.457 1.00 42.59  ? 209 TYR B CE1 1 
ATOM   4534 C  CE2 . TYR B 1 209 ? 1.880   20.739  -14.994 1.00 41.83  ? 209 TYR B CE2 1 
ATOM   4535 C  CZ  . TYR B 1 209 ? 2.552   21.845  -15.493 1.00 45.72  ? 209 TYR B CZ  1 
ATOM   4536 O  OH  . TYR B 1 209 ? 2.220   23.087  -15.011 1.00 40.95  ? 209 TYR B OH  1 
ATOM   4537 N  N   . ALA B 1 210 ? 3.560   15.201  -18.743 1.00 34.32  ? 210 ALA B N   1 
ATOM   4538 C  CA  . ALA B 1 210 ? 4.242   14.039  -19.351 1.00 31.20  ? 210 ALA B CA  1 
ATOM   4539 C  C   . ALA B 1 210 ? 4.128   14.144  -20.871 1.00 32.19  ? 210 ALA B C   1 
ATOM   4540 O  O   . ALA B 1 210 ? 5.115   13.822  -21.561 1.00 31.51  ? 210 ALA B O   1 
ATOM   4541 C  CB  . ALA B 1 210 ? 3.673   12.741  -18.854 1.00 30.85  ? 210 ALA B CB  1 
ATOM   4542 N  N   . ALA B 1 211 ? 2.967   14.556  -21.375 1.00 28.41  ? 211 ALA B N   1 
ATOM   4543 C  CA  . ALA B 1 211 ? 2.739   14.674  -22.822 1.00 32.62  ? 211 ALA B CA  1 
ATOM   4544 C  C   . ALA B 1 211 ? 3.706   15.735  -23.364 1.00 34.45  ? 211 ALA B C   1 
ATOM   4545 O  O   . ALA B 1 211 ? 4.399   15.461  -24.354 1.00 32.91  ? 211 ALA B O   1 
ATOM   4546 C  CB  . ALA B 1 211 ? 1.305   14.998  -23.113 1.00 30.70  ? 211 ALA B CB  1 
ATOM   4547 N  N   . VAL B 1 212 ? 3.789   16.890  -22.709 1.00 32.34  ? 212 VAL B N   1 
ATOM   4548 C  CA  . VAL B 1 212 ? 4.631   17.998  -23.214 1.00 32.95  ? 212 VAL B CA  1 
ATOM   4549 C  C   . VAL B 1 212 ? 6.069   17.499  -23.215 1.00 31.96  ? 212 VAL B C   1 
ATOM   4550 O  O   . VAL B 1 212 ? 6.715   17.671  -24.205 1.00 36.30  ? 212 VAL B O   1 
ATOM   4551 C  CB  . VAL B 1 212 ? 4.483   19.291  -22.397 1.00 32.92  ? 212 VAL B CB  1 
ATOM   4552 C  CG1 . VAL B 1 212 ? 5.490   20.323  -22.881 1.00 34.56  ? 212 VAL B CG1 1 
ATOM   4553 C  CG2 . VAL B 1 212 ? 3.069   19.844  -22.475 1.00 32.96  ? 212 VAL B CG2 1 
ATOM   4554 N  N   . ILE B 1 213 ? 6.532   16.897  -22.124 1.00 36.01  ? 213 ILE B N   1 
ATOM   4555 C  CA  . ILE B 1 213 ? 7.912   16.338  -22.000 1.00 36.45  ? 213 ILE B CA  1 
ATOM   4556 C  C   . ILE B 1 213 ? 8.189   15.374  -23.162 1.00 36.07  ? 213 ILE B C   1 
ATOM   4557 O  O   . ILE B 1 213 ? 9.346   15.277  -23.578 1.00 33.56  ? 213 ILE B O   1 
ATOM   4558 C  CB  . ILE B 1 213 ? 8.090   15.664  -20.622 1.00 42.47  ? 213 ILE B CB  1 
ATOM   4559 C  CG1 . ILE B 1 213 ? 8.154   16.711  -19.504 1.00 41.12  ? 213 ILE B CG1 1 
ATOM   4560 C  CG2 . ILE B 1 213 ? 9.293   14.718  -20.605 1.00 40.81  ? 213 ILE B CG2 1 
ATOM   4561 C  CD1 . ILE B 1 213 ? 7.938   16.147  -18.122 1.00 42.47  ? 213 ILE B CD1 1 
ATOM   4562 N  N   . ASN B 1 214 ? 7.172   14.688  -23.673 1.00 36.40  ? 214 ASN B N   1 
ATOM   4563 C  CA  . ASN B 1 214 ? 7.317   13.728  -24.801 1.00 37.13  ? 214 ASN B CA  1 
ATOM   4564 C  C   . ASN B 1 214 ? 6.942   14.385  -26.133 1.00 36.74  ? 214 ASN B C   1 
ATOM   4565 O  O   . ASN B 1 214 ? 6.795   13.655  -27.096 1.00 40.12  ? 214 ASN B O   1 
ATOM   4566 C  CB  . ASN B 1 214 ? 6.531   12.453  -24.516 1.00 36.07  ? 214 ASN B CB  1 
ATOM   4567 C  CG  . ASN B 1 214 ? 7.218   11.663  -23.428 1.00 39.03  ? 214 ASN B CG  1 
ATOM   4568 O  OD1 . ASN B 1 214 ? 8.136   10.903  -23.710 1.00 44.71  ? 214 ASN B OD1 1 
ATOM   4569 N  ND2 . ASN B 1 214 ? 6.877   11.927  -22.178 1.00 43.10  ? 214 ASN B ND2 1 
ATOM   4570 N  N   . GLY B 1 215 ? 6.826   15.712  -26.200 1.00 36.33  ? 215 GLY B N   1 
ATOM   4571 C  CA  . GLY B 1 215 ? 6.640   16.439  -27.474 1.00 38.22  ? 215 GLY B CA  1 
ATOM   4572 C  C   . GLY B 1 215 ? 5.224   16.388  -28.028 1.00 38.94  ? 215 GLY B C   1 
ATOM   4573 O  O   . GLY B 1 215 ? 5.042   16.756  -29.190 1.00 35.30  ? 215 GLY B O   1 
ATOM   4574 N  N   . ASP B 1 216 ? 4.234   15.966  -27.247 1.00 40.24  ? 216 ASP B N   1 
ATOM   4575 C  CA  . ASP B 1 216 ? 2.802   16.185  -27.582 1.00 44.98  ? 216 ASP B CA  1 
ATOM   4576 C  C   . ASP B 1 216 ? 2.383   17.538  -26.998 1.00 47.98  ? 216 ASP B C   1 
ATOM   4577 O  O   . ASP B 1 216 ? 2.302   17.631  -25.769 1.00 53.07  ? 216 ASP B O   1 
ATOM   4578 C  CB  . ASP B 1 216 ? 1.934   15.050  -27.030 1.00 51.60  ? 216 ASP B CB  1 
ATOM   4579 C  CG  . ASP B 1 216 ? 1.249   14.219  -28.093 1.00 49.55  ? 216 ASP B CG  1 
ATOM   4580 O  OD1 . ASP B 1 216 ? 1.173   14.701  -29.232 1.00 53.46  ? 216 ASP B OD1 1 
ATOM   4581 O  OD2 . ASP B 1 216 ? 0.763   13.117  -27.756 1.00 48.56  ? 216 ASP B OD2 1 
ATOM   4582 N  N   . ARG B 1 217 ? 2.144   18.547  -27.835 1.00 49.17  ? 217 ARG B N   1 
ATOM   4583 C  CA  . ARG B 1 217 ? 2.073   19.962  -27.380 1.00 48.91  ? 217 ARG B CA  1 
ATOM   4584 C  C   . ARG B 1 217 ? 0.896   20.727  -27.986 1.00 42.44  ? 217 ARG B C   1 
ATOM   4585 O  O   . ARG B 1 217 ? 0.750   21.919  -27.642 1.00 49.58  ? 217 ARG B O   1 
ATOM   4586 C  CB  . ARG B 1 217 ? 3.370   20.673  -27.773 1.00 54.15  ? 217 ARG B CB  1 
ATOM   4587 C  CG  . ARG B 1 217 ? 4.602   20.119  -27.075 1.00 59.40  ? 217 ARG B CG  1 
ATOM   4588 C  CD  . ARG B 1 217 ? 5.849   20.878  -27.480 1.00 59.93  ? 217 ARG B CD  1 
ATOM   4589 N  NE  . ARG B 1 217 ? 5.728   22.289  -27.140 1.00 55.62  ? 217 ARG B NE  1 
ATOM   4590 C  CZ  . ARG B 1 217 ? 6.304   22.887  -26.101 1.00 49.45  ? 217 ARG B CZ  1 
ATOM   4591 N  NH1 . ARG B 1 217 ? 7.084   22.229  -25.256 1.00 48.52  ? 217 ARG B NH1 1 
ATOM   4592 N  NH2 . ARG B 1 217 ? 6.098   24.174  -25.919 1.00 51.30  ? 217 ARG B NH2 1 
ATOM   4593 N  N   . TRP B 1 218 ? 0.086   20.090  -28.826 1.00 37.93  ? 218 TRP B N   1 
ATOM   4594 C  CA  . TRP B 1 218 ? -0.989  20.748  -29.613 1.00 39.56  ? 218 TRP B CA  1 
ATOM   4595 C  C   . TRP B 1 218 ? -1.999  21.457  -28.704 1.00 38.80  ? 218 TRP B C   1 
ATOM   4596 O  O   . TRP B 1 218 ? -2.607  22.429  -29.174 1.00 38.02  ? 218 TRP B O   1 
ATOM   4597 C  CB  . TRP B 1 218 ? -1.704  19.754  -30.534 1.00 38.83  ? 218 TRP B CB  1 
ATOM   4598 C  CG  . TRP B 1 218 ? -2.449  18.644  -29.853 1.00 39.92  ? 218 TRP B CG  1 
ATOM   4599 C  CD1 . TRP B 1 218 ? -2.036  17.347  -29.746 1.00 41.38  ? 218 TRP B CD1 1 
ATOM   4600 C  CD2 . TRP B 1 218 ? -3.763  18.693  -29.258 1.00 42.47  ? 218 TRP B CD2 1 
ATOM   4601 N  NE1 . TRP B 1 218 ? -2.983  16.589  -29.103 1.00 42.87  ? 218 TRP B NE1 1 
ATOM   4602 C  CE2 . TRP B 1 218 ? -4.056  17.383  -28.797 1.00 42.67  ? 218 TRP B CE2 1 
ATOM   4603 C  CE3 . TRP B 1 218 ? -4.723  19.702  -29.063 1.00 44.64  ? 218 TRP B CE3 1 
ATOM   4604 C  CZ2 . TRP B 1 218 ? -5.255  17.069  -28.152 1.00 44.19  ? 218 TRP B CZ2 1 
ATOM   4605 C  CZ3 . TRP B 1 218 ? -5.907  19.391  -28.424 1.00 40.08  ? 218 TRP B CZ3 1 
ATOM   4606 C  CH2 . TRP B 1 218 ? -6.168  18.091  -27.979 1.00 44.86  ? 218 TRP B CH2 1 
ATOM   4607 N  N   . PHE B 1 219 ? -2.239  20.942  -27.496 1.00 39.49  ? 219 PHE B N   1 
ATOM   4608 C  CA  . PHE B 1 219 ? -3.311  21.413  -26.572 1.00 36.04  ? 219 PHE B CA  1 
ATOM   4609 C  C   . PHE B 1 219 ? -2.817  22.650  -25.818 1.00 35.06  ? 219 PHE B C   1 
ATOM   4610 O  O   . PHE B 1 219 ? -3.612  23.261  -25.087 1.00 38.31  ? 219 PHE B O   1 
ATOM   4611 C  CB  . PHE B 1 219 ? -3.731  20.301  -25.602 1.00 34.60  ? 219 PHE B CB  1 
ATOM   4612 C  CG  . PHE B 1 219 ? -2.566  19.649  -24.905 1.00 34.68  ? 219 PHE B CG  1 
ATOM   4613 C  CD1 . PHE B 1 219 ? -1.968  20.259  -23.818 1.00 32.89  ? 219 PHE B CD1 1 
ATOM   4614 C  CD2 . PHE B 1 219 ? -2.030  18.455  -25.381 1.00 34.62  ? 219 PHE B CD2 1 
ATOM   4615 C  CE1 . PHE B 1 219 ? -0.867  19.682  -23.207 1.00 35.95  ? 219 PHE B CE1 1 
ATOM   4616 C  CE2 . PHE B 1 219 ? -0.934  17.876  -24.768 1.00 30.80  ? 219 PHE B CE2 1 
ATOM   4617 C  CZ  . PHE B 1 219 ? -0.350  18.498  -23.689 1.00 36.31  ? 219 PHE B CZ  1 
ATOM   4618 N  N   . LEU B 1 220 ? -1.526  22.968  -25.891 1.00 35.58  ? 220 LEU B N   1 
ATOM   4619 C  CA  . LEU B 1 220 ? -1.017  24.193  -25.235 1.00 38.62  ? 220 LEU B CA  1 
ATOM   4620 C  C   . LEU B 1 220 ? -1.693  25.405  -25.888 1.00 39.27  ? 220 LEU B C   1 
ATOM   4621 O  O   . LEU B 1 220 ? -2.208  25.272  -27.008 1.00 31.43  ? 220 LEU B O   1 
ATOM   4622 C  CB  . LEU B 1 220 ? 0.503   24.262  -25.332 1.00 39.44  ? 220 LEU B CB  1 
ATOM   4623 C  CG  . LEU B 1 220 ? 1.247   23.186  -24.544 1.00 41.32  ? 220 LEU B CG  1 
ATOM   4624 C  CD1 . LEU B 1 220 ? 2.741   23.404  -24.637 1.00 39.69  ? 220 LEU B CD1 1 
ATOM   4625 C  CD2 . LEU B 1 220 ? 0.804   23.134  -23.083 1.00 41.86  ? 220 LEU B CD2 1 
ATOM   4626 N  N   . ASN B 1 221 ? -1.770  26.524  -25.164 1.00 44.11  ? 221 ASN B N   1 
ATOM   4627 C  CA  . ASN B 1 221 ? -2.454  27.752  -25.657 1.00 39.24  ? 221 ASN B CA  1 
ATOM   4628 C  C   . ASN B 1 221 ? -1.915  28.953  -24.890 1.00 37.64  ? 221 ASN B C   1 
ATOM   4629 O  O   . ASN B 1 221 ? -1.201  28.741  -23.903 1.00 32.96  ? 221 ASN B O   1 
ATOM   4630 C  CB  . ASN B 1 221 ? -3.970  27.638  -25.550 1.00 37.47  ? 221 ASN B CB  1 
ATOM   4631 C  CG  . ASN B 1 221 ? -4.485  27.629  -24.123 1.00 38.42  ? 221 ASN B CG  1 
ATOM   4632 O  OD1 . ASN B 1 221 ? -3.802  28.046  -23.184 1.00 38.64  ? 221 ASN B OD1 1 
ATOM   4633 N  ND2 . ASN B 1 221 ? -5.719  27.181  -23.964 1.00 35.73  ? 221 ASN B ND2 1 
ATOM   4634 N  N   . ARG B 1 222 ? -2.248  30.159  -25.356 1.00 35.24  ? 222 ARG B N   1 
ATOM   4635 C  CA  . ARG B 1 222 ? -1.700  31.430  -24.830 1.00 32.46  ? 222 ARG B CA  1 
ATOM   4636 C  C   . ARG B 1 222 ? -2.344  31.764  -23.487 1.00 29.73  ? 222 ARG B C   1 
ATOM   4637 O  O   . ARG B 1 222 ? -1.868  32.678  -22.845 1.00 31.16  ? 222 ARG B O   1 
ATOM   4638 C  CB  . ARG B 1 222 ? -1.955  32.604  -25.784 1.00 33.93  ? 222 ARG B CB  1 
ATOM   4639 C  CG  . ARG B 1 222 ? -3.423  32.980  -25.983 1.00 36.16  ? 222 ARG B CG  1 
ATOM   4640 C  CD  . ARG B 1 222 ? -3.637  34.357  -26.629 1.00 37.56  ? 222 ARG B CD  1 
ATOM   4641 N  NE  . ARG B 1 222 ? -2.846  34.509  -27.841 1.00 38.07  ? 222 ARG B NE  1 
ATOM   4642 C  CZ  . ARG B 1 222 ? -1.948  35.459  -28.094 1.00 38.16  ? 222 ARG B CZ  1 
ATOM   4643 N  NH1 . ARG B 1 222 ? -1.719  36.452  -27.247 1.00 40.84  ? 222 ARG B NH1 1 
ATOM   4644 N  NH2 . ARG B 1 222 ? -1.304  35.433  -29.243 1.00 39.30  ? 222 ARG B NH2 1 
ATOM   4645 N  N   . PHE B 1 223 ? -3.421  31.105  -23.100 1.00 31.98  ? 223 PHE B N   1 
ATOM   4646 C  CA  . PHE B 1 223 ? -4.267  31.590  -21.981 1.00 35.43  ? 223 PHE B CA  1 
ATOM   4647 C  C   . PHE B 1 223 ? -3.715  31.120  -20.629 1.00 39.32  ? 223 PHE B C   1 
ATOM   4648 O  O   . PHE B 1 223 ? -2.873  30.174  -20.548 1.00 40.40  ? 223 PHE B O   1 
ATOM   4649 C  CB  . PHE B 1 223 ? -5.718  31.180  -22.201 1.00 34.97  ? 223 PHE B CB  1 
ATOM   4650 C  CG  . PHE B 1 223 ? -6.267  31.629  -23.524 1.00 35.65  ? 223 PHE B CG  1 
ATOM   4651 C  CD1 . PHE B 1 223 ? -6.527  32.971  -23.770 1.00 37.59  ? 223 PHE B CD1 1 
ATOM   4652 C  CD2 . PHE B 1 223 ? -6.496  30.711  -24.539 1.00 38.03  ? 223 PHE B CD2 1 
ATOM   4653 C  CE1 . PHE B 1 223 ? -7.021  33.382  -25.002 1.00 38.67  ? 223 PHE B CE1 1 
ATOM   4654 C  CE2 . PHE B 1 223 ? -7.002  31.121  -25.759 1.00 35.58  ? 223 PHE B CE2 1 
ATOM   4655 C  CZ  . PHE B 1 223 ? -7.249  32.456  -25.994 1.00 39.25  ? 223 PHE B CZ  1 
ATOM   4656 N  N   . THR B 1 224 ? -4.135  31.829  -19.577 1.00 42.54  ? 224 THR B N   1 
ATOM   4657 C  CA  . THR B 1 224 ? -3.985  31.384  -18.170 1.00 40.68  ? 224 THR B CA  1 
ATOM   4658 C  C   . THR B 1 224 ? -5.331  31.497  -17.435 1.00 39.59  ? 224 THR B C   1 
ATOM   4659 O  O   . THR B 1 224 ? -6.370  31.775  -18.059 1.00 39.42  ? 224 THR B O   1 
ATOM   4660 C  CB  . THR B 1 224 ? -2.798  32.081  -17.501 1.00 42.01  ? 224 THR B CB  1 
ATOM   4661 O  OG1 . THR B 1 224 ? -2.709  31.329  -16.293 1.00 46.26  ? 224 THR B OG1 1 
ATOM   4662 C  CG2 . THR B 1 224 ? -2.992  33.565  -17.262 1.00 40.64  ? 224 THR B CG2 1 
ATOM   4663 N  N   . THR B 1 225 ? -5.356  31.164  -16.157 1.00 38.97  ? 225 THR B N   1 
ATOM   4664 C  CA  . THR B 1 225 ? -6.625  31.148  -15.397 1.00 45.30  ? 225 THR B CA  1 
ATOM   4665 C  C   . THR B 1 225 ? -6.308  31.305  -13.910 1.00 44.66  ? 225 THR B C   1 
ATOM   4666 O  O   . THR B 1 225 ? -5.154  31.587  -13.577 1.00 46.16  ? 225 THR B O   1 
ATOM   4667 C  CB  . THR B 1 225 ? -7.442  29.889  -15.727 1.00 46.37  ? 225 THR B CB  1 
ATOM   4668 O  OG1 . THR B 1 225 ? -8.662  29.908  -14.982 1.00 48.66  ? 225 THR B OG1 1 
ATOM   4669 C  CG2 . THR B 1 225 ? -6.697  28.610  -15.418 1.00 51.37  ? 225 THR B CG2 1 
ATOM   4670 N  N   . THR B 1 226 ? -7.316  31.132  -13.061 1.00 50.69  ? 226 THR B N   1 
ATOM   4671 C  CA  . THR B 1 226 ? -7.166  31.084  -11.585 1.00 48.53  ? 226 THR B CA  1 
ATOM   4672 C  C   . THR B 1 226 ? -7.851  29.819  -11.062 1.00 44.07  ? 226 THR B C   1 
ATOM   4673 O  O   . THR B 1 226 ? -8.810  29.324  -11.735 1.00 43.97  ? 226 THR B O   1 
ATOM   4674 C  CB  . THR B 1 226 ? -7.748  32.352  -10.953 1.00 46.25  ? 226 THR B CB  1 
ATOM   4675 O  OG1 . THR B 1 226 ? -9.170  32.225  -11.008 1.00 40.77  ? 226 THR B OG1 1 
ATOM   4676 C  CG2 . THR B 1 226 ? -7.284  33.606  -11.668 1.00 48.32  ? 226 THR B CG2 1 
ATOM   4677 N  N   . LEU B 1 227 ? -7.405  29.360  -9.892  1.00 45.80  ? 227 LEU B N   1 
ATOM   4678 C  CA  . LEU B 1 227 ? -8.050  28.270  -9.115  1.00 50.41  ? 227 LEU B CA  1 
ATOM   4679 C  C   . LEU B 1 227 ? -9.571  28.464  -9.107  1.00 52.29  ? 227 LEU B C   1 
ATOM   4680 O  O   . LEU B 1 227 ? -10.284 27.571  -9.625  1.00 54.93  ? 227 LEU B O   1 
ATOM   4681 C  CB  . LEU B 1 227 ? -7.443  28.247  -7.707  1.00 53.30  ? 227 LEU B CB  1 
ATOM   4682 C  CG  . LEU B 1 227 ? -6.619  27.005  -7.345  1.00 58.00  ? 227 LEU B CG  1 
ATOM   4683 C  CD1 . LEU B 1 227 ? -5.819  26.471  -8.526  1.00 58.10  ? 227 LEU B CD1 1 
ATOM   4684 C  CD2 . LEU B 1 227 ? -5.680  27.294  -6.184  1.00 56.86  ? 227 LEU B CD2 1 
ATOM   4685 N  N   . ASN B 1 228 ? -10.052 29.600  -8.595  1.00 57.44  ? 228 ASN B N   1 
ATOM   4686 C  CA  . ASN B 1 228 ? -11.503 29.907  -8.484  1.00 58.62  ? 228 ASN B CA  1 
ATOM   4687 C  C   . ASN B 1 228 ? -12.214 29.648  -9.816  1.00 54.19  ? 228 ASN B C   1 
ATOM   4688 O  O   . ASN B 1 228 ? -13.207 28.887  -9.826  1.00 60.40  ? 228 ASN B O   1 
ATOM   4689 C  CB  . ASN B 1 228 ? -11.746 31.349  -8.035  1.00 66.67  ? 228 ASN B CB  1 
ATOM   4690 C  CG  . ASN B 1 228 ? -11.667 31.508  -6.534  1.00 72.19  ? 228 ASN B CG  1 
ATOM   4691 O  OD1 . ASN B 1 228 ? -12.645 31.900  -5.900  1.00 81.31  ? 228 ASN B OD1 1 
ATOM   4692 N  ND2 . ASN B 1 228 ? -10.520 31.185  -5.962  1.00 68.07  ? 228 ASN B ND2 1 
ATOM   4693 N  N   . ASP B 1 229 ? -11.757 30.288  -10.894 1.00 54.87  ? 229 ASP B N   1 
ATOM   4694 C  CA  . ASP B 1 229 ? -12.389 30.164  -12.236 1.00 57.07  ? 229 ASP B CA  1 
ATOM   4695 C  C   . ASP B 1 229 ? -12.281 28.698  -12.672 1.00 49.02  ? 229 ASP B C   1 
ATOM   4696 O  O   . ASP B 1 229 ? -13.304 28.107  -13.056 1.00 48.48  ? 229 ASP B O   1 
ATOM   4697 C  CB  . ASP B 1 229 ? -11.740 31.112  -13.252 1.00 61.35  ? 229 ASP B CB  1 
ATOM   4698 C  CG  . ASP B 1 229 ? -11.675 32.563  -12.805 1.00 65.70  ? 229 ASP B CG  1 
ATOM   4699 O  OD1 . ASP B 1 229 ? -12.731 33.107  -12.451 1.00 69.20  ? 229 ASP B OD1 1 
ATOM   4700 O  OD2 . ASP B 1 229 ? -10.562 33.125  -12.794 1.00 69.09  ? 229 ASP B OD2 1 
ATOM   4701 N  N   . PHE B 1 230 ? -11.076 28.126  -12.606 1.00 47.23  ? 230 PHE B N   1 
ATOM   4702 C  CA  . PHE B 1 230 ? -10.843 26.732  -13.064 1.00 45.37  ? 230 PHE B CA  1 
ATOM   4703 C  C   . PHE B 1 230 ? -11.753 25.806  -12.244 1.00 50.04  ? 230 PHE B C   1 
ATOM   4704 O  O   . PHE B 1 230 ? -12.443 24.954  -12.841 1.00 50.96  ? 230 PHE B O   1 
ATOM   4705 C  CB  . PHE B 1 230 ? -9.364  26.343  -12.984 1.00 48.10  ? 230 PHE B CB  1 
ATOM   4706 C  CG  . PHE B 1 230 ? -9.148  24.914  -13.410 1.00 48.96  ? 230 PHE B CG  1 
ATOM   4707 C  CD1 . PHE B 1 230 ? -9.255  24.553  -14.744 1.00 50.26  ? 230 PHE B CD1 1 
ATOM   4708 C  CD2 . PHE B 1 230 ? -8.965  23.914  -12.469 1.00 46.80  ? 230 PHE B CD2 1 
ATOM   4709 C  CE1 . PHE B 1 230 ? -9.132  23.229  -15.126 1.00 51.07  ? 230 PHE B CE1 1 
ATOM   4710 C  CE2 . PHE B 1 230 ? -8.849  22.590  -12.854 1.00 46.39  ? 230 PHE B CE2 1 
ATOM   4711 C  CZ  . PHE B 1 230 ? -8.918  22.253  -14.179 1.00 47.91  ? 230 PHE B CZ  1 
ATOM   4712 N  N   . ASN B 1 231 ? -11.821 26.010  -10.919 1.00 48.17  ? 231 ASN B N   1 
ATOM   4713 C  CA  . ASN B 1 231 ? -12.566 25.097  -10.003 1.00 48.75  ? 231 ASN B CA  1 
ATOM   4714 C  C   . ASN B 1 231 ? -14.071 25.145  -10.276 1.00 47.20  ? 231 ASN B C   1 
ATOM   4715 O  O   . ASN B 1 231 ? -14.720 24.106  -10.069 1.00 53.79  ? 231 ASN B O   1 
ATOM   4716 C  CB  . ASN B 1 231 ? -12.207 25.321  -8.532  1.00 47.50  ? 231 ASN B CB  1 
ATOM   4717 C  CG  . ASN B 1 231 ? -10.955 24.563  -8.151  1.00 46.03  ? 231 ASN B CG  1 
ATOM   4718 O  OD1 . ASN B 1 231 ? -10.795 23.407  -8.536  1.00 52.52  ? 231 ASN B OD1 1 
ATOM   4719 N  ND2 . ASN B 1 231 ? -10.051 25.196  -7.428  1.00 44.83  ? 231 ASN B ND2 1 
ATOM   4720 N  N   . LEU B 1 232 ? -14.615 26.255  -10.778 1.00 50.24  ? 232 LEU B N   1 
ATOM   4721 C  CA  . LEU B 1 232 ? -16.033 26.285  -11.235 1.00 54.18  ? 232 LEU B CA  1 
ATOM   4722 C  C   . LEU B 1 232 ? -16.204 25.378  -12.460 1.00 52.86  ? 232 LEU B C   1 
ATOM   4723 O  O   . LEU B 1 232 ? -17.235 24.692  -12.564 1.00 51.69  ? 232 LEU B O   1 
ATOM   4724 C  CB  . LEU B 1 232 ? -16.436 27.729  -11.532 1.00 61.24  ? 232 LEU B CB  1 
ATOM   4725 C  CG  . LEU B 1 232 ? -16.877 28.522  -10.303 1.00 65.60  ? 232 LEU B CG  1 
ATOM   4726 C  CD1 . LEU B 1 232 ? -16.796 30.024  -10.555 1.00 62.58  ? 232 LEU B CD1 1 
ATOM   4727 C  CD2 . LEU B 1 232 ? -18.282 28.103  -9.876  1.00 68.16  ? 232 LEU B CD2 1 
ATOM   4728 N  N   . VAL B 1 233 ? -15.214 25.362  -13.350 1.00 55.05  ? 233 VAL B N   1 
ATOM   4729 C  CA  . VAL B 1 233 ? -15.221 24.487  -14.558 1.00 55.10  ? 233 VAL B CA  1 
ATOM   4730 C  C   . VAL B 1 233 ? -15.064 23.035  -14.101 1.00 50.74  ? 233 VAL B C   1 
ATOM   4731 O  O   . VAL B 1 233 ? -15.830 22.183  -14.585 1.00 51.34  ? 233 VAL B O   1 
ATOM   4732 C  CB  . VAL B 1 233 ? -14.127 24.895  -15.565 1.00 55.07  ? 233 VAL B CB  1 
ATOM   4733 C  CG1 . VAL B 1 233 ? -14.174 24.048  -16.825 1.00 55.03  ? 233 VAL B CG1 1 
ATOM   4734 C  CG2 . VAL B 1 233 ? -14.220 26.374  -15.909 1.00 54.69  ? 233 VAL B CG2 1 
ATOM   4735 N  N   . ALA B 1 234 ? -14.115 22.766  -13.203 1.00 50.82  ? 234 ALA B N   1 
ATOM   4736 C  CA  . ALA B 1 234 ? -13.860 21.410  -12.653 1.00 54.31  ? 234 ALA B CA  1 
ATOM   4737 C  C   . ALA B 1 234 ? -15.170 20.820  -12.117 1.00 57.47  ? 234 ALA B C   1 
ATOM   4738 O  O   . ALA B 1 234 ? -15.609 19.756  -12.638 1.00 57.00  ? 234 ALA B O   1 
ATOM   4739 C  CB  . ALA B 1 234 ? -12.805 21.458  -11.573 1.00 55.40  ? 234 ALA B CB  1 
ATOM   4740 N  N   . MET B 1 235 ? -15.777 21.498  -11.132 1.00 57.25  ? 235 MET B N   1 
ATOM   4741 C  CA  . MET B 1 235 ? -17.041 21.070  -10.483 1.00 53.87  ? 235 MET B CA  1 
ATOM   4742 C  C   . MET B 1 235 ? -18.066 20.690  -11.559 1.00 50.72  ? 235 MET B C   1 
ATOM   4743 O  O   . MET B 1 235 ? -18.707 19.630  -11.409 1.00 48.27  ? 235 MET B O   1 
ATOM   4744 C  CB  . MET B 1 235 ? -17.621 22.169  -9.594  1.00 59.33  ? 235 MET B CB  1 
ATOM   4745 C  CG  . MET B 1 235 ? -18.967 21.785  -8.984  1.00 66.41  ? 235 MET B CG  1 
ATOM   4746 S  SD  . MET B 1 235 ? -19.558 22.947  -7.709  1.00 77.58  ? 235 MET B SD  1 
ATOM   4747 C  CE  . MET B 1 235 ? -18.703 22.365  -6.246  1.00 70.05  ? 235 MET B CE  1 
ATOM   4748 N  N   . LYS B 1 236 ? -18.198 21.498  -12.614 1.00 50.44  ? 236 LYS B N   1 
ATOM   4749 C  CA  . LYS B 1 236 ? -19.210 21.290  -13.688 1.00 54.22  ? 236 LYS B CA  1 
ATOM   4750 C  C   . LYS B 1 236 ? -18.964 19.944  -14.381 1.00 51.15  ? 236 LYS B C   1 
ATOM   4751 O  O   . LYS B 1 236 ? -19.949 19.319  -14.809 1.00 49.97  ? 236 LYS B O   1 
ATOM   4752 C  CB  . LYS B 1 236 ? -19.185 22.439  -14.705 1.00 62.11  ? 236 LYS B CB  1 
ATOM   4753 C  CG  . LYS B 1 236 ? -20.312 22.419  -15.743 1.00 71.57  ? 236 LYS B CG  1 
ATOM   4754 C  CD  . LYS B 1 236 ? -20.206 23.486  -16.841 1.00 76.52  ? 236 LYS B CD  1 
ATOM   4755 C  CE  . LYS B 1 236 ? -19.909 24.885  -16.332 1.00 78.11  ? 236 LYS B CE  1 
ATOM   4756 N  NZ  . LYS B 1 236 ? -20.935 25.356  -15.371 1.00 85.55  ? 236 LYS B NZ  1 
ATOM   4757 N  N   . TYR B 1 237 ? -17.704 19.510  -14.501 1.00 49.72  ? 237 TYR B N   1 
ATOM   4758 C  CA  . TYR B 1 237 ? -17.328 18.318  -15.307 1.00 46.16  ? 237 TYR B CA  1 
ATOM   4759 C  C   . TYR B 1 237 ? -17.020 17.119  -14.403 1.00 44.31  ? 237 TYR B C   1 
ATOM   4760 O  O   . TYR B 1 237 ? -16.507 16.121  -14.946 1.00 38.15  ? 237 TYR B O   1 
ATOM   4761 C  CB  . TYR B 1 237 ? -16.181 18.672  -16.258 1.00 47.50  ? 237 TYR B CB  1 
ATOM   4762 C  CG  . TYR B 1 237 ? -16.621 19.512  -17.429 1.00 50.14  ? 237 TYR B CG  1 
ATOM   4763 C  CD1 . TYR B 1 237 ? -16.621 20.903  -17.359 1.00 52.71  ? 237 TYR B CD1 1 
ATOM   4764 C  CD2 . TYR B 1 237 ? -17.099 18.918  -18.588 1.00 51.61  ? 237 TYR B CD2 1 
ATOM   4765 C  CE1 . TYR B 1 237 ? -17.063 21.685  -18.419 1.00 47.99  ? 237 TYR B CE1 1 
ATOM   4766 C  CE2 . TYR B 1 237 ? -17.543 19.682  -19.658 1.00 50.92  ? 237 TYR B CE2 1 
ATOM   4767 C  CZ  . TYR B 1 237 ? -17.523 21.066  -19.569 1.00 50.81  ? 237 TYR B CZ  1 
ATOM   4768 O  OH  . TYR B 1 237 ? -17.962 21.808  -20.623 1.00 55.32  ? 237 TYR B OH  1 
ATOM   4769 N  N   . ASN B 1 238 ? -17.403 17.171  -13.117 1.00 43.19  ? 238 ASN B N   1 
ATOM   4770 C  CA  . ASN B 1 238 ? -17.217 16.062  -12.139 1.00 44.24  ? 238 ASN B CA  1 
ATOM   4771 C  C   . ASN B 1 238 ? -15.719 15.817  -11.945 1.00 40.54  ? 238 ASN B C   1 
ATOM   4772 O  O   . ASN B 1 238 ? -15.297 14.664  -11.897 1.00 39.07  ? 238 ASN B O   1 
ATOM   4773 C  CB  . ASN B 1 238 ? -17.930 14.781  -12.574 1.00 46.30  ? 238 ASN B CB  1 
ATOM   4774 C  CG  . ASN B 1 238 ? -19.362 14.747  -12.100 1.00 53.69  ? 238 ASN B CG  1 
ATOM   4775 O  OD1 . ASN B 1 238 ? -19.839 15.699  -11.492 1.00 56.04  ? 238 ASN B OD1 1 
ATOM   4776 N  ND2 . ASN B 1 238 ? -20.056 13.653  -12.361 1.00 60.93  ? 238 ASN B ND2 1 
ATOM   4777 N  N   . TYR B 1 239 ? -14.960 16.895  -11.847 1.00 37.89  ? 239 TYR B N   1 
ATOM   4778 C  CA  . TYR B 1 239 ? -13.511 16.886  -11.590 1.00 41.11  ? 239 TYR B CA  1 
ATOM   4779 C  C   . TYR B 1 239 ? -13.300 17.288  -10.139 1.00 42.28  ? 239 TYR B C   1 
ATOM   4780 O  O   . TYR B 1 239 ? -13.946 18.246  -9.711  1.00 45.75  ? 239 TYR B O   1 
ATOM   4781 C  CB  . TYR B 1 239 ? -12.798 17.843  -12.546 1.00 37.58  ? 239 TYR B CB  1 
ATOM   4782 C  CG  . TYR B 1 239 ? -12.288 17.190  -13.804 1.00 35.21  ? 239 TYR B CG  1 
ATOM   4783 C  CD1 . TYR B 1 239 ? -13.137 16.498  -14.654 1.00 35.08  ? 239 TYR B CD1 1 
ATOM   4784 C  CD2 . TYR B 1 239 ? -10.945 17.259  -14.131 1.00 32.64  ? 239 TYR B CD2 1 
ATOM   4785 C  CE1 . TYR B 1 239 ? -12.662 15.899  -15.812 1.00 34.38  ? 239 TYR B CE1 1 
ATOM   4786 C  CE2 . TYR B 1 239 ? -10.455 16.667  -15.276 1.00 33.55  ? 239 TYR B CE2 1 
ATOM   4787 C  CZ  . TYR B 1 239 ? -11.313 15.990  -16.118 1.00 34.52  ? 239 TYR B CZ  1 
ATOM   4788 O  OH  . TYR B 1 239 ? -10.781 15.441  -17.240 1.00 34.48  ? 239 TYR B OH  1 
ATOM   4789 N  N   . GLU B 1 240 ? -12.383 16.615  -9.450  1.00 41.95  ? 240 GLU B N   1 
ATOM   4790 C  CA  . GLU B 1 240 ? -11.979 16.994  -8.077  1.00 40.45  ? 240 GLU B CA  1 
ATOM   4791 C  C   . GLU B 1 240 ? -11.567 18.460  -8.119  1.00 43.83  ? 240 GLU B C   1 
ATOM   4792 O  O   . GLU B 1 240 ? -11.081 18.948  -9.140  1.00 38.58  ? 240 GLU B O   1 
ATOM   4793 C  CB  . GLU B 1 240 ? -10.852 16.112  -7.538  1.00 38.73  ? 240 GLU B CB  1 
ATOM   4794 C  CG  . GLU B 1 240 ? -11.294 14.706  -7.197  1.00 43.84  ? 240 GLU B CG  1 
ATOM   4795 C  CD  . GLU B 1 240 ? -12.444 14.632  -6.206  1.00 44.22  ? 240 GLU B CD  1 
ATOM   4796 O  OE1 . GLU B 1 240 ? -12.236 15.027  -5.065  1.00 44.75  ? 240 GLU B OE1 1 
ATOM   4797 O  OE2 . GLU B 1 240 ? -13.533 14.171  -6.587  1.00 45.44  ? 240 GLU B OE2 1 
ATOM   4798 N  N   . PRO B 1 241 ? -11.784 19.205  -7.014  1.00 42.11  ? 241 PRO B N   1 
ATOM   4799 C  CA  . PRO B 1 241 ? -11.238 20.547  -6.888  1.00 42.29  ? 241 PRO B CA  1 
ATOM   4800 C  C   . PRO B 1 241 ? -9.701  20.521  -6.850  1.00 43.27  ? 241 PRO B C   1 
ATOM   4801 O  O   . PRO B 1 241 ? -9.104  19.617  -6.286  1.00 38.48  ? 241 PRO B O   1 
ATOM   4802 C  CB  . PRO B 1 241 ? -11.852 21.087  -5.584  1.00 43.83  ? 241 PRO B CB  1 
ATOM   4803 C  CG  . PRO B 1 241 ? -13.020 20.141  -5.283  1.00 43.72  ? 241 PRO B CG  1 
ATOM   4804 C  CD  . PRO B 1 241 ? -12.577 18.804  -5.839  1.00 44.63  ? 241 PRO B CD  1 
ATOM   4805 N  N   . LEU B 1 242 ? -9.088  21.513  -7.498  1.00 42.70  ? 242 LEU B N   1 
ATOM   4806 C  CA  . LEU B 1 242 ? -7.626  21.711  -7.490  1.00 40.75  ? 242 LEU B CA  1 
ATOM   4807 C  C   . LEU B 1 242 ? -7.261  22.654  -6.350  1.00 40.45  ? 242 LEU B C   1 
ATOM   4808 O  O   . LEU B 1 242 ? -7.737  23.786  -6.348  1.00 39.54  ? 242 LEU B O   1 
ATOM   4809 C  CB  . LEU B 1 242 ? -7.166  22.294  -8.823  1.00 41.22  ? 242 LEU B CB  1 
ATOM   4810 C  CG  . LEU B 1 242 ? -5.660  22.171  -9.058  1.00 40.55  ? 242 LEU B CG  1 
ATOM   4811 C  CD1 . LEU B 1 242 ? -5.262  20.714  -9.346  1.00 38.97  ? 242 LEU B CD1 1 
ATOM   4812 C  CD2 . LEU B 1 242 ? -5.220  23.086  -10.182 1.00 39.38  ? 242 LEU B CD2 1 
ATOM   4813 N  N   . THR B 1 243 ? -6.437  22.173  -5.426  1.00 45.67  ? 243 THR B N   1 
ATOM   4814 C  CA  . THR B 1 243 ? -6.008  22.919  -4.225  1.00 44.90  ? 243 THR B CA  1 
ATOM   4815 C  C   . THR B 1 243 ? -4.689  23.594  -4.562  1.00 44.32  ? 243 THR B C   1 
ATOM   4816 O  O   . THR B 1 243 ? -4.051  23.195  -5.553  1.00 42.05  ? 243 THR B O   1 
ATOM   4817 C  CB  . THR B 1 243 ? -5.919  22.011  -2.994  1.00 43.67  ? 243 THR B CB  1 
ATOM   4818 O  OG1 . THR B 1 243 ? -4.790  21.150  -3.117  1.00 47.83  ? 243 THR B OG1 1 
ATOM   4819 C  CG2 . THR B 1 243 ? -7.158  21.172  -2.783  1.00 46.42  ? 243 THR B CG2 1 
ATOM   4820 N  N   . GLN B 1 244 ? -4.317  24.579  -3.756  1.00 42.91  ? 244 GLN B N   1 
ATOM   4821 C  CA  . GLN B 1 244 ? -2.996  25.246  -3.817  1.00 44.68  ? 244 GLN B CA  1 
ATOM   4822 C  C   . GLN B 1 244 ? -1.886  24.209  -3.609  1.00 46.28  ? 244 GLN B C   1 
ATOM   4823 O  O   . GLN B 1 244 ? -0.800  24.374  -4.184  1.00 47.22  ? 244 GLN B O   1 
ATOM   4824 C  CB  . GLN B 1 244 ? -2.920  26.345  -2.756  1.00 44.06  ? 244 GLN B CB  1 
ATOM   4825 C  CG  . GLN B 1 244 ? -1.562  27.021  -2.704  1.00 43.38  ? 244 GLN B CG  1 
ATOM   4826 C  CD  . GLN B 1 244 ? -1.186  27.501  -4.080  1.00 43.15  ? 244 GLN B CD  1 
ATOM   4827 O  OE1 . GLN B 1 244 ? -2.015  28.035  -4.812  1.00 41.76  ? 244 GLN B OE1 1 
ATOM   4828 N  NE2 . GLN B 1 244 ? 0.055   27.253  -4.458  1.00 46.25  ? 244 GLN B NE2 1 
ATOM   4829 N  N   . ASP B 1 245 ? -2.142  23.179  -2.804  1.00 47.11  ? 245 ASP B N   1 
ATOM   4830 C  CA  . ASP B 1 245 ? -1.163  22.100  -2.499  1.00 49.35  ? 245 ASP B CA  1 
ATOM   4831 C  C   . ASP B 1 245 ? -0.801  21.352  -3.802  1.00 45.51  ? 245 ASP B C   1 
ATOM   4832 O  O   . ASP B 1 245 ? 0.387   21.080  -4.033  1.00 43.18  ? 245 ASP B O   1 
ATOM   4833 C  CB  . ASP B 1 245 ? -1.735  21.195  -1.406  1.00 54.87  ? 245 ASP B CB  1 
ATOM   4834 C  CG  . ASP B 1 245 ? -0.787  20.101  -0.962  1.00 65.50  ? 245 ASP B CG  1 
ATOM   4835 O  OD1 . ASP B 1 245 ? 0.359   20.435  -0.594  1.00 75.43  ? 245 ASP B OD1 1 
ATOM   4836 O  OD2 . ASP B 1 245 ? -1.201  18.919  -1.000  1.00 76.83  ? 245 ASP B OD2 1 
ATOM   4837 N  N   . HIS B 1 246 ? -1.790  21.060  -4.644  1.00 38.65  ? 246 HIS B N   1 
ATOM   4838 C  CA  . HIS B 1 246 ? -1.619  20.404  -5.967  1.00 40.28  ? 246 HIS B CA  1 
ATOM   4839 C  C   . HIS B 1 246 ? -0.712  21.252  -6.865  1.00 40.93  ? 246 HIS B C   1 
ATOM   4840 O  O   . HIS B 1 246 ? 0.133   20.661  -7.574  1.00 39.98  ? 246 HIS B O   1 
ATOM   4841 C  CB  . HIS B 1 246 ? -2.972  20.191  -6.651  1.00 38.43  ? 246 HIS B CB  1 
ATOM   4842 C  CG  . HIS B 1 246 ? -3.913  19.266  -5.952  1.00 41.16  ? 246 HIS B CG  1 
ATOM   4843 N  ND1 . HIS B 1 246 ? -5.294  19.406  -6.066  1.00 41.01  ? 246 HIS B ND1 1 
ATOM   4844 C  CD2 . HIS B 1 246 ? -3.700  18.176  -5.174  1.00 38.94  ? 246 HIS B CD2 1 
ATOM   4845 C  CE1 . HIS B 1 246 ? -5.885  18.441  -5.386  1.00 41.10  ? 246 HIS B CE1 1 
ATOM   4846 N  NE2 . HIS B 1 246 ? -4.933  17.670  -4.839  1.00 36.70  ? 246 HIS B NE2 1 
ATOM   4847 N  N   . VAL B 1 247 ? -0.893  22.581  -6.859  1.00 41.18  ? 247 VAL B N   1 
ATOM   4848 C  CA  . VAL B 1 247 ? -0.060  23.515  -7.673  1.00 40.97  ? 247 VAL B CA  1 
ATOM   4849 C  C   . VAL B 1 247 ? 1.387   23.396  -7.194  1.00 44.69  ? 247 VAL B C   1 
ATOM   4850 O  O   . VAL B 1 247 ? 2.282   23.348  -8.041  1.00 46.73  ? 247 VAL B O   1 
ATOM   4851 C  CB  . VAL B 1 247 ? -0.587  24.963  -7.640  1.00 42.08  ? 247 VAL B CB  1 
ATOM   4852 C  CG1 . VAL B 1 247 ? 0.397   25.955  -8.247  1.00 40.47  ? 247 VAL B CG1 1 
ATOM   4853 C  CG2 . VAL B 1 247 ? -1.940  25.073  -8.334  1.00 42.01  ? 247 VAL B CG2 1 
ATOM   4854 N  N   . ASP B 1 248 ? 1.611   23.283  -5.886  1.00 46.94  ? 248 ASP B N   1 
ATOM   4855 C  CA  . ASP B 1 248 ? 2.981   23.181  -5.316  1.00 47.05  ? 248 ASP B CA  1 
ATOM   4856 C  C   . ASP B 1 248 ? 3.616   21.841  -5.730  1.00 47.36  ? 248 ASP B C   1 
ATOM   4857 O  O   . ASP B 1 248 ? 4.804   21.829  -6.105  1.00 50.28  ? 248 ASP B O   1 
ATOM   4858 C  CB  . ASP B 1 248 ? 2.947   23.375  -3.798  1.00 47.28  ? 248 ASP B CB  1 
ATOM   4859 C  CG  . ASP B 1 248 ? 2.214   24.626  -3.344  1.00 48.36  ? 248 ASP B CG  1 
ATOM   4860 O  OD1 . ASP B 1 248 ? 2.119   25.596  -4.135  1.00 43.58  ? 248 ASP B OD1 1 
ATOM   4861 O  OD2 . ASP B 1 248 ? 1.714   24.609  -2.208  1.00 55.58  ? 248 ASP B OD2 1 
ATOM   4862 N  N   . ILE B 1 249 ? 2.848   20.754  -5.677  1.00 47.46  ? 249 ILE B N   1 
ATOM   4863 C  CA  . ILE B 1 249 ? 3.282   19.370  -6.038  1.00 47.81  ? 249 ILE B CA  1 
ATOM   4864 C  C   . ILE B 1 249 ? 3.612   19.289  -7.539  1.00 46.03  ? 249 ILE B C   1 
ATOM   4865 O  O   . ILE B 1 249 ? 4.469   18.460  -7.900  1.00 47.72  ? 249 ILE B O   1 
ATOM   4866 C  CB  . ILE B 1 249 ? 2.181   18.373  -5.621  1.00 54.21  ? 249 ILE B CB  1 
ATOM   4867 C  CG1 . ILE B 1 249 ? 2.041   18.318  -4.096  1.00 57.03  ? 249 ILE B CG1 1 
ATOM   4868 C  CG2 . ILE B 1 249 ? 2.421   16.992  -6.202  1.00 55.32  ? 249 ILE B CG2 1 
ATOM   4869 C  CD1 . ILE B 1 249 ? 0.780   17.628  -3.616  1.00 54.70  ? 249 ILE B CD1 1 
ATOM   4870 N  N   . LEU B 1 250 ? 2.959   20.097  -8.384  1.00 43.61  ? 250 LEU B N   1 
ATOM   4871 C  CA  . LEU B 1 250 ? 3.235   20.175  -9.850  1.00 47.43  ? 250 LEU B CA  1 
ATOM   4872 C  C   . LEU B 1 250 ? 4.397   21.136  -10.132 1.00 50.33  ? 250 LEU B C   1 
ATOM   4873 O  O   . LEU B 1 250 ? 4.846   21.180  -11.291 1.00 49.73  ? 250 LEU B O   1 
ATOM   4874 C  CB  . LEU B 1 250 ? 1.978   20.628  -10.602 1.00 42.72  ? 250 LEU B CB  1 
ATOM   4875 C  CG  . LEU B 1 250 ? 0.869   19.582  -10.715 1.00 40.77  ? 250 LEU B CG  1 
ATOM   4876 C  CD1 . LEU B 1 250 ? -0.450  20.220  -11.156 1.00 36.39  ? 250 LEU B CD1 1 
ATOM   4877 C  CD2 . LEU B 1 250 ? 1.276   18.464  -11.665 1.00 40.64  ? 250 LEU B CD2 1 
ATOM   4878 N  N   . GLY B 1 251 ? 4.870   21.869  -9.117  1.00 56.44  ? 251 GLY B N   1 
ATOM   4879 C  CA  . GLY B 1 251 ? 5.970   22.847  -9.237  1.00 58.20  ? 251 GLY B CA  1 
ATOM   4880 C  C   . GLY B 1 251 ? 7.127   22.338  -10.094 1.00 54.84  ? 251 GLY B C   1 
ATOM   4881 O  O   . GLY B 1 251 ? 7.561   23.028  -11.010 1.00 63.25  ? 251 GLY B O   1 
ATOM   4882 N  N   . PRO B 1 252 ? 7.674   21.132  -9.822  1.00 50.37  ? 252 PRO B N   1 
ATOM   4883 C  CA  . PRO B 1 252 ? 8.798   20.606  -10.590 1.00 52.97  ? 252 PRO B CA  1 
ATOM   4884 C  C   . PRO B 1 252 ? 8.515   20.563  -12.097 1.00 56.07  ? 252 PRO B C   1 
ATOM   4885 O  O   . PRO B 1 252 ? 9.310   21.081  -12.867 1.00 63.74  ? 252 PRO B O   1 
ATOM   4886 C  CB  . PRO B 1 252 ? 8.966   19.179  -10.051 1.00 52.93  ? 252 PRO B CB  1 
ATOM   4887 C  CG  . PRO B 1 252 ? 8.410   19.246  -8.656  1.00 51.60  ? 252 PRO B CG  1 
ATOM   4888 C  CD  . PRO B 1 252 ? 7.248   20.204  -8.766  1.00 50.96  ? 252 PRO B CD  1 
ATOM   4889 N  N   . LEU B 1 253 ? 7.387   19.957  -12.470 1.00 55.49  ? 253 LEU B N   1 
ATOM   4890 C  CA  . LEU B 1 253 ? 6.989   19.739  -13.884 1.00 49.40  ? 253 LEU B CA  1 
ATOM   4891 C  C   . LEU B 1 253 ? 6.725   21.095  -14.542 1.00 53.13  ? 253 LEU B C   1 
ATOM   4892 O  O   . LEU B 1 253 ? 7.049   21.236  -15.743 1.00 54.44  ? 253 LEU B O   1 
ATOM   4893 C  CB  . LEU B 1 253 ? 5.744   18.845  -13.935 1.00 46.14  ? 253 LEU B CB  1 
ATOM   4894 C  CG  . LEU B 1 253 ? 5.910   17.426  -13.389 1.00 44.43  ? 253 LEU B CG  1 
ATOM   4895 C  CD1 . LEU B 1 253 ? 4.558   16.746  -13.236 1.00 42.60  ? 253 LEU B CD1 1 
ATOM   4896 C  CD2 . LEU B 1 253 ? 6.818   16.593  -14.279 1.00 43.88  ? 253 LEU B CD2 1 
ATOM   4897 N  N   . SER B 1 254 ? 6.136   22.043  -13.799 1.00 56.21  ? 254 SER B N   1 
ATOM   4898 C  CA  . SER B 1 254 ? 5.797   23.408  -14.289 1.00 56.80  ? 254 SER B CA  1 
ATOM   4899 C  C   . SER B 1 254 ? 7.081   24.159  -14.642 1.00 57.58  ? 254 SER B C   1 
ATOM   4900 O  O   . SER B 1 254 ? 7.110   24.854  -15.692 1.00 56.15  ? 254 SER B O   1 
ATOM   4901 C  CB  . SER B 1 254 ? 4.993   24.198  -13.295 1.00 58.48  ? 254 SER B CB  1 
ATOM   4902 O  OG  . SER B 1 254 ? 4.784   25.529  -13.768 1.00 56.90  ? 254 SER B OG  1 
ATOM   4903 N  N   . ALA B 1 255 ? 8.082   24.031  -13.773 1.00 60.69  ? 255 ALA B N   1 
ATOM   4904 C  CA  . ALA B 1 255 ? 9.458   24.515  -13.995 1.00 66.68  ? 255 ALA B CA  1 
ATOM   4905 C  C   . ALA B 1 255 ? 9.955   23.905  -15.304 1.00 68.34  ? 255 ALA B C   1 
ATOM   4906 O  O   . ALA B 1 255 ? 10.002  24.635  -16.310 1.00 69.62  ? 255 ALA B O   1 
ATOM   4907 C  CB  . ALA B 1 255 ? 10.340  24.147  -12.826 1.00 67.95  ? 255 ALA B CB  1 
ATOM   4908 N  N   . GLN B 1 256 ? 10.180  22.589  -15.307 1.00 70.66  ? 256 GLN B N   1 
ATOM   4909 C  CA  . GLN B 1 256 ? 10.964  21.871  -16.347 1.00 67.02  ? 256 GLN B CA  1 
ATOM   4910 C  C   . GLN B 1 256 ? 10.350  22.009  -17.745 1.00 66.31  ? 256 GLN B C   1 
ATOM   4911 O  O   . GLN B 1 256 ? 11.059  21.699  -18.712 1.00 77.59  ? 256 GLN B O   1 
ATOM   4912 C  CB  . GLN B 1 256 ? 11.092  20.392  -16.013 1.00 66.71  ? 256 GLN B CB  1 
ATOM   4913 C  CG  . GLN B 1 256 ? 12.104  19.696  -16.903 1.00 71.44  ? 256 GLN B CG  1 
ATOM   4914 C  CD  . GLN B 1 256 ? 11.809  18.226  -17.042 1.00 76.52  ? 256 GLN B CD  1 
ATOM   4915 O  OE1 . GLN B 1 256 ? 11.556  17.527  -16.063 1.00 78.68  ? 256 GLN B OE1 1 
ATOM   4916 N  NE2 . GLN B 1 256 ? 11.841  17.751  -18.276 1.00 86.60  ? 256 GLN B NE2 1 
ATOM   4917 N  N   . THR B 1 257 ? 9.101   22.445  -17.876 1.00 58.07  ? 257 THR B N   1 
ATOM   4918 C  CA  . THR B 1 257 ? 8.439   22.605  -19.193 1.00 59.00  ? 257 THR B CA  1 
ATOM   4919 C  C   . THR B 1 257 ? 8.183   24.089  -19.506 1.00 60.79  ? 257 THR B C   1 
ATOM   4920 O  O   . THR B 1 257 ? 7.862   24.381  -20.656 1.00 58.84  ? 257 THR B O   1 
ATOM   4921 C  CB  . THR B 1 257 ? 7.141   21.793  -19.214 1.00 57.14  ? 257 THR B CB  1 
ATOM   4922 O  OG1 . THR B 1 257 ? 6.337   22.297  -18.148 1.00 58.58  ? 257 THR B OG1 1 
ATOM   4923 C  CG2 . THR B 1 257 ? 7.363   20.302  -19.053 1.00 53.64  ? 257 THR B CG2 1 
ATOM   4924 N  N   . GLY B 1 258 ? 8.286   24.996  -18.530 1.00 69.09  ? 258 GLY B N   1 
ATOM   4925 C  CA  . GLY B 1 258 ? 7.966   26.426  -18.722 1.00 69.19  ? 258 GLY B CA  1 
ATOM   4926 C  C   . GLY B 1 258 ? 6.486   26.641  -19.005 1.00 72.18  ? 258 GLY B C   1 
ATOM   4927 O  O   . GLY B 1 258 ? 6.134   27.704  -19.589 1.00 66.95  ? 258 GLY B O   1 
ATOM   4928 N  N   . ILE B 1 259 ? 5.644   25.669  -18.627 1.00 64.52  ? 259 ILE B N   1 
ATOM   4929 C  CA  . ILE B 1 259 ? 4.173   25.850  -18.495 1.00 63.56  ? 259 ILE B CA  1 
ATOM   4930 C  C   . ILE B 1 259 ? 3.855   25.928  -16.999 1.00 67.35  ? 259 ILE B C   1 
ATOM   4931 O  O   . ILE B 1 259 ? 4.236   24.997  -16.262 1.00 61.31  ? 259 ILE B O   1 
ATOM   4932 C  CB  . ILE B 1 259 ? 3.385   24.731  -19.202 1.00 63.51  ? 259 ILE B CB  1 
ATOM   4933 C  CG1 . ILE B 1 259 ? 3.664   24.699  -20.705 1.00 62.41  ? 259 ILE B CG1 1 
ATOM   4934 C  CG2 . ILE B 1 259 ? 1.896   24.875  -18.920 1.00 64.89  ? 259 ILE B CG2 1 
ATOM   4935 C  CD1 . ILE B 1 259 ? 4.787   23.787  -21.097 1.00 61.50  ? 259 ILE B CD1 1 
ATOM   4936 N  N   . ALA B 1 260 ? 3.229   27.030  -16.577 1.00 65.23  ? 260 ALA B N   1 
ATOM   4937 C  CA  . ALA B 1 260 ? 2.735   27.264  -15.203 1.00 62.09  ? 260 ALA B CA  1 
ATOM   4938 C  C   . ALA B 1 260 ? 1.430   26.494  -15.024 1.00 54.55  ? 260 ALA B C   1 
ATOM   4939 O  O   . ALA B 1 260 ? 0.664   26.403  -15.992 1.00 55.15  ? 260 ALA B O   1 
ATOM   4940 C  CB  . ALA B 1 260 ? 2.524   28.737  -14.968 1.00 64.45  ? 260 ALA B CB  1 
ATOM   4941 N  N   . VAL B 1 261 ? 1.166   25.992  -13.823 1.00 49.52  ? 261 VAL B N   1 
ATOM   4942 C  CA  . VAL B 1 261 ? 0.009   25.082  -13.593 1.00 46.20  ? 261 VAL B CA  1 
ATOM   4943 C  C   . VAL B 1 261 ? -1.265  25.745  -14.122 1.00 46.35  ? 261 VAL B C   1 
ATOM   4944 O  O   . VAL B 1 261 ? -2.080  25.050  -14.779 1.00 46.79  ? 261 VAL B O   1 
ATOM   4945 C  CB  . VAL B 1 261 ? -0.118  24.662  -12.119 1.00 45.83  ? 261 VAL B CB  1 
ATOM   4946 C  CG1 . VAL B 1 261 ? -1.316  23.742  -11.919 1.00 50.72  ? 261 VAL B CG1 1 
ATOM   4947 C  CG2 . VAL B 1 261 ? 1.155   24.000  -11.610 1.00 45.17  ? 261 VAL B CG2 1 
ATOM   4948 N  N   . LEU B 1 262 ? -1.461  27.039  -13.856 1.00 50.13  ? 262 LEU B N   1 
ATOM   4949 C  CA  . LEU B 1 262 ? -2.698  27.756  -14.284 1.00 45.16  ? 262 LEU B CA  1 
ATOM   4950 C  C   . LEU B 1 262 ? -2.663  27.996  -15.807 1.00 41.06  ? 262 LEU B C   1 
ATOM   4951 O  O   . LEU B 1 262 ? -3.739  28.011  -16.455 1.00 37.35  ? 262 LEU B O   1 
ATOM   4952 C  CB  . LEU B 1 262 ? -2.816  29.043  -13.455 1.00 50.32  ? 262 LEU B CB  1 
ATOM   4953 C  CG  . LEU B 1 262 ? -3.278  28.830  -12.010 1.00 49.04  ? 262 LEU B CG  1 
ATOM   4954 C  CD1 . LEU B 1 262 ? -3.205  30.118  -11.203 1.00 50.57  ? 262 LEU B CD1 1 
ATOM   4955 C  CD2 . LEU B 1 262 ? -4.694  28.261  -11.968 1.00 47.44  ? 262 LEU B CD2 1 
ATOM   4956 N  N   . ASP B 1 263 ? -1.466  28.094  -16.386 1.00 42.65  ? 263 ASP B N   1 
ATOM   4957 C  CA  . ASP B 1 263 ? -1.278  27.986  -17.860 1.00 47.47  ? 263 ASP B CA  1 
ATOM   4958 C  C   . ASP B 1 263 ? -1.803  26.609  -18.325 1.00 43.93  ? 263 ASP B C   1 
ATOM   4959 O  O   . ASP B 1 263 ? -2.682  26.576  -19.207 1.00 41.79  ? 263 ASP B O   1 
ATOM   4960 C  CB  . ASP B 1 263 ? 0.182   28.245  -18.235 1.00 46.43  ? 263 ASP B CB  1 
ATOM   4961 C  CG  . ASP B 1 263 ? 0.418   28.350  -19.730 1.00 45.33  ? 263 ASP B CG  1 
ATOM   4962 O  OD1 . ASP B 1 263 ? -0.547  28.144  -20.523 1.00 45.96  ? 263 ASP B OD1 1 
ATOM   4963 O  OD2 . ASP B 1 263 ? 1.564   28.634  -20.087 1.00 50.93  ? 263 ASP B OD2 1 
ATOM   4964 N  N   . MET B 1 264 ? -1.348  25.509  -17.712 1.00 40.32  ? 264 MET B N   1 
ATOM   4965 C  CA  . MET B 1 264 ? -1.823  24.152  -18.093 1.00 38.12  ? 264 MET B CA  1 
ATOM   4966 C  C   . MET B 1 264 ? -3.315  24.036  -17.772 1.00 41.12  ? 264 MET B C   1 
ATOM   4967 O  O   . MET B 1 264 ? -4.038  23.424  -18.578 1.00 38.89  ? 264 MET B O   1 
ATOM   4968 C  CB  . MET B 1 264 ? -1.035  23.050  -17.379 1.00 38.22  ? 264 MET B CB  1 
ATOM   4969 C  CG  . MET B 1 264 ? -1.271  21.671  -17.974 1.00 37.76  ? 264 MET B CG  1 
ATOM   4970 S  SD  . MET B 1 264 ? -0.537  21.524  -19.613 1.00 35.36  ? 264 MET B SD  1 
ATOM   4971 C  CE  . MET B 1 264 ? 1.120   21.046  -19.156 1.00 38.04  ? 264 MET B CE  1 
ATOM   4972 N  N   . CYS B 1 265 ? -3.784  24.604  -16.648 1.00 40.90  ? 265 CYS B N   1 
ATOM   4973 C  CA  . CYS B 1 265 ? -5.219  24.522  -16.271 1.00 43.71  ? 265 CYS B CA  1 
ATOM   4974 C  C   . CYS B 1 265 ? -6.061  25.126  -17.388 1.00 40.85  ? 265 CYS B C   1 
ATOM   4975 O  O   . CYS B 1 265 ? -7.127  24.577  -17.684 1.00 36.59  ? 265 CYS B O   1 
ATOM   4976 C  CB  . CYS B 1 265 ? -5.525  25.212  -14.949 1.00 48.31  ? 265 CYS B CB  1 
ATOM   4977 S  SG  . CYS B 1 265 ? -4.934  24.270  -13.524 1.00 48.53  ? 265 CYS B SG  1 
ATOM   4978 N  N   . ALA B 1 266 ? -5.566  26.203  -18.008 1.00 48.28  ? 266 ALA B N   1 
ATOM   4979 C  CA  . ALA B 1 266 ? -6.224  26.864  -19.158 1.00 45.73  ? 266 ALA B CA  1 
ATOM   4980 C  C   . ALA B 1 266 ? -6.315  25.873  -20.329 1.00 41.12  ? 266 ALA B C   1 
ATOM   4981 O  O   . ALA B 1 266 ? -7.399  25.800  -20.945 1.00 35.15  ? 266 ALA B O   1 
ATOM   4982 C  CB  . ALA B 1 266 ? -5.491  28.134  -19.526 1.00 50.42  ? 266 ALA B CB  1 
ATOM   4983 N  N   . SER B 1 267 ? -5.242  25.107  -20.596 1.00 40.55  ? 267 SER B N   1 
ATOM   4984 C  CA  . SER B 1 267 ? -5.258  23.991  -21.593 1.00 38.53  ? 267 SER B CA  1 
ATOM   4985 C  C   . SER B 1 267 ? -6.371  23.002  -21.220 1.00 34.41  ? 267 SER B C   1 
ATOM   4986 O  O   . SER B 1 267 ? -7.183  22.680  -22.093 1.00 30.46  ? 267 SER B O   1 
ATOM   4987 C  CB  . SER B 1 267 ? -3.920  23.304  -21.718 1.00 36.27  ? 267 SER B CB  1 
ATOM   4988 O  OG  . SER B 1 267 ? -2.982  24.098  -22.454 1.00 40.35  ? 267 SER B OG  1 
ATOM   4989 N  N   . LEU B 1 268 ? -6.431  22.562  -19.952 1.00 37.17  ? 268 LEU B N   1 
ATOM   4990 C  CA  . LEU B 1 268 ? -7.420  21.535  -19.505 1.00 37.72  ? 268 LEU B CA  1 
ATOM   4991 C  C   . LEU B 1 268 ? -8.832  22.119  -19.530 1.00 37.04  ? 268 LEU B C   1 
ATOM   4992 O  O   . LEU B 1 268 ? -9.804  21.399  -19.939 1.00 32.50  ? 268 LEU B O   1 
ATOM   4993 C  CB  . LEU B 1 268 ? -7.053  21.051  -18.100 1.00 37.25  ? 268 LEU B CB  1 
ATOM   4994 C  CG  . LEU B 1 268 ? -8.043  20.084  -17.447 1.00 35.47  ? 268 LEU B CG  1 
ATOM   4995 C  CD1 . LEU B 1 268 ? -8.370  18.910  -18.356 1.00 35.72  ? 268 LEU B CD1 1 
ATOM   4996 C  CD2 . LEU B 1 268 ? -7.488  19.591  -16.118 1.00 35.53  ? 268 LEU B CD2 1 
ATOM   4997 N  N   . LYS B 1 269 ? -8.977  23.380  -19.119 1.00 39.84  ? 269 LYS B N   1 
ATOM   4998 C  CA  . LYS B 1 269 ? -10.302 24.047  -19.201 1.00 46.41  ? 269 LYS B CA  1 
ATOM   4999 C  C   . LYS B 1 269 ? -10.843 23.830  -20.618 1.00 43.97  ? 269 LYS B C   1 
ATOM   5000 O  O   . LYS B 1 269 ? -11.975 23.376  -20.766 1.00 44.41  ? 269 LYS B O   1 
ATOM   5001 C  CB  . LYS B 1 269 ? -10.174 25.523  -18.812 1.00 52.78  ? 269 LYS B CB  1 
ATOM   5002 C  CG  . LYS B 1 269 ? -11.442 26.361  -18.983 1.00 60.32  ? 269 LYS B CG  1 
ATOM   5003 C  CD  . LYS B 1 269 ? -11.245 27.828  -18.605 1.00 63.28  ? 269 LYS B CD  1 
ATOM   5004 C  CE  . LYS B 1 269 ? -10.828 27.994  -17.153 1.00 69.51  ? 269 LYS B CE  1 
ATOM   5005 N  NZ  . LYS B 1 269 ? -10.816 29.409  -16.707 1.00 76.13  ? 269 LYS B NZ  1 
ATOM   5006 N  N   . GLU B 1 270 ? -10.014 24.095  -21.629 1.00 49.16  ? 270 GLU B N   1 
ATOM   5007 C  CA  . GLU B 1 270 ? -10.419 24.056  -23.059 1.00 48.05  ? 270 GLU B CA  1 
ATOM   5008 C  C   . GLU B 1 270 ? -10.745 22.620  -23.486 1.00 45.22  ? 270 GLU B C   1 
ATOM   5009 O  O   . GLU B 1 270 ? -11.692 22.468  -24.275 1.00 39.67  ? 270 GLU B O   1 
ATOM   5010 C  CB  . GLU B 1 270 ? -9.332  24.666  -23.951 1.00 51.22  ? 270 GLU B CB  1 
ATOM   5011 C  CG  . GLU B 1 270 ? -9.167  26.174  -23.792 1.00 54.81  ? 270 GLU B CG  1 
ATOM   5012 C  CD  . GLU B 1 270 ? -10.450 27.000  -23.807 1.00 55.14  ? 270 GLU B CD  1 
ATOM   5013 O  OE1 . GLU B 1 270 ? -11.382 26.653  -24.567 1.00 57.99  ? 270 GLU B OE1 1 
ATOM   5014 O  OE2 . GLU B 1 270 ? -10.523 27.981  -23.035 1.00 50.20  ? 270 GLU B OE2 1 
ATOM   5015 N  N   . LEU B 1 271 ? -9.985  21.612  -23.027 1.00 41.65  ? 271 LEU B N   1 
ATOM   5016 C  CA  . LEU B 1 271 ? -10.235 20.198  -23.438 1.00 41.49  ? 271 LEU B CA  1 
ATOM   5017 C  C   . LEU B 1 271 ? -11.594 19.724  -22.906 1.00 40.05  ? 271 LEU B C   1 
ATOM   5018 O  O   . LEU B 1 271 ? -12.262 18.984  -23.645 1.00 38.22  ? 271 LEU B O   1 
ATOM   5019 C  CB  . LEU B 1 271 ? -9.105  19.280  -22.963 1.00 39.17  ? 271 LEU B CB  1 
ATOM   5020 C  CG  . LEU B 1 271 ? -7.772  19.487  -23.674 1.00 39.28  ? 271 LEU B CG  1 
ATOM   5021 C  CD1 . LEU B 1 271 ? -6.612  18.983  -22.834 1.00 40.05  ? 271 LEU B CD1 1 
ATOM   5022 C  CD2 . LEU B 1 271 ? -7.776  18.823  -25.037 1.00 39.52  ? 271 LEU B CD2 1 
ATOM   5023 N  N   . LEU B 1 272 ? -11.974 20.091  -21.674 1.00 40.35  ? 272 LEU B N   1 
ATOM   5024 C  CA  . LEU B 1 272 ? -13.270 19.663  -21.073 1.00 44.51  ? 272 LEU B CA  1 
ATOM   5025 C  C   . LEU B 1 272 ? -14.434 20.262  -21.866 1.00 49.66  ? 272 LEU B C   1 
ATOM   5026 O  O   . LEU B 1 272 ? -15.457 19.577  -22.048 1.00 48.55  ? 272 LEU B O   1 
ATOM   5027 C  CB  . LEU B 1 272 ? -13.354 20.144  -19.627 1.00 47.18  ? 272 LEU B CB  1 
ATOM   5028 C  CG  . LEU B 1 272 ? -12.319 19.574  -18.666 1.00 47.18  ? 272 LEU B CG  1 
ATOM   5029 C  CD1 . LEU B 1 272 ? -12.373 20.295  -17.325 1.00 44.68  ? 272 LEU B CD1 1 
ATOM   5030 C  CD2 . LEU B 1 272 ? -12.518 18.081  -18.486 1.00 50.77  ? 272 LEU B CD2 1 
ATOM   5031 N  N   . GLN B 1 273 ? -14.283 21.524  -22.279 1.00 57.70  ? 273 GLN B N   1 
ATOM   5032 C  CA  . GLN B 1 273 ? -15.333 22.311  -22.984 1.00 57.00  ? 273 GLN B CA  1 
ATOM   5033 C  C   . GLN B 1 273 ? -15.399 21.879  -24.455 1.00 55.08  ? 273 GLN B C   1 
ATOM   5034 O  O   . GLN B 1 273 ? -16.511 21.809  -24.979 1.00 58.22  ? 273 GLN B O   1 
ATOM   5035 C  CB  . GLN B 1 273 ? -15.062 23.809  -22.789 1.00 56.02  ? 273 GLN B CB  1 
ATOM   5036 C  CG  . GLN B 1 273 ? -15.195 24.236  -21.329 1.00 55.96  ? 273 GLN B CG  1 
ATOM   5037 C  CD  . GLN B 1 273 ? -14.811 25.665  -21.020 1.00 55.95  ? 273 GLN B CD  1 
ATOM   5038 O  OE1 . GLN B 1 273 ? -13.997 26.282  -21.709 1.00 54.18  ? 273 GLN B OE1 1 
ATOM   5039 N  NE2 . GLN B 1 273 ? -15.392 26.200  -19.957 1.00 47.68  ? 273 GLN B NE2 1 
ATOM   5040 N  N   . ASN B 1 274 ? -14.264 21.540  -25.081 1.00 54.27  ? 274 ASN B N   1 
ATOM   5041 C  CA  . ASN B 1 274 ? -14.159 21.374  -26.560 1.00 52.73  ? 274 ASN B CA  1 
ATOM   5042 C  C   . ASN B 1 274 ? -13.872 19.929  -26.986 1.00 50.81  ? 274 ASN B C   1 
ATOM   5043 O  O   . ASN B 1 274 ? -14.043 19.655  -28.190 1.00 49.15  ? 274 ASN B O   1 
ATOM   5044 C  CB  . ASN B 1 274 ? -13.080 22.291  -27.133 1.00 50.43  ? 274 ASN B CB  1 
ATOM   5045 C  CG  . ASN B 1 274 ? -13.461 23.748  -26.988 1.00 53.69  ? 274 ASN B CG  1 
ATOM   5046 O  OD1 . ASN B 1 274 ? -14.418 24.184  -27.616 1.00 52.40  ? 274 ASN B OD1 1 
ATOM   5047 N  ND2 . ASN B 1 274 ? -12.756 24.495  -26.148 1.00 51.38  ? 274 ASN B ND2 1 
ATOM   5048 N  N   . GLY B 1 275 ? -13.423 19.061  -26.071 1.00 48.84  ? 275 GLY B N   1 
ATOM   5049 C  CA  . GLY B 1 275 ? -12.888 17.725  -26.409 1.00 48.07  ? 275 GLY B CA  1 
ATOM   5050 C  C   . GLY B 1 275 ? -11.515 17.833  -27.052 1.00 44.95  ? 275 GLY B C   1 
ATOM   5051 O  O   . GLY B 1 275 ? -10.896 18.902  -26.938 1.00 39.28  ? 275 GLY B O   1 
ATOM   5052 N  N   . MET B 1 276 ? -11.072 16.775  -27.735 1.00 46.13  ? 276 MET B N   1 
ATOM   5053 C  CA  . MET B 1 276 ? -9.721  16.664  -28.347 1.00 49.26  ? 276 MET B CA  1 
ATOM   5054 C  C   . MET B 1 276 ? -9.767  16.968  -29.856 1.00 46.54  ? 276 MET B C   1 
ATOM   5055 O  O   . MET B 1 276 ? -8.690  16.918  -30.502 1.00 46.15  ? 276 MET B O   1 
ATOM   5056 C  CB  . MET B 1 276 ? -9.165  15.255  -28.101 1.00 51.12  ? 276 MET B CB  1 
ATOM   5057 C  CG  . MET B 1 276 ? -8.808  14.997  -26.639 1.00 51.87  ? 276 MET B CG  1 
ATOM   5058 S  SD  . MET B 1 276 ? -7.616  13.634  -26.437 1.00 49.41  ? 276 MET B SD  1 
ATOM   5059 C  CE  . MET B 1 276 ? -7.714  13.403  -24.664 1.00 48.90  ? 276 MET B CE  1 
ATOM   5060 N  N   . ASN B 1 277 ? -10.942 17.310  -30.406 1.00 46.88  ? 277 ASN B N   1 
ATOM   5061 C  CA  . ASN B 1 277 ? -11.134 17.600  -31.855 1.00 50.11  ? 277 ASN B CA  1 
ATOM   5062 C  C   . ASN B 1 277 ? -10.377 16.538  -32.671 1.00 47.15  ? 277 ASN B C   1 
ATOM   5063 O  O   . ASN B 1 277 ? -9.506  16.899  -33.476 1.00 50.88  ? 277 ASN B O   1 
ATOM   5064 C  CB  . ASN B 1 277 ? -10.727 19.035  -32.229 1.00 56.77  ? 277 ASN B CB  1 
ATOM   5065 C  CG  . ASN B 1 277 ? -11.697 20.098  -31.741 1.00 66.01  ? 277 ASN B CG  1 
ATOM   5066 O  OD1 . ASN B 1 277 ? -11.299 21.038  -31.045 1.00 67.23  ? 277 ASN B OD1 1 
ATOM   5067 N  ND2 . ASN B 1 277 ? -12.968 19.973  -32.105 1.00 65.14  ? 277 ASN B ND2 1 
ATOM   5068 N  N   . GLY B 1 278 ? -10.669 15.261  -32.415 1.00 48.13  ? 278 GLY B N   1 
ATOM   5069 C  CA  . GLY B 1 278 ? -10.175 14.109  -33.192 1.00 47.32  ? 278 GLY B CA  1 
ATOM   5070 C  C   . GLY B 1 278 ? -8.703  13.821  -32.954 1.00 49.28  ? 278 GLY B C   1 
ATOM   5071 O  O   . GLY B 1 278 ? -8.099  13.105  -33.764 1.00 53.79  ? 278 GLY B O   1 
ATOM   5072 N  N   . ARG B 1 279 ? -8.113  14.345  -31.889 1.00 48.66  ? 279 ARG B N   1 
ATOM   5073 C  CA  . ARG B 1 279 ? -6.664  14.136  -31.638 1.00 51.48  ? 279 ARG B CA  1 
ATOM   5074 C  C   . ARG B 1 279 ? -6.484  13.156  -30.474 1.00 45.98  ? 279 ARG B C   1 
ATOM   5075 O  O   . ARG B 1 279 ? -7.483  12.655  -29.929 1.00 39.57  ? 279 ARG B O   1 
ATOM   5076 C  CB  . ARG B 1 279 ? -5.942  15.474  -31.440 1.00 58.62  ? 279 ARG B CB  1 
ATOM   5077 C  CG  . ARG B 1 279 ? -5.415  16.051  -32.747 1.00 63.63  ? 279 ARG B CG  1 
ATOM   5078 C  CD  . ARG B 1 279 ? -4.841  17.441  -32.635 1.00 66.97  ? 279 ARG B CD  1 
ATOM   5079 N  NE  . ARG B 1 279 ? -5.879  18.391  -32.259 1.00 78.71  ? 279 ARG B NE  1 
ATOM   5080 C  CZ  . ARG B 1 279 ? -5.910  19.677  -32.608 1.00 78.87  ? 279 ARG B CZ  1 
ATOM   5081 N  NH1 . ARG B 1 279 ? -4.961  20.198  -33.370 1.00 75.82  ? 279 ARG B NH1 1 
ATOM   5082 N  NH2 . ARG B 1 279 ? -6.908  20.439  -32.194 1.00 79.11  ? 279 ARG B NH2 1 
ATOM   5083 N  N   . THR B 1 280 ? -5.229  12.818  -30.193 1.00 42.55  ? 280 THR B N   1 
ATOM   5084 C  CA  . THR B 1 280 ? -4.827  12.008  -29.032 1.00 37.82  ? 280 THR B CA  1 
ATOM   5085 C  C   . THR B 1 280 ? -3.710  12.748  -28.303 1.00 35.29  ? 280 THR B C   1 
ATOM   5086 O  O   . THR B 1 280 ? -3.058  13.637  -28.883 1.00 33.16  ? 280 THR B O   1 
ATOM   5087 C  CB  . THR B 1 280 ? -4.349  10.610  -29.431 1.00 35.60  ? 280 THR B CB  1 
ATOM   5088 O  OG1 . THR B 1 280 ? -3.178  10.822  -30.211 1.00 36.32  ? 280 THR B OG1 1 
ATOM   5089 C  CG2 . THR B 1 280 ? -5.374  9.813   -30.202 1.00 37.50  ? 280 THR B CG2 1 
ATOM   5090 N  N   . ILE B 1 281 ? -3.511  12.344  -27.064 1.00 31.88  ? 281 ILE B N   1 
ATOM   5091 C  CA  . ILE B 1 281 ? -2.418  12.797  -26.182 1.00 30.48  ? 281 ILE B CA  1 
ATOM   5092 C  C   . ILE B 1 281 ? -1.805  11.525  -25.613 1.00 28.42  ? 281 ILE B C   1 
ATOM   5093 O  O   . ILE B 1 281 ? -2.516  10.792  -24.907 1.00 31.37  ? 281 ILE B O   1 
ATOM   5094 C  CB  . ILE B 1 281 ? -2.959  13.731  -25.083 1.00 31.76  ? 281 ILE B CB  1 
ATOM   5095 C  CG1 . ILE B 1 281 ? -3.667  14.962  -25.659 1.00 35.31  ? 281 ILE B CG1 1 
ATOM   5096 C  CG2 . ILE B 1 281 ? -1.846  14.111  -24.128 1.00 30.95  ? 281 ILE B CG2 1 
ATOM   5097 C  CD1 . ILE B 1 281 ? -4.438  15.766  -24.629 1.00 35.98  ? 281 ILE B CD1 1 
ATOM   5098 N  N   . LEU B 1 282 ? -0.536  11.287  -25.915 1.00 30.59  ? 282 LEU B N   1 
ATOM   5099 C  CA  . LEU B 1 282 ? 0.205   10.084  -25.479 1.00 32.64  ? 282 LEU B CA  1 
ATOM   5100 C  C   . LEU B 1 282 ? -0.623  8.841   -25.808 1.00 31.35  ? 282 LEU B C   1 
ATOM   5101 O  O   . LEU B 1 282 ? -0.765  8.026   -24.916 1.00 33.75  ? 282 LEU B O   1 
ATOM   5102 C  CB  . LEU B 1 282 ? 0.488   10.179  -23.972 1.00 32.16  ? 282 LEU B CB  1 
ATOM   5103 C  CG  . LEU B 1 282 ? 1.588   11.157  -23.573 1.00 33.56  ? 282 LEU B CG  1 
ATOM   5104 C  CD1 . LEU B 1 282 ? 1.736   11.262  -22.063 1.00 32.06  ? 282 LEU B CD1 1 
ATOM   5105 C  CD2 . LEU B 1 282 ? 2.918   10.780  -24.217 1.00 34.66  ? 282 LEU B CD2 1 
ATOM   5106 N  N   . GLY B 1 283 ? -1.172  8.741   -27.020 1.00 33.79  ? 283 GLY B N   1 
ATOM   5107 C  CA  . GLY B 1 283 ? -1.907  7.559   -27.531 1.00 35.76  ? 283 GLY B CA  1 
ATOM   5108 C  C   . GLY B 1 283 ? -3.180  7.253   -26.747 1.00 37.23  ? 283 GLY B C   1 
ATOM   5109 O  O   . GLY B 1 283 ? -3.597  6.069   -26.684 1.00 35.49  ? 283 GLY B O   1 
ATOM   5110 N  N   . SER B 1 284 ? -3.784  8.264   -26.126 1.00 35.08  ? 284 SER B N   1 
ATOM   5111 C  CA  . SER B 1 284 ? -5.117  8.130   -25.504 1.00 32.83  ? 284 SER B CA  1 
ATOM   5112 C  C   . SER B 1 284 ? -6.072  9.160   -26.109 1.00 33.88  ? 284 SER B C   1 
ATOM   5113 O  O   . SER B 1 284 ? -5.644  10.322  -26.395 1.00 29.90  ? 284 SER B O   1 
ATOM   5114 C  CB  . SER B 1 284 ? -5.023  8.274   -24.030 1.00 33.48  ? 284 SER B CB  1 
ATOM   5115 O  OG  . SER B 1 284 ? -6.309  8.196   -23.459 1.00 34.64  ? 284 SER B OG  1 
ATOM   5116 N  N   . ALA B 1 285 ? -7.330  8.761   -26.273 1.00 33.66  ? 285 ALA B N   1 
ATOM   5117 C  CA  . ALA B 1 285 ? -8.414  9.692   -26.653 1.00 39.28  ? 285 ALA B CA  1 
ATOM   5118 C  C   . ALA B 1 285 ? -9.120  10.219  -25.389 1.00 39.35  ? 285 ALA B C   1 
ATOM   5119 O  O   . ALA B 1 285 ? -9.959  11.134  -25.525 1.00 43.74  ? 285 ALA B O   1 
ATOM   5120 C  CB  . ALA B 1 285 ? -9.368  9.009   -27.612 1.00 41.55  ? 285 ALA B CB  1 
ATOM   5121 N  N   . LEU B 1 286 ? -8.808  9.679   -24.206 1.00 35.34  ? 286 LEU B N   1 
ATOM   5122 C  CA  . LEU B 1 286 ? -9.391  10.133  -22.913 1.00 35.25  ? 286 LEU B CA  1 
ATOM   5123 C  C   . LEU B 1 286 ? -8.361  10.955  -22.150 1.00 29.39  ? 286 LEU B C   1 
ATOM   5124 O  O   . LEU B 1 286 ? -7.188  10.863  -22.467 1.00 31.09  ? 286 LEU B O   1 
ATOM   5125 C  CB  . LEU B 1 286 ? -9.782  8.923   -22.067 1.00 37.86  ? 286 LEU B CB  1 
ATOM   5126 C  CG  . LEU B 1 286 ? -10.934 8.119   -22.631 1.00 39.44  ? 286 LEU B CG  1 
ATOM   5127 C  CD1 . LEU B 1 286 ? -11.078 6.796   -21.897 1.00 37.51  ? 286 LEU B CD1 1 
ATOM   5128 C  CD2 . LEU B 1 286 ? -12.211 8.947   -22.569 1.00 43.82  ? 286 LEU B CD2 1 
ATOM   5129 N  N   . LEU B 1 287 ? -8.814  11.693  -21.152 1.00 27.35  ? 287 LEU B N   1 
ATOM   5130 C  CA  . LEU B 1 287 ? -7.935  12.456  -20.241 1.00 32.38  ? 287 LEU B CA  1 
ATOM   5131 C  C   . LEU B 1 287 ? -7.518  11.512  -19.102 1.00 32.21  ? 287 LEU B C   1 
ATOM   5132 O  O   . LEU B 1 287 ? -8.331  11.273  -18.229 1.00 37.64  ? 287 LEU B O   1 
ATOM   5133 C  CB  . LEU B 1 287 ? -8.677  13.713  -19.767 1.00 30.92  ? 287 LEU B CB  1 
ATOM   5134 C  CG  . LEU B 1 287 ? -8.872  14.790  -20.844 1.00 33.52  ? 287 LEU B CG  1 
ATOM   5135 C  CD1 . LEU B 1 287 ? -9.616  16.010  -20.310 1.00 35.20  ? 287 LEU B CD1 1 
ATOM   5136 C  CD2 . LEU B 1 287 ? -7.551  15.224  -21.445 1.00 34.38  ? 287 LEU B CD2 1 
ATOM   5137 N  N   . GLU B 1 288 ? -6.302  10.968  -19.147 1.00 32.76  ? 288 GLU B N   1 
ATOM   5138 C  CA  . GLU B 1 288 ? -5.823  9.910   -18.207 1.00 35.09  ? 288 GLU B CA  1 
ATOM   5139 C  C   . GLU B 1 288 ? -5.549  10.511  -16.820 1.00 31.59  ? 288 GLU B C   1 
ATOM   5140 O  O   . GLU B 1 288 ? -4.814  11.515  -16.725 1.00 30.33  ? 288 GLU B O   1 
ATOM   5141 C  CB  . GLU B 1 288 ? -4.554  9.252   -18.758 1.00 42.54  ? 288 GLU B CB  1 
ATOM   5142 C  CG  . GLU B 1 288 ? -4.776  8.485   -20.057 1.00 45.89  ? 288 GLU B CG  1 
ATOM   5143 C  CD  . GLU B 1 288 ? -5.610  7.216   -19.947 1.00 49.41  ? 288 GLU B CD  1 
ATOM   5144 O  OE1 . GLU B 1 288 ? -5.570  6.556   -18.886 1.00 49.98  ? 288 GLU B OE1 1 
ATOM   5145 O  OE2 . GLU B 1 288 ? -6.269  6.867   -20.939 1.00 52.54  ? 288 GLU B OE2 1 
ATOM   5146 N  N   . ASP B 1 289 ? -6.085  9.899   -15.763 1.00 31.95  ? 289 ASP B N   1 
ATOM   5147 C  CA  . ASP B 1 289 ? -5.992  10.451  -14.384 1.00 29.40  ? 289 ASP B CA  1 
ATOM   5148 C  C   . ASP B 1 289 ? -5.372  9.436   -13.413 1.00 29.43  ? 289 ASP B C   1 
ATOM   5149 O  O   . ASP B 1 289 ? -5.507  9.654   -12.193 1.00 28.71  ? 289 ASP B O   1 
ATOM   5150 C  CB  . ASP B 1 289 ? -7.365  10.947  -13.921 1.00 30.92  ? 289 ASP B CB  1 
ATOM   5151 C  CG  . ASP B 1 289 ? -8.329  9.857   -13.490 1.00 30.35  ? 289 ASP B CG  1 
ATOM   5152 O  OD1 . ASP B 1 289 ? -8.101  8.667   -13.818 1.00 27.57  ? 289 ASP B OD1 1 
ATOM   5153 O  OD2 . ASP B 1 289 ? -9.298  10.204  -12.797 1.00 32.74  ? 289 ASP B OD2 1 
ATOM   5154 N  N   . GLU B 1 290 ? -4.684  8.392   -13.890 1.00 26.59  ? 290 GLU B N   1 
ATOM   5155 C  CA  . GLU B 1 290 ? -4.030  7.419   -12.977 1.00 27.16  ? 290 GLU B CA  1 
ATOM   5156 C  C   . GLU B 1 290 ? -2.495  7.548   -13.016 1.00 26.94  ? 290 GLU B C   1 
ATOM   5157 O  O   . GLU B 1 290 ? -1.809  6.551   -12.711 1.00 31.53  ? 290 GLU B O   1 
ATOM   5158 C  CB  . GLU B 1 290 ? -4.583  6.021   -13.248 1.00 27.99  ? 290 GLU B CB  1 
ATOM   5159 C  CG  . GLU B 1 290 ? -6.087  5.944   -13.005 1.00 30.93  ? 290 GLU B CG  1 
ATOM   5160 C  CD  . GLU B 1 290 ? -6.653  4.624   -12.488 1.00 30.91  ? 290 GLU B CD  1 
ATOM   5161 O  OE1 . GLU B 1 290 ? -5.950  3.597   -12.621 1.00 29.56  ? 290 GLU B OE1 1 
ATOM   5162 O  OE2 . GLU B 1 290 ? -7.823  4.620   -11.985 1.00 29.27  ? 290 GLU B OE2 1 
ATOM   5163 N  N   . PHE B 1 291 ? -1.961  8.738   -13.306 1.00 25.88  ? 291 PHE B N   1 
ATOM   5164 C  CA  . PHE B 1 291 ? -0.533  9.091   -13.085 1.00 25.71  ? 291 PHE B CA  1 
ATOM   5165 C  C   . PHE B 1 291 ? -0.469  10.301  -12.152 1.00 26.30  ? 291 PHE B C   1 
ATOM   5166 O  O   . PHE B 1 291 ? -1.056  11.346  -12.473 1.00 24.74  ? 291 PHE B O   1 
ATOM   5167 C  CB  . PHE B 1 291 ? 0.171   9.464   -14.385 1.00 26.85  ? 291 PHE B CB  1 
ATOM   5168 C  CG  . PHE B 1 291 ? 0.229   8.381   -15.431 1.00 28.17  ? 291 PHE B CG  1 
ATOM   5169 C  CD1 . PHE B 1 291 ? 1.251   7.455   -15.427 1.00 28.40  ? 291 PHE B CD1 1 
ATOM   5170 C  CD2 . PHE B 1 291 ? -0.698  8.328   -16.464 1.00 31.42  ? 291 PHE B CD2 1 
ATOM   5171 C  CE1 . PHE B 1 291 ? 1.344   6.498   -16.428 1.00 31.56  ? 291 PHE B CE1 1 
ATOM   5172 C  CE2 . PHE B 1 291 ? -0.609  7.363   -17.462 1.00 32.48  ? 291 PHE B CE2 1 
ATOM   5173 C  CZ  . PHE B 1 291 ? 0.409   6.442   -17.435 1.00 32.53  ? 291 PHE B CZ  1 
ATOM   5174 N  N   . THR B 1 292 ? 0.224   10.169  -11.023 1.00 28.13  ? 292 THR B N   1 
ATOM   5175 C  CA  . THR B 1 292 ? 0.475   11.290  -10.093 1.00 27.47  ? 292 THR B CA  1 
ATOM   5176 C  C   . THR B 1 292 ? 1.630   12.114  -10.637 1.00 28.57  ? 292 THR B C   1 
ATOM   5177 O  O   . THR B 1 292 ? 2.366   11.661  -11.516 1.00 32.26  ? 292 THR B O   1 
ATOM   5178 C  CB  . THR B 1 292 ? 0.766   10.803  -8.671  1.00 27.63  ? 292 THR B CB  1 
ATOM   5179 O  OG1 . THR B 1 292 ? 2.025   10.126  -8.708  1.00 26.35  ? 292 THR B OG1 1 
ATOM   5180 C  CG2 . THR B 1 292 ? -0.326  9.919   -8.123  1.00 26.67  ? 292 THR B CG2 1 
ATOM   5181 N  N   . PRO B 1 293 ? 1.809   13.353  -10.131 1.00 29.43  ? 293 PRO B N   1 
ATOM   5182 C  CA  . PRO B 1 293 ? 2.997   14.157  -10.428 1.00 28.66  ? 293 PRO B CA  1 
ATOM   5183 C  C   . PRO B 1 293 ? 4.284   13.387  -10.120 1.00 26.66  ? 293 PRO B C   1 
ATOM   5184 O  O   . PRO B 1 293 ? 5.224   13.415  -10.918 1.00 22.70  ? 293 PRO B O   1 
ATOM   5185 C  CB  . PRO B 1 293 ? 2.852   15.376  -9.513  1.00 27.87  ? 293 PRO B CB  1 
ATOM   5186 C  CG  . PRO B 1 293 ? 1.357   15.504  -9.335  1.00 30.45  ? 293 PRO B CG  1 
ATOM   5187 C  CD  . PRO B 1 293 ? 0.840   14.077  -9.295  1.00 30.53  ? 293 PRO B CD  1 
ATOM   5188 N  N   . PHE B 1 294 ? 4.295   12.684  -8.993  1.00 30.39  ? 294 PHE B N   1 
ATOM   5189 C  CA  . PHE B 1 294 ? 5.478   11.897  -8.596  1.00 34.86  ? 294 PHE B CA  1 
ATOM   5190 C  C   . PHE B 1 294 ? 5.672   10.808  -9.659  1.00 31.83  ? 294 PHE B C   1 
ATOM   5191 O  O   . PHE B 1 294 ? 6.782   10.681  -10.179 1.00 34.00  ? 294 PHE B O   1 
ATOM   5192 C  CB  . PHE B 1 294 ? 5.363   11.403  -7.159  1.00 41.39  ? 294 PHE B CB  1 
ATOM   5193 C  CG  . PHE B 1 294 ? 6.593   10.639  -6.768  1.00 54.15  ? 294 PHE B CG  1 
ATOM   5194 C  CD1 . PHE B 1 294 ? 7.698   11.270  -6.207  1.00 58.93  ? 294 PHE B CD1 1 
ATOM   5195 C  CD2 . PHE B 1 294 ? 6.690   9.296   -7.095  1.00 64.37  ? 294 PHE B CD2 1 
ATOM   5196 C  CE1 . PHE B 1 294 ? 8.851   10.555  -5.908  1.00 59.37  ? 294 PHE B CE1 1 
ATOM   5197 C  CE2 . PHE B 1 294 ? 7.837   8.589   -6.786  1.00 62.89  ? 294 PHE B CE2 1 
ATOM   5198 C  CZ  . PHE B 1 294 ? 8.917   9.212   -6.198  1.00 60.41  ? 294 PHE B CZ  1 
ATOM   5199 N  N   . ASP B 1 295 ? 4.608   10.108  -10.057 1.00 31.07  ? 295 ASP B N   1 
ATOM   5200 C  CA  . ASP B 1 295 ? 4.704   9.071   -11.122 1.00 31.78  ? 295 ASP B CA  1 
ATOM   5201 C  C   . ASP B 1 295 ? 5.434   9.646   -12.347 1.00 32.58  ? 295 ASP B C   1 
ATOM   5202 O  O   . ASP B 1 295 ? 6.344   8.974   -12.869 1.00 34.90  ? 295 ASP B O   1 
ATOM   5203 C  CB  . ASP B 1 295 ? 3.337   8.529   -11.520 1.00 30.45  ? 295 ASP B CB  1 
ATOM   5204 C  CG  . ASP B 1 295 ? 2.681   7.697   -10.438 1.00 30.24  ? 295 ASP B CG  1 
ATOM   5205 O  OD1 . ASP B 1 295 ? 3.403   7.300   -9.507  1.00 30.04  ? 295 ASP B OD1 1 
ATOM   5206 O  OD2 . ASP B 1 295 ? 1.462   7.470   -10.545 1.00 25.88  ? 295 ASP B OD2 1 
ATOM   5207 N  N   . VAL B 1 296 ? 5.062   10.845  -12.790 1.00 32.59  ? 296 VAL B N   1 
ATOM   5208 C  CA  . VAL B 1 296 ? 5.586   11.446  -14.050 1.00 33.44  ? 296 VAL B CA  1 
ATOM   5209 C  C   . VAL B 1 296 ? 7.054   11.849  -13.869 1.00 37.12  ? 296 VAL B C   1 
ATOM   5210 O  O   . VAL B 1 296 ? 7.890   11.565  -14.764 1.00 38.50  ? 296 VAL B O   1 
ATOM   5211 C  CB  . VAL B 1 296 ? 4.732   12.640  -14.494 1.00 32.35  ? 296 VAL B CB  1 
ATOM   5212 C  CG1 . VAL B 1 296 ? 5.363   13.341  -15.684 1.00 32.33  ? 296 VAL B CG1 1 
ATOM   5213 C  CG2 . VAL B 1 296 ? 3.311   12.196  -14.814 1.00 30.15  ? 296 VAL B CG2 1 
ATOM   5214 N  N   . VAL B 1 297 ? 7.363   12.491  -12.751 1.00 40.84  ? 297 VAL B N   1 
ATOM   5215 C  CA  . VAL B 1 297 ? 8.750   12.922  -12.430 1.00 42.32  ? 297 VAL B CA  1 
ATOM   5216 C  C   . VAL B 1 297 ? 9.630   11.664  -12.396 1.00 41.77  ? 297 VAL B C   1 
ATOM   5217 O  O   . VAL B 1 297 ? 10.723  11.696  -12.985 1.00 39.97  ? 297 VAL B O   1 
ATOM   5218 C  CB  . VAL B 1 297 ? 8.775   13.766  -11.134 1.00 44.37  ? 297 VAL B CB  1 
ATOM   5219 C  CG1 . VAL B 1 297 ? 10.128  13.766  -10.433 1.00 45.55  ? 297 VAL B CG1 1 
ATOM   5220 C  CG2 . VAL B 1 297 ? 8.324   15.194  -11.416 1.00 44.33  ? 297 VAL B CG2 1 
ATOM   5221 N  N   . ARG B 1 298 ? 9.178   10.584  -11.756 1.00 43.74  ? 298 ARG B N   1 
ATOM   5222 C  CA  . ARG B 1 298 ? 10.018  9.373   -11.527 1.00 46.91  ? 298 ARG B CA  1 
ATOM   5223 C  C   . ARG B 1 298 ? 10.285  8.656   -12.847 1.00 46.46  ? 298 ARG B C   1 
ATOM   5224 O  O   . ARG B 1 298 ? 11.427  8.186   -13.057 1.00 41.96  ? 298 ARG B O   1 
ATOM   5225 C  CB  . ARG B 1 298 ? 9.373   8.373   -10.568 1.00 57.15  ? 298 ARG B CB  1 
ATOM   5226 C  CG  . ARG B 1 298 ? 10.051  8.308   -9.206  1.00 75.14  ? 298 ARG B CG  1 
ATOM   5227 C  CD  . ARG B 1 298 ? 10.140  6.898   -8.631  1.00 87.36  ? 298 ARG B CD  1 
ATOM   5228 N  NE  . ARG B 1 298 ? 8.970   6.120   -8.999  1.00 90.48  ? 298 ARG B NE  1 
ATOM   5229 C  CZ  . ARG B 1 298 ? 7.940   5.834   -8.205  1.00 99.08  ? 298 ARG B CZ  1 
ATOM   5230 N  NH1 . ARG B 1 298 ? 7.912   6.200   -6.931  1.00 99.71  ? 298 ARG B NH1 1 
ATOM   5231 N  NH2 . ARG B 1 298 ? 6.932   5.140   -8.692  1.00 104.89 ? 298 ARG B NH2 1 
ATOM   5232 N  N   . GLN B 1 299 ? 9.254   8.535   -13.679 1.00 40.77  ? 299 GLN B N   1 
ATOM   5233 C  CA  . GLN B 1 299 ? 9.326   7.778   -14.952 1.00 40.89  ? 299 GLN B CA  1 
ATOM   5234 C  C   . GLN B 1 299 ? 10.206  8.551   -15.940 1.00 41.96  ? 299 GLN B C   1 
ATOM   5235 O  O   . GLN B 1 299 ? 10.974  7.899   -16.659 1.00 42.73  ? 299 GLN B O   1 
ATOM   5236 C  CB  . GLN B 1 299 ? 7.928   7.503   -15.526 1.00 36.50  ? 299 GLN B CB  1 
ATOM   5237 C  CG  . GLN B 1 299 ? 7.991   6.850   -16.902 1.00 35.63  ? 299 GLN B CG  1 
ATOM   5238 C  CD  . GLN B 1 299 ? 6.736   6.195   -17.424 1.00 32.53  ? 299 GLN B CD  1 
ATOM   5239 O  OE1 . GLN B 1 299 ? 6.704   5.765   -18.575 1.00 31.37  ? 299 GLN B OE1 1 
ATOM   5240 N  NE2 . GLN B 1 299 ? 5.694   6.127   -16.612 1.00 27.07  ? 299 GLN B NE2 1 
ATOM   5241 N  N   . CYS B 1 300 ? 10.117  9.884   -15.946 1.00 42.12  ? 300 CYS B N   1 
ATOM   5242 C  CA  . CYS B 1 300 ? 10.792  10.783  -16.923 1.00 45.03  ? 300 CYS B CA  1 
ATOM   5243 C  C   . CYS B 1 300 ? 12.238  11.098  -16.487 1.00 51.13  ? 300 CYS B C   1 
ATOM   5244 O  O   . CYS B 1 300 ? 12.948  11.715  -17.284 1.00 51.29  ? 300 CYS B O   1 
ATOM   5245 C  CB  . CYS B 1 300 ? 9.989   12.064  -17.105 1.00 43.33  ? 300 CYS B CB  1 
ATOM   5246 S  SG  . CYS B 1 300 ? 8.386   11.759  -17.884 1.00 44.13  ? 300 CYS B SG  1 
ATOM   5247 N  N   . SER B 1 301 ? 12.653  10.680  -15.279 1.00 56.17  ? 301 SER B N   1 
ATOM   5248 C  CA  . SER B 1 301 ? 14.001  10.896  -14.674 1.00 52.33  ? 301 SER B CA  1 
ATOM   5249 C  C   . SER B 1 301 ? 14.697  9.571   -14.323 1.00 51.10  ? 301 SER B C   1 
ATOM   5250 O  O   . SER B 1 301 ? 15.822  9.635   -13.828 1.00 53.81  ? 301 SER B O   1 
ATOM   5251 C  CB  . SER B 1 301 ? 13.892  11.769  -13.461 1.00 53.79  ? 301 SER B CB  1 
ATOM   5252 O  OG  . SER B 1 301 ? 13.355  13.028  -13.838 1.00 63.31  ? 301 SER B OG  1 
ATOM   5253 N  N   . GLY B 1 302 ? 14.041  8.426   -14.540 1.00 51.80  ? 302 GLY B N   1 
ATOM   5254 C  CA  . GLY B 1 302 ? 14.628  7.072   -14.470 1.00 46.68  ? 302 GLY B CA  1 
ATOM   5255 C  C   . GLY B 1 302 ? 14.979  6.630   -13.059 1.00 45.81  ? 302 GLY B C   1 
ATOM   5256 O  O   . GLY B 1 302 ? 15.942  5.863   -12.932 1.00 41.35  ? 302 GLY B O   1 
ATOM   5257 N  N   . VAL B 1 303 ? 14.226  7.045   -12.030 1.00 44.03  ? 303 VAL B N   1 
ATOM   5258 C  CA  . VAL B 1 303 ? 14.490  6.629   -10.614 1.00 44.35  ? 303 VAL B CA  1 
ATOM   5259 C  C   . VAL B 1 303 ? 14.409  5.092   -10.535 1.00 44.33  ? 303 VAL B C   1 
ATOM   5260 O  O   . VAL B 1 303 ? 13.592  4.461   -11.232 1.00 40.15  ? 303 VAL B O   1 
ATOM   5261 C  CB  . VAL B 1 303 ? 13.572  7.336   -9.590  1.00 46.61  ? 303 VAL B CB  1 
ATOM   5262 C  CG1 . VAL B 1 303 ? 13.461  6.578   -8.268  1.00 44.42  ? 303 VAL B CG1 1 
ATOM   5263 C  CG2 . VAL B 1 303 ? 14.015  8.771   -9.337  1.00 48.47  ? 303 VAL B CG2 1 
ATOM   5264 N  N   . THR B 1 304 ? 15.274  4.520   -9.708  1.00 42.63  ? 304 THR B N   1 
ATOM   5265 C  CA  . THR B 1 304 ? 15.629  3.084   -9.668  1.00 45.24  ? 304 THR B CA  1 
ATOM   5266 C  C   . THR B 1 304 ? 15.410  2.607   -8.219  1.00 48.28  ? 304 THR B C   1 
ATOM   5267 O  O   . THR B 1 304 ? 15.432  3.475   -7.313  1.00 48.97  ? 304 THR B O   1 
ATOM   5268 C  CB  . THR B 1 304 ? 17.052  2.987   -10.246 1.00 43.17  ? 304 THR B CB  1 
ATOM   5269 O  OG1 . THR B 1 304 ? 17.043  2.150   -11.403 1.00 38.41  ? 304 THR B OG1 1 
ATOM   5270 C  CG2 . THR B 1 304 ? 18.073  2.538   -9.225  1.00 41.57  ? 304 THR B CG2 1 
ATOM   5271 N  N   . PHE B 1 305 ? 15.231  1.299   -7.990  1.00 49.57  ? 305 PHE B N   1 
ATOM   5272 C  CA  . PHE B 1 305 ? 15.039  0.700   -6.633  1.00 52.49  ? 305 PHE B CA  1 
ATOM   5273 C  C   . PHE B 1 305 ? 16.127  -0.361  -6.397  1.00 54.90  ? 305 PHE B C   1 
ATOM   5274 O  O   . PHE B 1 305 ? 15.993  -1.471  -6.895  1.00 61.92  ? 305 PHE B O   1 
ATOM   5275 C  CB  . PHE B 1 305 ? 13.591  0.202   -6.487  1.00 47.82  ? 305 PHE B CB  1 
ATOM   5276 C  CG  . PHE B 1 305 ? 12.599  1.256   -6.909  1.00 45.38  ? 305 PHE B CG  1 
ATOM   5277 C  CD1 . PHE B 1 305 ? 12.279  2.315   -6.061  1.00 42.82  ? 305 PHE B CD1 1 
ATOM   5278 C  CD2 . PHE B 1 305 ? 12.113  1.275   -8.210  1.00 43.62  ? 305 PHE B CD2 1 
ATOM   5279 C  CE1 . PHE B 1 305 ? 11.430  3.326   -6.485  1.00 40.32  ? 305 PHE B CE1 1 
ATOM   5280 C  CE2 . PHE B 1 305 ? 11.286  2.303   -8.644  1.00 45.03  ? 305 PHE B CE2 1 
ATOM   5281 C  CZ  . PHE B 1 305 ? 10.937  3.320   -7.778  1.00 43.91  ? 305 PHE B CZ  1 
HETATM 5282 C  C4  C R9D C 2 .   ? 25.588  4.010   -29.534 0.25 33.72  ? 501 R9D A C4  1 
HETATM 5283 C  C4  D R9D C 2 .   ? 25.588  4.010   -29.534 0.25 33.72  ? 501 R9D A C4  1 
HETATM 5284 C  C5  C R9D C 2 .   ? 26.297  3.452   -30.640 0.25 33.11  ? 501 R9D A C5  1 
HETATM 5285 C  C5  D R9D C 2 .   ? 26.297  3.452   -30.640 0.25 33.11  ? 501 R9D A C5  1 
HETATM 5286 C  C6  C R9D C 2 .   ? 25.691  2.596   -31.557 0.25 31.17  ? 501 R9D A C6  1 
HETATM 5287 C  C6  D R9D C 2 .   ? 25.691  2.596   -31.557 0.25 31.17  ? 501 R9D A C6  1 
HETATM 5288 C  C7  C R9D C 2 .   ? 24.351  2.302   -31.353 0.25 32.06  ? 501 R9D A C7  1 
HETATM 5289 C  C7  D R9D C 2 .   ? 24.351  2.302   -31.353 0.25 32.06  ? 501 R9D A C7  1 
HETATM 5290 C  C8  C R9D C 2 .   ? 23.598  2.821   -30.307 0.25 31.94  ? 501 R9D A C8  1 
HETATM 5291 C  C8  D R9D C 2 .   ? 23.598  2.821   -30.307 0.25 31.94  ? 501 R9D A C8  1 
HETATM 5292 C  C9  C R9D C 2 .   ? 24.231  3.667   -29.421 0.25 32.08  ? 501 R9D A C9  1 
HETATM 5293 C  C9  D R9D C 2 .   ? 24.231  3.667   -29.421 0.25 32.08  ? 501 R9D A C9  1 
HETATM 5294 F  F   C R9D C 2 .   ? 23.725  1.472   -32.216 0.25 32.40  ? 501 R9D A F   1 
HETATM 5295 F  F   D R9D C 2 .   ? 23.725  1.472   -32.216 0.25 32.40  ? 501 R9D A F   1 
HETATM 5296 C  C3  C R9D C 2 .   ? 26.211  4.985   -28.504 0.25 35.06  ? 501 R9D A C3  1 
HETATM 5297 C  C3  D R9D C 2 .   ? 26.211  4.985   -28.504 0.25 35.06  ? 501 R9D A C3  1 
HETATM 5298 C  C2  C R9D C 2 .   ? 27.622  4.642   -27.869 0.25 36.97  ? 501 R9D A C2  1 
HETATM 5299 C  C2  D R9D C 2 .   ? 27.622  4.642   -27.869 0.25 36.97  ? 501 R9D A C2  1 
HETATM 5300 N  N   C R9D C 2 .   ? 28.234  5.979   -27.232 0.25 36.67  1 501 R9D A N   1 
HETATM 5301 N  N   D R9D C 2 .   ? 28.234  5.979   -27.232 0.25 36.67  1 501 R9D A N   1 
HETATM 5302 C  C1  C R9D C 2 .   ? 27.627  3.677   -26.659 0.25 37.81  ? 501 R9D A C1  1 
HETATM 5303 C  C1  D R9D C 2 .   ? 27.627  3.677   -26.659 0.25 37.81  ? 501 R9D A C1  1 
HETATM 5304 O  O1  C R9D C 2 .   ? 26.754  2.852   -26.480 0.25 35.93  ? 501 R9D A O1  1 
HETATM 5305 O  O1  D R9D C 2 .   ? 26.754  2.852   -26.480 0.25 35.93  ? 501 R9D A O1  1 
HETATM 5306 O  O   C R9D C 2 .   ? 28.658  3.823   -25.781 0.25 39.88  ? 501 R9D A O   1 
HETATM 5307 O  O   D R9D C 2 .   ? 28.658  3.823   -25.781 0.25 39.88  ? 501 R9D A O   1 
HETATM 5308 C  C   C R9D C 2 .   ? 29.933  3.250   -26.101 0.25 39.32  ? 501 R9D A C   1 
HETATM 5309 C  C   D R9D C 2 .   ? 29.933  3.250   -26.101 0.25 39.32  ? 501 R9D A C   1 
HETATM 5310 S  S   . DMS D 3 .   ? 17.017  4.939   -24.956 1.00 43.56  ? 502 DMS A S   1 
HETATM 5311 O  O   . DMS D 3 .   ? 16.412  4.308   -26.184 1.00 43.07  ? 502 DMS A O   1 
HETATM 5312 C  C1  . DMS D 3 .   ? 16.561  6.663   -24.966 1.00 41.35  ? 502 DMS A C1  1 
HETATM 5313 C  C2  . DMS D 3 .   ? 18.759  5.135   -25.289 1.00 44.41  ? 502 DMS A C2  1 
HETATM 5314 CL CL  . CL  E 4 .   ? 5.511   -14.988 -31.376 1.00 29.55  ? 503 CL  A CL  1 
HETATM 5315 CL CL  . CL  F 4 .   ? 4.754   -1.636  -28.471 1.00 48.15  ? 504 CL  A CL  1 
HETATM 5316 S  S   . DMS G 3 .   ? 6.369   4.169   -11.657 1.00 43.39  ? 401 DMS B S   1 
HETATM 5317 O  O   . DMS G 3 .   ? 7.545   3.244   -11.176 1.00 45.82  ? 401 DMS B O   1 
HETATM 5318 C  C1  . DMS G 3 .   ? 6.725   5.849   -11.227 1.00 47.89  ? 401 DMS B C1  1 
HETATM 5319 C  C2  . DMS G 3 .   ? 4.973   3.857   -10.582 1.00 44.77  ? 401 DMS B C2  1 
HETATM 5320 O  O   . HOH H 5 .   ? 29.059  -0.945  -38.015 1.00 36.40  ? 601 HOH A O   1 
HETATM 5321 O  O   . HOH H 5 .   ? -11.868 5.015   -37.905 1.00 30.15  ? 602 HOH A O   1 
HETATM 5322 O  O   . HOH H 5 .   ? -1.176  -14.924 -40.009 1.00 31.12  ? 603 HOH A O   1 
HETATM 5323 O  O   . HOH H 5 .   ? -8.411  2.091   -34.970 1.00 34.38  ? 604 HOH A O   1 
HETATM 5324 O  O   . HOH H 5 .   ? 29.947  -1.849  -14.143 1.00 32.38  ? 605 HOH A O   1 
HETATM 5325 O  O   . HOH H 5 .   ? 6.520   2.457   -34.473 1.00 36.88  ? 606 HOH A O   1 
HETATM 5326 O  O   . HOH H 5 .   ? 29.669  0.726   -42.424 1.00 23.94  ? 607 HOH A O   1 
HETATM 5327 O  O   . HOH H 5 .   ? -1.167  -11.202 -31.835 1.00 30.94  ? 608 HOH A O   1 
HETATM 5328 O  O   . HOH H 5 .   ? -18.801 -6.060  -48.703 1.00 29.42  ? 609 HOH A O   1 
HETATM 5329 O  O   . HOH H 5 .   ? -15.635 5.399   -43.019 1.00 37.81  ? 610 HOH A O   1 
HETATM 5330 O  O   . HOH H 5 .   ? -9.271  3.415   -32.431 1.00 33.86  ? 611 HOH A O   1 
HETATM 5331 O  O   . HOH H 5 .   ? -18.103 -10.202 -51.107 1.00 29.57  ? 612 HOH A O   1 
HETATM 5332 O  O   . HOH H 5 .   ? 1.112   -2.687  -24.271 1.00 30.53  ? 613 HOH A O   1 
HETATM 5333 O  O   . HOH H 5 .   ? 16.247  -14.032 -10.652 1.00 33.12  ? 614 HOH A O   1 
HETATM 5334 O  O   . HOH H 5 .   ? 26.492  -2.166  -37.054 1.00 30.99  ? 615 HOH A O   1 
HETATM 5335 O  O   . HOH H 5 .   ? 15.588  -5.660  -17.844 1.00 31.87  ? 616 HOH A O   1 
HETATM 5336 O  O   . HOH H 5 .   ? -15.741 -11.812 -50.627 1.00 30.86  ? 617 HOH A O   1 
HETATM 5337 O  O   . HOH H 5 .   ? -5.710  -5.458  -28.165 1.00 26.41  ? 618 HOH A O   1 
HETATM 5338 O  O   . HOH H 5 .   ? -15.499 0.841   -42.135 1.00 36.08  ? 619 HOH A O   1 
HETATM 5339 O  O   . HOH H 5 .   ? 22.538  -15.890 -27.197 1.00 30.27  ? 620 HOH A O   1 
HETATM 5340 O  O   . HOH H 5 .   ? 2.723   -10.604 -22.794 1.00 27.22  ? 621 HOH A O   1 
HETATM 5341 O  O   . HOH H 5 .   ? -14.885 -15.078 -45.977 1.00 39.62  ? 622 HOH A O   1 
HETATM 5342 O  O   . HOH H 5 .   ? 9.062   -13.147 -11.542 1.00 26.51  ? 623 HOH A O   1 
HETATM 5343 O  O   . HOH H 5 .   ? 24.726  -3.069  -30.129 1.00 22.94  ? 624 HOH A O   1 
HETATM 5344 O  O   . HOH H 5 .   ? -2.845  0.006   -28.544 1.00 42.92  ? 625 HOH A O   1 
HETATM 5345 O  O   . HOH H 5 .   ? 17.084  9.998   -22.048 1.00 43.67  ? 626 HOH A O   1 
HETATM 5346 O  O   . HOH H 5 .   ? -18.749 -9.213  -46.989 1.00 27.03  ? 627 HOH A O   1 
HETATM 5347 O  O   . HOH H 5 .   ? -0.579  -7.467  -23.134 1.00 30.64  ? 628 HOH A O   1 
HETATM 5348 O  O   . HOH H 5 .   ? 15.377  -5.624  -7.965  1.00 45.45  ? 629 HOH A O   1 
HETATM 5349 O  O   . HOH H 5 .   ? -13.282 -13.973 -47.978 1.00 36.85  ? 630 HOH A O   1 
HETATM 5350 O  O   . HOH H 5 .   ? 6.382   -17.520 -21.847 1.00 33.98  ? 631 HOH A O   1 
HETATM 5351 O  O   . HOH H 5 .   ? 32.866  -6.699  -37.196 1.00 31.70  ? 632 HOH A O   1 
HETATM 5352 O  O   . HOH H 5 .   ? 21.409  -5.580  -37.788 1.00 28.08  ? 633 HOH A O   1 
HETATM 5353 O  O   . HOH H 5 .   ? 20.860  -7.928  -36.547 1.00 22.91  ? 634 HOH A O   1 
HETATM 5354 O  O   . HOH H 5 .   ? 11.741  6.432   -36.799 1.00 33.52  ? 635 HOH A O   1 
HETATM 5355 O  O   . HOH H 5 .   ? -8.343  -11.366 -47.646 1.00 33.79  ? 636 HOH A O   1 
HETATM 5356 O  O   . HOH H 5 .   ? 13.750  -3.512  -33.282 1.00 28.23  ? 637 HOH A O   1 
HETATM 5357 O  O   . HOH H 5 .   ? -1.510  -7.534  -20.511 1.00 29.80  ? 638 HOH A O   1 
HETATM 5358 O  O   A HOH H 5 .   ? 33.040  3.026   -24.340 0.25 38.52  ? 639 HOH A O   1 
HETATM 5359 O  O   B HOH H 5 .   ? 33.040  3.026   -24.340 0.25 38.52  ? 639 HOH A O   1 
HETATM 5360 O  O   C HOH H 5 .   ? 32.946  1.748   -24.536 0.25 29.14  ? 639 HOH A O   1 
HETATM 5361 O  O   D HOH H 5 .   ? 32.946  1.748   -24.536 0.25 29.14  ? 639 HOH A O   1 
HETATM 5362 O  O   . HOH H 5 .   ? 3.630   -19.698 -23.743 1.00 29.91  ? 640 HOH A O   1 
HETATM 5363 O  O   . HOH H 5 .   ? 8.827   -14.032 -24.870 1.00 36.13  ? 641 HOH A O   1 
HETATM 5364 O  O   . HOH H 5 .   ? 15.376  -14.242 -27.858 1.00 33.56  ? 642 HOH A O   1 
HETATM 5365 O  O   . HOH H 5 .   ? -3.732  -8.898  -37.510 1.00 26.63  ? 643 HOH A O   1 
HETATM 5366 O  O   . HOH H 5 .   ? 12.789  -18.493 -31.330 1.00 34.97  ? 644 HOH A O   1 
HETATM 5367 O  O   . HOH H 5 .   ? -16.168 -16.596 -38.641 1.00 32.79  ? 645 HOH A O   1 
HETATM 5368 O  O   . HOH H 5 .   ? 7.702   4.933   -27.645 1.00 38.21  ? 646 HOH A O   1 
HETATM 5369 O  O   . HOH H 5 .   ? 23.520  -4.256  -37.033 1.00 21.90  ? 647 HOH A O   1 
HETATM 5370 O  O   . HOH H 5 .   ? -3.347  -17.726 -42.766 1.00 39.08  ? 648 HOH A O   1 
HETATM 5371 O  O   . HOH H 5 .   ? -8.537  -1.412  -22.635 1.00 32.94  ? 649 HOH A O   1 
HETATM 5372 O  O   . HOH H 5 .   ? 35.733  0.778   -35.569 1.00 32.99  ? 650 HOH A O   1 
HETATM 5373 O  O   . HOH H 5 .   ? -24.318 -9.214  -43.334 1.00 37.41  ? 651 HOH A O   1 
HETATM 5374 O  O   . HOH H 5 .   ? 19.431  5.533   -28.953 1.00 28.06  ? 652 HOH A O   1 
HETATM 5375 O  O   . HOH H 5 .   ? 21.912  3.161   -22.591 1.00 34.84  ? 653 HOH A O   1 
HETATM 5376 O  O   . HOH H 5 .   ? 31.139  -4.529  -37.603 1.00 31.37  ? 654 HOH A O   1 
HETATM 5377 O  O   . HOH H 5 .   ? -19.914 -7.519  -45.453 1.00 32.27  ? 655 HOH A O   1 
HETATM 5378 O  O   A HOH H 5 .   ? 21.605  4.059   -28.022 0.25 44.71  ? 656 HOH A O   1 
HETATM 5379 O  O   B HOH H 5 .   ? 21.605  4.059   -28.022 0.25 44.71  ? 656 HOH A O   1 
HETATM 5380 O  O   C HOH H 5 .   ? 21.335  3.795   -27.659 0.25 45.99  ? 656 HOH A O   1 
HETATM 5381 O  O   D HOH H 5 .   ? 21.335  3.795   -27.659 0.25 45.99  ? 656 HOH A O   1 
HETATM 5382 O  O   . HOH H 5 .   ? 16.051  -16.308 -29.698 1.00 34.10  ? 657 HOH A O   1 
HETATM 5383 O  O   . HOH H 5 .   ? -1.197  -8.513  -37.355 1.00 36.34  ? 658 HOH A O   1 
HETATM 5384 O  O   . HOH H 5 .   ? -17.507 -15.845 -45.393 1.00 41.71  ? 659 HOH A O   1 
HETATM 5385 O  O   A HOH H 5 .   ? 22.779  4.485   -25.823 0.25 42.76  ? 660 HOH A O   1 
HETATM 5386 O  O   B HOH H 5 .   ? 22.779  4.485   -25.823 0.25 42.76  ? 660 HOH A O   1 
HETATM 5387 O  O   C HOH H 5 .   ? 21.845  4.299   -24.539 0.25 42.63  ? 660 HOH A O   1 
HETATM 5388 O  O   D HOH H 5 .   ? 21.845  4.299   -24.539 0.25 42.63  ? 660 HOH A O   1 
HETATM 5389 O  O   . HOH H 5 .   ? -14.544 -17.790 -40.396 1.00 32.54  ? 661 HOH A O   1 
HETATM 5390 O  O   . HOH I 5 .   ? -1.723  26.238  -22.046 1.00 38.32  ? 501 HOH B O   1 
HETATM 5391 O  O   . HOH I 5 .   ? -11.997 -0.126  -1.320  1.00 26.33  ? 502 HOH B O   1 
HETATM 5392 O  O   . HOH I 5 .   ? -4.720  6.937   -16.522 1.00 33.19  ? 503 HOH B O   1 
HETATM 5393 O  O   . HOH I 5 .   ? -0.875  14.042  -30.618 1.00 48.10  ? 504 HOH B O   1 
HETATM 5394 O  O   . HOH I 5 .   ? -0.133  -9.600  -3.966  1.00 45.84  ? 505 HOH B O   1 
HETATM 5395 O  O   . HOH I 5 .   ? 1.015   5.473   -12.123 1.00 24.54  ? 506 HOH B O   1 
HETATM 5396 O  O   . HOH I 5 .   ? 14.743  10.226  -23.741 1.00 41.97  ? 507 HOH B O   1 
HETATM 5397 O  O   . HOH I 5 .   ? -14.570 2.405   5.476   1.00 33.78  ? 508 HOH B O   1 
HETATM 5398 O  O   . HOH I 5 .   ? 2.875   8.498   -6.870  1.00 32.10  ? 509 HOH B O   1 
HETATM 5399 O  O   . HOH I 5 .   ? 2.670   4.424   -7.813  1.00 33.13  ? 510 HOH B O   1 
HETATM 5400 O  O   . HOH I 5 .   ? -20.935 -1.060  -7.949  1.00 38.62  ? 511 HOH B O   1 
HETATM 5401 O  O   . HOH I 5 .   ? -3.668  2.712   -13.623 1.00 31.48  ? 512 HOH B O   1 
HETATM 5402 O  O   . HOH I 5 .   ? -8.045  2.408   -10.325 1.00 27.24  ? 513 HOH B O   1 
HETATM 5403 O  O   . HOH I 5 .   ? -2.577  12.587  -6.958  1.00 37.85  ? 514 HOH B O   1 
HETATM 5404 O  O   . HOH I 5 .   ? -12.514 -7.247  13.576  1.00 31.42  ? 515 HOH B O   1 
HETATM 5405 O  O   . HOH I 5 .   ? -2.924  11.051  -14.884 1.00 24.31  ? 516 HOH B O   1 
HETATM 5406 O  O   . HOH I 5 .   ? 10.770  8.362   -21.304 1.00 39.47  ? 517 HOH B O   1 
HETATM 5407 O  O   . HOH I 5 .   ? 11.011  -10.848 -0.907  1.00 45.82  ? 518 HOH B O   1 
HETATM 5408 O  O   . HOH I 5 .   ? -12.677 -9.927  5.019   1.00 25.66  ? 519 HOH B O   1 
HETATM 5409 O  O   . HOH I 5 .   ? -1.172  8.000   -22.212 1.00 38.62  ? 520 HOH B O   1 
HETATM 5410 O  O   . HOH I 5 .   ? -1.597  -0.497  5.061   1.00 29.42  ? 521 HOH B O   1 
HETATM 5411 O  O   . HOH I 5 .   ? 10.911  -5.631  -6.048  1.00 40.35  ? 522 HOH B O   1 
HETATM 5412 O  O   . HOH I 5 .   ? 5.237   6.329   -13.852 1.00 31.90  ? 523 HOH B O   1 
HETATM 5413 O  O   . HOH I 5 .   ? -15.826 3.015   -9.377  1.00 38.03  ? 524 HOH B O   1 
HETATM 5414 O  O   . HOH I 5 .   ? -12.277 5.385   3.320   1.00 26.33  ? 525 HOH B O   1 
HETATM 5415 O  O   . HOH I 5 .   ? 3.094   4.525   -13.780 1.00 23.96  ? 526 HOH B O   1 
HETATM 5416 O  O   . HOH I 5 .   ? 10.816  -3.882  7.673   1.00 27.72  ? 527 HOH B O   1 
HETATM 5417 O  O   . HOH I 5 .   ? -7.192  16.868  -8.012  1.00 35.45  ? 528 HOH B O   1 
HETATM 5418 O  O   . HOH I 5 .   ? -10.723 -14.868 -3.706  1.00 32.36  ? 529 HOH B O   1 
HETATM 5419 O  O   . HOH I 5 .   ? 0.976   7.576   -5.018  1.00 33.52  ? 530 HOH B O   1 
HETATM 5420 O  O   . HOH I 5 .   ? 4.766   7.314   -25.383 1.00 33.79  ? 531 HOH B O   1 
HETATM 5421 O  O   . HOH I 5 .   ? -8.310  6.132   -25.135 1.00 29.66  ? 532 HOH B O   1 
HETATM 5422 O  O   . HOH I 5 .   ? -19.222 -7.663  7.773   1.00 33.12  ? 533 HOH B O   1 
HETATM 5423 O  O   . HOH I 5 .   ? -16.498 -4.373  7.371   1.00 32.92  ? 534 HOH B O   1 
HETATM 5424 O  O   . HOH I 5 .   ? -7.160  14.988  -6.293  1.00 41.26  ? 535 HOH B O   1 
# 
