data_9IVB
# 
_entry.id   9IVB 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9IVB         pdb_00009ivb 10.2210/pdb9ivb/pdb 
WWPDB D_1300049722 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2025-01-22 
2 'Structure model' 1 1 2025-02-12 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9IVB 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yonghenc@163.com 
_pdbx_contact_author.name_first         Yongheng 
_pdbx_contact_author.name_last          Chen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8139-6892 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lin, H.'    1 ? 
'Chen, Y.H.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                134 
_citation.page_last                 134 
_citation.title                     
'Characterization of Bozitinib as a potential therapeutic agent for MET-amplified gastric cancer.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-07490-5 
_citation.pdbx_database_id_PubMed   39875456 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lin, H.'   1 ? 
primary 'Qu, L.'    2 ? 
primary 'Wei, H.'   3 ? 
primary 'Guo, M.'   4 ? 
primary 'Chen, X.'  5 ? 
primary 'Lin, Q.'   6 ? 
primary 'Zhang, H.' 7 ? 
primary 'Dai, S.'   8 ? 
primary 'Chen, Y.'  9 ? 
# 
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 'Hepatocyte growth factor receptor' 34842.320 2  2.7.10.1 ? 'kinase domain' ? 
2 non-polymer syn bozitinib                           424.382   2  ?        ? ?               ? 
3 water       nat water                               18.015    72 ?        ? ?               ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'HGF receptor,HGF/SF receptor,Proto-oncogene c-Met,Scatter factor receptor,SF receptor,Tyrosine-protein kinase Met' 
# 
_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       
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_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 bozitinib A1L3A 
3 water     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ASP n 
1 3   SER n 
1 4   ASP n 
1 5   ILE n 
1 6   SER n 
1 7   SER n 
1 8   PRO n 
1 9   LEU n 
1 10  LEU n 
1 11  GLN n 
1 12  ASN n 
1 13  THR n 
1 14  VAL n 
1 15  HIS n 
1 16  ILE n 
1 17  ASP n 
1 18  LEU n 
1 19  SER n 
1 20  ALA n 
1 21  LEU n 
1 22  ASN n 
1 23  PRO n 
1 24  GLU n 
1 25  LEU n 
1 26  VAL n 
1 27  GLN n 
1 28  ALA n 
1 29  VAL n 
1 30  GLN n 
1 31  HIS n 
1 32  VAL n 
1 33  VAL n 
1 34  ILE n 
1 35  GLY n 
1 36  PRO n 
1 37  SER n 
1 38  SER n 
1 39  LEU n 
1 40  ILE n 
1 41  VAL n 
1 42  HIS n 
1 43  PHE n 
1 44  ASN n 
1 45  GLU n 
1 46  VAL n 
1 47  ILE n 
1 48  GLY n 
1 49  ARG n 
1 50  GLY n 
1 51  HIS n 
1 52  PHE n 
1 53  GLY n 
1 54  CYS n 
1 55  VAL n 
1 56  TYR n 
1 57  HIS n 
1 58  GLY n 
1 59  THR n 
1 60  LEU n 
1 61  LEU n 
1 62  ASP n 
1 63  ASN n 
1 64  ASP n 
1 65  GLY n 
1 66  LYS n 
1 67  LYS n 
1 68  ILE n 
1 69  HIS n 
1 70  CYS n 
1 71  ALA n 
1 72  VAL n 
1 73  LYS n 
1 74  SER n 
1 75  LEU n 
1 76  ASN n 
1 77  ARG n 
1 78  ILE n 
1 79  THR n 
1 80  ASP n 
1 81  ILE n 
1 82  GLY n 
1 83  GLU n 
1 84  VAL n 
1 85  SER n 
1 86  GLN n 
1 87  PHE n 
1 88  LEU n 
1 89  THR n 
1 90  GLU n 
1 91  GLY n 
1 92  ILE n 
1 93  ILE n 
1 94  MET n 
1 95  LYS n 
1 96  ASP n 
1 97  PHE n 
1 98  SER n 
1 99  HIS n 
1 100 PRO n 
1 101 ASN n 
1 102 VAL n 
1 103 LEU n 
1 104 SER n 
1 105 LEU n 
1 106 LEU n 
1 107 GLY n 
1 108 ILE n 
1 109 CYS n 
1 110 LEU n 
1 111 ARG n 
1 112 SER n 
1 113 GLU n 
1 114 GLY n 
1 115 SER n 
1 116 PRO n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 LEU n 
1 121 PRO n 
1 122 TYR n 
1 123 MET n 
1 124 LYS n 
1 125 HIS n 
1 126 GLY n 
1 127 ASP n 
1 128 LEU n 
1 129 ARG n 
1 130 ASN n 
1 131 PHE n 
1 132 ILE n 
1 133 ARG n 
1 134 ASN n 
1 135 GLU n 
1 136 THR n 
1 137 HIS n 
1 138 ASN n 
1 139 PRO n 
1 140 THR n 
1 141 VAL n 
1 142 LYS n 
1 143 ASP n 
1 144 LEU n 
1 145 ILE n 
1 146 GLY n 
1 147 PHE n 
1 148 GLY n 
1 149 LEU n 
1 150 GLN n 
1 151 VAL n 
1 152 ALA n 
1 153 LYS n 
1 154 GLY n 
1 155 MET n 
1 156 LYS n 
1 157 TYR n 
1 158 LEU n 
1 159 ALA n 
1 160 SER n 
1 161 LYS n 
1 162 LYS n 
1 163 PHE n 
1 164 VAL n 
1 165 HIS n 
1 166 ARG n 
1 167 ASP n 
1 168 LEU n 
1 169 ALA n 
1 170 ALA n 
1 171 ARG n 
1 172 ASN n 
1 173 CYS n 
1 174 MET n 
1 175 LEU n 
1 176 ASP n 
1 177 GLU n 
1 178 LYS n 
1 179 PHE n 
1 180 THR n 
1 181 VAL n 
1 182 LYS n 
1 183 VAL n 
1 184 ALA n 
1 185 ASP n 
1 186 PHE n 
1 187 GLY n 
1 188 LEU n 
1 189 ALA n 
1 190 ARG n 
1 191 ASP n 
1 192 MET n 
1 193 TYR n 
1 194 ASP n 
1 195 LYS n 
1 196 GLU n 
1 197 TYR n 
1 198 TYR n 
1 199 SER n 
1 200 VAL n 
1 201 HIS n 
1 202 ASN n 
1 203 LYS n 
1 204 THR n 
1 205 GLY n 
1 206 ALA n 
1 207 LYS n 
1 208 LEU n 
1 209 PRO n 
1 210 VAL n 
1 211 LYS n 
1 212 TRP n 
1 213 MET n 
1 214 ALA n 
1 215 LEU n 
1 216 GLU n 
1 217 SER n 
1 218 LEU n 
1 219 GLN n 
1 220 THR n 
1 221 GLN n 
1 222 LYS n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 LYS n 
1 227 SER n 
1 228 ASP n 
1 229 VAL n 
1 230 TRP n 
1 231 SER n 
1 232 PHE n 
1 233 GLY n 
1 234 VAL n 
1 235 LEU n 
1 236 LEU n 
1 237 TRP n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 THR n 
1 242 ARG n 
1 243 GLY n 
1 244 ALA n 
1 245 PRO n 
1 246 PRO n 
1 247 TYR n 
1 248 PRO n 
1 249 ASP n 
1 250 VAL n 
1 251 ASN n 
1 252 THR n 
1 253 PHE n 
1 254 ASP n 
1 255 ILE n 
1 256 THR n 
1 257 VAL n 
1 258 TYR n 
1 259 LEU n 
1 260 LEU n 
1 261 GLN n 
1 262 GLY n 
1 263 ARG n 
1 264 ARG n 
1 265 LEU n 
1 266 LEU n 
1 267 GLN n 
1 268 PRO n 
1 269 GLU n 
1 270 TYR n 
1 271 CYS n 
1 272 PRO n 
1 273 ASP n 
1 274 PRO n 
1 275 LEU n 
1 276 TYR n 
1 277 GLU n 
1 278 VAL n 
1 279 MET n 
1 280 LEU n 
1 281 LYS n 
1 282 CYS n 
1 283 TRP n 
1 284 HIS n 
1 285 PRO n 
1 286 LYS n 
1 287 ALA n 
1 288 GLU n 
1 289 MET n 
1 290 ARG n 
1 291 PRO n 
1 292 SER n 
1 293 PHE n 
1 294 SER n 
1 295 GLU n 
1 296 LEU n 
1 297 VAL n 
1 298 SER n 
1 299 ARG n 
1 300 ILE n 
1 301 SER n 
1 302 ALA n 
1 303 ILE n 
1 304 PHE n 
1 305 SER n 
1 306 THR n 
1 307 PHE n 
1 308 ILE n 
1 309 GLY 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                   309 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MET 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L3A non-polymer         . bozitinib       
;9-[bis(fluoranyl)-(6-fluoranyl-2-methyl-indazol-5-yl)methyl]-3-(1-cyclopropylpyrazol-4-yl)-1$l^{4},2,7,8-tetrazabicyclo[4.3.0]nona-1,3,5,8-tetraene; Vebreltinib
;
'C20 H15 F3 N8'  424.382 
ALA   'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER           ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1038 ?    ?   ?   A . n 
A 1 2   ASP 2   1039 ?    ?   ?   A . n 
A 1 3   SER 3   1040 1040 SER SER A . n 
A 1 4   ASP 4   1041 1041 ASP ASP A . n 
A 1 5   ILE 5   1042 1042 ILE ILE A . n 
A 1 6   SER 6   1043 1043 SER SER A . n 
A 1 7   SER 7   1044 1044 SER SER A . n 
A 1 8   PRO 8   1045 1045 PRO PRO A . n 
A 1 9   LEU 9   1046 1046 LEU LEU A . n 
A 1 10  LEU 10  1047 1047 LEU LEU A . n 
A 1 11  GLN 11  1048 1048 GLN GLN A . n 
A 1 12  ASN 12  1049 1049 ASN ASN A . n 
A 1 13  THR 13  1050 1050 THR THR A . n 
A 1 14  VAL 14  1051 1051 VAL VAL A . n 
A 1 15  HIS 15  1052 1052 HIS HIS A . n 
A 1 16  ILE 16  1053 1053 ILE ILE A . n 
A 1 17  ASP 17  1054 1054 ASP ASP A . n 
A 1 18  LEU 18  1055 1055 LEU LEU A . n 
A 1 19  SER 19  1056 1056 SER SER A . n 
A 1 20  ALA 20  1057 1057 ALA ALA A . n 
A 1 21  LEU 21  1058 1058 LEU LEU A . n 
A 1 22  ASN 22  1059 1059 ASN ASN A . n 
A 1 23  PRO 23  1060 1060 PRO PRO A . n 
A 1 24  GLU 24  1061 1061 GLU GLU A . n 
A 1 25  LEU 25  1062 1062 LEU LEU A . n 
A 1 26  VAL 26  1063 1063 VAL VAL A . n 
A 1 27  GLN 27  1064 1064 GLN GLN A . n 
A 1 28  ALA 28  1065 1065 ALA ALA A . n 
A 1 29  VAL 29  1066 1066 VAL VAL A . n 
A 1 30  GLN 30  1067 1067 GLN GLN A . n 
A 1 31  HIS 31  1068 1068 HIS HIS A . n 
A 1 32  VAL 32  1069 1069 VAL VAL A . n 
A 1 33  VAL 33  1070 1070 VAL VAL A . n 
A 1 34  ILE 34  1071 1071 ILE ILE A . n 
A 1 35  GLY 35  1072 1072 GLY GLY A . n 
A 1 36  PRO 36  1073 1073 PRO PRO A . n 
A 1 37  SER 37  1074 1074 SER SER A . n 
A 1 38  SER 38  1075 1075 SER SER A . n 
A 1 39  LEU 39  1076 1076 LEU LEU A . n 
A 1 40  ILE 40  1077 1077 ILE ILE A . n 
A 1 41  VAL 41  1078 1078 VAL VAL A . n 
A 1 42  HIS 42  1079 1079 HIS HIS A . n 
A 1 43  PHE 43  1080 1080 PHE PHE A . n 
A 1 44  ASN 44  1081 1081 ASN ASN A . n 
A 1 45  GLU 45  1082 1082 GLU GLU A . n 
A 1 46  VAL 46  1083 1083 VAL VAL A . n 
A 1 47  ILE 47  1084 1084 ILE ILE A . n 
A 1 48  GLY 48  1085 1085 GLY GLY A . n 
A 1 49  ARG 49  1086 1086 ARG ARG A . n 
A 1 50  GLY 50  1087 1087 GLY GLY A . n 
A 1 51  HIS 51  1088 1088 HIS HIS A . n 
A 1 52  PHE 52  1089 1089 PHE PHE A . n 
A 1 53  GLY 53  1090 1090 GLY GLY A . n 
A 1 54  CYS 54  1091 1091 CYS CYS A . n 
A 1 55  VAL 55  1092 1092 VAL VAL A . n 
A 1 56  TYR 56  1093 1093 TYR TYR A . n 
A 1 57  HIS 57  1094 1094 HIS HIS A . n 
A 1 58  GLY 58  1095 1095 GLY GLY A . n 
A 1 59  THR 59  1096 1096 THR THR A . n 
A 1 60  LEU 60  1097 1097 LEU LEU A . n 
A 1 61  LEU 61  1098 1098 LEU LEU A . n 
A 1 62  ASP 62  1099 1099 ASP ASP A . n 
A 1 63  ASN 63  1100 1100 ASN ASN A . n 
A 1 64  ASP 64  1101 1101 ASP ASP A . n 
A 1 65  GLY 65  1102 1102 GLY GLY A . n 
A 1 66  LYS 66  1103 1103 LYS LYS A . n 
A 1 67  LYS 67  1104 1104 LYS LYS A . n 
A 1 68  ILE 68  1105 1105 ILE ILE A . n 
A 1 69  HIS 69  1106 1106 HIS HIS A . n 
A 1 70  CYS 70  1107 1107 CYS CYS A . n 
A 1 71  ALA 71  1108 1108 ALA ALA A . n 
A 1 72  VAL 72  1109 1109 VAL VAL A . n 
A 1 73  LYS 73  1110 1110 LYS LYS A . n 
A 1 74  SER 74  1111 1111 SER SER A . n 
A 1 75  LEU 75  1112 1112 LEU LEU A . n 
A 1 76  ASN 76  1113 1113 ASN ASN A . n 
A 1 77  ARG 77  1114 1114 ARG ARG A . n 
A 1 78  ILE 78  1115 1115 ILE ILE A . n 
A 1 79  THR 79  1116 1116 THR THR A . n 
A 1 80  ASP 80  1117 1117 ASP ASP A . n 
A 1 81  ILE 81  1118 1118 ILE ILE A . n 
A 1 82  GLY 82  1119 1119 GLY GLY A . n 
A 1 83  GLU 83  1120 1120 GLU GLU A . n 
A 1 84  VAL 84  1121 1121 VAL VAL A . n 
A 1 85  SER 85  1122 1122 SER SER A . n 
A 1 86  GLN 86  1123 1123 GLN GLN A . n 
A 1 87  PHE 87  1124 1124 PHE PHE A . n 
A 1 88  LEU 88  1125 1125 LEU LEU A . n 
A 1 89  THR 89  1126 1126 THR THR A . n 
A 1 90  GLU 90  1127 1127 GLU GLU A . n 
A 1 91  GLY 91  1128 1128 GLY GLY A . n 
A 1 92  ILE 92  1129 1129 ILE ILE A . n 
A 1 93  ILE 93  1130 1130 ILE ILE A . n 
A 1 94  MET 94  1131 1131 MET MET A . n 
A 1 95  LYS 95  1132 1132 LYS LYS A . n 
A 1 96  ASP 96  1133 1133 ASP ASP A . n 
A 1 97  PHE 97  1134 1134 PHE PHE A . n 
A 1 98  SER 98  1135 1135 SER SER A . n 
A 1 99  HIS 99  1136 1136 HIS HIS A . n 
A 1 100 PRO 100 1137 1137 PRO PRO A . n 
A 1 101 ASN 101 1138 1138 ASN ASN A . n 
A 1 102 VAL 102 1139 1139 VAL VAL A . n 
A 1 103 LEU 103 1140 1140 LEU LEU A . n 
A 1 104 SER 104 1141 1141 SER SER A . n 
A 1 105 LEU 105 1142 1142 LEU LEU A . n 
A 1 106 LEU 106 1143 1143 LEU LEU A . n 
A 1 107 GLY 107 1144 1144 GLY GLY A . n 
A 1 108 ILE 108 1145 1145 ILE ILE A . n 
A 1 109 CYS 109 1146 1146 CYS CYS A . n 
A 1 110 LEU 110 1147 1147 LEU LEU A . n 
A 1 111 ARG 111 1148 ?    ?   ?   A . n 
A 1 112 SER 112 1149 ?    ?   ?   A . n 
A 1 113 GLU 113 1150 ?    ?   ?   A . n 
A 1 114 GLY 114 1151 1151 GLY GLY A . n 
A 1 115 SER 115 1152 1152 SER SER A . n 
A 1 116 PRO 116 1153 1153 PRO PRO A . n 
A 1 117 LEU 117 1154 1154 LEU LEU A . n 
A 1 118 VAL 118 1155 1155 VAL VAL A . n 
A 1 119 VAL 119 1156 1156 VAL VAL A . n 
A 1 120 LEU 120 1157 1157 LEU LEU A . n 
A 1 121 PRO 121 1158 1158 PRO PRO A . n 
A 1 122 TYR 122 1159 1159 TYR TYR A . n 
A 1 123 MET 123 1160 1160 MET MET A . n 
A 1 124 LYS 124 1161 1161 LYS LYS A . n 
A 1 125 HIS 125 1162 1162 HIS HIS A . n 
A 1 126 GLY 126 1163 1163 GLY GLY A . n 
A 1 127 ASP 127 1164 1164 ASP ASP A . n 
A 1 128 LEU 128 1165 1165 LEU LEU A . n 
A 1 129 ARG 129 1166 1166 ARG ARG A . n 
A 1 130 ASN 130 1167 1167 ASN ASN A . n 
A 1 131 PHE 131 1168 1168 PHE PHE A . n 
A 1 132 ILE 132 1169 1169 ILE ILE A . n 
A 1 133 ARG 133 1170 1170 ARG ARG A . n 
A 1 134 ASN 134 1171 1171 ASN ASN A . n 
A 1 135 GLU 135 1172 1172 GLU GLU A . n 
A 1 136 THR 136 1173 1173 THR THR A . n 
A 1 137 HIS 137 1174 1174 HIS HIS A . n 
A 1 138 ASN 138 1175 1175 ASN ASN A . n 
A 1 139 PRO 139 1176 1176 PRO PRO A . n 
A 1 140 THR 140 1177 1177 THR THR A . n 
A 1 141 VAL 141 1178 1178 VAL VAL A . n 
A 1 142 LYS 142 1179 1179 LYS LYS A . n 
A 1 143 ASP 143 1180 1180 ASP ASP A . n 
A 1 144 LEU 144 1181 1181 LEU LEU A . n 
A 1 145 ILE 145 1182 1182 ILE ILE A . n 
A 1 146 GLY 146 1183 1183 GLY GLY A . n 
A 1 147 PHE 147 1184 1184 PHE PHE A . n 
A 1 148 GLY 148 1185 1185 GLY GLY A . n 
A 1 149 LEU 149 1186 1186 LEU LEU A . n 
A 1 150 GLN 150 1187 1187 GLN GLN A . n 
A 1 151 VAL 151 1188 1188 VAL VAL A . n 
A 1 152 ALA 152 1189 1189 ALA ALA A . n 
A 1 153 LYS 153 1190 1190 LYS LYS A . n 
A 1 154 GLY 154 1191 1191 GLY GLY A . n 
A 1 155 MET 155 1192 1192 MET MET A . n 
A 1 156 LYS 156 1193 1193 LYS LYS A . n 
A 1 157 TYR 157 1194 1194 TYR TYR A . n 
A 1 158 LEU 158 1195 1195 LEU LEU A . n 
A 1 159 ALA 159 1196 1196 ALA ALA A . n 
A 1 160 SER 160 1197 1197 SER SER A . n 
A 1 161 LYS 161 1198 1198 LYS LYS A . n 
A 1 162 LYS 162 1199 1199 LYS LYS A . n 
A 1 163 PHE 163 1200 1200 PHE PHE A . n 
A 1 164 VAL 164 1201 1201 VAL VAL A . n 
A 1 165 HIS 165 1202 1202 HIS HIS A . n 
A 1 166 ARG 166 1203 1203 ARG ARG A . n 
A 1 167 ASP 167 1204 1204 ASP ASP A . n 
A 1 168 LEU 168 1205 1205 LEU LEU A . n 
A 1 169 ALA 169 1206 1206 ALA ALA A . n 
A 1 170 ALA 170 1207 1207 ALA ALA A . n 
A 1 171 ARG 171 1208 1208 ARG ARG A . n 
A 1 172 ASN 172 1209 1209 ASN ASN A . n 
A 1 173 CYS 173 1210 1210 CYS CYS A . n 
A 1 174 MET 174 1211 1211 MET MET A . n 
A 1 175 LEU 175 1212 1212 LEU LEU A . n 
A 1 176 ASP 176 1213 1213 ASP ASP A . n 
A 1 177 GLU 177 1214 1214 GLU GLU A . n 
A 1 178 LYS 178 1215 1215 LYS LYS A . n 
A 1 179 PHE 179 1216 1216 PHE PHE A . n 
A 1 180 THR 180 1217 1217 THR THR A . n 
A 1 181 VAL 181 1218 1218 VAL VAL A . n 
A 1 182 LYS 182 1219 1219 LYS LYS A . n 
A 1 183 VAL 183 1220 1220 VAL VAL A . n 
A 1 184 ALA 184 1221 1221 ALA ALA A . n 
A 1 185 ASP 185 1222 1222 ASP ASP A . n 
A 1 186 PHE 186 1223 1223 PHE PHE A . n 
A 1 187 GLY 187 1224 1224 GLY GLY A . n 
A 1 188 LEU 188 1225 1225 LEU LEU A . n 
A 1 189 ALA 189 1226 1226 ALA ALA A . n 
A 1 190 ARG 190 1227 1227 ARG ARG A . n 
A 1 191 ASP 191 1228 1228 ASP ASP A . n 
A 1 192 MET 192 1229 1229 MET MET A . n 
A 1 193 TYR 193 1230 1230 TYR TYR A . n 
A 1 194 ASP 194 1231 1231 ASP ASP A . n 
A 1 195 LYS 195 1232 1232 LYS LYS A . n 
A 1 196 GLU 196 1233 1233 GLU GLU A . n 
A 1 197 TYR 197 1234 1234 TYR TYR A . n 
A 1 198 TYR 198 1235 1235 TYR TYR A . n 
A 1 199 SER 199 1236 1236 SER SER A . n 
A 1 200 VAL 200 1237 1237 VAL VAL A . n 
A 1 201 HIS 201 1238 1238 HIS HIS A . n 
A 1 202 ASN 202 1239 1239 ASN ASN A . n 
A 1 203 LYS 203 1240 1240 LYS LYS A . n 
A 1 204 THR 204 1241 1241 THR THR A . n 
A 1 205 GLY 205 1242 1242 GLY GLY A . n 
A 1 206 ALA 206 1243 1243 ALA ALA A . n 
A 1 207 LYS 207 1244 1244 LYS LYS A . n 
A 1 208 LEU 208 1245 1245 LEU LEU A . n 
A 1 209 PRO 209 1246 1246 PRO PRO A . n 
A 1 210 VAL 210 1247 1247 VAL VAL A . n 
A 1 211 LYS 211 1248 1248 LYS LYS A . n 
A 1 212 TRP 212 1249 1249 TRP TRP A . n 
A 1 213 MET 213 1250 1250 MET MET A . n 
A 1 214 ALA 214 1251 1251 ALA ALA A . n 
A 1 215 LEU 215 1252 1252 LEU LEU A . n 
A 1 216 GLU 216 1253 1253 GLU GLU A . n 
A 1 217 SER 217 1254 1254 SER SER A . n 
A 1 218 LEU 218 1255 1255 LEU LEU A . n 
A 1 219 GLN 219 1256 1256 GLN GLN A . n 
A 1 220 THR 220 1257 1257 THR THR A . n 
A 1 221 GLN 221 1258 1258 GLN GLN A . n 
A 1 222 LYS 222 1259 1259 LYS LYS A . n 
A 1 223 PHE 223 1260 1260 PHE PHE A . n 
A 1 224 THR 224 1261 1261 THR THR A . n 
A 1 225 THR 225 1262 1262 THR THR A . n 
A 1 226 LYS 226 1263 1263 LYS LYS A . n 
A 1 227 SER 227 1264 1264 SER SER A . n 
A 1 228 ASP 228 1265 1265 ASP ASP A . n 
A 1 229 VAL 229 1266 1266 VAL VAL A . n 
A 1 230 TRP 230 1267 1267 TRP TRP A . n 
A 1 231 SER 231 1268 1268 SER SER A . n 
A 1 232 PHE 232 1269 1269 PHE PHE A . n 
A 1 233 GLY 233 1270 1270 GLY GLY A . n 
A 1 234 VAL 234 1271 1271 VAL VAL A . n 
A 1 235 LEU 235 1272 1272 LEU LEU A . n 
A 1 236 LEU 236 1273 1273 LEU LEU A . n 
A 1 237 TRP 237 1274 1274 TRP TRP A . n 
A 1 238 GLU 238 1275 1275 GLU GLU A . n 
A 1 239 LEU 239 1276 1276 LEU LEU A . n 
A 1 240 MET 240 1277 1277 MET MET A . n 
A 1 241 THR 241 1278 1278 THR THR A . n 
A 1 242 ARG 242 1279 1279 ARG ARG A . n 
A 1 243 GLY 243 1280 1280 GLY GLY A . n 
A 1 244 ALA 244 1281 1281 ALA ALA A . n 
A 1 245 PRO 245 1282 1282 PRO PRO A . n 
A 1 246 PRO 246 1283 1283 PRO PRO A . n 
A 1 247 TYR 247 1284 1284 TYR TYR A . n 
A 1 248 PRO 248 1285 1285 PRO PRO A . n 
A 1 249 ASP 249 1286 1286 ASP ASP A . n 
A 1 250 VAL 250 1287 1287 VAL VAL A . n 
A 1 251 ASN 251 1288 1288 ASN ASN A . n 
A 1 252 THR 252 1289 1289 THR THR A . n 
A 1 253 PHE 253 1290 1290 PHE PHE A . n 
A 1 254 ASP 254 1291 1291 ASP ASP A . n 
A 1 255 ILE 255 1292 1292 ILE ILE A . n 
A 1 256 THR 256 1293 1293 THR THR A . n 
A 1 257 VAL 257 1294 1294 VAL VAL A . n 
A 1 258 TYR 258 1295 1295 TYR TYR A . n 
A 1 259 LEU 259 1296 1296 LEU LEU A . n 
A 1 260 LEU 260 1297 1297 LEU LEU A . n 
A 1 261 GLN 261 1298 1298 GLN GLN A . n 
A 1 262 GLY 262 1299 1299 GLY GLY A . n 
A 1 263 ARG 263 1300 1300 ARG ARG A . n 
A 1 264 ARG 264 1301 1301 ARG ARG A . n 
A 1 265 LEU 265 1302 1302 LEU LEU A . n 
A 1 266 LEU 266 1303 1303 LEU LEU A . n 
A 1 267 GLN 267 1304 1304 GLN GLN A . n 
A 1 268 PRO 268 1305 1305 PRO PRO A . n 
A 1 269 GLU 269 1306 1306 GLU GLU A . n 
A 1 270 TYR 270 1307 1307 TYR TYR A . n 
A 1 271 CYS 271 1308 1308 CYS CYS A . n 
A 1 272 PRO 272 1309 1309 PRO PRO A . n 
A 1 273 ASP 273 1310 1310 ASP ASP A . n 
A 1 274 PRO 274 1311 1311 PRO PRO A . n 
A 1 275 LEU 275 1312 1312 LEU LEU A . n 
A 1 276 TYR 276 1313 1313 TYR TYR A . n 
A 1 277 GLU 277 1314 1314 GLU GLU A . n 
A 1 278 VAL 278 1315 1315 VAL VAL A . n 
A 1 279 MET 279 1316 1316 MET MET A . n 
A 1 280 LEU 280 1317 1317 LEU LEU A . n 
A 1 281 LYS 281 1318 1318 LYS LYS A . n 
A 1 282 CYS 282 1319 1319 CYS CYS A . n 
A 1 283 TRP 283 1320 1320 TRP TRP A . n 
A 1 284 HIS 284 1321 1321 HIS HIS A . n 
A 1 285 PRO 285 1322 1322 PRO PRO A . n 
A 1 286 LYS 286 1323 1323 LYS LYS A . n 
A 1 287 ALA 287 1324 1324 ALA ALA A . n 
A 1 288 GLU 288 1325 1325 GLU GLU A . n 
A 1 289 MET 289 1326 1326 MET MET A . n 
A 1 290 ARG 290 1327 1327 ARG ARG A . n 
A 1 291 PRO 291 1328 1328 PRO PRO A . n 
A 1 292 SER 292 1329 1329 SER SER A . n 
A 1 293 PHE 293 1330 1330 PHE PHE A . n 
A 1 294 SER 294 1331 1331 SER SER A . n 
A 1 295 GLU 295 1332 1332 GLU GLU A . n 
A 1 296 LEU 296 1333 1333 LEU LEU A . n 
A 1 297 VAL 297 1334 1334 VAL VAL A . n 
A 1 298 SER 298 1335 1335 SER SER A . n 
A 1 299 ARG 299 1336 1336 ARG ARG A . n 
A 1 300 ILE 300 1337 1337 ILE ILE A . n 
A 1 301 SER 301 1338 1338 SER SER A . n 
A 1 302 ALA 302 1339 1339 ALA ALA A . n 
A 1 303 ILE 303 1340 1340 ILE ILE A . n 
A 1 304 PHE 304 1341 1341 PHE PHE A . n 
A 1 305 SER 305 1342 1342 SER SER A . n 
A 1 306 THR 306 1343 1343 THR THR A . n 
A 1 307 PHE 307 1344 1344 PHE PHE A . n 
A 1 308 ILE 308 1345 ?    ?   ?   A . n 
A 1 309 GLY 309 1346 ?    ?   ?   A . n 
B 1 1   GLY 1   1038 ?    ?   ?   B . n 
B 1 2   ASP 2   1039 ?    ?   ?   B . n 
B 1 3   SER 3   1040 ?    ?   ?   B . n 
B 1 4   ASP 4   1041 ?    ?   ?   B . n 
B 1 5   ILE 5   1042 ?    ?   ?   B . n 
B 1 6   SER 6   1043 ?    ?   ?   B . n 
B 1 7   SER 7   1044 ?    ?   ?   B . n 
B 1 8   PRO 8   1045 1045 PRO PRO B . n 
B 1 9   LEU 9   1046 1046 LEU LEU B . n 
B 1 10  LEU 10  1047 1047 LEU LEU B . n 
B 1 11  GLN 11  1048 1048 GLN GLN B . n 
B 1 12  ASN 12  1049 1049 ASN ASN B . n 
B 1 13  THR 13  1050 1050 THR THR B . n 
B 1 14  VAL 14  1051 1051 VAL VAL B . n 
B 1 15  HIS 15  1052 1052 HIS HIS B . n 
B 1 16  ILE 16  1053 1053 ILE ILE B . n 
B 1 17  ASP 17  1054 1054 ASP ASP B . n 
B 1 18  LEU 18  1055 1055 LEU LEU B . n 
B 1 19  SER 19  1056 1056 SER SER B . n 
B 1 20  ALA 20  1057 1057 ALA ALA B . n 
B 1 21  LEU 21  1058 1058 LEU LEU B . n 
B 1 22  ASN 22  1059 1059 ASN ASN B . n 
B 1 23  PRO 23  1060 1060 PRO PRO B . n 
B 1 24  GLU 24  1061 1061 GLU GLU B . n 
B 1 25  LEU 25  1062 1062 LEU LEU B . n 
B 1 26  VAL 26  1063 1063 VAL VAL B . n 
B 1 27  GLN 27  1064 1064 GLN GLN B . n 
B 1 28  ALA 28  1065 1065 ALA ALA B . n 
B 1 29  VAL 29  1066 1066 VAL VAL B . n 
B 1 30  GLN 30  1067 1067 GLN GLN B . n 
B 1 31  HIS 31  1068 1068 HIS HIS B . n 
B 1 32  VAL 32  1069 1069 VAL VAL B . n 
B 1 33  VAL 33  1070 1070 VAL VAL B . n 
B 1 34  ILE 34  1071 1071 ILE ILE B . n 
B 1 35  GLY 35  1072 1072 GLY GLY B . n 
B 1 36  PRO 36  1073 1073 PRO PRO B . n 
B 1 37  SER 37  1074 1074 SER SER B . n 
B 1 38  SER 38  1075 1075 SER SER B . n 
B 1 39  LEU 39  1076 1076 LEU LEU B . n 
B 1 40  ILE 40  1077 1077 ILE ILE B . n 
B 1 41  VAL 41  1078 1078 VAL VAL B . n 
B 1 42  HIS 42  1079 1079 HIS HIS B . n 
B 1 43  PHE 43  1080 1080 PHE PHE B . n 
B 1 44  ASN 44  1081 1081 ASN ASN B . n 
B 1 45  GLU 45  1082 1082 GLU GLU B . n 
B 1 46  VAL 46  1083 1083 VAL VAL B . n 
B 1 47  ILE 47  1084 1084 ILE ILE B . n 
B 1 48  GLY 48  1085 1085 GLY GLY B . n 
B 1 49  ARG 49  1086 1086 ARG ARG B . n 
B 1 50  GLY 50  1087 1087 GLY GLY B . n 
B 1 51  HIS 51  1088 1088 HIS HIS B . n 
B 1 52  PHE 52  1089 1089 PHE PHE B . n 
B 1 53  GLY 53  1090 1090 GLY GLY B . n 
B 1 54  CYS 54  1091 1091 CYS CYS B . n 
B 1 55  VAL 55  1092 1092 VAL VAL B . n 
B 1 56  TYR 56  1093 1093 TYR TYR B . n 
B 1 57  HIS 57  1094 1094 HIS HIS B . n 
B 1 58  GLY 58  1095 1095 GLY GLY B . n 
B 1 59  THR 59  1096 1096 THR THR B . n 
B 1 60  LEU 60  1097 1097 LEU LEU B . n 
B 1 61  LEU 61  1098 1098 LEU LEU B . n 
B 1 62  ASP 62  1099 1099 ASP ASP B . n 
B 1 63  ASN 63  1100 ?    ?   ?   B . n 
B 1 64  ASP 64  1101 ?    ?   ?   B . n 
B 1 65  GLY 65  1102 1102 GLY GLY B . n 
B 1 66  LYS 66  1103 1103 LYS LYS B . n 
B 1 67  LYS 67  1104 1104 LYS LYS B . n 
B 1 68  ILE 68  1105 1105 ILE ILE B . n 
B 1 69  HIS 69  1106 1106 HIS HIS B . n 
B 1 70  CYS 70  1107 1107 CYS CYS B . n 
B 1 71  ALA 71  1108 1108 ALA ALA B . n 
B 1 72  VAL 72  1109 1109 VAL VAL B . n 
B 1 73  LYS 73  1110 1110 LYS LYS B . n 
B 1 74  SER 74  1111 1111 SER SER B . n 
B 1 75  LEU 75  1112 1112 LEU LEU B . n 
B 1 76  ASN 76  1113 1113 ASN ASN B . n 
B 1 77  ARG 77  1114 1114 ARG ARG B . n 
B 1 78  ILE 78  1115 1115 ILE ILE B . n 
B 1 79  THR 79  1116 1116 THR THR B . n 
B 1 80  ASP 80  1117 1117 ASP ASP B . n 
B 1 81  ILE 81  1118 1118 ILE ILE B . n 
B 1 82  GLY 82  1119 1119 GLY GLY B . n 
B 1 83  GLU 83  1120 1120 GLU GLU B . n 
B 1 84  VAL 84  1121 1121 VAL VAL B . n 
B 1 85  SER 85  1122 1122 SER SER B . n 
B 1 86  GLN 86  1123 1123 GLN GLN B . n 
B 1 87  PHE 87  1124 1124 PHE PHE B . n 
B 1 88  LEU 88  1125 1125 LEU LEU B . n 
B 1 89  THR 89  1126 1126 THR THR B . n 
B 1 90  GLU 90  1127 1127 GLU GLU B . n 
B 1 91  GLY 91  1128 1128 GLY GLY B . n 
B 1 92  ILE 92  1129 1129 ILE ILE B . n 
B 1 93  ILE 93  1130 1130 ILE ILE B . n 
B 1 94  MET 94  1131 1131 MET MET B . n 
B 1 95  LYS 95  1132 1132 LYS LYS B . n 
B 1 96  ASP 96  1133 1133 ASP ASP B . n 
B 1 97  PHE 97  1134 1134 PHE PHE B . n 
B 1 98  SER 98  1135 1135 SER SER B . n 
B 1 99  HIS 99  1136 1136 HIS HIS B . n 
B 1 100 PRO 100 1137 1137 PRO PRO B . n 
B 1 101 ASN 101 1138 1138 ASN ASN B . n 
B 1 102 VAL 102 1139 1139 VAL VAL B . n 
B 1 103 LEU 103 1140 1140 LEU LEU B . n 
B 1 104 SER 104 1141 1141 SER SER B . n 
B 1 105 LEU 105 1142 1142 LEU LEU B . n 
B 1 106 LEU 106 1143 1143 LEU LEU B . n 
B 1 107 GLY 107 1144 1144 GLY GLY B . n 
B 1 108 ILE 108 1145 1145 ILE ILE B . n 
B 1 109 CYS 109 1146 1146 CYS CYS B . n 
B 1 110 LEU 110 1147 1147 LEU LEU B . n 
B 1 111 ARG 111 1148 ?    ?   ?   B . n 
B 1 112 SER 112 1149 ?    ?   ?   B . n 
B 1 113 GLU 113 1150 ?    ?   ?   B . n 
B 1 114 GLY 114 1151 ?    ?   ?   B . n 
B 1 115 SER 115 1152 1152 SER SER B . n 
B 1 116 PRO 116 1153 1153 PRO PRO B . n 
B 1 117 LEU 117 1154 1154 LEU LEU B . n 
B 1 118 VAL 118 1155 1155 VAL VAL B . n 
B 1 119 VAL 119 1156 1156 VAL VAL B . n 
B 1 120 LEU 120 1157 1157 LEU LEU B . n 
B 1 121 PRO 121 1158 1158 PRO PRO B . n 
B 1 122 TYR 122 1159 1159 TYR TYR B . n 
B 1 123 MET 123 1160 1160 MET MET B . n 
B 1 124 LYS 124 1161 1161 LYS LYS B . n 
B 1 125 HIS 125 1162 1162 HIS HIS B . n 
B 1 126 GLY 126 1163 1163 GLY GLY B . n 
B 1 127 ASP 127 1164 1164 ASP ASP B . n 
B 1 128 LEU 128 1165 1165 LEU LEU B . n 
B 1 129 ARG 129 1166 1166 ARG ARG B . n 
B 1 130 ASN 130 1167 1167 ASN ASN B . n 
B 1 131 PHE 131 1168 1168 PHE PHE B . n 
B 1 132 ILE 132 1169 1169 ILE ILE B . n 
B 1 133 ARG 133 1170 1170 ARG ARG B . n 
B 1 134 ASN 134 1171 1171 ASN ASN B . n 
B 1 135 GLU 135 1172 1172 GLU GLU B . n 
B 1 136 THR 136 1173 1173 THR THR B . n 
B 1 137 HIS 137 1174 1174 HIS HIS B . n 
B 1 138 ASN 138 1175 1175 ASN ASN B . n 
B 1 139 PRO 139 1176 1176 PRO PRO B . n 
B 1 140 THR 140 1177 1177 THR THR B . n 
B 1 141 VAL 141 1178 1178 VAL VAL B . n 
B 1 142 LYS 142 1179 1179 LYS LYS B . n 
B 1 143 ASP 143 1180 1180 ASP ASP B . n 
B 1 144 LEU 144 1181 1181 LEU LEU B . n 
B 1 145 ILE 145 1182 1182 ILE ILE B . n 
B 1 146 GLY 146 1183 1183 GLY GLY B . n 
B 1 147 PHE 147 1184 1184 PHE PHE B . n 
B 1 148 GLY 148 1185 1185 GLY GLY B . n 
B 1 149 LEU 149 1186 1186 LEU LEU B . n 
B 1 150 GLN 150 1187 1187 GLN GLN B . n 
B 1 151 VAL 151 1188 1188 VAL VAL B . n 
B 1 152 ALA 152 1189 1189 ALA ALA B . n 
B 1 153 LYS 153 1190 1190 LYS LYS B . n 
B 1 154 GLY 154 1191 1191 GLY GLY B . n 
B 1 155 MET 155 1192 1192 MET MET B . n 
B 1 156 LYS 156 1193 1193 LYS LYS B . n 
B 1 157 TYR 157 1194 1194 TYR TYR B . n 
B 1 158 LEU 158 1195 1195 LEU LEU B . n 
B 1 159 ALA 159 1196 1196 ALA ALA B . n 
B 1 160 SER 160 1197 1197 SER SER B . n 
B 1 161 LYS 161 1198 1198 LYS LYS B . n 
B 1 162 LYS 162 1199 1199 LYS LYS B . n 
B 1 163 PHE 163 1200 1200 PHE PHE B . n 
B 1 164 VAL 164 1201 1201 VAL VAL B . n 
B 1 165 HIS 165 1202 1202 HIS HIS B . n 
B 1 166 ARG 166 1203 1203 ARG ARG B . n 
B 1 167 ASP 167 1204 1204 ASP ASP B . n 
B 1 168 LEU 168 1205 1205 LEU LEU B . n 
B 1 169 ALA 169 1206 1206 ALA ALA B . n 
B 1 170 ALA 170 1207 1207 ALA ALA B . n 
B 1 171 ARG 171 1208 1208 ARG ARG B . n 
B 1 172 ASN 172 1209 1209 ASN ASN B . n 
B 1 173 CYS 173 1210 1210 CYS CYS B . n 
B 1 174 MET 174 1211 1211 MET MET B . n 
B 1 175 LEU 175 1212 1212 LEU LEU B . n 
B 1 176 ASP 176 1213 1213 ASP ASP B . n 
B 1 177 GLU 177 1214 1214 GLU GLU B . n 
B 1 178 LYS 178 1215 1215 LYS LYS B . n 
B 1 179 PHE 179 1216 1216 PHE PHE B . n 
B 1 180 THR 180 1217 1217 THR THR B . n 
B 1 181 VAL 181 1218 1218 VAL VAL B . n 
B 1 182 LYS 182 1219 1219 LYS LYS B . n 
B 1 183 VAL 183 1220 1220 VAL VAL B . n 
B 1 184 ALA 184 1221 1221 ALA ALA B . n 
B 1 185 ASP 185 1222 1222 ASP ASP B . n 
B 1 186 PHE 186 1223 1223 PHE PHE B . n 
B 1 187 GLY 187 1224 1224 GLY GLY B . n 
B 1 188 LEU 188 1225 1225 LEU LEU B . n 
B 1 189 ALA 189 1226 1226 ALA ALA B . n 
B 1 190 ARG 190 1227 1227 ARG ARG B . n 
B 1 191 ASP 191 1228 1228 ASP ASP B . n 
B 1 192 MET 192 1229 1229 MET MET B . n 
B 1 193 TYR 193 1230 1230 TYR TYR B . n 
B 1 194 ASP 194 1231 1231 ASP ASP B . n 
B 1 195 LYS 195 1232 1232 LYS LYS B . n 
B 1 196 GLU 196 1233 1233 GLU GLU B . n 
B 1 197 TYR 197 1234 1234 TYR TYR B . n 
B 1 198 TYR 198 1235 1235 TYR TYR B . n 
B 1 199 SER 199 1236 1236 SER SER B . n 
B 1 200 VAL 200 1237 1237 VAL VAL B . n 
B 1 201 HIS 201 1238 1238 HIS HIS B . n 
B 1 202 ASN 202 1239 1239 ASN ASN B . n 
B 1 203 LYS 203 1240 1240 LYS LYS B . n 
B 1 204 THR 204 1241 1241 THR THR B . n 
B 1 205 GLY 205 1242 1242 GLY GLY B . n 
B 1 206 ALA 206 1243 1243 ALA ALA B . n 
B 1 207 LYS 207 1244 1244 LYS LYS B . n 
B 1 208 LEU 208 1245 1245 LEU LEU B . n 
B 1 209 PRO 209 1246 1246 PRO PRO B . n 
B 1 210 VAL 210 1247 1247 VAL VAL B . n 
B 1 211 LYS 211 1248 1248 LYS LYS B . n 
B 1 212 TRP 212 1249 1249 TRP TRP B . n 
B 1 213 MET 213 1250 1250 MET MET B . n 
B 1 214 ALA 214 1251 1251 ALA ALA B . n 
B 1 215 LEU 215 1252 1252 LEU LEU B . n 
B 1 216 GLU 216 1253 1253 GLU GLU B . n 
B 1 217 SER 217 1254 1254 SER SER B . n 
B 1 218 LEU 218 1255 1255 LEU LEU B . n 
B 1 219 GLN 219 1256 1256 GLN GLN B . n 
B 1 220 THR 220 1257 1257 THR THR B . n 
B 1 221 GLN 221 1258 1258 GLN GLN B . n 
B 1 222 LYS 222 1259 1259 LYS LYS B . n 
B 1 223 PHE 223 1260 1260 PHE PHE B . n 
B 1 224 THR 224 1261 1261 THR THR B . n 
B 1 225 THR 225 1262 1262 THR THR B . n 
B 1 226 LYS 226 1263 1263 LYS LYS B . n 
B 1 227 SER 227 1264 1264 SER SER B . n 
B 1 228 ASP 228 1265 1265 ASP ASP B . n 
B 1 229 VAL 229 1266 1266 VAL VAL B . n 
B 1 230 TRP 230 1267 1267 TRP TRP B . n 
B 1 231 SER 231 1268 1268 SER SER B . n 
B 1 232 PHE 232 1269 1269 PHE PHE B . n 
B 1 233 GLY 233 1270 1270 GLY GLY B . n 
B 1 234 VAL 234 1271 1271 VAL VAL B . n 
B 1 235 LEU 235 1272 1272 LEU LEU B . n 
B 1 236 LEU 236 1273 1273 LEU LEU B . n 
B 1 237 TRP 237 1274 1274 TRP TRP B . n 
B 1 238 GLU 238 1275 1275 GLU GLU B . n 
B 1 239 LEU 239 1276 1276 LEU LEU B . n 
B 1 240 MET 240 1277 1277 MET MET B . n 
B 1 241 THR 241 1278 1278 THR THR B . n 
B 1 242 ARG 242 1279 1279 ARG ARG B . n 
B 1 243 GLY 243 1280 1280 GLY GLY B . n 
B 1 244 ALA 244 1281 1281 ALA ALA B . n 
B 1 245 PRO 245 1282 1282 PRO PRO B . n 
B 1 246 PRO 246 1283 1283 PRO PRO B . n 
B 1 247 TYR 247 1284 1284 TYR TYR B . n 
B 1 248 PRO 248 1285 1285 PRO PRO B . n 
B 1 249 ASP 249 1286 1286 ASP ASP B . n 
B 1 250 VAL 250 1287 1287 VAL VAL B . n 
B 1 251 ASN 251 1288 1288 ASN ASN B . n 
B 1 252 THR 252 1289 1289 THR THR B . n 
B 1 253 PHE 253 1290 1290 PHE PHE B . n 
B 1 254 ASP 254 1291 1291 ASP ASP B . n 
B 1 255 ILE 255 1292 1292 ILE ILE B . n 
B 1 256 THR 256 1293 1293 THR THR B . n 
B 1 257 VAL 257 1294 1294 VAL VAL B . n 
B 1 258 TYR 258 1295 1295 TYR TYR B . n 
B 1 259 LEU 259 1296 1296 LEU LEU B . n 
B 1 260 LEU 260 1297 1297 LEU LEU B . n 
B 1 261 GLN 261 1298 1298 GLN GLN B . n 
B 1 262 GLY 262 1299 1299 GLY GLY B . n 
B 1 263 ARG 263 1300 1300 ARG ARG B . n 
B 1 264 ARG 264 1301 1301 ARG ARG B . n 
B 1 265 LEU 265 1302 1302 LEU LEU B . n 
B 1 266 LEU 266 1303 1303 LEU LEU B . n 
B 1 267 GLN 267 1304 1304 GLN GLN B . n 
B 1 268 PRO 268 1305 1305 PRO PRO B . n 
B 1 269 GLU 269 1306 1306 GLU GLU B . n 
B 1 270 TYR 270 1307 1307 TYR TYR B . n 
B 1 271 CYS 271 1308 1308 CYS CYS B . n 
B 1 272 PRO 272 1309 1309 PRO PRO B . n 
B 1 273 ASP 273 1310 1310 ASP ASP B . n 
B 1 274 PRO 274 1311 1311 PRO PRO B . n 
B 1 275 LEU 275 1312 1312 LEU LEU B . n 
B 1 276 TYR 276 1313 1313 TYR TYR B . n 
B 1 277 GLU 277 1314 1314 GLU GLU B . n 
B 1 278 VAL 278 1315 1315 VAL VAL B . n 
B 1 279 MET 279 1316 1316 MET MET B . n 
B 1 280 LEU 280 1317 1317 LEU LEU B . n 
B 1 281 LYS 281 1318 1318 LYS LYS B . n 
B 1 282 CYS 282 1319 1319 CYS CYS B . n 
B 1 283 TRP 283 1320 1320 TRP TRP B . n 
B 1 284 HIS 284 1321 1321 HIS HIS B . n 
B 1 285 PRO 285 1322 1322 PRO PRO B . n 
B 1 286 LYS 286 1323 1323 LYS LYS B . n 
B 1 287 ALA 287 1324 1324 ALA ALA B . n 
B 1 288 GLU 288 1325 1325 GLU GLU B . n 
B 1 289 MET 289 1326 1326 MET MET B . n 
B 1 290 ARG 290 1327 1327 ARG ARG B . n 
B 1 291 PRO 291 1328 1328 PRO PRO B . n 
B 1 292 SER 292 1329 1329 SER SER B . n 
B 1 293 PHE 293 1330 1330 PHE PHE B . n 
B 1 294 SER 294 1331 1331 SER SER B . n 
B 1 295 GLU 295 1332 1332 GLU GLU B . n 
B 1 296 LEU 296 1333 1333 LEU LEU B . n 
B 1 297 VAL 297 1334 1334 VAL VAL B . n 
B 1 298 SER 298 1335 1335 SER SER B . n 
B 1 299 ARG 299 1336 1336 ARG ARG B . n 
B 1 300 ILE 300 1337 1337 ILE ILE B . n 
B 1 301 SER 301 1338 1338 SER SER B . n 
B 1 302 ALA 302 1339 1339 ALA ALA B . n 
B 1 303 ILE 303 1340 1340 ILE ILE B . n 
B 1 304 PHE 304 1341 1341 PHE PHE B . n 
B 1 305 SER 305 1342 1342 SER SER B . n 
B 1 306 THR 306 1343 1343 THR THR B . n 
B 1 307 PHE 307 1344 1344 PHE PHE B . n 
B 1 308 ILE 308 1345 ?    ?   ?   B . n 
B 1 309 GLY 309 1346 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L3A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L3A 
_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 A1L3A 1  1401 2  A1L3A DRG A . 
D 2 A1L3A 1  1401 1  A1L3A DRG B . 
E 3 HOH   1  1501 38 HOH   HOH A . 
E 3 HOH   2  1502 49 HOH   HOH A . 
E 3 HOH   3  1503 39 HOH   HOH A . 
E 3 HOH   4  1504 21 HOH   HOH A . 
E 3 HOH   5  1505 22 HOH   HOH A . 
E 3 HOH   6  1506 73 HOH   HOH A . 
E 3 HOH   7  1507 47 HOH   HOH A . 
E 3 HOH   8  1508 3  HOH   HOH A . 
E 3 HOH   9  1509 82 HOH   HOH A . 
E 3 HOH   10 1510 8  HOH   HOH A . 
E 3 HOH   11 1511 50 HOH   HOH A . 
E 3 HOH   12 1512 7  HOH   HOH A . 
E 3 HOH   13 1513 43 HOH   HOH A . 
E 3 HOH   14 1514 23 HOH   HOH A . 
E 3 HOH   15 1515 35 HOH   HOH A . 
E 3 HOH   16 1516 62 HOH   HOH A . 
E 3 HOH   17 1517 15 HOH   HOH A . 
E 3 HOH   18 1518 11 HOH   HOH A . 
E 3 HOH   19 1519 51 HOH   HOH A . 
E 3 HOH   20 1520 10 HOH   HOH A . 
E 3 HOH   21 1521 56 HOH   HOH A . 
E 3 HOH   22 1522 36 HOH   HOH A . 
E 3 HOH   23 1523 79 HOH   HOH A . 
E 3 HOH   24 1524 69 HOH   HOH A . 
E 3 HOH   25 1525 26 HOH   HOH A . 
E 3 HOH   26 1526 78 HOH   HOH A . 
E 3 HOH   27 1527 58 HOH   HOH A . 
E 3 HOH   28 1528 34 HOH   HOH A . 
E 3 HOH   29 1529 61 HOH   HOH A . 
E 3 HOH   30 1530 66 HOH   HOH A . 
E 3 HOH   31 1531 60 HOH   HOH A . 
E 3 HOH   32 1532 87 HOH   HOH A . 
E 3 HOH   33 1533 89 HOH   HOH A . 
E 3 HOH   34 1534 77 HOH   HOH A . 
E 3 HOH   35 1535 41 HOH   HOH A . 
F 3 HOH   1  1501 63 HOH   HOH B . 
F 3 HOH   2  1502 5  HOH   HOH B . 
F 3 HOH   3  1503 1  HOH   HOH B . 
F 3 HOH   4  1504 9  HOH   HOH B . 
F 3 HOH   5  1505 37 HOH   HOH B . 
F 3 HOH   6  1506 13 HOH   HOH B . 
F 3 HOH   7  1507 28 HOH   HOH B . 
F 3 HOH   8  1508 4  HOH   HOH B . 
F 3 HOH   9  1509 2  HOH   HOH B . 
F 3 HOH   10 1510 40 HOH   HOH B . 
F 3 HOH   11 1511 55 HOH   HOH B . 
F 3 HOH   12 1512 17 HOH   HOH B . 
F 3 HOH   13 1513 46 HOH   HOH B . 
F 3 HOH   14 1514 12 HOH   HOH B . 
F 3 HOH   15 1515 53 HOH   HOH B . 
F 3 HOH   16 1516 76 HOH   HOH B . 
F 3 HOH   17 1517 67 HOH   HOH B . 
F 3 HOH   18 1518 84 HOH   HOH B . 
F 3 HOH   19 1519 45 HOH   HOH B . 
F 3 HOH   20 1520 25 HOH   HOH B . 
F 3 HOH   21 1521 68 HOH   HOH B . 
F 3 HOH   22 1522 18 HOH   HOH B . 
F 3 HOH   23 1523 72 HOH   HOH B . 
F 3 HOH   24 1524 42 HOH   HOH B . 
F 3 HOH   25 1525 27 HOH   HOH B . 
F 3 HOH   26 1526 85 HOH   HOH B . 
F 3 HOH   27 1527 75 HOH   HOH B . 
F 3 HOH   28 1528 33 HOH   HOH B . 
F 3 HOH   29 1529 54 HOH   HOH B . 
F 3 HOH   30 1530 31 HOH   HOH B . 
F 3 HOH   31 1531 16 HOH   HOH B . 
F 3 HOH   32 1532 52 HOH   HOH B . 
F 3 HOH   33 1533 30 HOH   HOH B . 
F 3 HOH   34 1534 57 HOH   HOH B . 
F 3 HOH   35 1535 65 HOH   HOH B . 
F 3 HOH   36 1536 86 HOH   HOH B . 
F 3 HOH   37 1537 80 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASN 1081 ? CG  ? A ASN 44  CG  
2   1 Y 1 A ASN 1081 ? OD1 ? A ASN 44  OD1 
3   1 Y 1 A ASN 1081 ? ND2 ? A ASN 44  ND2 
4   1 Y 1 A GLU 1082 ? CG  ? A GLU 45  CG  
5   1 Y 1 A GLU 1082 ? CD  ? A GLU 45  CD  
6   1 Y 1 A GLU 1082 ? OE1 ? A GLU 45  OE1 
7   1 Y 1 A GLU 1082 ? OE2 ? A GLU 45  OE2 
8   1 Y 1 A ARG 1086 ? CG  ? A ARG 49  CG  
9   1 Y 1 A ARG 1086 ? CD  ? A ARG 49  CD  
10  1 Y 1 A ARG 1086 ? NE  ? A ARG 49  NE  
11  1 Y 1 A ARG 1086 ? CZ  ? A ARG 49  CZ  
12  1 Y 1 A ARG 1086 ? NH1 ? A ARG 49  NH1 
13  1 Y 1 A ARG 1086 ? NH2 ? A ARG 49  NH2 
14  1 Y 1 A ASP 1099 ? CG  ? A ASP 62  CG  
15  1 Y 1 A ASP 1099 ? OD1 ? A ASP 62  OD1 
16  1 Y 1 A ASP 1099 ? OD2 ? A ASP 62  OD2 
17  1 Y 1 A ASN 1100 ? CG  ? A ASN 63  CG  
18  1 Y 1 A ASN 1100 ? OD1 ? A ASN 63  OD1 
19  1 Y 1 A ASN 1100 ? ND2 ? A ASN 63  ND2 
20  1 Y 1 A LYS 1103 ? CG  ? A LYS 66  CG  
21  1 Y 1 A LYS 1103 ? CD  ? A LYS 66  CD  
22  1 Y 1 A LYS 1103 ? CE  ? A LYS 66  CE  
23  1 Y 1 A LYS 1103 ? NZ  ? A LYS 66  NZ  
24  1 Y 1 A LYS 1104 ? CG  ? A LYS 67  CG  
25  1 Y 1 A LYS 1104 ? CD  ? A LYS 67  CD  
26  1 Y 1 A LYS 1104 ? CE  ? A LYS 67  CE  
27  1 Y 1 A LYS 1104 ? NZ  ? A LYS 67  NZ  
28  1 Y 1 A ILE 1118 ? CG1 ? A ILE 81  CG1 
29  1 Y 1 A ILE 1118 ? CG2 ? A ILE 81  CG2 
30  1 Y 1 A ILE 1118 ? CD1 ? A ILE 81  CD1 
31  1 Y 1 A GLU 1120 ? CG  ? A GLU 83  CG  
32  1 Y 1 A GLU 1120 ? CD  ? A GLU 83  CD  
33  1 Y 1 A GLU 1120 ? OE1 ? A GLU 83  OE1 
34  1 Y 1 A GLU 1120 ? OE2 ? A GLU 83  OE2 
35  1 Y 1 A GLN 1123 ? CG  ? A GLN 86  CG  
36  1 Y 1 A GLN 1123 ? CD  ? A GLN 86  CD  
37  1 Y 1 A GLN 1123 ? OE1 ? A GLN 86  OE1 
38  1 Y 1 A GLN 1123 ? NE2 ? A GLN 86  NE2 
39  1 Y 1 A SER 1152 ? OG  ? A SER 115 OG  
40  1 Y 1 A LYS 1240 ? CG  ? A LYS 203 CG  
41  1 Y 1 A LYS 1240 ? CD  ? A LYS 203 CD  
42  1 Y 1 A LYS 1240 ? CE  ? A LYS 203 CE  
43  1 Y 1 A LYS 1240 ? NZ  ? A LYS 203 NZ  
44  1 Y 1 A VAL 1294 ? CG1 ? A VAL 257 CG1 
45  1 Y 1 A VAL 1294 ? CG2 ? A VAL 257 CG2 
46  1 Y 1 A LYS 1323 ? CD  ? A LYS 286 CD  
47  1 Y 1 A LYS 1323 ? CE  ? A LYS 286 CE  
48  1 Y 1 A LYS 1323 ? NZ  ? A LYS 286 NZ  
49  1 Y 1 A PHE 1344 ? CG  ? A PHE 307 CG  
50  1 Y 1 A PHE 1344 ? CD1 ? A PHE 307 CD1 
51  1 Y 1 A PHE 1344 ? CD2 ? A PHE 307 CD2 
52  1 Y 1 A PHE 1344 ? CE1 ? A PHE 307 CE1 
53  1 Y 1 A PHE 1344 ? CE2 ? A PHE 307 CE2 
54  1 Y 1 A PHE 1344 ? CZ  ? A PHE 307 CZ  
55  1 Y 1 B GLN 1064 ? CG  ? B GLN 27  CG  
56  1 Y 1 B GLN 1064 ? CD  ? B GLN 27  CD  
57  1 Y 1 B GLN 1064 ? OE1 ? B GLN 27  OE1 
58  1 Y 1 B GLN 1064 ? NE2 ? B GLN 27  NE2 
59  1 Y 1 B HIS 1068 ? CG  ? B HIS 31  CG  
60  1 Y 1 B HIS 1068 ? ND1 ? B HIS 31  ND1 
61  1 Y 1 B HIS 1068 ? CD2 ? B HIS 31  CD2 
62  1 Y 1 B HIS 1068 ? CE1 ? B HIS 31  CE1 
63  1 Y 1 B HIS 1068 ? NE2 ? B HIS 31  NE2 
64  1 Y 1 B ILE 1077 ? CG1 ? B ILE 40  CG1 
65  1 Y 1 B ILE 1077 ? CG2 ? B ILE 40  CG2 
66  1 Y 1 B ILE 1077 ? CD1 ? B ILE 40  CD1 
67  1 Y 1 B ASN 1081 ? CG  ? B ASN 44  CG  
68  1 Y 1 B ASN 1081 ? OD1 ? B ASN 44  OD1 
69  1 Y 1 B ASN 1081 ? ND2 ? B ASN 44  ND2 
70  1 Y 1 B ASP 1099 ? CG  ? B ASP 62  CG  
71  1 Y 1 B ASP 1099 ? OD1 ? B ASP 62  OD1 
72  1 Y 1 B ASP 1099 ? OD2 ? B ASP 62  OD2 
73  1 Y 1 B LYS 1103 ? CG  ? B LYS 66  CG  
74  1 Y 1 B LYS 1103 ? CD  ? B LYS 66  CD  
75  1 Y 1 B LYS 1103 ? CE  ? B LYS 66  CE  
76  1 Y 1 B LYS 1103 ? NZ  ? B LYS 66  NZ  
77  1 Y 1 B LYS 1104 ? CG  ? B LYS 67  CG  
78  1 Y 1 B LYS 1104 ? CD  ? B LYS 67  CD  
79  1 Y 1 B LYS 1104 ? CE  ? B LYS 67  CE  
80  1 Y 1 B LYS 1104 ? NZ  ? B LYS 67  NZ  
81  1 Y 1 B ILE 1105 ? CG1 ? B ILE 68  CG1 
82  1 Y 1 B ILE 1105 ? CG2 ? B ILE 68  CG2 
83  1 Y 1 B ILE 1105 ? CD1 ? B ILE 68  CD1 
84  1 Y 1 B ILE 1118 ? CG1 ? B ILE 81  CG1 
85  1 Y 1 B ILE 1118 ? CG2 ? B ILE 81  CG2 
86  1 Y 1 B ILE 1118 ? CD1 ? B ILE 81  CD1 
87  1 Y 1 B GLU 1120 ? CG  ? B GLU 83  CG  
88  1 Y 1 B GLU 1120 ? CD  ? B GLU 83  CD  
89  1 Y 1 B GLU 1120 ? OE1 ? B GLU 83  OE1 
90  1 Y 1 B GLU 1120 ? OE2 ? B GLU 83  OE2 
91  1 Y 1 B LYS 1161 ? CG  ? B LYS 124 CG  
92  1 Y 1 B LYS 1161 ? CD  ? B LYS 124 CD  
93  1 Y 1 B LYS 1161 ? CE  ? B LYS 124 CE  
94  1 Y 1 B LYS 1161 ? NZ  ? B LYS 124 NZ  
95  1 Y 1 B LYS 1215 ? CG  ? B LYS 178 CG  
96  1 Y 1 B LYS 1215 ? CD  ? B LYS 178 CD  
97  1 Y 1 B LYS 1215 ? CE  ? B LYS 178 CE  
98  1 Y 1 B LYS 1215 ? NZ  ? B LYS 178 NZ  
99  1 Y 1 B ARG 1227 ? CG  ? B ARG 190 CG  
100 1 Y 1 B ARG 1227 ? CD  ? B ARG 190 CD  
101 1 Y 1 B ARG 1227 ? NE  ? B ARG 190 NE  
102 1 Y 1 B ARG 1227 ? CZ  ? B ARG 190 CZ  
103 1 Y 1 B ARG 1227 ? NH1 ? B ARG 190 NH1 
104 1 Y 1 B ARG 1227 ? NH2 ? B ARG 190 NH2 
105 1 Y 1 B LYS 1232 ? CG  ? B LYS 195 CG  
106 1 Y 1 B LYS 1232 ? CD  ? B LYS 195 CD  
107 1 Y 1 B LYS 1232 ? CE  ? B LYS 195 CE  
108 1 Y 1 B LYS 1232 ? NZ  ? B LYS 195 NZ  
109 1 Y 1 B ILE 1292 ? CG1 ? B ILE 255 CG1 
110 1 Y 1 B ILE 1292 ? CG2 ? B ILE 255 CG2 
111 1 Y 1 B ILE 1292 ? CD1 ? B ILE 255 CD1 
112 1 Y 1 B GLN 1298 ? CG  ? B GLN 261 CG  
113 1 Y 1 B GLN 1298 ? CD  ? B GLN 261 CD  
114 1 Y 1 B GLN 1298 ? OE1 ? B GLN 261 OE1 
115 1 Y 1 B GLN 1298 ? NE2 ? B GLN 261 NE2 
116 1 Y 1 B ARG 1300 ? CG  ? B ARG 263 CG  
117 1 Y 1 B ARG 1300 ? CD  ? B ARG 263 CD  
118 1 Y 1 B ARG 1300 ? NE  ? B ARG 263 NE  
119 1 Y 1 B ARG 1300 ? CZ  ? B ARG 263 CZ  
120 1 Y 1 B ARG 1300 ? NH1 ? B ARG 263 NH1 
121 1 Y 1 B ARG 1300 ? NH2 ? B ARG 263 NH2 
122 1 Y 1 B GLU 1314 ? CG  ? B GLU 277 CG  
123 1 Y 1 B GLU 1314 ? CD  ? B GLU 277 CD  
124 1 Y 1 B GLU 1314 ? OE1 ? B GLU 277 OE1 
125 1 Y 1 B GLU 1314 ? OE2 ? B GLU 277 OE2 
126 1 Y 1 B LYS 1318 ? CG  ? B LYS 281 CG  
127 1 Y 1 B LYS 1318 ? CD  ? B LYS 281 CD  
128 1 Y 1 B LYS 1318 ? CE  ? B LYS 281 CE  
129 1 Y 1 B LYS 1318 ? NZ  ? B LYS 281 NZ  
130 1 Y 1 B LYS 1323 ? CD  ? B LYS 286 CD  
131 1 Y 1 B LYS 1323 ? CE  ? B LYS 286 CE  
132 1 Y 1 B LYS 1323 ? NZ  ? B LYS 286 NZ  
133 1 Y 1 B GLU 1325 ? CG  ? B GLU 288 CG  
134 1 Y 1 B GLU 1325 ? CD  ? B GLU 288 CD  
135 1 Y 1 B GLU 1325 ? OE1 ? B GLU 288 OE1 
136 1 Y 1 B GLU 1325 ? OE2 ? B GLU 288 OE2 
137 1 Y 1 B PHE 1344 ? CG  ? B PHE 307 CG  
138 1 Y 1 B PHE 1344 ? CD1 ? B PHE 307 CD1 
139 1 Y 1 B PHE 1344 ? CD2 ? B PHE 307 CD2 
140 1 Y 1 B PHE 1344 ? CE1 ? B PHE 307 CE1 
141 1 Y 1 B PHE 1344 ? CE2 ? B PHE 307 CE2 
142 1 Y 1 B PHE 1344 ? CZ  ? B PHE 307 CZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? xia2   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.69 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IVB 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.568 
_cell.length_a_esd                 ? 
_cell.length_b                     66.168 
_cell.length_b_esd                 ? 
_cell.length_c                     79.617 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IVB 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IVB 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.23 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.8 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '15-30% PEG8K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 1' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97851 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97851 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IVB 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               34.13 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     23820 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.970 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.41 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1746 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.639 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9IVB 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.35 
_refine.ls_d_res_low                             34.10 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     23807 
_refine.ls_number_reflns_R_free                  2036 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.75 
_refine.ls_percent_reflns_R_free                 8.55 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2834 
_refine.ls_R_factor_R_free                       0.2730 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2482 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          83.23 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5EOB 
_refine.pdbx_stereochemistry_target_values       TWIN_LSQ_F 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 37.15 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.35 
_refine_hist.d_res_low                        34.10 
_refine_hist.number_atoms_solvent             72 
_refine_hist.number_atoms_total               4734 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4600 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         62 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 4786 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.790 ? 6522 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.884 ? 672  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.046 ? 742  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 814  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.35 2.41  . . 131 1511 90.00 . . . . 0.3183 . . . . . . . . . . . 0.3153 
'X-RAY DIFFRACTION' 2.41 2.47  . . 144 1555 92.00 . . . . 0.2997 . . . . . . . . . . . 0.3161 
'X-RAY DIFFRACTION' 2.47 2.54  . . 145 1523 91.00 . . . . 0.3024 . . . . . . . . . . . 0.3150 
'X-RAY DIFFRACTION' 2.54 2.63  . . 134 1571 92.00 . . . . 0.3086 . . . . . . . . . . . 0.2753 
'X-RAY DIFFRACTION' 2.63 2.72  . . 144 1572 92.00 . . . . 0.3045 . . . . . . . . . . . 0.3301 
'X-RAY DIFFRACTION' 2.72 2.83  . . 151 1525 91.00 . . . . 0.3041 . . . . . . . . . . . 0.3607 
'X-RAY DIFFRACTION' 2.83 2.96  . . 136 1569 92.00 . . . . 0.3090 . . . . . . . . . . . 0.3286 
'X-RAY DIFFRACTION' 2.96 3.11  . . 143 1542 92.00 . . . . 0.3043 . . . . . . . . . . . 0.3060 
'X-RAY DIFFRACTION' 3.11 3.31  . . 147 1565 91.00 . . . . 0.3003 . . . . . . . . . . . 0.3417 
'X-RAY DIFFRACTION' 3.31 3.56  . . 145 1544 91.00 . . . . 0.2877 . . . . . . . . . . . 0.3062 
'X-RAY DIFFRACTION' 3.56 3.92  . . 141 1584 92.00 . . . . 0.2749 . . . . . . . . . . . 0.2972 
'X-RAY DIFFRACTION' 3.92 4.49  . . 142 1558 91.00 . . . . 0.2490 . . . . . . . . . . . 0.2554 
'X-RAY DIFFRACTION' 4.49 5.65  . . 145 1574 92.00 . . . . 0.2448 . . . . . . . . . . . 0.2857 
'X-RAY DIFFRACTION' 5.65 34.10 . . 150 1616 91.00 . . . . 0.2510 . . . . . . . . . . . 0.2441 
# 
_struct.entry_id                     9IVB 
_struct.title                        'Crystal structure of c-Met kinase domain bound by bozitinib' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9IVB 
_struct_keywords.text            'c-Met, Bozitinib, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MET_HUMAN 
_struct_ref.pdbx_db_accession          P08581 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITD
IGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLAS
KKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELM
TRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIG
;
_struct_ref.pdbx_align_begin           1038 
# 
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 9IVB A 1 ? 309 ? P08581 1038 ? 1346 ? 1038 1346 
2 1 9IVB B 1 ? 309 ? P08581 1038 ? 1346 ? 1038 1346 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 9   ? LEU A 18  ? LEU A 1046 LEU A 1055 1 ? 10 
HELX_P HELX_P2  AA2 ASN A 22  ? HIS A 31  ? ASN A 1059 HIS A 1068 1 ? 10 
HELX_P HELX_P3  AA3 GLY A 35  ? SER A 37  ? GLY A 1072 SER A 1074 5 ? 3  
HELX_P HELX_P4  AA4 GLY A 82  ? ILE A 92  ? GLY A 1119 ILE A 1129 1 ? 11 
HELX_P HELX_P5  AA5 ILE A 93  ? PHE A 97  ? ILE A 1130 PHE A 1134 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 127 ? ASN A 134 ? ASP A 1164 ASN A 1171 1 ? 8  
HELX_P HELX_P7  AA7 THR A 140 ? LYS A 161 ? THR A 1177 LYS A 1198 1 ? 22 
HELX_P HELX_P8  AA8 PHE A 186 ? ARG A 190 ? PHE A 1223 ARG A 1227 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 194 ? TYR A 198 ? ASP A 1231 TYR A 1235 5 ? 5  
HELX_P HELX_P10 AB1 PRO A 209 ? MET A 213 ? PRO A 1246 MET A 1250 5 ? 5  
HELX_P HELX_P11 AB2 ALA A 214 ? GLN A 221 ? ALA A 1251 GLN A 1258 1 ? 8  
HELX_P HELX_P12 AB3 THR A 224 ? THR A 241 ? THR A 1261 THR A 1278 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 254 ? GLY A 262 ? ASP A 1291 GLY A 1299 1 ? 9  
HELX_P HELX_P14 AB5 PRO A 272 ? TRP A 283 ? PRO A 1309 TRP A 1320 1 ? 12 
HELX_P HELX_P15 AB6 LYS A 286 ? ARG A 290 ? LYS A 1323 ARG A 1327 5 ? 5  
HELX_P HELX_P16 AB7 SER A 292 ? THR A 306 ? SER A 1329 THR A 1343 1 ? 15 
HELX_P HELX_P17 AB8 LEU B 9   ? LEU B 18  ? LEU B 1046 LEU B 1055 1 ? 10 
HELX_P HELX_P18 AB9 ASN B 22  ? GLN B 30  ? ASN B 1059 GLN B 1067 1 ? 9  
HELX_P HELX_P19 AC1 GLY B 35  ? SER B 37  ? GLY B 1072 SER B 1074 5 ? 3  
HELX_P HELX_P20 AC2 ASP B 80  ? ILE B 92  ? ASP B 1117 ILE B 1129 1 ? 13 
HELX_P HELX_P21 AC3 ILE B 93  ? PHE B 97  ? ILE B 1130 PHE B 1134 5 ? 5  
HELX_P HELX_P22 AC4 ASP B 127 ? ASN B 134 ? ASP B 1164 ASN B 1171 1 ? 8  
HELX_P HELX_P23 AC5 THR B 140 ? LYS B 161 ? THR B 1177 LYS B 1198 1 ? 22 
HELX_P HELX_P24 AC6 ALA B 169 ? ARG B 171 ? ALA B 1206 ARG B 1208 5 ? 3  
HELX_P HELX_P25 AC7 PHE B 186 ? ARG B 190 ? PHE B 1223 ARG B 1227 5 ? 5  
HELX_P HELX_P26 AC8 ASP B 194 ? GLU B 196 ? ASP B 1231 GLU B 1233 5 ? 3  
HELX_P HELX_P27 AC9 GLU B 216 ? GLN B 221 ? GLU B 1253 GLN B 1258 1 ? 6  
HELX_P HELX_P28 AD1 THR B 224 ? ARG B 242 ? THR B 1261 ARG B 1279 1 ? 19 
HELX_P HELX_P29 AD2 ASN B 251 ? PHE B 253 ? ASN B 1288 PHE B 1290 5 ? 3  
HELX_P HELX_P30 AD3 ASP B 254 ? GLN B 261 ? ASP B 1291 GLN B 1298 1 ? 8  
HELX_P HELX_P31 AD4 PRO B 272 ? TRP B 283 ? PRO B 1309 TRP B 1320 1 ? 12 
HELX_P HELX_P32 AD5 SER B 292 ? THR B 306 ? SER B 1329 THR B 1343 1 ? 15 
# 
_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 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 33  ? ILE A 34  ? VAL A 1070 ILE A 1071 
AA1 2 GLY A 107 ? CYS A 109 ? GLY A 1144 CYS A 1146 
AA1 3 LEU A 117 ? PRO A 121 ? LEU A 1154 PRO A 1158 
AA1 4 LYS A 67  ? SER A 74  ? LYS A 1104 SER A 1111 
AA1 5 GLY A 53  ? LEU A 61  ? GLY A 1090 LEU A 1098 
AA1 6 LEU A 39  ? GLY A 50  ? LEU A 1076 GLY A 1087 
AA2 1 CYS A 173 ? LEU A 175 ? CYS A 1210 LEU A 1212 
AA2 2 VAL A 181 ? VAL A 183 ? VAL A 1218 VAL A 1220 
AA3 1 SER A 199 ? VAL A 200 ? SER A 1236 VAL A 1237 
AA3 2 LYS A 207 ? LEU A 208 ? LYS A 1244 LEU A 1245 
AA4 1 VAL B 33  ? ILE B 34  ? VAL B 1070 ILE B 1071 
AA4 2 GLY B 107 ? CYS B 109 ? GLY B 1144 CYS B 1146 
AA4 3 LEU B 117 ? PRO B 121 ? LEU B 1154 PRO B 1158 
AA4 4 ILE B 68  ? SER B 74  ? ILE B 1105 SER B 1111 
AA4 5 CYS B 54  ? LEU B 60  ? CYS B 1091 LEU B 1097 
AA4 6 LEU B 39  ? ARG B 49  ? LEU B 1076 ARG B 1086 
AA5 1 CYS B 173 ? LEU B 175 ? CYS B 1210 LEU B 1212 
AA5 2 VAL B 181 ? VAL B 183 ? VAL B 1218 VAL B 1220 
AA6 1 TYR B 198 ? VAL B 200 ? TYR B 1235 VAL B 1237 
AA6 2 LYS B 207 ? PRO B 209 ? LYS B 1244 PRO B 1246 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 34  ? N ILE A 1071 O ILE A 108 ? O ILE A 1145 
AA1 2 3 N GLY A 107 ? N GLY A 1144 O VAL A 119 ? O VAL A 1156 
AA1 3 4 O VAL A 118 ? O VAL A 1155 N LYS A 73  ? N LYS A 1110 
AA1 4 5 O SER A 74  ? O SER A 1111 N CYS A 54  ? N CYS A 1091 
AA1 5 6 O VAL A 55  ? O VAL A 1092 N GLY A 48  ? N GLY A 1085 
AA2 1 2 N MET A 174 ? N MET A 1211 O LYS A 182 ? O LYS A 1219 
AA3 1 2 N SER A 199 ? N SER A 1236 O LEU A 208 ? O LEU A 1245 
AA4 1 2 N ILE B 34  ? N ILE B 1071 O ILE B 108 ? O ILE B 1145 
AA4 2 3 N CYS B 109 ? N CYS B 1146 O LEU B 117 ? O LEU B 1154 
AA4 3 4 O LEU B 120 ? O LEU B 1157 N ALA B 71  ? N ALA B 1108 
AA4 4 5 O CYS B 70  ? O CYS B 1107 N GLY B 58  ? N GLY B 1095 
AA4 5 6 O VAL B 55  ? O VAL B 1092 N GLY B 48  ? N GLY B 1085 
AA5 1 2 N MET B 174 ? N MET B 1211 O LYS B 182 ? O LYS B 1219 
AA6 1 2 N SER B 199 ? N SER B 1236 O LEU B 208 ? O LEU B 1245 
# 
_pdbx_entry_details.entry_id                   9IVB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OG B SER 1264 ? ? O   B HOH 1501 ? ? 2.00 
2 1 O  B ASP 1291 ? ? O   B HOH 1502 ? ? 2.03 
3 1 O  A HIS 1202 ? ? NH2 A ARG 1227 ? ? 2.06 
4 1 NZ A LYS 1190 ? ? O   A HOH 1501 ? ? 2.06 
5 1 O  B TRP 1249 ? ? OG  B SER 1268 ? ? 2.12 
6 1 O  B HOH 1523 ? ? O   B HOH 1534 ? ? 2.12 
7 1 N  B TYR 1295 ? ? O   B HOH 1502 ? ? 2.15 
8 1 O  B LYS 1248 ? ? O   B HOH 1503 ? ? 2.18 
9 1 OG A SER 1329 ? ? O   A HOH 1502 ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 1265 ? ? CG A ASP 1265 ? ? OD1 A ASP 1265 ? ? 127.36 118.30 9.06  0.90 N 
2 1 CB A ASP 1265 ? ? CG A ASP 1265 ? ? OD2 A ASP 1265 ? ? 109.32 118.30 -8.98 0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 1099 ? ? -105.14 -159.90 
2  1 ARG A 1203 ? ? 81.17   -14.77  
3  1 ASP A 1204 ? ? -143.14 50.23   
4  1 LEU B 1098 ? ? -102.18 -161.22 
5  1 ARG B 1203 ? ? 83.43   -14.37  
6  1 ALA B 1221 ? ? -124.93 -159.59 
7  1 ASP B 1228 ? ? 179.39  166.57  
8  1 LYS B 1240 ? ? -101.30 -62.65  
9  1 ARG B 1279 ? ? 62.76   -124.25 
10 1 THR B 1343 ? ? -104.33 -158.39 
# 
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 1038 ? A GLY 1   
2  1 Y 1 A ASP 1039 ? A ASP 2   
3  1 Y 1 A ARG 1148 ? A ARG 111 
4  1 Y 1 A SER 1149 ? A SER 112 
5  1 Y 1 A GLU 1150 ? A GLU 113 
6  1 Y 1 A ILE 1345 ? A ILE 308 
7  1 Y 1 A GLY 1346 ? A GLY 309 
8  1 Y 1 B GLY 1038 ? B GLY 1   
9  1 Y 1 B ASP 1039 ? B ASP 2   
10 1 Y 1 B SER 1040 ? B SER 3   
11 1 Y 1 B ASP 1041 ? B ASP 4   
12 1 Y 1 B ILE 1042 ? B ILE 5   
13 1 Y 1 B SER 1043 ? B SER 6   
14 1 Y 1 B SER 1044 ? B SER 7   
15 1 Y 1 B ASN 1100 ? B ASN 63  
16 1 Y 1 B ASP 1101 ? B ASP 64  
17 1 Y 1 B ARG 1148 ? B ARG 111 
18 1 Y 1 B SER 1149 ? B SER 112 
19 1 Y 1 B GLU 1150 ? B GLU 113 
20 1 Y 1 B GLY 1151 ? B GLY 114 
21 1 Y 1 B ILE 1345 ? B ILE 308 
22 1 Y 1 B GLY 1346 ? B GLY 309 
# 
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 
A1L3A CAA  C Y N 1   
A1L3A CAB  C Y N 2   
A1L3A CAC  C Y N 3   
A1L3A CAD  C Y N 4   
A1L3A CAI  C Y N 5   
A1L3A CAJ  C N N 6   
A1L3A CAM  C Y N 7   
A1L3A CAN  C Y N 8   
A1L3A CAO  C Y N 9   
A1L3A CAP  C Y N 10  
A1L3A CAQ  C Y N 11  
A1L3A CAR  C Y N 12  
A1L3A CAS  C Y N 13  
A1L3A CAT  C N N 14  
A1L3A CAZ  C Y N 15  
A1L3A CBA  C Y N 16  
A1L3A CBB  C Y N 17  
A1L3A CBC  C N N 18  
A1L3A CBD  C N N 19  
A1L3A CBE  C N N 20  
A1L3A FAU  F N N 21  
A1L3A FAV  F N N 22  
A1L3A FAW  F N N 23  
A1L3A NAE  N Y N 24  
A1L3A NAF  N Y N 25  
A1L3A NAG  N Y N 26  
A1L3A NAH  N Y N 27  
A1L3A NAK  N Y N 28  
A1L3A NAL  N Y N 29  
A1L3A NAX  N Y N 30  
A1L3A NAY  N Y N 31  
A1L3A H1   H N N 32  
A1L3A H2   H N N 33  
A1L3A H3   H N N 34  
A1L3A H4   H N N 35  
A1L3A H5   H N N 36  
A1L3A H6   H N N 37  
A1L3A H7   H N N 38  
A1L3A H8   H N N 39  
A1L3A H9   H N N 40  
A1L3A H10  H N N 41  
A1L3A H11  H N N 42  
A1L3A H12  H N N 43  
A1L3A H13  H N N 44  
A1L3A H14  H N N 45  
A1L3A H15  H N N 46  
ALA   N    N N N 47  
ALA   CA   C N S 48  
ALA   C    C N N 49  
ALA   O    O N N 50  
ALA   CB   C N N 51  
ALA   OXT  O N N 52  
ALA   H    H N N 53  
ALA   H2   H N N 54  
ALA   HA   H N N 55  
ALA   HB1  H N N 56  
ALA   HB2  H N N 57  
ALA   HB3  H N N 58  
ALA   HXT  H N N 59  
ARG   N    N N N 60  
ARG   CA   C N S 61  
ARG   C    C N N 62  
ARG   O    O N N 63  
ARG   CB   C N N 64  
ARG   CG   C N N 65  
ARG   CD   C N N 66  
ARG   NE   N N N 67  
ARG   CZ   C N N 68  
ARG   NH1  N N N 69  
ARG   NH2  N N N 70  
ARG   OXT  O N N 71  
ARG   H    H N N 72  
ARG   H2   H N N 73  
ARG   HA   H N N 74  
ARG   HB2  H N N 75  
ARG   HB3  H N N 76  
ARG   HG2  H N N 77  
ARG   HG3  H N N 78  
ARG   HD2  H N N 79  
ARG   HD3  H N N 80  
ARG   HE   H N N 81  
ARG   HH11 H N N 82  
ARG   HH12 H N N 83  
ARG   HH21 H N N 84  
ARG   HH22 H N N 85  
ARG   HXT  H N N 86  
ASN   N    N N N 87  
ASN   CA   C N S 88  
ASN   C    C N N 89  
ASN   O    O N N 90  
ASN   CB   C N N 91  
ASN   CG   C N N 92  
ASN   OD1  O N N 93  
ASN   ND2  N N N 94  
ASN   OXT  O N N 95  
ASN   H    H N N 96  
ASN   H2   H N N 97  
ASN   HA   H N N 98  
ASN   HB2  H N N 99  
ASN   HB3  H N N 100 
ASN   HD21 H N N 101 
ASN   HD22 H N N 102 
ASN   HXT  H N N 103 
ASP   N    N N N 104 
ASP   CA   C N S 105 
ASP   C    C N N 106 
ASP   O    O N N 107 
ASP   CB   C N N 108 
ASP   CG   C N N 109 
ASP   OD1  O N N 110 
ASP   OD2  O N N 111 
ASP   OXT  O N N 112 
ASP   H    H N N 113 
ASP   H2   H N N 114 
ASP   HA   H N N 115 
ASP   HB2  H N N 116 
ASP   HB3  H N N 117 
ASP   HD2  H N N 118 
ASP   HXT  H N N 119 
CYS   N    N N N 120 
CYS   CA   C N R 121 
CYS   C    C N N 122 
CYS   O    O N N 123 
CYS   CB   C N N 124 
CYS   SG   S N N 125 
CYS   OXT  O N N 126 
CYS   H    H N N 127 
CYS   H2   H N N 128 
CYS   HA   H N N 129 
CYS   HB2  H N N 130 
CYS   HB3  H N N 131 
CYS   HG   H N N 132 
CYS   HXT  H N N 133 
GLN   N    N N N 134 
GLN   CA   C N S 135 
GLN   C    C N N 136 
GLN   O    O N N 137 
GLN   CB   C N N 138 
GLN   CG   C N N 139 
GLN   CD   C N N 140 
GLN   OE1  O N N 141 
GLN   NE2  N N N 142 
GLN   OXT  O N N 143 
GLN   H    H N N 144 
GLN   H2   H N N 145 
GLN   HA   H N N 146 
GLN   HB2  H N N 147 
GLN   HB3  H N N 148 
GLN   HG2  H N N 149 
GLN   HG3  H N N 150 
GLN   HE21 H N N 151 
GLN   HE22 H N N 152 
GLN   HXT  H N N 153 
GLU   N    N N N 154 
GLU   CA   C N S 155 
GLU   C    C N N 156 
GLU   O    O N N 157 
GLU   CB   C N N 158 
GLU   CG   C N N 159 
GLU   CD   C N N 160 
GLU   OE1  O N N 161 
GLU   OE2  O N N 162 
GLU   OXT  O N N 163 
GLU   H    H N N 164 
GLU   H2   H N N 165 
GLU   HA   H N N 166 
GLU   HB2  H N N 167 
GLU   HB3  H N N 168 
GLU   HG2  H N N 169 
GLU   HG3  H N N 170 
GLU   HE2  H N N 171 
GLU   HXT  H N N 172 
GLY   N    N N N 173 
GLY   CA   C N N 174 
GLY   C    C N N 175 
GLY   O    O N N 176 
GLY   OXT  O N N 177 
GLY   H    H N N 178 
GLY   H2   H N N 179 
GLY   HA2  H N N 180 
GLY   HA3  H N N 181 
GLY   HXT  H N N 182 
HIS   N    N N N 183 
HIS   CA   C N S 184 
HIS   C    C N N 185 
HIS   O    O N N 186 
HIS   CB   C N N 187 
HIS   CG   C Y N 188 
HIS   ND1  N Y N 189 
HIS   CD2  C Y N 190 
HIS   CE1  C Y N 191 
HIS   NE2  N Y N 192 
HIS   OXT  O N N 193 
HIS   H    H N N 194 
HIS   H2   H N N 195 
HIS   HA   H N N 196 
HIS   HB2  H N N 197 
HIS   HB3  H N N 198 
HIS   HD1  H N N 199 
HIS   HD2  H N N 200 
HIS   HE1  H N N 201 
HIS   HE2  H N N 202 
HIS   HXT  H N N 203 
HOH   O    O N N 204 
HOH   H1   H N N 205 
HOH   H2   H N N 206 
ILE   N    N N N 207 
ILE   CA   C N S 208 
ILE   C    C N N 209 
ILE   O    O N N 210 
ILE   CB   C N S 211 
ILE   CG1  C N N 212 
ILE   CG2  C N N 213 
ILE   CD1  C N N 214 
ILE   OXT  O N N 215 
ILE   H    H N N 216 
ILE   H2   H N N 217 
ILE   HA   H N N 218 
ILE   HB   H N N 219 
ILE   HG12 H N N 220 
ILE   HG13 H N N 221 
ILE   HG21 H N N 222 
ILE   HG22 H N N 223 
ILE   HG23 H N N 224 
ILE   HD11 H N N 225 
ILE   HD12 H N N 226 
ILE   HD13 H N N 227 
ILE   HXT  H N N 228 
LEU   N    N N N 229 
LEU   CA   C N S 230 
LEU   C    C N N 231 
LEU   O    O N N 232 
LEU   CB   C N N 233 
LEU   CG   C N N 234 
LEU   CD1  C N N 235 
LEU   CD2  C N N 236 
LEU   OXT  O N N 237 
LEU   H    H N N 238 
LEU   H2   H N N 239 
LEU   HA   H N N 240 
LEU   HB2  H N N 241 
LEU   HB3  H N N 242 
LEU   HG   H N N 243 
LEU   HD11 H N N 244 
LEU   HD12 H N N 245 
LEU   HD13 H N N 246 
LEU   HD21 H N N 247 
LEU   HD22 H N N 248 
LEU   HD23 H N N 249 
LEU   HXT  H N N 250 
LYS   N    N N N 251 
LYS   CA   C N S 252 
LYS   C    C N N 253 
LYS   O    O N N 254 
LYS   CB   C N N 255 
LYS   CG   C N N 256 
LYS   CD   C N N 257 
LYS   CE   C N N 258 
LYS   NZ   N N N 259 
LYS   OXT  O N N 260 
LYS   H    H N N 261 
LYS   H2   H N N 262 
LYS   HA   H N N 263 
LYS   HB2  H N N 264 
LYS   HB3  H N N 265 
LYS   HG2  H N N 266 
LYS   HG3  H N N 267 
LYS   HD2  H N N 268 
LYS   HD3  H N N 269 
LYS   HE2  H N N 270 
LYS   HE3  H N N 271 
LYS   HZ1  H N N 272 
LYS   HZ2  H N N 273 
LYS   HZ3  H N N 274 
LYS   HXT  H N N 275 
MET   N    N N N 276 
MET   CA   C N S 277 
MET   C    C N N 278 
MET   O    O N N 279 
MET   CB   C N N 280 
MET   CG   C N N 281 
MET   SD   S N N 282 
MET   CE   C N N 283 
MET   OXT  O N N 284 
MET   H    H N N 285 
MET   H2   H N N 286 
MET   HA   H N N 287 
MET   HB2  H N N 288 
MET   HB3  H N N 289 
MET   HG2  H N N 290 
MET   HG3  H N N 291 
MET   HE1  H N N 292 
MET   HE2  H N N 293 
MET   HE3  H N N 294 
MET   HXT  H N N 295 
PHE   N    N N N 296 
PHE   CA   C N S 297 
PHE   C    C N N 298 
PHE   O    O N N 299 
PHE   CB   C N N 300 
PHE   CG   C Y N 301 
PHE   CD1  C Y N 302 
PHE   CD2  C Y N 303 
PHE   CE1  C Y N 304 
PHE   CE2  C Y N 305 
PHE   CZ   C Y N 306 
PHE   OXT  O N N 307 
PHE   H    H N N 308 
PHE   H2   H N N 309 
PHE   HA   H N N 310 
PHE   HB2  H N N 311 
PHE   HB3  H N N 312 
PHE   HD1  H N N 313 
PHE   HD2  H N N 314 
PHE   HE1  H N N 315 
PHE   HE2  H N N 316 
PHE   HZ   H N N 317 
PHE   HXT  H N N 318 
PRO   N    N N N 319 
PRO   CA   C N S 320 
PRO   C    C N N 321 
PRO   O    O N N 322 
PRO   CB   C N N 323 
PRO   CG   C N N 324 
PRO   CD   C N N 325 
PRO   OXT  O N N 326 
PRO   H    H N N 327 
PRO   HA   H N N 328 
PRO   HB2  H N N 329 
PRO   HB3  H N N 330 
PRO   HG2  H N N 331 
PRO   HG3  H N N 332 
PRO   HD2  H N N 333 
PRO   HD3  H N N 334 
PRO   HXT  H N N 335 
SER   N    N N N 336 
SER   CA   C N S 337 
SER   C    C N N 338 
SER   O    O N N 339 
SER   CB   C N N 340 
SER   OG   O N N 341 
SER   OXT  O N N 342 
SER   H    H N N 343 
SER   H2   H N N 344 
SER   HA   H N N 345 
SER   HB2  H N N 346 
SER   HB3  H N N 347 
SER   HG   H N N 348 
SER   HXT  H N N 349 
THR   N    N N N 350 
THR   CA   C N S 351 
THR   C    C N N 352 
THR   O    O N N 353 
THR   CB   C N R 354 
THR   OG1  O N N 355 
THR   CG2  C N N 356 
THR   OXT  O N N 357 
THR   H    H N N 358 
THR   H2   H N N 359 
THR   HA   H N N 360 
THR   HB   H N N 361 
THR   HG1  H N N 362 
THR   HG21 H N N 363 
THR   HG22 H N N 364 
THR   HG23 H N N 365 
THR   HXT  H N N 366 
TRP   N    N N N 367 
TRP   CA   C N S 368 
TRP   C    C N N 369 
TRP   O    O N N 370 
TRP   CB   C N N 371 
TRP   CG   C Y N 372 
TRP   CD1  C Y N 373 
TRP   CD2  C Y N 374 
TRP   NE1  N Y N 375 
TRP   CE2  C Y N 376 
TRP   CE3  C Y N 377 
TRP   CZ2  C Y N 378 
TRP   CZ3  C Y N 379 
TRP   CH2  C Y N 380 
TRP   OXT  O N N 381 
TRP   H    H N N 382 
TRP   H2   H N N 383 
TRP   HA   H N N 384 
TRP   HB2  H N N 385 
TRP   HB3  H N N 386 
TRP   HD1  H N N 387 
TRP   HE1  H N N 388 
TRP   HE3  H N N 389 
TRP   HZ2  H N N 390 
TRP   HZ3  H N N 391 
TRP   HH2  H N N 392 
TRP   HXT  H N N 393 
TYR   N    N N N 394 
TYR   CA   C N S 395 
TYR   C    C N N 396 
TYR   O    O N N 397 
TYR   CB   C N N 398 
TYR   CG   C Y N 399 
TYR   CD1  C Y N 400 
TYR   CD2  C Y N 401 
TYR   CE1  C Y N 402 
TYR   CE2  C Y N 403 
TYR   CZ   C Y N 404 
TYR   OH   O N N 405 
TYR   OXT  O N N 406 
TYR   H    H N N 407 
TYR   H2   H N N 408 
TYR   HA   H N N 409 
TYR   HB2  H N N 410 
TYR   HB3  H N N 411 
TYR   HD1  H N N 412 
TYR   HD2  H N N 413 
TYR   HE1  H N N 414 
TYR   HE2  H N N 415 
TYR   HH   H N N 416 
TYR   HXT  H N N 417 
VAL   N    N N N 418 
VAL   CA   C N S 419 
VAL   C    C N N 420 
VAL   O    O N N 421 
VAL   CB   C N N 422 
VAL   CG1  C N N 423 
VAL   CG2  C N N 424 
VAL   OXT  O N N 425 
VAL   H    H N N 426 
VAL   H2   H N N 427 
VAL   HA   H N N 428 
VAL   HB   H N N 429 
VAL   HG11 H N N 430 
VAL   HG12 H N N 431 
VAL   HG13 H N N 432 
VAL   HG21 H N N 433 
VAL   HG22 H N N 434 
VAL   HG23 H N N 435 
VAL   HXT  H N N 436 
# 
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 
A1L3A CAT NAL  sing N N 1   
A1L3A NAL CAM  sing Y N 2   
A1L3A NAL NAK  sing Y N 3   
A1L3A CAM CAN  doub Y N 4   
A1L3A NAK CAS  doub Y N 5   
A1L3A CAN CAS  sing Y N 6   
A1L3A CAN CAO  sing Y N 7   
A1L3A CAS CAR  sing Y N 8   
A1L3A CAO CAP  doub Y N 9   
A1L3A CAR CAQ  doub Y N 10  
A1L3A CAP CAQ  sing Y N 11  
A1L3A CAP CAJ  sing N N 12  
A1L3A FAV CAJ  sing N N 13  
A1L3A CAQ FAU  sing N N 14  
A1L3A FAW CAJ  sing N N 15  
A1L3A NAY CAZ  doub Y N 16  
A1L3A NAY NAX  sing Y N 17  
A1L3A CAJ CAI  sing N N 18  
A1L3A CAZ CBA  sing Y N 19  
A1L3A CBD CBC  sing N N 20  
A1L3A CBD CBE  sing N N 21  
A1L3A NAX CBC  sing N N 22  
A1L3A NAX CBB  sing Y N 23  
A1L3A CBC CBE  sing N N 24  
A1L3A NAE NAF  sing Y N 25  
A1L3A NAE CAD  doub Y N 26  
A1L3A CBA CBB  doub Y N 27  
A1L3A CBA CAD  sing N N 28  
A1L3A CAI NAF  sing Y N 29  
A1L3A CAI NAG  doub Y N 30  
A1L3A NAF CAA  sing Y N 31  
A1L3A CAD CAC  sing Y N 32  
A1L3A NAG NAH  sing Y N 33  
A1L3A CAA NAH  doub Y N 34  
A1L3A CAA CAB  sing Y N 35  
A1L3A CAC CAB  doub Y N 36  
A1L3A CAB H1   sing N N 37  
A1L3A CAC H2   sing N N 38  
A1L3A CAM H3   sing N N 39  
A1L3A CAO H4   sing N N 40  
A1L3A CAR H5   sing N N 41  
A1L3A CAT H6   sing N N 42  
A1L3A CAT H7   sing N N 43  
A1L3A CAT H8   sing N N 44  
A1L3A CAZ H9   sing N N 45  
A1L3A CBB H10  sing N N 46  
A1L3A CBC H11  sing N N 47  
A1L3A CBD H12  sing N N 48  
A1L3A CBD H13  sing N N 49  
A1L3A CBE H14  sing N N 50  
A1L3A CBE H15  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5EOB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9IVB 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.018326 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000539 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015113 
_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]   0.012566 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
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 3   ? 19.212  -28.177 18.557  1.00 16.54 ?  1040 SER   A N   1 
ATOM   2    C CA  . SER   A 1 3   ? 20.132  -29.288 18.765  1.00 25.77 ?  1040 SER   A CA  1 
ATOM   3    C C   . SER   A 1 3   ? 19.422  -30.487 19.381  1.00 34.83 ?  1040 SER   A C   1 
ATOM   4    O O   . SER   A 1 3   ? 19.842  -31.630 19.200  1.00 37.64 ?  1040 SER   A O   1 
ATOM   5    C CB  . SER   A 1 3   ? 21.300  -28.864 19.660  1.00 29.72 ?  1040 SER   A CB  1 
ATOM   6    O OG  . SER   A 1 3   ? 22.007  -27.767 19.107  1.00 23.89 ?  1040 SER   A OG  1 
ATOM   7    N N   . ASP   A 1 4   ? 18.341  -30.224 20.106  1.00 22.73 ?  1041 ASP   A N   1 
ATOM   8    C CA  . ASP   A 1 4   ? 17.656  -31.245 20.883  1.00 28.43 ?  1041 ASP   A CA  1 
ATOM   9    C C   . ASP   A 1 4   ? 16.269  -31.528 20.318  1.00 22.80 ?  1041 ASP   A C   1 
ATOM   10   O O   . ASP   A 1 4   ? 15.743  -30.792 19.478  1.00 19.68 ?  1041 ASP   A O   1 
ATOM   11   C CB  . ASP   A 1 4   ? 17.546  -30.821 22.353  1.00 29.78 ?  1041 ASP   A CB  1 
ATOM   12   C CG  . ASP   A 1 4   ? 18.883  -30.825 23.062  1.00 27.08 ?  1041 ASP   A CG  1 
ATOM   13   O OD1 . ASP   A 1 4   ? 19.564  -31.872 23.040  1.00 19.03 ?  1041 ASP   A OD1 1 
ATOM   14   O OD2 . ASP   A 1 4   ? 19.252  -29.783 23.645  1.00 23.62 -1 1041 ASP   A OD2 1 
ATOM   15   N N   . ILE   A 1 5   ? 15.686  -32.626 20.809  1.00 22.15 ?  1042 ILE   A N   1 
ATOM   16   C CA  . ILE   A 1 5   ? 14.314  -32.992 20.474  1.00 25.15 ?  1042 ILE   A CA  1 
ATOM   17   C C   . ILE   A 1 5   ? 13.316  -32.081 21.171  1.00 25.34 ?  1042 ILE   A C   1 
ATOM   18   O O   . ILE   A 1 5   ? 12.196  -31.894 20.680  1.00 18.49 ?  1042 ILE   A O   1 
ATOM   19   C CB  . ILE   A 1 5   ? 14.090  -34.494 20.789  1.00 22.27 ?  1042 ILE   A CB  1 
ATOM   20   C CG1 . ILE   A 1 5   ? 14.206  -34.857 22.288  1.00 25.69 ?  1042 ILE   A CG1 1 
ATOM   21   C CG2 . ILE   A 1 5   ? 15.061  -35.339 19.998  1.00 23.18 ?  1042 ILE   A CG2 1 
ATOM   22   C CD1 . ILE   A 1 5   ? 13.027  -34.490 23.192  1.00 29.85 ?  1042 ILE   A CD1 1 
ATOM   23   N N   . SER   A 1 6   ? 13.711  -31.480 22.289  1.00 26.16 ?  1043 SER   A N   1 
ATOM   24   C CA  . SER   A 1 6   ? 12.797  -30.757 23.160  1.00 21.69 ?  1043 SER   A CA  1 
ATOM   25   C C   . SER   A 1 6   ? 12.795  -29.255 22.930  1.00 12.22 ?  1043 SER   A C   1 
ATOM   26   O O   . SER   A 1 6   ? 11.774  -28.605 23.178  1.00 14.82 ?  1043 SER   A O   1 
ATOM   27   C CB  . SER   A 1 6   ? 13.151  -31.041 24.621  1.00 21.08 ?  1043 SER   A CB  1 
ATOM   28   O OG  . SER   A 1 6   ? 14.518  -30.755 24.862  1.00 22.98 ?  1043 SER   A OG  1 
ATOM   29   N N   . SER   A 1 7   ? 13.906  -28.682 22.462  1.00 13.22 ?  1044 SER   A N   1 
ATOM   30   C CA  . SER   A 1 7   ? 14.022  -27.232 22.297  1.00 14.02 ?  1044 SER   A CA  1 
ATOM   31   C C   . SER   A 1 7   ? 14.520  -26.858 20.902  1.00 15.41 ?  1044 SER   A C   1 
ATOM   32   O O   . SER   A 1 7   ? 15.462  -26.079 20.759  1.00 19.84 ?  1044 SER   A O   1 
ATOM   33   C CB  . SER   A 1 7   ? 14.952  -26.668 23.365  1.00 12.38 ?  1044 SER   A CB  1 
ATOM   34   O OG  . SER   A 1 7   ? 14.619  -27.178 24.644  1.00 13.00 ?  1044 SER   A OG  1 
ATOM   35   N N   . PRO   A 1 8   ? 13.900  -27.380 19.843  1.00 15.41 ?  1045 PRO   A N   1 
ATOM   36   C CA  . PRO   A 1 8   ? 14.393  -27.064 18.501  1.00 16.17 ?  1045 PRO   A CA  1 
ATOM   37   C C   . PRO   A 1 8   ? 14.077  -25.625 18.134  1.00 21.10 ?  1045 PRO   A C   1 
ATOM   38   O O   . PRO   A 1 8   ? 13.106  -25.036 18.614  1.00 21.27 ?  1045 PRO   A O   1 
ATOM   39   C CB  . PRO   A 1 8   ? 13.632  -28.045 17.608  1.00 15.00 ?  1045 PRO   A CB  1 
ATOM   40   C CG  . PRO   A 1 8   ? 12.338  -28.214 18.304  1.00 14.16 ?  1045 PRO   A CG  1 
ATOM   41   C CD  . PRO   A 1 8   ? 12.649  -28.160 19.780  1.00 12.30 ?  1045 PRO   A CD  1 
ATOM   42   N N   . LEU   A 1 9   ? 14.924  -25.058 17.279  1.00 21.34 ?  1046 LEU   A N   1 
ATOM   43   C CA  . LEU   A 1 9   ? 14.683  -23.715 16.776  1.00 23.05 ?  1046 LEU   A CA  1 
ATOM   44   C C   . LEU   A 1 9   ? 13.345  -23.661 16.043  1.00 25.72 ?  1046 LEU   A C   1 
ATOM   45   O O   . LEU   A 1 9   ? 12.836  -24.671 15.548  1.00 22.53 ?  1046 LEU   A O   1 
ATOM   46   C CB  . LEU   A 1 9   ? 15.811  -23.279 15.841  1.00 22.24 ?  1046 LEU   A CB  1 
ATOM   47   C CG  . LEU   A 1 9   ? 17.206  -23.016 16.415  1.00 29.56 ?  1046 LEU   A CG  1 
ATOM   48   C CD1 . LEU   A 1 9   ? 17.898  -21.948 15.592  1.00 30.53 ?  1046 LEU   A CD1 1 
ATOM   49   C CD2 . LEU   A 1 9   ? 17.157  -22.608 17.875  1.00 26.11 ?  1046 LEU   A CD2 1 
ATOM   50   N N   . LEU   A 1 10  ? 12.776  -22.455 15.978  1.00 26.91 ?  1047 LEU   A N   1 
ATOM   51   C CA  . LEU   A 1 10  ? 11.446  -22.288 15.397  1.00 24.04 ?  1047 LEU   A CA  1 
ATOM   52   C C   . LEU   A 1 10  ? 11.411  -22.756 13.948  1.00 21.57 ?  1047 LEU   A C   1 
ATOM   53   O O   . LEU   A 1 10  ? 10.515  -23.509 13.550  1.00 28.76 ?  1047 LEU   A O   1 
ATOM   54   C CB  . LEU   A 1 10  ? 11.004  -20.827 15.512  1.00 24.08 ?  1047 LEU   A CB  1 
ATOM   55   C CG  . LEU   A 1 10  ? 9.848   -20.337 14.634  1.00 25.38 ?  1047 LEU   A CG  1 
ATOM   56   C CD1 . LEU   A 1 10  ? 9.057   -19.293 15.384  1.00 24.11 ?  1047 LEU   A CD1 1 
ATOM   57   C CD2 . LEU   A 1 10  ? 10.351  -19.743 13.321  1.00 19.86 ?  1047 LEU   A CD2 1 
ATOM   58   N N   . GLN   A 1 11  ? 12.383  -22.318 13.141  1.00 20.47 ?  1048 GLN   A N   1 
ATOM   59   C CA  . GLN   A 1 11  ? 12.386  -22.674 11.725  1.00 22.88 ?  1048 GLN   A CA  1 
ATOM   60   C C   . GLN   A 1 11  ? 12.456  -24.181 11.526  1.00 20.71 ?  1048 GLN   A C   1 
ATOM   61   O O   . GLN   A 1 11  ? 11.945  -24.700 10.527  1.00 16.70 ?  1048 GLN   A O   1 
ATOM   62   C CB  . GLN   A 1 11  ? 13.553  -21.992 11.012  1.00 26.54 ?  1048 GLN   A CB  1 
ATOM   63   C CG  . GLN   A 1 11  ? 13.218  -20.629 10.428  1.00 28.56 ?  1048 GLN   A CG  1 
ATOM   64   C CD  . GLN   A 1 11  ? 13.823  -20.420 9.053   1.00 28.34 ?  1048 GLN   A CD  1 
ATOM   65   O OE1 . GLN   A 1 11  ? 14.095  -21.378 8.329   1.00 25.44 ?  1048 GLN   A OE1 1 
ATOM   66   N NE2 . GLN   A 1 11  ? 14.039  -19.162 8.685   1.00 30.03 ?  1048 GLN   A NE2 1 
ATOM   67   N N   . ASN   A 1 12  ? 13.075  -24.898 12.463  1.00 19.43 ?  1049 ASN   A N   1 
ATOM   68   C CA  . ASN   A 1 12  ? 13.145  -26.348 12.374  1.00 19.03 ?  1049 ASN   A CA  1 
ATOM   69   C C   . ASN   A 1 12  ? 11.853  -27.025 12.812  1.00 19.27 ?  1049 ASN   A C   1 
ATOM   70   O O   . ASN   A 1 12  ? 11.580  -28.143 12.365  1.00 18.88 ?  1049 ASN   A O   1 
ATOM   71   C CB  . ASN   A 1 12  ? 14.316  -26.869 13.208  1.00 17.78 ?  1049 ASN   A CB  1 
ATOM   72   C CG  . ASN   A 1 12  ? 15.657  -26.607 12.552  1.00 17.74 ?  1049 ASN   A CG  1 
ATOM   73   O OD1 . ASN   A 1 12  ? 15.779  -26.640 11.327  1.00 14.93 ?  1049 ASN   A OD1 1 
ATOM   74   N ND2 . ASN   A 1 12  ? 16.671  -26.342 13.365  1.00 16.20 ?  1049 ASN   A ND2 1 
ATOM   75   N N   . THR   A 1 13  ? 11.049  -26.378 13.662  1.00 20.57 ?  1050 THR   A N   1 
ATOM   76   C CA  . THR   A 1 13  ? 9.776   -26.969 14.063  1.00 22.08 ?  1050 THR   A CA  1 
ATOM   77   C C   . THR   A 1 13  ? 8.843   -27.177 12.878  1.00 17.50 ?  1050 THR   A C   1 
ATOM   78   O O   . THR   A 1 13  ? 7.881   -27.944 12.987  1.00 18.10 ?  1050 THR   A O   1 
ATOM   79   C CB  . THR   A 1 13  ? 9.088   -26.104 15.122  1.00 26.06 ?  1050 THR   A CB  1 
ATOM   80   O OG1 . THR   A 1 13  ? 8.826   -24.800 14.588  1.00 21.54 ?  1050 THR   A OG1 1 
ATOM   81   C CG2 . THR   A 1 13  ? 9.966   -25.980 16.358  1.00 22.48 ?  1050 THR   A CG2 1 
ATOM   82   N N   . VAL   A 1 14  ? 9.099   -26.503 11.755  1.00 17.95 ?  1051 VAL   A N   1 
ATOM   83   C CA  . VAL   A 1 14  ? 8.432   -26.856 10.506  1.00 18.40 ?  1051 VAL   A CA  1 
ATOM   84   C C   . VAL   A 1 14  ? 8.817   -28.269 10.090  1.00 17.65 ?  1051 VAL   A C   1 
ATOM   85   O O   . VAL   A 1 14  ? 7.968   -29.074 9.690   1.00 15.57 ?  1051 VAL   A O   1 
ATOM   86   C CB  . VAL   A 1 14  ? 8.775   -25.833 9.409   1.00 17.12 ?  1051 VAL   A CB  1 
ATOM   87   C CG1 . VAL   A 1 14  ? 8.344   -26.355 8.052   1.00 16.51 ?  1051 VAL   A CG1 1 
ATOM   88   C CG2 . VAL   A 1 14  ? 8.117   -24.495 9.709   1.00 18.35 ?  1051 VAL   A CG2 1 
ATOM   89   N N   . HIS   A 1 15  ? 10.110  -28.591 10.179  1.00 16.03 ?  1052 HIS   A N   1 
ATOM   90   C CA  . HIS   A 1 15  ? 10.561  -29.946 9.880   1.00 17.96 ?  1052 HIS   A CA  1 
ATOM   91   C C   . HIS   A 1 15  ? 9.977   -30.950 10.866  1.00 16.99 ?  1052 HIS   A C   1 
ATOM   92   O O   . HIS   A 1 15  ? 9.568   -32.050 10.477  1.00 16.12 ?  1052 HIS   A O   1 
ATOM   93   C CB  . HIS   A 1 15  ? 12.088  -30.010 9.907   1.00 12.46 ?  1052 HIS   A CB  1 
ATOM   94   C CG  . HIS   A 1 15  ? 12.739  -29.558 8.638   1.00 15.07 ?  1052 HIS   A CG  1 
ATOM   95   N ND1 . HIS   A 1 15  ? 13.742  -28.613 8.613   1.00 16.06 ?  1052 HIS   A ND1 1 
ATOM   96   C CD2 . HIS   A 1 15  ? 12.538  -29.928 7.351   1.00 12.85 ?  1052 HIS   A CD2 1 
ATOM   97   C CE1 . HIS   A 1 15  ? 14.129  -28.418 7.365   1.00 14.83 ?  1052 HIS   A CE1 1 
ATOM   98   N NE2 . HIS   A 1 15  ? 13.413  -29.203 6.580   1.00 14.10 ?  1052 HIS   A NE2 1 
ATOM   99   N N   . ILE   A 1 16  ? 9.924   -30.586 12.147  1.00 14.67 ?  1053 ILE   A N   1 
ATOM   100  C CA  . ILE   A 1 16  ? 9.495   -31.529 13.177  1.00 16.77 ?  1053 ILE   A CA  1 
ATOM   101  C C   . ILE   A 1 16  ? 7.992   -31.766 13.095  1.00 16.37 ?  1053 ILE   A C   1 
ATOM   102  O O   . ILE   A 1 16  ? 7.536   -32.888 12.846  1.00 21.68 ?  1053 ILE   A O   1 
ATOM   103  C CB  . ILE   A 1 16  ? 9.913   -31.032 14.572  1.00 19.34 ?  1053 ILE   A CB  1 
ATOM   104  C CG1 . ILE   A 1 16  ? 11.431  -31.120 14.734  1.00 16.94 ?  1053 ILE   A CG1 1 
ATOM   105  C CG2 . ILE   A 1 16  ? 9.219   -31.837 15.658  1.00 16.28 ?  1053 ILE   A CG2 1 
ATOM   106  C CD1 . ILE   A 1 16  ? 12.096  -29.794 14.963  1.00 16.57 ?  1053 ILE   A CD1 1 
ATOM   107  N N   . ASP   A 1 17  ? 7.199   -30.716 13.301  1.00 15.94 ?  1054 ASP   A N   1 
ATOM   108  C CA  . ASP   A 1 17  ? 5.753   -30.869 13.404  1.00 16.15 ?  1054 ASP   A CA  1 
ATOM   109  C C   . ASP   A 1 17  ? 5.054   -30.973 12.053  1.00 15.56 ?  1054 ASP   A C   1 
ATOM   110  O O   . ASP   A 1 17  ? 3.837   -31.179 12.024  1.00 18.56 ?  1054 ASP   A O   1 
ATOM   111  C CB  . ASP   A 1 17  ? 5.158   -29.709 14.205  1.00 11.44 ?  1054 ASP   A CB  1 
ATOM   112  C CG  . ASP   A 1 17  ? 5.644   -29.686 15.641  1.00 16.29 ?  1054 ASP   A CG  1 
ATOM   113  O OD1 . ASP   A 1 17  ? 6.766   -29.195 15.884  1.00 22.55 ?  1054 ASP   A OD1 1 
ATOM   114  O OD2 . ASP   A 1 17  ? 4.907   -30.166 16.528  1.00 18.93 -1 1054 ASP   A OD2 1 
ATOM   115  N N   . LEU   A 1 18  ? 5.779   -30.838 10.941  1.00 17.23 ?  1055 LEU   A N   1 
ATOM   116  C CA  . LEU   A 1 18  ? 5.214   -31.015 9.603   1.00 16.40 ?  1055 LEU   A CA  1 
ATOM   117  C C   . LEU   A 1 18  ? 6.156   -31.915 8.799   1.00 14.23 ?  1055 LEU   A C   1 
ATOM   118  O O   . LEU   A 1 18  ? 6.764   -31.492 7.814   1.00 15.32 ?  1055 LEU   A O   1 
ATOM   119  C CB  . LEU   A 1 18  ? 4.986   -29.672 8.907   1.00 16.37 ?  1055 LEU   A CB  1 
ATOM   120  C CG  . LEU   A 1 18  ? 3.953   -28.728 9.524   1.00 16.44 ?  1055 LEU   A CG  1 
ATOM   121  C CD1 . LEU   A 1 18  ? 4.002   -27.367 8.845   1.00 18.94 ?  1055 LEU   A CD1 1 
ATOM   122  C CD2 . LEU   A 1 18  ? 2.558   -29.326 9.436   1.00 12.04 ?  1055 LEU   A CD2 1 
ATOM   123  N N   . SER   A 1 19  ? 6.269   -33.171 9.231   1.00 19.62 ?  1056 SER   A N   1 
ATOM   124  C CA  . SER   A 1 19  ? 7.141   -34.135 8.572   1.00 14.19 ?  1056 SER   A CA  1 
ATOM   125  C C   . SER   A 1 19  ? 6.559   -34.676 7.273   1.00 13.77 ?  1056 SER   A C   1 
ATOM   126  O O   . SER   A 1 19  ? 7.293   -35.296 6.498   1.00 12.26 ?  1056 SER   A O   1 
ATOM   127  C CB  . SER   A 1 19  ? 7.443   -35.297 9.519   1.00 16.82 ?  1056 SER   A CB  1 
ATOM   128  O OG  . SER   A 1 19  ? 7.741   -34.822 10.820  1.00 20.79 ?  1056 SER   A OG  1 
ATOM   129  N N   . ALA   A 1 20  ? 5.270   -34.458 7.016   1.00 15.60 ?  1057 ALA   A N   1 
ATOM   130  C CA  . ALA   A 1 20  ? 4.617   -34.949 5.812   1.00 18.06 ?  1057 ALA   A CA  1 
ATOM   131  C C   . ALA   A 1 20  ? 4.504   -33.879 4.732   1.00 13.66 ?  1057 ALA   A C   1 
ATOM   132  O O   . ALA   A 1 20  ? 3.633   -33.976 3.863   1.00 12.68 ?  1057 ALA   A O   1 
ATOM   133  C CB  . ALA   A 1 20  ? 3.234   -35.506 6.152   1.00 14.02 ?  1057 ALA   A CB  1 
ATOM   134  N N   . LEU   A 1 21  ? 5.370   -32.870 4.762   1.00 14.47 ?  1058 LEU   A N   1 
ATOM   135  C CA  . LEU   A 1 21  ? 5.296   -31.755 3.831   1.00 13.75 ?  1058 LEU   A CA  1 
ATOM   136  C C   . LEU   A 1 21  ? 6.369   -31.857 2.754   1.00 12.84 ?  1058 LEU   A C   1 
ATOM   137  O O   . LEU   A 1 21  ? 7.463   -32.381 2.981   1.00 12.38 ?  1058 LEU   A O   1 
ATOM   138  C CB  . LEU   A 1 21  ? 5.441   -30.419 4.563   1.00 15.93 ?  1058 LEU   A CB  1 
ATOM   139  C CG  . LEU   A 1 21  ? 4.172   -29.581 4.730   1.00 18.08 ?  1058 LEU   A CG  1 
ATOM   140  C CD1 . LEU   A 1 21  ? 4.524   -28.131 5.031   1.00 14.85 ?  1058 LEU   A CD1 1 
ATOM   141  C CD2 . LEU   A 1 21  ? 3.292   -29.682 3.496   1.00 21.94 ?  1058 LEU   A CD2 1 
ATOM   142  N N   . ASN   A 1 22  ? 6.028   -31.351 1.576   1.00 11.37 ?  1059 ASN   A N   1 
ATOM   143  C CA  . ASN   A 1 22  ? 6.999   -31.145 0.513   1.00 12.45 ?  1059 ASN   A CA  1 
ATOM   144  C C   . ASN   A 1 22  ? 8.200   -30.371 1.054   1.00 11.07 ?  1059 ASN   A C   1 
ATOM   145  O O   . ASN   A 1 22  ? 8.028   -29.478 1.894   1.00 13.17 ?  1059 ASN   A O   1 
ATOM   146  C CB  . ASN   A 1 22  ? 6.337   -30.365 -0.630  1.00 13.14 ?  1059 ASN   A CB  1 
ATOM   147  C CG  . ASN   A 1 22  ? 7.008   -30.581 -1.972  1.00 11.83 ?  1059 ASN   A CG  1 
ATOM   148  O OD1 . ASN   A 1 22  ? 8.224   -30.458 -2.105  1.00 12.81 ?  1059 ASN   A OD1 1 
ATOM   149  N ND2 . ASN   A 1 22  ? 6.206   -30.882 -2.987  1.00 11.23 ?  1059 ASN   A ND2 1 
ATOM   150  N N   . PRO   A 1 23  ? 9.427   -30.699 0.634   1.00 14.78 ?  1060 PRO   A N   1 
ATOM   151  C CA  . PRO   A 1 23  ? 10.552  -29.802 0.956   1.00 15.44 ?  1060 PRO   A CA  1 
ATOM   152  C C   . PRO   A 1 23  ? 10.332  -28.400 0.416   1.00 13.30 ?  1060 PRO   A C   1 
ATOM   153  O O   . PRO   A 1 23  ? 10.575  -27.411 1.121   1.00 15.04 ?  1060 PRO   A O   1 
ATOM   154  C CB  . PRO   A 1 23  ? 11.752  -30.498 0.298   1.00 12.90 ?  1060 PRO   A CB  1 
ATOM   155  C CG  . PRO   A 1 23  ? 11.361  -31.927 0.213   1.00 14.78 ?  1060 PRO   A CG  1 
ATOM   156  C CD  . PRO   A 1 23  ? 9.879   -31.941 -0.018  1.00 13.74 ?  1060 PRO   A CD  1 
ATOM   157  N N   . GLU   A 1 24  ? 9.875   -28.303 -0.838  1.00 12.08 ?  1061 GLU   A N   1 
ATOM   158  C CA  . GLU   A 1 24  ? 9.432   -27.035 -1.409  1.00 11.14 ?  1061 GLU   A CA  1 
ATOM   159  C C   . GLU   A 1 24  ? 8.509   -26.286 -0.458  1.00 12.93 ?  1061 GLU   A C   1 
ATOM   160  O O   . GLU   A 1 24  ? 8.626   -25.067 -0.293  1.00 21.23 ?  1061 GLU   A O   1 
ATOM   161  C CB  . GLU   A 1 24  ? 8.719   -27.307 -2.733  1.00 15.33 ?  1061 GLU   A CB  1 
ATOM   162  C CG  . GLU   A 1 24  ? 8.970   -26.317 -3.842  1.00 17.68 ?  1061 GLU   A CG  1 
ATOM   163  C CD  . GLU   A 1 24  ? 8.293   -26.747 -5.127  1.00 25.90 ?  1061 GLU   A CD  1 
ATOM   164  O OE1 . GLU   A 1 24  ? 7.048   -26.839 -5.135  1.00 27.41 ?  1061 GLU   A OE1 1 
ATOM   165  O OE2 . GLU   A 1 24  ? 9.001   -27.008 -6.121  1.00 29.36 -1 1061 GLU   A OE2 1 
ATOM   166  N N   . LEU   A 1 25  ? 7.593   -27.007 0.188   1.00 11.74 ?  1062 LEU   A N   1 
ATOM   167  C CA  . LEU   A 1 25  ? 6.616   -26.380 1.069   1.00 13.09 ?  1062 LEU   A CA  1 
ATOM   168  C C   . LEU   A 1 25  ? 7.177   -26.135 2.460   1.00 15.81 ?  1062 LEU   A C   1 
ATOM   169  O O   . LEU   A 1 25  ? 6.697   -25.242 3.167   1.00 14.95 ?  1062 LEU   A O   1 
ATOM   170  C CB  . LEU   A 1 25  ? 5.367   -27.251 1.163   1.00 13.50 ?  1062 LEU   A CB  1 
ATOM   171  C CG  . LEU   A 1 25  ? 4.234   -27.032 0.166   1.00 12.49 ?  1062 LEU   A CG  1 
ATOM   172  C CD1 . LEU   A 1 25  ? 4.748   -26.789 -1.240  1.00 14.31 ?  1062 LEU   A CD1 1 
ATOM   173  C CD2 . LEU   A 1 25  ? 3.400   -28.274 0.191   1.00 13.79 ?  1062 LEU   A CD2 1 
ATOM   174  N N   . VAL   A 1 26  ? 8.168   -26.927 2.874   1.00 17.96 ?  1063 VAL   A N   1 
ATOM   175  C CA  . VAL   A 1 26  ? 8.845   -26.670 4.141   1.00 16.61 ?  1063 VAL   A CA  1 
ATOM   176  C C   . VAL   A 1 26  ? 9.422   -25.262 4.144   1.00 18.14 ?  1063 VAL   A C   1 
ATOM   177  O O   . VAL   A 1 26  ? 9.231   -24.493 5.093   1.00 16.99 ?  1063 VAL   A O   1 
ATOM   178  C CB  . VAL   A 1 26  ? 9.933   -27.730 4.390   1.00 14.01 ?  1063 VAL   A CB  1 
ATOM   179  C CG1 . VAL   A 1 26  ? 11.015  -27.181 5.305   1.00 15.02 ?  1063 VAL   A CG1 1 
ATOM   180  C CG2 . VAL   A 1 26  ? 9.319   -28.988 4.977   1.00 15.69 ?  1063 VAL   A CG2 1 
ATOM   181  N N   . GLN   A 1 27  ? 10.114  -24.896 3.063   1.00 18.67 ?  1064 GLN   A N   1 
ATOM   182  C CA  . GLN   A 1 27  ? 10.652  -23.546 2.939   1.00 20.65 ?  1064 GLN   A CA  1 
ATOM   183  C C   . GLN   A 1 27  ? 9.545   -22.511 2.780   1.00 18.74 ?  1064 GLN   A C   1 
ATOM   184  O O   . GLN   A 1 27  ? 9.693   -21.374 3.241   1.00 17.70 ?  1064 GLN   A O   1 
ATOM   185  C CB  . GLN   A 1 27  ? 11.618  -23.484 1.755   1.00 18.07 ?  1064 GLN   A CB  1 
ATOM   186  C CG  . GLN   A 1 27  ? 12.320  -22.150 1.579   1.00 21.23 ?  1064 GLN   A CG  1 
ATOM   187  C CD  . GLN   A 1 27  ? 12.852  -21.961 0.173   1.00 21.29 ?  1064 GLN   A CD  1 
ATOM   188  O OE1 . GLN   A 1 27  ? 12.514  -22.719 -0.738  1.00 19.87 ?  1064 GLN   A OE1 1 
ATOM   189  N NE2 . GLN   A 1 27  ? 13.690  -20.948 -0.013  1.00 19.91 ?  1064 GLN   A NE2 1 
ATOM   190  N N   . ALA   A 1 28  ? 8.433   -22.884 2.139   1.00 19.23 ?  1065 ALA   A N   1 
ATOM   191  C CA  . ALA   A 1 28  ? 7.327   -21.948 1.965   1.00 15.16 ?  1065 ALA   A CA  1 
ATOM   192  C C   . ALA   A 1 28  ? 6.729   -21.550 3.308   1.00 14.94 ?  1065 ALA   A C   1 
ATOM   193  O O   . ALA   A 1 28  ? 6.603   -20.360 3.617   1.00 19.95 ?  1065 ALA   A O   1 
ATOM   194  C CB  . ALA   A 1 28  ? 6.259   -22.558 1.058   1.00 12.76 ?  1065 ALA   A CB  1 
ATOM   195  N N   . VAL   A 1 29  ? 6.353   -22.539 4.126   1.00 16.41 ?  1066 VAL   A N   1 
ATOM   196  C CA  . VAL   A 1 29  ? 5.817   -22.243 5.453   1.00 15.74 ?  1066 VAL   A CA  1 
ATOM   197  C C   . VAL   A 1 29  ? 6.906   -21.933 6.465   1.00 15.95 ?  1066 VAL   A C   1 
ATOM   198  O O   . VAL   A 1 29  ? 6.587   -21.621 7.618   1.00 16.87 ?  1066 VAL   A O   1 
ATOM   199  C CB  . VAL   A 1 29  ? 4.940   -23.398 5.977   1.00 15.47 ?  1066 VAL   A CB  1 
ATOM   200  C CG1 . VAL   A 1 29  ? 3.983   -23.869 4.896   1.00 17.78 ?  1066 VAL   A CG1 1 
ATOM   201  C CG2 . VAL   A 1 29  ? 5.800   -24.544 6.458   1.00 22.43 ?  1066 VAL   A CG2 1 
ATOM   202  N N   . GLN   A 1 30  ? 8.183   -22.015 6.075   1.00 17.04 ?  1067 GLN   A N   1 
ATOM   203  C CA  . GLN   A 1 30  ? 9.255   -21.526 6.936   1.00 15.05 ?  1067 GLN   A CA  1 
ATOM   204  C C   . GLN   A 1 30  ? 9.349   -20.009 6.906   1.00 15.56 ?  1067 GLN   A C   1 
ATOM   205  O O   . GLN   A 1 30  ? 9.809   -19.398 7.878   1.00 14.05 ?  1067 GLN   A O   1 
ATOM   206  C CB  . GLN   A 1 30  ? 10.601  -22.130 6.527   1.00 14.13 ?  1067 GLN   A CB  1 
ATOM   207  C CG  . GLN   A 1 30  ? 11.134  -23.177 7.494   1.00 19.28 ?  1067 GLN   A CG  1 
ATOM   208  C CD  . GLN   A 1 30  ? 12.174  -24.082 6.862   1.00 13.59 ?  1067 GLN   A CD  1 
ATOM   209  O OE1 . GLN   A 1 30  ? 12.478  -23.964 5.675   1.00 12.91 ?  1067 GLN   A OE1 1 
ATOM   210  N NE2 . GLN   A 1 30  ? 12.728  -24.990 7.657   1.00 17.07 ?  1067 GLN   A NE2 1 
ATOM   211  N N   . HIS   A 1 31  ? 8.927   -19.390 5.806   1.00 11.47 ?  1068 HIS   A N   1 
ATOM   212  C CA  . HIS   A 1 31  ? 8.945   -17.941 5.676   1.00 13.16 ?  1068 HIS   A CA  1 
ATOM   213  C C   . HIS   A 1 31  ? 7.841   -17.260 6.471   1.00 15.57 ?  1068 HIS   A C   1 
ATOM   214  O O   . HIS   A 1 31  ? 7.855   -16.030 6.589   1.00 19.08 ?  1068 HIS   A O   1 
ATOM   215  C CB  . HIS   A 1 31  ? 8.816   -17.551 4.200   1.00 12.44 ?  1068 HIS   A CB  1 
ATOM   216  C CG  . HIS   A 1 31  ? 10.112  -17.564 3.451   1.00 16.19 ?  1068 HIS   A CG  1 
ATOM   217  N ND1 . HIS   A 1 31  ? 11.334  -17.439 4.076   1.00 18.90 ?  1068 HIS   A ND1 1 
ATOM   218  C CD2 . HIS   A 1 31  ? 10.376  -17.686 2.129   1.00 17.28 ?  1068 HIS   A CD2 1 
ATOM   219  C CE1 . HIS   A 1 31  ? 12.295  -17.483 3.170   1.00 14.79 ?  1068 HIS   A CE1 1 
ATOM   220  N NE2 . HIS   A 1 31  ? 11.741  -17.632 1.981   1.00 17.30 ?  1068 HIS   A NE2 1 
ATOM   221  N N   . VAL   A 1 32  ? 6.886   -18.019 7.011   1.00 13.14 ?  1069 VAL   A N   1 
ATOM   222  C CA  . VAL   A 1 32  ? 5.663   -17.433 7.548   1.00 12.28 ?  1069 VAL   A CA  1 
ATOM   223  C C   . VAL   A 1 32  ? 5.378   -18.015 8.933   1.00 13.01 ?  1069 VAL   A C   1 
ATOM   224  O O   . VAL   A 1 32  ? 4.242   -17.978 9.417   1.00 12.43 ?  1069 VAL   A O   1 
ATOM   225  C CB  . VAL   A 1 32  ? 4.489   -17.665 6.571   1.00 10.62 ?  1069 VAL   A CB  1 
ATOM   226  C CG1 . VAL   A 1 32  ? 3.291   -16.825 6.935   1.00 7.25  ?  1069 VAL   A CG1 1 
ATOM   227  C CG2 . VAL   A 1 32  ? 4.898   -17.359 5.134   1.00 19.88 ?  1069 VAL   A CG2 1 
ATOM   228  N N   . VAL   A 1 33  ? 6.408   -18.548 9.596   1.00 14.66 ?  1070 VAL   A N   1 
ATOM   229  C CA  . VAL   A 1 33  ? 6.200   -19.142 10.912  1.00 16.63 ?  1070 VAL   A CA  1 
ATOM   230  C C   . VAL   A 1 33  ? 5.946   -18.049 11.940  1.00 10.77 ?  1070 VAL   A C   1 
ATOM   231  O O   . VAL   A 1 33  ? 6.528   -16.958 11.874  1.00 16.60 ?  1070 VAL   A O   1 
ATOM   232  C CB  . VAL   A 1 33  ? 7.400   -20.006 11.338  1.00 20.05 ?  1070 VAL   A CB  1 
ATOM   233  C CG1 . VAL   A 1 33  ? 6.977   -21.004 12.411  1.00 20.55 ?  1070 VAL   A CG1 1 
ATOM   234  C CG2 . VAL   A 1 33  ? 8.003   -20.719 10.160  1.00 20.66 ?  1070 VAL   A CG2 1 
ATOM   235  N N   . ILE   A 1 34  ? 5.080   -18.346 12.905  1.00 11.80 ?  1071 ILE   A N   1 
ATOM   236  C CA  . ILE   A 1 34  ? 4.799   -17.461 14.029  1.00 14.95 ?  1071 ILE   A CA  1 
ATOM   237  C C   . ILE   A 1 34  ? 5.275   -18.142 15.303  1.00 13.74 ?  1071 ILE   A C   1 
ATOM   238  O O   . ILE   A 1 34  ? 4.927   -19.300 15.563  1.00 16.78 ?  1071 ILE   A O   1 
ATOM   239  C CB  . ILE   A 1 34  ? 3.302   -17.117 14.123  1.00 13.18 ?  1071 ILE   A CB  1 
ATOM   240  C CG1 . ILE   A 1 34  ? 2.922   -16.066 13.081  1.00 13.08 ?  1071 ILE   A CG1 1 
ATOM   241  C CG2 . ILE   A 1 34  ? 2.944   -16.630 15.521  1.00 18.26 ?  1071 ILE   A CG2 1 
ATOM   242  C CD1 . ILE   A 1 34  ? 1.466   -15.668 13.137  1.00 13.41 ?  1071 ILE   A CD1 1 
ATOM   243  N N   . GLY   A 1 35  ? 6.071   -17.428 16.093  1.00 14.22 ?  1072 GLY   A N   1 
ATOM   244  C CA  . GLY   A 1 35  ? 6.470   -17.909 17.391  1.00 14.09 ?  1072 GLY   A CA  1 
ATOM   245  C C   . GLY   A 1 35  ? 5.291   -17.977 18.339  1.00 14.35 ?  1072 GLY   A C   1 
ATOM   246  O O   . GLY   A 1 35  ? 4.482   -17.048 18.424  1.00 17.56 ?  1072 GLY   A O   1 
ATOM   247  N N   . PRO   A 1 36  ? 5.161   -19.095 19.060  1.00 16.21 ?  1073 PRO   A N   1 
ATOM   248  C CA  . PRO   A 1 36  ? 4.052   -19.212 20.022  1.00 18.96 ?  1073 PRO   A CA  1 
ATOM   249  C C   . PRO   A 1 36  ? 4.045   -18.120 21.078  1.00 17.97 ?  1073 PRO   A C   1 
ATOM   250  O O   . PRO   A 1 36  ? 2.967   -17.673 21.489  1.00 14.17 ?  1073 PRO   A O   1 
ATOM   251  C CB  . PRO   A 1 36  ? 4.274   -20.601 20.636  1.00 11.39 ?  1073 PRO   A CB  1 
ATOM   252  C CG  . PRO   A 1 36  ? 5.011   -21.359 19.586  1.00 12.87 ?  1073 PRO   A CG  1 
ATOM   253  C CD  . PRO   A 1 36  ? 5.907   -20.356 18.916  1.00 15.06 ?  1073 PRO   A CD  1 
ATOM   254  N N   . SER   A 1 37  ? 5.217   -17.669 21.527  1.00 15.32 ?  1074 SER   A N   1 
ATOM   255  C CA  . SER   A 1 37  ? 5.275   -16.588 22.506  1.00 17.18 ?  1074 SER   A CA  1 
ATOM   256  C C   . SER   A 1 37  ? 4.868   -15.241 21.925  1.00 18.62 ?  1074 SER   A C   1 
ATOM   257  O O   . SER   A 1 37  ? 4.853   -14.249 22.663  1.00 18.97 ?  1074 SER   A O   1 
ATOM   258  C CB  . SER   A 1 37  ? 6.683   -16.487 23.096  1.00 20.59 ?  1074 SER   A CB  1 
ATOM   259  O OG  . SER   A 1 37  ? 7.176   -17.762 23.465  1.00 20.56 ?  1074 SER   A OG  1 
ATOM   260  N N   . SER   A 1 38  ? 4.546   -15.179 20.634  1.00 16.40 ?  1075 SER   A N   1 
ATOM   261  C CA  . SER   A 1 38  ? 4.125   -13.946 19.986  1.00 17.49 ?  1075 SER   A CA  1 
ATOM   262  C C   . SER   A 1 38  ? 2.639   -13.937 19.649  1.00 21.22 ?  1075 SER   A C   1 
ATOM   263  O O   . SER   A 1 38  ? 2.168   -12.995 19.003  1.00 24.43 ?  1075 SER   A O   1 
ATOM   264  C CB  . SER   A 1 38  ? 4.948   -13.708 18.718  1.00 19.07 ?  1075 SER   A CB  1 
ATOM   265  O OG  . SER   A 1 38  ? 6.297   -13.411 19.034  1.00 25.56 ?  1075 SER   A OG  1 
ATOM   266  N N   . LEU   A 1 39  ? 1.886   -14.955 20.065  1.00 14.98 ?  1076 LEU   A N   1 
ATOM   267  C CA  . LEU   A 1 39  ? 0.459   -15.004 19.763  1.00 19.54 ?  1076 LEU   A CA  1 
ATOM   268  C C   . LEU   A 1 39  ? -0.288  -15.673 20.906  1.00 18.27 ?  1076 LEU   A C   1 
ATOM   269  O O   . LEU   A 1 39  ? 0.033   -16.804 21.282  1.00 20.46 ?  1076 LEU   A O   1 
ATOM   270  C CB  . LEU   A 1 39  ? 0.195   -15.740 18.448  1.00 20.61 ?  1076 LEU   A CB  1 
ATOM   271  C CG  . LEU   A 1 39  ? -1.277  -15.791 18.029  1.00 18.90 ?  1076 LEU   A CG  1 
ATOM   272  C CD1 . LEU   A 1 39  ? -1.612  -14.658 17.077  1.00 13.33 ?  1076 LEU   A CD1 1 
ATOM   273  C CD2 . LEU   A 1 39  ? -1.611  -17.130 17.397  1.00 12.93 ?  1076 LEU   A CD2 1 
ATOM   274  N N   . ILE   A 1 40  ? -1.283  -14.973 21.446  1.00 19.94 ?  1077 ILE   A N   1 
ATOM   275  C CA  . ILE   A 1 40  ? -2.199  -15.522 22.440  1.00 20.40 ?  1077 ILE   A CA  1 
ATOM   276  C C   . ILE   A 1 40  ? -3.517  -15.829 21.748  1.00 19.74 ?  1077 ILE   A C   1 
ATOM   277  O O   . ILE   A 1 40  ? -4.100  -14.955 21.093  1.00 15.94 ?  1077 ILE   A O   1 
ATOM   278  C CB  . ILE   A 1 40  ? -2.412  -14.546 23.610  1.00 21.13 ?  1077 ILE   A CB  1 
ATOM   279  C CG1 . ILE   A 1 40  ? -1.077  -14.176 24.262  1.00 20.28 ?  1077 ILE   A CG1 1 
ATOM   280  C CG2 . ILE   A 1 40  ? -3.374  -15.137 24.634  1.00 16.60 ?  1077 ILE   A CG2 1 
ATOM   281  C CD1 . ILE   A 1 40  ? -0.261  -15.368 24.704  1.00 22.35 ?  1077 ILE   A CD1 1 
ATOM   282  N N   . VAL   A 1 41  ? -3.988  -17.063 21.884  1.00 20.18 ?  1078 VAL   A N   1 
ATOM   283  C CA  . VAL   A 1 41  ? -5.246  -17.490 21.284  1.00 19.87 ?  1078 VAL   A CA  1 
ATOM   284  C C   . VAL   A 1 41  ? -6.302  -17.560 22.376  1.00 20.94 ?  1078 VAL   A C   1 
ATOM   285  O O   . VAL   A 1 41  ? -6.162  -18.321 23.341  1.00 20.12 ?  1078 VAL   A O   1 
ATOM   286  C CB  . VAL   A 1 41  ? -5.103  -18.843 20.573  1.00 16.84 ?  1078 VAL   A CB  1 
ATOM   287  C CG1 . VAL   A 1 41  ? -6.434  -19.256 19.980  1.00 20.49 ?  1078 VAL   A CG1 1 
ATOM   288  C CG2 . VAL   A 1 41  ? -4.035  -18.768 19.496  1.00 14.36 ?  1078 VAL   A CG2 1 
ATOM   289  N N   . HIS   A 1 42  ? -7.362  -16.770 22.225  1.00 18.05 ?  1079 HIS   A N   1 
ATOM   290  C CA  . HIS   A 1 42  ? -8.493  -16.812 23.147  1.00 21.74 ?  1079 HIS   A CA  1 
ATOM   291  C C   . HIS   A 1 42  ? -9.414  -17.944 22.719  1.00 22.67 ?  1079 HIS   A C   1 
ATOM   292  O O   . HIS   A 1 42  ? -10.214 -17.793 21.795  1.00 26.02 ?  1079 HIS   A O   1 
ATOM   293  C CB  . HIS   A 1 42  ? -9.242  -15.484 23.160  1.00 20.06 ?  1079 HIS   A CB  1 
ATOM   294  C CG  . HIS   A 1 42  ? -8.399  -14.312 23.548  1.00 24.62 ?  1079 HIS   A CG  1 
ATOM   295  N ND1 . HIS   A 1 42  ? -7.789  -14.210 24.780  1.00 20.19 ?  1079 HIS   A ND1 1 
ATOM   296  C CD2 . HIS   A 1 42  ? -8.081  -13.181 22.876  1.00 21.43 ?  1079 HIS   A CD2 1 
ATOM   297  C CE1 . HIS   A 1 42  ? -7.122  -13.073 24.846  1.00 24.66 ?  1079 HIS   A CE1 1 
ATOM   298  N NE2 . HIS   A 1 42  ? -7.287  -12.428 23.705  1.00 24.28 ?  1079 HIS   A NE2 1 
ATOM   299  N N   . PHE   A 1 43  ? -9.300  -19.090 23.383  1.00 20.90 ?  1080 PHE   A N   1 
ATOM   300  C CA  . PHE   A 1 43  ? -10.248 -20.175 23.179  1.00 25.03 ?  1080 PHE   A CA  1 
ATOM   301  C C   . PHE   A 1 43  ? -11.513 -20.002 24.011  1.00 28.45 ?  1080 PHE   A C   1 
ATOM   302  O O   . PHE   A 1 43  ? -12.287 -20.955 24.149  1.00 31.69 ?  1080 PHE   A O   1 
ATOM   303  C CB  . PHE   A 1 43  ? -9.593  -21.522 23.497  1.00 27.39 ?  1080 PHE   A CB  1 
ATOM   304  C CG  . PHE   A 1 43  ? -8.436  -21.864 22.599  1.00 21.93 ?  1080 PHE   A CG  1 
ATOM   305  C CD1 . PHE   A 1 43  ? -8.653  -22.321 21.309  1.00 20.93 ?  1080 PHE   A CD1 1 
ATOM   306  C CD2 . PHE   A 1 43  ? -7.132  -21.737 23.048  1.00 14.91 ?  1080 PHE   A CD2 1 
ATOM   307  C CE1 . PHE   A 1 43  ? -7.590  -22.639 20.482  1.00 22.27 ?  1080 PHE   A CE1 1 
ATOM   308  C CE2 . PHE   A 1 43  ? -6.066  -22.054 22.228  1.00 12.49 ?  1080 PHE   A CE2 1 
ATOM   309  C CZ  . PHE   A 1 43  ? -6.295  -22.509 20.944  1.00 13.60 ?  1080 PHE   A CZ  1 
ATOM   310  N N   . ASN   A 1 44  ? -11.734 -18.807 24.563  1.00 27.66 ?  1081 ASN   A N   1 
ATOM   311  C CA  . ASN   A 1 44  ? -12.907 -18.559 25.392  1.00 24.31 ?  1081 ASN   A CA  1 
ATOM   312  C C   . ASN   A 1 44  ? -14.156 -18.299 24.560  1.00 22.97 ?  1081 ASN   A C   1 
ATOM   313  O O   . ASN   A 1 44  ? -15.268 -18.582 25.019  1.00 29.24 ?  1081 ASN   A O   1 
ATOM   314  C CB  . ASN   A 1 44  ? -12.647 -17.376 26.326  1.00 17.68 ?  1081 ASN   A CB  1 
ATOM   315  N N   . GLU   A 1 45  ? -14.001 -17.768 23.349  1.00 24.65 ?  1082 GLU   A N   1 
ATOM   316  C CA  . GLU   A 1 45  ? -15.138 -17.468 22.490  1.00 24.14 ?  1082 GLU   A CA  1 
ATOM   317  C C   . GLU   A 1 45  ? -14.759 -17.723 21.041  1.00 22.47 ?  1082 GLU   A C   1 
ATOM   318  O O   . GLU   A 1 45  ? -13.690 -17.300 20.591  1.00 20.77 ?  1082 GLU   A O   1 
ATOM   319  C CB  . GLU   A 1 45  ? -15.604 -16.018 22.669  1.00 26.98 ?  1082 GLU   A CB  1 
ATOM   320  N N   . VAL   A 1 46  ? -15.637 -18.410 20.320  1.00 27.18 ?  1083 VAL   A N   1 
ATOM   321  C CA  . VAL   A 1 46  ? -15.428 -18.720 18.911  1.00 23.45 ?  1083 VAL   A CA  1 
ATOM   322  C C   . VAL   A 1 46  ? -16.113 -17.653 18.070  1.00 22.85 ?  1083 VAL   A C   1 
ATOM   323  O O   . VAL   A 1 46  ? -17.297 -17.358 18.269  1.00 29.95 ?  1083 VAL   A O   1 
ATOM   324  C CB  . VAL   A 1 46  ? -15.971 -20.118 18.573  1.00 23.32 ?  1083 VAL   A CB  1 
ATOM   325  C CG1 . VAL   A 1 46  ? -15.840 -20.395 17.089  1.00 22.66 ?  1083 VAL   A CG1 1 
ATOM   326  C CG2 . VAL   A 1 46  ? -15.251 -21.179 19.387  1.00 19.01 ?  1083 VAL   A CG2 1 
ATOM   327  N N   . ILE   A 1 47  ? -15.371 -17.072 17.129  1.00 23.55 ?  1084 ILE   A N   1 
ATOM   328  C CA  . ILE   A 1 47  ? -15.903 -16.054 16.231  1.00 19.35 ?  1084 ILE   A CA  1 
ATOM   329  C C   . ILE   A 1 47  ? -16.131 -16.602 14.829  1.00 18.68 ?  1084 ILE   A C   1 
ATOM   330  O O   . ILE   A 1 47  ? -16.338 -15.827 13.889  1.00 18.92 ?  1084 ILE   A O   1 
ATOM   331  C CB  . ILE   A 1 47  ? -14.997 -14.813 16.192  1.00 20.85 ?  1084 ILE   A CB  1 
ATOM   332  C CG1 . ILE   A 1 47  ? -13.630 -15.161 15.597  1.00 19.82 ?  1084 ILE   A CG1 1 
ATOM   333  C CG2 . ILE   A 1 47  ? -14.843 -14.223 17.587  1.00 19.55 ?  1084 ILE   A CG2 1 
ATOM   334  C CD1 . ILE   A 1 47  ? -12.625 -14.031 15.674  1.00 23.60 ?  1084 ILE   A CD1 1 
ATOM   335  N N   . GLY   A 1 48  ? -16.101 -17.921 14.661  1.00 21.70 ?  1085 GLY   A N   1 
ATOM   336  C CA  . GLY   A 1 48  ? -16.323 -18.522 13.361  1.00 21.40 ?  1085 GLY   A CA  1 
ATOM   337  C C   . GLY   A 1 48  ? -16.164 -20.027 13.374  1.00 19.82 ?  1085 GLY   A C   1 
ATOM   338  O O   . GLY   A 1 48  ? -15.238 -20.554 13.997  1.00 20.24 ?  1085 GLY   A O   1 
ATOM   339  N N   . ARG   A 1 49  ? -17.060 -20.732 12.690  1.00 22.65 ?  1086 ARG   A N   1 
ATOM   340  C CA  . ARG   A 1 49  ? -17.034 -22.187 12.627  1.00 22.14 ?  1086 ARG   A CA  1 
ATOM   341  C C   . ARG   A 1 49  ? -16.967 -22.630 11.173  1.00 25.21 ?  1086 ARG   A C   1 
ATOM   342  O O   . ARG   A 1 49  ? -17.756 -22.170 10.341  1.00 21.42 ?  1086 ARG   A O   1 
ATOM   343  C CB  . ARG   A 1 49  ? -18.265 -22.790 13.310  1.00 23.40 ?  1086 ARG   A CB  1 
ATOM   344  N N   . GLY   A 1 50  ? -16.018 -23.518 10.874  1.00 19.44 ?  1087 GLY   A N   1 
ATOM   345  C CA  . GLY   A 1 50  ? -15.901 -24.113 9.560   1.00 16.56 ?  1087 GLY   A CA  1 
ATOM   346  C C   . GLY   A 1 50  ? -15.793 -25.624 9.664   1.00 18.64 ?  1087 GLY   A C   1 
ATOM   347  O O   . GLY   A 1 50  ? -15.730 -26.188 10.758  1.00 19.63 ?  1087 GLY   A O   1 
ATOM   348  N N   . HIS   A 1 51  ? -15.769 -26.266 8.495   1.00 17.15 ?  1088 HIS   A N   1 
ATOM   349  C CA  . HIS   A 1 51  ? -15.711 -27.722 8.467   1.00 20.23 ?  1088 HIS   A CA  1 
ATOM   350  C C   . HIS   A 1 51  ? -14.337 -28.268 8.839   1.00 19.10 ?  1088 HIS   A C   1 
ATOM   351  O O   . HIS   A 1 51  ? -14.228 -29.459 9.149   1.00 31.50 ?  1088 HIS   A O   1 
ATOM   352  C CB  . HIS   A 1 51  ? -16.122 -28.247 7.090   1.00 24.78 ?  1088 HIS   A CB  1 
ATOM   353  C CG  . HIS   A 1 51  ? -16.149 -29.741 7.003   1.00 23.33 ?  1088 HIS   A CG  1 
ATOM   354  N ND1 . HIS   A 1 51  ? -15.489 -30.442 6.018   1.00 28.61 ?  1088 HIS   A ND1 1 
ATOM   355  C CD2 . HIS   A 1 51  ? -16.737 -30.668 7.795   1.00 25.53 ?  1088 HIS   A CD2 1 
ATOM   356  C CE1 . HIS   A 1 51  ? -15.675 -31.737 6.202   1.00 25.99 ?  1088 HIS   A CE1 1 
ATOM   357  N NE2 . HIS   A 1 51  ? -16.432 -31.901 7.272   1.00 22.26 ?  1088 HIS   A NE2 1 
ATOM   358  N N   . PHE   A 1 52  ? -13.294 -27.440 8.820   1.00 16.55 ?  1089 PHE   A N   1 
ATOM   359  C CA  . PHE   A 1 52  ? -11.975 -27.869 9.262   1.00 15.28 ?  1089 PHE   A CA  1 
ATOM   360  C C   . PHE   A 1 52  ? -11.695 -27.522 10.719  1.00 15.52 ?  1089 PHE   A C   1 
ATOM   361  O O   . PHE   A 1 52  ? -10.710 -28.014 11.277  1.00 14.11 ?  1089 PHE   A O   1 
ATOM   362  C CB  . PHE   A 1 52  ? -10.885 -27.248 8.379   1.00 16.92 ?  1089 PHE   A CB  1 
ATOM   363  C CG  . PHE   A 1 52  ? -10.995 -27.610 6.928   1.00 14.95 ?  1089 PHE   A CG  1 
ATOM   364  C CD1 . PHE   A 1 52  ? -11.264 -28.911 6.540   1.00 16.63 ?  1089 PHE   A CD1 1 
ATOM   365  C CD2 . PHE   A 1 52  ? -10.815 -26.647 5.950   1.00 14.58 ?  1089 PHE   A CD2 1 
ATOM   366  C CE1 . PHE   A 1 52  ? -11.361 -29.242 5.202   1.00 14.85 ?  1089 PHE   A CE1 1 
ATOM   367  C CE2 . PHE   A 1 52  ? -10.910 -26.972 4.611   1.00 13.08 ?  1089 PHE   A CE2 1 
ATOM   368  C CZ  . PHE   A 1 52  ? -11.183 -28.270 4.237   1.00 15.05 ?  1089 PHE   A CZ  1 
ATOM   369  N N   . GLY   A 1 53  ? -12.519 -26.693 11.335  1.00 17.78 ?  1090 GLY   A N   1 
ATOM   370  C CA  . GLY   A 1 53  ? -12.275 -26.242 12.692  1.00 16.09 ?  1090 GLY   A CA  1 
ATOM   371  C C   . GLY   A 1 53  ? -12.853 -24.856 12.895  1.00 14.02 ?  1090 GLY   A C   1 
ATOM   372  O O   . GLY   A 1 53  ? -13.421 -24.254 11.989  1.00 13.19 ?  1090 GLY   A O   1 
ATOM   373  N N   . CYS   A 1 54  ? -12.686 -24.357 14.115  1.00 15.32 ?  1091 CYS   A N   1 
ATOM   374  C CA  . CYS   A 1 54  ? -13.287 -23.098 14.530  1.00 14.51 ?  1091 CYS   A CA  1 
ATOM   375  C C   . CYS   A 1 54  ? -12.304 -21.938 14.386  1.00 17.77 ?  1091 CYS   A C   1 
ATOM   376  O O   . CYS   A 1 54  ? -11.113 -22.120 14.122  1.00 13.53 ?  1091 CYS   A O   1 
ATOM   377  C CB  . CYS   A 1 54  ? -13.788 -23.197 15.974  1.00 20.29 ?  1091 CYS   A CB  1 
ATOM   378  S SG  . CYS   A 1 54  ? -15.310 -24.155 16.159  1.00 43.10 ?  1091 CYS   A SG  1 
ATOM   379  N N   . VAL   A 1 55  ? -12.831 -20.727 14.559  1.00 16.33 ?  1092 VAL   A N   1 
ATOM   380  C CA  . VAL   A 1 55  ? -12.062 -19.492 14.460  1.00 17.26 ?  1092 VAL   A CA  1 
ATOM   381  C C   . VAL   A 1 55  ? -12.167 -18.757 15.788  1.00 20.32 ?  1092 VAL   A C   1 
ATOM   382  O O   . VAL   A 1 55  ? -13.270 -18.574 16.316  1.00 19.94 ?  1092 VAL   A O   1 
ATOM   383  C CB  . VAL   A 1 55  ? -12.555 -18.600 13.305  1.00 15.56 ?  1092 VAL   A CB  1 
ATOM   384  C CG1 . VAL   A 1 55  ? -11.491 -17.590 12.931  1.00 15.35 ?  1092 VAL   A CG1 1 
ATOM   385  C CG2 . VAL   A 1 55  ? -12.935 -19.442 12.101  1.00 14.85 ?  1092 VAL   A CG2 1 
ATOM   386  N N   . TYR   A 1 56  ? -11.026 -18.329 16.319  1.00 16.49 ?  1093 TYR   A N   1 
ATOM   387  C CA  . TYR   A 1 56  ? -10.957 -17.729 17.641  1.00 19.31 ?  1093 TYR   A CA  1 
ATOM   388  C C   . TYR   A 1 56  ? -10.338 -16.343 17.559  1.00 22.01 ?  1093 TYR   A C   1 
ATOM   389  O O   . TYR   A 1 56  ? -9.571  -16.038 16.640  1.00 24.55 ?  1093 TYR   A O   1 
ATOM   390  C CB  . TYR   A 1 56  ? -10.138 -18.601 18.603  1.00 22.35 ?  1093 TYR   A CB  1 
ATOM   391  C CG  . TYR   A 1 56  ? -10.619 -20.031 18.691  1.00 21.40 ?  1093 TYR   A CG  1 
ATOM   392  C CD1 . TYR   A 1 56  ? -10.290 -20.957 17.709  1.00 17.49 ?  1093 TYR   A CD1 1 
ATOM   393  C CD2 . TYR   A 1 56  ? -11.403 -20.455 19.754  1.00 23.32 ?  1093 TYR   A CD2 1 
ATOM   394  C CE1 . TYR   A 1 56  ? -10.730 -22.261 17.782  1.00 21.22 ?  1093 TYR   A CE1 1 
ATOM   395  C CE2 . TYR   A 1 56  ? -11.845 -21.760 19.838  1.00 21.35 ?  1093 TYR   A CE2 1 
ATOM   396  C CZ  . TYR   A 1 56  ? -11.507 -22.658 18.848  1.00 26.80 ?  1093 TYR   A CZ  1 
ATOM   397  O OH  . TYR   A 1 56  ? -11.946 -23.960 18.925  1.00 34.25 ?  1093 TYR   A OH  1 
ATOM   398  N N   . HIS   A 1 57  ? -10.682 -15.500 18.527  1.00 22.28 ?  1094 HIS   A N   1 
ATOM   399  C CA  . HIS   A 1 57  ? -10.017 -14.212 18.643  1.00 25.43 ?  1094 HIS   A CA  1 
ATOM   400  C C   . HIS   A 1 57  ? -8.600  -14.408 19.163  1.00 25.29 ?  1094 HIS   A C   1 
ATOM   401  O O   . HIS   A 1 57  ? -8.362  -15.198 20.081  1.00 20.93 ?  1094 HIS   A O   1 
ATOM   402  C CB  . HIS   A 1 57  ? -10.796 -13.282 19.566  1.00 19.85 ?  1094 HIS   A CB  1 
ATOM   403  C CG  . HIS   A 1 57  ? -10.541 -11.833 19.300  1.00 25.11 ?  1094 HIS   A CG  1 
ATOM   404  N ND1 . HIS   A 1 57  ? -11.149 -11.151 18.268  1.00 27.24 ?  1094 HIS   A ND1 1 
ATOM   405  C CD2 . HIS   A 1 57  ? -9.738  -10.938 19.922  1.00 28.61 ?  1094 HIS   A CD2 1 
ATOM   406  C CE1 . HIS   A 1 57  ? -10.729 -9.899  18.265  1.00 26.62 ?  1094 HIS   A CE1 1 
ATOM   407  N NE2 . HIS   A 1 57  ? -9.876  -9.742  19.261  1.00 33.67 ?  1094 HIS   A NE2 1 
ATOM   408  N N   . GLY   A 1 58  ? -7.649  -13.688 18.561  1.00 20.65 ?  1095 GLY   A N   1 
ATOM   409  C CA  . GLY   A 1 58  ? -6.252  -13.855 18.887  1.00 22.32 ?  1095 GLY   A CA  1 
ATOM   410  C C   . GLY   A 1 58  ? -5.569  -12.521 19.135  1.00 20.56 ?  1095 GLY   A C   1 
ATOM   411  O O   . GLY   A 1 58  ? -6.150  -11.449 18.945  1.00 25.68 ?  1095 GLY   A O   1 
ATOM   412  N N   . THR   A 1 59  ? -4.315  -12.614 19.583  1.00 15.82 ?  1096 THR   A N   1 
ATOM   413  C CA  . THR   A 1 59  ? -3.480  -11.446 19.874  1.00 17.04 ?  1096 THR   A CA  1 
ATOM   414  C C   . THR   A 1 59  ? -2.085  -11.726 19.323  1.00 15.91 ?  1096 THR   A C   1 
ATOM   415  O O   . THR   A 1 59  ? -1.320  -12.478 19.930  1.00 15.21 ?  1096 THR   A O   1 
ATOM   416  C CB  . THR   A 1 59  ? -3.409  -11.151 21.370  1.00 21.74 ?  1096 THR   A CB  1 
ATOM   417  O OG1 . THR   A 1 59  ? -2.326  -11.891 21.946  1.00 22.94 ?  1096 THR   A OG1 1 
ATOM   418  C CG2 . THR   A 1 59  ? -4.695  -11.540 22.077  1.00 18.10 ?  1096 THR   A CG2 1 
ATOM   419  N N   . LEU   A 1 60  ? -1.750  -11.114 18.192  1.00 17.80 ?  1097 LEU   A N   1 
ATOM   420  C CA  . LEU   A 1 60  ? -0.433  -11.269 17.590  1.00 19.70 ?  1097 LEU   A CA  1 
ATOM   421  C C   . LEU   A 1 60  ? 0.482   -10.131 18.030  1.00 21.48 ?  1097 LEU   A C   1 
ATOM   422  O O   . LEU   A 1 60  ? 0.069   -8.969  18.075  1.00 23.25 ?  1097 LEU   A O   1 
ATOM   423  C CB  . LEU   A 1 60  ? -0.530  -11.311 16.063  1.00 17.55 ?  1097 LEU   A CB  1 
ATOM   424  C CG  . LEU   A 1 60  ? 0.764   -11.599 15.298  1.00 15.19 ?  1097 LEU   A CG  1 
ATOM   425  C CD1 . LEU   A 1 60  ? 1.435   -12.854 15.830  1.00 18.04 ?  1097 LEU   A CD1 1 
ATOM   426  C CD2 . LEU   A 1 60  ? 0.487   -11.734 13.810  1.00 11.28 ?  1097 LEU   A CD2 1 
ATOM   427  N N   . LEU   A 1 61  ? 1.723   -10.476 18.362  1.00 16.52 ?  1098 LEU   A N   1 
ATOM   428  C CA  . LEU   A 1 61  ? 2.727   -9.520  18.812  1.00 25.02 ?  1098 LEU   A CA  1 
ATOM   429  C C   . LEU   A 1 61  ? 3.801   -9.390  17.739  1.00 30.68 ?  1098 LEU   A C   1 
ATOM   430  O O   . LEU   A 1 61  ? 4.350   -10.398 17.281  1.00 29.43 ?  1098 LEU   A O   1 
ATOM   431  C CB  . LEU   A 1 61  ? 3.342   -9.955  20.147  1.00 23.00 ?  1098 LEU   A CB  1 
ATOM   432  C CG  . LEU   A 1 61  ? 2.480   -9.839  21.413  1.00 18.77 ?  1098 LEU   A CG  1 
ATOM   433  C CD1 . LEU   A 1 61  ? 1.390   -10.906 21.480  1.00 19.51 ?  1098 LEU   A CD1 1 
ATOM   434  C CD2 . LEU   A 1 61  ? 3.348   -9.891  22.663  1.00 25.63 ?  1098 LEU   A CD2 1 
ATOM   435  N N   . ASP   A 1 62  ? 4.102   -8.154  17.347  1.00 35.63 ?  1099 ASP   A N   1 
ATOM   436  C CA  . ASP   A 1 62  ? 4.897   -7.881  16.161  1.00 42.37 ?  1099 ASP   A CA  1 
ATOM   437  C C   . ASP   A 1 62  ? 6.319   -7.449  16.540  1.00 42.87 ?  1099 ASP   A C   1 
ATOM   438  O O   . ASP   A 1 62  ? 6.793   -7.720  17.650  1.00 38.07 ?  1099 ASP   A O   1 
ATOM   439  C CB  . ASP   A 1 62  ? 4.174   -6.827  15.312  1.00 40.94 ?  1099 ASP   A CB  1 
ATOM   440  N N   . ASN   A 1 63  ? 7.012   -6.782  15.607  1.00 43.82 ?  1100 ASN   A N   1 
ATOM   441  C CA  . ASN   A 1 63  ? 8.387   -6.348  15.849  1.00 42.99 ?  1100 ASN   A CA  1 
ATOM   442  C C   . ASN   A 1 63  ? 8.469   -5.382  17.021  1.00 40.35 ?  1100 ASN   A C   1 
ATOM   443  O O   . ASN   A 1 63  ? 9.497   -5.320  17.705  1.00 39.75 ?  1100 ASN   A O   1 
ATOM   444  C CB  . ASN   A 1 63  ? 8.967   -5.707  14.589  1.00 37.69 ?  1100 ASN   A CB  1 
ATOM   445  N N   . ASP   A 1 64  ? 7.415   -4.610  17.251  1.00 46.37 ?  1101 ASP   A N   1 
ATOM   446  C CA  . ASP   A 1 64  ? 7.205   -3.907  18.503  1.00 45.58 ?  1101 ASP   A CA  1 
ATOM   447  C C   . ASP   A 1 64  ? 6.045   -4.566  19.236  1.00 43.50 ?  1101 ASP   A C   1 
ATOM   448  O O   . ASP   A 1 64  ? 5.249   -5.301  18.644  1.00 37.73 ?  1101 ASP   A O   1 
ATOM   449  C CB  . ASP   A 1 64  ? 6.928   -2.417  18.269  1.00 42.00 ?  1101 ASP   A CB  1 
ATOM   450  C CG  . ASP   A 1 64  ? 7.821   -1.819  17.198  1.00 47.64 ?  1101 ASP   A CG  1 
ATOM   451  O OD1 . ASP   A 1 64  ? 7.578   -2.084  16.002  1.00 47.58 ?  1101 ASP   A OD1 1 
ATOM   452  O OD2 . ASP   A 1 64  ? 8.769   -1.086  17.553  1.00 43.10 -1 1101 ASP   A OD2 1 
ATOM   453  N N   . GLY   A 1 65  ? 5.949   -4.295  20.535  1.00 38.91 ?  1102 GLY   A N   1 
ATOM   454  C CA  . GLY   A 1 65  ? 4.969   -4.959  21.376  1.00 31.34 ?  1102 GLY   A CA  1 
ATOM   455  C C   . GLY   A 1 65  ? 3.530   -4.828  20.914  1.00 32.63 ?  1102 GLY   A C   1 
ATOM   456  O O   . GLY   A 1 65  ? 2.653   -5.540  21.413  1.00 34.10 ?  1102 GLY   A O   1 
ATOM   457  N N   . LYS   A 1 66  ? 3.278   -3.933  19.959  1.00 33.95 ?  1103 LYS   A N   1 
ATOM   458  C CA  . LYS   A 1 66  ? 1.926   -3.678  19.477  1.00 27.59 ?  1103 LYS   A CA  1 
ATOM   459  C C   . LYS   A 1 66  ? 1.064   -4.924  19.326  1.00 33.86 ?  1103 LYS   A C   1 
ATOM   460  O O   . LYS   A 1 66  ? 1.426   -5.867  18.616  1.00 31.37 ?  1103 LYS   A O   1 
ATOM   461  C CB  . LYS   A 1 66  ? 1.971   -2.906  18.156  1.00 23.37 ?  1103 LYS   A CB  1 
ATOM   462  N N   . LYS   A 1 67  ? -0.082  -4.919  20.002  1.00 25.97 ?  1104 LYS   A N   1 
ATOM   463  C CA  . LYS   A 1 67  ? -1.024  -6.031  19.959  1.00 27.82 ?  1104 LYS   A CA  1 
ATOM   464  C C   . LYS   A 1 67  ? -2.011  -5.795  18.822  1.00 29.16 ?  1104 LYS   A C   1 
ATOM   465  O O   . LYS   A 1 67  ? -2.878  -4.920  18.915  1.00 33.07 ?  1104 LYS   A O   1 
ATOM   466  C CB  . LYS   A 1 67  ? -1.749  -6.172  21.295  1.00 21.09 ?  1104 LYS   A CB  1 
ATOM   467  N N   . ILE   A 1 68  ? -1.880  -6.571  17.752  1.00 26.18 ?  1105 ILE   A N   1 
ATOM   468  C CA  . ILE   A 1 68  ? -2.803  -6.523  16.626  1.00 24.64 ?  1105 ILE   A CA  1 
ATOM   469  C C   . ILE   A 1 68  ? -3.822  -7.639  16.804  1.00 23.81 ?  1105 ILE   A C   1 
ATOM   470  O O   . ILE   A 1 68  ? -3.458  -8.814  16.939  1.00 18.81 ?  1105 ILE   A O   1 
ATOM   471  C CB  . ILE   A 1 68  ? -2.067  -6.645  15.281  1.00 24.97 ?  1105 ILE   A CB  1 
ATOM   472  C CG1 . ILE   A 1 68  ? -0.967  -7.704  15.354  1.00 24.46 ?  1105 ILE   A CG1 1 
ATOM   473  C CG2 . ILE   A 1 68  ? -1.470  -5.306  14.870  1.00 26.23 ?  1105 ILE   A CG2 1 
ATOM   474  C CD1 . ILE   A 1 68  ? -0.552  -8.245  14.001  1.00 21.95 ?  1105 ILE   A CD1 1 
ATOM   475  N N   . HIS   A 1 69  ? -5.096  -7.271  16.825  1.00 26.12 ?  1106 HIS   A N   1 
ATOM   476  C CA  . HIS   A 1 69  ? -6.161  -8.254  16.890  1.00 22.50 ?  1106 HIS   A CA  1 
ATOM   477  C C   . HIS   A 1 69  ? -6.151  -9.150  15.659  1.00 20.18 ?  1106 HIS   A C   1 
ATOM   478  O O   . HIS   A 1 69  ? -5.687  -8.773  14.579  1.00 19.91 ?  1106 HIS   A O   1 
ATOM   479  C CB  . HIS   A 1 69  ? -7.503  -7.552  17.018  1.00 24.34 ?  1106 HIS   A CB  1 
ATOM   480  C CG  . HIS   A 1 69  ? -7.711  -6.915  18.349  1.00 28.95 ?  1106 HIS   A CG  1 
ATOM   481  N ND1 . HIS   A 1 69  ? -8.625  -5.905  18.559  1.00 28.11 ?  1106 HIS   A ND1 1 
ATOM   482  C CD2 . HIS   A 1 69  ? -7.182  -7.201  19.561  1.00 30.96 ?  1106 HIS   A CD2 1 
ATOM   483  C CE1 . HIS   A 1 69  ? -8.611  -5.557  19.833  1.00 33.13 ?  1106 HIS   A CE1 1 
ATOM   484  N NE2 . HIS   A 1 69  ? -7.743  -6.329  20.463  1.00 30.06 ?  1106 HIS   A NE2 1 
ATOM   485  N N   . CYS   A 1 70  ? -6.668  -10.360 15.834  1.00 21.45 ?  1107 CYS   A N   1 
ATOM   486  C CA  . CYS   A 1 70  ? -6.703  -11.295 14.725  1.00 20.05 ?  1107 CYS   A CA  1 
ATOM   487  C C   . CYS   A 1 70  ? -7.768  -12.342 14.990  1.00 18.83 ?  1107 CYS   A C   1 
ATOM   488  O O   . CYS   A 1 70  ? -8.263  -12.493 16.110  1.00 21.11 ?  1107 CYS   A O   1 
ATOM   489  C CB  . CYS   A 1 70  ? -5.338  -11.956 14.504  1.00 20.33 ?  1107 CYS   A CB  1 
ATOM   490  S SG  . CYS   A 1 70  ? -4.683  -12.826 15.934  1.00 22.55 ?  1107 CYS   A SG  1 
ATOM   491  N N   . ALA   A 1 71  ? -8.134  -13.035 13.923  1.00 21.03 ?  1108 ALA   A N   1 
ATOM   492  C CA  . ALA   A 1 71  ? -8.841  -14.298 14.006  1.00 20.26 ?  1108 ALA   A CA  1 
ATOM   493  C C   . ALA   A 1 71  ? -7.853  -15.410 13.692  1.00 16.09 ?  1108 ALA   A C   1 
ATOM   494  O O   . ALA   A 1 71  ? -7.066  -15.304 12.747  1.00 14.10 ?  1108 ALA   A O   1 
ATOM   495  C CB  . ALA   A 1 71  ? -10.018 -14.337 13.033  1.00 18.12 ?  1108 ALA   A CB  1 
ATOM   496  N N   . VAL   A 1 72  ? -7.874  -16.464 14.499  1.00 20.49 ?  1109 VAL   A N   1 
ATOM   497  C CA  . VAL   A 1 72  ? -6.963  -17.588 14.333  1.00 19.03 ?  1109 VAL   A CA  1 
ATOM   498  C C   . VAL   A 1 72  ? -7.799  -18.814 13.988  1.00 16.66 ?  1109 VAL   A C   1 
ATOM   499  O O   . VAL   A 1 72  ? -8.601  -19.285 14.806  1.00 20.33 ?  1109 VAL   A O   1 
ATOM   500  C CB  . VAL   A 1 72  ? -6.094  -17.817 15.578  1.00 17.60 ?  1109 VAL   A CB  1 
ATOM   501  C CG1 . VAL   A 1 72  ? -6.930  -17.768 16.844  1.00 18.08 ?  1109 VAL   A CG1 1 
ATOM   502  C CG2 . VAL   A 1 72  ? -5.339  -19.129 15.467  1.00 17.31 ?  1109 VAL   A CG2 1 
ATOM   503  N N   . LYS   A 1 73  ? -7.630  -19.317 12.768  1.00 14.80 ?  1110 LYS   A N   1 
ATOM   504  C CA  . LYS   A 1 73  ? -8.404  -20.455 12.292  1.00 14.80 ?  1110 LYS   A CA  1 
ATOM   505  C C   . LYS   A 1 73  ? -7.760  -21.745 12.783  1.00 14.51 ?  1110 LYS   A C   1 
ATOM   506  O O   . LYS   A 1 73  ? -6.587  -22.007 12.498  1.00 13.96 ?  1110 LYS   A O   1 
ATOM   507  C CB  . LYS   A 1 73  ? -8.489  -20.440 10.768  1.00 15.29 ?  1110 LYS   A CB  1 
ATOM   508  C CG  . LYS   A 1 73  ? -9.206  -21.637 10.165  1.00 13.98 ?  1110 LYS   A CG  1 
ATOM   509  C CD  . LYS   A 1 73  ? -10.654 -21.681 10.622  1.00 13.14 ?  1110 LYS   A CD  1 
ATOM   510  C CE  . LYS   A 1 73  ? -11.467 -22.695 9.839   1.00 14.86 ?  1110 LYS   A CE  1 
ATOM   511  N NZ  . LYS   A 1 73  ? -11.383 -22.478 8.371   1.00 13.20 ?  1110 LYS   A NZ  1 
ATOM   512  N N   . SER   A 1 74  ? -8.523  -22.545 13.522  1.00 14.23 ?  1111 SER   A N   1 
ATOM   513  C CA  . SER   A 1 74  ? -8.058  -23.839 13.999  1.00 14.11 ?  1111 SER   A CA  1 
ATOM   514  C C   . SER   A 1 74  ? -8.371  -24.922 12.976  1.00 14.55 ?  1111 SER   A C   1 
ATOM   515  O O   . SER   A 1 74  ? -9.423  -24.897 12.335  1.00 14.20 ?  1111 SER   A O   1 
ATOM   516  C CB  . SER   A 1 74  ? -8.711  -24.183 15.337  1.00 19.69 ?  1111 SER   A CB  1 
ATOM   517  O OG  . SER   A 1 74  ? -8.792  -25.585 15.513  1.00 17.83 ?  1111 SER   A OG  1 
ATOM   518  N N   . LEU   A 1 75  ? -7.449  -25.874 12.827  1.00 15.61 ?  1112 LEU   A N   1 
ATOM   519  C CA  . LEU   A 1 75  ? -7.624  -27.011 11.929  1.00 16.17 ?  1112 LEU   A CA  1 
ATOM   520  C C   . LEU   A 1 75  ? -7.694  -28.321 12.708  1.00 19.94 ?  1112 LEU   A C   1 
ATOM   521  O O   . LEU   A 1 75  ? -7.213  -29.355 12.242  1.00 25.88 ?  1112 LEU   A O   1 
ATOM   522  C CB  . LEU   A 1 75  ? -6.498  -27.066 10.897  1.00 17.61 ?  1112 LEU   A CB  1 
ATOM   523  C CG  . LEU   A 1 75  ? -6.324  -25.901 9.919   1.00 11.67 ?  1112 LEU   A CG  1 
ATOM   524  C CD1 . LEU   A 1 75  ? -4.970  -25.990 9.240   1.00 13.45 ?  1112 LEU   A CD1 1 
ATOM   525  C CD2 . LEU   A 1 75  ? -7.422  -25.887 8.876   1.00 16.72 ?  1112 LEU   A CD2 1 
ATOM   526  N N   . ASN   A 1 76  ? -8.288  -28.293 13.903  1.00 19.14 ?  1113 ASN   A N   1 
ATOM   527  C CA  . ASN   A 1 76  ? -8.283  -29.477 14.755  1.00 19.05 ?  1113 ASN   A CA  1 
ATOM   528  C C   . ASN   A 1 76  ? -9.106  -30.614 14.160  1.00 23.23 ?  1113 ASN   A C   1 
ATOM   529  O O   . ASN   A 1 76  ? -8.760  -31.787 14.338  1.00 27.75 ?  1113 ASN   A O   1 
ATOM   530  C CB  . ASN   A 1 76  ? -8.804  -29.122 16.148  1.00 14.99 ?  1113 ASN   A CB  1 
ATOM   531  C CG  . ASN   A 1 76  ? -10.252 -28.667 16.133  1.00 19.96 ?  1113 ASN   A CG  1 
ATOM   532  O OD1 . ASN   A 1 76  ? -10.786 -28.283 15.092  1.00 17.98 ?  1113 ASN   A OD1 1 
ATOM   533  N ND2 . ASN   A 1 76  ? -10.898 -28.715 17.292  1.00 21.31 ?  1113 ASN   A ND2 1 
ATOM   534  N N   . ARG   A 1 77  ? -10.188 -30.292 13.447  1.00 21.64 ?  1114 ARG   A N   1 
ATOM   535  C CA  . ARG   A 1 77  ? -11.116 -31.330 13.014  1.00 21.67 ?  1114 ARG   A CA  1 
ATOM   536  C C   . ARG   A 1 77  ? -10.579 -32.151 11.849  1.00 24.56 ?  1114 ARG   A C   1 
ATOM   537  O O   . ARG   A 1 77  ? -10.936 -33.328 11.719  1.00 26.09 ?  1114 ARG   A O   1 
ATOM   538  C CB  . ARG   A 1 77  ? -12.469 -30.719 12.647  1.00 19.35 ?  1114 ARG   A CB  1 
ATOM   539  C CG  . ARG   A 1 77  ? -13.642 -31.640 12.950  1.00 27.90 ?  1114 ARG   A CG  1 
ATOM   540  C CD  . ARG   A 1 77  ? -14.965 -30.892 12.964  1.00 31.20 ?  1114 ARG   A CD  1 
ATOM   541  N NE  . ARG   A 1 77  ? -15.867 -31.411 13.986  1.00 30.77 ?  1114 ARG   A NE  1 
ATOM   542  C CZ  . ARG   A 1 77  ? -15.968 -30.922 15.215  1.00 34.81 ?  1114 ARG   A CZ  1 
ATOM   543  N NH1 . ARG   A 1 77  ? -15.239 -29.892 15.611  1.00 28.10 ?  1114 ARG   A NH1 1 
ATOM   544  N NH2 . ARG   A 1 77  ? -16.823 -31.481 16.067  1.00 33.90 ?  1114 ARG   A NH2 1 
ATOM   545  N N   . ILE   A 1 78  ? -9.743  -31.572 10.991  1.00 19.69 ?  1115 ILE   A N   1 
ATOM   546  C CA  . ILE   A 1 78  ? -9.082  -32.380 9.970   1.00 21.04 ?  1115 ILE   A CA  1 
ATOM   547  C C   . ILE   A 1 78  ? -8.006  -33.206 10.670  1.00 22.74 ?  1115 ILE   A C   1 
ATOM   548  O O   . ILE   A 1 78  ? -6.978  -32.678 11.104  1.00 25.22 ?  1115 ILE   A O   1 
ATOM   549  C CB  . ILE   A 1 78  ? -8.505  -31.522 8.835   1.00 21.50 ?  1115 ILE   A CB  1 
ATOM   550  C CG1 . ILE   A 1 78  ? -7.498  -32.328 8.010   1.00 21.06 ?  1115 ILE   A CG1 1 
ATOM   551  C CG2 . ILE   A 1 78  ? -7.896  -30.234 9.365   1.00 19.85 ?  1115 ILE   A CG2 1 
ATOM   552  C CD1 . ILE   A 1 78  ? -6.967  -31.590 6.805   1.00 27.67 ?  1115 ILE   A CD1 1 
ATOM   553  N N   . THR   A 1 79  ? -8.258  -34.508 10.802  1.00 20.11 ?  1116 THR   A N   1 
ATOM   554  C CA  . THR   A 1 79  ? -7.474  -35.367 11.679  1.00 22.63 ?  1116 THR   A CA  1 
ATOM   555  C C   . THR   A 1 79  ? -6.258  -35.977 10.999  1.00 28.46 ?  1116 THR   A C   1 
ATOM   556  O O   . THR   A 1 79  ? -5.225  -36.167 11.652  1.00 24.41 ?  1116 THR   A O   1 
ATOM   557  C CB  . THR   A 1 79  ? -8.358  -36.490 12.229  1.00 15.96 ?  1116 THR   A CB  1 
ATOM   558  O OG1 . THR   A 1 79  ? -9.223  -36.962 11.189  1.00 19.68 ?  1116 THR   A OG1 1 
ATOM   559  C CG2 . THR   A 1 79  ? -9.201  -35.985 13.388  1.00 12.45 ?  1116 THR   A CG2 1 
ATOM   560  N N   . ASP   A 1 80  ? -6.356  -36.294 9.711   1.00 26.67 ?  1117 ASP   A N   1 
ATOM   561  C CA  . ASP   A 1 80  ? -5.260  -36.951 9.011   1.00 22.04 ?  1117 ASP   A CA  1 
ATOM   562  C C   . ASP   A 1 80  ? -4.124  -35.961 8.782   1.00 23.18 ?  1117 ASP   A C   1 
ATOM   563  O O   . ASP   A 1 80  ? -4.302  -34.948 8.097   1.00 18.50 ?  1117 ASP   A O   1 
ATOM   564  C CB  . ASP   A 1 80  ? -5.756  -37.530 7.688   1.00 22.68 ?  1117 ASP   A CB  1 
ATOM   565  C CG  . ASP   A 1 80  ? -4.707  -38.370 6.987   1.00 24.99 ?  1117 ASP   A CG  1 
ATOM   566  O OD1 . ASP   A 1 80  ? -4.210  -39.335 7.604   1.00 25.64 -1 1117 ASP   A OD1 1 
ATOM   567  O OD2 . ASP   A 1 80  ? -4.378  -38.065 5.821   1.00 31.22 ?  1117 ASP   A OD2 1 
ATOM   568  N N   . ILE   A 1 81  ? -2.954  -36.259 9.347   1.00 21.75 ?  1118 ILE   A N   1 
ATOM   569  C CA  . ILE   A 1 81  ? -1.801  -35.365 9.289   1.00 16.54 ?  1118 ILE   A CA  1 
ATOM   570  C C   . ILE   A 1 81  ? -1.139  -35.435 7.917   1.00 19.64 ?  1118 ILE   A C   1 
ATOM   571  O O   . ILE   A 1 81  ? -0.029  -34.927 7.725   1.00 22.16 ?  1118 ILE   A O   1 
ATOM   572  C CB  . ILE   A 1 81  ? -0.789  -35.695 10.401  1.00 13.09 ?  1118 ILE   A CB  1 
ATOM   573  N N   . GLY   A 1 82  ? -1.808  -36.074 6.962   1.00 19.44 ?  1119 GLY   A N   1 
ATOM   574  C CA  . GLY   A 1 82  ? -1.368  -36.073 5.582   1.00 18.85 ?  1119 GLY   A CA  1 
ATOM   575  C C   . GLY   A 1 82  ? -2.323  -35.269 4.729   1.00 17.86 ?  1119 GLY   A C   1 
ATOM   576  O O   . GLY   A 1 82  ? -1.943  -34.719 3.691   1.00 16.17 ?  1119 GLY   A O   1 
ATOM   577  N N   . GLU   A 1 83  ? -3.584  -35.209 5.163   1.00 19.09 ?  1120 GLU   A N   1 
ATOM   578  C CA  . GLU   A 1 83  ? -4.533  -34.285 4.552   1.00 22.23 ?  1120 GLU   A CA  1 
ATOM   579  C C   . GLU   A 1 83  ? -4.217  -32.850 4.949   1.00 18.25 ?  1120 GLU   A C   1 
ATOM   580  O O   . GLU   A 1 83  ? -4.395  -31.923 4.149   1.00 21.48 ?  1120 GLU   A O   1 
ATOM   581  C CB  . GLU   A 1 83  ? -5.960  -34.656 4.953   1.00 24.59 ?  1120 GLU   A CB  1 
ATOM   582  N N   . VAL   A 1 84  ? -3.753  -32.650 6.187   1.00 20.21 ?  1121 VAL   A N   1 
ATOM   583  C CA  . VAL   A 1 84  ? -3.254  -31.343 6.609   1.00 18.50 ?  1121 VAL   A CA  1 
ATOM   584  C C   . VAL   A 1 84  ? -2.163  -30.868 5.661   1.00 19.36 ?  1121 VAL   A C   1 
ATOM   585  O O   . VAL   A 1 84  ? -2.185  -29.732 5.172   1.00 18.03 ?  1121 VAL   A O   1 
ATOM   586  C CB  . VAL   A 1 84  ? -2.743  -31.409 8.060   1.00 18.87 ?  1121 VAL   A CB  1 
ATOM   587  C CG1 . VAL   A 1 84  ? -1.989  -30.136 8.418   1.00 18.80 ?  1121 VAL   A CG1 1 
ATOM   588  C CG2 . VAL   A 1 84  ? -3.895  -31.647 9.023   1.00 16.60 ?  1121 VAL   A CG2 1 
ATOM   589  N N   . SER   A 1 85  ? -1.193  -31.743 5.381   1.00 18.39 ?  1122 SER   A N   1 
ATOM   590  C CA  . SER   A 1 85  ? -0.105  -31.390 4.476   1.00 20.30 ?  1122 SER   A CA  1 
ATOM   591  C C   . SER   A 1 85  ? -0.629  -31.054 3.087   1.00 16.78 ?  1122 SER   A C   1 
ATOM   592  O O   . SER   A 1 85  ? -0.097  -30.164 2.413   1.00 13.72 ?  1122 SER   A O   1 
ATOM   593  C CB  . SER   A 1 85  ? 0.901   -32.535 4.404   1.00 17.35 ?  1122 SER   A CB  1 
ATOM   594  O OG  . SER   A 1 85  ? 1.085   -33.123 5.680   1.00 21.18 ?  1122 SER   A OG  1 
ATOM   595  N N   . GLN   A 1 86  ? -1.667  -31.763 2.638   1.00 17.45 ?  1123 GLN   A N   1 
ATOM   596  C CA  . GLN   A 1 86  ? -2.299  -31.413 1.372   1.00 16.33 ?  1123 GLN   A CA  1 
ATOM   597  C C   . GLN   A 1 86  ? -2.928  -30.030 1.443   1.00 17.35 ?  1123 GLN   A C   1 
ATOM   598  O O   . GLN   A 1 86  ? -2.841  -29.252 0.488   1.00 20.79 ?  1123 GLN   A O   1 
ATOM   599  C CB  . GLN   A 1 86  ? -3.348  -32.460 0.997   1.00 15.20 ?  1123 GLN   A CB  1 
ATOM   600  N N   . PHE   A 1 87  ? -3.553  -29.700 2.577   1.00 15.74 ?  1124 PHE   A N   1 
ATOM   601  C CA  . PHE   A 1 87  ? -4.202  -28.400 2.717   1.00 16.59 ?  1124 PHE   A CA  1 
ATOM   602  C C   . PHE   A 1 87  ? -3.188  -27.265 2.664   1.00 16.82 ?  1124 PHE   A C   1 
ATOM   603  O O   . PHE   A 1 87  ? -3.423  -26.241 2.011   1.00 12.89 ?  1124 PHE   A O   1 
ATOM   604  C CB  . PHE   A 1 87  ? -4.998  -28.352 4.020   1.00 16.41 ?  1124 PHE   A CB  1 
ATOM   605  C CG  . PHE   A 1 87  ? -5.895  -27.154 4.138   1.00 11.10 ?  1124 PHE   A CG  1 
ATOM   606  C CD1 . PHE   A 1 87  ? -6.795  -26.843 3.133   1.00 14.75 ?  1124 PHE   A CD1 1 
ATOM   607  C CD2 . PHE   A 1 87  ? -5.842  -26.342 5.258   1.00 13.36 ?  1124 PHE   A CD2 1 
ATOM   608  C CE1 . PHE   A 1 87  ? -7.622  -25.742 3.240   1.00 14.76 ?  1124 PHE   A CE1 1 
ATOM   609  C CE2 . PHE   A 1 87  ? -6.667  -25.239 5.372   1.00 15.73 ?  1124 PHE   A CE2 1 
ATOM   610  C CZ  . PHE   A 1 87  ? -7.558  -24.939 4.361   1.00 11.35 ?  1124 PHE   A CZ  1 
ATOM   611  N N   . LEU   A 1 88  ? -2.051  -27.424 3.348   1.00 14.91 ?  1125 LEU   A N   1 
ATOM   612  C CA  . LEU   A 1 88  ? -0.998  -26.419 3.263   1.00 13.29 ?  1125 LEU   A CA  1 
ATOM   613  C C   . LEU   A 1 88  ? -0.406  -26.353 1.862   1.00 13.64 ?  1125 LEU   A C   1 
ATOM   614  O O   . LEU   A 1 88  ? 0.100   -25.302 1.451   1.00 17.14 ?  1125 LEU   A O   1 
ATOM   615  C CB  . LEU   A 1 88  ? 0.090   -26.709 4.296   1.00 12.16 ?  1125 LEU   A CB  1 
ATOM   616  C CG  . LEU   A 1 88  ? -0.355  -26.656 5.760   1.00 10.54 ?  1125 LEU   A CG  1 
ATOM   617  C CD1 . LEU   A 1 88  ? 0.694   -27.271 6.672   1.00 10.68 ?  1125 LEU   A CD1 1 
ATOM   618  C CD2 . LEU   A 1 88  ? -0.661  -25.228 6.181   1.00 13.54 ?  1125 LEU   A CD2 1 
ATOM   619  N N   . THR   A 1 89  ? -0.463  -27.458 1.115   1.00 12.46 ?  1126 THR   A N   1 
ATOM   620  C CA  . THR   A 1 89  ? -0.030  -27.437 -0.278  1.00 14.99 ?  1126 THR   A CA  1 
ATOM   621  C C   . THR   A 1 89  ? -0.951  -26.572 -1.126  1.00 14.62 ?  1126 THR   A C   1 
ATOM   622  O O   . THR   A 1 89  ? -0.489  -25.852 -2.020  1.00 12.22 ?  1126 THR   A O   1 
ATOM   623  C CB  . THR   A 1 89  ? 0.016   -28.859 -0.842  1.00 19.56 ?  1126 THR   A CB  1 
ATOM   624  O OG1 . THR   A 1 89  ? 0.649   -29.735 0.100   1.00 12.47 ?  1126 THR   A OG1 1 
ATOM   625  C CG2 . THR   A 1 89  ? 0.780   -28.892 -2.162  1.00 15.14 ?  1126 THR   A CG2 1 
ATOM   626  N N   . GLU   A 1 90  ? -2.258  -26.627 -0.856  1.00 20.01 ?  1127 GLU   A N   1 
ATOM   627  C CA  . GLU   A 1 90  ? -3.221  -25.933 -1.704  1.00 17.06 ?  1127 GLU   A CA  1 
ATOM   628  C C   . GLU   A 1 90  ? -3.098  -24.420 -1.576  1.00 16.68 ?  1127 GLU   A C   1 
ATOM   629  O O   . GLU   A 1 90  ? -3.186  -23.700 -2.577  1.00 15.79 ?  1127 GLU   A O   1 
ATOM   630  C CB  . GLU   A 1 90  ? -4.648  -26.367 -1.360  1.00 19.00 ?  1127 GLU   A CB  1 
ATOM   631  C CG  . GLU   A 1 90  ? -4.872  -27.866 -1.245  1.00 23.57 ?  1127 GLU   A CG  1 
ATOM   632  C CD  . GLU   A 1 90  ? -4.588  -28.610 -2.533  1.00 29.10 ?  1127 GLU   A CD  1 
ATOM   633  O OE1 . GLU   A 1 90  ? -5.089  -28.179 -3.592  1.00 39.84 ?  1127 GLU   A OE1 1 
ATOM   634  O OE2 . GLU   A 1 90  ? -3.868  -29.630 -2.484  1.00 32.44 -1 1127 GLU   A OE2 1 
ATOM   635  N N   . GLY   A 1 91  ? -2.895  -23.916 -0.361  1.00 17.34 ?  1128 GLY   A N   1 
ATOM   636  C CA  . GLY   A 1 91  ? -3.104  -22.501 -0.131  1.00 19.96 ?  1128 GLY   A CA  1 
ATOM   637  C C   . GLY   A 1 91  ? -1.951  -21.666 0.387   1.00 17.50 ?  1128 GLY   A C   1 
ATOM   638  O O   . GLY   A 1 91  ? -2.134  -20.469 0.627   1.00 20.79 ?  1128 GLY   A O   1 
ATOM   639  N N   . ILE   A 1 92  ? -0.765  -22.254 0.563   1.00 20.17 ?  1129 ILE   A N   1 
ATOM   640  C CA  . ILE   A 1 92  ? 0.365   -21.477 1.064   1.00 16.71 ?  1129 ILE   A CA  1 
ATOM   641  C C   . ILE   A 1 92  ? 0.758   -20.372 0.093   1.00 17.50 ?  1129 ILE   A C   1 
ATOM   642  O O   . ILE   A 1 92  ? 1.428   -19.411 0.486   1.00 19.93 ?  1129 ILE   A O   1 
ATOM   643  C CB  . ILE   A 1 92  ? 1.564   -22.395 1.374   1.00 16.76 ?  1129 ILE   A CB  1 
ATOM   644  C CG1 . ILE   A 1 92  ? 2.565   -21.668 2.274   1.00 15.38 ?  1129 ILE   A CG1 1 
ATOM   645  C CG2 . ILE   A 1 92  ? 2.238   -22.846 0.091   1.00 16.31 ?  1129 ILE   A CG2 1 
ATOM   646  C CD1 . ILE   A 1 92  ? 1.952   -21.113 3.539   1.00 13.45 ?  1129 ILE   A CD1 1 
ATOM   647  N N   . ILE   A 1 93  ? 0.334   -20.471 -1.169  1.00 17.21 ?  1130 ILE   A N   1 
ATOM   648  C CA  . ILE   A 1 93  ? 0.549   -19.412 -2.143  1.00 19.01 ?  1130 ILE   A CA  1 
ATOM   649  C C   . ILE   A 1 93  ? -0.127  -18.107 -1.736  1.00 20.38 ?  1130 ILE   A C   1 
ATOM   650  O O   . ILE   A 1 93  ? 0.145   -17.061 -2.332  1.00 18.16 ?  1130 ILE   A O   1 
ATOM   651  C CB  . ILE   A 1 93  ? 0.062   -19.882 -3.534  1.00 20.26 ?  1130 ILE   A CB  1 
ATOM   652  C CG1 . ILE   A 1 93  ? 0.622   -18.989 -4.645  1.00 19.65 ?  1130 ILE   A CG1 1 
ATOM   653  C CG2 . ILE   A 1 93  ? -1.458  -19.933 -3.580  1.00 18.56 ?  1130 ILE   A CG2 1 
ATOM   654  C CD1 . ILE   A 1 93  ? 0.568   -19.618 -6.021  1.00 21.20 ?  1130 ILE   A CD1 1 
ATOM   655  N N   . MET   A 1 94  ? -1.000  -18.146 -0.725  1.00 21.30 ?  1131 MET   A N   1 
ATOM   656  C CA  . MET   A 1 94  ? -1.583  -16.923 -0.183  1.00 20.42 ?  1131 MET   A CA  1 
ATOM   657  C C   . MET   A 1 94  ? -0.512  -15.956 0.305   1.00 22.03 ?  1131 MET   A C   1 
ATOM   658  O O   . MET   A 1 94  ? -0.724  -14.737 0.291   1.00 23.03 ?  1131 MET   A O   1 
ATOM   659  C CB  . MET   A 1 94  ? -2.542  -17.272 0.956   1.00 18.20 ?  1131 MET   A CB  1 
ATOM   660  C CG  . MET   A 1 94  ? -3.078  -16.079 1.733   1.00 22.39 ?  1131 MET   A CG  1 
ATOM   661  S SD  . MET   A 1 94  ? -4.392  -16.531 2.879   1.00 39.46 ?  1131 MET   A SD  1 
ATOM   662  C CE  . MET   A 1 94  ? -4.662  -18.230 2.407   1.00 15.52 ?  1131 MET   A CE  1 
ATOM   663  N N   . LYS   A 1 95  ? 0.644   -16.475 0.728   1.00 22.55 ?  1132 LYS   A N   1 
ATOM   664  C CA  . LYS   A 1 95  ? 1.708   -15.613 1.234   1.00 22.23 ?  1132 LYS   A CA  1 
ATOM   665  C C   . LYS   A 1 95  ? 2.204   -14.641 0.170   1.00 20.61 ?  1132 LYS   A C   1 
ATOM   666  O O   . LYS   A 1 95  ? 2.733   -13.575 0.505   1.00 20.24 ?  1132 LYS   A O   1 
ATOM   667  C CB  . LYS   A 1 95  ? 2.863   -16.464 1.768   1.00 21.25 ?  1132 LYS   A CB  1 
ATOM   668  C CG  . LYS   A 1 95  ? 3.840   -16.950 0.705   1.00 21.72 ?  1132 LYS   A CG  1 
ATOM   669  C CD  . LYS   A 1 95  ? 4.894   -17.876 1.294   1.00 20.75 ?  1132 LYS   A CD  1 
ATOM   670  C CE  . LYS   A 1 95  ? 6.141   -17.924 0.421   1.00 18.64 ?  1132 LYS   A CE  1 
ATOM   671  N NZ  . LYS   A 1 95  ? 7.048   -16.770 0.676   1.00 26.24 ?  1132 LYS   A NZ  1 
ATOM   672  N N   . ASP   A 1 96  ? 2.036   -14.978 -1.110  1.00 20.68 ?  1133 ASP   A N   1 
ATOM   673  C CA  . ASP   A 1 96  ? 2.461   -14.102 -2.194  1.00 23.45 ?  1133 ASP   A CA  1 
ATOM   674  C C   . ASP   A 1 96  ? 1.429   -13.039 -2.546  1.00 19.60 ?  1133 ASP   A C   1 
ATOM   675  O O   . ASP   A 1 96  ? 1.756   -12.107 -3.289  1.00 23.30 ?  1133 ASP   A O   1 
ATOM   676  C CB  . ASP   A 1 96  ? 2.779   -14.925 -3.446  1.00 25.60 ?  1133 ASP   A CB  1 
ATOM   677  C CG  . ASP   A 1 96  ? 3.789   -16.024 -3.184  1.00 26.99 ?  1133 ASP   A CG  1 
ATOM   678  O OD1 . ASP   A 1 96  ? 4.536   -15.922 -2.189  1.00 25.78 ?  1133 ASP   A OD1 1 
ATOM   679  O OD2 . ASP   A 1 96  ? 3.836   -16.989 -3.974  1.00 34.64 -1 1133 ASP   A OD2 1 
ATOM   680  N N   . PHE   A 1 97  ? 0.204   -13.149 -2.038  1.00 18.65 ?  1134 PHE   A N   1 
ATOM   681  C CA  . PHE   A 1 97  ? -0.873  -12.242 -2.408  1.00 21.53 ?  1134 PHE   A CA  1 
ATOM   682  C C   . PHE   A 1 97  ? -0.923  -11.061 -1.446  1.00 17.24 ?  1134 PHE   A C   1 
ATOM   683  O O   . PHE   A 1 97  ? -0.835  -11.239 -0.227  1.00 21.36 ?  1134 PHE   A O   1 
ATOM   684  C CB  . PHE   A 1 97  ? -2.215  -12.976 -2.415  1.00 19.64 ?  1134 PHE   A CB  1 
ATOM   685  C CG  . PHE   A 1 97  ? -2.286  -14.101 -3.409  1.00 22.49 ?  1134 PHE   A CG  1 
ATOM   686  C CD1 . PHE   A 1 97  ? -1.529  -14.070 -4.569  1.00 20.52 ?  1134 PHE   A CD1 1 
ATOM   687  C CD2 . PHE   A 1 97  ? -3.111  -15.191 -3.184  1.00 23.77 ?  1134 PHE   A CD2 1 
ATOM   688  C CE1 . PHE   A 1 97  ? -1.592  -15.105 -5.483  1.00 20.11 ?  1134 PHE   A CE1 1 
ATOM   689  C CE2 . PHE   A 1 97  ? -3.179  -16.228 -4.096  1.00 20.77 ?  1134 PHE   A CE2 1 
ATOM   690  C CZ  . PHE   A 1 97  ? -2.419  -16.184 -5.247  1.00 17.66 ?  1134 PHE   A CZ  1 
ATOM   691  N N   . SER   A 1 98  ? -1.068  -9.858  -2.000  1.00 16.91 ?  1135 SER   A N   1 
ATOM   692  C CA  . SER   A 1 98  ? -1.156  -8.643  -1.192  1.00 19.98 ?  1135 SER   A CA  1 
ATOM   693  C C   . SER   A 1 98  ? -1.987  -7.622  -1.956  1.00 17.97 ?  1135 SER   A C   1 
ATOM   694  O O   . SER   A 1 98  ? -1.521  -7.060  -2.951  1.00 14.26 ?  1135 SER   A O   1 
ATOM   695  C CB  . SER   A 1 98  ? 0.230   -8.091  -0.870  1.00 17.62 ?  1135 SER   A CB  1 
ATOM   696  O OG  . SER   A 1 98  ? 0.140   -6.961  -0.020  1.00 23.92 ?  1135 SER   A OG  1 
ATOM   697  N N   . HIS   A 1 99  ? -3.214  -7.381  -1.486  1.00 16.74 ?  1136 HIS   A N   1 
ATOM   698  C CA  . HIS   A 1 99  ? -4.134  -6.444  -2.111  1.00 11.74 ?  1136 HIS   A CA  1 
ATOM   699  C C   . HIS   A 1 99  ? -5.083  -5.938  -1.036  1.00 14.59 ?  1136 HIS   A C   1 
ATOM   700  O O   . HIS   A 1 99  ? -5.433  -6.702  -0.124  1.00 12.15 ?  1136 HIS   A O   1 
ATOM   701  C CB  . HIS   A 1 99  ? -4.923  -7.094  -3.253  1.00 13.17 ?  1136 HIS   A CB  1 
ATOM   702  C CG  . HIS   A 1 99  ? -5.685  -6.119  -4.098  1.00 15.44 ?  1136 HIS   A CG  1 
ATOM   703  N ND1 . HIS   A 1 99  ? -6.952  -5.684  -3.773  1.00 14.39 ?  1136 HIS   A ND1 1 
ATOM   704  C CD2 . HIS   A 1 99  ? -5.357  -5.490  -5.252  1.00 15.47 ?  1136 HIS   A CD2 1 
ATOM   705  C CE1 . HIS   A 1 99  ? -7.373  -4.833  -4.691  1.00 10.70 ?  1136 HIS   A CE1 1 
ATOM   706  N NE2 . HIS   A 1 99  ? -6.424  -4.698  -5.600  1.00 13.68 ?  1136 HIS   A NE2 1 
ATOM   707  N N   . PRO   A 1 100 ? -5.500  -4.670  -1.097  1.00 13.83 ?  1137 PRO   A N   1 
ATOM   708  C CA  . PRO   A 1 100 ? -6.419  -4.156  -0.069  1.00 11.63 ?  1137 PRO   A CA  1 
ATOM   709  C C   . PRO   A 1 100 ? -7.764  -4.859  -0.039  1.00 13.68 ?  1137 PRO   A C   1 
ATOM   710  O O   . PRO   A 1 100 ? -8.413  -4.867  1.013   1.00 14.58 ?  1137 PRO   A O   1 
ATOM   711  C CB  . PRO   A 1 100 ? -6.568  -2.673  -0.442  1.00 12.22 ?  1137 PRO   A CB  1 
ATOM   712  C CG  . PRO   A 1 100 ? -6.140  -2.589  -1.878  1.00 12.93 ?  1137 PRO   A CG  1 
ATOM   713  C CD  . PRO   A 1 100 ? -5.057  -3.608  -2.015  1.00 12.04 ?  1137 PRO   A CD  1 
ATOM   714  N N   . ASN   A 1 101 ? -8.205  -5.453  -1.148  1.00 12.83 ?  1138 ASN   A N   1 
ATOM   715  C CA  . ASN   A 1 101 ? -9.492  -6.132  -1.214  1.00 14.63 ?  1138 ASN   A CA  1 
ATOM   716  C C   . ASN   A 1 101 ? -9.363  -7.650  -1.136  1.00 14.60 ?  1138 ASN   A C   1 
ATOM   717  O O   . ASN   A 1 101 ? -10.288 -8.367  -1.533  1.00 17.64 ?  1138 ASN   A O   1 
ATOM   718  C CB  . ASN   A 1 101 ? -10.236 -5.731  -2.488  1.00 11.90 ?  1138 ASN   A CB  1 
ATOM   719  C CG  . ASN   A 1 101 ? -10.506 -4.240  -2.561  1.00 12.40 ?  1138 ASN   A CG  1 
ATOM   720  O OD1 . ASN   A 1 101 ? -10.137 -3.577  -3.530  1.00 11.64 ?  1138 ASN   A OD1 1 
ATOM   721  N ND2 . ASN   A 1 101 ? -11.152 -3.705  -1.531  1.00 9.22  ?  1138 ASN   A ND2 1 
ATOM   722  N N   . VAL   A 1 102 ? -8.240  -8.153  -0.629  1.00 13.93 ?  1139 VAL   A N   1 
ATOM   723  C CA  . VAL   A 1 102 ? -7.988  -9.584  -0.519  1.00 14.54 ?  1139 VAL   A CA  1 
ATOM   724  C C   . VAL   A 1 102 ? -7.610  -9.892  0.921   1.00 14.48 ?  1139 VAL   A C   1 
ATOM   725  O O   . VAL   A 1 102 ? -6.793  -9.180  1.517   1.00 16.20 ?  1139 VAL   A O   1 
ATOM   726  C CB  . VAL   A 1 102 ? -6.875  -10.041 -1.483  1.00 15.14 ?  1139 VAL   A CB  1 
ATOM   727  C CG1 . VAL   A 1 102 ? -6.455  -11.469 -1.181  1.00 12.87 ?  1139 VAL   A CG1 1 
ATOM   728  C CG2 . VAL   A 1 102 ? -7.338  -9.913  -2.926  1.00 14.56 ?  1139 VAL   A CG2 1 
ATOM   729  N N   . LEU   A 1 103 ? -8.214  -10.935 1.485   1.00 15.45 ?  1140 LEU   A N   1 
ATOM   730  C CA  . LEU   A 1 103 ? -7.848  -11.367 2.827   1.00 18.01 ?  1140 LEU   A CA  1 
ATOM   731  C C   . LEU   A 1 103 ? -6.406  -11.851 2.835   1.00 15.30 ?  1140 LEU   A C   1 
ATOM   732  O O   . LEU   A 1 103 ? -6.048  -12.777 2.101   1.00 15.77 ?  1140 LEU   A O   1 
ATOM   733  C CB  . LEU   A 1 103 ? -8.783  -12.473 3.308   1.00 17.50 ?  1140 LEU   A CB  1 
ATOM   734  C CG  . LEU   A 1 103 ? -8.422  -13.062 4.674   1.00 20.24 ?  1140 LEU   A CG  1 
ATOM   735  C CD1 . LEU   A 1 103 ? -8.785  -12.092 5.787   1.00 20.60 ?  1140 LEU   A CD1 1 
ATOM   736  C CD2 . LEU   A 1 103 ? -9.095  -14.409 4.888   1.00 14.25 ?  1140 LEU   A CD2 1 
ATOM   737  N N   . SER   A 1 104 ? -5.579  -11.215 3.654   1.00 17.77 ?  1141 SER   A N   1 
ATOM   738  C CA  . SER   A 1 104 ? -4.177  -11.580 3.756   1.00 17.45 ?  1141 SER   A CA  1 
ATOM   739  C C   . SER   A 1 104 ? -3.979  -12.631 4.843   1.00 19.51 ?  1141 SER   A C   1 
ATOM   740  O O   . SER   A 1 104 ? -4.895  -12.971 5.595   1.00 21.33 ?  1141 SER   A O   1 
ATOM   741  C CB  . SER   A 1 104 ? -3.323  -10.345 4.042   1.00 16.69 ?  1141 SER   A CB  1 
ATOM   742  O OG  . SER   A 1 104 ? -3.763  -9.686  5.216   1.00 23.32 ?  1141 SER   A OG  1 
ATOM   743  N N   . LEU   A 1 105 ? -2.758  -13.153 4.917   1.00 17.48 ?  1142 LEU   A N   1 
ATOM   744  C CA  . LEU   A 1 105 ? -2.387  -14.149 5.911   1.00 21.28 ?  1142 LEU   A CA  1 
ATOM   745  C C   . LEU   A 1 105 ? -1.226  -13.615 6.735   1.00 13.47 ?  1142 LEU   A C   1 
ATOM   746  O O   . LEU   A 1 105 ? -0.216  -13.172 6.178   1.00 11.27 ?  1142 LEU   A O   1 
ATOM   747  C CB  . LEU   A 1 105 ? -2.015  -15.478 5.246   1.00 19.04 ?  1142 LEU   A CB  1 
ATOM   748  C CG  . LEU   A 1 105 ? -1.587  -16.624 6.164   1.00 16.77 ?  1142 LEU   A CG  1 
ATOM   749  C CD1 . LEU   A 1 105 ? -2.244  -17.920 5.735   1.00 19.90 ?  1142 LEU   A CD1 1 
ATOM   750  C CD2 . LEU   A 1 105 ? -0.086  -16.775 6.147   1.00 12.95 ?  1142 LEU   A CD2 1 
ATOM   751  N N   . LEU   A 1 106 ? -1.375  -13.654 8.057   1.00 11.95 ?  1143 LEU   A N   1 
ATOM   752  C CA  . LEU   A 1 106 ? -0.342  -13.157 8.956   1.00 12.31 ?  1143 LEU   A CA  1 
ATOM   753  C C   . LEU   A 1 106 ? 0.720   -14.206 9.263   1.00 14.36 ?  1143 LEU   A C   1 
ATOM   754  O O   . LEU   A 1 106 ? 1.909   -13.876 9.333   1.00 15.98 ?  1143 LEU   A O   1 
ATOM   755  C CB  . LEU   A 1 106 ? -0.975  -12.654 10.255  1.00 14.05 ?  1143 LEU   A CB  1 
ATOM   756  C CG  . LEU   A 1 106 ? -2.090  -11.627 10.058  1.00 15.04 ?  1143 LEU   A CG  1 
ATOM   757  C CD1 . LEU   A 1 106 ? -2.691  -11.217 11.392  1.00 17.27 ?  1143 LEU   A CD1 1 
ATOM   758  C CD2 . LEU   A 1 106 ? -1.578  -10.413 9.291   1.00 9.04  ?  1143 LEU   A CD2 1 
ATOM   759  N N   . GLY   A 1 107 ? 0.326   -15.460 9.443   1.00 15.29 ?  1144 GLY   A N   1 
ATOM   760  C CA  . GLY   A 1 107 ? 1.301   -16.497 9.711   1.00 16.73 ?  1144 GLY   A CA  1 
ATOM   761  C C   . GLY   A 1 107 ? 0.641   -17.809 10.059  1.00 13.92 ?  1144 GLY   A C   1 
ATOM   762  O O   . GLY   A 1 107 ? -0.580  -17.906 10.216  1.00 14.48 ?  1144 GLY   A O   1 
ATOM   763  N N   . ILE   A 1 108 ? 1.485   -18.833 10.171  1.00 16.49 ?  1145 ILE   A N   1 
ATOM   764  C CA  . ILE   A 1 108 ? 1.083   -20.164 10.612  1.00 11.60 ?  1145 ILE   A CA  1 
ATOM   765  C C   . ILE   A 1 108 ? 1.825   -20.461 11.905  1.00 12.19 ?  1145 ILE   A C   1 
ATOM   766  O O   . ILE   A 1 108 ? 3.061   -20.410 11.942  1.00 14.76 ?  1145 ILE   A O   1 
ATOM   767  C CB  . ILE   A 1 108 ? 1.381   -21.236 9.553   1.00 11.56 ?  1145 ILE   A CB  1 
ATOM   768  C CG1 . ILE   A 1 108 ? 0.801   -20.829 8.201   1.00 7.69  ?  1145 ILE   A CG1 1 
ATOM   769  C CG2 . ILE   A 1 108 ? 0.826   -22.584 9.989   1.00 11.23 ?  1145 ILE   A CG2 1 
ATOM   770  C CD1 . ILE   A 1 108 ? 1.466   -21.509 7.038   1.00 8.62  ?  1145 ILE   A CD1 1 
ATOM   771  N N   . CYS   A 1 109 ? 1.078   -20.766 12.960  1.00 7.87  ?  1146 CYS   A N   1 
ATOM   772  C CA  . CYS   A 1 109 ? 1.650   -21.037 14.271  1.00 10.81 ?  1146 CYS   A CA  1 
ATOM   773  C C   . CYS   A 1 109 ? 1.772   -22.540 14.477  1.00 15.91 ?  1146 CYS   A C   1 
ATOM   774  O O   . CYS   A 1 109 ? 0.785   -23.271 14.337  1.00 15.13 ?  1146 CYS   A O   1 
ATOM   775  C CB  . CYS   A 1 109 ? 0.796   -20.420 15.378  1.00 12.04 ?  1146 CYS   A CB  1 
ATOM   776  S SG  . CYS   A 1 109 ? 1.587   -20.419 17.001  1.00 16.50 ?  1146 CYS   A SG  1 
ATOM   777  N N   . LEU   A 1 110 ? 2.981   -22.992 14.805  1.00 17.13 ?  1147 LEU   A N   1 
ATOM   778  C CA  . LEU   A 1 110 ? 3.260   -24.404 15.063  1.00 19.46 ?  1147 LEU   A CA  1 
ATOM   779  C C   . LEU   A 1 110 ? 2.915   -25.261 13.849  1.00 20.03 ?  1147 LEU   A C   1 
ATOM   780  O O   . LEU   A 1 110 ? 3.736   -25.435 12.948  1.00 23.44 ?  1147 LEU   A O   1 
ATOM   781  C CB  . LEU   A 1 110 ? 2.497   -24.881 16.309  1.00 16.37 ?  1147 LEU   A CB  1 
ATOM   782  C CG  . LEU   A 1 110 ? 2.311   -26.376 16.583  1.00 19.19 ?  1147 LEU   A CG  1 
ATOM   783  C CD1 . LEU   A 1 110 ? 2.321   -26.623 18.080  1.00 19.56 ?  1147 LEU   A CD1 1 
ATOM   784  C CD2 . LEU   A 1 110 ? 1.013   -26.903 15.980  1.00 26.66 ?  1147 LEU   A CD2 1 
ATOM   785  N N   . GLY   A 1 114 ? -3.601  -29.626 18.095  1.00 15.19 ?  1151 GLY   A N   1 
ATOM   786  C CA  . GLY   A 1 114 ? -2.406  -30.266 17.575  1.00 19.11 ?  1151 GLY   A CA  1 
ATOM   787  C C   . GLY   A 1 114 ? -2.076  -29.833 16.161  1.00 21.12 ?  1151 GLY   A C   1 
ATOM   788  O O   . GLY   A 1 114 ? -0.909  -29.774 15.772  1.00 16.34 ?  1151 GLY   A O   1 
ATOM   789  N N   . SER   A 1 115 ? -3.116  -29.533 15.387  1.00 20.92 ?  1152 SER   A N   1 
ATOM   790  C CA  . SER   A 1 115 ? -2.933  -29.043 14.035  1.00 15.94 ?  1152 SER   A CA  1 
ATOM   791  C C   . SER   A 1 115 ? -2.355  -27.628 14.064  1.00 17.05 ?  1152 SER   A C   1 
ATOM   792  O O   . SER   A 1 115 ? -2.415  -26.945 15.089  1.00 22.82 ?  1152 SER   A O   1 
ATOM   793  C CB  . SER   A 1 115 ? -4.264  -29.061 13.289  1.00 15.51 ?  1152 SER   A CB  1 
ATOM   794  N N   . PRO   A 1 116 ? -1.777  -27.168 12.955  1.00 18.98 ?  1153 PRO   A N   1 
ATOM   795  C CA  . PRO   A 1 116 ? -1.284  -25.786 12.902  1.00 15.11 ?  1153 PRO   A CA  1 
ATOM   796  C C   . PRO   A 1 116 ? -2.428  -24.788 13.008  1.00 14.86 ?  1153 PRO   A C   1 
ATOM   797  O O   . PRO   A 1 116 ? -3.612  -25.132 12.962  1.00 14.98 ?  1153 PRO   A O   1 
ATOM   798  C CB  . PRO   A 1 116 ? -0.588  -25.700 11.540  1.00 10.25 ?  1153 PRO   A CB  1 
ATOM   799  C CG  . PRO   A 1 116 ? -1.172  -26.812 10.740  1.00 17.13 ?  1153 PRO   A CG  1 
ATOM   800  C CD  . PRO   A 1 116 ? -1.452  -27.907 11.723  1.00 18.03 ?  1153 PRO   A CD  1 
ATOM   801  N N   . LEU   A 1 117 ? -2.050  -23.521 13.154  1.00 18.48 ?  1154 LEU   A N   1 
ATOM   802  C CA  . LEU   A 1 117 ? -2.996  -22.431 13.348  1.00 13.60 ?  1154 LEU   A CA  1 
ATOM   803  C C   . LEU   A 1 117 ? -2.895  -21.456 12.186  1.00 11.94 ?  1154 LEU   A C   1 
ATOM   804  O O   . LEU   A 1 117 ? -1.798  -21.004 11.842  1.00 12.70 ?  1154 LEU   A O   1 
ATOM   805  C CB  . LEU   A 1 117 ? -2.733  -21.707 14.671  1.00 10.65 ?  1154 LEU   A CB  1 
ATOM   806  C CG  . LEU   A 1 117 ? -3.117  -22.478 15.935  1.00 10.83 ?  1154 LEU   A CG  1 
ATOM   807  C CD1 . LEU   A 1 117 ? -2.640  -21.749 17.182  1.00 10.69 ?  1154 LEU   A CD1 1 
ATOM   808  C CD2 . LEU   A 1 117 ? -4.619  -22.711 15.985  1.00 8.30  ?  1154 LEU   A CD2 1 
ATOM   809  N N   . VAL   A 1 118 ? -4.037  -21.137 11.585  1.00 14.94 ?  1155 VAL   A N   1 
ATOM   810  C CA  . VAL   A 1 118 ? -4.109  -20.148 10.516  1.00 15.90 ?  1155 VAL   A CA  1 
ATOM   811  C C   . VAL   A 1 118 ? -4.382  -18.791 11.153  1.00 15.28 ?  1155 VAL   A C   1 
ATOM   812  O O   . VAL   A 1 118 ? -5.488  -18.532 11.634  1.00 16.71 ?  1155 VAL   A O   1 
ATOM   813  C CB  . VAL   A 1 118 ? -5.189  -20.505 9.489   1.00 19.42 ?  1155 VAL   A CB  1 
ATOM   814  C CG1 . VAL   A 1 118 ? -4.981  -19.716 8.211   1.00 14.86 ?  1155 VAL   A CG1 1 
ATOM   815  C CG2 . VAL   A 1 118 ? -5.188  -22.002 9.213   1.00 16.79 ?  1155 VAL   A CG2 1 
ATOM   816  N N   . VAL   A 1 119 ? -3.375  -17.924 11.160  1.00 15.29 ?  1156 VAL   A N   1 
ATOM   817  C CA  . VAL   A 1 119 ? -3.485  -16.593 11.745  1.00 16.21 ?  1156 VAL   A CA  1 
ATOM   818  C C   . VAL   A 1 119 ? -3.844  -15.614 10.637  1.00 15.33 ?  1156 VAL   A C   1 
ATOM   819  O O   . VAL   A 1 119 ? -3.098  -15.461 9.662   1.00 14.95 ?  1156 VAL   A O   1 
ATOM   820  C CB  . VAL   A 1 119 ? -2.187  -16.183 12.456  1.00 12.36 ?  1156 VAL   A CB  1 
ATOM   821  C CG1 . VAL   A 1 119 ? -2.354  -14.828 13.119  1.00 13.92 ?  1156 VAL   A CG1 1 
ATOM   822  C CG2 . VAL   A 1 119 ? -1.800  -17.239 13.480  1.00 15.45 ?  1156 VAL   A CG2 1 
ATOM   823  N N   . LEU   A 1 120 ? -4.984  -14.957 10.786  1.00 15.85 ?  1157 LEU   A N   1 
ATOM   824  C CA  . LEU   A 1 120 ? -5.560  -14.075 9.785   1.00 13.90 ?  1157 LEU   A CA  1 
ATOM   825  C C   . LEU   A 1 120 ? -5.947  -12.761 10.441  1.00 18.60 ?  1157 LEU   A C   1 
ATOM   826  O O   . LEU   A 1 120 ? -6.155  -12.706 11.658  1.00 18.86 ?  1157 LEU   A O   1 
ATOM   827  C CB  . LEU   A 1 120 ? -6.793  -14.727 9.141   1.00 16.17 ?  1157 LEU   A CB  1 
ATOM   828  C CG  . LEU   A 1 120 ? -6.582  -16.163 8.659   1.00 18.09 ?  1157 LEU   A CG  1 
ATOM   829  C CD1 . LEU   A 1 120 ? -7.808  -17.008 8.937   1.00 13.13 ?  1157 LEU   A CD1 1 
ATOM   830  C CD2 . LEU   A 1 120 ? -6.236  -16.190 7.179   1.00 18.12 ?  1157 LEU   A CD2 1 
ATOM   831  N N   . PRO   A 1 121 ? -6.047  -11.680 9.669   1.00 16.94 ?  1158 PRO   A N   1 
ATOM   832  C CA  . PRO   A 1 121 ? -6.461  -10.403 10.260  1.00 18.35 ?  1158 PRO   A CA  1 
ATOM   833  C C   . PRO   A 1 121 ? -7.891  -10.473 10.778  1.00 17.07 ?  1158 PRO   A C   1 
ATOM   834  O O   . PRO   A 1 121 ? -8.752  -11.134 10.195  1.00 14.31 ?  1158 PRO   A O   1 
ATOM   835  C CB  . PRO   A 1 121 ? -6.324  -9.412  9.098   1.00 14.00 ?  1158 PRO   A CB  1 
ATOM   836  C CG  . PRO   A 1 121 ? -6.405  -10.255 7.870   1.00 17.44 ?  1158 PRO   A CG  1 
ATOM   837  C CD  . PRO   A 1 121 ? -5.748  -11.549 8.233   1.00 17.52 ?  1158 PRO   A CD  1 
ATOM   838  N N   . TYR   A 1 122 ? -8.130  -9.796  11.899  1.00 18.14 ?  1159 TYR   A N   1 
ATOM   839  C CA  . TYR   A 1 122 ? -9.465  -9.746  12.476  1.00 17.31 ?  1159 TYR   A CA  1 
ATOM   840  C C   . TYR   A 1 122 ? -10.378 -8.886  11.614  1.00 19.82 ?  1159 TYR   A C   1 
ATOM   841  O O   . TYR   A 1 122 ? -9.976  -7.831  11.120  1.00 22.63 ?  1159 TYR   A O   1 
ATOM   842  C CB  . TYR   A 1 122 ? -9.410  -9.188  13.897  1.00 19.88 ?  1159 TYR   A CB  1 
ATOM   843  C CG  . TYR   A 1 122 ? -10.754 -9.085  14.582  1.00 18.97 ?  1159 TYR   A CG  1 
ATOM   844  C CD1 . TYR   A 1 122 ? -11.447 -10.223 14.972  1.00 18.45 ?  1159 TYR   A CD1 1 
ATOM   845  C CD2 . TYR   A 1 122 ? -11.327 -7.848  14.848  1.00 17.49 ?  1159 TYR   A CD2 1 
ATOM   846  C CE1 . TYR   A 1 122 ? -12.673 -10.133 15.604  1.00 19.32 ?  1159 TYR   A CE1 1 
ATOM   847  C CE2 . TYR   A 1 122 ? -12.553 -7.749  15.478  1.00 19.59 ?  1159 TYR   A CE2 1 
ATOM   848  C CZ  . TYR   A 1 122 ? -13.222 -8.893  15.853  1.00 18.05 ?  1159 TYR   A CZ  1 
ATOM   849  O OH  . TYR   A 1 122 ? -14.442 -8.797  16.481  1.00 15.06 ?  1159 TYR   A OH  1 
ATOM   850  N N   . MET   A 1 123 ? -11.614 -9.341  11.438  1.00 14.67 ?  1160 MET   A N   1 
ATOM   851  C CA  . MET   A 1 123 ? -12.600 -8.655  10.608  1.00 15.21 ?  1160 MET   A CA  1 
ATOM   852  C C   . MET   A 1 123 ? -13.711 -8.152  11.520  1.00 17.17 ?  1160 MET   A C   1 
ATOM   853  O O   . MET   A 1 123 ? -14.563 -8.926  11.963  1.00 17.84 ?  1160 MET   A O   1 
ATOM   854  C CB  . MET   A 1 123 ? -13.125 -9.584  9.527   1.00 16.13 ?  1160 MET   A CB  1 
ATOM   855  C CG  . MET   A 1 123 ? -12.010 -10.126 8.693   1.00 16.44 ?  1160 MET   A CG  1 
ATOM   856  S SD  . MET   A 1 123 ? -11.389 -8.805  7.658   1.00 16.16 ?  1160 MET   A SD  1 
ATOM   857  C CE  . MET   A 1 123 ? -9.661  -8.822  8.114   1.00 12.97 ?  1160 MET   A CE  1 
ATOM   858  N N   . LYS   A 1 124 ? -13.696 -6.845  11.786  1.00 16.72 ?  1161 LYS   A N   1 
ATOM   859  C CA  . LYS   A 1 124 ? -14.541 -6.285  12.834  1.00 15.73 ?  1161 LYS   A CA  1 
ATOM   860  C C   . LYS   A 1 124 ? -16.025 -6.484  12.551  1.00 11.84 ?  1161 LYS   A C   1 
ATOM   861  O O   . LYS   A 1 124 ? -16.813 -6.653  13.488  1.00 15.01 ?  1161 LYS   A O   1 
ATOM   862  C CB  . LYS   A 1 124 ? -14.227 -4.800  13.008  1.00 16.90 ?  1161 LYS   A CB  1 
ATOM   863  C CG  . LYS   A 1 124 ? -14.656 -4.236  14.345  1.00 20.22 ?  1161 LYS   A CG  1 
ATOM   864  C CD  . LYS   A 1 124 ? -15.442 -2.954  14.168  1.00 20.17 ?  1161 LYS   A CD  1 
ATOM   865  C CE  . LYS   A 1 124 ? -16.184 -2.587  15.439  1.00 19.34 ?  1161 LYS   A CE  1 
ATOM   866  N NZ  . LYS   A 1 124 ? -16.825 -1.247  15.335  1.00 24.41 ?  1161 LYS   A NZ  1 
ATOM   867  N N   . HIS   A 1 125 ? -16.429 -6.476  11.281  1.00 13.53 ?  1162 HIS   A N   1 
ATOM   868  C CA  . HIS   A 1 125 ? -17.842 -6.505  10.925  1.00 14.19 ?  1162 HIS   A CA  1 
ATOM   869  C C   . HIS   A 1 125 ? -18.286 -7.832  10.319  1.00 17.68 ?  1162 HIS   A C   1 
ATOM   870  O O   . HIS   A 1 125 ? -19.381 -7.904  9.751   1.00 13.31 ?  1162 HIS   A O   1 
ATOM   871  C CB  . HIS   A 1 125 ? -18.166 -5.355  9.970   1.00 15.87 ?  1162 HIS   A CB  1 
ATOM   872  C CG  . HIS   A 1 125 ? -18.074 -4.005  10.608  1.00 17.79 ?  1162 HIS   A CG  1 
ATOM   873  N ND1 . HIS   A 1 125 ? -19.084 -3.480  11.386  1.00 20.47 ?  1162 HIS   A ND1 1 
ATOM   874  C CD2 . HIS   A 1 125 ? -17.090 -3.075  10.592  1.00 17.05 ?  1162 HIS   A CD2 1 
ATOM   875  C CE1 . HIS   A 1 125 ? -18.728 -2.284  11.819  1.00 20.20 ?  1162 HIS   A CE1 1 
ATOM   876  N NE2 . HIS   A 1 125 ? -17.522 -2.015  11.352  1.00 23.42 ?  1162 HIS   A NE2 1 
ATOM   877  N N   . GLY   A 1 126 ? -17.475 -8.880  10.429  1.00 13.71 ?  1163 GLY   A N   1 
ATOM   878  C CA  . GLY   A 1 126 ? -17.916 -10.173 9.949   1.00 15.05 ?  1163 GLY   A CA  1 
ATOM   879  C C   . GLY   A 1 126 ? -17.955 -10.257 8.430   1.00 15.41 ?  1163 GLY   A C   1 
ATOM   880  O O   . GLY   A 1 126 ? -17.311 -9.491  7.708   1.00 15.02 ?  1163 GLY   A O   1 
ATOM   881  N N   . ASP   A 1 127 ? -18.741 -11.214 7.949   1.00 9.76  ?  1164 ASP   A N   1 
ATOM   882  C CA  . ASP   A 1 127 ? -18.799 -11.525 6.530   1.00 11.62 ?  1164 ASP   A CA  1 
ATOM   883  C C   . ASP   A 1 127 ? -19.781 -10.609 5.806   1.00 12.94 ?  1164 ASP   A C   1 
ATOM   884  O O   . ASP   A 1 127 ? -20.666 -9.997  6.408   1.00 13.00 ?  1164 ASP   A O   1 
ATOM   885  C CB  . ASP   A 1 127 ? -19.178 -12.991 6.318   1.00 13.43 ?  1164 ASP   A CB  1 
ATOM   886  C CG  . ASP   A 1 127 ? -20.660 -13.238 6.476   1.00 12.38 ?  1164 ASP   A CG  1 
ATOM   887  O OD1 . ASP   A 1 127 ? -21.112 -13.392 7.629   1.00 11.70 ?  1164 ASP   A OD1 1 
ATOM   888  O OD2 . ASP   A 1 127 ? -21.369 -13.282 5.449   1.00 12.46 -1 1164 ASP   A OD2 1 
ATOM   889  N N   . LEU   A 1 128 ? -19.613 -10.536 4.483   1.00 11.49 ?  1165 LEU   A N   1 
ATOM   890  C CA  . LEU   A 1 128 ? -20.348 -9.560  3.684   1.00 11.53 ?  1165 LEU   A CA  1 
ATOM   891  C C   . LEU   A 1 128 ? -21.850 -9.817  3.718   1.00 14.18 ?  1165 LEU   A C   1 
ATOM   892  O O   . LEU   A 1 128 ? -22.647 -8.871  3.717   1.00 16.91 ?  1165 LEU   A O   1 
ATOM   893  C CB  . LEU   A 1 128 ? -19.832 -9.575  2.245   1.00 13.29 ?  1165 LEU   A CB  1 
ATOM   894  C CG  . LEU   A 1 128 ? -20.560 -8.711  1.215   1.00 14.97 ?  1165 LEU   A CG  1 
ATOM   895  C CD1 . LEU   A 1 128 ? -20.259 -7.238  1.438   1.00 12.37 ?  1165 LEU   A CD1 1 
ATOM   896  C CD2 . LEU   A 1 128 ? -20.170 -9.132  -0.191  1.00 11.91 ?  1165 LEU   A CD2 1 
ATOM   897  N N   . ARG   A 1 129 ? -22.258 -11.087 3.754   1.00 16.41 ?  1166 ARG   A N   1 
ATOM   898  C CA  . ARG   A 1 129 ? -23.684 -11.393 3.704   1.00 16.77 ?  1166 ARG   A CA  1 
ATOM   899  C C   . ARG   A 1 129 ? -24.378 -11.024 5.008   1.00 17.19 ?  1166 ARG   A C   1 
ATOM   900  O O   . ARG   A 1 129 ? -25.408 -10.341 5.000   1.00 19.31 ?  1166 ARG   A O   1 
ATOM   901  C CB  . ARG   A 1 129 ? -23.906 -12.869 3.388   1.00 17.07 ?  1166 ARG   A CB  1 
ATOM   902  C CG  . ARG   A 1 129 ? -25.368 -13.185 3.153   1.00 18.34 ?  1166 ARG   A CG  1 
ATOM   903  C CD  . ARG   A 1 129 ? -25.553 -14.374 2.240   1.00 21.26 ?  1166 ARG   A CD  1 
ATOM   904  N NE  . ARG   A 1 129 ? -26.963 -14.715 2.079   1.00 16.68 ?  1166 ARG   A NE  1 
ATOM   905  C CZ  . ARG   A 1 129 ? -27.643 -15.524 2.882   1.00 19.54 ?  1166 ARG   A CZ  1 
ATOM   906  N NH1 . ARG   A 1 129 ? -27.078 -16.093 3.935   1.00 21.72 ?  1166 ARG   A NH1 1 
ATOM   907  N NH2 . ARG   A 1 129 ? -28.927 -15.762 2.626   1.00 20.21 ?  1166 ARG   A NH2 1 
ATOM   908  N N   . ASN   A 1 130 ? -23.835 -11.475 6.142   1.00 14.76 ?  1167 ASN   A N   1 
ATOM   909  C CA  . ASN   A 1 130 ? -24.475 -11.196 7.424   1.00 15.23 ?  1167 ASN   A CA  1 
ATOM   910  C C   . ASN   A 1 130 ? -24.563 -9.700  7.695   1.00 20.28 ?  1167 ASN   A C   1 
ATOM   911  O O   . ASN   A 1 130 ? -25.439 -9.257  8.446   1.00 20.17 ?  1167 ASN   A O   1 
ATOM   912  C CB  . ASN   A 1 130 ? -23.720 -11.896 8.554   1.00 14.17 ?  1167 ASN   A CB  1 
ATOM   913  C CG  . ASN   A 1 130 ? -24.113 -13.353 8.703   1.00 17.10 ?  1167 ASN   A CG  1 
ATOM   914  O OD1 . ASN   A 1 130 ? -25.296 -13.694 8.685   1.00 13.28 ?  1167 ASN   A OD1 1 
ATOM   915  N ND2 . ASN   A 1 130 ? -23.120 -14.222 8.854   1.00 15.26 ?  1167 ASN   A ND2 1 
ATOM   916  N N   . PHE   A 1 131 ? -23.673 -8.909  7.092   1.00 16.53 ?  1168 PHE   A N   1 
ATOM   917  C CA  . PHE   A 1 131 ? -23.716 -7.463  7.281   1.00 14.93 ?  1168 PHE   A CA  1 
ATOM   918  C C   . PHE   A 1 131 ? -24.879 -6.842  6.517   1.00 16.48 ?  1168 PHE   A C   1 
ATOM   919  O O   . PHE   A 1 131 ? -25.648 -6.049  7.073   1.00 20.46 ?  1168 PHE   A O   1 
ATOM   920  C CB  . PHE   A 1 131 ? -22.390 -6.839  6.846   1.00 16.23 ?  1168 PHE   A CB  1 
ATOM   921  C CG  . PHE   A 1 131 ? -22.345 -5.346  6.997   1.00 18.45 ?  1168 PHE   A CG  1 
ATOM   922  C CD1 . PHE   A 1 131 ? -22.102 -4.769  8.232   1.00 19.42 ?  1168 PHE   A CD1 1 
ATOM   923  C CD2 . PHE   A 1 131 ? -22.546 -4.519  5.903   1.00 17.31 ?  1168 PHE   A CD2 1 
ATOM   924  C CE1 . PHE   A 1 131 ? -22.061 -3.396  8.375   1.00 21.93 ?  1168 PHE   A CE1 1 
ATOM   925  C CE2 . PHE   A 1 131 ? -22.506 -3.145  6.040   1.00 24.36 ?  1168 PHE   A CE2 1 
ATOM   926  C CZ  . PHE   A 1 131 ? -22.263 -2.583  7.278   1.00 20.77 ?  1168 PHE   A CZ  1 
ATOM   927  N N   . ILE   A 1 132 ? -25.026 -7.192  5.236   1.00 17.47 ?  1169 ILE   A N   1 
ATOM   928  C CA  . ILE   A 1 132 ? -26.079 -6.613  4.409   1.00 17.34 ?  1169 ILE   A CA  1 
ATOM   929  C C   . ILE   A 1 132 ? -27.462 -7.148  4.745   1.00 16.24 ?  1169 ILE   A C   1 
ATOM   930  O O   . ILE   A 1 132 ? -28.456 -6.631  4.225   1.00 14.16 ?  1169 ILE   A O   1 
ATOM   931  C CB  . ILE   A 1 132 ? -25.785 -6.848  2.913   1.00 14.82 ?  1169 ILE   A CB  1 
ATOM   932  C CG1 . ILE   A 1 132 ? -25.922 -8.330  2.562   1.00 17.23 ?  1169 ILE   A CG1 1 
ATOM   933  C CG2 . ILE   A 1 132 ? -24.395 -6.345  2.560   1.00 11.70 ?  1169 ILE   A CG2 1 
ATOM   934  C CD1 . ILE   A 1 132 ? -25.486 -8.667  1.151   1.00 14.46 ?  1169 ILE   A CD1 1 
ATOM   935  N N   . ARG   A 1 133 ? -27.556 -8.167  5.596   1.00 15.01 ?  1170 ARG   A N   1 
ATOM   936  C CA  . ARG   A 1 133 ? -28.842 -8.713  6.005   1.00 15.88 ?  1170 ARG   A CA  1 
ATOM   937  C C   . ARG   A 1 133 ? -29.288 -8.229  7.376   1.00 17.47 ?  1170 ARG   A C   1 
ATOM   938  O O   . ARG   A 1 133 ? -30.453 -8.433  7.737   1.00 18.23 ?  1170 ARG   A O   1 
ATOM   939  C CB  . ARG   A 1 133 ? -28.796 -10.245 6.006   1.00 18.64 ?  1170 ARG   A CB  1 
ATOM   940  C CG  . ARG   A 1 133 ? -28.417 -10.853 4.671   1.00 18.66 ?  1170 ARG   A CG  1 
ATOM   941  C CD  . ARG   A 1 133 ? -28.507 -12.363 4.714   1.00 14.66 ?  1170 ARG   A CD  1 
ATOM   942  N NE  . ARG   A 1 133 ? -29.887 -12.817 4.821   1.00 20.33 ?  1170 ARG   A NE  1 
ATOM   943  C CZ  . ARG   A 1 133 ? -30.411 -13.363 5.909   1.00 26.26 ?  1170 ARG   A CZ  1 
ATOM   944  N NH1 . ARG   A 1 133 ? -29.693 -13.542 7.006   1.00 28.41 ?  1170 ARG   A NH1 1 
ATOM   945  N NH2 . ARG   A 1 133 ? -31.686 -13.738 5.897   1.00 20.01 ?  1170 ARG   A NH2 1 
ATOM   946  N N   . ASN   A 1 134 ? -28.399 -7.601  8.142   1.00 14.42 ?  1171 ASN   A N   1 
ATOM   947  C CA  . ASN   A 1 134 ? -28.750 -7.142  9.478   1.00 15.63 ?  1171 ASN   A CA  1 
ATOM   948  C C   . ASN   A 1 134 ? -29.845 -6.089  9.403   1.00 19.74 ?  1171 ASN   A C   1 
ATOM   949  O O   . ASN   A 1 134 ? -29.710 -5.090  8.689   1.00 23.13 ?  1171 ASN   A O   1 
ATOM   950  C CB  . ASN   A 1 134 ? -27.516 -6.586  10.187  1.00 18.11 ?  1171 ASN   A CB  1 
ATOM   951  C CG  . ASN   A 1 134 ? -27.647 -6.622  11.697  1.00 23.82 ?  1171 ASN   A CG  1 
ATOM   952  O OD1 . ASN   A 1 134 ? -28.754 -6.624  12.236  1.00 29.11 ?  1171 ASN   A OD1 1 
ATOM   953  N ND2 . ASN   A 1 134 ? -26.515 -6.654  12.390  1.00 29.49 ?  1171 ASN   A ND2 1 
ATOM   954  N N   . GLU   A 1 135 ? -30.938 -6.333  10.131  1.00 21.96 ?  1172 GLU   A N   1 
ATOM   955  C CA  . GLU   A 1 135 ? -32.048 -5.386  10.191  1.00 23.36 ?  1172 GLU   A CA  1 
ATOM   956  C C   . GLU   A 1 135 ? -31.561 -3.982  10.525  1.00 19.93 ?  1172 GLU   A C   1 
ATOM   957  O O   . GLU   A 1 135 ? -31.934 -3.004  9.866   1.00 17.03 ?  1172 GLU   A O   1 
ATOM   958  C CB  . GLU   A 1 135 ? -33.062 -5.854  11.237  1.00 24.46 ?  1172 GLU   A CB  1 
ATOM   959  C CG  . GLU   A 1 135 ? -34.511 -5.535  10.925  1.00 29.23 ?  1172 GLU   A CG  1 
ATOM   960  C CD  . GLU   A 1 135 ? -35.444 -6.653  11.342  1.00 33.77 ?  1172 GLU   A CD  1 
ATOM   961  O OE1 . GLU   A 1 135 ? -36.017 -6.565  12.449  1.00 29.92 ?  1172 GLU   A OE1 1 
ATOM   962  O OE2 . GLU   A 1 135 ? -35.603 -7.619  10.566  1.00 35.63 -1 1172 GLU   A OE2 1 
ATOM   963  N N   . THR   A 1 136 ? -30.710 -3.870  11.542  1.00 18.39 ?  1173 THR   A N   1 
ATOM   964  C CA  . THR   A 1 136 ? -30.298 -2.593  12.105  1.00 21.40 ?  1173 THR   A CA  1 
ATOM   965  C C   . THR   A 1 136 ? -29.186 -1.910  11.313  1.00 22.61 ?  1173 THR   A C   1 
ATOM   966  O O   . THR   A 1 136 ? -28.553 -0.987  11.839  1.00 29.07 ?  1173 THR   A O   1 
ATOM   967  C CB  . THR   A 1 136 ? -29.858 -2.788  13.557  1.00 24.52 ?  1173 THR   A CB  1 
ATOM   968  O OG1 . THR   A 1 136 ? -28.652 -3.562  13.591  1.00 27.28 ?  1173 THR   A OG1 1 
ATOM   969  C CG2 . THR   A 1 136 ? -30.939 -3.516  14.343  1.00 18.96 ?  1173 THR   A CG2 1 
ATOM   970  N N   . HIS   A 1 137 ? -28.929 -2.329  10.078  1.00 25.90 ?  1174 HIS   A N   1 
ATOM   971  C CA  . HIS   A 1 137 ? -27.909 -1.721  9.235   1.00 23.83 ?  1174 HIS   A CA  1 
ATOM   972  C C   . HIS   A 1 137 ? -28.573 -1.098  8.016   1.00 19.60 ?  1174 HIS   A C   1 
ATOM   973  O O   . HIS   A 1 137 ? -29.496 -1.681  7.438   1.00 19.96 ?  1174 HIS   A O   1 
ATOM   974  C CB  . HIS   A 1 137 ? -26.858 -2.749  8.808   1.00 15.17 ?  1174 HIS   A CB  1 
ATOM   975  C CG  . HIS   A 1 137 ? -26.072 -3.317  9.950   1.00 26.69 ?  1174 HIS   A CG  1 
ATOM   976  N ND1 . HIS   A 1 137 ? -24.895 -4.011  9.771   1.00 29.52 ?  1174 HIS   A ND1 1 
ATOM   977  C CD2 . HIS   A 1 137 ? -26.294 -3.292  11.285  1.00 25.28 ?  1174 HIS   A CD2 1 
ATOM   978  C CE1 . HIS   A 1 137 ? -24.426 -4.389  10.947  1.00 27.40 ?  1174 HIS   A CE1 1 
ATOM   979  N NE2 . HIS   A 1 137 ? -25.256 -3.965  11.882  1.00 32.26 ?  1174 HIS   A NE2 1 
ATOM   980  N N   . ASN   A 1 138 ? -28.102 0.085   7.625   1.00 18.12 ?  1175 ASN   A N   1 
ATOM   981  C CA  . ASN   A 1 138 ? -28.761 0.898   6.603   1.00 20.80 ?  1175 ASN   A CA  1 
ATOM   982  C C   . ASN   A 1 138 ? -27.783 1.262   5.492   1.00 18.48 ?  1175 ASN   A C   1 
ATOM   983  O O   . ASN   A 1 138 ? -27.364 2.419   5.373   1.00 18.80 ?  1175 ASN   A O   1 
ATOM   984  C CB  . ASN   A 1 138 ? -29.361 2.158   7.227   1.00 12.95 ?  1175 ASN   A CB  1 
ATOM   985  C CG  . ASN   A 1 138 ? -30.240 1.853   8.422   1.00 12.73 ?  1175 ASN   A CG  1 
ATOM   986  O OD1 . ASN   A 1 138 ? -29.928 2.236   9.549   1.00 20.44 ?  1175 ASN   A OD1 1 
ATOM   987  N ND2 . ASN   A 1 138 ? -31.347 1.163   8.181   1.00 12.15 ?  1175 ASN   A ND2 1 
ATOM   988  N N   . PRO   A 1 139 ? -27.416 0.302   4.642   1.00 16.46 ?  1176 PRO   A N   1 
ATOM   989  C CA  . PRO   A 1 139 ? -26.595 0.635   3.471   1.00 14.11 ?  1176 PRO   A CA  1 
ATOM   990  C C   . PRO   A 1 139 ? -27.471 1.150   2.338   1.00 16.81 ?  1176 PRO   A C   1 
ATOM   991  O O   . PRO   A 1 139 ? -28.497 0.552   2.007   1.00 17.17 ?  1176 PRO   A O   1 
ATOM   992  C CB  . PRO   A 1 139 ? -25.936 -0.699  3.107   1.00 15.71 ?  1176 PRO   A CB  1 
ATOM   993  C CG  . PRO   A 1 139 ? -26.891 -1.740  3.600   1.00 17.36 ?  1176 PRO   A CG  1 
ATOM   994  C CD  . PRO   A 1 139 ? -27.746 -1.133  4.693   1.00 17.43 ?  1176 PRO   A CD  1 
ATOM   995  N N   . THR   A 1 140 ? -27.068 2.272   1.749   1.00 15.96 ?  1177 THR   A N   1 
ATOM   996  C CA  . THR   A 1 140 ? -27.801 2.792   0.608   1.00 13.55 ?  1177 THR   A CA  1 
ATOM   997  C C   . THR   A 1 140 ? -27.509 1.953   -0.634  1.00 13.35 ?  1177 THR   A C   1 
ATOM   998  O O   . THR   A 1 140 ? -26.695 1.026   -0.620  1.00 15.85 ?  1177 THR   A O   1 
ATOM   999  C CB  . THR   A 1 140 ? -27.446 4.257   0.352   1.00 15.49 ?  1177 THR   A CB  1 
ATOM   1000 O OG1 . THR   A 1 140 ? -26.036 4.381   0.126   1.00 18.55 ?  1177 THR   A OG1 1 
ATOM   1001 C CG2 . THR   A 1 140 ? -27.853 5.119   1.535   1.00 15.51 ?  1177 THR   A CG2 1 
ATOM   1002 N N   . VAL   A 1 141 ? -28.207 2.287   -1.721  1.00 16.49 ?  1178 VAL   A N   1 
ATOM   1003 C CA  . VAL   A 1 141 ? -27.963 1.624   -2.999  1.00 16.80 ?  1178 VAL   A CA  1 
ATOM   1004 C C   . VAL   A 1 141 ? -26.512 1.810   -3.418  1.00 16.22 ?  1178 VAL   A C   1 
ATOM   1005 O O   . VAL   A 1 141 ? -25.836 0.858   -3.827  1.00 14.85 ?  1178 VAL   A O   1 
ATOM   1006 C CB  . VAL   A 1 141 ? -28.929 2.159   -4.071  1.00 18.80 ?  1178 VAL   A CB  1 
ATOM   1007 C CG1 . VAL   A 1 141 ? -28.891 1.275   -5.308  1.00 20.06 ?  1178 VAL   A CG1 1 
ATOM   1008 C CG2 . VAL   A 1 141 ? -30.341 2.258   -3.513  1.00 23.59 ?  1178 VAL   A CG2 1 
ATOM   1009 N N   . LYS   A 1 142 ? -26.012 3.044   -3.314  1.00 23.70 ?  1179 LYS   A N   1 
ATOM   1010 C CA  . LYS   A 1 142 ? -24.633 3.333   -3.697  1.00 16.16 ?  1179 LYS   A CA  1 
ATOM   1011 C C   . LYS   A 1 142 ? -23.645 2.538   -2.852  1.00 15.56 ?  1179 LYS   A C   1 
ATOM   1012 O O   . LYS   A 1 142 ? -22.599 2.107   -3.350  1.00 16.67 ?  1179 LYS   A O   1 
ATOM   1013 C CB  . LYS   A 1 142 ? -24.367 4.833   -3.571  1.00 17.18 ?  1179 LYS   A CB  1 
ATOM   1014 C CG  . LYS   A 1 142 ? -23.094 5.318   -4.244  1.00 17.04 ?  1179 LYS   A CG  1 
ATOM   1015 C CD  . LYS   A 1 142 ? -22.527 6.529   -3.515  1.00 24.50 ?  1179 LYS   A CD  1 
ATOM   1016 C CE  . LYS   A 1 142 ? -21.314 7.100   -4.232  1.00 21.66 ?  1179 LYS   A CE  1 
ATOM   1017 N NZ  . LYS   A 1 142 ? -21.691 8.180   -5.186  1.00 23.47 ?  1179 LYS   A NZ  1 
ATOM   1018 N N   . ASP   A 1 143 ? -23.964 2.326   -1.573  1.00 14.31 ?  1180 ASP   A N   1 
ATOM   1019 C CA  . ASP   A 1 143 ? -23.073 1.573   -0.696  1.00 12.04 ?  1180 ASP   A CA  1 
ATOM   1020 C C   . ASP   A 1 143 ? -22.874 0.149   -1.201  1.00 13.03 ?  1180 ASP   A C   1 
ATOM   1021 O O   . ASP   A 1 143 ? -21.739 -0.301  -1.394  1.00 12.34 ?  1180 ASP   A O   1 
ATOM   1022 C CB  . ASP   A 1 143 ? -23.627 1.562   0.728   1.00 14.86 ?  1180 ASP   A CB  1 
ATOM   1023 C CG  . ASP   A 1 143 ? -23.442 2.887   1.435   1.00 17.50 ?  1180 ASP   A CG  1 
ATOM   1024 O OD1 . ASP   A 1 143 ? -22.485 3.614   1.096   1.00 25.43 ?  1180 ASP   A OD1 1 
ATOM   1025 O OD2 . ASP   A 1 143 ? -24.251 3.199   2.334   1.00 20.30 -1 1180 ASP   A OD2 1 
ATOM   1026 N N   . LEU   A 1 144 ? -23.975 -0.574  -1.426  1.00 12.99 ?  1181 LEU   A N   1 
ATOM   1027 C CA  . LEU   A 1 144 ? -23.880 -1.971  -1.837  1.00 12.71 ?  1181 LEU   A CA  1 
ATOM   1028 C C   . LEU   A 1 144 ? -23.155 -2.121  -3.168  1.00 12.42 ?  1181 LEU   A C   1 
ATOM   1029 O O   . LEU   A 1 144 ? -22.464 -3.123  -3.387  1.00 9.21  ?  1181 LEU   A O   1 
ATOM   1030 C CB  . LEU   A 1 144 ? -25.278 -2.581  -1.920  1.00 11.70 ?  1181 LEU   A CB  1 
ATOM   1031 C CG  . LEU   A 1 144 ? -26.085 -2.540  -0.622  1.00 13.00 ?  1181 LEU   A CG  1 
ATOM   1032 C CD1 . LEU   A 1 144 ? -27.529 -2.914  -0.884  1.00 12.41 ?  1181 LEU   A CD1 1 
ATOM   1033 C CD2 . LEU   A 1 144 ? -25.473 -3.456  0.426   1.00 12.13 ?  1181 LEU   A CD2 1 
ATOM   1034 N N   . ILE   A 1 145 ? -23.302 -1.145  -4.067  1.00 12.84 ?  1182 ILE   A N   1 
ATOM   1035 C CA  . ILE   A 1 145 ? -22.544 -1.175  -5.313  1.00 11.89 ?  1182 ILE   A CA  1 
ATOM   1036 C C   . ILE   A 1 145 ? -21.066 -0.937  -5.038  1.00 11.78 ?  1182 ILE   A C   1 
ATOM   1037 O O   . ILE   A 1 145 ? -20.201 -1.498  -5.722  1.00 15.30 ?  1182 ILE   A O   1 
ATOM   1038 C CB  . ILE   A 1 145 ? -23.110 -0.147  -6.312  1.00 12.08 ?  1182 ILE   A CB  1 
ATOM   1039 C CG1 . ILE   A 1 145 ? -24.597 -0.409  -6.557  1.00 13.28 ?  1182 ILE   A CG1 1 
ATOM   1040 C CG2 . ILE   A 1 145 ? -22.345 -0.195  -7.627  1.00 7.81  ?  1182 ILE   A CG2 1 
ATOM   1041 C CD1 . ILE   A 1 145 ? -25.240 0.540   -7.546  1.00 10.43 ?  1182 ILE   A CD1 1 
ATOM   1042 N N   . GLY   A 1 146 ? -20.750 -0.115  -4.035  1.00 13.44 ?  1183 GLY   A N   1 
ATOM   1043 C CA  . GLY   A 1 146 ? -19.359 0.065   -3.655  1.00 10.56 ?  1183 GLY   A CA  1 
ATOM   1044 C C   . GLY   A 1 146 ? -18.732 -1.216  -3.140  1.00 12.20 ?  1183 GLY   A C   1 
ATOM   1045 O O   . GLY   A 1 146 ? -17.569 -1.509  -3.427  1.00 12.49 ?  1183 GLY   A O   1 
ATOM   1046 N N   . PHE   A 1 147 ? -19.495 -1.996  -2.370  1.00 7.58  ?  1184 PHE   A N   1 
ATOM   1047 C CA  . PHE   A 1 147 ? -19.028 -3.314  -1.953  1.00 10.93 ?  1184 PHE   A CA  1 
ATOM   1048 C C   . PHE   A 1 147 ? -18.721 -4.194  -3.161  1.00 10.56 ?  1184 PHE   A C   1 
ATOM   1049 O O   . PHE   A 1 147 ? -17.674 -4.849  -3.215  1.00 11.07 ?  1184 PHE   A O   1 
ATOM   1050 C CB  . PHE   A 1 147 ? -20.071 -3.981  -1.055  1.00 12.27 ?  1184 PHE   A CB  1 
ATOM   1051 C CG  . PHE   A 1 147 ? -20.186 -3.370  0.314   1.00 10.08 ?  1184 PHE   A CG  1 
ATOM   1052 C CD1 . PHE   A 1 147 ? -19.133 -2.662  0.870   1.00 9.15  ?  1184 PHE   A CD1 1 
ATOM   1053 C CD2 . PHE   A 1 147 ? -21.350 -3.517  1.050   1.00 9.47  ?  1184 PHE   A CD2 1 
ATOM   1054 C CE1 . PHE   A 1 147 ? -19.242 -2.109  2.132   1.00 9.00  ?  1184 PHE   A CE1 1 
ATOM   1055 C CE2 . PHE   A 1 147 ? -21.466 -2.967  2.310   1.00 12.29 ?  1184 PHE   A CE2 1 
ATOM   1056 C CZ  . PHE   A 1 147 ? -20.410 -2.262  2.852   1.00 14.31 ?  1184 PHE   A CZ  1 
ATOM   1057 N N   . GLY   A 1 148 ? -19.628 -4.221  -4.145  1.00 11.23 ?  1185 GLY   A N   1 
ATOM   1058 C CA  . GLY   A 1 148 ? -19.403 -5.033  -5.331  1.00 8.99  ?  1185 GLY   A CA  1 
ATOM   1059 C C   . GLY   A 1 148 ? -18.262 -4.515  -6.176  1.00 10.10 ?  1185 GLY   A C   1 
ATOM   1060 O O   . GLY   A 1 148 ? -17.650 -5.271  -6.941  1.00 11.73 ?  1185 GLY   A O   1 
ATOM   1061 N N   . LEU   A 1 149 ? -17.972 -3.218  -6.046  1.00 12.54 ?  1186 LEU   A N   1 
ATOM   1062 C CA  . LEU   A 1 149 ? -16.786 -2.611  -6.632  1.00 11.68 ?  1186 LEU   A CA  1 
ATOM   1063 C C   . LEU   A 1 149 ? -15.510 -3.155  -6.003  1.00 12.51 ?  1186 LEU   A C   1 
ATOM   1064 O O   . LEU   A 1 149 ? -14.532 -3.448  -6.705  1.00 12.60 ?  1186 LEU   A O   1 
ATOM   1065 C CB  . LEU   A 1 149 ? -16.879 -1.088  -6.473  1.00 11.28 ?  1186 LEU   A CB  1 
ATOM   1066 C CG  . LEU   A 1 149 ? -15.630 -0.406  -7.004  1.00 12.29 ?  1186 LEU   A CG  1 
ATOM   1067 C CD1 . LEU   A 1 149 ? -15.461 -0.994  -8.349  1.00 12.03 ?  1186 LEU   A CD1 1 
ATOM   1068 C CD2 . LEU   A 1 149 ? -15.823 1.113   -7.125  1.00 18.65 ?  1186 LEU   A CD2 1 
ATOM   1069 N N   . GLN   A 1 150 ? -15.498 -3.265  -4.680  1.00 14.04 ?  1187 GLN   A N   1 
ATOM   1070 C CA  . GLN   A 1 150 ? -14.290 -3.657  -3.971  1.00 10.59 ?  1187 GLN   A CA  1 
ATOM   1071 C C   . GLN   A 1 150 ? -13.935 -5.109  -4.249  1.00 11.22 ?  1187 GLN   A C   1 
ATOM   1072 O O   . GLN   A 1 150 ? -12.760 -5.441  -4.445  1.00 11.23 ?  1187 GLN   A O   1 
ATOM   1073 C CB  . GLN   A 1 150 ? -14.492 -3.422  -2.480  1.00 10.13 ?  1187 GLN   A CB  1 
ATOM   1074 C CG  . GLN   A 1 150 ? -14.586 -1.959  -2.105  1.00 9.45  ?  1187 GLN   A CG  1 
ATOM   1075 C CD  . GLN   A 1 150 ? -14.602 -1.757  -0.609  1.00 9.10  ?  1187 GLN   A CD  1 
ATOM   1076 O OE1 . GLN   A 1 150 ? -13.579 -1.902  0.056   1.00 8.71  ?  1187 GLN   A OE1 1 
ATOM   1077 N NE2 . GLN   A 1 150 ? -15.766 -1.415  -0.069  1.00 9.90  ?  1187 GLN   A NE2 1 
ATOM   1078 N N   . VAL   A 1 151 ? -14.935 -5.989  -4.265  1.00 12.67 ?  1188 VAL   A N   1 
ATOM   1079 C CA  . VAL   A 1 151 ? -14.675 -7.395  -4.551  1.00 15.83 ?  1188 VAL   A CA  1 
ATOM   1080 C C   . VAL   A 1 151 ? -14.181 -7.565  -5.982  1.00 16.01 ?  1188 VAL   A C   1 
ATOM   1081 O O   . VAL   A 1 151 ? -13.339 -8.426  -6.265  1.00 12.57 ?  1188 VAL   A O   1 
ATOM   1082 C CB  . VAL   A 1 151 ? -15.934 -8.233  -4.268  1.00 14.19 ?  1188 VAL   A CB  1 
ATOM   1083 C CG1 . VAL   A 1 151 ? -16.272 -8.181  -2.796  1.00 16.56 ?  1188 VAL   A CG1 1 
ATOM   1084 C CG2 . VAL   A 1 151 ? -17.099 -7.702  -5.046  1.00 13.07 ?  1188 VAL   A CG2 1 
ATOM   1085 N N   . ALA   A 1 152 ? -14.679 -6.736  -6.904  1.00 12.00 ?  1189 ALA   A N   1 
ATOM   1086 C CA  . ALA   A 1 152 ? -14.236 -6.821  -8.292  1.00 10.85 ?  1189 ALA   A CA  1 
ATOM   1087 C C   . ALA   A 1 152 ? -12.757 -6.484  -8.420  1.00 12.78 ?  1189 ALA   A C   1 
ATOM   1088 O O   . ALA   A 1 152 ? -12.047 -7.072  -9.245  1.00 13.90 ?  1189 ALA   A O   1 
ATOM   1089 C CB  . ALA   A 1 152 ? -15.077 -5.895  -9.170  1.00 13.17 ?  1189 ALA   A CB  1 
ATOM   1090 N N   . LYS   A 1 153 ? -12.273 -5.540  -7.610  1.00 14.75 ?  1190 LYS   A N   1 
ATOM   1091 C CA  . LYS   A 1 153 ? -10.858 -5.185  -7.647  1.00 13.19 ?  1190 LYS   A CA  1 
ATOM   1092 C C   . LYS   A 1 153 ? -9.992  -6.327  -7.132  1.00 13.53 ?  1190 LYS   A C   1 
ATOM   1093 O O   . LYS   A 1 153 ? -9.056  -6.763  -7.811  1.00 12.19 ?  1190 LYS   A O   1 
ATOM   1094 C CB  . LYS   A 1 153 ? -10.614 -3.918  -6.829  1.00 13.71 ?  1190 LYS   A CB  1 
ATOM   1095 C CG  . LYS   A 1 153 ? -10.994 -2.632  -7.539  1.00 14.04 ?  1190 LYS   A CG  1 
ATOM   1096 C CD  . LYS   A 1 153 ? -11.585 -1.632  -6.564  1.00 16.77 ?  1190 LYS   A CD  1 
ATOM   1097 C CE  . LYS   A 1 153 ? -11.345 -0.205  -7.025  1.00 15.54 ?  1190 LYS   A CE  1 
ATOM   1098 N NZ  . LYS   A 1 153 ? -11.149 0.717   -5.872  1.00 12.99 ?  1190 LYS   A NZ  1 
ATOM   1099 N N   . GLY   A 1 154 ? -10.287 -6.818  -5.925  1.00 13.92 ?  1191 GLY   A N   1 
ATOM   1100 C CA  . GLY   A 1 154 ? -9.529  -7.936  -5.387  1.00 13.11 ?  1191 GLY   A CA  1 
ATOM   1101 C C   . GLY   A 1 154 ? -9.588  -9.162  -6.277  1.00 14.46 ?  1191 GLY   A C   1 
ATOM   1102 O O   . GLY   A 1 154 ? -8.587  -9.862  -6.452  1.00 13.05 ?  1191 GLY   A O   1 
ATOM   1103 N N   . MET   A 1 155 ? -10.766 -9.439  -6.852  1.00 11.83 ?  1192 MET   A N   1 
ATOM   1104 C CA  . MET   A 1 155 ? -10.885 -10.493 -7.858  1.00 13.40 ?  1192 MET   A CA  1 
ATOM   1105 C C   . MET   A 1 155 ? -10.010 -10.216 -9.065  1.00 12.66 ?  1192 MET   A C   1 
ATOM   1106 O O   . MET   A 1 155 ? -9.400  -11.138 -9.620  1.00 12.95 ?  1192 MET   A O   1 
ATOM   1107 C CB  . MET   A 1 155 ? -12.331 -10.649 -8.317  1.00 12.22 ?  1192 MET   A CB  1 
ATOM   1108 C CG  . MET   A 1 155 ? -13.161 -11.576 -7.468  1.00 10.06 ?  1192 MET   A CG  1 
ATOM   1109 S SD  . MET   A 1 155 ? -12.459 -13.246 -7.297  1.00 13.41 ?  1192 MET   A SD  1 
ATOM   1110 C CE  . MET   A 1 155 ? -12.142 -13.803 -8.967  1.00 9.48  ?  1192 MET   A CE  1 
ATOM   1111 N N   . LYS   A 1 156 ? -9.983  -8.963  -9.520  1.00 10.75 ?  1193 LYS   A N   1 
ATOM   1112 C CA  . LYS   A 1 156 ? -9.100  -8.600  -10.619 1.00 11.96 ?  1193 LYS   A CA  1 
ATOM   1113 C C   . LYS   A 1 156 ? -7.645  -8.841  -10.245 1.00 14.51 ?  1193 LYS   A C   1 
ATOM   1114 O O   . LYS   A 1 156 ? -6.834  -9.237  -11.091 1.00 15.23 ?  1193 LYS   A O   1 
ATOM   1115 C CB  . LYS   A 1 156 ? -9.318  -7.140  -11.010 1.00 12.26 ?  1193 LYS   A CB  1 
ATOM   1116 C CG  . LYS   A 1 156 ? -8.515  -6.724  -12.225 1.00 14.10 ?  1193 LYS   A CG  1 
ATOM   1117 C CD  . LYS   A 1 156 ? -7.777  -5.415  -12.014 1.00 16.05 ?  1193 LYS   A CD  1 
ATOM   1118 C CE  . LYS   A 1 156 ? -8.586  -4.240  -12.518 1.00 23.40 ?  1193 LYS   A CE  1 
ATOM   1119 N NZ  . LYS   A 1 156 ? -7.750  -3.278  -13.288 1.00 20.09 ?  1193 LYS   A NZ  1 
ATOM   1120 N N   . TYR   A 1 157 ? -7.298  -8.615  -8.976  1.00 13.09 ?  1194 TYR   A N   1 
ATOM   1121 C CA  . TYR   A 1 157 ? -5.943  -8.898  -8.519  1.00 13.22 ?  1194 TYR   A CA  1 
ATOM   1122 C C   . TYR   A 1 157 ? -5.672  -10.397 -8.511  1.00 14.56 ?  1194 TYR   A C   1 
ATOM   1123 O O   . TYR   A 1 157 ? -4.627  -10.852 -8.991  1.00 16.60 ?  1194 TYR   A O   1 
ATOM   1124 C CB  . TYR   A 1 157 ? -5.719  -8.309  -7.127  1.00 11.76 ?  1194 TYR   A CB  1 
ATOM   1125 C CG  . TYR   A 1 157 ? -4.429  -8.768  -6.487  1.00 13.00 ?  1194 TYR   A CG  1 
ATOM   1126 C CD1 . TYR   A 1 157 ? -3.224  -8.155  -6.802  1.00 13.98 ?  1194 TYR   A CD1 1 
ATOM   1127 C CD2 . TYR   A 1 157 ? -4.413  -9.816  -5.575  1.00 12.69 ?  1194 TYR   A CD2 1 
ATOM   1128 C CE1 . TYR   A 1 157 ? -2.040  -8.570  -6.228  1.00 14.07 ?  1194 TYR   A CE1 1 
ATOM   1129 C CE2 . TYR   A 1 157 ? -3.232  -10.240 -4.995  1.00 15.30 ?  1194 TYR   A CE2 1 
ATOM   1130 C CZ  . TYR   A 1 157 ? -2.048  -9.612  -5.326  1.00 15.16 ?  1194 TYR   A CZ  1 
ATOM   1131 O OH  . TYR   A 1 157 ? -0.868  -10.024 -4.753  1.00 12.46 ?  1194 TYR   A OH  1 
ATOM   1132 N N   . LEU   A 1 158 ? -6.601  -11.179 -7.956  1.00 10.68 ?  1195 LEU   A N   1 
ATOM   1133 C CA  . LEU   A 1 158 ? -6.421  -12.626 -7.918  1.00 13.34 ?  1195 LEU   A CA  1 
ATOM   1134 C C   . LEU   A 1 158 ? -6.417  -13.217 -9.321  1.00 14.39 ?  1195 LEU   A C   1 
ATOM   1135 O O   . LEU   A 1 158 ? -5.664  -14.155 -9.604  1.00 16.67 ?  1195 LEU   A O   1 
ATOM   1136 C CB  . LEU   A 1 158 ? -7.514  -13.268 -7.063  1.00 8.43  ?  1195 LEU   A CB  1 
ATOM   1137 C CG  . LEU   A 1 158 ? -7.489  -12.902 -5.577  1.00 10.48 ?  1195 LEU   A CG  1 
ATOM   1138 C CD1 . LEU   A 1 158 ? -8.611  -13.597 -4.828  1.00 9.95  ?  1195 LEU   A CD1 1 
ATOM   1139 C CD2 . LEU   A 1 158 ? -6.141  -13.241 -4.961  1.00 12.08 ?  1195 LEU   A CD2 1 
ATOM   1140 N N   . ALA   A 1 159 ? -7.247  -12.676 -10.217 1.00 12.80 ?  1196 ALA   A N   1 
ATOM   1141 C CA  . ALA   A 1 159 ? -7.255  -13.152 -11.596 1.00 11.83 ?  1196 ALA   A CA  1 
ATOM   1142 C C   . ALA   A 1 159 ? -5.920  -12.899 -12.284 1.00 11.88 ?  1196 ALA   A C   1 
ATOM   1143 O O   . ALA   A 1 159 ? -5.510  -13.682 -13.148 1.00 13.09 ?  1196 ALA   A O   1 
ATOM   1144 C CB  . ALA   A 1 159 ? -8.389  -12.489 -12.378 1.00 9.19  ?  1196 ALA   A CB  1 
ATOM   1145 N N   . SER   A 1 160 ? -5.230  -11.816 -11.919 1.00 14.20 ?  1197 SER   A N   1 
ATOM   1146 C CA  . SER   A 1 160 ? -3.925  -11.533 -12.504 1.00 14.69 ?  1197 SER   A CA  1 
ATOM   1147 C C   . SER   A 1 160 ? -2.869  -12.542 -12.073 1.00 19.12 ?  1197 SER   A C   1 
ATOM   1148 O O   . SER   A 1 160 ? -1.869  -12.714 -12.777 1.00 15.60 ?  1197 SER   A O   1 
ATOM   1149 C CB  . SER   A 1 160 ? -3.476  -10.118 -12.135 1.00 15.70 ?  1197 SER   A CB  1 
ATOM   1150 O OG  . SER   A 1 160 ? -3.527  -9.916  -10.734 1.00 16.26 ?  1197 SER   A OG  1 
ATOM   1151 N N   . LYS   A 1 161 ? -3.068  -13.207 -10.938 1.00 17.51 ?  1198 LYS   A N   1 
ATOM   1152 C CA  . LYS   A 1 161 ? -2.172  -14.257 -10.477 1.00 17.30 ?  1198 LYS   A CA  1 
ATOM   1153 C C   . LYS   A 1 161 ? -2.535  -15.625 -11.040 1.00 16.61 ?  1198 LYS   A C   1 
ATOM   1154 O O   . LYS   A 1 161 ? -2.023  -16.637 -10.550 1.00 20.65 ?  1198 LYS   A O   1 
ATOM   1155 C CB  . LYS   A 1 161 ? -2.168  -14.309 -8.946  1.00 18.31 ?  1198 LYS   A CB  1 
ATOM   1156 C CG  . LYS   A 1 161 ? -1.756  -13.004 -8.287  1.00 15.73 ?  1198 LYS   A CG  1 
ATOM   1157 C CD  . LYS   A 1 161 ? -0.431  -12.508 -8.841  1.00 12.29 ?  1198 LYS   A CD  1 
ATOM   1158 C CE  . LYS   A 1 161 ? -0.203  -11.045 -8.506  1.00 15.11 ?  1198 LYS   A CE  1 
ATOM   1159 N NZ  . LYS   A 1 161 ? 0.675   -10.388 -9.513  1.00 17.10 ?  1198 LYS   A NZ  1 
ATOM   1160 N N   . LYS   A 1 162 ? -3.402  -15.672 -12.055 1.00 17.47 ?  1199 LYS   A N   1 
ATOM   1161 C CA  . LYS   A 1 162 ? -3.884  -16.928 -12.633 1.00 16.10 ?  1199 LYS   A CA  1 
ATOM   1162 C C   . LYS   A 1 162 ? -4.462  -17.838 -11.551 1.00 18.91 ?  1199 LYS   A C   1 
ATOM   1163 O O   . LYS   A 1 162 ? -4.326  -19.062 -11.596 1.00 18.15 ?  1199 LYS   A O   1 
ATOM   1164 C CB  . LYS   A 1 162 ? -2.774  -17.636 -13.414 1.00 15.99 ?  1199 LYS   A CB  1 
ATOM   1165 C CG  . LYS   A 1 162 ? -2.418  -16.972 -14.737 1.00 14.35 ?  1199 LYS   A CG  1 
ATOM   1166 C CD  . LYS   A 1 162 ? -3.449  -17.282 -15.809 1.00 17.30 ?  1199 LYS   A CD  1 
ATOM   1167 C CE  . LYS   A 1 162 ? -3.062  -16.670 -17.145 1.00 21.26 ?  1199 LYS   A CE  1 
ATOM   1168 N NZ  . LYS   A 1 162 ? -2.952  -15.186 -17.070 1.00 19.87 ?  1199 LYS   A NZ  1 
ATOM   1169 N N   . PHE   A 1 163 ? -5.121  -17.228 -10.569 1.00 15.34 ?  1200 PHE   A N   1 
ATOM   1170 C CA  . PHE   A 1 163 ? -5.611  -17.922 -9.384  1.00 15.82 ?  1200 PHE   A CA  1 
ATOM   1171 C C   . PHE   A 1 163 ? -7.129  -18.025 -9.448  1.00 14.51 ?  1200 PHE   A C   1 
ATOM   1172 O O   . PHE   A 1 163 ? -7.821  -17.008 -9.556  1.00 10.94 ?  1200 PHE   A O   1 
ATOM   1173 C CB  . PHE   A 1 163 ? -5.172  -17.192 -8.114  1.00 15.52 ?  1200 PHE   A CB  1 
ATOM   1174 C CG  . PHE   A 1 163 ? -5.559  -17.893 -6.845  1.00 15.38 ?  1200 PHE   A CG  1 
ATOM   1175 C CD1 . PHE   A 1 163 ? -4.781  -18.924 -6.345  1.00 16.40 ?  1200 PHE   A CD1 1 
ATOM   1176 C CD2 . PHE   A 1 163 ? -6.694  -17.516 -6.147  1.00 14.86 ?  1200 PHE   A CD2 1 
ATOM   1177 C CE1 . PHE   A 1 163 ? -5.133  -19.571 -5.175  1.00 14.49 ?  1200 PHE   A CE1 1 
ATOM   1178 C CE2 . PHE   A 1 163 ? -7.051  -18.159 -4.977  1.00 14.43 ?  1200 PHE   A CE2 1 
ATOM   1179 C CZ  . PHE   A 1 163 ? -6.269  -19.188 -4.491  1.00 14.55 ?  1200 PHE   A CZ  1 
ATOM   1180 N N   . VAL   A 1 164 ? -7.640  -19.249 -9.372  1.00 21.13 ?  1201 VAL   A N   1 
ATOM   1181 C CA  . VAL   A 1 164 ? -9.072  -19.520 -9.438  1.00 15.45 ?  1201 VAL   A CA  1 
ATOM   1182 C C   . VAL   A 1 164 ? -9.555  -19.750 -8.009  1.00 15.31 ?  1201 VAL   A C   1 
ATOM   1183 O O   . VAL   A 1 164 ? -9.262  -20.784 -7.403  1.00 14.51 ?  1201 VAL   A O   1 
ATOM   1184 C CB  . VAL   A 1 164 ? -9.371  -20.727 -10.341 1.00 12.08 ?  1201 VAL   A CB  1 
ATOM   1185 C CG1 . VAL   A 1 164 ? -10.823 -21.157 -10.212 1.00 17.73 ?  1201 VAL   A CG1 1 
ATOM   1186 C CG2 . VAL   A 1 164 ? -9.022  -20.412 -11.793 1.00 11.63 ?  1201 VAL   A CG2 1 
ATOM   1187 N N   . HIS   A 1 165 ? -10.282 -18.779 -7.457  1.00 11.45 ?  1202 HIS   A N   1 
ATOM   1188 C CA  . HIS   A 1 165 ? -10.719 -18.855 -6.063  1.00 10.77 ?  1202 HIS   A CA  1 
ATOM   1189 C C   . HIS   A 1 165 ? -11.766 -19.953 -5.859  1.00 12.64 ?  1202 HIS   A C   1 
ATOM   1190 O O   . HIS   A 1 165 ? -11.738 -20.646 -4.838  1.00 13.42 ?  1202 HIS   A O   1 
ATOM   1191 C CB  . HIS   A 1 165 ? -11.209 -17.463 -5.639  1.00 9.39  ?  1202 HIS   A CB  1 
ATOM   1192 C CG  . HIS   A 1 165 ? -11.805 -17.363 -4.273  1.00 8.52  ?  1202 HIS   A CG  1 
ATOM   1193 N ND1 . HIS   A 1 165 ? -13.093 -17.770 -3.998  1.00 9.35  ?  1202 HIS   A ND1 1 
ATOM   1194 C CD2 . HIS   A 1 165 ? -11.368 -16.728 -3.160  1.00 9.29  ?  1202 HIS   A CD2 1 
ATOM   1195 C CE1 . HIS   A 1 165 ? -13.381 -17.484 -2.739  1.00 9.16  ?  1202 HIS   A CE1 1 
ATOM   1196 N NE2 . HIS   A 1 165 ? -12.351 -16.850 -2.209  1.00 7.84  ?  1202 HIS   A NE2 1 
ATOM   1197 N N   . ARG   A 1 166 ? -12.678 -20.148 -6.818  1.00 12.40 ?  1203 ARG   A N   1 
ATOM   1198 C CA  . ARG   A 1 166 ? -13.636 -21.253 -6.922  1.00 13.90 ?  1203 ARG   A CA  1 
ATOM   1199 C C   . ARG   A 1 166 ? -14.886 -21.076 -6.057  1.00 9.16  ?  1203 ARG   A C   1 
ATOM   1200 O O   . ARG   A 1 166 ? -15.857 -21.809 -6.260  1.00 10.50 ?  1203 ARG   A O   1 
ATOM   1201 C CB  . ARG   A 1 166 ? -13.026 -22.627 -6.574  1.00 15.39 ?  1203 ARG   A CB  1 
ATOM   1202 C CG  . ARG   A 1 166 ? -12.182 -23.293 -7.640  1.00 17.42 ?  1203 ARG   A CG  1 
ATOM   1203 C CD  . ARG   A 1 166 ? -12.045 -24.789 -7.351  1.00 19.73 ?  1203 ARG   A CD  1 
ATOM   1204 N NE  . ARG   A 1 166 ? -12.062 -25.085 -5.921  1.00 24.10 ?  1203 ARG   A NE  1 
ATOM   1205 C CZ  . ARG   A 1 166 ? -13.092 -25.615 -5.274  1.00 34.50 ?  1203 ARG   A CZ  1 
ATOM   1206 N NH1 . ARG   A 1 166 ? -14.216 -25.925 -5.900  1.00 30.77 ?  1203 ARG   A NH1 1 
ATOM   1207 N NH2 . ARG   A 1 166 ? -12.996 -25.831 -3.965  1.00 33.28 ?  1203 ARG   A NH2 1 
ATOM   1208 N N   . ASP   A 1 167 ? -14.900 -20.162 -5.096  1.00 10.82 ?  1204 ASP   A N   1 
ATOM   1209 C CA  . ASP   A 1 167 ? -16.012 -20.074 -4.157  1.00 13.03 ?  1204 ASP   A CA  1 
ATOM   1210 C C   . ASP   A 1 167 ? -16.298 -18.608 -3.823  1.00 9.88  ?  1204 ASP   A C   1 
ATOM   1211 O O   . ASP   A 1 167 ? -16.404 -18.223 -2.658  1.00 6.97  ?  1204 ASP   A O   1 
ATOM   1212 C CB  . ASP   A 1 167 ? -15.707 -20.902 -2.906  1.00 9.52  ?  1204 ASP   A CB  1 
ATOM   1213 C CG  . ASP   A 1 167 ? -16.917 -21.090 -2.008  1.00 11.51 ?  1204 ASP   A CG  1 
ATOM   1214 O OD1 . ASP   A 1 167 ? -18.055 -20.991 -2.508  1.00 13.32 ?  1204 ASP   A OD1 1 
ATOM   1215 O OD2 . ASP   A 1 167 ? -16.725 -21.343 -0.798  1.00 10.50 -1 1204 ASP   A OD2 1 
ATOM   1216 N N   . LEU   A 1 168 ? -16.434 -17.760 -4.850  1.00 9.10  ?  1205 LEU   A N   1 
ATOM   1217 C CA  . LEU   A 1 168 ? -16.754 -16.352 -4.618  1.00 10.14 ?  1205 LEU   A CA  1 
ATOM   1218 C C   . LEU   A 1 168 ? -18.242 -16.220 -4.320  1.00 13.14 ?  1205 LEU   A C   1 
ATOM   1219 O O   . LEU   A 1 168 ? -19.084 -16.657 -5.113  1.00 12.03 ?  1205 LEU   A O   1 
ATOM   1220 C CB  . LEU   A 1 168 ? -16.371 -15.466 -5.805  1.00 9.29  ?  1205 LEU   A CB  1 
ATOM   1221 C CG  . LEU   A 1 168 ? -16.641 -13.979 -5.535  1.00 11.48 ?  1205 LEU   A CG  1 
ATOM   1222 C CD1 . LEU   A 1 168 ? -15.821 -13.688 -4.280  1.00 9.89  ?  1205 LEU   A CD1 1 
ATOM   1223 C CD2 . LEU   A 1 168 ? -16.322 -12.976 -6.676  1.00 9.53  ?  1205 LEU   A CD2 1 
ATOM   1224 N N   . ALA   A 1 169 ? -18.556 -15.626 -3.172  1.00 10.72 ?  1206 ALA   A N   1 
ATOM   1225 C CA  . ALA   A 1 169 ? -19.927 -15.414 -2.731  1.00 10.17 ?  1206 ALA   A CA  1 
ATOM   1226 C C   . ALA   A 1 169 ? -19.907 -14.472 -1.536  1.00 9.28  ?  1206 ALA   A C   1 
ATOM   1227 O O   . ALA   A 1 169 ? -18.905 -14.371 -0.823  1.00 10.45 ?  1206 ALA   A O   1 
ATOM   1228 C CB  . ALA   A 1 169 ? -20.615 -16.733 -2.367  1.00 11.43 ?  1206 ALA   A CB  1 
ATOM   1229 N N   . ALA   A 1 170 ? -21.041 -13.799 -1.315  1.00 11.90 ?  1207 ALA   A N   1 
ATOM   1230 C CA  . ALA   A 1 170 ? -21.156 -12.788 -0.267  1.00 12.07 ?  1207 ALA   A CA  1 
ATOM   1231 C C   . ALA   A 1 170 ? -20.956 -13.342 1.138   1.00 13.21 ?  1207 ALA   A C   1 
ATOM   1232 O O   . ALA   A 1 170 ? -20.763 -12.557 2.071   1.00 14.17 ?  1207 ALA   A O   1 
ATOM   1233 C CB  . ALA   A 1 170 ? -22.518 -12.095 -0.349  1.00 10.81 ?  1207 ALA   A CB  1 
ATOM   1234 N N   . ARG   A 1 171 ? -21.018 -14.659 1.320   1.00 13.05 ?  1208 ARG   A N   1 
ATOM   1235 C CA  . ARG   A 1 171 ? -20.680 -15.253 2.606   1.00 14.38 ?  1208 ARG   A CA  1 
ATOM   1236 C C   . ARG   A 1 171 ? -19.183 -15.440 2.777   1.00 11.60 ?  1208 ARG   A C   1 
ATOM   1237 O O   . ARG   A 1 171 ? -18.738 -15.781 3.878   1.00 13.63 ?  1208 ARG   A O   1 
ATOM   1238 C CB  . ARG   A 1 171 ? -21.374 -16.606 2.765   1.00 15.95 ?  1208 ARG   A CB  1 
ATOM   1239 C CG  . ARG   A 1 171 ? -20.911 -17.634 1.751   1.00 9.96  ?  1208 ARG   A CG  1 
ATOM   1240 C CD  . ARG   A 1 171 ? -21.638 -18.956 1.899   1.00 13.29 ?  1208 ARG   A CD  1 
ATOM   1241 N NE  . ARG   A 1 171 ? -21.132 -19.931 0.941   1.00 17.18 ?  1208 ARG   A NE  1 
ATOM   1242 C CZ  . ARG   A 1 171 ? -21.552 -20.030 -0.312  1.00 16.29 ?  1208 ARG   A CZ  1 
ATOM   1243 N NH1 . ARG   A 1 171 ? -22.508 -19.247 -0.784  1.00 16.65 ?  1208 ARG   A NH1 1 
ATOM   1244 N NH2 . ARG   A 1 171 ? -20.996 -20.934 -1.113  1.00 18.17 ?  1208 ARG   A NH2 1 
ATOM   1245 N N   . ASN   A 1 172 ? -18.404 -15.226 1.716   1.00 11.23 ?  1209 ASN   A N   1 
ATOM   1246 C CA  . ASN   A 1 172 ? -16.975 -15.506 1.712   1.00 11.72 ?  1209 ASN   A CA  1 
ATOM   1247 C C   . ASN   A 1 172 ? -16.136 -14.244 1.551   1.00 12.45 ?  1209 ASN   A C   1 
ATOM   1248 O O   . ASN   A 1 172 ? -14.960 -14.327 1.188   1.00 11.71 ?  1209 ASN   A O   1 
ATOM   1249 C CB  . ASN   A 1 172 ? -16.645 -16.511 0.609   1.00 13.39 ?  1209 ASN   A CB  1 
ATOM   1250 C CG  . ASN   A 1 172 ? -17.272 -17.867 0.856   1.00 12.10 ?  1209 ASN   A CG  1 
ATOM   1251 O OD1 . ASN   A 1 172 ? -17.526 -18.246 2.000   1.00 11.48 ?  1209 ASN   A OD1 1 
ATOM   1252 N ND2 . ASN   A 1 172 ? -17.523 -18.607 -0.215  1.00 10.54 ?  1209 ASN   A ND2 1 
ATOM   1253 N N   . CYS   A 1 173 ? -16.720 -13.078 1.806   1.00 9.00  ?  1210 CYS   A N   1 
ATOM   1254 C CA  . CYS   A 1 173 ? -16.006 -11.811 1.796   1.00 8.79  ?  1210 CYS   A CA  1 
ATOM   1255 C C   . CYS   A 1 173 ? -16.231 -11.118 3.130   1.00 12.18 ?  1210 CYS   A C   1 
ATOM   1256 O O   . CYS   A 1 173 ? -17.357 -11.079 3.632   1.00 15.74 ?  1210 CYS   A O   1 
ATOM   1257 C CB  . CYS   A 1 173 ? -16.475 -10.921 0.647   1.00 10.70 ?  1210 CYS   A CB  1 
ATOM   1258 S SG  . CYS   A 1 173 ? -16.153 -11.613 -0.981  1.00 8.87  ?  1210 CYS   A SG  1 
ATOM   1259 N N   . MET   A 1 174 ? -15.163 -10.577 3.703   1.00 11.43 ?  1211 MET   A N   1 
ATOM   1260 C CA  . MET   A 1 174 ? -15.205 -10.034 5.052   1.00 11.83 ?  1211 MET   A CA  1 
ATOM   1261 C C   . MET   A 1 174 ? -15.073 -8.516  5.026   1.00 11.99 ?  1211 MET   A C   1 
ATOM   1262 O O   . MET   A 1 174 ? -14.695 -7.912  4.019   1.00 12.87 ?  1211 MET   A O   1 
ATOM   1263 C CB  . MET   A 1 174 ? -14.103 -10.658 5.913   1.00 12.38 ?  1211 MET   A CB  1 
ATOM   1264 C CG  . MET   A 1 174 ? -14.200 -12.172 6.015   1.00 17.24 ?  1211 MET   A CG  1 
ATOM   1265 S SD  . MET   A 1 174 ? -15.585 -12.773 7.006   1.00 29.67 ?  1211 MET   A SD  1 
ATOM   1266 C CE  . MET   A 1 174 ? -15.132 -12.241 8.651   1.00 17.40 ?  1211 MET   A CE  1 
ATOM   1267 N N   . LEU   A 1 175 ? -15.393 -7.904  6.165   1.00 12.40 ?  1212 LEU   A N   1 
ATOM   1268 C CA  . LEU   A 1 175 ? -15.393 -6.455  6.323   1.00 10.28 ?  1212 LEU   A CA  1 
ATOM   1269 C C   . LEU   A 1 175 ? -14.583 -6.101  7.560   1.00 10.73 ?  1212 LEU   A C   1 
ATOM   1270 O O   . LEU   A 1 175 ? -14.913 -6.545  8.664   1.00 11.12 ?  1212 LEU   A O   1 
ATOM   1271 C CB  . LEU   A 1 175 ? -16.821 -5.918  6.459   1.00 8.17  ?  1212 LEU   A CB  1 
ATOM   1272 C CG  . LEU   A 1 175 ? -17.728 -5.890  5.230   1.00 8.99  ?  1212 LEU   A CG  1 
ATOM   1273 C CD1 . LEU   A 1 175 ? -19.138 -5.531  5.650   1.00 16.01 ?  1212 LEU   A CD1 1 
ATOM   1274 C CD2 . LEU   A 1 175 ? -17.215 -4.900  4.205   1.00 10.28 ?  1212 LEU   A CD2 1 
ATOM   1275 N N   . ASP   A 1 176 ? -13.535 -5.300  7.382   1.00 11.76 ?  1213 ASP   A N   1 
ATOM   1276 C CA  . ASP   A 1 176 ? -12.766 -4.804  8.516   1.00 17.53 ?  1213 ASP   A CA  1 
ATOM   1277 C C   . ASP   A 1 176 ? -13.490 -3.604  9.128   1.00 17.86 ?  1213 ASP   A C   1 
ATOM   1278 O O   . ASP   A 1 176 ? -14.629 -3.287  8.772   1.00 18.09 ?  1213 ASP   A O   1 
ATOM   1279 C CB  . ASP   A 1 176 ? -11.332 -4.484  8.092   1.00 19.77 ?  1213 ASP   A CB  1 
ATOM   1280 C CG  . ASP   A 1 176 ? -11.247 -3.375  7.053   1.00 17.80 ?  1213 ASP   A CG  1 
ATOM   1281 O OD1 . ASP   A 1 176 ? -12.283 -2.769  6.708   1.00 14.68 ?  1213 ASP   A OD1 1 
ATOM   1282 O OD2 . ASP   A 1 176 ? -10.123 -3.105  6.579   1.00 16.34 -1 1213 ASP   A OD2 1 
ATOM   1283 N N   . GLU   A 1 177 ? -12.835 -2.911  10.060  1.00 16.54 ?  1214 GLU   A N   1 
ATOM   1284 C CA  . GLU   A 1 177 ? -13.479 -1.794  10.739  1.00 22.08 ?  1214 GLU   A CA  1 
ATOM   1285 C C   . GLU   A 1 177 ? -13.552 -0.535  9.883   1.00 21.16 ?  1214 GLU   A C   1 
ATOM   1286 O O   . GLU   A 1 177 ? -14.226 0.421   10.280  1.00 19.36 ?  1214 GLU   A O   1 
ATOM   1287 C CB  . GLU   A 1 177 ? -12.765 -1.486  12.060  1.00 26.65 ?  1214 GLU   A CB  1 
ATOM   1288 C CG  . GLU   A 1 177 ? -11.528 -0.608  11.940  1.00 28.63 ?  1214 GLU   A CG  1 
ATOM   1289 C CD  . GLU   A 1 177 ? -10.402 -1.280  11.181  1.00 34.27 ?  1214 GLU   A CD  1 
ATOM   1290 O OE1 . GLU   A 1 177 ? -9.580  -0.560  10.575  1.00 33.84 ?  1214 GLU   A OE1 1 
ATOM   1291 O OE2 . GLU   A 1 177 ? -10.340 -2.529  11.188  1.00 38.29 -1 1214 GLU   A OE2 1 
ATOM   1292 N N   . LYS   A 1 178 ? -12.878 -0.506  8.735   1.00 22.95 ?  1215 LYS   A N   1 
ATOM   1293 C CA  . LYS   A 1 178 ? -13.037 0.561   7.757   1.00 13.08 ?  1215 LYS   A CA  1 
ATOM   1294 C C   . LYS   A 1 178 ? -13.951 0.156   6.610   1.00 15.01 ?  1215 LYS   A C   1 
ATOM   1295 O O   . LYS   A 1 178 ? -13.995 0.851   5.589   1.00 11.16 ?  1215 LYS   A O   1 
ATOM   1296 C CB  . LYS   A 1 178 ? -11.675 0.995   7.211   1.00 19.84 ?  1215 LYS   A CB  1 
ATOM   1297 C CG  . LYS   A 1 178 ? -10.776 1.666   8.234   1.00 18.08 ?  1215 LYS   A CG  1 
ATOM   1298 C CD  . LYS   A 1 178 ? -9.456  2.080   7.605   1.00 18.12 ?  1215 LYS   A CD  1 
ATOM   1299 C CE  . LYS   A 1 178 ? -8.530  2.720   8.624   1.00 14.45 ?  1215 LYS   A CE  1 
ATOM   1300 N NZ  . LYS   A 1 178 ? -7.197  3.017   8.032   1.00 13.01 ?  1215 LYS   A NZ  1 
ATOM   1301 N N   . PHE   A 1 179 ? -14.667 -0.962  6.754   1.00 17.17 ?  1216 PHE   A N   1 
ATOM   1302 C CA  . PHE   A 1 179 ? -15.608 -1.457  5.750   1.00 13.47 ?  1216 PHE   A CA  1 
ATOM   1303 C C   . PHE   A 1 179 ? -14.939 -1.677  4.398   1.00 10.69 ?  1216 PHE   A C   1 
ATOM   1304 O O   . PHE   A 1 179 ? -15.584 -1.597  3.349   1.00 9.75  ?  1216 PHE   A O   1 
ATOM   1305 C CB  . PHE   A 1 179 ? -16.819 -0.530  5.624   1.00 14.74 ?  1216 PHE   A CB  1 
ATOM   1306 C CG  . PHE   A 1 179 ? -17.528 -0.302  6.925   1.00 18.17 ?  1216 PHE   A CG  1 
ATOM   1307 C CD1 . PHE   A 1 179 ? -18.432 -1.235  7.407   1.00 15.60 ?  1216 PHE   A CD1 1 
ATOM   1308 C CD2 . PHE   A 1 179 ? -17.274 0.830   7.681   1.00 17.45 ?  1216 PHE   A CD2 1 
ATOM   1309 C CE1 . PHE   A 1 179 ? -19.080 -1.037  8.609   1.00 18.26 ?  1216 PHE   A CE1 1 
ATOM   1310 C CE2 . PHE   A 1 179 ? -17.920 1.034   8.885   1.00 19.56 ?  1216 PHE   A CE2 1 
ATOM   1311 C CZ  . PHE   A 1 179 ? -18.824 0.101   9.349   1.00 20.29 ?  1216 PHE   A CZ  1 
ATOM   1312 N N   . THR   A 1 180 ? -13.639 -1.949  4.418   1.00 13.99 ?  1217 THR   A N   1 
ATOM   1313 C CA  . THR   A 1 180 ? -12.975 -2.488  3.242   1.00 12.53 ?  1217 THR   A CA  1 
ATOM   1314 C C   . THR   A 1 180 ? -13.354 -3.954  3.094   1.00 12.81 ?  1217 THR   A C   1 
ATOM   1315 O O   . THR   A 1 180 ? -13.254 -4.731  4.049   1.00 11.60 ?  1217 THR   A O   1 
ATOM   1316 C CB  . THR   A 1 180 ? -11.459 -2.341  3.361   1.00 15.16 ?  1217 THR   A CB  1 
ATOM   1317 O OG1 . THR   A 1 180 ? -11.109 -0.951  3.361   1.00 13.10 ?  1217 THR   A OG1 1 
ATOM   1318 C CG2 . THR   A 1 180 ? -10.765 -3.031  2.197   1.00 12.06 ?  1217 THR   A CG2 1 
ATOM   1319 N N   . VAL   A 1 181 ? -13.816 -4.325  1.914   1.00 10.47 ?  1218 VAL   A N   1 
ATOM   1320 C CA  . VAL   A 1 181 ? -14.198 -5.703  1.646   1.00 11.07 ?  1218 VAL   A CA  1 
ATOM   1321 C C   . VAL   A 1 181 ? -12.948 -6.472  1.265   1.00 15.20 ?  1218 VAL   A C   1 
ATOM   1322 O O   . VAL   A 1 181 ? -12.121 -5.993  0.484   1.00 14.76 ?  1218 VAL   A O   1 
ATOM   1323 C CB  . VAL   A 1 181 ? -15.259 -5.786  0.535   1.00 11.59 ?  1218 VAL   A CB  1 
ATOM   1324 C CG1 . VAL   A 1 181 ? -15.937 -7.148  0.562   1.00 13.86 ?  1218 VAL   A CG1 1 
ATOM   1325 C CG2 . VAL   A 1 181 ? -16.272 -4.673  0.690   1.00 15.75 ?  1218 VAL   A CG2 1 
ATOM   1326 N N   . LYS   A 1 182 ? -12.788 -7.660  1.829   1.00 11.39 ?  1219 LYS   A N   1 
ATOM   1327 C CA  . LYS   A 1 182 ? -11.689 -8.531  1.442   1.00 11.57 ?  1219 LYS   A CA  1 
ATOM   1328 C C   . LYS   A 1 182 ? -12.259 -9.847  0.964   1.00 11.22 ?  1219 LYS   A C   1 
ATOM   1329 O O   . LYS   A 1 182 ? -12.949 -10.530 1.726   1.00 13.81 ?  1219 LYS   A O   1 
ATOM   1330 C CB  . LYS   A 1 182 ? -10.729 -8.796  2.594   1.00 11.92 ?  1219 LYS   A CB  1 
ATOM   1331 C CG  . LYS   A 1 182 ? -9.986  -7.595  3.089   1.00 12.22 ?  1219 LYS   A CG  1 
ATOM   1332 C CD  . LYS   A 1 182 ? -9.067  -7.961  4.224   1.00 14.91 ?  1219 LYS   A CD  1 
ATOM   1333 C CE  . LYS   A 1 182 ? -8.363  -6.729  4.743   1.00 15.91 ?  1219 LYS   A CE  1 
ATOM   1334 N NZ  . LYS   A 1 182 ? -7.489  -6.112  3.707   1.00 31.67 ?  1219 LYS   A NZ  1 
ATOM   1335 N N   . VAL   A 1 183 ? -11.948 -10.216 -0.280  1.00 9.32  ?  1220 VAL   A N   1 
ATOM   1336 C CA  . VAL   A 1 183 ? -12.237 -11.575 -0.709  1.00 11.60 ?  1220 VAL   A CA  1 
ATOM   1337 C C   . VAL   A 1 183 ? -11.530 -12.543 0.209   1.00 12.34 ?  1220 VAL   A C   1 
ATOM   1338 O O   . VAL   A 1 183 ? -10.328 -12.417 0.467   1.00 18.21 ?  1220 VAL   A O   1 
ATOM   1339 C CB  . VAL   A 1 183 ? -11.790 -11.833 -2.154  1.00 12.08 ?  1220 VAL   A CB  1 
ATOM   1340 C CG1 . VAL   A 1 183 ? -12.233 -13.216 -2.541  1.00 6.77  ?  1220 VAL   A CG1 1 
ATOM   1341 C CG2 . VAL   A 1 183 ? -12.314 -10.799 -3.095  1.00 11.51 ?  1220 VAL   A CG2 1 
ATOM   1342 N N   . ALA   A 1 184 ? -12.263 -13.550 0.661   1.00 10.39 ?  1221 ALA   A N   1 
ATOM   1343 C CA  . ALA   A 1 184 ? -11.733 -14.502 1.616   1.00 13.60 ?  1221 ALA   A CA  1 
ATOM   1344 C C   . ALA   A 1 184 ? -12.128 -15.909 1.171   1.00 10.42 ?  1221 ALA   A C   1 
ATOM   1345 O O   . ALA   A 1 184 ? -12.448 -16.154 0.001   1.00 8.42  ?  1221 ALA   A O   1 
ATOM   1346 C CB  . ALA   A 1 184 ? -12.227 -14.119 3.015   1.00 14.31 ?  1221 ALA   A CB  1 
ATOM   1347 N N   . ASP   A 1 185 ? -12.082 -16.852 2.115   1.00 9.24  ?  1222 ASP   A N   1 
ATOM   1348 C CA  . ASP   A 1 185 ? -12.446 -18.249 1.871   1.00 10.02 ?  1222 ASP   A CA  1 
ATOM   1349 C C   . ASP   A 1 185 ? -11.597 -18.860 0.757   1.00 11.66 ?  1222 ASP   A C   1 
ATOM   1350 O O   . ASP   A 1 185 ? -12.099 -19.571 -0.115  1.00 11.82 ?  1222 ASP   A O   1 
ATOM   1351 C CB  . ASP   A 1 185 ? -13.938 -18.376 1.559   1.00 9.52  ?  1222 ASP   A CB  1 
ATOM   1352 C CG  . ASP   A 1 185 ? -14.432 -19.809 1.597   1.00 13.00 ?  1222 ASP   A CG  1 
ATOM   1353 O OD1 . ASP   A 1 185 ? -14.652 -20.342 2.703   1.00 12.32 ?  1222 ASP   A OD1 1 
ATOM   1354 O OD2 . ASP   A 1 185 ? -14.609 -20.399 0.511   1.00 14.18 -1 1222 ASP   A OD2 1 
ATOM   1355 N N   . PHE   A 1 186 ? -10.297 -18.579 0.782   1.00 14.61 ?  1223 PHE   A N   1 
ATOM   1356 C CA  . PHE   A 1 186 ? -9.381  -19.127 -0.207  1.00 18.06 ?  1223 PHE   A CA  1 
ATOM   1357 C C   . PHE   A 1 186 ? -8.074  -19.511 0.468   1.00 13.74 ?  1223 PHE   A C   1 
ATOM   1358 O O   . PHE   A 1 186 ? -7.635  -18.862 1.421   1.00 15.14 ?  1223 PHE   A O   1 
ATOM   1359 C CB  . PHE   A 1 186 ? -9.118  -18.138 -1.351  1.00 14.53 ?  1223 PHE   A CB  1 
ATOM   1360 C CG  . PHE   A 1 186 ? -8.238  -16.981 -0.972  1.00 15.76 ?  1223 PHE   A CG  1 
ATOM   1361 C CD1 . PHE   A 1 186 ? -8.765  -15.874 -0.327  1.00 17.34 ?  1223 PHE   A CD1 1 
ATOM   1362 C CD2 . PHE   A 1 186 ? -6.887  -16.992 -1.279  1.00 15.88 ?  1223 PHE   A CD2 1 
ATOM   1363 C CE1 . PHE   A 1 186 ? -7.957  -14.808 0.019   1.00 15.11 ?  1223 PHE   A CE1 1 
ATOM   1364 C CE2 . PHE   A 1 186 ? -6.076  -15.929 -0.936  1.00 16.08 ?  1223 PHE   A CE2 1 
ATOM   1365 C CZ  . PHE   A 1 186 ? -6.612  -14.837 -0.286  1.00 15.49 ?  1223 PHE   A CZ  1 
ATOM   1366 N N   . GLY   A 1 187 ? -7.464  -20.579 -0.034  1.00 13.39 ?  1224 GLY   A N   1 
ATOM   1367 C CA  . GLY   A 1 187 ? -6.183  -21.013 0.501   1.00 12.00 ?  1224 GLY   A CA  1 
ATOM   1368 C C   . GLY   A 1 187 ? -6.341  -21.638 1.872   1.00 12.79 ?  1224 GLY   A C   1 
ATOM   1369 O O   . GLY   A 1 187 ? -7.178  -22.521 2.086   1.00 14.68 ?  1224 GLY   A O   1 
ATOM   1370 N N   . LEU   A 1 188 ? -5.514  -21.184 2.816   1.00 12.23 ?  1225 LEU   A N   1 
ATOM   1371 C CA  . LEU   A 1 188 ? -5.623  -21.597 4.209   1.00 11.96 ?  1225 LEU   A CA  1 
ATOM   1372 C C   . LEU   A 1 188 ? -6.917  -21.132 4.861   1.00 10.18 ?  1225 LEU   A C   1 
ATOM   1373 O O   . LEU   A 1 188 ? -7.258  -21.626 5.940   1.00 12.74 ?  1225 LEU   A O   1 
ATOM   1374 C CB  . LEU   A 1 188 ? -4.435  -21.068 5.016   1.00 13.14 ?  1225 LEU   A CB  1 
ATOM   1375 C CG  . LEU   A 1 188 ? -3.070  -21.746 4.882   1.00 8.35  ?  1225 LEU   A CG  1 
ATOM   1376 C CD1 . LEU   A 1 188 ? -2.294  -21.182 3.710   1.00 8.36  ?  1225 LEU   A CD1 1 
ATOM   1377 C CD2 . LEU   A 1 188 ? -2.277  -21.595 6.170   1.00 8.51  ?  1225 LEU   A CD2 1 
ATOM   1378 N N   . ALA   A 1 189 ? -7.629  -20.189 4.248   1.00 10.97 ?  1226 ALA   A N   1 
ATOM   1379 C CA  . ALA   A 1 189 ? -8.922  -19.736 4.741   1.00 12.63 ?  1226 ALA   A CA  1 
ATOM   1380 C C   . ALA   A 1 189 ? -10.087 -20.439 4.058   1.00 10.45 ?  1226 ALA   A C   1 
ATOM   1381 O O   . ALA   A 1 189 ? -11.242 -20.199 4.425   1.00 10.76 ?  1226 ALA   A O   1 
ATOM   1382 C CB  . ALA   A 1 189 ? -9.054  -18.219 4.561   1.00 8.60  ?  1226 ALA   A CB  1 
ATOM   1383 N N   . ARG   A 1 190 ? -9.810  -21.298 3.080   1.00 9.25  ?  1227 ARG   A N   1 
ATOM   1384 C CA  . ARG   A 1 190 ? -10.863 -22.017 2.377   1.00 11.38 ?  1227 ARG   A CA  1 
ATOM   1385 C C   . ARG   A 1 190 ? -11.522 -23.029 3.305   1.00 11.32 ?  1227 ARG   A C   1 
ATOM   1386 O O   . ARG   A 1 190 ? -10.840 -23.812 3.972   1.00 11.04 ?  1227 ARG   A O   1 
ATOM   1387 C CB  . ARG   A 1 190 ? -10.285 -22.718 1.148   1.00 10.94 ?  1227 ARG   A CB  1 
ATOM   1388 C CG  . ARG   A 1 190 ? -11.200 -23.756 0.523   1.00 11.72 ?  1227 ARG   A CG  1 
ATOM   1389 C CD  . ARG   A 1 190 ? -12.407 -23.104 -0.117  1.00 14.92 ?  1227 ARG   A CD  1 
ATOM   1390 N NE  . ARG   A 1 190 ? -12.025 -21.932 -0.892  1.00 15.14 ?  1227 ARG   A NE  1 
ATOM   1391 C CZ  . ARG   A 1 190 ? -11.862 -21.922 -2.206  1.00 16.04 ?  1227 ARG   A CZ  1 
ATOM   1392 N NH1 . ARG   A 1 190 ? -12.054 -23.009 -2.937  1.00 14.32 ?  1227 ARG   A NH1 1 
ATOM   1393 N NH2 . ARG   A 1 190 ? -11.494 -20.793 -2.802  1.00 14.07 ?  1227 ARG   A NH2 1 
ATOM   1394 N N   . ASP   A 1 191 ? -12.848 -23.012 3.344   1.00 9.90  ?  1228 ASP   A N   1 
ATOM   1395 C CA  . ASP   A 1 191 ? -13.626 -23.885 4.220   1.00 11.18 ?  1228 ASP   A CA  1 
ATOM   1396 C C   . ASP   A 1 191 ? -15.088 -23.799 3.792   1.00 10.74 ?  1228 ASP   A C   1 
ATOM   1397 O O   . ASP   A 1 191 ? -15.414 -23.234 2.741   1.00 11.73 ?  1228 ASP   A O   1 
ATOM   1398 C CB  . ASP   A 1 191 ? -13.444 -23.503 5.690   1.00 12.08 ?  1228 ASP   A CB  1 
ATOM   1399 C CG  . ASP   A 1 191 ? -13.509 -24.699 6.616   1.00 16.71 ?  1228 ASP   A CG  1 
ATOM   1400 O OD1 . ASP   A 1 191 ? -14.021 -25.755 6.187   1.00 17.92 ?  1228 ASP   A OD1 1 
ATOM   1401 O OD2 . ASP   A 1 191 ? -13.053 -24.583 7.773   1.00 14.86 -1 1228 ASP   A OD2 1 
ATOM   1402 N N   . MET   A 1 192 ? -15.967 -24.370 4.610   1.00 11.73 ?  1229 MET   A N   1 
ATOM   1403 C CA  . MET   A 1 192 ? -17.415 -24.274 4.439   1.00 14.07 ?  1229 MET   A CA  1 
ATOM   1404 C C   . MET   A 1 192 ? -17.964 -23.578 5.678   1.00 15.11 ?  1229 MET   A C   1 
ATOM   1405 O O   . MET   A 1 192 ? -18.225 -24.226 6.696   1.00 15.86 ?  1229 MET   A O   1 
ATOM   1406 C CB  . MET   A 1 192 ? -18.051 -25.648 4.254   1.00 15.48 ?  1229 MET   A CB  1 
ATOM   1407 C CG  . MET   A 1 192 ? -18.267 -26.066 2.810   1.00 14.26 ?  1229 MET   A CG  1 
ATOM   1408 S SD  . MET   A 1 192 ? -18.865 -27.765 2.664   1.00 19.16 ?  1229 MET   A SD  1 
ATOM   1409 C CE  . MET   A 1 192 ? -19.452 -28.075 4.328   1.00 18.63 ?  1229 MET   A CE  1 
ATOM   1410 N N   . TYR   A 1 193 ? -18.134 -22.261 5.600   1.00 10.83 ?  1230 TYR   A N   1 
ATOM   1411 C CA  . TYR   A 1 193 ? -18.587 -21.487 6.747   1.00 10.77 ?  1230 TYR   A CA  1 
ATOM   1412 C C   . TYR   A 1 193 ? -20.105 -21.426 6.857   1.00 13.50 ?  1230 TYR   A C   1 
ATOM   1413 O O   . TYR   A 1 193 ? -20.621 -20.877 7.837   1.00 9.49  ?  1230 TYR   A O   1 
ATOM   1414 C CB  . TYR   A 1 193 ? -17.984 -20.080 6.691   1.00 10.57 ?  1230 TYR   A CB  1 
ATOM   1415 C CG  . TYR   A 1 193 ? -16.471 -20.097 6.772   1.00 8.98  ?  1230 TYR   A CG  1 
ATOM   1416 C CD1 . TYR   A 1 193 ? -15.823 -20.240 7.992   1.00 9.30  ?  1230 TYR   A CD1 1 
ATOM   1417 C CD2 . TYR   A 1 193 ? -15.692 -19.993 5.627   1.00 9.08  ?  1230 TYR   A CD2 1 
ATOM   1418 C CE1 . TYR   A 1 193 ? -14.443 -20.267 8.071   1.00 7.75  ?  1230 TYR   A CE1 1 
ATOM   1419 C CE2 . TYR   A 1 193 ? -14.310 -20.019 5.697   1.00 8.28  ?  1230 TYR   A CE2 1 
ATOM   1420 C CZ  . TYR   A 1 193 ? -13.692 -20.156 6.921   1.00 8.76  ?  1230 TYR   A CZ  1 
ATOM   1421 O OH  . TYR   A 1 193 ? -12.317 -20.183 6.994   1.00 7.71  ?  1230 TYR   A OH  1 
ATOM   1422 N N   . ASP   A 1 194 ? -20.827 -21.984 5.883   1.00 17.54 ?  1231 ASP   A N   1 
ATOM   1423 C CA  . ASP   A 1 194 ? -22.266 -22.219 6.005   1.00 17.57 ?  1231 ASP   A CA  1 
ATOM   1424 C C   . ASP   A 1 194 ? -22.580 -23.412 5.105   1.00 14.46 ?  1231 ASP   A C   1 
ATOM   1425 O O   . ASP   A 1 194 ? -22.658 -23.267 3.882   1.00 11.74 ?  1231 ASP   A O   1 
ATOM   1426 C CB  . ASP   A 1 194 ? -23.074 -20.986 5.620   1.00 15.08 ?  1231 ASP   A CB  1 
ATOM   1427 C CG  . ASP   A 1 194 ? -24.574 -21.238 5.636   1.00 18.70 ?  1231 ASP   A CG  1 
ATOM   1428 O OD1 . ASP   A 1 194 ? -25.013 -22.247 6.229   1.00 15.62 ?  1231 ASP   A OD1 1 
ATOM   1429 O OD2 . ASP   A 1 194 ? -25.318 -20.420 5.056   1.00 20.63 -1 1231 ASP   A OD2 1 
ATOM   1430 N N   . LYS   A 1 195 ? -22.761 -24.583 5.722   1.00 14.38 ?  1232 LYS   A N   1 
ATOM   1431 C CA  . LYS   A 1 195 ? -22.850 -25.834 4.975   1.00 17.57 ?  1232 LYS   A CA  1 
ATOM   1432 C C   . LYS   A 1 195 ? -24.079 -25.912 4.080   1.00 14.11 ?  1232 LYS   A C   1 
ATOM   1433 O O   . LYS   A 1 195 ? -24.101 -26.728 3.151   1.00 16.70 ?  1232 LYS   A O   1 
ATOM   1434 C CB  . LYS   A 1 195 ? -22.858 -27.017 5.945   1.00 16.51 ?  1232 LYS   A CB  1 
ATOM   1435 C CG  . LYS   A 1 195 ? -21.971 -26.829 7.165   1.00 18.22 ?  1232 LYS   A CG  1 
ATOM   1436 C CD  . LYS   A 1 195 ? -22.555 -27.520 8.391   1.00 24.74 ?  1232 LYS   A CD  1 
ATOM   1437 C CE  . LYS   A 1 195 ? -23.523 -26.611 9.135   1.00 20.31 ?  1232 LYS   A CE  1 
ATOM   1438 N NZ  . LYS   A 1 195 ? -23.835 -27.129 10.497  1.00 22.16 ?  1232 LYS   A NZ  1 
ATOM   1439 N N   . GLU   A 1 196 ? -25.091 -25.076 4.327   1.00 14.95 ?  1233 GLU   A N   1 
ATOM   1440 C CA  . GLU   A 1 196 ? -26.402 -25.268 3.713   1.00 16.69 ?  1233 GLU   A CA  1 
ATOM   1441 C C   . GLU   A 1 196 ? -26.348 -25.222 2.188   1.00 16.24 ?  1233 GLU   A C   1 
ATOM   1442 O O   . GLU   A 1 196 ? -27.176 -25.855 1.521   1.00 11.81 ?  1233 GLU   A O   1 
ATOM   1443 C CB  . GLU   A 1 196 ? -27.374 -24.213 4.250   1.00 16.67 ?  1233 GLU   A CB  1 
ATOM   1444 C CG  . GLU   A 1 196 ? -28.717 -24.151 3.542   1.00 19.10 ?  1233 GLU   A CG  1 
ATOM   1445 C CD  . GLU   A 1 196 ? -29.655 -23.137 4.164   1.00 22.20 ?  1233 GLU   A CD  1 
ATOM   1446 O OE1 . GLU   A 1 196 ? -29.325 -22.603 5.244   1.00 23.32 ?  1233 GLU   A OE1 1 
ATOM   1447 O OE2 . GLU   A 1 196 ? -30.722 -22.873 3.571   1.00 23.48 -1 1233 GLU   A OE2 1 
ATOM   1448 N N   . TYR   A 1 197 ? -25.379 -24.511 1.615   1.00 13.83 ?  1234 TYR   A N   1 
ATOM   1449 C CA  . TYR   A 1 197 ? -25.357 -24.249 0.182   1.00 13.48 ?  1234 TYR   A CA  1 
ATOM   1450 C C   . TYR   A 1 197 ? -24.379 -25.130 -0.585  1.00 13.15 ?  1234 TYR   A C   1 
ATOM   1451 O O   . TYR   A 1 197 ? -24.149 -24.884 -1.774  1.00 15.35 ?  1234 TYR   A O   1 
ATOM   1452 C CB  . TYR   A 1 197 ? -25.023 -22.779 -0.075  1.00 13.95 ?  1234 TYR   A CB  1 
ATOM   1453 C CG  . TYR   A 1 197 ? -26.036 -21.818 0.495   1.00 17.38 ?  1234 TYR   A CG  1 
ATOM   1454 C CD1 . TYR   A 1 197 ? -27.219 -21.550 -0.178  1.00 16.45 ?  1234 TYR   A CD1 1 
ATOM   1455 C CD2 . TYR   A 1 197 ? -25.811 -21.183 1.709   1.00 17.19 ?  1234 TYR   A CD2 1 
ATOM   1456 C CE1 . TYR   A 1 197 ? -28.150 -20.673 0.339   1.00 17.50 ?  1234 TYR   A CE1 1 
ATOM   1457 C CE2 . TYR   A 1 197 ? -26.737 -20.304 2.235   1.00 19.74 ?  1234 TYR   A CE2 1 
ATOM   1458 C CZ  . TYR   A 1 197 ? -27.905 -20.053 1.545   1.00 20.27 ?  1234 TYR   A CZ  1 
ATOM   1459 O OH  . TYR   A 1 197 ? -28.833 -19.178 2.062   1.00 20.55 ?  1234 TYR   A OH  1 
ATOM   1460 N N   . TYR   A 1 198 ? -23.806 -26.147 0.048   1.00 12.76 ?  1235 TYR   A N   1 
ATOM   1461 C CA  . TYR   A 1 198 ? -22.748 -26.935 -0.564  1.00 15.70 ?  1235 TYR   A CA  1 
ATOM   1462 C C   . TYR   A 1 198 ? -23.200 -28.364 -0.823  1.00 17.43 ?  1235 TYR   A C   1 
ATOM   1463 O O   . TYR   A 1 198 ? -23.814 -29.001 0.038   1.00 17.95 ?  1235 TYR   A O   1 
ATOM   1464 C CB  . TYR   A 1 198 ? -21.499 -26.949 0.317   1.00 16.36 ?  1235 TYR   A CB  1 
ATOM   1465 C CG  . TYR   A 1 198 ? -20.786 -25.623 0.361   1.00 18.17 ?  1235 TYR   A CG  1 
ATOM   1466 C CD1 . TYR   A 1 198 ? -19.856 -25.284 -0.612  1.00 16.07 ?  1235 TYR   A CD1 1 
ATOM   1467 C CD2 . TYR   A 1 198 ? -21.048 -24.705 1.368   1.00 15.29 ?  1235 TYR   A CD2 1 
ATOM   1468 C CE1 . TYR   A 1 198 ? -19.202 -24.074 -0.579  1.00 14.78 ?  1235 TYR   A CE1 1 
ATOM   1469 C CE2 . TYR   A 1 198 ? -20.395 -23.492 1.411   1.00 17.37 ?  1235 TYR   A CE2 1 
ATOM   1470 C CZ  . TYR   A 1 198 ? -19.474 -23.181 0.435   1.00 15.58 ?  1235 TYR   A CZ  1 
ATOM   1471 O OH  . TYR   A 1 198 ? -18.826 -21.968 0.473   1.00 18.49 ?  1235 TYR   A OH  1 
ATOM   1472 N N   . SER   A 1 199 ? -22.882 -28.861 -2.013  1.00 15.77 ?  1236 SER   A N   1 
ATOM   1473 C CA  . SER   A 1 199 ? -23.012 -30.273 -2.334  1.00 17.64 ?  1236 SER   A CA  1 
ATOM   1474 C C   . SER   A 1 199 ? -21.627 -30.900 -2.359  1.00 19.13 ?  1236 SER   A C   1 
ATOM   1475 O O   . SER   A 1 199 ? -20.736 -30.420 -3.069  1.00 18.93 ?  1236 SER   A O   1 
ATOM   1476 C CB  . SER   A 1 199 ? -23.702 -30.479 -3.683  1.00 20.75 ?  1236 SER   A CB  1 
ATOM   1477 O OG  . SER   A 1 199 ? -23.775 -31.858 -4.006  1.00 17.56 ?  1236 SER   A OG  1 
ATOM   1478 N N   . VAL   A 1 200 ? -21.443 -31.958 -1.575  1.00 22.22 ?  1237 VAL   A N   1 
ATOM   1479 C CA  . VAL   A 1 200 ? -20.219 -32.747 -1.641  1.00 16.33 ?  1237 VAL   A CA  1 
ATOM   1480 C C   . VAL   A 1 200 ? -20.385 -33.768 -2.760  1.00 13.76 ?  1237 VAL   A C   1 
ATOM   1481 O O   . VAL   A 1 200 ? -21.219 -34.672 -2.669  1.00 18.04 ?  1237 VAL   A O   1 
ATOM   1482 C CB  . VAL   A 1 200 ? -19.907 -33.437 -0.310  1.00 15.47 ?  1237 VAL   A CB  1 
ATOM   1483 C CG1 . VAL   A 1 200 ? -18.545 -34.099 -0.389  1.00 20.24 ?  1237 VAL   A CG1 1 
ATOM   1484 C CG2 . VAL   A 1 200 ? -19.962 -32.441 0.838   1.00 20.28 ?  1237 VAL   A CG2 1 
ATOM   1485 N N   . HIS   A 1 201 ? -19.607 -33.611 -3.825  1.00 12.07 ?  1238 HIS   A N   1 
ATOM   1486 C CA  . HIS   A 1 201 ? -19.536 -34.633 -4.857  1.00 15.93 ?  1238 HIS   A CA  1 
ATOM   1487 C C   . HIS   A 1 201 ? -19.117 -35.958 -4.226  1.00 17.95 ?  1238 HIS   A C   1 
ATOM   1488 O O   . HIS   A 1 201 ? -18.357 -35.992 -3.255  1.00 15.49 ?  1238 HIS   A O   1 
ATOM   1489 C CB  . HIS   A 1 201 ? -18.553 -34.193 -5.942  1.00 16.61 ?  1238 HIS   A CB  1 
ATOM   1490 C CG  . HIS   A 1 201 ? -18.636 -34.990 -7.204  1.00 18.22 ?  1238 HIS   A CG  1 
ATOM   1491 N ND1 . HIS   A 1 201 ? -18.166 -36.281 -7.301  1.00 16.36 ?  1238 HIS   A ND1 1 
ATOM   1492 C CD2 . HIS   A 1 201 ? -19.122 -34.673 -8.427  1.00 20.84 ?  1238 HIS   A CD2 1 
ATOM   1493 C CE1 . HIS   A 1 201 ? -18.365 -36.728 -8.528  1.00 22.15 ?  1238 HIS   A CE1 1 
ATOM   1494 N NE2 . HIS   A 1 201 ? -18.943 -35.772 -9.232  1.00 25.75 ?  1238 HIS   A NE2 1 
ATOM   1495 N N   . ASN   A 1 202 ? -19.648 -37.060 -4.756  1.00 19.56 ?  1239 ASN   A N   1 
ATOM   1496 C CA  . ASN   A 1 202 ? -19.487 -38.362 -4.119  1.00 20.72 ?  1239 ASN   A CA  1 
ATOM   1497 C C   . ASN   A 1 202 ? -18.479 -39.269 -4.815  1.00 13.90 ?  1239 ASN   A C   1 
ATOM   1498 O O   . ASN   A 1 202 ? -18.321 -40.423 -4.402  1.00 19.77 ?  1239 ASN   A O   1 
ATOM   1499 C CB  . ASN   A 1 202 ? -20.842 -39.073 -4.009  1.00 23.44 ?  1239 ASN   A CB  1 
ATOM   1500 C CG  . ASN   A 1 202 ? -21.506 -39.284 -5.352  1.00 17.04 ?  1239 ASN   A CG  1 
ATOM   1501 O OD1 . ASN   A 1 202 ? -21.241 -38.561 -6.312  1.00 20.25 ?  1239 ASN   A OD1 1 
ATOM   1502 N ND2 . ASN   A 1 202 ? -22.384 -40.278 -5.425  1.00 17.31 ?  1239 ASN   A ND2 1 
ATOM   1503 N N   . LYS   A 1 203 ? -17.803 -38.790 -5.857  1.00 15.59 ?  1240 LYS   A N   1 
ATOM   1504 C CA  . LYS   A 1 203 ? -16.614 -39.445 -6.390  1.00 22.29 ?  1240 LYS   A CA  1 
ATOM   1505 C C   . LYS   A 1 203 ? -15.374 -38.607 -6.111  1.00 21.16 ?  1240 LYS   A C   1 
ATOM   1506 O O   . LYS   A 1 203 ? -14.473 -39.043 -5.389  1.00 17.34 ?  1240 LYS   A O   1 
ATOM   1507 C CB  . LYS   A 1 203 ? -16.766 -39.705 -7.894  1.00 27.62 ?  1240 LYS   A CB  1 
ATOM   1508 N N   . THR   A 1 204 ? -15.308 -37.404 -6.673  1.00 21.98 ?  1241 THR   A N   1 
ATOM   1509 C CA  . THR   A 1 204 ? -14.398 -36.392 -6.163  1.00 14.94 ?  1241 THR   A CA  1 
ATOM   1510 C C   . THR   A 1 204 ? -14.943 -35.855 -4.849  1.00 14.84 ?  1241 THR   A C   1 
ATOM   1511 O O   . THR   A 1 204 ? -16.147 -35.642 -4.706  1.00 24.31 ?  1241 THR   A O   1 
ATOM   1512 C CB  . THR   A 1 204 ? -14.248 -35.250 -7.167  1.00 17.53 ?  1241 THR   A CB  1 
ATOM   1513 O OG1 . THR   A 1 204 ? -15.320 -34.316 -6.987  1.00 18.04 ?  1241 THR   A OG1 1 
ATOM   1514 C CG2 . THR   A 1 204 ? -14.290 -35.780 -8.590  1.00 18.49 ?  1241 THR   A CG2 1 
ATOM   1515 N N   . GLY   A 1 205 ? -14.061 -35.637 -3.880  1.00 15.25 ?  1242 GLY   A N   1 
ATOM   1516 C CA  . GLY   A 1 205 ? -14.528 -35.041 -2.642  1.00 17.03 ?  1242 GLY   A CA  1 
ATOM   1517 C C   . GLY   A 1 205 ? -14.939 -33.587 -2.747  1.00 17.63 ?  1242 GLY   A C   1 
ATOM   1518 O O   . GLY   A 1 205 ? -15.249 -32.974 -1.721  1.00 16.58 ?  1242 GLY   A O   1 
ATOM   1519 N N   . ALA   A 1 206 ? -14.970 -33.037 -3.961  1.00 16.22 ?  1243 ALA   A N   1 
ATOM   1520 C CA  . ALA   A 1 206 ? -15.138 -31.605 -4.168  1.00 18.11 ?  1243 ALA   A CA  1 
ATOM   1521 C C   . ALA   A 1 206 ? -16.412 -31.085 -3.514  1.00 21.15 ?  1243 ALA   A C   1 
ATOM   1522 O O   . ALA   A 1 206 ? -17.436 -31.771 -3.450  1.00 19.61 ?  1243 ALA   A O   1 
ATOM   1523 C CB  . ALA   A 1 206 ? -15.161 -31.286 -5.663  1.00 19.05 ?  1243 ALA   A CB  1 
ATOM   1524 N N   . LYS   A 1 207 ? -16.335 -29.851 -3.028  1.00 19.40 ?  1244 LYS   A N   1 
ATOM   1525 C CA  . LYS   A 1 207 ? -17.446 -29.167 -2.384  1.00 18.38 ?  1244 LYS   A CA  1 
ATOM   1526 C C   . LYS   A 1 207 ? -18.002 -28.129 -3.348  1.00 18.52 ?  1244 LYS   A C   1 
ATOM   1527 O O   . LYS   A 1 207 ? -17.256 -27.283 -3.851  1.00 21.19 ?  1244 LYS   A O   1 
ATOM   1528 C CB  . LYS   A 1 207 ? -16.985 -28.515 -1.081  1.00 17.93 ?  1244 LYS   A CB  1 
ATOM   1529 C CG  . LYS   A 1 207 ? -16.057 -29.408 -0.274  1.00 18.83 ?  1244 LYS   A CG  1 
ATOM   1530 C CD  . LYS   A 1 207 ? -15.926 -28.934 1.157   1.00 16.34 ?  1244 LYS   A CD  1 
ATOM   1531 C CE  . LYS   A 1 207 ? -15.187 -29.951 2.007   1.00 16.66 ?  1244 LYS   A CE  1 
ATOM   1532 N NZ  . LYS   A 1 207 ? -15.225 -29.583 3.448   1.00 25.75 ?  1244 LYS   A NZ  1 
ATOM   1533 N N   . LEU   A 1 208 ? -19.303 -28.192 -3.604  1.00 19.22 ?  1245 LEU   A N   1 
ATOM   1534 C CA  . LEU   A 1 208 ? -19.902 -27.468 -4.726  1.00 19.89 ?  1245 LEU   A CA  1 
ATOM   1535 C C   . LEU   A 1 208 ? -20.960 -26.474 -4.266  1.00 21.87 ?  1245 LEU   A C   1 
ATOM   1536 O O   . LEU   A 1 208 ? -22.008 -26.890 -3.737  1.00 18.53 ?  1245 LEU   A O   1 
ATOM   1537 C CB  . LEU   A 1 208 ? -20.505 -28.463 -5.715  1.00 19.68 ?  1245 LEU   A CB  1 
ATOM   1538 C CG  . LEU   A 1 208 ? -19.473 -29.305 -6.466  1.00 21.32 ?  1245 LEU   A CG  1 
ATOM   1539 C CD1 . LEU   A 1 208 ? -20.131 -30.148 -7.546  1.00 18.49 ?  1245 LEU   A CD1 1 
ATOM   1540 C CD2 . LEU   A 1 208 ? -18.381 -28.424 -7.059  1.00 20.01 ?  1245 LEU   A CD2 1 
ATOM   1541 N N   . PRO   A 1 209 ? -20.742 -25.166 -4.444  1.00 17.35 ?  1246 PRO   A N   1 
ATOM   1542 C CA  . PRO   A 1 209 ? -21.771 -24.138 -4.154  1.00 17.50 ?  1246 PRO   A CA  1 
ATOM   1543 C C   . PRO   A 1 209 ? -22.693 -23.913 -5.354  1.00 18.13 ?  1246 PRO   A C   1 
ATOM   1544 O O   . PRO   A 1 209 ? -22.570 -22.952 -6.115  1.00 17.74 ?  1246 PRO   A O   1 
ATOM   1545 C CB  . PRO   A 1 209 ? -20.935 -22.895 -3.836  1.00 16.15 ?  1246 PRO   A CB  1 
ATOM   1546 C CG  . PRO   A 1 209 ? -19.475 -23.283 -4.074  1.00 14.86 ?  1246 PRO   A CG  1 
ATOM   1547 C CD  . PRO   A 1 209 ? -19.459 -24.564 -4.826  1.00 16.73 ?  1246 PRO   A CD  1 
ATOM   1548 N N   . VAL   A 1 210 ? -23.662 -24.823 -5.499  1.00 18.94 ?  1247 VAL   A N   1 
ATOM   1549 C CA  . VAL   A 1 210 ? -24.429 -24.954 -6.739  1.00 20.01 ?  1247 VAL   A CA  1 
ATOM   1550 C C   . VAL   A 1 210 ? -25.095 -23.639 -7.128  1.00 15.97 ?  1247 VAL   A C   1 
ATOM   1551 O O   . VAL   A 1 210 ? -25.109 -23.260 -8.306  1.00 12.28 ?  1247 VAL   A O   1 
ATOM   1552 C CB  . VAL   A 1 210 ? -25.463 -26.087 -6.599  1.00 16.95 ?  1247 VAL   A CB  1 
ATOM   1553 C CG1 . VAL   A 1 210 ? -26.123 -26.377 -7.937  1.00 20.65 ?  1247 VAL   A CG1 1 
ATOM   1554 C CG2 . VAL   A 1 210 ? -24.801 -27.336 -6.037  1.00 23.94 ?  1247 VAL   A CG2 1 
ATOM   1555 N N   . LYS   A 1 211 ? -25.662 -22.926 -6.153  1.00 12.41 ?  1248 LYS   A N   1 
ATOM   1556 C CA  . LYS   A 1 211 ? -26.352 -21.676 -6.450  1.00 15.44 ?  1248 LYS   A CA  1 
ATOM   1557 C C   . LYS   A 1 211 ? -25.419 -20.592 -6.976  1.00 18.84 ?  1248 LYS   A C   1 
ATOM   1558 O O   . LYS   A 1 211 ? -25.905 -19.592 -7.515  1.00 16.91 ?  1248 LYS   A O   1 
ATOM   1559 C CB  . LYS   A 1 211 ? -27.079 -21.172 -5.202  1.00 16.30 ?  1248 LYS   A CB  1 
ATOM   1560 C CG  . LYS   A 1 211 ? -28.130 -22.127 -4.658  1.00 16.20 ?  1248 LYS   A CG  1 
ATOM   1561 C CD  . LYS   A 1 211 ? -29.258 -22.314 -5.653  1.00 17.86 ?  1248 LYS   A CD  1 
ATOM   1562 C CE  . LYS   A 1 211 ? -30.415 -23.102 -5.058  1.00 20.59 ?  1248 LYS   A CE  1 
ATOM   1563 N NZ  . LYS   A 1 211 ? -30.968 -22.456 -3.836  1.00 20.82 ?  1248 LYS   A NZ  1 
ATOM   1564 N N   . TRP   A 1 212 ? -24.102 -20.767 -6.840  1.00 17.39 ?  1249 TRP   A N   1 
ATOM   1565 C CA  . TRP   A 1 212 ? -23.126 -19.795 -7.310  1.00 14.46 ?  1249 TRP   A CA  1 
ATOM   1566 C C   . TRP   A 1 212 ? -22.256 -20.305 -8.450  1.00 16.66 ?  1249 TRP   A C   1 
ATOM   1567 O O   . TRP   A 1 212 ? -21.504 -19.513 -9.029  1.00 16.08 ?  1249 TRP   A O   1 
ATOM   1568 C CB  . TRP   A 1 212 ? -22.216 -19.353 -6.152  1.00 14.18 ?  1249 TRP   A CB  1 
ATOM   1569 C CG  . TRP   A 1 212 ? -22.875 -18.409 -5.197  1.00 15.15 ?  1249 TRP   A CG  1 
ATOM   1570 C CD1 . TRP   A 1 212 ? -22.755 -17.050 -5.175  1.00 15.57 ?  1249 TRP   A CD1 1 
ATOM   1571 C CD2 . TRP   A 1 212 ? -23.754 -18.752 -4.120  1.00 18.89 ?  1249 TRP   A CD2 1 
ATOM   1572 N NE1 . TRP   A 1 212 ? -23.510 -16.525 -4.154  1.00 14.34 ?  1249 TRP   A NE1 1 
ATOM   1573 C CE2 . TRP   A 1 212 ? -24.132 -17.549 -3.490  1.00 15.88 ?  1249 TRP   A CE2 1 
ATOM   1574 C CE3 . TRP   A 1 212 ? -24.259 -19.958 -3.627  1.00 17.66 ?  1249 TRP   A CE3 1 
ATOM   1575 C CZ2 . TRP   A 1 212 ? -24.992 -17.518 -2.394  1.00 16.47 ?  1249 TRP   A CZ2 1 
ATOM   1576 C CZ3 . TRP   A 1 212 ? -25.114 -19.925 -2.539  1.00 20.34 ?  1249 TRP   A CZ3 1 
ATOM   1577 C CH2 . TRP   A 1 212 ? -25.472 -18.714 -1.935  1.00 18.52 ?  1249 TRP   A CH2 1 
ATOM   1578 N N   . MET   A 1 213 ? -22.334 -21.589 -8.790  1.00 15.97 ?  1250 MET   A N   1 
ATOM   1579 C CA  . MET   A 1 213 ? -21.453 -22.164 -9.797  1.00 15.11 ?  1250 MET   A CA  1 
ATOM   1580 C C   . MET   A 1 213 ? -21.947 -21.866 -11.207 1.00 15.59 ?  1250 MET   A C   1 
ATOM   1581 O O   . MET   A 1 213 ? -23.151 -21.772 -11.465 1.00 18.08 ?  1250 MET   A O   1 
ATOM   1582 C CB  . MET   A 1 213 ? -21.335 -23.675 -9.611  1.00 19.78 ?  1250 MET   A CB  1 
ATOM   1583 C CG  . MET   A 1 213 ? -20.762 -24.087 -8.274  1.00 20.23 ?  1250 MET   A CG  1 
ATOM   1584 S SD  . MET   A 1 213 ? -20.750 -25.870 -8.047  1.00 23.41 ?  1250 MET   A SD  1 
ATOM   1585 C CE  . MET   A 1 213 ? -20.185 -26.416 -9.656  1.00 21.54 ?  1250 MET   A CE  1 
ATOM   1586 N N   . ALA   A 1 214 ? -20.995 -21.726 -12.125 1.00 15.28 ?  1251 ALA   A N   1 
ATOM   1587 C CA  . ALA   A 1 214 ? -21.325 -21.532 -13.525 1.00 18.15 ?  1251 ALA   A CA  1 
ATOM   1588 C C   . ALA   A 1 214 ? -21.879 -22.822 -14.122 1.00 16.37 ?  1251 ALA   A C   1 
ATOM   1589 O O   . ALA   A 1 214 ? -21.695 -23.918 -13.585 1.00 14.75 ?  1251 ALA   A O   1 
ATOM   1590 C CB  . ALA   A 1 214 ? -20.096 -21.069 -14.308 1.00 18.61 ?  1251 ALA   A CB  1 
ATOM   1591 N N   . LEU   A 1 215 ? -22.568 -22.678 -15.256 1.00 16.16 ?  1252 LEU   A N   1 
ATOM   1592 C CA  . LEU   A 1 215 ? -23.243 -23.824 -15.858 1.00 22.16 ?  1252 LEU   A CA  1 
ATOM   1593 C C   . LEU   A 1 215 ? -22.243 -24.874 -16.327 1.00 20.20 ?  1252 LEU   A C   1 
ATOM   1594 O O   . LEU   A 1 215 ? -22.474 -26.077 -16.158 1.00 20.92 ?  1252 LEU   A O   1 
ATOM   1595 C CB  . LEU   A 1 215 ? -24.126 -23.366 -17.018 1.00 21.04 ?  1252 LEU   A CB  1 
ATOM   1596 C CG  . LEU   A 1 215 ? -24.879 -24.483 -17.745 1.00 21.03 ?  1252 LEU   A CG  1 
ATOM   1597 C CD1 . LEU   A 1 215 ? -25.727 -25.278 -16.765 1.00 20.14 ?  1252 LEU   A CD1 1 
ATOM   1598 C CD2 . LEU   A 1 215 ? -25.737 -23.917 -18.864 1.00 16.34 ?  1252 LEU   A CD2 1 
ATOM   1599 N N   . GLU   A 1 216 ? -21.126 -24.442 -16.917 1.00 19.32 ?  1253 GLU   A N   1 
ATOM   1600 C CA  . GLU   A 1 216 ? -20.106 -25.401 -17.326 1.00 19.15 ?  1253 GLU   A CA  1 
ATOM   1601 C C   . GLU   A 1 216 ? -19.441 -26.056 -16.122 1.00 18.76 ?  1253 GLU   A C   1 
ATOM   1602 O O   . GLU   A 1 216 ? -18.929 -27.176 -16.231 1.00 23.31 ?  1253 GLU   A O   1 
ATOM   1603 C CB  . GLU   A 1 216 ? -19.059 -24.722 -18.210 1.00 19.17 ?  1253 GLU   A CB  1 
ATOM   1604 C CG  . GLU   A 1 216 ? -18.097 -23.811 -17.463 1.00 19.46 ?  1253 GLU   A CG  1 
ATOM   1605 C CD  . GLU   A 1 216 ? -18.453 -22.346 -17.602 1.00 21.21 ?  1253 GLU   A CD  1 
ATOM   1606 O OE1 . GLU   A 1 216 ? -17.715 -21.500 -17.055 1.00 26.75 ?  1253 GLU   A OE1 1 
ATOM   1607 O OE2 . GLU   A 1 216 ? -19.469 -22.040 -18.260 1.00 22.91 -1 1253 GLU   A OE2 1 
ATOM   1608 N N   . SER   A 1 217 ? -19.446 -25.381 -14.969 1.00 20.35 ?  1254 SER   A N   1 
ATOM   1609 C CA  . SER   A 1 217 ? -18.838 -25.955 -13.773 1.00 21.28 ?  1254 SER   A CA  1 
ATOM   1610 C C   . SER   A 1 217 ? -19.662 -27.119 -13.240 1.00 21.98 ?  1254 SER   A C   1 
ATOM   1611 O O   . SER   A 1 217 ? -19.107 -28.087 -12.708 1.00 19.10 ?  1254 SER   A O   1 
ATOM   1612 C CB  . SER   A 1 217 ? -18.670 -24.880 -12.701 1.00 16.97 ?  1254 SER   A CB  1 
ATOM   1613 O OG  . SER   A 1 217 ? -17.493 -24.124 -12.920 1.00 17.61 ?  1254 SER   A OG  1 
ATOM   1614 N N   . LEU   A 1 218 ? -20.988 -27.043 -13.365 1.00 18.91 ?  1255 LEU   A N   1 
ATOM   1615 C CA  . LEU   A 1 218 ? -21.825 -28.157 -12.935 1.00 19.18 ?  1255 LEU   A CA  1 
ATOM   1616 C C   . LEU   A 1 218 ? -21.700 -29.345 -13.878 1.00 19.24 ?  1255 LEU   A C   1 
ATOM   1617 O O   . LEU   A 1 218 ? -21.790 -30.497 -13.438 1.00 22.94 ?  1255 LEU   A O   1 
ATOM   1618 C CB  . LEU   A 1 218 ? -23.283 -27.711 -12.833 1.00 21.39 ?  1255 LEU   A CB  1 
ATOM   1619 C CG  . LEU   A 1 218 ? -23.582 -26.692 -11.734 1.00 24.21 ?  1255 LEU   A CG  1 
ATOM   1620 C CD1 . LEU   A 1 218 ? -24.839 -25.900 -12.057 1.00 19.43 ?  1255 LEU   A CD1 1 
ATOM   1621 C CD2 . LEU   A 1 218 ? -23.708 -27.394 -10.394 1.00 22.72 ?  1255 LEU   A CD2 1 
ATOM   1622 N N   . GLN   A 1 219 ? -21.481 -29.089 -15.167 1.00 18.44 ?  1256 GLN   A N   1 
ATOM   1623 C CA  . GLN   A 1 219 ? -21.409 -30.156 -16.155 1.00 19.77 ?  1256 GLN   A CA  1 
ATOM   1624 C C   . GLN   A 1 219 ? -20.061 -30.867 -16.169 1.00 21.02 ?  1256 GLN   A C   1 
ATOM   1625 O O   . GLN   A 1 219 ? -19.992 -32.020 -16.609 1.00 20.15 ?  1256 GLN   A O   1 
ATOM   1626 C CB  . GLN   A 1 219 ? -21.702 -29.596 -17.549 1.00 15.16 ?  1256 GLN   A CB  1 
ATOM   1627 C CG  . GLN   A 1 219 ? -23.135 -29.131 -17.749 1.00 18.07 ?  1256 GLN   A CG  1 
ATOM   1628 C CD  . GLN   A 1 219 ? -23.301 -28.279 -18.992 1.00 20.07 ?  1256 GLN   A CD  1 
ATOM   1629 O OE1 . GLN   A 1 219 ? -22.322 -27.923 -19.649 1.00 26.56 ?  1256 GLN   A OE1 1 
ATOM   1630 N NE2 . GLN   A 1 219 ? -24.543 -27.950 -19.323 1.00 18.28 ?  1256 GLN   A NE2 1 
ATOM   1631 N N   . THR   A 1 220 ? -18.995 -30.218 -15.700 1.00 22.45 ?  1257 THR   A N   1 
ATOM   1632 C CA  . THR   A 1 220 ? -17.650 -30.768 -15.820 1.00 21.46 ?  1257 THR   A CA  1 
ATOM   1633 C C   . THR   A 1 220 ? -16.817 -30.684 -14.547 1.00 22.49 ?  1257 THR   A C   1 
ATOM   1634 O O   . THR   A 1 220 ? -15.843 -31.438 -14.428 1.00 17.23 ?  1257 THR   A O   1 
ATOM   1635 C CB  . THR   A 1 220 ? -16.887 -30.062 -16.954 1.00 20.46 ?  1257 THR   A CB  1 
ATOM   1636 O OG1 . THR   A 1 220 ? -17.790 -29.776 -18.028 1.00 26.62 ?  1257 THR   A OG1 1 
ATOM   1637 C CG2 . THR   A 1 220 ? -15.770 -30.948 -17.489 1.00 20.18 ?  1257 THR   A CG2 1 
ATOM   1638 N N   . GLN   A 1 221 ? -17.167 -29.815 -13.594 1.00 23.65 ?  1258 GLN   A N   1 
ATOM   1639 C CA  . GLN   A 1 221 ? -16.375 -29.584 -12.382 1.00 18.56 ?  1258 GLN   A CA  1 
ATOM   1640 C C   . GLN   A 1 221 ? -14.976 -29.070 -12.713 1.00 23.41 ?  1258 GLN   A C   1 
ATOM   1641 O O   . GLN   A 1 221 ? -14.019 -29.314 -11.975 1.00 27.45 ?  1258 GLN   A O   1 
ATOM   1642 C CB  . GLN   A 1 221 ? -16.294 -30.839 -11.506 1.00 22.38 ?  1258 GLN   A CB  1 
ATOM   1643 C CG  . GLN   A 1 221 ? -16.102 -30.550 -10.024 1.00 24.39 ?  1258 GLN   A CG  1 
ATOM   1644 C CD  . GLN   A 1 221 ? -16.004 -31.811 -9.189  1.00 21.69 ?  1258 GLN   A CD  1 
ATOM   1645 O OE1 . GLN   A 1 221 ? -17.014 -32.429 -8.856  1.00 24.29 ?  1258 GLN   A OE1 1 
ATOM   1646 N NE2 . GLN   A 1 221 ? -14.782 -32.201 -8.850  1.00 15.88 ?  1258 GLN   A NE2 1 
ATOM   1647 N N   . LYS   A 1 222 ? -14.846 -28.351 -13.824 1.00 26.64 ?  1259 LYS   A N   1 
ATOM   1648 C CA  . LYS   A 1 222 ? -13.591 -27.718 -14.220 1.00 23.66 ?  1259 LYS   A CA  1 
ATOM   1649 C C   . LYS   A 1 222 ? -13.754 -26.214 -14.017 1.00 21.42 ?  1259 LYS   A C   1 
ATOM   1650 O O   . LYS   A 1 222 ? -14.289 -25.517 -14.882 1.00 23.08 ?  1259 LYS   A O   1 
ATOM   1651 C CB  . LYS   A 1 222 ? -13.234 -28.065 -15.664 1.00 24.51 ?  1259 LYS   A CB  1 
ATOM   1652 C CG  . LYS   A 1 222 ? -12.933 -29.537 -15.879 1.00 30.79 ?  1259 LYS   A CG  1 
ATOM   1653 C CD  . LYS   A 1 222 ? -12.166 -29.775 -17.167 1.00 32.38 ?  1259 LYS   A CD  1 
ATOM   1654 C CE  . LYS   A 1 222 ? -11.711 -31.223 -17.268 1.00 32.86 ?  1259 LYS   A CE  1 
ATOM   1655 N NZ  . LYS   A 1 222 ? -10.547 -31.388 -18.181 1.00 41.02 ?  1259 LYS   A NZ  1 
ATOM   1656 N N   . PHE   A 1 223 ? -13.297 -25.718 -12.869 1.00 26.23 ?  1260 PHE   A N   1 
ATOM   1657 C CA  . PHE   A 1 223 ? -13.440 -24.307 -12.525 1.00 21.32 ?  1260 PHE   A CA  1 
ATOM   1658 C C   . PHE   A 1 223 ? -12.385 -23.463 -13.240 1.00 22.42 ?  1260 PHE   A C   1 
ATOM   1659 O O   . PHE   A 1 223 ? -11.262 -23.920 -13.458 1.00 22.90 ?  1260 PHE   A O   1 
ATOM   1660 C CB  . PHE   A 1 223 ? -13.316 -24.132 -11.013 1.00 21.04 ?  1260 PHE   A CB  1 
ATOM   1661 C CG  . PHE   A 1 223 ? -14.505 -24.631 -10.245 1.00 25.46 ?  1260 PHE   A CG  1 
ATOM   1662 C CD1 . PHE   A 1 223 ? -15.588 -23.801 -10.017 1.00 22.93 ?  1260 PHE   A CD1 1 
ATOM   1663 C CD2 . PHE   A 1 223 ? -14.540 -25.923 -9.746  1.00 15.30 ?  1260 PHE   A CD2 1 
ATOM   1664 C CE1 . PHE   A 1 223 ? -16.684 -24.246 -9.314  1.00 17.99 ?  1260 PHE   A CE1 1 
ATOM   1665 C CE2 . PHE   A 1 223 ? -15.635 -26.375 -9.039  1.00 17.27 ?  1260 PHE   A CE2 1 
ATOM   1666 C CZ  . PHE   A 1 223 ? -16.709 -25.535 -8.822  1.00 24.86 ?  1260 PHE   A CZ  1 
ATOM   1667 N N   . THR   A 1 224 ? -12.739 -22.221 -13.602 1.00 17.73 ?  1261 THR   A N   1 
ATOM   1668 C CA  . THR   A 1 224 ? -11.845 -21.353 -14.384 1.00 18.41 ?  1261 THR   A CA  1 
ATOM   1669 C C   . THR   A 1 224 ? -11.913 -19.920 -13.890 1.00 21.74 ?  1261 THR   A C   1 
ATOM   1670 O O   . THR   A 1 224 ? -12.634 -19.606 -12.949 1.00 23.53 ?  1261 THR   A O   1 
ATOM   1671 C CB  . THR   A 1 224 ? -12.193 -21.329 -15.873 1.00 18.57 ?  1261 THR   A CB  1 
ATOM   1672 O OG1 . THR   A 1 224 ? -13.528 -20.829 -16.037 1.00 26.47 ?  1261 THR   A OG1 1 
ATOM   1673 C CG2 . THR   A 1 224 ? -12.050 -22.694 -16.490 1.00 13.43 ?  1261 THR   A CG2 1 
ATOM   1674 N N   . THR   A 1 225 ? -11.194 -19.013 -14.551 1.00 20.63 ?  1262 THR   A N   1 
ATOM   1675 C CA  . THR   A 1 225 ? -11.411 -17.622 -14.170 1.00 17.83 ?  1262 THR   A CA  1 
ATOM   1676 C C   . THR   A 1 225 ? -12.743 -17.093 -14.722 1.00 17.84 ?  1262 THR   A C   1 
ATOM   1677 O O   . THR   A 1 225 ? -13.359 -16.196 -14.124 1.00 18.85 ?  1262 THR   A O   1 
ATOM   1678 C CB  . THR   A 1 225 ? -10.210 -16.745 -14.541 1.00 18.74 ?  1262 THR   A CB  1 
ATOM   1679 O OG1 . THR   A 1 225 ? -9.123  -17.015 -13.641 1.00 20.44 ?  1262 THR   A OG1 1 
ATOM   1680 C CG2 . THR   A 1 225 ? -10.540 -15.267 -14.390 1.00 14.12 ?  1262 THR   A CG2 1 
ATOM   1681 N N   . LYS   A 1 226 ? -13.236 -17.667 -15.818 1.00 16.19 ?  1263 LYS   A N   1 
ATOM   1682 C CA  . LYS   A 1 226 ? -14.532 -17.234 -16.316 1.00 18.87 ?  1263 LYS   A CA  1 
ATOM   1683 C C   . LYS   A 1 226 ? -15.657 -17.670 -15.387 1.00 16.34 ?  1263 LYS   A C   1 
ATOM   1684 O O   . LYS   A 1 226 ? -16.655 -16.957 -15.261 1.00 18.51 ?  1263 LYS   A O   1 
ATOM   1685 C CB  . LYS   A 1 226 ? -14.752 -17.748 -17.736 1.00 16.27 ?  1263 LYS   A CB  1 
ATOM   1686 C CG  . LYS   A 1 226 ? -13.874 -17.029 -18.733 1.00 13.94 ?  1263 LYS   A CG  1 
ATOM   1687 C CD  . LYS   A 1 226 ? -13.845 -15.539 -18.440 1.00 19.14 ?  1263 LYS   A CD  1 
ATOM   1688 C CE  . LYS   A 1 226 ? -13.516 -14.783 -19.704 1.00 19.22 ?  1263 LYS   A CE  1 
ATOM   1689 N NZ  . LYS   A 1 226 ? -13.519 -13.311 -19.522 1.00 25.50 ?  1263 LYS   A NZ  1 
ATOM   1690 N N   . SER   A 1 227 ? -15.498 -18.795 -14.681 1.00 19.01 ?  1264 SER   A N   1 
ATOM   1691 C CA  . SER   A 1 227 ? -16.554 -19.227 -13.764 1.00 16.02 ?  1264 SER   A CA  1 
ATOM   1692 C C   . SER   A 1 227 ? -16.643 -18.385 -12.498 1.00 14.18 ?  1264 SER   A C   1 
ATOM   1693 O O   . SER   A 1 227 ? -17.686 -18.384 -11.838 1.00 16.69 ?  1264 SER   A O   1 
ATOM   1694 C CB  . SER   A 1 227 ? -16.374 -20.698 -13.389 1.00 16.81 ?  1264 SER   A CB  1 
ATOM   1695 O OG  . SER   A 1 227 ? -15.154 -20.922 -12.705 1.00 15.10 ?  1264 SER   A OG  1 
ATOM   1696 N N   . ASP   A 1 228 ? -15.598 -17.670 -12.124 1.00 13.00 ?  1265 ASP   A N   1 
ATOM   1697 C CA  . ASP   A 1 228 ? -15.791 -16.769 -11.003 1.00 13.69 ?  1265 ASP   A CA  1 
ATOM   1698 C C   . ASP   A 1 228 ? -16.530 -15.524 -11.438 1.00 12.24 ?  1265 ASP   A C   1 
ATOM   1699 O O   . ASP   A 1 228 ? -17.225 -14.905 -10.625 1.00 13.37 ?  1265 ASP   A O   1 
ATOM   1700 C CB  . ASP   A 1 228 ? -14.476 -16.347 -10.442 1.00 12.85 ?  1265 ASP   A CB  1 
ATOM   1701 C CG  . ASP   A 1 228 ? -13.774 -17.442 -9.719  1.00 13.08 ?  1265 ASP   A CG  1 
ATOM   1702 O OD1 . ASP   A 1 228 ? -14.264 -18.535 -9.323  1.00 12.54 ?  1265 ASP   A OD1 1 
ATOM   1703 O OD2 . ASP   A 1 228 ? -12.582 -17.113 -9.526  1.00 15.91 -1 1265 ASP   A OD2 1 
ATOM   1704 N N   . VAL   A 1 229 ? -16.420 -15.154 -12.716 1.00 12.38 ?  1266 VAL   A N   1 
ATOM   1705 C CA  . VAL   A 1 229 ? -17.210 -14.026 -13.184 1.00 16.11 ?  1266 VAL   A CA  1 
ATOM   1706 C C   . VAL   A 1 229 ? -18.685 -14.324 -12.975 1.00 15.03 ?  1266 VAL   A C   1 
ATOM   1707 O O   . VAL   A 1 229 ? -19.425 -13.496 -12.434 1.00 18.49 ?  1266 VAL   A O   1 
ATOM   1708 C CB  . VAL   A 1 229 ? -16.878 -13.689 -14.647 1.00 15.95 ?  1266 VAL   A CB  1 
ATOM   1709 C CG1 . VAL   A 1 229 ? -17.863 -12.672 -15.162 1.00 15.70 ?  1266 VAL   A CG1 1 
ATOM   1710 C CG2 . VAL   A 1 229 ? -15.456 -13.149 -14.737 1.00 12.11 ?  1266 VAL   A CG2 1 
ATOM   1711 N N   . TRP   A 1 230 ? -19.103 -15.554 -13.288 1.00 11.52 ?  1267 TRP   A N   1 
ATOM   1712 C CA  . TRP   A 1 230 ? -20.458 -15.999 -12.977 1.00 11.70 ?  1267 TRP   A CA  1 
ATOM   1713 C C   . TRP   A 1 230 ? -20.770 -15.824 -11.495 1.00 12.00 ?  1267 TRP   A C   1 
ATOM   1714 O O   . TRP   A 1 230 ? -21.770 -15.197 -11.129 1.00 12.40 ?  1267 TRP   A O   1 
ATOM   1715 C CB  . TRP   A 1 230 ? -20.629 -17.464 -13.392 1.00 13.69 ?  1267 TRP   A CB  1 
ATOM   1716 C CG  . TRP   A 1 230 ? -22.024 -18.001 -13.222 1.00 13.13 ?  1267 TRP   A CG  1 
ATOM   1717 C CD1 . TRP   A 1 230 ? -22.688 -18.220 -12.048 1.00 11.05 ?  1267 TRP   A CD1 1 
ATOM   1718 C CD2 . TRP   A 1 230 ? -22.919 -18.400 -14.267 1.00 13.20 ?  1267 TRP   A CD2 1 
ATOM   1719 N NE1 . TRP   A 1 230 ? -23.942 -18.721 -12.299 1.00 11.54 ?  1267 TRP   A NE1 1 
ATOM   1720 C CE2 . TRP   A 1 230 ? -24.108 -18.842 -13.653 1.00 13.71 ?  1267 TRP   A CE2 1 
ATOM   1721 C CE3 . TRP   A 1 230 ? -22.832 -18.424 -15.662 1.00 16.23 ?  1267 TRP   A CE3 1 
ATOM   1722 C CZ2 . TRP   A 1 230 ? -25.199 -19.301 -14.386 1.00 12.73 ?  1267 TRP   A CZ2 1 
ATOM   1723 C CZ3 . TRP   A 1 230 ? -23.916 -18.879 -16.387 1.00 15.26 ?  1267 TRP   A CZ3 1 
ATOM   1724 C CH2 . TRP   A 1 230 ? -25.083 -19.312 -15.748 1.00 11.96 ?  1267 TRP   A CH2 1 
ATOM   1725 N N   . SER   A 1 231 ? -19.918 -16.377 -10.626 1.00 14.66 ?  1268 SER   A N   1 
ATOM   1726 C CA  . SER   A 1 231 ? -20.129 -16.263 -9.187  1.00 14.53 ?  1268 SER   A CA  1 
ATOM   1727 C C   . SER   A 1 231 ? -20.117 -14.816 -8.711  1.00 13.01 ?  1268 SER   A C   1 
ATOM   1728 O O   . SER   A 1 231 ? -20.662 -14.523 -7.641  1.00 11.75 ?  1268 SER   A O   1 
ATOM   1729 C CB  . SER   A 1 231 ? -19.061 -17.059 -8.435  1.00 10.11 ?  1268 SER   A CB  1 
ATOM   1730 O OG  . SER   A 1 231 ? -19.054 -18.418 -8.835  1.00 16.92 ?  1268 SER   A OG  1 
ATOM   1731 N N   . PHE   A 1 232 ? -19.507 -13.908 -9.475  1.00 12.92 ?  1269 PHE   A N   1 
ATOM   1732 C CA  . PHE   A 1 232 ? -19.464 -12.509 -9.063  1.00 15.34 ?  1269 PHE   A CA  1 
ATOM   1733 C C   . PHE   A 1 232 ? -20.804 -11.816 -9.285  1.00 14.90 ?  1269 PHE   A C   1 
ATOM   1734 O O   . PHE   A 1 232 ? -21.200 -10.954 -8.496  1.00 14.91 ?  1269 PHE   A O   1 
ATOM   1735 C CB  . PHE   A 1 232 ? -18.362 -11.767 -9.812  1.00 15.10 ?  1269 PHE   A CB  1 
ATOM   1736 C CG  . PHE   A 1 232 ? -18.378 -10.291 -9.573  1.00 16.05 ?  1269 PHE   A CG  1 
ATOM   1737 C CD1 . PHE   A 1 232 ? -17.922 -9.771  -8.378  1.00 12.72 ?  1269 PHE   A CD1 1 
ATOM   1738 C CD2 . PHE   A 1 232 ? -18.888 -9.425  -10.525 1.00 15.50 ?  1269 PHE   A CD2 1 
ATOM   1739 C CE1 . PHE   A 1 232 ? -17.950 -8.416  -8.151  1.00 15.99 ?  1269 PHE   A CE1 1 
ATOM   1740 C CE2 . PHE   A 1 232 ? -18.918 -8.069  -10.301 1.00 16.84 ?  1269 PHE   A CE2 1 
ATOM   1741 C CZ  . PHE   A 1 232 ? -18.448 -7.563  -9.109  1.00 14.88 ?  1269 PHE   A CZ  1 
ATOM   1742 N N   . GLY   A 1 233 ? -21.497 -12.146 -10.376 1.00 14.03 ?  1270 GLY   A N   1 
ATOM   1743 C CA  . GLY   A 1 233 ? -22.789 -11.537 -10.638 1.00 14.66 ?  1270 GLY   A CA  1 
ATOM   1744 C C   . GLY   A 1 233 ? -23.879 -12.024 -9.713  1.00 13.57 ?  1270 GLY   A C   1 
ATOM   1745 O O   . GLY   A 1 233 ? -24.766 -11.249 -9.340  1.00 14.10 ?  1270 GLY   A O   1 
ATOM   1746 N N   . VAL   A 1 234 ? -23.848 -13.308 -9.347  1.00 13.53 ?  1271 VAL   A N   1 
ATOM   1747 C CA  . VAL   A 1 234 ? -24.657 -13.774 -8.226  1.00 12.84 ?  1271 VAL   A CA  1 
ATOM   1748 C C   . VAL   A 1 234 ? -24.319 -12.972 -6.980  1.00 15.11 ?  1271 VAL   A C   1 
ATOM   1749 O O   . VAL   A 1 234 ? -25.202 -12.616 -6.191  1.00 17.55 ?  1271 VAL   A O   1 
ATOM   1750 C CB  . VAL   A 1 234 ? -24.443 -15.283 -8.003  1.00 10.29 ?  1271 VAL   A CB  1 
ATOM   1751 C CG1 . VAL   A 1 234 ? -25.420 -15.818 -6.962  1.00 15.63 ?  1271 VAL   A CG1 1 
ATOM   1752 C CG2 . VAL   A 1 234 ? -24.580 -16.039 -9.314  1.00 15.43 ?  1271 VAL   A CG2 1 
ATOM   1753 N N   . LEU   A 1 235 ? -23.032 -12.670 -6.790  1.00 12.48 ?  1272 LEU   A N   1 
ATOM   1754 C CA  . LEU   A 1 235 ? -22.620 -11.826 -5.676  1.00 11.51 ?  1272 LEU   A CA  1 
ATOM   1755 C C   . LEU   A 1 235 ? -23.194 -10.423 -5.808  1.00 13.66 ?  1272 LEU   A C   1 
ATOM   1756 O O   . LEU   A 1 235 ? -23.645 -9.836  -4.818  1.00 12.64 ?  1272 LEU   A O   1 
ATOM   1757 C CB  . LEU   A 1 235 ? -21.095 -11.787 -5.593  1.00 10.29 ?  1272 LEU   A CB  1 
ATOM   1758 C CG  . LEU   A 1 235 ? -20.452 -10.697 -4.742  1.00 12.66 ?  1272 LEU   A CG  1 
ATOM   1759 C CD1 . LEU   A 1 235 ? -20.812 -10.893 -3.292  1.00 18.01 ?  1272 LEU   A CD1 1 
ATOM   1760 C CD2 . LEU   A 1 235 ? -18.948 -10.728 -4.928  1.00 10.91 ?  1272 LEU   A CD2 1 
ATOM   1761 N N   . LEU   A 1 236 ? -23.182 -9.863  -7.020  1.00 13.34 ?  1273 LEU   A N   1 
ATOM   1762 C CA  . LEU   A 1 236 ? -23.921 -8.627  -7.256  1.00 13.95 ?  1273 LEU   A CA  1 
ATOM   1763 C C   . LEU   A 1 236 ? -25.383 -8.798  -6.864  1.00 13.55 ?  1273 LEU   A C   1 
ATOM   1764 O O   . LEU   A 1 236 ? -25.997 -7.894  -6.288  1.00 11.75 ?  1273 LEU   A O   1 
ATOM   1765 C CB  . LEU   A 1 236 ? -23.814 -8.214  -8.724  1.00 17.23 ?  1273 LEU   A CB  1 
ATOM   1766 C CG  . LEU   A 1 236 ? -22.477 -7.721  -9.284  1.00 17.03 ?  1273 LEU   A CG  1 
ATOM   1767 C CD1 . LEU   A 1 236 ? -22.422 -7.905  -10.796 1.00 19.06 ?  1273 LEU   A CD1 1 
ATOM   1768 C CD2 . LEU   A 1 236 ? -22.219 -6.267  -8.920  1.00 14.57 ?  1273 LEU   A CD2 1 
ATOM   1769 N N   . TRP   A 1 237 ? -25.954 -9.967  -7.160  1.00 15.05 ?  1274 TRP   A N   1 
ATOM   1770 C CA  . TRP   A 1 237 ? -27.375 -10.187 -6.905  1.00 12.69 ?  1274 TRP   A CA  1 
ATOM   1771 C C   . TRP   A 1 237 ? -27.674 -10.184 -5.411  1.00 12.61 ?  1274 TRP   A C   1 
ATOM   1772 O O   . TRP   A 1 237 ? -28.608 -9.511  -4.959  1.00 11.48 ?  1274 TRP   A O   1 
ATOM   1773 C CB  . TRP   A 1 237 ? -27.831 -11.491 -7.575  1.00 14.33 ?  1274 TRP   A CB  1 
ATOM   1774 C CG  . TRP   A 1 237 ? -29.310 -11.648 -7.622  1.00 14.39 ?  1274 TRP   A CG  1 
ATOM   1775 C CD1 . TRP   A 1 237 ? -30.119 -11.272 -8.633  1.00 14.87 ?  1274 TRP   A CD1 1 
ATOM   1776 C CD2 . TRP   A 1 237 ? -30.174 -12.191 -6.608  1.00 15.22 ?  1274 TRP   A CD2 1 
ATOM   1777 N NE1 . TRP   A 1 237 ? -31.415 -11.543 -8.347  1.00 17.81 ?  1274 TRP   A NE1 1 
ATOM   1778 C CE2 . TRP   A 1 237 ? -31.485 -12.108 -7.109  1.00 14.59 ?  1274 TRP   A CE2 1 
ATOM   1779 C CE3 . TRP   A 1 237 ? -29.974 -12.740 -5.337  1.00 14.36 ?  1274 TRP   A CE3 1 
ATOM   1780 C CZ2 . TRP   A 1 237 ? -32.589 -12.545 -6.405  1.00 10.92 ?  1274 TRP   A CZ2 1 
ATOM   1781 C CZ3 . TRP   A 1 237 ? -31.097 -13.181 -4.629  1.00 14.70 ?  1274 TRP   A CZ3 1 
ATOM   1782 C CH2 . TRP   A 1 237 ? -32.383 -13.076 -5.173  1.00 11.17 ?  1274 TRP   A CH2 1 
ATOM   1783 N N   . GLU   A 1 238 ? -26.873 -10.909 -4.630  1.00 14.03 ?  1275 GLU   A N   1 
ATOM   1784 C CA  . GLU   A 1 238 ? -27.022 -10.906 -3.177  1.00 14.41 ?  1275 GLU   A CA  1 
ATOM   1785 C C   . GLU   A 1 238 ? -26.995 -9.485  -2.626  1.00 14.46 ?  1275 GLU   A C   1 
ATOM   1786 O O   . GLU   A 1 238 ? -27.837 -9.107  -1.802  1.00 14.56 ?  1275 GLU   A O   1 
ATOM   1787 C CB  . GLU   A 1 238 ? -25.913 -11.749 -2.557  1.00 14.94 ?  1275 GLU   A CB  1 
ATOM   1788 C CG  . GLU   A 1 238 ? -25.838 -13.122 -3.187  1.00 15.79 ?  1275 GLU   A CG  1 
ATOM   1789 C CD  . GLU   A 1 238 ? -24.803 -13.980 -2.539  1.00 11.04 ?  1275 GLU   A CD  1 
ATOM   1790 O OE1 . GLU   A 1 238 ? -25.005 -14.301 -1.356  1.00 10.85 ?  1275 GLU   A OE1 1 
ATOM   1791 O OE2 . GLU   A 1 238 ? -23.798 -14.326 -3.198  1.00 12.94 -1 1275 GLU   A OE2 1 
ATOM   1792 N N   . LEU   A 1 239 ? -26.052 -8.670  -3.104  1.00 12.95 ?  1276 LEU   A N   1 
ATOM   1793 C CA  . LEU   A 1 239 ? -25.945 -7.293  -2.633  1.00 12.79 ?  1276 LEU   A CA  1 
ATOM   1794 C C   . LEU   A 1 239 ? -27.220 -6.507  -2.921  1.00 15.13 ?  1276 LEU   A C   1 
ATOM   1795 O O   . LEU   A 1 239 ? -27.778 -5.860  -2.028  1.00 16.40 ?  1276 LEU   A O   1 
ATOM   1796 C CB  . LEU   A 1 239 ? -24.734 -6.615  -3.277  1.00 14.12 ?  1276 LEU   A CB  1 
ATOM   1797 C CG  . LEU   A 1 239 ? -23.360 -7.165  -2.889  1.00 10.05 ?  1276 LEU   A CG  1 
ATOM   1798 C CD1 . LEU   A 1 239 ? -22.290 -6.595  -3.802  1.00 7.87  ?  1276 LEU   A CD1 1 
ATOM   1799 C CD2 . LEU   A 1 239 ? -23.046 -6.869  -1.433  1.00 9.34  ?  1276 LEU   A CD2 1 
ATOM   1800 N N   . MET   A 1 240 ? -27.707 -6.566  -4.163  1.00 12.84 ?  1277 MET   A N   1 
ATOM   1801 C CA  . MET   A 1 240 ? -28.885 -5.785  -4.531  1.00 14.20 ?  1277 MET   A CA  1 
ATOM   1802 C C   . MET   A 1 240 ? -30.139 -6.274  -3.816  1.00 17.64 ?  1277 MET   A C   1 
ATOM   1803 O O   . MET   A 1 240 ? -31.072 -5.492  -3.601  1.00 17.56 ?  1277 MET   A O   1 
ATOM   1804 C CB  . MET   A 1 240 ? -29.078 -5.815  -6.045  1.00 17.90 ?  1277 MET   A CB  1 
ATOM   1805 C CG  . MET   A 1 240 ? -27.976 -5.089  -6.798  1.00 17.64 ?  1277 MET   A CG  1 
ATOM   1806 S SD  . MET   A 1 240 ? -27.994 -3.314  -6.473  1.00 18.21 ?  1277 MET   A SD  1 
ATOM   1807 C CE  . MET   A 1 240 ? -26.602 -3.144  -5.360  1.00 10.98 ?  1277 MET   A CE  1 
ATOM   1808 N N   . THR   A 1 241 ? -30.184 -7.550  -3.445  1.00 17.09 ?  1278 THR   A N   1 
ATOM   1809 C CA  . THR   A 1 241 ? -31.243 -8.068  -2.591  1.00 17.49 ?  1278 THR   A CA  1 
ATOM   1810 C C   . THR   A 1 241 ? -30.858 -8.042  -1.119  1.00 16.16 ?  1278 THR   A C   1 
ATOM   1811 O O   . THR   A 1 241 ? -31.646 -8.485  -0.276  1.00 13.70 ?  1278 THR   A O   1 
ATOM   1812 C CB  . THR   A 1 241 ? -31.606 -9.497  -3.005  1.00 14.12 ?  1278 THR   A CB  1 
ATOM   1813 O OG1 . THR   A 1 241 ? -30.478 -10.357 -2.801  1.00 13.43 ?  1278 THR   A OG1 1 
ATOM   1814 C CG2 . THR   A 1 241 ? -32.010 -9.539  -4.471  1.00 15.01 ?  1278 THR   A CG2 1 
ATOM   1815 N N   . ARG   A 1 242 ? -29.666 -7.531  -0.803  1.00 17.38 ?  1279 ARG   A N   1 
ATOM   1816 C CA  . ARG   A 1 242 ? -29.158 -7.446  0.566   1.00 15.56 ?  1279 ARG   A CA  1 
ATOM   1817 C C   . ARG   A 1 242 ? -29.121 -8.823  1.226   1.00 12.58 ?  1279 ARG   A C   1 
ATOM   1818 O O   . ARG   A 1 242 ? -29.550 -9.005  2.367   1.00 11.67 ?  1279 ARG   A O   1 
ATOM   1819 C CB  . ARG   A 1 242 ? -29.968 -6.446  1.396   1.00 13.40 ?  1279 ARG   A CB  1 
ATOM   1820 C CG  . ARG   A 1 242 ? -29.526 -5.008  1.174   1.00 18.79 ?  1279 ARG   A CG  1 
ATOM   1821 C CD  . ARG   A 1 242 ? -30.188 -4.017  2.121   1.00 23.31 ?  1279 ARG   A CD  1 
ATOM   1822 N NE  . ARG   A 1 242 ? -29.794 -4.224  3.509   1.00 14.50 ?  1279 ARG   A NE  1 
ATOM   1823 C CZ  . ARG   A 1 242 ? -30.536 -3.887  4.555   1.00 21.90 ?  1279 ARG   A CZ  1 
ATOM   1824 N NH1 . ARG   A 1 242 ? -31.714 -3.302  4.407   1.00 25.56 ?  1279 ARG   A NH1 1 
ATOM   1825 N NH2 . ARG   A 1 242 ? -30.083 -4.136  5.780   1.00 21.08 ?  1279 ARG   A NH2 1 
ATOM   1826 N N   . GLY   A 1 243 ? -28.604 -9.801  0.486   1.00 14.69 ?  1280 GLY   A N   1 
ATOM   1827 C CA  . GLY   A 1 243 ? -28.372 -11.122 1.032   1.00 17.05 ?  1280 GLY   A CA  1 
ATOM   1828 C C   . GLY   A 1 243 ? -29.531 -12.085 0.942   1.00 15.39 ?  1280 GLY   A C   1 
ATOM   1829 O O   . GLY   A 1 243 ? -29.678 -12.943 1.819   1.00 15.96 ?  1280 GLY   A O   1 
ATOM   1830 N N   . ALA   A 1 244 ? -30.365 -11.973 -0.082  1.00 16.45 ?  1281 ALA   A N   1 
ATOM   1831 C CA  . ALA   A 1 244 ? -31.430 -12.949 -0.223  1.00 16.98 ?  1281 ALA   A CA  1 
ATOM   1832 C C   . ALA   A 1 244 ? -30.892 -14.228 -0.861  1.00 16.81 ?  1281 ALA   A C   1 
ATOM   1833 O O   . ALA   A 1 244 ? -29.980 -14.179 -1.691  1.00 15.87 ?  1281 ALA   A O   1 
ATOM   1834 C CB  . ALA   A 1 244 ? -32.568 -12.388 -1.068  1.00 14.98 ?  1281 ALA   A CB  1 
ATOM   1835 N N   . PRO   A 1 245 ? -31.427 -15.383 -0.474  1.00 15.03 ?  1282 PRO   A N   1 
ATOM   1836 C CA  . PRO   A 1 245 ? -31.005 -16.643 -1.093  1.00 17.24 ?  1282 PRO   A CA  1 
ATOM   1837 C C   . PRO   A 1 245 ? -31.294 -16.640 -2.582  1.00 14.04 ?  1282 PRO   A C   1 
ATOM   1838 O O   . PRO   A 1 245 ? -32.376 -16.216 -3.014  1.00 14.56 ?  1282 PRO   A O   1 
ATOM   1839 C CB  . PRO   A 1 245 ? -31.853 -17.696 -0.364  1.00 17.87 ?  1282 PRO   A CB  1 
ATOM   1840 C CG  . PRO   A 1 245 ? -32.193 -17.068 0.942   1.00 15.21 ?  1282 PRO   A CG  1 
ATOM   1841 C CD  . PRO   A 1 245 ? -32.337 -15.600 0.663   1.00 14.88 ?  1282 PRO   A CD  1 
ATOM   1842 N N   . PRO   A 1 246 ? -30.346 -17.088 -3.402  1.00 12.13 ?  1283 PRO   A N   1 
ATOM   1843 C CA  . PRO   A 1 246 ? -30.602 -17.176 -4.843  1.00 14.36 ?  1283 PRO   A CA  1 
ATOM   1844 C C   . PRO   A 1 246 ? -31.413 -18.415 -5.188  1.00 15.23 ?  1283 PRO   A C   1 
ATOM   1845 O O   . PRO   A 1 246 ? -31.240 -19.483 -4.595  1.00 18.75 ?  1283 PRO   A O   1 
ATOM   1846 C CB  . PRO   A 1 246 ? -29.194 -17.245 -5.446  1.00 14.97 ?  1283 PRO   A CB  1 
ATOM   1847 C CG  . PRO   A 1 246 ? -28.369 -17.868 -4.374  1.00 12.81 ?  1283 PRO   A CG  1 
ATOM   1848 C CD  . PRO   A 1 246 ? -28.947 -17.401 -3.064  1.00 11.11 ?  1283 PRO   A CD  1 
ATOM   1849 N N   . TYR   A 1 247 ? -32.306 -18.259 -6.164  1.00 13.07 ?  1284 TYR   A N   1 
ATOM   1850 C CA  . TYR   A 1 247 ? -33.196 -19.312 -6.614  1.00 17.54 ?  1284 TYR   A CA  1 
ATOM   1851 C C   . TYR   A 1 247 ? -33.960 -19.986 -5.468  1.00 18.09 ?  1284 TYR   A C   1 
ATOM   1852 O O   . TYR   A 1 247 ? -33.791 -21.165 -5.204  1.00 20.85 ?  1284 TYR   A O   1 
ATOM   1853 C CB  . TYR   A 1 247 ? -32.421 -20.376 -7.406  1.00 16.56 ?  1284 TYR   A CB  1 
ATOM   1854 C CG  . TYR   A 1 247 ? -31.373 -19.862 -8.365  1.00 14.26 ?  1284 TYR   A CG  1 
ATOM   1855 C CD1 . TYR   A 1 247 ? -31.712 -19.462 -9.651  1.00 15.26 ?  1284 TYR   A CD1 1 
ATOM   1856 C CD2 . TYR   A 1 247 ? -30.035 -19.817 -7.997  1.00 12.60 ?  1284 TYR   A CD2 1 
ATOM   1857 C CE1 . TYR   A 1 247 ? -30.750 -19.013 -10.537 1.00 16.38 ?  1284 TYR   A CE1 1 
ATOM   1858 C CE2 . TYR   A 1 247 ? -29.066 -19.369 -8.875  1.00 12.96 ?  1284 TYR   A CE2 1 
ATOM   1859 C CZ  . TYR   A 1 247 ? -29.429 -18.968 -10.143 1.00 13.80 ?  1284 TYR   A CZ  1 
ATOM   1860 O OH  . TYR   A 1 247 ? -28.467 -18.520 -11.020 1.00 11.85 ?  1284 TYR   A OH  1 
ATOM   1861 N N   . PRO   A 1 248 ? -34.826 -19.232 -4.767  1.00 18.73 ?  1285 PRO   A N   1 
ATOM   1862 C CA  . PRO   A 1 248 ? -35.621 -19.869 -3.704  1.00 19.08 ?  1285 PRO   A CA  1 
ATOM   1863 C C   . PRO   A 1 248 ? -36.686 -20.809 -4.237  1.00 27.29 ?  1285 PRO   A C   1 
ATOM   1864 O O   . PRO   A 1 248 ? -37.129 -21.699 -3.500  1.00 33.67 ?  1285 PRO   A O   1 
ATOM   1865 C CB  . PRO   A 1 248 ? -36.247 -18.679 -2.958  1.00 23.13 ?  1285 PRO   A CB  1 
ATOM   1866 C CG  . PRO   A 1 248 ? -35.598 -17.444 -3.529  1.00 18.87 ?  1285 PRO   A CG  1 
ATOM   1867 C CD  . PRO   A 1 248 ? -35.147 -17.805 -4.903  1.00 21.46 ?  1285 PRO   A CD  1 
ATOM   1868 N N   . ASP   A 1 249 ? -37.109 -20.643 -5.487  1.00 27.77 ?  1286 ASP   A N   1 
ATOM   1869 C CA  . ASP   A 1 249 ? -38.078 -21.528 -6.118  1.00 25.19 ?  1286 ASP   A CA  1 
ATOM   1870 C C   . ASP   A 1 249 ? -37.421 -22.670 -6.881  1.00 25.38 ?  1286 ASP   A C   1 
ATOM   1871 O O   . ASP   A 1 249 ? -38.126 -23.448 -7.532  1.00 28.56 ?  1286 ASP   A O   1 
ATOM   1872 C CB  . ASP   A 1 249 ? -38.977 -20.731 -7.069  1.00 30.95 ?  1286 ASP   A CB  1 
ATOM   1873 C CG  . ASP   A 1 249 ? -39.761 -19.646 -6.358  1.00 34.83 ?  1286 ASP   A CG  1 
ATOM   1874 O OD1 . ASP   A 1 249 ? -39.489 -19.398 -5.165  1.00 36.61 ?  1286 ASP   A OD1 1 
ATOM   1875 O OD2 . ASP   A 1 249 ? -40.646 -19.038 -6.996  1.00 38.37 -1 1286 ASP   A OD2 1 
ATOM   1876 N N   . VAL   A 1 250 ? -36.096 -22.782 -6.825  1.00 22.94 ?  1287 VAL   A N   1 
ATOM   1877 C CA  . VAL   A 1 250 ? -35.343 -23.767 -7.594  1.00 23.84 ?  1287 VAL   A CA  1 
ATOM   1878 C C   . VAL   A 1 250 ? -34.403 -24.478 -6.633  1.00 24.62 ?  1287 VAL   A C   1 
ATOM   1879 O O   . VAL   A 1 250 ? -33.400 -23.898 -6.200  1.00 21.56 ?  1287 VAL   A O   1 
ATOM   1880 C CB  . VAL   A 1 250 ? -34.550 -23.124 -8.741  1.00 21.35 ?  1287 VAL   A CB  1 
ATOM   1881 C CG1 . VAL   A 1 250 ? -34.102 -24.178 -9.744  1.00 21.52 ?  1287 VAL   A CG1 1 
ATOM   1882 C CG2 . VAL   A 1 250 ? -35.369 -22.039 -9.410  1.00 24.43 ?  1287 VAL   A CG2 1 
ATOM   1883 N N   . ASN   A 1 251 ? -34.717 -25.727 -6.300  1.00 23.42 ?  1288 ASN   A N   1 
ATOM   1884 C CA  . ASN   A 1 251 ? -33.790 -26.497 -5.489  1.00 22.66 ?  1288 ASN   A CA  1 
ATOM   1885 C C   . ASN   A 1 251 ? -32.600 -26.939 -6.340  1.00 21.05 ?  1288 ASN   A C   1 
ATOM   1886 O O   . ASN   A 1 251 ? -32.584 -26.793 -7.566  1.00 25.54 ?  1288 ASN   A O   1 
ATOM   1887 C CB  . ASN   A 1 251 ? -34.495 -27.690 -4.836  1.00 23.18 ?  1288 ASN   A CB  1 
ATOM   1888 C CG  . ASN   A 1 251 ? -35.102 -28.648 -5.843  1.00 21.04 ?  1288 ASN   A CG  1 
ATOM   1889 O OD1 . ASN   A 1 251 ? -34.423 -29.149 -6.736  1.00 26.85 ?  1288 ASN   A OD1 1 
ATOM   1890 N ND2 . ASN   A 1 251 ? -36.394 -28.914 -5.692  1.00 19.81 ?  1288 ASN   A ND2 1 
ATOM   1891 N N   . THR   A 1 252 ? -31.596 -27.500 -5.663  1.00 19.37 ?  1289 THR   A N   1 
ATOM   1892 C CA  . THR   A 1 252 ? -30.291 -27.715 -6.285  1.00 21.99 ?  1289 THR   A CA  1 
ATOM   1893 C C   . THR   A 1 252 ? -30.383 -28.586 -7.533  1.00 23.54 ?  1289 THR   A C   1 
ATOM   1894 O O   . THR   A 1 252 ? -29.646 -28.368 -8.502  1.00 26.82 ?  1289 THR   A O   1 
ATOM   1895 C CB  . THR   A 1 252 ? -29.338 -28.344 -5.273  1.00 19.48 ?  1289 THR   A CB  1 
ATOM   1896 O OG1 . THR   A 1 252 ? -30.005 -29.416 -4.593  1.00 19.49 ?  1289 THR   A OG1 1 
ATOM   1897 C CG2 . THR   A 1 252 ? -28.895 -27.309 -4.258  1.00 16.84 ?  1289 THR   A CG2 1 
ATOM   1898 N N   . PHE   A 1 253 ? -31.281 -29.572 -7.531  1.00 17.97 ?  1290 PHE   A N   1 
ATOM   1899 C CA  . PHE   A 1 253 ? -31.325 -30.545 -8.620  1.00 19.32 ?  1290 PHE   A CA  1 
ATOM   1900 C C   . PHE   A 1 253 ? -31.640 -29.872 -9.951  1.00 21.59 ?  1290 PHE   A C   1 
ATOM   1901 O O   . PHE   A 1 253 ? -30.832 -29.906 -10.887 1.00 22.65 ?  1290 PHE   A O   1 
ATOM   1902 C CB  . PHE   A 1 253 ? -32.351 -31.638 -8.306  1.00 18.26 ?  1290 PHE   A CB  1 
ATOM   1903 C CG  . PHE   A 1 253 ? -32.426 -32.000 -6.848  1.00 17.02 ?  1290 PHE   A CG  1 
ATOM   1904 C CD1 . PHE   A 1 253 ? -31.276 -32.283 -6.128  1.00 18.34 ?  1290 PHE   A CD1 1 
ATOM   1905 C CD2 . PHE   A 1 253 ? -33.646 -32.058 -6.199  1.00 17.31 ?  1290 PHE   A CD2 1 
ATOM   1906 C CE1 . PHE   A 1 253 ? -31.346 -32.608 -4.790  1.00 20.21 ?  1290 PHE   A CE1 1 
ATOM   1907 C CE2 . PHE   A 1 253 ? -33.719 -32.384 -4.858  1.00 16.57 ?  1290 PHE   A CE2 1 
ATOM   1908 C CZ  . PHE   A 1 253 ? -32.567 -32.660 -4.154  1.00 18.49 ?  1290 PHE   A CZ  1 
ATOM   1909 N N   . ASP   A 1 254 ? -32.809 -29.243 -10.051 1.00 24.82 ?  1291 ASP   A N   1 
ATOM   1910 C CA  . ASP   A 1 254 ? -33.238 -28.618 -11.295 1.00 28.42 ?  1291 ASP   A CA  1 
ATOM   1911 C C   . ASP   A 1 254 ? -32.563 -27.276 -11.556 1.00 22.39 ?  1291 ASP   A C   1 
ATOM   1912 O O   . ASP   A 1 254 ? -33.008 -26.547 -12.449 1.00 23.44 ?  1291 ASP   A O   1 
ATOM   1913 C CB  . ASP   A 1 254 ? -34.759 -28.439 -11.304 1.00 22.37 ?  1291 ASP   A CB  1 
ATOM   1914 C CG  . ASP   A 1 254 ? -35.253 -27.569 -10.166 1.00 32.43 ?  1291 ASP   A CG  1 
ATOM   1915 O OD1 . ASP   A 1 254 ? -34.830 -27.795 -9.016  1.00 29.43 ?  1291 ASP   A OD1 1 
ATOM   1916 O OD2 . ASP   A 1 254 ? -36.067 -26.657 -10.422 1.00 38.26 -1 1291 ASP   A OD2 1 
ATOM   1917 N N   . ILE   A 1 255 ? -31.512 -26.932 -10.807 1.00 24.38 ?  1292 ILE   A N   1 
ATOM   1918 C CA  . ILE   A 1 255 ? -30.783 -25.695 -11.076 1.00 26.13 ?  1292 ILE   A CA  1 
ATOM   1919 C C   . ILE   A 1 255 ? -30.180 -25.728 -12.474 1.00 23.91 ?  1292 ILE   A C   1 
ATOM   1920 O O   . ILE   A 1 255 ? -30.186 -24.722 -13.194 1.00 23.20 ?  1292 ILE   A O   1 
ATOM   1921 C CB  . ILE   A 1 255 ? -29.713 -25.454 -9.996  1.00 23.33 ?  1292 ILE   A CB  1 
ATOM   1922 C CG1 . ILE   A 1 255 ? -30.365 -24.861 -8.749  1.00 19.97 ?  1292 ILE   A CG1 1 
ATOM   1923 C CG2 . ILE   A 1 255 ? -28.609 -24.545 -10.517 1.00 26.31 ?  1292 ILE   A CG2 1 
ATOM   1924 C CD1 . ILE   A 1 255 ? -30.461 -23.353 -8.780  1.00 19.21 ?  1292 ILE   A CD1 1 
ATOM   1925 N N   . THR   A 1 256 ? -29.672 -26.890 -12.888 1.00 22.74 ?  1293 THR   A N   1 
ATOM   1926 C CA  . THR   A 1 256 ? -29.148 -27.025 -14.242 1.00 19.53 ?  1293 THR   A CA  1 
ATOM   1927 C C   . THR   A 1 256 ? -30.255 -26.868 -15.277 1.00 21.13 ?  1293 THR   A C   1 
ATOM   1928 O O   . THR   A 1 256 ? -30.037 -26.286 -16.346 1.00 21.17 ?  1293 THR   A O   1 
ATOM   1929 C CB  . THR   A 1 256 ? -28.454 -28.377 -14.404 1.00 17.35 ?  1293 THR   A CB  1 
ATOM   1930 O OG1 . THR   A 1 256 ? -27.554 -28.587 -13.308 1.00 20.20 ?  1293 THR   A OG1 1 
ATOM   1931 C CG2 . THR   A 1 256 ? -27.673 -28.424 -15.709 1.00 18.86 ?  1293 THR   A CG2 1 
ATOM   1932 N N   . VAL   A 1 257 ? -31.450 -27.381 -14.978 1.00 23.97 ?  1294 VAL   A N   1 
ATOM   1933 C CA  . VAL   A 1 257 ? -32.570 -27.243 -15.904 1.00 26.22 ?  1294 VAL   A CA  1 
ATOM   1934 C C   . VAL   A 1 257 ? -32.988 -25.783 -16.020 1.00 24.55 ?  1294 VAL   A C   1 
ATOM   1935 O O   . VAL   A 1 257 ? -33.377 -25.318 -17.097 1.00 23.89 ?  1294 VAL   A O   1 
ATOM   1936 C CB  . VAL   A 1 257 ? -33.743 -28.136 -15.459 1.00 27.19 ?  1294 VAL   A CB  1 
ATOM   1937 N N   . TYR   A 1 258 ? -32.913 -25.041 -14.913 1.00 23.68 ?  1295 TYR   A N   1 
ATOM   1938 C CA  . TYR   A 1 258 ? -33.216 -23.613 -14.939 1.00 21.24 ?  1295 TYR   A CA  1 
ATOM   1939 C C   . TYR   A 1 258 ? -32.259 -22.868 -15.861 1.00 22.95 ?  1295 TYR   A C   1 
ATOM   1940 O O   . TYR   A 1 258 ? -32.679 -22.035 -16.673 1.00 22.05 ?  1295 TYR   A O   1 
ATOM   1941 C CB  . TYR   A 1 258 ? -33.152 -23.060 -13.513 1.00 22.16 ?  1295 TYR   A CB  1 
ATOM   1942 C CG  . TYR   A 1 258 ? -33.758 -21.687 -13.301 1.00 24.49 ?  1295 TYR   A CG  1 
ATOM   1943 C CD1 . TYR   A 1 258 ? -33.055 -20.530 -13.619 1.00 20.56 ?  1295 TYR   A CD1 1 
ATOM   1944 C CD2 . TYR   A 1 258 ? -35.012 -21.549 -12.724 1.00 21.83 ?  1295 TYR   A CD2 1 
ATOM   1945 C CE1 . TYR   A 1 258 ? -33.603 -19.276 -13.397 1.00 22.19 ?  1295 TYR   A CE1 1 
ATOM   1946 C CE2 . TYR   A 1 258 ? -35.568 -20.303 -12.503 1.00 22.59 ?  1295 TYR   A CE2 1 
ATOM   1947 C CZ  . TYR   A 1 258 ? -34.862 -19.171 -12.842 1.00 21.05 ?  1295 TYR   A CZ  1 
ATOM   1948 O OH  . TYR   A 1 258 ? -35.416 -17.930 -12.621 1.00 22.15 ?  1295 TYR   A OH  1 
ATOM   1949 N N   . LEU   A 1 259 ? -30.965 -23.174 -15.765 1.00 19.57 ?  1296 LEU   A N   1 
ATOM   1950 C CA  . LEU   A 1 259 ? -29.943 -22.441 -16.501 1.00 20.07 ?  1296 LEU   A CA  1 
ATOM   1951 C C   . LEU   A 1 259 ? -29.736 -22.948 -17.921 1.00 21.71 ?  1296 LEU   A C   1 
ATOM   1952 O O   . LEU   A 1 259 ? -29.249 -22.188 -18.766 1.00 18.48 ?  1296 LEU   A O   1 
ATOM   1953 C CB  . LEU   A 1 259 ? -28.617 -22.491 -15.739 1.00 19.02 ?  1296 LEU   A CB  1 
ATOM   1954 C CG  . LEU   A 1 259 ? -28.704 -21.980 -14.299 1.00 17.75 ?  1296 LEU   A CG  1 
ATOM   1955 C CD1 . LEU   A 1 259 ? -27.549 -22.507 -13.464 1.00 21.33 ?  1296 LEU   A CD1 1 
ATOM   1956 C CD2 . LEU   A 1 259 ? -28.747 -20.456 -14.271 1.00 17.89 ?  1296 LEU   A CD2 1 
ATOM   1957 N N   . LEU   A 1 260 ? -30.078 -24.204 -18.207 1.00 19.21 ?  1297 LEU   A N   1 
ATOM   1958 C CA  . LEU   A 1 260 ? -30.031 -24.678 -19.584 1.00 19.99 ?  1297 LEU   A CA  1 
ATOM   1959 C C   . LEU   A 1 260 ? -31.220 -24.188 -20.399 1.00 18.19 ?  1297 LEU   A C   1 
ATOM   1960 O O   . LEU   A 1 260 ? -31.133 -24.139 -21.631 1.00 21.49 ?  1297 LEU   A O   1 
ATOM   1961 C CB  . LEU   A 1 260 ? -29.960 -26.206 -19.623 1.00 25.31 ?  1297 LEU   A CB  1 
ATOM   1962 C CG  . LEU   A 1 260 ? -28.556 -26.784 -19.813 1.00 23.04 ?  1297 LEU   A CG  1 
ATOM   1963 C CD1 . LEU   A 1 260 ? -28.526 -28.266 -19.472 1.00 19.19 ?  1297 LEU   A CD1 1 
ATOM   1964 C CD2 . LEU   A 1 260 ? -28.061 -26.543 -21.232 1.00 20.59 ?  1297 LEU   A CD2 1 
ATOM   1965 N N   . GLN   A 1 261 ? -32.323 -23.826 -19.739 1.00 21.82 ?  1298 GLN   A N   1 
ATOM   1966 C CA  . GLN   A 1 261 ? -33.425 -23.170 -20.435 1.00 23.40 ?  1298 GLN   A CA  1 
ATOM   1967 C C   . GLN   A 1 261 ? -33.026 -21.787 -20.931 1.00 19.00 ?  1298 GLN   A C   1 
ATOM   1968 O O   . GLN   A 1 261 ? -33.585 -21.297 -21.920 1.00 21.82 ?  1298 GLN   A O   1 
ATOM   1969 C CB  . GLN   A 1 261 ? -34.637 -23.049 -19.511 1.00 22.37 ?  1298 GLN   A CB  1 
ATOM   1970 C CG  . GLN   A 1 261 ? -35.411 -24.332 -19.277 1.00 23.92 ?  1298 GLN   A CG  1 
ATOM   1971 C CD  . GLN   A 1 261 ? -36.336 -24.228 -18.078 1.00 23.04 ?  1298 GLN   A CD  1 
ATOM   1972 O OE1 . GLN   A 1 261 ? -36.500 -23.154 -17.499 1.00 29.05 ?  1298 GLN   A OE1 1 
ATOM   1973 N NE2 . GLN   A 1 261 ? -36.935 -25.347 -17.691 1.00 27.25 ?  1298 GLN   A NE2 1 
ATOM   1974 N N   . GLY   A 1 262 ? -32.067 -21.151 -20.264 1.00 18.33 ?  1299 GLY   A N   1 
ATOM   1975 C CA  . GLY   A 1 262 ? -31.747 -19.760 -20.496 1.00 18.20 ?  1299 GLY   A CA  1 
ATOM   1976 C C   . GLY   A 1 262 ? -32.279 -18.818 -19.440 1.00 14.66 ?  1299 GLY   A C   1 
ATOM   1977 O O   . GLY   A 1 262 ? -32.128 -17.599 -19.587 1.00 15.73 ?  1299 GLY   A O   1 
ATOM   1978 N N   . ARG   A 1 263 ? -32.898 -19.343 -18.386 1.00 13.87 ?  1300 ARG   A N   1 
ATOM   1979 C CA  . ARG   A 1 263 ? -33.442 -18.515 -17.321 1.00 18.54 ?  1300 ARG   A CA  1 
ATOM   1980 C C   . ARG   A 1 263 ? -32.340 -18.140 -16.338 1.00 16.06 ?  1300 ARG   A C   1 
ATOM   1981 O O   . ARG   A 1 263 ? -31.556 -18.995 -15.914 1.00 16.02 ?  1300 ARG   A O   1 
ATOM   1982 C CB  . ARG   A 1 263 ? -34.567 -19.253 -16.596 1.00 20.13 ?  1300 ARG   A CB  1 
ATOM   1983 C CG  . ARG   A 1 263 ? -35.911 -19.255 -17.303 1.00 19.61 ?  1300 ARG   A CG  1 
ATOM   1984 C CD  . ARG   A 1 263 ? -36.924 -20.054 -16.492 1.00 21.46 ?  1300 ARG   A CD  1 
ATOM   1985 N NE  . ARG   A 1 263 ? -38.134 -20.363 -17.246 1.00 27.89 ?  1300 ARG   A NE  1 
ATOM   1986 C CZ  . ARG   A 1 263 ? -39.288 -19.725 -17.104 1.00 27.59 ?  1300 ARG   A CZ  1 
ATOM   1987 N NH1 . ARG   A 1 263 ? -39.428 -18.731 -16.242 1.00 27.18 ?  1300 ARG   A NH1 1 
ATOM   1988 N NH2 . ARG   A 1 263 ? -40.329 -20.098 -17.842 1.00 24.26 ?  1300 ARG   A NH2 1 
ATOM   1989 N N   . ARG   A 1 264 ? -32.283 -16.864 -15.977 1.00 12.74 ?  1301 ARG   A N   1 
ATOM   1990 C CA  . ARG   A 1 264 ? -31.344 -16.355 -14.987 1.00 12.87 ?  1301 ARG   A CA  1 
ATOM   1991 C C   . ARG   A 1 264 ? -32.113 -15.773 -13.806 1.00 15.23 ?  1301 ARG   A C   1 
ATOM   1992 O O   . ARG   A 1 264 ? -33.343 -15.835 -13.743 1.00 12.83 ?  1301 ARG   A O   1 
ATOM   1993 C CB  . ARG   A 1 264 ? -30.416 -15.302 -15.599 1.00 11.20 ?  1301 ARG   A CB  1 
ATOM   1994 C CG  . ARG   A 1 264 ? -29.602 -15.790 -16.779 1.00 11.77 ?  1301 ARG   A CG  1 
ATOM   1995 C CD  . ARG   A 1 264 ? -28.462 -16.681 -16.327 1.00 13.18 ?  1301 ARG   A CD  1 
ATOM   1996 N NE  . ARG   A 1 264 ? -27.899 -17.436 -17.438 1.00 13.24 ?  1301 ARG   A NE  1 
ATOM   1997 C CZ  . ARG   A 1 264 ? -28.402 -18.571 -17.902 1.00 13.80 ?  1301 ARG   A CZ  1 
ATOM   1998 N NH1 . ARG   A 1 264 ? -29.471 -19.125 -17.355 1.00 16.20 ?  1301 ARG   A NH1 1 
ATOM   1999 N NH2 . ARG   A 1 264 ? -27.819 -19.163 -18.940 1.00 16.11 ?  1301 ARG   A NH2 1 
ATOM   2000 N N   . LEU   A 1 265 ? -31.370 -15.200 -12.863 1.00 15.80 ?  1302 LEU   A N   1 
ATOM   2001 C CA  . LEU   A 1 265 ? -31.991 -14.522 -11.736 1.00 14.45 ?  1302 LEU   A CA  1 
ATOM   2002 C C   . LEU   A 1 265 ? -32.655 -13.231 -12.198 1.00 13.27 ?  1302 LEU   A C   1 
ATOM   2003 O O   . LEU   A 1 265 ? -32.099 -12.479 -13.003 1.00 13.90 ?  1302 LEU   A O   1 
ATOM   2004 C CB  . LEU   A 1 265 ? -30.953 -14.226 -10.654 1.00 14.55 ?  1302 LEU   A CB  1 
ATOM   2005 C CG  . LEU   A 1 265 ? -30.571 -15.405 -9.759  1.00 14.34 ?  1302 LEU   A CG  1 
ATOM   2006 C CD1 . LEU   A 1 265 ? -29.502 -14.998 -8.759  1.00 15.34 ?  1302 LEU   A CD1 1 
ATOM   2007 C CD2 . LEU   A 1 265 ? -31.801 -15.943 -9.043  1.00 11.68 ?  1302 LEU   A CD2 1 
ATOM   2008 N N   . LEU   A 1 266 ? -33.857 -12.981 -11.686 1.00 17.45 ?  1303 LEU   A N   1 
ATOM   2009 C CA  . LEU   A 1 266 ? -34.620 -11.815 -12.101 1.00 16.33 ?  1303 LEU   A CA  1 
ATOM   2010 C C   . LEU   A 1 266 ? -34.007 -10.539 -11.533 1.00 17.41 ?  1303 LEU   A C   1 
ATOM   2011 O O   . LEU   A 1 266 ? -33.208 -10.563 -10.593 1.00 16.35 ?  1303 LEU   A O   1 
ATOM   2012 C CB  . LEU   A 1 266 ? -36.077 -11.945 -11.658 1.00 10.24 ?  1303 LEU   A CB  1 
ATOM   2013 C CG  . LEU   A 1 266 ? -36.907 -12.963 -12.440 1.00 8.67  ?  1303 LEU   A CG  1 
ATOM   2014 C CD1 . LEU   A 1 266 ? -38.378 -12.864 -12.069 1.00 8.65  ?  1303 LEU   A CD1 1 
ATOM   2015 C CD2 . LEU   A 1 266 ? -36.715 -12.771 -13.936 1.00 7.66  ?  1303 LEU   A CD2 1 
ATOM   2016 N N   . GLN   A 1 267 ? -34.393 -9.416  -12.117 1.00 15.78 ?  1304 GLN   A N   1 
ATOM   2017 C CA  . GLN   A 1 267 ? -33.861 -8.134  -11.677 1.00 15.91 ?  1304 GLN   A CA  1 
ATOM   2018 C C   . GLN   A 1 267 ? -34.466 -7.741  -10.340 1.00 16.32 ?  1304 GLN   A C   1 
ATOM   2019 O O   . GLN   A 1 267 ? -35.693 -7.612  -10.239 1.00 18.23 ?  1304 GLN   A O   1 
ATOM   2020 C CB  . GLN   A 1 267 ? -34.147 -7.052  -12.701 1.00 16.19 ?  1304 GLN   A CB  1 
ATOM   2021 C CG  . GLN   A 1 267 ? -33.528 -5.723  -12.346 1.00 16.54 ?  1304 GLN   A CG  1 
ATOM   2022 C CD  . GLN   A 1 267 ? -33.855 -4.661  -13.359 1.00 18.81 ?  1304 GLN   A CD  1 
ATOM   2023 O OE1 . GLN   A 1 267 ? -34.487 -4.938  -14.380 1.00 21.80 ?  1304 GLN   A OE1 1 
ATOM   2024 N NE2 . GLN   A 1 267 ? -33.411 -3.439  -13.101 1.00 17.80 ?  1304 GLN   A NE2 1 
ATOM   2025 N N   . PRO   A 1 268 ? -33.659 -7.518  -9.307  1.00 15.80 ?  1305 PRO   A N   1 
ATOM   2026 C CA  . PRO   A 1 268 ? -34.213 -7.107  -8.014  1.00 17.84 ?  1305 PRO   A CA  1 
ATOM   2027 C C   . PRO   A 1 268 ? -34.904 -5.755  -8.111  1.00 17.74 ?  1305 PRO   A C   1 
ATOM   2028 O O   . PRO   A 1 268 ? -34.681 -4.970  -9.037  1.00 18.87 ?  1305 PRO   A O   1 
ATOM   2029 C CB  . PRO   A 1 268 ? -32.983 -7.046  -7.098  1.00 18.33 ?  1305 PRO   A CB  1 
ATOM   2030 C CG  . PRO   A 1 268 ? -31.907 -7.806  -7.822  1.00 16.27 ?  1305 PRO   A CG  1 
ATOM   2031 C CD  . PRO   A 1 268 ? -32.194 -7.648  -9.276  1.00 13.42 ?  1305 PRO   A CD  1 
ATOM   2032 N N   . GLU   A 1 269 ? -35.765 -5.493  -7.125  1.00 20.69 ?  1306 GLU   A N   1 
ATOM   2033 C CA  . GLU   A 1 269 ? -36.558 -4.269  -7.128  1.00 29.93 ?  1306 GLU   A CA  1 
ATOM   2034 C C   . GLU   A 1 269 ? -35.682 -3.022  -7.117  1.00 24.92 ?  1306 GLU   A C   1 
ATOM   2035 O O   . GLU   A 1 269 ? -36.059 -1.994  -7.691  1.00 21.15 ?  1306 GLU   A O   1 
ATOM   2036 C CB  . GLU   A 1 269 ? -37.509 -4.271  -5.927  1.00 28.36 ?  1306 GLU   A CB  1 
ATOM   2037 C CG  . GLU   A 1 269 ? -38.263 -2.968  -5.692  1.00 30.82 ?  1306 GLU   A CG  1 
ATOM   2038 C CD  . GLU   A 1 269 ? -39.435 -2.776  -6.637  1.00 34.25 ?  1306 GLU   A CD  1 
ATOM   2039 O OE1 . GLU   A 1 269 ? -39.646 -3.634  -7.520  1.00 40.34 ?  1306 GLU   A OE1 1 
ATOM   2040 O OE2 . GLU   A 1 269 ? -40.150 -1.763  -6.490  1.00 36.17 -1 1306 GLU   A OE2 1 
ATOM   2041 N N   . TYR   A 1 270 ? -34.509 -3.096  -6.496  1.00 21.33 ?  1307 TYR   A N   1 
ATOM   2042 C CA  . TYR   A 1 270 ? -33.641 -1.941  -6.309  1.00 21.69 ?  1307 TYR   A CA  1 
ATOM   2043 C C   . TYR   A 1 270 ? -32.263 -2.175  -6.913  1.00 19.40 ?  1307 TYR   A C   1 
ATOM   2044 O O   . TYR   A 1 270 ? -31.235 -1.855  -6.314  1.00 21.46 ?  1307 TYR   A O   1 
ATOM   2045 C CB  . TYR   A 1 270 ? -33.535 -1.592  -4.829  1.00 23.88 ?  1307 TYR   A CB  1 
ATOM   2046 C CG  . TYR   A 1 270 ? -34.857 -1.159  -4.251  1.00 24.90 ?  1307 TYR   A CG  1 
ATOM   2047 C CD1 . TYR   A 1 270 ? -35.447 0.034   -4.642  1.00 22.73 ?  1307 TYR   A CD1 1 
ATOM   2048 C CD2 . TYR   A 1 270 ? -35.535 -1.961  -3.346  1.00 18.00 ?  1307 TYR   A CD2 1 
ATOM   2049 C CE1 . TYR   A 1 270 ? -36.661 0.430   -4.125  1.00 23.70 ?  1307 TYR   A CE1 1 
ATOM   2050 C CE2 . TYR   A 1 270 ? -36.753 -1.576  -2.831  1.00 23.09 ?  1307 TYR   A CE2 1 
ATOM   2051 C CZ  . TYR   A 1 270 ? -37.312 -0.379  -3.220  1.00 28.94 ?  1307 TYR   A CZ  1 
ATOM   2052 O OH  . TYR   A 1 270 ? -38.526 0.011   -2.705  1.00 21.47 ?  1307 TYR   A OH  1 
ATOM   2053 N N   . CYS   A 1 271 ? -32.232 -2.739  -8.114  1.00 20.09 ?  1308 CYS   A N   1 
ATOM   2054 C CA  . CYS   A 1 271 ? -31.001 -2.881  -8.874  1.00 19.79 ?  1308 CYS   A CA  1 
ATOM   2055 C C   . CYS   A 1 271 ? -31.120 -2.059  -10.147 1.00 15.97 ?  1308 CYS   A C   1 
ATOM   2056 O O   . CYS   A 1 271 ? -32.025 -2.318  -10.959 1.00 19.24 ?  1308 CYS   A O   1 
ATOM   2057 C CB  . CYS   A 1 271 ? -30.720 -4.342  -9.210  1.00 14.15 ?  1308 CYS   A CB  1 
ATOM   2058 S SG  . CYS   A 1 271 ? -29.438 -4.519  -10.447 1.00 18.22 ?  1308 CYS   A SG  1 
ATOM   2059 N N   . PRO   A 1 272 ? -30.260 -1.066  -10.362 1.00 14.42 ?  1309 PRO   A N   1 
ATOM   2060 C CA  . PRO   A 1 272 ? -30.347 -0.277  -11.594 1.00 18.64 ?  1309 PRO   A CA  1 
ATOM   2061 C C   . PRO   A 1 272 ? -30.177 -1.156  -12.823 1.00 16.84 ?  1309 PRO   A C   1 
ATOM   2062 O O   . PRO   A 1 272 ? -29.397 -2.110  -12.825 1.00 18.07 ?  1309 PRO   A O   1 
ATOM   2063 C CB  . PRO   A 1 272 ? -29.200 0.734   -11.458 1.00 18.51 ?  1309 PRO   A CB  1 
ATOM   2064 C CG  . PRO   A 1 272 ? -28.314 0.195   -10.378 1.00 19.31 ?  1309 PRO   A CG  1 
ATOM   2065 C CD  . PRO   A 1 272 ? -29.198 -0.587  -9.463  1.00 15.37 ?  1309 PRO   A CD  1 
ATOM   2066 N N   . ASP   A 1 273 ? -30.932 -0.824  -13.869 1.00 15.90 ?  1310 ASP   A N   1 
ATOM   2067 C CA  . ASP   A 1 273 ? -30.839 -1.548  -15.135 1.00 12.84 ?  1310 ASP   A CA  1 
ATOM   2068 C C   . ASP   A 1 273 ? -29.418 -1.710  -15.669 1.00 15.66 ?  1310 ASP   A C   1 
ATOM   2069 O O   . ASP   A 1 273 ? -29.099 -2.812  -16.146 1.00 21.92 ?  1310 ASP   A O   1 
ATOM   2070 C CB  . ASP   A 1 273 ? -31.724 -0.861  -16.185 1.00 15.23 ?  1310 ASP   A CB  1 
ATOM   2071 C CG  . ASP   A 1 273 ? -33.204 -1.009  -15.888 1.00 16.71 ?  1310 ASP   A CG  1 
ATOM   2072 O OD1 . ASP   A 1 273 ? -33.560 -1.204  -14.706 1.00 18.87 ?  1310 ASP   A OD1 1 
ATOM   2073 O OD2 . ASP   A 1 273 ? -34.012 -0.932  -16.837 1.00 18.63 -1 1310 ASP   A OD2 1 
ATOM   2074 N N   . PRO   A 1 274 ? -28.532 -0.704  -15.642 1.00 21.57 ?  1311 PRO   A N   1 
ATOM   2075 C CA  . PRO   A 1 274 ? -27.165 -0.960  -16.126 1.00 20.62 ?  1311 PRO   A CA  1 
ATOM   2076 C C   . PRO   A 1 274 ? -26.393 -1.926  -15.247 1.00 18.66 ?  1311 PRO   A C   1 
ATOM   2077 O O   . PRO   A 1 274 ? -25.487 -2.604  -15.745 1.00 18.24 ?  1311 PRO   A O   1 
ATOM   2078 C CB  . PRO   A 1 274 ? -26.516 0.434   -16.149 1.00 19.11 ?  1311 PRO   A CB  1 
ATOM   2079 C CG  . PRO   A 1 274 ? -27.593 1.405   -15.811 1.00 21.66 ?  1311 PRO   A CG  1 
ATOM   2080 C CD  . PRO   A 1 274 ? -28.660 0.662   -15.104 1.00 22.26 ?  1311 PRO   A CD  1 
ATOM   2081 N N   . LEU   A 1 275 ? -26.726 -2.017  -13.958 1.00 17.44 ?  1312 LEU   A N   1 
ATOM   2082 C CA  . LEU   A 1 275 ? -26.080 -2.998  -13.094 1.00 18.58 ?  1312 LEU   A CA  1 
ATOM   2083 C C   . LEU   A 1 275 ? -26.636 -4.397  -13.329 1.00 21.03 ?  1312 LEU   A C   1 
ATOM   2084 O O   . LEU   A 1 275 ? -25.876 -5.372  -13.363 1.00 16.20 ?  1312 LEU   A O   1 
ATOM   2085 C CB  . LEU   A 1 275 ? -26.244 -2.594  -11.629 1.00 13.18 ?  1312 LEU   A CB  1 
ATOM   2086 C CG  . LEU   A 1 275 ? -25.530 -3.481  -10.612 1.00 13.39 ?  1312 LEU   A CG  1 
ATOM   2087 C CD1 . LEU   A 1 275 ? -24.042 -3.546  -10.905 1.00 15.65 ?  1312 LEU   A CD1 1 
ATOM   2088 C CD2 . LEU   A 1 275 ? -25.781 -2.992  -9.199  1.00 13.11 ?  1312 LEU   A CD2 1 
ATOM   2089 N N   . TYR   A 1 276 ? -27.956 -4.516  -13.493 1.00 22.15 ?  1313 TYR   A N   1 
ATOM   2090 C CA  . TYR   A 1 276 ? -28.540 -5.815  -13.806 1.00 18.17 ?  1313 TYR   A CA  1 
ATOM   2091 C C   . TYR   A 1 276 ? -28.091 -6.310  -15.173 1.00 22.25 ?  1313 TYR   A C   1 
ATOM   2092 O O   . TYR   A 1 276 ? -27.972 -7.522  -15.386 1.00 19.68 ?  1313 TYR   A O   1 
ATOM   2093 C CB  . TYR   A 1 276 ? -30.064 -5.741  -13.746 1.00 19.89 ?  1313 TYR   A CB  1 
ATOM   2094 C CG  . TYR   A 1 276 ? -30.748 -7.053  -14.059 1.00 21.55 ?  1313 TYR   A CG  1 
ATOM   2095 C CD1 . TYR   A 1 276 ? -30.609 -8.148  -13.216 1.00 21.04 ?  1313 TYR   A CD1 1 
ATOM   2096 C CD2 . TYR   A 1 276 ? -31.529 -7.196  -15.198 1.00 18.26 ?  1313 TYR   A CD2 1 
ATOM   2097 C CE1 . TYR   A 1 276 ? -31.230 -9.350  -13.500 1.00 18.29 ?  1313 TYR   A CE1 1 
ATOM   2098 C CE2 . TYR   A 1 276 ? -32.155 -8.393  -15.488 1.00 20.45 ?  1313 TYR   A CE2 1 
ATOM   2099 C CZ  . TYR   A 1 276 ? -32.005 -9.465  -14.634 1.00 16.00 ?  1313 TYR   A CZ  1 
ATOM   2100 O OH  . TYR   A 1 276 ? -32.626 -10.659 -14.923 1.00 14.47 ?  1313 TYR   A OH  1 
ATOM   2101 N N   . GLU   A 1 277 ? -27.843 -5.393  -16.110 1.00 18.35 ?  1314 GLU   A N   1 
ATOM   2102 C CA  . GLU   A 1 277 ? -27.289 -5.794  -17.399 1.00 25.34 ?  1314 GLU   A CA  1 
ATOM   2103 C C   . GLU   A 1 277 ? -25.884 -6.360  -17.238 1.00 21.78 ?  1314 GLU   A C   1 
ATOM   2104 O O   . GLU   A 1 277 ? -25.496 -7.287  -17.958 1.00 20.13 ?  1314 GLU   A O   1 
ATOM   2105 C CB  . GLU   A 1 277 ? -27.286 -4.608  -18.362 1.00 21.31 ?  1314 GLU   A CB  1 
ATOM   2106 C CG  . GLU   A 1 277 ? -28.517 -4.530  -19.244 1.00 23.69 ?  1314 GLU   A CG  1 
ATOM   2107 C CD  . GLU   A 1 277 ? -28.481 -5.537  -20.374 1.00 31.38 ?  1314 GLU   A CD  1 
ATOM   2108 O OE1 . GLU   A 1 277 ? -27.367 -5.883  -20.821 1.00 33.86 ?  1314 GLU   A OE1 1 
ATOM   2109 O OE2 . GLU   A 1 277 ? -29.561 -5.980  -20.817 1.00 33.90 -1 1314 GLU   A OE2 1 
ATOM   2110 N N   . VAL   A 1 278 ? -25.108 -5.814  -16.298 1.00 19.14 ?  1315 VAL   A N   1 
ATOM   2111 C CA  . VAL   A 1 278 ? -23.789 -6.368  -16.001 1.00 20.82 ?  1315 VAL   A CA  1 
ATOM   2112 C C   . VAL   A 1 278 ? -23.916 -7.798  -15.489 1.00 20.53 ?  1315 VAL   A C   1 
ATOM   2113 O O   . VAL   A 1 278 ? -23.131 -8.682  -15.851 1.00 18.35 ?  1315 VAL   A O   1 
ATOM   2114 C CB  . VAL   A 1 278 ? -23.054 -5.464  -14.994 1.00 21.08 ?  1315 VAL   A CB  1 
ATOM   2115 C CG1 . VAL   A 1 278 ? -21.792 -6.129  -14.517 1.00 18.88 ?  1315 VAL   A CG1 1 
ATOM   2116 C CG2 . VAL   A 1 278 ? -22.724 -4.125  -15.637 1.00 22.22 ?  1315 VAL   A CG2 1 
ATOM   2117 N N   . MET   A 1 279 ? -24.916 -8.044  -14.650 1.00 17.60 ?  1316 MET   A N   1 
ATOM   2118 C CA  . MET   A 1 279 ? -25.161 -9.377  -14.119 1.00 19.68 ?  1316 MET   A CA  1 
ATOM   2119 C C   . MET   A 1 279 ? -25.403 -10.381 -15.243 1.00 18.31 ?  1316 MET   A C   1 
ATOM   2120 O O   . MET   A 1 279 ? -24.855 -11.491 -15.233 1.00 17.26 ?  1316 MET   A O   1 
ATOM   2121 C CB  . MET   A 1 279 ? -26.359 -9.264  -13.197 1.00 18.29 ?  1316 MET   A CB  1 
ATOM   2122 C CG  . MET   A 1 279 ? -26.031 -8.464  -11.982 1.00 16.90 ?  1316 MET   A CG  1 
ATOM   2123 S SD  . MET   A 1 279 ? -27.495 -8.308  -11.008 1.00 22.61 ?  1316 MET   A SD  1 
ATOM   2124 C CE  . MET   A 1 279 ? -27.567 -10.039 -10.413 1.00 16.78 ?  1316 MET   A CE  1 
ATOM   2125 N N   . LEU   A 1 280 ? -26.193 -9.989  -16.242 1.00 18.98 ?  1317 LEU   A N   1 
ATOM   2126 C CA  . LEU   A 1 280 ? -26.541 -10.907 -17.318 1.00 16.28 ?  1317 LEU   A CA  1 
ATOM   2127 C C   . LEU   A 1 280 ? -25.338 -11.238 -18.188 1.00 17.36 ?  1317 LEU   A C   1 
ATOM   2128 O O   . LEU   A 1 280 ? -25.254 -12.347 -18.725 1.00 18.84 ?  1317 LEU   A O   1 
ATOM   2129 C CB  . LEU   A 1 280 ? -27.666 -10.313 -18.165 1.00 12.73 ?  1317 LEU   A CB  1 
ATOM   2130 C CG  . LEU   A 1 280 ? -29.105 -10.632 -17.745 1.00 19.51 ?  1317 LEU   A CG  1 
ATOM   2131 C CD1 . LEU   A 1 280 ? -29.280 -10.574 -16.235 1.00 21.69 ?  1317 LEU   A CD1 1 
ATOM   2132 C CD2 . LEU   A 1 280 ? -30.079 -9.687  -18.433 1.00 19.30 ?  1317 LEU   A CD2 1 
ATOM   2133 N N   . LYS   A 1 281 ? -24.400 -10.300 -18.336 1.00 18.37 ?  1318 LYS   A N   1 
ATOM   2134 C CA  . LYS   A 1 281 ? -23.209 -10.574 -19.131 1.00 18.44 ?  1318 LYS   A CA  1 
ATOM   2135 C C   . LYS   A 1 281 ? -22.299 -11.571 -18.426 1.00 17.26 ?  1318 LYS   A C   1 
ATOM   2136 O O   . LYS   A 1 281 ? -21.686 -12.429 -19.074 1.00 15.61 ?  1318 LYS   A O   1 
ATOM   2137 C CB  . LYS   A 1 281 ? -22.462 -9.273  -19.421 1.00 20.19 ?  1318 LYS   A CB  1 
ATOM   2138 C CG  . LYS   A 1 281 ? -23.075 -8.447  -20.538 1.00 17.77 ?  1318 LYS   A CG  1 
ATOM   2139 C CD  . LYS   A 1 281 ? -22.516 -7.037  -20.555 1.00 21.82 ?  1318 LYS   A CD  1 
ATOM   2140 C CE  . LYS   A 1 281 ? -23.068 -6.250  -21.728 1.00 20.55 ?  1318 LYS   A CE  1 
ATOM   2141 N NZ  . LYS   A 1 281 ? -22.401 -6.653  -22.996 1.00 20.58 ?  1318 LYS   A NZ  1 
ATOM   2142 N N   . CYS   A 1 282 ? -22.201 -11.473 -17.097 1.00 15.75 ?  1319 CYS   A N   1 
ATOM   2143 C CA  . CYS   A 1 282 ? -21.414 -12.424 -16.323 1.00 16.61 ?  1319 CYS   A CA  1 
ATOM   2144 C C   . CYS   A 1 282 ? -21.986 -13.831 -16.383 1.00 17.30 ?  1319 CYS   A C   1 
ATOM   2145 O O   . CYS   A 1 282 ? -21.252 -14.797 -16.147 1.00 20.72 ?  1319 CYS   A O   1 
ATOM   2146 C CB  . CYS   A 1 282 ? -21.328 -11.970 -14.868 1.00 14.56 ?  1319 CYS   A CB  1 
ATOM   2147 S SG  . CYS   A 1 282 ? -20.647 -10.317 -14.630 1.00 20.00 ?  1319 CYS   A SG  1 
ATOM   2148 N N   . TRP   A 1 283 ? -23.276 -13.964 -16.686 1.00 11.53 ?  1320 TRP   A N   1 
ATOM   2149 C CA  . TRP   A 1 283 ? -23.944 -15.255 -16.771 1.00 12.51 ?  1320 TRP   A CA  1 
ATOM   2150 C C   . TRP   A 1 283 ? -24.113 -15.724 -18.212 1.00 14.27 ?  1320 TRP   A C   1 
ATOM   2151 O O   . TRP   A 1 283 ? -25.021 -16.510 -18.504 1.00 17.48 ?  1320 TRP   A O   1 
ATOM   2152 C CB  . TRP   A 1 283 ? -25.304 -15.196 -16.076 1.00 14.70 ?  1320 TRP   A CB  1 
ATOM   2153 C CG  . TRP   A 1 283 ? -25.257 -14.844 -14.616 1.00 16.29 ?  1320 TRP   A CG  1 
ATOM   2154 C CD1 . TRP   A 1 283 ? -24.278 -15.167 -13.719 1.00 12.09 ?  1320 TRP   A CD1 1 
ATOM   2155 C CD2 . TRP   A 1 283 ? -26.245 -14.110 -13.882 1.00 11.57 ?  1320 TRP   A CD2 1 
ATOM   2156 N NE1 . TRP   A 1 283 ? -24.595 -14.674 -12.475 1.00 11.17 ?  1320 TRP   A NE1 1 
ATOM   2157 C CE2 . TRP   A 1 283 ? -25.801 -14.027 -12.548 1.00 10.82 ?  1320 TRP   A CE2 1 
ATOM   2158 C CE3 . TRP   A 1 283 ? -27.463 -13.516 -14.226 1.00 9.58  ?  1320 TRP   A CE3 1 
ATOM   2159 C CZ2 . TRP   A 1 283 ? -26.526 -13.363 -11.560 1.00 12.36 ?  1320 TRP   A CZ2 1 
ATOM   2160 C CZ3 . TRP   A 1 283 ? -28.183 -12.864 -13.243 1.00 12.48 ?  1320 TRP   A CZ3 1 
ATOM   2161 C CH2 . TRP   A 1 283 ? -27.713 -12.792 -11.927 1.00 12.65 ?  1320 TRP   A CH2 1 
ATOM   2162 N N   . HIS   A 1 284 ? -23.260 -15.260 -19.117 1.00 13.97 ?  1321 HIS   A N   1 
ATOM   2163 C CA  . HIS   A 1 284 ? -23.365 -15.666 -20.514 1.00 18.04 ?  1321 HIS   A CA  1 
ATOM   2164 C C   . HIS   A 1 284 ? -23.038 -17.151 -20.646 1.00 15.48 ?  1321 HIS   A C   1 
ATOM   2165 O O   . HIS   A 1 284 ? -22.058 -17.619 -20.055 1.00 14.47 ?  1321 HIS   A O   1 
ATOM   2166 C CB  . HIS   A 1 284 ? -22.427 -14.834 -21.387 1.00 15.38 ?  1321 HIS   A CB  1 
ATOM   2167 C CG  . HIS   A 1 284 ? -22.706 -14.951 -22.855 1.00 16.97 ?  1321 HIS   A CG  1 
ATOM   2168 N ND1 . HIS   A 1 284 ? -22.627 -16.146 -23.535 1.00 18.60 ?  1321 HIS   A ND1 1 
ATOM   2169 C CD2 . HIS   A 1 284 ? -23.062 -14.020 -23.771 1.00 13.94 ?  1321 HIS   A CD2 1 
ATOM   2170 C CE1 . HIS   A 1 284 ? -22.924 -15.949 -24.807 1.00 16.74 ?  1321 HIS   A CE1 1 
ATOM   2171 N NE2 . HIS   A 1 284 ? -23.191 -14.667 -24.977 1.00 13.24 ?  1321 HIS   A NE2 1 
ATOM   2172 N N   . PRO   A 1 285 ? -23.837 -17.920 -21.392 1.00 22.80 ?  1322 PRO   A N   1 
ATOM   2173 C CA  . PRO   A 1 285 ? -23.565 -19.363 -21.523 1.00 18.43 ?  1322 PRO   A CA  1 
ATOM   2174 C C   . PRO   A 1 285 ? -22.191 -19.691 -22.085 1.00 18.38 ?  1322 PRO   A C   1 
ATOM   2175 O O   . PRO   A 1 285 ? -21.652 -20.760 -21.771 1.00 16.89 ?  1322 PRO   A O   1 
ATOM   2176 C CB  . PRO   A 1 285 ? -24.682 -19.853 -22.459 1.00 16.56 ?  1322 PRO   A CB  1 
ATOM   2177 C CG  . PRO   A 1 285 ? -25.435 -18.625 -22.900 1.00 12.76 ?  1322 PRO   A CG  1 
ATOM   2178 C CD  . PRO   A 1 285 ? -25.169 -17.561 -21.898 1.00 19.32 ?  1322 PRO   A CD  1 
ATOM   2179 N N   . LYS   A 1 286 ? -21.587 -18.805 -22.873 1.00 17.04 ?  1323 LYS   A N   1 
ATOM   2180 C CA  . LYS   A 1 286 ? -20.226 -19.004 -23.365 1.00 13.88 ?  1323 LYS   A CA  1 
ATOM   2181 C C   . LYS   A 1 286 ? -19.256 -18.288 -22.429 1.00 17.85 ?  1323 LYS   A C   1 
ATOM   2182 O O   . LYS   A 1 286 ? -19.274 -17.058 -22.326 1.00 21.31 ?  1323 LYS   A O   1 
ATOM   2183 C CB  . LYS   A 1 286 ? -20.094 -18.500 -24.799 1.00 16.03 ?  1323 LYS   A CB  1 
ATOM   2184 C CG  . LYS   A 1 286 ? -20.961 -19.249 -25.799 1.00 20.38 ?  1323 LYS   A CG  1 
ATOM   2185 N N   . ALA   A 1 287 ? -18.401 -19.064 -21.754 1.00 22.94 ?  1324 ALA   A N   1 
ATOM   2186 C CA  . ALA   A 1 287 ? -17.559 -18.510 -20.696 1.00 20.90 ?  1324 ALA   A CA  1 
ATOM   2187 C C   . ALA   A 1 287 ? -16.577 -17.479 -21.236 1.00 19.93 ?  1324 ALA   A C   1 
ATOM   2188 O O   . ALA   A 1 287 ? -16.316 -16.461 -20.585 1.00 20.10 ?  1324 ALA   A O   1 
ATOM   2189 C CB  . ALA   A 1 287 ? -16.814 -19.636 -19.980 1.00 15.37 ?  1324 ALA   A CB  1 
ATOM   2190 N N   . GLU   A 1 288 ? -16.026 -17.720 -22.426 1.00 20.30 ?  1325 GLU   A N   1 
ATOM   2191 C CA  . GLU   A 1 288 ? -15.063 -16.796 -23.014 1.00 19.61 ?  1325 GLU   A CA  1 
ATOM   2192 C C   . GLU   A 1 288 ? -15.675 -15.450 -23.379 1.00 17.32 ?  1325 GLU   A C   1 
ATOM   2193 O O   . GLU   A 1 288 ? -14.925 -14.500 -23.633 1.00 20.60 ?  1325 GLU   A O   1 
ATOM   2194 C CB  . GLU   A 1 288 ? -14.425 -17.425 -24.254 1.00 19.79 ?  1325 GLU   A CB  1 
ATOM   2195 C CG  . GLU   A 1 288 ? -15.366 -17.561 -25.442 1.00 23.31 ?  1325 GLU   A CG  1 
ATOM   2196 C CD  . GLU   A 1 288 ? -16.337 -18.715 -25.285 1.00 27.49 ?  1325 GLU   A CD  1 
ATOM   2197 O OE1 . GLU   A 1 288 ? -17.096 -18.993 -26.237 1.00 27.23 ?  1325 GLU   A OE1 1 
ATOM   2198 O OE2 . GLU   A 1 288 ? -16.343 -19.340 -24.203 1.00 31.02 -1 1325 GLU   A OE2 1 
ATOM   2199 N N   . MET   A 1 289 ? -17.002 -15.341 -23.411 1.00 17.73 ?  1326 MET   A N   1 
ATOM   2200 C CA  . MET   A 1 289 ? -17.678 -14.099 -23.754 1.00 15.41 ?  1326 MET   A CA  1 
ATOM   2201 C C   . MET   A 1 289 ? -18.206 -13.358 -22.532 1.00 13.91 ?  1326 MET   A C   1 
ATOM   2202 O O   . MET   A 1 289 ? -18.903 -12.350 -22.685 1.00 16.04 ?  1326 MET   A O   1 
ATOM   2203 C CB  . MET   A 1 289 ? -18.815 -14.375 -24.738 1.00 17.08 ?  1326 MET   A CB  1 
ATOM   2204 C CG  . MET   A 1 289 ? -18.377 -14.340 -26.193 1.00 17.79 ?  1326 MET   A CG  1 
ATOM   2205 S SD  . MET   A 1 289 ? -19.651 -14.898 -27.336 1.00 34.57 ?  1326 MET   A SD  1 
ATOM   2206 C CE  . MET   A 1 289 ? -18.648 -15.428 -28.724 1.00 13.38 ?  1326 MET   A CE  1 
ATOM   2207 N N   . ARG   A 1 290 ? -17.894 -13.833 -21.329 1.00 15.89 ?  1327 ARG   A N   1 
ATOM   2208 C CA  . ARG   A 1 290 ? -18.246 -13.107 -20.121 1.00 16.04 ?  1327 ARG   A CA  1 
ATOM   2209 C C   . ARG   A 1 290 ? -17.258 -11.964 -19.887 1.00 21.09 ?  1327 ARG   A C   1 
ATOM   2210 O O   . ARG   A 1 290 ? -16.108 -12.029 -20.331 1.00 18.93 ?  1327 ARG   A O   1 
ATOM   2211 C CB  . ARG   A 1 290 ? -18.245 -14.042 -18.916 1.00 15.58 ?  1327 ARG   A CB  1 
ATOM   2212 C CG  . ARG   A 1 290 ? -19.340 -15.095 -18.927 1.00 14.63 ?  1327 ARG   A CG  1 
ATOM   2213 C CD  . ARG   A 1 290 ? -18.978 -16.237 -17.994 1.00 14.11 ?  1327 ARG   A CD  1 
ATOM   2214 N NE  . ARG   A 1 290 ? -19.806 -17.418 -18.198 1.00 21.98 ?  1327 ARG   A NE  1 
ATOM   2215 C CZ  . ARG   A 1 290 ? -19.664 -18.552 -17.525 1.00 16.63 ?  1327 ARG   A CZ  1 
ATOM   2216 N NH1 . ARG   A 1 290 ? -18.720 -18.699 -16.611 1.00 16.64 ?  1327 ARG   A NH1 1 
ATOM   2217 N NH2 . ARG   A 1 290 ? -20.484 -19.566 -17.783 1.00 15.98 ?  1327 ARG   A NH2 1 
ATOM   2218 N N   . PRO   A 1 291 ? -17.680 -10.904 -19.197 1.00 18.17 ?  1328 PRO   A N   1 
ATOM   2219 C CA  . PRO   A 1 291 ? -16.769 -9.777  -18.965 1.00 15.81 ?  1328 PRO   A CA  1 
ATOM   2220 C C   . PRO   A 1 291 ? -15.631 -10.161 -18.034 1.00 21.60 ?  1328 PRO   A C   1 
ATOM   2221 O O   . PRO   A 1 291 ? -15.802 -10.949 -17.101 1.00 17.30 ?  1328 PRO   A O   1 
ATOM   2222 C CB  . PRO   A 1 291 ? -17.675 -8.715  -18.332 1.00 17.99 ?  1328 PRO   A CB  1 
ATOM   2223 C CG  . PRO   A 1 291 ? -18.767 -9.496  -17.692 1.00 19.30 ?  1328 PRO   A CG  1 
ATOM   2224 C CD  . PRO   A 1 291 ? -19.009 -10.661 -18.610 1.00 17.46 ?  1328 PRO   A CD  1 
ATOM   2225 N N   . SER   A 1 292 ? -14.458 -9.596  -18.302 1.00 20.48 ?  1329 SER   A N   1 
ATOM   2226 C CA  . SER   A 1 292 ? -13.311 -9.790  -17.434 1.00 15.39 ?  1329 SER   A CA  1 
ATOM   2227 C C   . SER   A 1 292 ? -13.459 -8.948  -16.169 1.00 18.58 ?  1329 SER   A C   1 
ATOM   2228 O O   . SER   A 1 292 ? -14.252 -8.005  -16.107 1.00 16.41 ?  1329 SER   A O   1 
ATOM   2229 C CB  . SER   A 1 292 ? -12.018 -9.429  -18.167 1.00 19.31 ?  1329 SER   A CB  1 
ATOM   2230 O OG  . SER   A 1 292 ? -11.063 -8.877  -17.279 1.00 26.60 ?  1329 SER   A OG  1 
ATOM   2231 N N   . PHE   A 1 293 ? -12.680 -9.306  -15.145 1.00 17.83 ?  1330 PHE   A N   1 
ATOM   2232 C CA  . PHE   A 1 293 ? -12.744 -8.570  -13.888 1.00 18.38 ?  1330 PHE   A CA  1 
ATOM   2233 C C   . PHE   A 1 293 ? -12.181 -7.162  -14.016 1.00 15.30 ?  1330 PHE   A C   1 
ATOM   2234 O O   . PHE   A 1 293 ? -12.551 -6.287  -13.225 1.00 14.94 ?  1330 PHE   A O   1 
ATOM   2235 C CB  . PHE   A 1 293 ? -12.011 -9.338  -12.787 1.00 15.95 ?  1330 PHE   A CB  1 
ATOM   2236 C CG  . PHE   A 1 293 ? -12.829 -10.439 -12.177 1.00 14.51 ?  1330 PHE   A CG  1 
ATOM   2237 C CD1 . PHE   A 1 293 ? -13.900 -10.146 -11.349 1.00 16.11 ?  1330 PHE   A CD1 1 
ATOM   2238 C CD2 . PHE   A 1 293 ? -12.536 -11.766 -12.442 1.00 13.17 ?  1330 PHE   A CD2 1 
ATOM   2239 C CE1 . PHE   A 1 293 ? -14.661 -11.154 -10.791 1.00 16.64 ?  1330 PHE   A CE1 1 
ATOM   2240 C CE2 . PHE   A 1 293 ? -13.295 -12.777 -11.892 1.00 12.96 ?  1330 PHE   A CE2 1 
ATOM   2241 C CZ  . PHE   A 1 293 ? -14.359 -12.471 -11.063 1.00 16.16 ?  1330 PHE   A CZ  1 
ATOM   2242 N N   . SER   A 1 294 ? -11.300 -6.923  -14.990 1.00 12.41 ?  1331 SER   A N   1 
ATOM   2243 C CA  . SER   A 1 294 ? -10.831 -5.568  -15.251 1.00 16.43 ?  1331 SER   A CA  1 
ATOM   2244 C C   . SER   A 1 294 ? -11.845 -4.771  -16.064 1.00 20.75 ?  1331 SER   A C   1 
ATOM   2245 O O   . SER   A 1 294 ? -11.886 -3.540  -15.968 1.00 22.37 ?  1331 SER   A O   1 
ATOM   2246 C CB  . SER   A 1 294 ? -9.484  -5.598  -15.971 1.00 10.28 ?  1331 SER   A CB  1 
ATOM   2247 O OG  . SER   A 1 294 ? -9.637  -6.010  -17.317 1.00 16.59 ?  1331 SER   A OG  1 
ATOM   2248 N N   . GLU   A 1 295 ? -12.652 -5.447  -16.879 1.00 16.06 ?  1332 GLU   A N   1 
ATOM   2249 C CA  . GLU   A 1 295 ? -13.783 -4.781  -17.512 1.00 18.98 ?  1332 GLU   A CA  1 
ATOM   2250 C C   . GLU   A 1 295 ? -14.930 -4.586  -16.532 1.00 17.66 ?  1332 GLU   A C   1 
ATOM   2251 O O   . GLU   A 1 295 ? -15.676 -3.607  -16.640 1.00 17.01 ?  1332 GLU   A O   1 
ATOM   2252 C CB  . GLU   A 1 295 ? -14.256 -5.583  -18.723 1.00 17.01 ?  1332 GLU   A CB  1 
ATOM   2253 C CG  . GLU   A 1 295 ? -13.145 -5.989  -19.671 1.00 14.20 ?  1332 GLU   A CG  1 
ATOM   2254 C CD  . GLU   A 1 295 ? -13.661 -6.751  -20.873 1.00 20.22 ?  1332 GLU   A CD  1 
ATOM   2255 O OE1 . GLU   A 1 295 ? -14.628 -7.525  -20.716 1.00 15.11 ?  1332 GLU   A OE1 1 
ATOM   2256 O OE2 . GLU   A 1 295 ? -13.100 -6.577  -21.974 1.00 20.64 -1 1332 GLU   A OE2 1 
ATOM   2257 N N   . LEU   A 1 296 ? -15.075 -5.502  -15.574 1.00 18.41 ?  1333 LEU   A N   1 
ATOM   2258 C CA  . LEU   A 1 296 ? -16.091 -5.357  -14.538 1.00 17.52 ?  1333 LEU   A CA  1 
ATOM   2259 C C   . LEU   A 1 296 ? -15.815 -4.142  -13.667 1.00 15.39 ?  1333 LEU   A C   1 
ATOM   2260 O O   . LEU   A 1 296 ? -16.730 -3.373  -13.344 1.00 15.46 ?  1333 LEU   A O   1 
ATOM   2261 C CB  . LEU   A 1 296 ? -16.131 -6.625  -13.690 1.00 13.52 ?  1333 LEU   A CB  1 
ATOM   2262 C CG  . LEU   A 1 296 ? -17.091 -7.698  -14.192 1.00 17.36 ?  1333 LEU   A CG  1 
ATOM   2263 C CD1 . LEU   A 1 296 ? -16.983 -8.950  -13.346 1.00 15.29 ?  1333 LEU   A CD1 1 
ATOM   2264 C CD2 . LEU   A 1 296 ? -18.499 -7.159  -14.176 1.00 17.56 ?  1333 LEU   A CD2 1 
ATOM   2265 N N   . VAL   A 1 297 ? -14.556 -3.958  -13.278 1.00 14.51 ?  1334 VAL   A N   1 
ATOM   2266 C CA  . VAL   A 1 297 ? -14.191 -2.801  -12.480 1.00 18.99 ?  1334 VAL   A CA  1 
ATOM   2267 C C   . VAL   A 1 297 ? -14.387 -1.511  -13.277 1.00 14.68 ?  1334 VAL   A C   1 
ATOM   2268 O O   . VAL   A 1 297 ? -14.644 -0.453  -12.697 1.00 10.56 ?  1334 VAL   A O   1 
ATOM   2269 C CB  . VAL   A 1 297 ? -12.750 -2.983  -11.958 1.00 14.24 ?  1334 VAL   A CB  1 
ATOM   2270 C CG1 . VAL   A 1 297 ? -11.739 -3.012  -13.096 1.00 14.00 ?  1334 VAL   A CG1 1 
ATOM   2271 C CG2 . VAL   A 1 297 ? -12.411 -1.972  -10.869 1.00 17.87 ?  1334 VAL   A CG2 1 
ATOM   2272 N N   . SER   A 1 298 ? -14.328 -1.564  -14.607 1.00 13.34 ?  1335 SER   A N   1 
ATOM   2273 C CA  . SER   A 1 298 ? -14.596 -0.345  -15.363 1.00 14.97 ?  1335 SER   A CA  1 
ATOM   2274 C C   . SER   A 1 298 ? -16.084 -0.021  -15.364 1.00 18.10 ?  1335 SER   A C   1 
ATOM   2275 O O   . SER   A 1 298 ? -16.474 1.134   -15.163 1.00 15.97 ?  1335 SER   A O   1 
ATOM   2276 C CB  . SER   A 1 298 ? -14.060 -0.467  -16.786 1.00 18.87 ?  1335 SER   A CB  1 
ATOM   2277 O OG  . SER   A 1 298 ? -12.706 -0.869  -16.749 1.00 27.63 ?  1335 SER   A OG  1 
ATOM   2278 N N   . ARG   A 1 299 ? -16.933 -1.038  -15.538 1.00 15.03 ?  1336 ARG   A N   1 
ATOM   2279 C CA  . ARG   A 1 299 ? -18.374 -0.812  -15.620 1.00 14.50 ?  1336 ARG   A CA  1 
ATOM   2280 C C   . ARG   A 1 299 ? -18.959 -0.439  -14.262 1.00 14.28 ?  1336 ARG   A C   1 
ATOM   2281 O O   . ARG   A 1 299 ? -19.774 0.486   -14.156 1.00 17.47 ?  1336 ARG   A O   1 
ATOM   2282 C CB  . ARG   A 1 299 ? -19.059 -2.060  -16.174 1.00 16.70 ?  1336 ARG   A CB  1 
ATOM   2283 C CG  . ARG   A 1 299 ? -18.560 -2.474  -17.548 1.00 18.91 ?  1336 ARG   A CG  1 
ATOM   2284 C CD  . ARG   A 1 299 ? -18.938 -3.911  -17.861 1.00 27.72 ?  1336 ARG   A CD  1 
ATOM   2285 N NE  . ARG   A 1 299 ? -18.909 -4.179  -19.293 1.00 31.09 ?  1336 ARG   A NE  1 
ATOM   2286 C CZ  . ARG   A 1 299 ? -19.914 -3.926  -20.119 1.00 32.76 ?  1336 ARG   A CZ  1 
ATOM   2287 N NH1 . ARG   A 1 299 ? -21.050 -3.405  -19.684 1.00 30.59 ?  1336 ARG   A NH1 1 
ATOM   2288 N NH2 . ARG   A 1 299 ? -19.777 -4.203  -21.413 1.00 31.02 ?  1336 ARG   A NH2 1 
ATOM   2289 N N   . ILE   A 1 300 ? -18.556 -1.154  -13.211 1.00 12.31 ?  1337 ILE   A N   1 
ATOM   2290 C CA  . ILE   A 1 300 ? -19.130 -0.924  -11.889 1.00 15.80 ?  1337 ILE   A CA  1 
ATOM   2291 C C   . ILE   A 1 300 ? -18.739 0.453   -11.357 1.00 15.31 ?  1337 ILE   A C   1 
ATOM   2292 O O   . ILE   A 1 300 ? -19.551 1.126   -10.710 1.00 14.72 ?  1337 ILE   A O   1 
ATOM   2293 C CB  . ILE   A 1 300 ? -18.716 -2.052  -10.927 1.00 13.63 ?  1337 ILE   A CB  1 
ATOM   2294 C CG1 . ILE   A 1 300 ? -19.283 -3.390  -11.405 1.00 14.09 ?  1337 ILE   A CG1 1 
ATOM   2295 C CG2 . ILE   A 1 300 ? -19.184 -1.750  -9.508  1.00 13.19 ?  1337 ILE   A CG2 1 
ATOM   2296 C CD1 . ILE   A 1 300 ? -19.256 -4.469  -10.355 1.00 9.30  ?  1337 ILE   A CD1 1 
ATOM   2297 N N   . SER   A 1 301 ? -17.496 0.901   -11.610 1.00 14.88 ?  1338 SER   A N   1 
ATOM   2298 C CA  . SER   A 1 301 ? -17.098 2.241   -11.160 1.00 12.98 ?  1338 SER   A CA  1 
ATOM   2299 C C   . SER   A 1 301 ? -17.933 3.321   -11.802 1.00 13.86 ?  1338 SER   A C   1 
ATOM   2300 O O   . SER   A 1 301 ? -18.287 4.303   -11.142 1.00 12.49 ?  1338 SER   A O   1 
ATOM   2301 C CB  . SER   A 1 301 ? -15.628 2.549   -11.447 1.00 13.28 ?  1338 SER   A CB  1 
ATOM   2302 O OG  . SER   A 1 301 ? -15.330 2.421   -12.826 1.00 15.05 ?  1338 SER   A OG  1 
ATOM   2303 N N   . ALA   A 1 302 ? -18.195 3.197   -13.100 1.00 15.92 ?  1339 ALA   A N   1 
ATOM   2304 C CA  . ALA   A 1 302 ? -19.028 4.185   -13.767 1.00 13.48 ?  1339 ALA   A CA  1 
ATOM   2305 C C   . ALA   A 1 302 ? -20.434 4.186   -13.185 1.00 15.32 ?  1339 ALA   A C   1 
ATOM   2306 O O   . ALA   A 1 302 ? -21.072 5.239   -13.085 1.00 17.38 ?  1339 ALA   A O   1 
ATOM   2307 C CB  . ALA   A 1 302 ? -19.061 3.915   -15.269 1.00 11.59 ?  1339 ALA   A CB  1 
ATOM   2308 N N   . ILE   A 1 303 ? -20.930 3.013   -12.787 1.00 14.62 ?  1340 ILE   A N   1 
ATOM   2309 C CA  . ILE   A 1 303 ? -22.247 2.933   -12.167 1.00 14.26 ?  1340 ILE   A CA  1 
ATOM   2310 C C   . ILE   A 1 303 ? -22.196 3.440   -10.731 1.00 21.00 ?  1340 ILE   A C   1 
ATOM   2311 O O   . ILE   A 1 303 ? -23.163 4.035   -10.238 1.00 22.57 ?  1340 ILE   A O   1 
ATOM   2312 C CB  . ILE   A 1 303 ? -22.772 1.486   -12.247 1.00 12.76 ?  1340 ILE   A CB  1 
ATOM   2313 C CG1 . ILE   A 1 303 ? -22.948 1.066   -13.707 1.00 16.39 ?  1340 ILE   A CG1 1 
ATOM   2314 C CG2 . ILE   A 1 303 ? -24.084 1.336   -11.492 1.00 15.09 ?  1340 ILE   A CG2 1 
ATOM   2315 C CD1 . ILE   A 1 303 ? -23.251 -0.405  -13.886 1.00 12.73 ?  1340 ILE   A CD1 1 
ATOM   2316 N N   . PHE   A 1 304 ? -21.069 3.238   -10.045 1.00 15.61 ?  1341 PHE   A N   1 
ATOM   2317 C CA  . PHE   A 1 304 ? -20.971 3.625   -8.641  1.00 12.68 ?  1341 PHE   A CA  1 
ATOM   2318 C C   . PHE   A 1 304 ? -20.880 5.137   -8.473  1.00 17.72 ?  1341 PHE   A C   1 
ATOM   2319 O O   . PHE   A 1 304 ? -21.394 5.681   -7.489  1.00 19.69 ?  1341 PHE   A O   1 
ATOM   2320 C CB  . PHE   A 1 304 ? -19.766 2.937   -8.000  1.00 13.61 ?  1341 PHE   A CB  1 
ATOM   2321 C CG  . PHE   A 1 304 ? -19.474 3.394   -6.601  1.00 14.07 ?  1341 PHE   A CG  1 
ATOM   2322 C CD1 . PHE   A 1 304 ? -20.319 3.060   -5.557  1.00 9.83  ?  1341 PHE   A CD1 1 
ATOM   2323 C CD2 . PHE   A 1 304 ? -18.344 4.145   -6.326  1.00 14.40 ?  1341 PHE   A CD2 1 
ATOM   2324 C CE1 . PHE   A 1 304 ? -20.047 3.475   -4.269  1.00 8.83  ?  1341 PHE   A CE1 1 
ATOM   2325 C CE2 . PHE   A 1 304 ? -18.068 4.562   -5.039  1.00 10.26 ?  1341 PHE   A CE2 1 
ATOM   2326 C CZ  . PHE   A 1 304 ? -18.921 4.226   -4.009  1.00 12.29 ?  1341 PHE   A CZ  1 
ATOM   2327 N N   . SER   A 1 305 ? -20.235 5.831   -9.414  1.00 14.04 ?  1342 SER   A N   1 
ATOM   2328 C CA  . SER   A 1 305 ? -20.130 7.284   -9.327  1.00 18.30 ?  1342 SER   A CA  1 
ATOM   2329 C C   . SER   A 1 305 ? -21.461 7.948   -9.660  1.00 18.34 ?  1342 SER   A C   1 
ATOM   2330 O O   . SER   A 1 305 ? -22.053 8.640   -8.823  1.00 23.50 ?  1342 SER   A O   1 
ATOM   2331 C CB  . SER   A 1 305 ? -19.028 7.789   -10.261 1.00 15.63 ?  1342 SER   A CB  1 
ATOM   2332 O OG  . SER   A 1 305 ? -17.750 7.362   -9.823  1.00 22.85 ?  1342 SER   A OG  1 
ATOM   2333 N N   . THR   A 1 306 ? -21.951 7.736   -10.879 1.00 16.72 ?  1343 THR   A N   1 
ATOM   2334 C CA  . THR   A 1 306 ? -23.193 8.343   -11.330 1.00 15.28 ?  1343 THR   A CA  1 
ATOM   2335 C C   . THR   A 1 306 ? -24.374 7.866   -10.483 1.00 22.58 ?  1343 THR   A C   1 
ATOM   2336 O O   . THR   A 1 306 ? -24.258 6.975   -9.638  1.00 24.91 ?  1343 THR   A O   1 
ATOM   2337 C CB  . THR   A 1 306 ? -23.446 8.010   -12.799 1.00 16.02 ?  1343 THR   A CB  1 
ATOM   2338 O OG1 . THR   A 1 306 ? -23.823 6.632   -12.915 1.00 17.15 ?  1343 THR   A OG1 1 
ATOM   2339 C CG2 . THR   A 1 306 ? -22.194 8.257   -13.627 1.00 11.14 ?  1343 THR   A CG2 1 
ATOM   2340 N N   . PHE   A 1 307 ? -25.528 8.478   -10.727 1.00 22.43 ?  1344 PHE   A N   1 
ATOM   2341 C CA  . PHE   A 1 307 ? -26.760 8.095   -10.046 1.00 17.86 ?  1344 PHE   A CA  1 
ATOM   2342 C C   . PHE   A 1 307 ? -27.721 7.427   -11.023 1.00 19.39 ?  1344 PHE   A C   1 
ATOM   2343 O O   . PHE   A 1 307 ? -27.686 7.698   -12.224 1.00 21.08 ?  1344 PHE   A O   1 
ATOM   2344 C CB  . PHE   A 1 307 ? -27.423 9.312   -9.400  1.00 21.24 ?  1344 PHE   A CB  1 
ATOM   2345 N N   . PRO   B 1 8   ? -9.308  -10.101 -52.040 1.00 18.58 ?  1045 PRO   B N   1 
ATOM   2346 C CA  . PRO   B 1 8   ? -9.460  -10.194 -53.492 1.00 23.48 ?  1045 PRO   B CA  1 
ATOM   2347 C C   . PRO   B 1 8   ? -10.341 -9.085  -54.046 1.00 21.16 ?  1045 PRO   B C   1 
ATOM   2348 O O   . PRO   B 1 8   ? -10.901 -8.310  -53.273 1.00 16.70 ?  1045 PRO   B O   1 
ATOM   2349 C CB  . PRO   B 1 8   ? -10.125 -11.555 -53.678 1.00 20.42 ?  1045 PRO   B CB  1 
ATOM   2350 C CG  . PRO   B 1 8   ? -10.985 -11.683 -52.470 1.00 16.53 ?  1045 PRO   B CG  1 
ATOM   2351 C CD  . PRO   B 1 8   ? -10.208 -11.036 -51.341 1.00 21.88 ?  1045 PRO   B CD  1 
ATOM   2352 N N   . LEU   B 1 9   ? -10.465 -9.020  -55.373 1.00 19.64 ?  1046 LEU   B N   1 
ATOM   2353 C CA  . LEU   B 1 9   ? -11.347 -8.025  -55.973 1.00 18.42 ?  1046 LEU   B CA  1 
ATOM   2354 C C   . LEU   B 1 9   ? -12.794 -8.244  -55.560 1.00 21.17 ?  1046 LEU   B C   1 
ATOM   2355 O O   . LEU   B 1 9   ? -13.584 -7.293  -55.538 1.00 23.32 ?  1046 LEU   B O   1 
ATOM   2356 C CB  . LEU   B 1 9   ? -11.231 -8.052  -57.496 1.00 18.21 ?  1046 LEU   B CB  1 
ATOM   2357 C CG  . LEU   B 1 9   ? -10.176 -7.157  -58.151 1.00 29.59 ?  1046 LEU   B CG  1 
ATOM   2358 C CD1 . LEU   B 1 9   ? -8.848  -7.140  -57.386 1.00 26.23 ?  1046 LEU   B CD1 1 
ATOM   2359 C CD2 . LEU   B 1 9   ? -9.977  -7.552  -59.600 1.00 23.97 ?  1046 LEU   B CD2 1 
ATOM   2360 N N   . LEU   B 1 10  ? -13.160 -9.484  -55.234 1.00 22.45 ?  1047 LEU   B N   1 
ATOM   2361 C CA  . LEU   B 1 10  ? -14.522 -9.773  -54.803 1.00 19.76 ?  1047 LEU   B CA  1 
ATOM   2362 C C   . LEU   B 1 10  ? -14.808 -9.148  -53.442 1.00 19.24 ?  1047 LEU   B C   1 
ATOM   2363 O O   . LEU   B 1 10  ? -15.729 -8.337  -53.297 1.00 19.12 ?  1047 LEU   B O   1 
ATOM   2364 C CB  . LEU   B 1 10  ? -14.748 -11.284 -54.763 1.00 22.46 ?  1047 LEU   B CB  1 
ATOM   2365 C CG  . LEU   B 1 10  ? -16.172 -11.704 -54.407 1.00 16.68 ?  1047 LEU   B CG  1 
ATOM   2366 C CD1 . LEU   B 1 10  ? -17.147 -11.149 -55.431 1.00 14.96 ?  1047 LEU   B CD1 1 
ATOM   2367 C CD2 . LEU   B 1 10  ? -16.283 -13.216 -54.313 1.00 20.37 ?  1047 LEU   B CD2 1 
ATOM   2368 N N   . GLN   B 1 11  ? -14.021 -9.516  -52.428 1.00 18.69 ?  1048 GLN   B N   1 
ATOM   2369 C CA  . GLN   B 1 11  ? -14.195 -8.945  -51.098 1.00 18.59 ?  1048 GLN   B CA  1 
ATOM   2370 C C   . GLN   B 1 11  ? -13.819 -7.471  -51.035 1.00 16.34 ?  1048 GLN   B C   1 
ATOM   2371 O O   . GLN   B 1 11  ? -14.057 -6.833  -50.004 1.00 13.50 ?  1048 GLN   B O   1 
ATOM   2372 C CB  . GLN   B 1 11  ? -13.373 -9.733  -50.075 1.00 15.32 ?  1048 GLN   B CB  1 
ATOM   2373 C CG  . GLN   B 1 11  ? -13.855 -11.160 -49.855 1.00 17.97 ?  1048 GLN   B CG  1 
ATOM   2374 C CD  . GLN   B 1 11  ? -13.050 -11.896 -48.800 1.00 24.72 ?  1048 GLN   B CD  1 
ATOM   2375 O OE1 . GLN   B 1 11  ? -11.922 -12.321 -49.045 1.00 26.62 ?  1048 GLN   B OE1 1 
ATOM   2376 N NE2 . GLN   B 1 11  ? -13.630 -12.050 -47.616 1.00 29.36 ?  1048 GLN   B NE2 1 
ATOM   2377 N N   . ASN   B 1 12  ? -13.244 -6.917  -52.102 1.00 15.65 ?  1049 ASN   B N   1 
ATOM   2378 C CA  . ASN   B 1 12  ? -12.905 -5.502  -52.141 1.00 14.68 ?  1049 ASN   B CA  1 
ATOM   2379 C C   . ASN   B 1 12  ? -14.063 -4.624  -52.595 1.00 16.39 ?  1049 ASN   B C   1 
ATOM   2380 O O   . ASN   B 1 12  ? -14.095 -3.438  -52.248 1.00 17.70 ?  1049 ASN   B O   1 
ATOM   2381 C CB  . ASN   B 1 12  ? -11.705 -5.273  -53.067 1.00 16.13 ?  1049 ASN   B CB  1 
ATOM   2382 C CG  . ASN   B 1 12  ? -11.252 -3.829  -53.090 1.00 18.67 ?  1049 ASN   B CG  1 
ATOM   2383 O OD1 . ASN   B 1 12  ? -10.770 -3.305  -52.087 1.00 17.78 ?  1049 ASN   B OD1 1 
ATOM   2384 N ND2 . ASN   B 1 12  ? -11.399 -3.180  -54.240 1.00 15.97 ?  1049 ASN   B ND2 1 
ATOM   2385 N N   . THR   B 1 13  ? -15.014 -5.174  -53.353 1.00 15.12 ?  1050 THR   B N   1 
ATOM   2386 C CA  . THR   B 1 13  ? -16.134 -4.377  -53.838 1.00 14.89 ?  1050 THR   B CA  1 
ATOM   2387 C C   . THR   B 1 13  ? -17.134 -4.029  -52.743 1.00 14.94 ?  1050 THR   B C   1 
ATOM   2388 O O   . THR   B 1 13  ? -18.033 -3.220  -52.991 1.00 15.18 ?  1050 THR   B O   1 
ATOM   2389 C CB  . THR   B 1 13  ? -16.847 -5.102  -54.981 1.00 17.29 ?  1050 THR   B CB  1 
ATOM   2390 O OG1 . THR   B 1 13  ? -17.059 -6.474  -54.626 1.00 18.61 ?  1050 THR   B OG1 1 
ATOM   2391 C CG2 . THR   B 1 13  ? -16.013 -5.032  -56.252 1.00 16.19 ?  1050 THR   B CG2 1 
ATOM   2392 N N   . VAL   B 1 14  ? -17.011 -4.619  -51.552 1.00 13.33 ?  1051 VAL   B N   1 
ATOM   2393 C CA  . VAL   B 1 14  ? -17.805 -4.152  -50.419 1.00 13.03 ?  1051 VAL   B CA  1 
ATOM   2394 C C   . VAL   B 1 14  ? -17.400 -2.731  -50.054 1.00 13.77 ?  1051 VAL   B C   1 
ATOM   2395 O O   . VAL   B 1 14  ? -18.240 -1.901  -49.688 1.00 16.18 ?  1051 VAL   B O   1 
ATOM   2396 C CB  . VAL   B 1 14  ? -17.657 -5.111  -49.224 1.00 12.33 ?  1051 VAL   B CB  1 
ATOM   2397 C CG1 . VAL   B 1 14  ? -18.436 -4.595  -48.023 1.00 11.25 ?  1051 VAL   B CG1 1 
ATOM   2398 C CG2 . VAL   B 1 14  ? -18.124 -6.498  -49.608 1.00 11.37 ?  1051 VAL   B CG2 1 
ATOM   2399 N N   . HIS   B 1 15  ? -16.103 -2.428  -50.154 1.00 17.73 ?  1052 HIS   B N   1 
ATOM   2400 C CA  . HIS   B 1 15  ? -15.650 -1.051  -50.007 1.00 14.72 ?  1052 HIS   B CA  1 
ATOM   2401 C C   . HIS   B 1 15  ? -16.212 -0.161  -51.106 1.00 13.57 ?  1052 HIS   B C   1 
ATOM   2402 O O   . HIS   B 1 15  ? -16.448 1.031   -50.883 1.00 18.51 ?  1052 HIS   B O   1 
ATOM   2403 C CB  . HIS   B 1 15  ? -14.122 -0.992  -50.035 1.00 13.74 ?  1052 HIS   B CB  1 
ATOM   2404 C CG  . HIS   B 1 15  ? -13.463 -1.611  -48.843 1.00 11.62 ?  1052 HIS   B CG  1 
ATOM   2405 N ND1 . HIS   B 1 15  ? -12.498 -2.589  -48.953 1.00 15.94 ?  1052 HIS   B ND1 1 
ATOM   2406 C CD2 . HIS   B 1 15  ? -13.617 -1.382  -47.517 1.00 11.55 ?  1052 HIS   B CD2 1 
ATOM   2407 C CE1 . HIS   B 1 15  ? -12.092 -2.942  -47.746 1.00 13.05 ?  1052 HIS   B CE1 1 
ATOM   2408 N NE2 . HIS   B 1 15  ? -12.755 -2.224  -46.858 1.00 11.87 ?  1052 HIS   B NE2 1 
ATOM   2409 N N   . ILE   B 1 16  ? -16.442 -0.723  -52.289 1.00 11.12 ?  1053 ILE   B N   1 
ATOM   2410 C CA  . ILE   B 1 16  ? -16.736 0.073   -53.476 1.00 11.96 ?  1053 ILE   B CA  1 
ATOM   2411 C C   . ILE   B 1 16  ? -18.236 0.256   -53.679 1.00 14.58 ?  1053 ILE   B C   1 
ATOM   2412 O O   . ILE   B 1 16  ? -18.689 1.350   -54.024 1.00 12.12 ?  1053 ILE   B O   1 
ATOM   2413 C CB  . ILE   B 1 16  ? -16.069 -0.579  -54.703 1.00 10.50 ?  1053 ILE   B CB  1 
ATOM   2414 C CG1 . ILE   B 1 16  ? -14.553 -0.636  -54.504 1.00 10.66 ?  1053 ILE   B CG1 1 
ATOM   2415 C CG2 . ILE   B 1 16  ? -16.421 0.176   -55.973 1.00 10.44 ?  1053 ILE   B CG2 1 
ATOM   2416 C CD1 . ILE   B 1 16  ? -13.784 -1.054  -55.736 1.00 8.11  ?  1053 ILE   B CD1 1 
ATOM   2417 N N   . ASP   B 1 17  ? -19.030 -0.794  -53.479 1.00 11.54 ?  1054 ASP   B N   1 
ATOM   2418 C CA  . ASP   B 1 17  ? -20.473 -0.701  -53.646 1.00 10.89 ?  1054 ASP   B CA  1 
ATOM   2419 C C   . ASP   B 1 17  ? -21.221 -0.562  -52.328 1.00 10.14 ?  1054 ASP   B C   1 
ATOM   2420 O O   . ASP   B 1 17  ? -22.441 -0.370  -52.345 1.00 12.80 ?  1054 ASP   B O   1 
ATOM   2421 C CB  . ASP   B 1 17  ? -21.001 -1.922  -54.408 1.00 11.70 ?  1054 ASP   B CB  1 
ATOM   2422 C CG  . ASP   B 1 17  ? -20.658 -1.876  -55.882 1.00 17.47 ?  1054 ASP   B CG  1 
ATOM   2423 O OD1 . ASP   B 1 17  ? -20.539 -0.759  -56.430 1.00 28.59 -1 1054 ASP   B OD1 1 
ATOM   2424 O OD2 . ASP   B 1 17  ? -20.503 -2.953  -56.494 1.00 18.96 ?  1054 ASP   B OD2 1 
ATOM   2425 N N   . LEU   B 1 18  ? -20.527 -0.655  -51.195 1.00 9.73  ?  1055 LEU   B N   1 
ATOM   2426 C CA  . LEU   B 1 18  ? -21.126 -0.430  -49.887 1.00 15.23 ?  1055 LEU   B CA  1 
ATOM   2427 C C   . LEU   B 1 18  ? -20.154 0.381   -49.027 1.00 11.71 ?  1055 LEU   B C   1 
ATOM   2428 O O   . LEU   B 1 18  ? -19.734 -0.026  -47.948 1.00 10.35 ?  1055 LEU   B O   1 
ATOM   2429 C CB  . LEU   B 1 18  ? -21.503 -1.748  -49.214 1.00 11.74 ?  1055 LEU   B CB  1 
ATOM   2430 C CG  . LEU   B 1 18  ? -22.597 -2.591  -49.871 1.00 13.02 ?  1055 LEU   B CG  1 
ATOM   2431 C CD1 . LEU   B 1 18  ? -22.579 -4.008  -49.319 1.00 14.58 ?  1055 LEU   B CD1 1 
ATOM   2432 C CD2 . LEU   B 1 18  ? -23.963 -1.950  -49.673 1.00 9.37  ?  1055 LEU   B CD2 1 
ATOM   2433 N N   . SER   B 1 19  ? -19.790 1.565   -49.520 1.00 15.76 ?  1056 SER   B N   1 
ATOM   2434 C CA  . SER   B 1 19  ? -18.893 2.456   -48.793 1.00 18.20 ?  1056 SER   B CA  1 
ATOM   2435 C C   . SER   B 1 19  ? -19.561 3.129   -47.602 1.00 12.71 ?  1056 SER   B C   1 
ATOM   2436 O O   . SER   B 1 19  ? -18.922 3.964   -46.953 1.00 8.20  ?  1056 SER   B O   1 
ATOM   2437 C CB  . SER   B 1 19  ? -18.334 3.518   -49.741 1.00 10.19 ?  1056 SER   B CB  1 
ATOM   2438 O OG  . SER   B 1 19  ? -19.373 4.136   -50.481 1.00 11.19 ?  1056 SER   B OG  1 
ATOM   2439 N N   . ALA   B 1 20  ? -20.812 2.790   -47.297 1.00 13.70 ?  1057 ALA   B N   1 
ATOM   2440 C CA  . ALA   B 1 20  ? -21.544 3.389   -46.191 1.00 9.96  ?  1057 ALA   B CA  1 
ATOM   2441 C C   . ALA   B 1 20  ? -21.617 2.488   -44.965 1.00 11.24 ?  1057 ALA   B C   1 
ATOM   2442 O O   . ALA   B 1 20  ? -22.290 2.843   -43.992 1.00 12.03 ?  1057 ALA   B O   1 
ATOM   2443 C CB  . ALA   B 1 20  ? -22.959 3.765   -46.642 1.00 10.72 ?  1057 ALA   B CB  1 
ATOM   2444 N N   . LEU   B 1 21  ? -20.951 1.336   -44.988 1.00 13.30 ?  1058 LEU   B N   1 
ATOM   2445 C CA  . LEU   B 1 21  ? -20.907 0.434   -43.845 1.00 10.59 ?  1058 LEU   B CA  1 
ATOM   2446 C C   . LEU   B 1 21  ? -19.673 0.742   -43.012 1.00 8.63  ?  1058 LEU   B C   1 
ATOM   2447 O O   . LEU   B 1 21  ? -18.616 1.065   -43.558 1.00 8.28  ?  1058 LEU   B O   1 
ATOM   2448 C CB  . LEU   B 1 21  ? -20.864 -1.023  -44.308 1.00 14.38 ?  1058 LEU   B CB  1 
ATOM   2449 C CG  . LEU   B 1 21  ? -21.853 -1.439  -45.396 1.00 15.74 ?  1058 LEU   B CG  1 
ATOM   2450 C CD1 . LEU   B 1 21  ? -21.597 -2.868  -45.843 1.00 11.92 ?  1058 LEU   B CD1 1 
ATOM   2451 C CD2 . LEU   B 1 21  ? -23.273 -1.285  -44.915 1.00 14.61 ?  1058 LEU   B CD2 1 
ATOM   2452 N N   . ASN   B 1 22  ? -19.804 0.638   -41.691 1.00 8.24  ?  1059 ASN   B N   1 
ATOM   2453 C CA  . ASN   B 1 22  ? -18.657 0.859   -40.824 1.00 8.53  ?  1059 ASN   B CA  1 
ATOM   2454 C C   . ASN   B 1 22  ? -17.629 -0.258  -41.034 1.00 11.08 ?  1059 ASN   B C   1 
ATOM   2455 O O   . ASN   B 1 22  ? -17.950 -1.297  -41.614 1.00 10.67 ?  1059 ASN   B O   1 
ATOM   2456 C CB  . ASN   B 1 22  ? -19.106 0.962   -39.363 1.00 8.00  ?  1059 ASN   B CB  1 
ATOM   2457 C CG  . ASN   B 1 22  ? -19.912 -0.228  -38.903 1.00 10.87 ?  1059 ASN   B CG  1 
ATOM   2458 O OD1 . ASN   B 1 22  ? -19.863 -1.298  -39.500 1.00 13.73 ?  1059 ASN   B OD1 1 
ATOM   2459 N ND2 . ASN   B 1 22  ? -20.662 -0.046  -37.823 1.00 8.55  ?  1059 ASN   B ND2 1 
ATOM   2460 N N   . PRO   B 1 23  ? -16.374 -0.058  -40.601 1.00 16.01 ?  1060 PRO   B N   1 
ATOM   2461 C CA  . PRO   B 1 23  ? -15.333 -1.047  -40.944 1.00 12.38 ?  1060 PRO   B CA  1 
ATOM   2462 C C   . PRO   B 1 23  ? -15.630 -2.449  -40.445 1.00 15.96 ?  1060 PRO   B C   1 
ATOM   2463 O O   . PRO   B 1 23  ? -15.345 -3.425  -41.151 1.00 13.26 ?  1060 PRO   B O   1 
ATOM   2464 C CB  . PRO   B 1 23  ? -14.069 -0.471  -40.288 1.00 12.73 ?  1060 PRO   B CB  1 
ATOM   2465 C CG  . PRO   B 1 23  ? -14.362 0.964   -40.062 1.00 15.77 ?  1060 PRO   B CG  1 
ATOM   2466 C CD  . PRO   B 1 23  ? -15.824 1.044   -39.789 1.00 12.90 ?  1060 PRO   B CD  1 
ATOM   2467 N N   . GLU   B 1 24  ? -16.194 -2.576  -39.242 1.00 13.62 ?  1061 GLU   B N   1 
ATOM   2468 C CA  . GLU   B 1 24  ? -16.495 -3.894  -38.691 1.00 13.68 ?  1061 GLU   B CA  1 
ATOM   2469 C C   . GLU   B 1 24  ? -17.436 -4.672  -39.601 1.00 16.55 ?  1061 GLU   B C   1 
ATOM   2470 O O   . GLU   B 1 24  ? -17.198 -5.848  -39.900 1.00 22.93 ?  1061 GLU   B O   1 
ATOM   2471 C CB  . GLU   B 1 24  ? -17.100 -3.746  -37.296 1.00 21.19 ?  1061 GLU   B CB  1 
ATOM   2472 C CG  . GLU   B 1 24  ? -17.681 -5.026  -36.733 1.00 28.88 ?  1061 GLU   B CG  1 
ATOM   2473 C CD  . GLU   B 1 24  ? -17.901 -4.952  -35.238 1.00 42.88 ?  1061 GLU   B CD  1 
ATOM   2474 O OE1 . GLU   B 1 24  ? -18.928 -4.381  -34.815 1.00 46.24 ?  1061 GLU   B OE1 1 
ATOM   2475 O OE2 . GLU   B 1 24  ? -17.047 -5.464  -34.485 1.00 59.30 -1 1061 GLU   B OE2 1 
ATOM   2476 N N   . LEU   B 1 25  ? -18.511 -4.026  -40.058 1.00 13.53 ?  1062 LEU   B N   1 
ATOM   2477 C CA  . LEU   B 1 25  ? -19.499 -4.729  -40.866 1.00 17.32 ?  1062 LEU   B CA  1 
ATOM   2478 C C   . LEU   B 1 25  ? -18.980 -5.011  -42.268 1.00 15.36 ?  1062 LEU   B C   1 
ATOM   2479 O O   . LEU   B 1 25  ? -19.409 -5.983  -42.900 1.00 15.25 ?  1062 LEU   B O   1 
ATOM   2480 C CB  . LEU   B 1 25  ? -20.800 -3.933  -40.936 1.00 13.60 ?  1062 LEU   B CB  1 
ATOM   2481 C CG  . LEU   B 1 25  ? -21.938 -4.660  -41.650 1.00 19.73 ?  1062 LEU   B CG  1 
ATOM   2482 C CD1 . LEU   B 1 25  ? -22.856 -5.246  -40.612 1.00 17.14 ?  1062 LEU   B CD1 1 
ATOM   2483 C CD2 . LEU   B 1 25  ? -22.707 -3.737  -42.558 1.00 18.72 ?  1062 LEU   B CD2 1 
ATOM   2484 N N   . VAL   B 1 26  ? -18.065 -4.181  -42.773 1.00 12.31 ?  1063 VAL   B N   1 
ATOM   2485 C CA  . VAL   B 1 26  ? -17.392 -4.520  -44.021 1.00 12.61 ?  1063 VAL   B CA  1 
ATOM   2486 C C   . VAL   B 1 26  ? -16.695 -5.867  -43.883 1.00 14.39 ?  1063 VAL   B C   1 
ATOM   2487 O O   . VAL   B 1 26  ? -16.760 -6.711  -44.782 1.00 16.25 ?  1063 VAL   B O   1 
ATOM   2488 C CB  . VAL   B 1 26  ? -16.410 -3.405  -44.427 1.00 14.44 ?  1063 VAL   B CB  1 
ATOM   2489 C CG1 . VAL   B 1 26  ? -15.649 -3.798  -45.683 1.00 13.62 ?  1063 VAL   B CG1 1 
ATOM   2490 C CG2 . VAL   B 1 26  ? -17.151 -2.095  -44.643 1.00 11.34 ?  1063 VAL   B CG2 1 
ATOM   2491 N N   . GLN   B 1 27  ? -16.053 -6.104  -42.736 1.00 15.09 ?  1064 GLN   B N   1 
ATOM   2492 C CA  . GLN   B 1 27  ? -15.388 -7.378  -42.486 1.00 19.65 ?  1064 GLN   B CA  1 
ATOM   2493 C C   . GLN   B 1 27  ? -16.362 -8.528  -42.262 1.00 14.57 ?  1064 GLN   B C   1 
ATOM   2494 O O   . GLN   B 1 27  ? -15.933 -9.686  -42.303 1.00 12.43 ?  1064 GLN   B O   1 
ATOM   2495 C CB  . GLN   B 1 27  ? -14.448 -7.257  -41.285 1.00 17.03 ?  1064 GLN   B CB  1 
ATOM   2496 N N   . ALA   B 1 28  ? -17.656 -8.253  -42.077 1.00 15.78 ?  1065 ALA   B N   1 
ATOM   2497 C CA  . ALA   B 1 28  ? -18.661 -9.310  -41.988 1.00 15.03 ?  1065 ALA   B CA  1 
ATOM   2498 C C   . ALA   B 1 28  ? -19.288 -9.630  -43.340 1.00 14.49 ?  1065 ALA   B C   1 
ATOM   2499 O O   . ALA   B 1 28  ? -19.594 -10.793 -43.620 1.00 13.79 ?  1065 ALA   B O   1 
ATOM   2500 C CB  . ALA   B 1 28  ? -19.757 -8.924  -40.993 1.00 13.03 ?  1065 ALA   B CB  1 
ATOM   2501 N N   . VAL   B 1 29  ? -19.452 -8.623  -44.202 1.00 17.25 ?  1066 VAL   B N   1 
ATOM   2502 C CA  . VAL   B 1 29  ? -20.078 -8.846  -45.503 1.00 15.42 ?  1066 VAL   B CA  1 
ATOM   2503 C C   . VAL   B 1 29  ? -19.130 -9.591  -46.442 1.00 13.29 ?  1066 VAL   B C   1 
ATOM   2504 O O   . VAL   B 1 29  ? -19.532 -10.547 -47.114 1.00 15.01 ?  1066 VAL   B O   1 
ATOM   2505 C CB  . VAL   B 1 29  ? -20.548 -7.510  -46.110 1.00 15.90 ?  1066 VAL   B CB  1 
ATOM   2506 C CG1 . VAL   B 1 29  ? -21.117 -7.731  -47.500 1.00 14.77 ?  1066 VAL   B CG1 1 
ATOM   2507 C CG2 . VAL   B 1 29  ? -21.592 -6.856  -45.211 1.00 16.60 ?  1066 VAL   B CG2 1 
ATOM   2508 N N   . GLN   B 1 30  ? -17.860 -9.165  -46.503 1.00 13.17 ?  1067 GLN   B N   1 
ATOM   2509 C CA  . GLN   B 1 30  ? -16.873 -9.809  -47.377 1.00 14.76 ?  1067 GLN   B CA  1 
ATOM   2510 C C   . GLN   B 1 30  ? -16.820 -11.319 -47.172 1.00 14.95 ?  1067 GLN   B C   1 
ATOM   2511 O O   . GLN   B 1 30  ? -16.576 -12.069 -48.125 1.00 14.67 ?  1067 GLN   B O   1 
ATOM   2512 C CB  . GLN   B 1 30  ? -15.481 -9.223  -47.114 1.00 11.57 ?  1067 GLN   B CB  1 
ATOM   2513 C CG  . GLN   B 1 30  ? -15.355 -7.716  -47.260 1.00 16.77 ?  1067 GLN   B CG  1 
ATOM   2514 C CD  . GLN   B 1 30  ? -13.995 -7.207  -46.798 1.00 12.36 ?  1067 GLN   B CD  1 
ATOM   2515 O OE1 . GLN   B 1 30  ? -13.707 -7.195  -45.600 1.00 11.18 ?  1067 GLN   B OE1 1 
ATOM   2516 N NE2 . GLN   B 1 30  ? -13.162 -6.775  -47.741 1.00 10.40 ?  1067 GLN   B NE2 1 
ATOM   2517 N N   . HIS   B 1 31  ? -17.024 -11.783 -45.937 1.00 12.44 ?  1068 HIS   B N   1 
ATOM   2518 C CA  . HIS   B 1 31  ? -17.025 -13.209 -45.630 1.00 17.79 ?  1068 HIS   B CA  1 
ATOM   2519 C C   . HIS   B 1 31  ? -18.243 -13.935 -46.179 1.00 17.19 ?  1068 HIS   B C   1 
ATOM   2520 O O   . HIS   B 1 31  ? -18.350 -15.149 -45.987 1.00 20.40 ?  1068 HIS   B O   1 
ATOM   2521 C CB  . HIS   B 1 31  ? -16.947 -13.418 -44.116 1.00 16.06 ?  1068 HIS   B CB  1 
ATOM   2522 N N   . VAL   B 1 32  ? -19.140 -13.224 -46.866 1.00 12.63 ?  1069 VAL   B N   1 
ATOM   2523 C CA  . VAL   B 1 32  ? -20.417 -13.759 -47.316 1.00 14.25 ?  1069 VAL   B CA  1 
ATOM   2524 C C   . VAL   B 1 32  ? -20.703 -13.411 -48.774 1.00 14.74 ?  1069 VAL   B C   1 
ATOM   2525 O O   . VAL   B 1 32  ? -21.648 -13.944 -49.361 1.00 13.31 ?  1069 VAL   B O   1 
ATOM   2526 C CB  . VAL   B 1 32  ? -21.539 -13.249 -46.374 1.00 13.81 ?  1069 VAL   B CB  1 
ATOM   2527 C CG1 . VAL   B 1 32  ? -22.938 -13.289 -46.966 1.00 16.37 ?  1069 VAL   B CG1 1 
ATOM   2528 C CG2 . VAL   B 1 32  ? -21.498 -14.011 -45.054 1.00 12.45 ?  1069 VAL   B CG2 1 
ATOM   2529 N N   . VAL   B 1 33  ? -19.844 -12.610 -49.407 1.00 15.68 ?  1070 VAL   B N   1 
ATOM   2530 C CA  . VAL   B 1 33  ? -20.120 -12.072 -50.735 1.00 14.90 ?  1070 VAL   B CA  1 
ATOM   2531 C C   . VAL   B 1 33  ? -20.071 -13.175 -51.785 1.00 15.71 ?  1070 VAL   B C   1 
ATOM   2532 O O   . VAL   B 1 33  ? -19.134 -13.983 -51.823 1.00 18.99 ?  1070 VAL   B O   1 
ATOM   2533 C CB  . VAL   B 1 33  ? -19.121 -10.955 -51.066 1.00 15.25 ?  1070 VAL   B CB  1 
ATOM   2534 C CG1 . VAL   B 1 33  ? -19.259 -10.525 -52.518 1.00 19.31 ?  1070 VAL   B CG1 1 
ATOM   2535 C CG2 . VAL   B 1 33  ? -19.337 -9.780  -50.145 1.00 16.11 ?  1070 VAL   B CG2 1 
ATOM   2536 N N   . ILE   B 1 34  ? -21.088 -13.198 -52.661 1.00 15.67 ?  1071 ILE   B N   1 
ATOM   2537 C CA  . ILE   B 1 34  ? -21.120 -14.052 -53.843 1.00 16.36 ?  1071 ILE   B CA  1 
ATOM   2538 C C   . ILE   B 1 34  ? -20.597 -13.263 -55.035 1.00 21.23 ?  1071 ILE   B C   1 
ATOM   2539 O O   . ILE   B 1 34  ? -20.775 -12.043 -55.128 1.00 18.43 ?  1071 ILE   B O   1 
ATOM   2540 C CB  . ILE   B 1 34  ? -22.548 -14.577 -54.114 1.00 19.85 ?  1071 ILE   B CB  1 
ATOM   2541 C CG1 . ILE   B 1 34  ? -23.103 -15.313 -52.897 1.00 17.04 ?  1071 ILE   B CG1 1 
ATOM   2542 C CG2 . ILE   B 1 34  ? -22.577 -15.493 -55.330 1.00 23.99 ?  1071 ILE   B CG2 1 
ATOM   2543 C CD1 . ILE   B 1 34  ? -24.491 -15.860 -53.123 1.00 14.56 ?  1071 ILE   B CD1 1 
ATOM   2544 N N   . GLY   B 1 35  ? -19.941 -13.960 -55.959 1.00 25.50 ?  1072 GLY   B N   1 
ATOM   2545 C CA  . GLY   B 1 35  ? -19.580 -13.383 -57.231 1.00 25.40 ?  1072 GLY   B CA  1 
ATOM   2546 C C   . GLY   B 1 35  ? -20.684 -13.575 -58.252 1.00 29.94 ?  1072 GLY   B C   1 
ATOM   2547 O O   . GLY   B 1 35  ? -21.272 -14.655 -58.367 1.00 33.01 ?  1072 GLY   B O   1 
ATOM   2548 N N   . PRO   B 1 36  ? -20.998 -12.516 -59.003 1.00 36.91 ?  1073 PRO   B N   1 
ATOM   2549 C CA  . PRO   B 1 36  ? -22.052 -12.619 -60.028 1.00 37.73 ?  1073 PRO   B CA  1 
ATOM   2550 C C   . PRO   B 1 36  ? -21.859 -13.767 -61.005 1.00 35.71 ?  1073 PRO   B C   1 
ATOM   2551 O O   . PRO   B 1 36  ? -22.851 -14.295 -61.526 1.00 31.62 ?  1073 PRO   B O   1 
ATOM   2552 C CB  . PRO   B 1 36  ? -21.989 -11.261 -60.745 1.00 42.61 ?  1073 PRO   B CB  1 
ATOM   2553 C CG  . PRO   B 1 36  ? -20.935 -10.447 -60.039 1.00 31.23 ?  1073 PRO   B CG  1 
ATOM   2554 C CD  . PRO   B 1 36  ? -20.588 -11.126 -58.760 1.00 32.85 ?  1073 PRO   B CD  1 
ATOM   2555 N N   . SER   B 1 37  ? -20.616 -14.177 -61.271 1.00 36.92 ?  1074 SER   B N   1 
ATOM   2556 C CA  . SER   B 1 37  ? -20.384 -15.353 -62.104 1.00 32.63 ?  1074 SER   B CA  1 
ATOM   2557 C C   . SER   B 1 37  ? -20.931 -16.629 -61.479 1.00 34.22 ?  1074 SER   B C   1 
ATOM   2558 O O   . SER   B 1 37  ? -20.986 -17.658 -62.162 1.00 33.60 ?  1074 SER   B O   1 
ATOM   2559 C CB  . SER   B 1 37  ? -18.887 -15.524 -62.376 1.00 35.75 ?  1074 SER   B CB  1 
ATOM   2560 O OG  . SER   B 1 37  ? -18.167 -15.708 -61.169 1.00 35.17 ?  1074 SER   B OG  1 
ATOM   2561 N N   . SER   B 1 38  ? -21.334 -16.589 -60.210 1.00 36.06 ?  1075 SER   B N   1 
ATOM   2562 C CA  . SER   B 1 38  ? -21.811 -17.765 -59.500 1.00 36.12 ?  1075 SER   B CA  1 
ATOM   2563 C C   . SER   B 1 38  ? -23.296 -17.709 -59.168 1.00 36.17 ?  1075 SER   B C   1 
ATOM   2564 O O   . SER   B 1 38  ? -23.809 -18.645 -58.546 1.00 34.04 ?  1075 SER   B O   1 
ATOM   2565 C CB  . SER   B 1 38  ? -21.004 -17.960 -58.211 1.00 30.32 ?  1075 SER   B CB  1 
ATOM   2566 O OG  . SER   B 1 38  ? -21.571 -18.975 -57.402 1.00 35.59 ?  1075 SER   B OG  1 
ATOM   2567 N N   . LEU   B 1 39  ? -24.002 -16.651 -59.563 1.00 31.07 ?  1076 LEU   B N   1 
ATOM   2568 C CA  . LEU   B 1 39  ? -25.420 -16.498 -59.247 1.00 32.20 ?  1076 LEU   B CA  1 
ATOM   2569 C C   . LEU   B 1 39  ? -26.187 -16.202 -60.528 1.00 32.18 ?  1076 LEU   B C   1 
ATOM   2570 O O   . LEU   B 1 39  ? -26.110 -15.090 -61.060 1.00 33.70 ?  1076 LEU   B O   1 
ATOM   2571 C CB  . LEU   B 1 39  ? -25.639 -15.394 -58.214 1.00 27.30 ?  1076 LEU   B CB  1 
ATOM   2572 C CG  . LEU   B 1 39  ? -27.022 -15.366 -57.560 1.00 22.76 ?  1076 LEU   B CG  1 
ATOM   2573 C CD1 . LEU   B 1 39  ? -27.511 -16.775 -57.259 1.00 25.89 ?  1076 LEU   B CD1 1 
ATOM   2574 C CD2 . LEU   B 1 39  ? -27.001 -14.526 -56.300 1.00 20.05 ?  1076 LEU   B CD2 1 
ATOM   2575 N N   . ILE   B 1 40  ? -26.927 -17.194 -61.016 1.00 29.91 ?  1077 ILE   B N   1 
ATOM   2576 C CA  . ILE   B 1 40  ? -27.795 -17.048 -62.178 1.00 30.50 ?  1077 ILE   B CA  1 
ATOM   2577 C C   . ILE   B 1 40  ? -29.200 -16.753 -61.667 1.00 30.19 ?  1077 ILE   B C   1 
ATOM   2578 O O   . ILE   B 1 40  ? -29.897 -17.650 -61.182 1.00 28.27 ?  1077 ILE   B O   1 
ATOM   2579 C CB  . ILE   B 1 40  ? -27.772 -18.301 -63.063 1.00 26.38 ?  1077 ILE   B CB  1 
ATOM   2580 N N   . VAL   B 1 41  ? -29.620 -15.495 -61.774 1.00 28.78 ?  1078 VAL   B N   1 
ATOM   2581 C CA  . VAL   B 1 41  ? -30.897 -15.041 -61.238 1.00 20.59 ?  1078 VAL   B CA  1 
ATOM   2582 C C   . VAL   B 1 41  ? -31.893 -14.917 -62.382 1.00 22.20 ?  1078 VAL   B C   1 
ATOM   2583 O O   . VAL   B 1 41  ? -31.607 -14.270 -63.398 1.00 26.53 ?  1078 VAL   B O   1 
ATOM   2584 C CB  . VAL   B 1 41  ? -30.742 -13.703 -60.495 1.00 23.15 ?  1078 VAL   B CB  1 
ATOM   2585 C CG1 . VAL   B 1 41  ? -32.095 -13.187 -60.038 1.00 23.70 ?  1078 VAL   B CG1 1 
ATOM   2586 C CG2 . VAL   B 1 41  ? -29.798 -13.857 -59.316 1.00 19.30 ?  1078 VAL   B CG2 1 
ATOM   2587 N N   . HIS   B 1 42  ? -33.063 -15.532 -62.216 1.00 19.79 ?  1079 HIS   B N   1 
ATOM   2588 C CA  . HIS   B 1 42  ? -34.125 -15.512 -63.219 1.00 26.24 ?  1079 HIS   B CA  1 
ATOM   2589 C C   . HIS   B 1 42  ? -35.183 -14.514 -62.765 1.00 25.61 ?  1079 HIS   B C   1 
ATOM   2590 O O   . HIS   B 1 42  ? -35.976 -14.797 -61.863 1.00 22.91 ?  1079 HIS   B O   1 
ATOM   2591 C CB  . HIS   B 1 42  ? -34.710 -16.907 -63.410 1.00 32.41 ?  1079 HIS   B CB  1 
ATOM   2592 C CG  . HIS   B 1 42  ? -33.682 -17.992 -63.387 1.00 23.49 ?  1079 HIS   B CG  1 
ATOM   2593 N ND1 . HIS   B 1 42  ? -33.354 -18.683 -62.240 1.00 20.03 ?  1079 HIS   B ND1 1 
ATOM   2594 C CD2 . HIS   B 1 42  ? -32.897 -18.498 -64.367 1.00 25.76 ?  1079 HIS   B CD2 1 
ATOM   2595 C CE1 . HIS   B 1 42  ? -32.414 -19.569 -62.516 1.00 25.78 ?  1079 HIS   B CE1 1 
ATOM   2596 N NE2 . HIS   B 1 42  ? -32.120 -19.478 -63.800 1.00 27.19 ?  1079 HIS   B NE2 1 
ATOM   2597 N N   . PHE   B 1 43  ? -35.190 -13.340 -63.395 1.00 27.30 ?  1080 PHE   B N   1 
ATOM   2598 C CA  . PHE   B 1 43  ? -36.130 -12.291 -63.029 1.00 28.03 ?  1080 PHE   B CA  1 
ATOM   2599 C C   . PHE   B 1 43  ? -37.502 -12.479 -63.659 1.00 28.76 ?  1080 PHE   B C   1 
ATOM   2600 O O   . PHE   B 1 43  ? -38.440 -11.765 -63.286 1.00 28.88 ?  1080 PHE   B O   1 
ATOM   2601 C CB  . PHE   B 1 43  ? -35.553 -10.925 -63.400 1.00 27.21 ?  1080 PHE   B CB  1 
ATOM   2602 C CG  . PHE   B 1 43  ? -34.346 -10.546 -62.589 1.00 24.55 ?  1080 PHE   B CG  1 
ATOM   2603 C CD1 . PHE   B 1 43  ? -34.481 -10.137 -61.274 1.00 32.76 ?  1080 PHE   B CD1 1 
ATOM   2604 C CD2 . PHE   B 1 43  ? -33.076 -10.617 -63.133 1.00 22.32 ?  1080 PHE   B CD2 1 
ATOM   2605 C CE1 . PHE   B 1 43  ? -33.375 -9.795  -60.519 1.00 29.78 ?  1080 PHE   B CE1 1 
ATOM   2606 C CE2 . PHE   B 1 43  ? -31.964 -10.275 -62.382 1.00 20.36 ?  1080 PHE   B CE2 1 
ATOM   2607 C CZ  . PHE   B 1 43  ? -32.116 -9.862  -61.074 1.00 21.66 ?  1080 PHE   B CZ  1 
ATOM   2608 N N   . ASN   B 1 44  ? -37.646 -13.421 -64.593 1.00 26.87 ?  1081 ASN   B N   1 
ATOM   2609 C CA  . ASN   B 1 44  ? -38.967 -13.795 -65.081 1.00 28.33 ?  1081 ASN   B CA  1 
ATOM   2610 C C   . ASN   B 1 44  ? -39.757 -14.595 -64.056 1.00 26.26 ?  1081 ASN   B C   1 
ATOM   2611 O O   . ASN   B 1 44  ? -40.931 -14.895 -64.298 1.00 26.42 ?  1081 ASN   B O   1 
ATOM   2612 C CB  . ASN   B 1 44  ? -38.843 -14.600 -66.375 1.00 27.69 ?  1081 ASN   B CB  1 
ATOM   2613 N N   . GLU   B 1 45  ? -39.147 -14.946 -62.927 1.00 22.15 ?  1082 GLU   B N   1 
ATOM   2614 C CA  . GLU   B 1 45  ? -39.789 -15.741 -61.886 1.00 25.89 ?  1082 GLU   B CA  1 
ATOM   2615 C C   . GLU   B 1 45  ? -39.814 -14.928 -60.599 1.00 22.47 ?  1082 GLU   B C   1 
ATOM   2616 O O   . GLU   B 1 45  ? -38.803 -14.835 -59.897 1.00 23.99 ?  1082 GLU   B O   1 
ATOM   2617 C CB  . GLU   B 1 45  ? -39.060 -17.064 -61.676 1.00 22.28 ?  1082 GLU   B CB  1 
ATOM   2618 C CG  . GLU   B 1 45  ? -39.154 -18.024 -62.842 1.00 23.56 ?  1082 GLU   B CG  1 
ATOM   2619 C CD  . GLU   B 1 45  ? -38.123 -19.129 -62.758 1.00 26.56 ?  1082 GLU   B CD  1 
ATOM   2620 O OE1 . GLU   B 1 45  ? -37.350 -19.299 -63.724 1.00 27.99 ?  1082 GLU   B OE1 1 
ATOM   2621 O OE2 . GLU   B 1 45  ? -38.082 -19.822 -61.720 1.00 23.36 -1 1082 GLU   B OE2 1 
ATOM   2622 N N   . VAL   B 1 46  ? -40.964 -14.344 -60.284 1.00 25.09 ?  1083 VAL   B N   1 
ATOM   2623 C CA  . VAL   B 1 46  ? -41.203 -13.749 -58.976 1.00 25.06 ?  1083 VAL   B CA  1 
ATOM   2624 C C   . VAL   B 1 46  ? -41.945 -14.769 -58.125 1.00 19.47 ?  1083 VAL   B C   1 
ATOM   2625 O O   . VAL   B 1 46  ? -43.012 -15.257 -58.516 1.00 19.61 ?  1083 VAL   B O   1 
ATOM   2626 C CB  . VAL   B 1 46  ? -41.998 -12.438 -59.086 1.00 20.04 ?  1083 VAL   B CB  1 
ATOM   2627 C CG1 . VAL   B 1 46  ? -42.208 -11.841 -57.707 1.00 21.84 ?  1083 VAL   B CG1 1 
ATOM   2628 C CG2 . VAL   B 1 46  ? -41.283 -11.457 -59.999 1.00 17.97 ?  1083 VAL   B CG2 1 
ATOM   2629 N N   . ILE   B 1 47  ? -41.377 -15.101 -56.967 1.00 18.77 ?  1084 ILE   B N   1 
ATOM   2630 C CA  . ILE   B 1 47  ? -41.940 -16.090 -56.058 1.00 19.98 ?  1084 ILE   B CA  1 
ATOM   2631 C C   . ILE   B 1 47  ? -42.249 -15.511 -54.691 1.00 17.54 ?  1084 ILE   B C   1 
ATOM   2632 O O   . ILE   B 1 47  ? -42.821 -16.209 -53.849 1.00 25.49 ?  1084 ILE   B O   1 
ATOM   2633 C CB  . ILE   B 1 47  ? -41.016 -17.317 -55.916 1.00 16.12 ?  1084 ILE   B CB  1 
ATOM   2634 C CG1 . ILE   B 1 47  ? -39.726 -16.933 -55.196 1.00 21.54 ?  1084 ILE   B CG1 1 
ATOM   2635 C CG2 . ILE   B 1 47  ? -40.688 -17.903 -57.283 1.00 16.11 ?  1084 ILE   B CG2 1 
ATOM   2636 C CD1 . ILE   B 1 47  ? -38.663 -18.008 -55.229 1.00 18.50 ?  1084 ILE   B CD1 1 
ATOM   2637 N N   . GLY   B 1 48  ? -41.883 -14.262 -54.441 1.00 14.68 ?  1085 GLY   B N   1 
ATOM   2638 C CA  . GLY   B 1 48  ? -42.214 -13.616 -53.188 1.00 18.52 ?  1085 GLY   B CA  1 
ATOM   2639 C C   . GLY   B 1 48  ? -42.125 -12.118 -53.339 1.00 20.01 ?  1085 GLY   B C   1 
ATOM   2640 O O   . GLY   B 1 48  ? -41.415 -11.606 -54.209 1.00 20.49 ?  1085 GLY   B O   1 
ATOM   2641 N N   . ARG   B 1 49  ? -42.852 -11.407 -52.481 1.00 17.88 ?  1086 ARG   B N   1 
ATOM   2642 C CA  . ARG   B 1 49  ? -42.869 -9.951  -52.515 1.00 16.21 ?  1086 ARG   B CA  1 
ATOM   2643 C C   . ARG   B 1 49  ? -42.979 -9.423  -51.095 1.00 16.66 ?  1086 ARG   B C   1 
ATOM   2644 O O   . ARG   B 1 49  ? -43.937 -9.743  -50.384 1.00 19.41 ?  1086 ARG   B O   1 
ATOM   2645 C CB  . ARG   B 1 49  ? -44.027 -9.423  -53.369 1.00 14.25 ?  1086 ARG   B CB  1 
ATOM   2646 C CG  . ARG   B 1 49  ? -43.739 -9.353  -54.860 1.00 19.25 ?  1086 ARG   B CG  1 
ATOM   2647 C CD  . ARG   B 1 49  ? -45.023 -9.447  -55.667 1.00 23.01 ?  1086 ARG   B CD  1 
ATOM   2648 N NE  . ARG   B 1 49  ? -45.054 -8.483  -56.759 1.00 26.10 ?  1086 ARG   B NE  1 
ATOM   2649 C CZ  . ARG   B 1 49  ? -44.817 -8.779  -58.029 1.00 31.98 ?  1086 ARG   B CZ  1 
ATOM   2650 N NH1 . ARG   B 1 49  ? -44.526 -10.013 -58.409 1.00 29.51 ?  1086 ARG   B NH1 1 
ATOM   2651 N NH2 . ARG   B 1 49  ? -44.875 -7.814  -58.943 1.00 37.64 ?  1086 ARG   B NH2 1 
ATOM   2652 N N   . GLY   B 1 50  ? -41.996 -8.624  -50.685 1.00 14.37 ?  1087 GLY   B N   1 
ATOM   2653 C CA  . GLY   B 1 50  ? -42.056 -7.881  -49.451 1.00 15.94 ?  1087 GLY   B CA  1 
ATOM   2654 C C   . GLY   B 1 50  ? -42.169 -6.391  -49.729 1.00 16.97 ?  1087 GLY   B C   1 
ATOM   2655 O O   . GLY   B 1 50  ? -42.283 -5.944  -50.868 1.00 16.59 ?  1087 GLY   B O   1 
ATOM   2656 N N   . HIS   B 1 51  ? -42.134 -5.618  -48.645 1.00 17.80 ?  1088 HIS   B N   1 
ATOM   2657 C CA  . HIS   B 1 51  ? -42.150 -4.169  -48.793 1.00 18.89 ?  1088 HIS   B CA  1 
ATOM   2658 C C   . HIS   B 1 51  ? -40.851 -3.636  -49.382 1.00 18.72 ?  1088 HIS   B C   1 
ATOM   2659 O O   . HIS   B 1 51  ? -40.841 -2.526  -49.924 1.00 22.03 ?  1088 HIS   B O   1 
ATOM   2660 C CB  . HIS   B 1 51  ? -42.422 -3.499  -47.445 1.00 16.20 ?  1088 HIS   B CB  1 
ATOM   2661 C CG  . HIS   B 1 51  ? -42.662 -2.026  -47.544 1.00 25.20 ?  1088 HIS   B CG  1 
ATOM   2662 N ND1 . HIS   B 1 51  ? -41.913 -1.101  -46.850 1.00 24.27 ?  1088 HIS   B ND1 1 
ATOM   2663 C CD2 . HIS   B 1 51  ? -43.564 -1.316  -48.262 1.00 20.36 ?  1088 HIS   B CD2 1 
ATOM   2664 C CE1 . HIS   B 1 51  ? -42.345 0.115   -47.134 1.00 26.62 ?  1088 HIS   B CE1 1 
ATOM   2665 N NE2 . HIS   B 1 51  ? -43.347 0.012   -47.988 1.00 30.01 ?  1088 HIS   B NE2 1 
ATOM   2666 N N   . PHE   B 1 52  ? -39.763 -4.403  -49.301 1.00 16.48 ?  1089 PHE   B N   1 
ATOM   2667 C CA  . PHE   B 1 52  ? -38.455 -3.947  -49.751 1.00 15.87 ?  1089 PHE   B CA  1 
ATOM   2668 C C   . PHE   B 1 52  ? -38.118 -4.376  -51.173 1.00 13.06 ?  1089 PHE   B C   1 
ATOM   2669 O O   . PHE   B 1 52  ? -37.155 -3.855  -51.745 1.00 13.80 ?  1089 PHE   B O   1 
ATOM   2670 C CB  . PHE   B 1 52  ? -37.366 -4.452  -48.799 1.00 12.21 ?  1089 PHE   B CB  1 
ATOM   2671 C CG  . PHE   B 1 52  ? -37.416 -3.828  -47.434 1.00 10.99 ?  1089 PHE   B CG  1 
ATOM   2672 C CD1 . PHE   B 1 52  ? -37.906 -2.544  -47.263 1.00 15.98 ?  1089 PHE   B CD1 1 
ATOM   2673 C CD2 . PHE   B 1 52  ? -36.974 -4.524  -46.322 1.00 12.10 ?  1089 PHE   B CD2 1 
ATOM   2674 C CE1 . PHE   B 1 52  ? -37.953 -1.966  -46.008 1.00 14.07 ?  1089 PHE   B CE1 1 
ATOM   2675 C CE2 . PHE   B 1 52  ? -37.019 -3.953  -45.064 1.00 10.72 ?  1089 PHE   B CE2 1 
ATOM   2676 C CZ  . PHE   B 1 52  ? -37.509 -2.672  -44.908 1.00 15.73 ?  1089 PHE   B CZ  1 
ATOM   2677 N N   . GLY   B 1 53  ? -38.866 -5.301  -51.752 1.00 15.50 ?  1090 GLY   B N   1 
ATOM   2678 C CA  . GLY   B 1 53  ? -38.598 -5.723  -53.111 1.00 16.63 ?  1090 GLY   B CA  1 
ATOM   2679 C C   . GLY   B 1 53  ? -39.125 -7.117  -53.371 1.00 13.24 ?  1090 GLY   B C   1 
ATOM   2680 O O   . GLY   B 1 53  ? -39.730 -7.756  -52.509 1.00 14.06 ?  1090 GLY   B O   1 
ATOM   2681 N N   . CYS   B 1 54  ? -38.871 -7.576  -54.591 1.00 14.40 ?  1091 CYS   B N   1 
ATOM   2682 C CA  . CYS   B 1 54  ? -39.335 -8.870  -55.060 1.00 16.72 ?  1091 CYS   B CA  1 
ATOM   2683 C C   . CYS   B 1 54  ? -38.353 -9.973  -54.677 1.00 19.61 ?  1091 CYS   B C   1 
ATOM   2684 O O   . CYS   B 1 54  ? -37.163 -9.734  -54.456 1.00 19.55 ?  1091 CYS   B O   1 
ATOM   2685 C CB  . CYS   B 1 54  ? -39.527 -8.851  -56.578 1.00 18.48 ?  1091 CYS   B CB  1 
ATOM   2686 S SG  . CYS   B 1 54  ? -41.145 -8.269  -57.128 1.00 33.88 ?  1091 CYS   B SG  1 
ATOM   2687 N N   . VAL   B 1 55  ? -38.873 -11.195 -54.600 1.00 20.83 ?  1092 VAL   B N   1 
ATOM   2688 C CA  . VAL   B 1 55  ? -38.071 -12.393 -54.383 1.00 18.31 ?  1092 VAL   B CA  1 
ATOM   2689 C C   . VAL   B 1 55  ? -38.105 -13.225 -55.657 1.00 20.09 ?  1092 VAL   B C   1 
ATOM   2690 O O   . VAL   B 1 55  ? -39.145 -13.325 -56.319 1.00 18.38 ?  1092 VAL   B O   1 
ATOM   2691 C CB  . VAL   B 1 55  ? -38.571 -13.204 -53.172 1.00 15.36 ?  1092 VAL   B CB  1 
ATOM   2692 C CG1 . VAL   B 1 55  ? -37.504 -14.184 -52.711 1.00 18.22 ?  1092 VAL   B CG1 1 
ATOM   2693 C CG2 . VAL   B 1 55  ? -38.952 -12.269 -52.033 1.00 18.83 ?  1092 VAL   B CG2 1 
ATOM   2694 N N   . TYR   B 1 56  ? -36.965 -13.817 -56.003 1.00 23.07 ?  1093 TYR   B N   1 
ATOM   2695 C CA  . TYR   B 1 56  ? -36.791 -14.491 -57.281 1.00 25.75 ?  1093 TYR   B CA  1 
ATOM   2696 C C   . TYR   B 1 56  ? -36.248 -15.897 -57.060 1.00 19.14 ?  1093 TYR   B C   1 
ATOM   2697 O O   . TYR   B 1 56  ? -35.673 -16.204 -56.014 1.00 20.81 ?  1093 TYR   B O   1 
ATOM   2698 C CB  . TYR   B 1 56  ? -35.834 -13.706 -58.199 1.00 22.97 ?  1093 TYR   B CB  1 
ATOM   2699 C CG  . TYR   B 1 56  ? -36.319 -12.324 -58.601 1.00 28.18 ?  1093 TYR   B CG  1 
ATOM   2700 C CD1 . TYR   B 1 56  ? -37.107 -12.144 -59.729 1.00 24.40 ?  1093 TYR   B CD1 1 
ATOM   2701 C CD2 . TYR   B 1 56  ? -35.971 -11.198 -57.862 1.00 29.63 ?  1093 TYR   B CD2 1 
ATOM   2702 C CE1 . TYR   B 1 56  ? -37.545 -10.886 -60.106 1.00 23.01 ?  1093 TYR   B CE1 1 
ATOM   2703 C CE2 . TYR   B 1 56  ? -36.406 -9.934  -58.233 1.00 30.17 ?  1093 TYR   B CE2 1 
ATOM   2704 C CZ  . TYR   B 1 56  ? -37.192 -9.786  -59.356 1.00 26.20 ?  1093 TYR   B CZ  1 
ATOM   2705 O OH  . TYR   B 1 56  ? -37.626 -8.535  -59.730 1.00 32.50 ?  1093 TYR   B OH  1 
ATOM   2706 N N   . HIS   B 1 57  ? -36.422 -16.747 -58.072 1.00 22.52 ?  1094 HIS   B N   1 
ATOM   2707 C CA  . HIS   B 1 57  ? -35.915 -18.116 -58.057 1.00 23.75 ?  1094 HIS   B CA  1 
ATOM   2708 C C   . HIS   B 1 57  ? -34.593 -18.162 -58.815 1.00 25.82 ?  1094 HIS   B C   1 
ATOM   2709 O O   . HIS   B 1 57  ? -34.560 -17.930 -60.029 1.00 27.34 ?  1094 HIS   B O   1 
ATOM   2710 C CB  . HIS   B 1 57  ? -36.927 -19.083 -58.676 1.00 19.66 ?  1094 HIS   B CB  1 
ATOM   2711 C CG  . HIS   B 1 57  ? -36.522 -20.526 -58.597 1.00 22.48 ?  1094 HIS   B CG  1 
ATOM   2712 N ND1 . HIS   B 1 57  ? -37.322 -21.549 -59.060 1.00 23.85 ?  1094 HIS   B ND1 1 
ATOM   2713 C CD2 . HIS   B 1 57  ? -35.404 -21.115 -58.109 1.00 19.01 ?  1094 HIS   B CD2 1 
ATOM   2714 C CE1 . HIS   B 1 57  ? -36.717 -22.706 -58.855 1.00 22.16 ?  1094 HIS   B CE1 1 
ATOM   2715 N NE2 . HIS   B 1 57  ? -35.550 -22.470 -58.283 1.00 20.58 ?  1094 HIS   B NE2 1 
ATOM   2716 N N   . GLY   B 1 58  ? -33.508 -18.456 -58.135 1.00 20.34 ?  1095 GLY   B N   1 
ATOM   2717 C CA  . GLY   B 1 58  ? -32.254 -18.607 -58.810 1.00 21.25 ?  1095 GLY   B CA  1 
ATOM   2718 C C   . GLY   B 1 58  ? -31.369 -19.764 -58.465 1.00 22.50 ?  1095 GLY   B C   1 
ATOM   2719 O O   . GLY   B 1 58  ? -31.672 -20.591 -57.628 1.00 22.68 ?  1095 GLY   B O   1 
ATOM   2720 N N   . THR   B 1 59  ? -30.271 -19.841 -59.153 1.00 23.79 ?  1096 THR   B N   1 
ATOM   2721 C CA  . THR   B 1 59  ? -29.314 -20.912 -58.954 1.00 26.29 ?  1096 THR   B CA  1 
ATOM   2722 C C   . THR   B 1 59  ? -27.961 -20.510 -58.451 1.00 25.77 ?  1096 THR   B C   1 
ATOM   2723 O O   . THR   B 1 59  ? -27.217 -19.834 -59.127 1.00 24.56 ?  1096 THR   B O   1 
ATOM   2724 C CB  . THR   B 1 59  ? -29.094 -21.732 -60.228 1.00 25.47 ?  1096 THR   B CB  1 
ATOM   2725 O OG1 . THR   B 1 59  ? -28.311 -21.010 -61.179 1.00 28.40 ?  1096 THR   B OG1 1 
ATOM   2726 C CG2 . THR   B 1 59  ? -30.408 -22.136 -60.865 1.00 28.93 ?  1096 THR   B CG2 1 
ATOM   2727 N N   . LEU   B 1 60  ? -27.667 -20.866 -57.224 1.00 27.56 ?  1097 LEU   B N   1 
ATOM   2728 C CA  . LEU   B 1 60  ? -26.355 -20.661 -56.678 1.00 32.35 ?  1097 LEU   B CA  1 
ATOM   2729 C C   . LEU   B 1 60  ? -25.357 -21.803 -57.074 1.00 29.48 ?  1097 LEU   B C   1 
ATOM   2730 O O   . LEU   B 1 60  ? -25.623 -22.943 -56.854 1.00 25.39 ?  1097 LEU   B O   1 
ATOM   2731 C CB  . LEU   B 1 60  ? -26.463 -20.410 -55.188 1.00 28.24 ?  1097 LEU   B CB  1 
ATOM   2732 C CG  . LEU   B 1 60  ? -25.225 -19.905 -54.465 1.00 30.10 ?  1097 LEU   B CG  1 
ATOM   2733 C CD1 . LEU   B 1 60  ? -24.389 -18.934 -55.262 1.00 29.12 ?  1097 LEU   B CD1 1 
ATOM   2734 C CD2 . LEU   B 1 60  ? -25.670 -19.259 -53.186 1.00 28.50 ?  1097 LEU   B CD2 1 
ATOM   2735 N N   . LEU   B 1 61  ? -24.209 -21.462 -57.643 1.00 29.91 ?  1098 LEU   B N   1 
ATOM   2736 C CA  . LEU   B 1 61  ? -23.204 -22.447 -58.076 1.00 37.69 ?  1098 LEU   B CA  1 
ATOM   2737 C C   . LEU   B 1 61  ? -22.017 -22.564 -57.100 1.00 39.63 ?  1098 LEU   B C   1 
ATOM   2738 O O   . LEU   B 1 61  ? -22.178 -22.232 -55.926 1.00 36.52 ?  1098 LEU   B O   1 
ATOM   2739 C CB  . LEU   B 1 61  ? -22.757 -22.151 -59.510 1.00 36.09 ?  1098 LEU   B CB  1 
ATOM   2740 C CG  . LEU   B 1 61  ? -23.678 -22.271 -60.705 1.00 33.05 ?  1098 LEU   B CG  1 
ATOM   2741 C CD1 . LEU   B 1 61  ? -24.411 -20.976 -61.003 1.00 31.45 ?  1098 LEU   B CD1 1 
ATOM   2742 C CD2 . LEU   B 1 61  ? -22.847 -22.694 -61.899 1.00 32.60 ?  1098 LEU   B CD2 1 
ATOM   2743 N N   . ASP   B 1 62  ? -20.878 -23.120 -57.555 1.00 38.50 ?  1099 ASP   B N   1 
ATOM   2744 C CA  . ASP   B 1 62  ? -19.654 -23.182 -56.694 1.00 43.29 ?  1099 ASP   B CA  1 
ATOM   2745 C C   . ASP   B 1 62  ? -18.385 -22.850 -57.495 1.00 44.99 ?  1099 ASP   B C   1 
ATOM   2746 O O   . ASP   B 1 62  ? -17.685 -21.908 -57.106 1.00 43.93 ?  1099 ASP   B O   1 
ATOM   2747 C CB  . ASP   B 1 62  ? -19.518 -24.495 -55.939 1.00 40.84 ?  1099 ASP   B CB  1 
ATOM   2748 N N   . GLY   B 1 65  ? -18.886 -25.677 -59.190 1.00 43.91 ?  1102 GLY   B N   1 
ATOM   2749 C CA  . GLY   B 1 65  ? -19.620 -25.591 -60.475 1.00 38.54 ?  1102 GLY   B CA  1 
ATOM   2750 C C   . GLY   B 1 65  ? -20.914 -26.341 -60.374 1.00 31.19 ?  1102 GLY   B C   1 
ATOM   2751 O O   . GLY   B 1 65  ? -21.385 -26.784 -61.417 1.00 24.12 ?  1102 GLY   B O   1 
ATOM   2752 N N   . LYS   B 1 66  ? -21.412 -26.485 -59.154 1.00 33.94 ?  1103 LYS   B N   1 
ATOM   2753 C CA  . LYS   B 1 66  ? -22.669 -27.220 -58.879 1.00 39.75 ?  1103 LYS   B CA  1 
ATOM   2754 C C   . LYS   B 1 66  ? -23.807 -26.226 -58.667 1.00 40.36 ?  1103 LYS   B C   1 
ATOM   2755 O O   . LYS   B 1 66  ? -23.585 -25.279 -57.922 1.00 39.53 ?  1103 LYS   B O   1 
ATOM   2756 C CB  . LYS   B 1 66  ? -22.561 -28.040 -57.597 1.00 37.23 ?  1103 LYS   B CB  1 
ATOM   2757 N N   . LYS   B 1 67  ? -24.998 -26.523 -59.156 1.00 34.40 ?  1104 LYS   B N   1 
ATOM   2758 C CA  . LYS   B 1 67  ? -26.115 -25.558 -59.131 1.00 28.77 ?  1104 LYS   B CA  1 
ATOM   2759 C C   . LYS   B 1 67  ? -27.195 -25.814 -58.066 1.00 28.08 ?  1104 LYS   B C   1 
ATOM   2760 O O   . LYS   B 1 67  ? -28.207 -26.393 -58.432 1.00 30.74 ?  1104 LYS   B O   1 
ATOM   2761 C CB  . LYS   B 1 67  ? -26.687 -25.638 -60.548 1.00 25.23 ?  1104 LYS   B CB  1 
ATOM   2762 N N   . ILE   B 1 68  ? -27.018 -25.338 -56.832 1.00 27.46 ?  1105 ILE   B N   1 
ATOM   2763 C CA  . ILE   B 1 68  ? -28.112 -25.392 -55.810 1.00 27.44 ?  1105 ILE   B CA  1 
ATOM   2764 C C   . ILE   B 1 68  ? -29.192 -24.295 -56.042 1.00 24.76 ?  1105 ILE   B C   1 
ATOM   2765 O O   . ILE   B 1 68  ? -28.933 -23.348 -56.795 1.00 21.53 ?  1105 ILE   B O   1 
ATOM   2766 C CB  . ILE   B 1 68  ? -27.544 -25.305 -54.393 1.00 26.11 ?  1105 ILE   B CB  1 
ATOM   2767 N N   . HIS   B 1 69  ? -30.370 -24.437 -55.431 1.00 17.90 ?  1106 HIS   B N   1 
ATOM   2768 C CA  . HIS   B 1 69  ? -31.509 -23.541 -55.592 1.00 18.55 ?  1106 HIS   B CA  1 
ATOM   2769 C C   . HIS   B 1 69  ? -31.727 -22.536 -54.470 1.00 14.75 ?  1106 HIS   B C   1 
ATOM   2770 O O   . HIS   B 1 69  ? -31.841 -22.910 -53.299 1.00 16.27 ?  1106 HIS   B O   1 
ATOM   2771 C CB  . HIS   B 1 69  ? -32.822 -24.325 -55.619 1.00 19.68 ?  1106 HIS   B CB  1 
ATOM   2772 C CG  . HIS   B 1 69  ? -32.976 -25.198 -56.823 1.00 21.41 ?  1106 HIS   B CG  1 
ATOM   2773 N ND1 . HIS   B 1 69  ? -34.030 -25.076 -57.702 1.00 22.95 ?  1106 HIS   B ND1 1 
ATOM   2774 C CD2 . HIS   B 1 69  ? -32.206 -26.205 -57.296 1.00 25.62 ?  1106 HIS   B CD2 1 
ATOM   2775 C CE1 . HIS   B 1 69  ? -33.900 -25.969 -58.667 1.00 19.01 ?  1106 HIS   B CE1 1 
ATOM   2776 N NE2 . HIS   B 1 69  ? -32.804 -26.669 -58.442 1.00 26.42 ?  1106 HIS   B NE2 1 
ATOM   2777 N N   . CYS   B 1 70  ? -31.800 -21.256 -54.834 1.00 16.61 ?  1107 CYS   B N   1 
ATOM   2778 C CA  . CYS   B 1 70  ? -31.925 -20.204 -53.837 1.00 14.72 ?  1107 CYS   B CA  1 
ATOM   2779 C C   . CYS   B 1 70  ? -32.981 -19.167 -54.190 1.00 13.37 ?  1107 CYS   B C   1 
ATOM   2780 O O   . CYS   B 1 70  ? -33.333 -18.985 -55.358 1.00 13.50 ?  1107 CYS   B O   1 
ATOM   2781 C CB  . CYS   B 1 70  ? -30.551 -19.532 -53.756 1.00 13.32 ?  1107 CYS   B CB  1 
ATOM   2782 S SG  . CYS   B 1 70  ? -29.924 -18.957 -55.347 1.00 22.67 ?  1107 CYS   B SG  1 
ATOM   2783 N N   . ALA   B 1 71  ? -33.474 -18.485 -53.159 1.00 12.60 ?  1108 ALA   B N   1 
ATOM   2784 C CA  . ALA   B 1 71  ? -34.358 -17.338 -53.313 1.00 15.01 ?  1108 ALA   B CA  1 
ATOM   2785 C C   . ALA   B 1 71  ? -33.529 -16.066 -53.182 1.00 13.93 ?  1108 ALA   B C   1 
ATOM   2786 O O   . ALA   B 1 71  ? -32.949 -15.804 -52.122 1.00 13.51 ?  1108 ALA   B O   1 
ATOM   2787 C CB  . ALA   B 1 71  ? -35.478 -17.362 -52.273 1.00 17.13 ?  1108 ALA   B CB  1 
ATOM   2788 N N   . VAL   B 1 72  ? -33.471 -15.285 -54.255 1.00 13.98 ?  1109 VAL   B N   1 
ATOM   2789 C CA  . VAL   B 1 72  ? -32.664 -14.072 -54.307 1.00 16.66 ?  1109 VAL   B CA  1 
ATOM   2790 C C   . VAL   B 1 72  ? -33.587 -12.900 -53.993 1.00 16.94 ?  1109 VAL   B C   1 
ATOM   2791 O O   . VAL   B 1 72  ? -34.387 -12.477 -54.833 1.00 13.39 ?  1109 VAL   B O   1 
ATOM   2792 C CB  . VAL   B 1 72  ? -31.973 -13.909 -55.663 1.00 18.70 ?  1109 VAL   B CB  1 
ATOM   2793 C CG1 . VAL   B 1 72  ? -31.112 -12.657 -55.671 1.00 12.80 ?  1109 VAL   B CG1 1 
ATOM   2794 C CG2 . VAL   B 1 72  ? -31.137 -15.140 -55.979 1.00 18.76 ?  1109 VAL   B CG2 1 
ATOM   2795 N N   . LYS   B 1 73  ? -33.472 -12.370 -52.778 1.00 16.04 ?  1110 LYS   B N   1 
ATOM   2796 C CA  . LYS   B 1 73  ? -34.301 -11.262 -52.323 1.00 14.88 ?  1110 LYS   B CA  1 
ATOM   2797 C C   . LYS   B 1 73  ? -33.671 -9.936  -52.733 1.00 17.01 ?  1110 LYS   B C   1 
ATOM   2798 O O   . LYS   B 1 73  ? -32.476 -9.713  -52.510 1.00 15.43 ?  1110 LYS   B O   1 
ATOM   2799 C CB  . LYS   B 1 73  ? -34.480 -11.317 -50.805 1.00 17.47 ?  1110 LYS   B CB  1 
ATOM   2800 C CG  . LYS   B 1 73  ? -35.001 -10.030 -50.183 1.00 16.25 ?  1110 LYS   B CG  1 
ATOM   2801 C CD  . LYS   B 1 73  ? -36.498 -9.877  -50.395 1.00 15.64 ?  1110 LYS   B CD  1 
ATOM   2802 C CE  . LYS   B 1 73  ? -37.046 -8.693  -49.615 1.00 12.34 ?  1110 LYS   B CE  1 
ATOM   2803 N NZ  . LYS   B 1 73  ? -36.985 -8.917  -48.143 1.00 9.83  ?  1110 LYS   B NZ  1 
ATOM   2804 N N   . SER   B 1 74  ? -34.477 -9.061  -53.326 1.00 19.72 ?  1111 SER   B N   1 
ATOM   2805 C CA  . SER   B 1 74  ? -34.034 -7.741  -53.745 1.00 15.69 ?  1111 SER   B CA  1 
ATOM   2806 C C   . SER   B 1 74  ? -34.454 -6.692  -52.722 1.00 16.58 ?  1111 SER   B C   1 
ATOM   2807 O O   . SER   B 1 74  ? -35.461 -6.843  -52.026 1.00 17.81 ?  1111 SER   B O   1 
ATOM   2808 C CB  . SER   B 1 74  ? -34.604 -7.385  -55.120 1.00 17.66 ?  1111 SER   B CB  1 
ATOM   2809 O OG  . SER   B 1 74  ? -34.640 -5.982  -55.310 1.00 17.70 ?  1111 SER   B OG  1 
ATOM   2810 N N   . LEU   B 1 75  ? -33.663 -5.621  -52.637 1.00 18.77 ?  1112 LEU   B N   1 
ATOM   2811 C CA  . LEU   B 1 75  ? -33.923 -4.520  -51.716 1.00 18.55 ?  1112 LEU   B CA  1 
ATOM   2812 C C   . LEU   B 1 75  ? -33.968 -3.186  -52.451 1.00 20.65 ?  1112 LEU   B C   1 
ATOM   2813 O O   . LEU   B 1 75  ? -33.691 -2.139  -51.860 1.00 21.17 ?  1112 LEU   B O   1 
ATOM   2814 C CB  . LEU   B 1 75  ? -32.871 -4.471  -50.607 1.00 19.35 ?  1112 LEU   B CB  1 
ATOM   2815 C CG  . LEU   B 1 75  ? -32.697 -5.680  -49.688 1.00 16.22 ?  1112 LEU   B CG  1 
ATOM   2816 C CD1 . LEU   B 1 75  ? -31.501 -5.467  -48.770 1.00 14.22 ?  1112 LEU   B CD1 1 
ATOM   2817 C CD2 . LEU   B 1 75  ? -33.956 -5.935  -48.876 1.00 16.51 ?  1112 LEU   B CD2 1 
ATOM   2818 N N   . ASN   B 1 76  ? -34.316 -3.204  -53.741 1.00 22.72 ?  1113 ASN   B N   1 
ATOM   2819 C CA  . ASN   B 1 76  ? -34.270 -1.982  -54.538 1.00 21.09 ?  1113 ASN   B CA  1 
ATOM   2820 C C   . ASN   B 1 76  ? -35.294 -0.948  -54.089 1.00 20.03 ?  1113 ASN   B C   1 
ATOM   2821 O O   . ASN   B 1 76  ? -35.113 0.242   -54.366 1.00 25.39 ?  1113 ASN   B O   1 
ATOM   2822 C CB  . ASN   B 1 76  ? -34.465 -2.305  -56.023 1.00 18.89 ?  1113 ASN   B CB  1 
ATOM   2823 C CG  . ASN   B 1 76  ? -35.770 -3.031  -56.302 1.00 27.28 ?  1113 ASN   B CG  1 
ATOM   2824 O OD1 . ASN   B 1 76  ? -36.548 -3.318  -55.392 1.00 31.77 ?  1113 ASN   B OD1 1 
ATOM   2825 N ND2 . ASN   B 1 76  ? -36.016 -3.329  -57.574 1.00 30.42 ?  1113 ASN   B ND2 1 
ATOM   2826 N N   . ARG   B 1 77  ? -36.361 -1.368  -53.403 1.00 21.84 ?  1114 ARG   B N   1 
ATOM   2827 C CA  . ARG   B 1 77  ? -37.317 -0.409  -52.865 1.00 19.56 ?  1114 ARG   B CA  1 
ATOM   2828 C C   . ARG   B 1 77  ? -36.764 0.353   -51.668 1.00 22.37 ?  1114 ARG   B C   1 
ATOM   2829 O O   . ARG   B 1 77  ? -37.426 1.278   -51.186 1.00 19.65 ?  1114 ARG   B O   1 
ATOM   2830 C CB  . ARG   B 1 77  ? -38.621 -1.116  -52.492 1.00 18.57 ?  1114 ARG   B CB  1 
ATOM   2831 C CG  . ARG   B 1 77  ? -39.321 -1.758  -53.683 1.00 20.29 ?  1114 ARG   B CG  1 
ATOM   2832 C CD  . ARG   B 1 77  ? -40.750 -2.164  -53.354 1.00 31.23 ?  1114 ARG   B CD  1 
ATOM   2833 N NE  . ARG   B 1 77  ? -41.272 -1.463  -52.188 1.00 33.97 ?  1114 ARG   B NE  1 
ATOM   2834 C CZ  . ARG   B 1 77  ? -42.226 -0.543  -52.231 1.00 29.08 ?  1114 ARG   B CZ  1 
ATOM   2835 N NH1 . ARG   B 1 77  ? -42.786 -0.181  -53.373 1.00 32.74 ?  1114 ARG   B NH1 1 
ATOM   2836 N NH2 . ARG   B 1 77  ? -42.629 0.027   -51.098 1.00 26.66 ?  1114 ARG   B NH2 1 
ATOM   2837 N N   . ILE   B 1 78  ? -35.584 -0.019  -51.175 1.00 23.79 ?  1115 ILE   B N   1 
ATOM   2838 C CA  . ILE   B 1 78  ? -34.823 0.822   -50.251 1.00 23.88 ?  1115 ILE   B CA  1 
ATOM   2839 C C   . ILE   B 1 78  ? -33.906 1.658   -51.138 1.00 27.74 ?  1115 ILE   B C   1 
ATOM   2840 O O   . ILE   B 1 78  ? -32.793 1.256   -51.479 1.00 24.64 ?  1115 ILE   B O   1 
ATOM   2841 C CB  . ILE   B 1 78  ? -34.051 0.001   -49.221 1.00 18.55 ?  1115 ILE   B CB  1 
ATOM   2842 C CG1 . ILE   B 1 78  ? -34.922 -1.118  -48.656 1.00 14.15 ?  1115 ILE   B CG1 1 
ATOM   2843 C CG2 . ILE   B 1 78  ? -33.582 0.892   -48.086 1.00 17.92 ?  1115 ILE   B CG2 1 
ATOM   2844 C CD1 . ILE   B 1 78  ? -34.254 -1.905  -47.547 1.00 14.88 ?  1115 ILE   B CD1 1 
ATOM   2845 N N   . THR   B 1 79  ? -34.392 2.838   -51.527 1.00 24.76 ?  1116 THR   B N   1 
ATOM   2846 C CA  . THR   B 1 79  ? -33.738 3.602   -52.585 1.00 25.70 ?  1116 THR   B CA  1 
ATOM   2847 C C   . THR   B 1 79  ? -32.375 4.127   -52.146 1.00 28.65 ?  1116 THR   B C   1 
ATOM   2848 O O   . THR   B 1 79  ? -31.367 3.906   -52.828 1.00 30.73 ?  1116 THR   B O   1 
ATOM   2849 C CB  . THR   B 1 79  ? -34.640 4.753   -53.032 1.00 30.83 ?  1116 THR   B CB  1 
ATOM   2850 O OG1 . THR   B 1 79  ? -35.319 5.302   -51.895 1.00 27.30 ?  1116 THR   B OG1 1 
ATOM   2851 C CG2 . THR   B 1 79  ? -35.669 4.260   -54.040 1.00 25.57 ?  1116 THR   B CG2 1 
ATOM   2852 N N   . ASP   B 1 80  ? -32.319 4.827   -51.017 1.00 25.34 ?  1117 ASP   B N   1 
ATOM   2853 C CA  . ASP   B 1 80  ? -31.086 5.477   -50.598 1.00 27.39 ?  1117 ASP   B CA  1 
ATOM   2854 C C   . ASP   B 1 80  ? -30.183 4.505   -49.845 1.00 26.47 ?  1117 ASP   B C   1 
ATOM   2855 O O   . ASP   B 1 80  ? -30.647 3.548   -49.219 1.00 26.51 ?  1117 ASP   B O   1 
ATOM   2856 C CB  . ASP   B 1 80  ? -31.385 6.716   -49.746 1.00 22.89 ?  1117 ASP   B CB  1 
ATOM   2857 C CG  . ASP   B 1 80  ? -31.539 6.401   -48.271 1.00 25.03 ?  1117 ASP   B CG  1 
ATOM   2858 O OD1 . ASP   B 1 80  ? -32.237 5.423   -47.927 1.00 33.92 ?  1117 ASP   B OD1 1 
ATOM   2859 O OD2 . ASP   B 1 80  ? -30.961 7.144   -47.451 1.00 22.46 -1 1117 ASP   B OD2 1 
ATOM   2860 N N   . ILE   B 1 81  ? -28.876 4.770   -49.912 1.00 23.41 ?  1118 ILE   B N   1 
ATOM   2861 C CA  . ILE   B 1 81  ? -27.886 3.797   -49.460 1.00 23.97 ?  1118 ILE   B CA  1 
ATOM   2862 C C   . ILE   B 1 81  ? -27.860 3.704   -47.939 1.00 24.23 ?  1118 ILE   B C   1 
ATOM   2863 O O   . ILE   B 1 81  ? -27.606 2.631   -47.378 1.00 18.54 ?  1118 ILE   B O   1 
ATOM   2864 C CB  . ILE   B 1 81  ? -26.499 4.151   -50.026 1.00 17.67 ?  1118 ILE   B CB  1 
ATOM   2865 N N   . GLY   B 1 82  ? -28.110 4.818   -47.248 1.00 26.14 ?  1119 GLY   B N   1 
ATOM   2866 C CA  . GLY   B 1 82  ? -27.987 4.824   -45.797 1.00 20.37 ?  1119 GLY   B CA  1 
ATOM   2867 C C   . GLY   B 1 82  ? -28.875 3.794   -45.127 1.00 20.88 ?  1119 GLY   B C   1 
ATOM   2868 O O   . GLY   B 1 82  ? -28.429 3.044   -44.254 1.00 17.70 ?  1119 GLY   B O   1 
ATOM   2869 N N   . GLU   B 1 83  ? -30.147 3.741   -45.530 1.00 24.81 ?  1120 GLU   B N   1 
ATOM   2870 C CA  . GLU   B 1 83  ? -31.053 2.737   -44.981 1.00 19.37 ?  1120 GLU   B CA  1 
ATOM   2871 C C   . GLU   B 1 83  ? -30.659 1.336   -45.430 1.00 21.10 ?  1120 GLU   B C   1 
ATOM   2872 O O   . GLU   B 1 83  ? -30.715 0.388   -44.637 1.00 18.81 ?  1120 GLU   B O   1 
ATOM   2873 C CB  . GLU   B 1 83  ? -32.492 3.049   -45.387 1.00 18.14 ?  1120 GLU   B CB  1 
ATOM   2874 N N   . VAL   B 1 84  ? -30.266 1.183   -46.699 1.00 17.26 ?  1121 VAL   B N   1 
ATOM   2875 C CA  . VAL   B 1 84  ? -29.712 -0.089  -47.156 1.00 13.10 ?  1121 VAL   B CA  1 
ATOM   2876 C C   . VAL   B 1 84  ? -28.580 -0.520  -46.237 1.00 18.11 ?  1121 VAL   B C   1 
ATOM   2877 O O   . VAL   B 1 84  ? -28.488 -1.686  -45.838 1.00 20.87 ?  1121 VAL   B O   1 
ATOM   2878 C CB  . VAL   B 1 84  ? -29.234 0.024   -48.617 1.00 15.59 ?  1121 VAL   B CB  1 
ATOM   2879 C CG1 . VAL   B 1 84  ? -28.565 -1.261  -49.058 1.00 19.46 ?  1121 VAL   B CG1 1 
ATOM   2880 C CG2 . VAL   B 1 84  ? -30.387 0.363   -49.538 1.00 18.32 ?  1121 VAL   B CG2 1 
ATOM   2881 N N   . SER   B 1 85  ? -27.720 0.426   -45.860 1.00 18.08 ?  1122 SER   B N   1 
ATOM   2882 C CA  . SER   B 1 85  ? -26.570 0.098   -45.030 1.00 15.77 ?  1122 SER   B CA  1 
ATOM   2883 C C   . SER   B 1 85  ? -26.975 -0.265  -43.607 1.00 16.52 ?  1122 SER   B C   1 
ATOM   2884 O O   . SER   B 1 85  ? -26.274 -1.039  -42.947 1.00 16.36 ?  1122 SER   B O   1 
ATOM   2885 C CB  . SER   B 1 85  ? -25.588 1.267   -45.038 1.00 13.66 ?  1122 SER   B CB  1 
ATOM   2886 O OG  . SER   B 1 85  ? -24.980 1.382   -46.312 1.00 14.43 ?  1122 SER   B OG  1 
ATOM   2887 N N   . GLN   B 1 86  ? -28.104 0.260   -43.124 1.00 15.17 ?  1123 GLN   B N   1 
ATOM   2888 C CA  . GLN   B 1 86  ? -28.550 -0.061  -41.771 1.00 14.86 ?  1123 GLN   B CA  1 
ATOM   2889 C C   . GLN   B 1 86  ? -29.183 -1.445  -41.702 1.00 16.60 ?  1123 GLN   B C   1 
ATOM   2890 O O   . GLN   B 1 86  ? -28.981 -2.174  -40.725 1.00 13.82 ?  1123 GLN   B O   1 
ATOM   2891 C CB  . GLN   B 1 86  ? -29.534 0.997   -41.275 1.00 15.54 ?  1123 GLN   B CB  1 
ATOM   2892 C CG  . GLN   B 1 86  ? -29.896 0.868   -39.805 1.00 16.86 ?  1123 GLN   B CG  1 
ATOM   2893 C CD  . GLN   B 1 86  ? -28.702 1.058   -38.890 1.00 21.87 ?  1123 GLN   B CD  1 
ATOM   2894 O OE1 . GLN   B 1 86  ? -27.739 1.741   -39.240 1.00 29.25 ?  1123 GLN   B OE1 1 
ATOM   2895 N NE2 . GLN   B 1 86  ? -28.761 0.456   -37.709 1.00 16.62 ?  1123 GLN   B NE2 1 
ATOM   2896 N N   . PHE   B 1 87  ? -29.962 -1.812  -42.722 1.00 19.15 ?  1124 PHE   B N   1 
ATOM   2897 C CA  . PHE   B 1 87  ? -30.535 -3.152  -42.791 1.00 16.33 ?  1124 PHE   B CA  1 
ATOM   2898 C C   . PHE   B 1 87  ? -29.449 -4.217  -42.707 1.00 17.62 ?  1124 PHE   B C   1 
ATOM   2899 O O   . PHE   B 1 87  ? -29.557 -5.177  -41.935 1.00 15.76 ?  1124 PHE   B O   1 
ATOM   2900 C CB  . PHE   B 1 87  ? -31.335 -3.303  -44.084 1.00 18.07 ?  1124 PHE   B CB  1 
ATOM   2901 C CG  . PHE   B 1 87  ? -32.246 -4.492  -44.099 1.00 15.85 ?  1124 PHE   B CG  1 
ATOM   2902 C CD1 . PHE   B 1 87  ? -33.454 -4.463  -43.425 1.00 18.86 ?  1124 PHE   B CD1 1 
ATOM   2903 C CD2 . PHE   B 1 87  ? -31.899 -5.637  -44.796 1.00 17.32 ?  1124 PHE   B CD2 1 
ATOM   2904 C CE1 . PHE   B 1 87  ? -34.296 -5.556  -43.441 1.00 18.62 ?  1124 PHE   B CE1 1 
ATOM   2905 C CE2 . PHE   B 1 87  ? -32.737 -6.731  -44.817 1.00 21.01 ?  1124 PHE   B CE2 1 
ATOM   2906 C CZ  . PHE   B 1 87  ? -33.936 -6.691  -44.138 1.00 17.47 ?  1124 PHE   B CZ  1 
ATOM   2907 N N   . LEU   B 1 88  ? -28.390 -4.057  -43.504 1.00 17.37 ?  1125 LEU   B N   1 
ATOM   2908 C CA  . LEU   B 1 88  ? -27.262 -4.981  -43.449 1.00 15.61 ?  1125 LEU   B CA  1 
ATOM   2909 C C   . LEU   B 1 88  ? -26.616 -4.989  -42.067 1.00 13.58 ?  1125 LEU   B C   1 
ATOM   2910 O O   . LEU   B 1 88  ? -26.166 -6.038  -41.593 1.00 13.32 ?  1125 LEU   B O   1 
ATOM   2911 C CB  . LEU   B 1 88  ? -26.239 -4.618  -44.531 1.00 14.66 ?  1125 LEU   B CB  1 
ATOM   2912 C CG  . LEU   B 1 88  ? -26.463 -5.027  -45.997 1.00 16.74 ?  1125 LEU   B CG  1 
ATOM   2913 C CD1 . LEU   B 1 88  ? -27.829 -4.656  -46.576 1.00 18.48 ?  1125 LEU   B CD1 1 
ATOM   2914 C CD2 . LEU   B 1 88  ? -25.347 -4.436  -46.854 1.00 16.72 ?  1125 LEU   B CD2 1 
ATOM   2915 N N   . THR   B 1 89  ? -26.572 -3.834  -41.401 1.00 14.22 ?  1126 THR   B N   1 
ATOM   2916 C CA  . THR   B 1 89  ? -25.988 -3.768  -40.064 1.00 15.25 ?  1126 THR   B CA  1 
ATOM   2917 C C   . THR   B 1 89  ? -26.799 -4.589  -39.068 1.00 12.37 ?  1126 THR   B C   1 
ATOM   2918 O O   . THR   B 1 89  ? -26.243 -5.367  -38.284 1.00 13.11 ?  1126 THR   B O   1 
ATOM   2919 C CB  . THR   B 1 89  ? -25.891 -2.308  -39.614 1.00 18.90 ?  1126 THR   B CB  1 
ATOM   2920 O OG1 . THR   B 1 89  ? -24.872 -1.642  -40.371 1.00 13.54 ?  1126 THR   B OG1 1 
ATOM   2921 C CG2 . THR   B 1 89  ? -25.554 -2.221  -38.135 1.00 14.27 ?  1126 THR   B CG2 1 
ATOM   2922 N N   . GLU   B 1 90  ? -28.125 -4.438  -39.095 1.00 14.31 ?  1127 GLU   B N   1 
ATOM   2923 C CA  . GLU   B 1 90  ? -28.967 -5.120  -38.120 1.00 13.66 ?  1127 GLU   B CA  1 
ATOM   2924 C C   . GLU   B 1 90  ? -29.073 -6.614  -38.399 1.00 17.61 ?  1127 GLU   B C   1 
ATOM   2925 O O   . GLU   B 1 90  ? -29.218 -7.406  -37.461 1.00 19.58 ?  1127 GLU   B O   1 
ATOM   2926 C CB  . GLU   B 1 90  ? -30.364 -4.499  -38.103 1.00 21.00 ?  1127 GLU   B CB  1 
ATOM   2927 C CG  . GLU   B 1 90  ? -30.384 -2.983  -38.032 1.00 17.75 ?  1127 GLU   B CG  1 
ATOM   2928 C CD  . GLU   B 1 90  ? -31.776 -2.436  -37.791 1.00 23.45 ?  1127 GLU   B CD  1 
ATOM   2929 O OE1 . GLU   B 1 90  ? -32.516 -3.027  -36.976 1.00 31.80 ?  1127 GLU   B OE1 1 
ATOM   2930 O OE2 . GLU   B 1 90  ? -32.134 -1.419  -38.421 1.00 31.96 -1 1127 GLU   B OE2 1 
ATOM   2931 N N   . GLY   B 1 91  ? -29.002 -7.019  -39.666 1.00 13.92 ?  1128 GLY   B N   1 
ATOM   2932 C CA  . GLY   B 1 91  ? -29.307 -8.383  -40.047 1.00 15.53 ?  1128 GLY   B CA  1 
ATOM   2933 C C   . GLY   B 1 91  ? -28.168 -9.257  -40.517 1.00 17.18 ?  1128 GLY   B C   1 
ATOM   2934 O O   . GLY   B 1 91  ? -28.422 -10.383 -40.964 1.00 11.97 ?  1128 GLY   B O   1 
ATOM   2935 N N   . ILE   B 1 92  ? -26.918 -8.797  -40.437 1.00 16.42 ?  1129 ILE   B N   1 
ATOM   2936 C CA  . ILE   B 1 92  ? -25.808 -9.623  -40.900 1.00 12.55 ?  1129 ILE   B CA  1 
ATOM   2937 C C   . ILE   B 1 92  ? -25.473 -10.741 -39.920 1.00 12.79 ?  1129 ILE   B C   1 
ATOM   2938 O O   . ILE   B 1 92  ? -24.795 -11.703 -40.300 1.00 14.11 ?  1129 ILE   B O   1 
ATOM   2939 C CB  . ILE   B 1 92  ? -24.557 -8.769  -41.161 1.00 14.63 ?  1129 ILE   B CB  1 
ATOM   2940 C CG1 . ILE   B 1 92  ? -23.656 -9.443  -42.198 1.00 14.89 ?  1129 ILE   B CG1 1 
ATOM   2941 C CG2 . ILE   B 1 92  ? -23.791 -8.546  -39.869 1.00 15.82 ?  1129 ILE   B CG2 1 
ATOM   2942 C CD1 . ILE   B 1 92  ? -24.355 -9.763  -43.500 1.00 14.15 ?  1129 ILE   B CD1 1 
ATOM   2943 N N   . ILE   B 1 93  ? -25.937 -10.649 -38.671 1.00 11.27 ?  1130 ILE   B N   1 
ATOM   2944 C CA  . ILE   B 1 93  ? -25.645 -11.680 -37.683 1.00 10.76 ?  1130 ILE   B CA  1 
ATOM   2945 C C   . ILE   B 1 93  ? -26.321 -13.006 -38.005 1.00 12.67 ?  1130 ILE   B C   1 
ATOM   2946 O O   . ILE   B 1 93  ? -25.990 -14.026 -37.391 1.00 14.46 ?  1130 ILE   B O   1 
ATOM   2947 C CB  . ILE   B 1 93  ? -26.042 -11.189 -36.273 1.00 9.41  ?  1130 ILE   B CB  1 
ATOM   2948 C CG1 . ILE   B 1 93  ? -25.444 -12.091 -35.186 1.00 9.93  ?  1130 ILE   B CG1 1 
ATOM   2949 C CG2 . ILE   B 1 93  ? -27.556 -11.099 -36.141 1.00 14.93 ?  1130 ILE   B CG2 1 
ATOM   2950 C CD1 . ILE   B 1 93  ? -25.727 -11.630 -33.769 1.00 8.69  ?  1130 ILE   B CD1 1 
ATOM   2951 N N   . MET   B 1 94  ? -27.245 -13.035 -38.970 1.00 15.99 ?  1131 MET   B N   1 
ATOM   2952 C CA  . MET   B 1 94  ? -27.833 -14.312 -39.363 1.00 17.20 ?  1131 MET   B CA  1 
ATOM   2953 C C   . MET   B 1 94  ? -26.830 -15.225 -40.062 1.00 18.02 ?  1131 MET   B C   1 
ATOM   2954 O O   . MET   B 1 94  ? -27.153 -16.391 -40.316 1.00 15.16 ?  1131 MET   B O   1 
ATOM   2955 C CB  . MET   B 1 94  ? -29.080 -14.079 -40.233 1.00 15.19 ?  1131 MET   B CB  1 
ATOM   2956 C CG  . MET   B 1 94  ? -28.828 -13.820 -41.706 1.00 14.99 ?  1131 MET   B CG  1 
ATOM   2957 S SD  . MET   B 1 94  ? -30.276 -13.264 -42.630 1.00 23.95 ?  1131 MET   B SD  1 
ATOM   2958 C CE  . MET   B 1 94  ? -31.092 -14.812 -43.005 1.00 15.03 ?  1131 MET   B CE  1 
ATOM   2959 N N   . LYS   B 1 95  ? -25.620 -14.733 -40.358 1.00 13.54 ?  1132 LYS   B N   1 
ATOM   2960 C CA  . LYS   B 1 95  ? -24.543 -15.603 -40.827 1.00 13.70 ?  1132 LYS   B CA  1 
ATOM   2961 C C   . LYS   B 1 95  ? -23.996 -16.472 -39.704 1.00 14.10 ?  1132 LYS   B C   1 
ATOM   2962 O O   . LYS   B 1 95  ? -23.464 -17.558 -39.962 1.00 13.50 ?  1132 LYS   B O   1 
ATOM   2963 C CB  . LYS   B 1 95  ? -23.419 -14.763 -41.444 1.00 13.40 ?  1132 LYS   B CB  1 
ATOM   2964 C CG  . LYS   B 1 95  ? -22.455 -14.170 -40.424 1.00 12.83 ?  1132 LYS   B CG  1 
ATOM   2965 C CD  . LYS   B 1 95  ? -21.209 -13.575 -41.059 1.00 12.77 ?  1132 LYS   B CD  1 
ATOM   2966 C CE  . LYS   B 1 95  ? -20.015 -13.697 -40.122 1.00 10.20 ?  1132 LYS   B CE  1 
ATOM   2967 N NZ  . LYS   B 1 95  ? -20.388 -13.458 -38.698 1.00 22.05 ?  1132 LYS   B NZ  1 
ATOM   2968 N N   . ASP   B 1 96  ? -24.115 -16.017 -38.462 1.00 12.90 ?  1133 ASP   B N   1 
ATOM   2969 C CA  . ASP   B 1 96  ? -23.674 -16.757 -37.289 1.00 11.73 ?  1133 ASP   B CA  1 
ATOM   2970 C C   . ASP   B 1 96  ? -24.580 -17.927 -36.956 1.00 13.92 ?  1133 ASP   B C   1 
ATOM   2971 O O   . ASP   B 1 96  ? -24.385 -18.522 -35.890 1.00 10.82 ?  1133 ASP   B O   1 
ATOM   2972 C CB  . ASP   B 1 96  ? -23.598 -15.816 -36.082 1.00 13.37 ?  1133 ASP   B CB  1 
ATOM   2973 C CG  . ASP   B 1 96  ? -22.542 -14.734 -36.241 1.00 22.37 ?  1133 ASP   B CG  1 
ATOM   2974 O OD1 . ASP   B 1 96  ? -22.158 -14.430 -37.388 1.00 13.84 ?  1133 ASP   B OD1 1 
ATOM   2975 O OD2 . ASP   B 1 96  ? -22.106 -14.174 -35.213 1.00 19.29 -1 1133 ASP   B OD2 1 
ATOM   2976 N N   . PHE   B 1 97  ? -25.549 -18.293 -37.792 1.00 13.34 ?  1134 PHE   B N   1 
ATOM   2977 C CA  . PHE   B 1 97  ? -26.630 -19.179 -37.386 1.00 14.52 ?  1134 PHE   B CA  1 
ATOM   2978 C C   . PHE   B 1 97  ? -26.657 -20.444 -38.233 1.00 12.08 ?  1134 PHE   B C   1 
ATOM   2979 O O   . PHE   B 1 97  ? -26.495 -20.393 -39.457 1.00 16.97 ?  1134 PHE   B O   1 
ATOM   2980 C CB  . PHE   B 1 97  ? -27.974 -18.453 -37.474 1.00 10.21 ?  1134 PHE   B CB  1 
ATOM   2981 C CG  . PHE   B 1 97  ? -28.160 -17.418 -36.406 1.00 15.40 ?  1134 PHE   B CG  1 
ATOM   2982 C CD1 . PHE   B 1 97  ? -27.654 -17.627 -35.136 1.00 11.56 ?  1134 PHE   B CD1 1 
ATOM   2983 C CD2 . PHE   B 1 97  ? -28.823 -16.232 -36.671 1.00 16.88 ?  1134 PHE   B CD2 1 
ATOM   2984 C CE1 . PHE   B 1 97  ? -27.811 -16.678 -34.148 1.00 18.18 ?  1134 PHE   B CE1 1 
ATOM   2985 C CE2 . PHE   B 1 97  ? -28.984 -15.277 -35.684 1.00 15.05 ?  1134 PHE   B CE2 1 
ATOM   2986 C CZ  . PHE   B 1 97  ? -28.477 -15.501 -34.421 1.00 15.34 ?  1134 PHE   B CZ  1 
ATOM   2987 N N   . SER   B 1 98  ? -26.871 -21.577 -37.566 1.00 9.78  ?  1135 SER   B N   1 
ATOM   2988 C CA  . SER   B 1 98  ? -26.939 -22.875 -38.232 1.00 12.95 ?  1135 SER   B CA  1 
ATOM   2989 C C   . SER   B 1 98  ? -27.862 -23.774 -37.420 1.00 11.25 ?  1135 SER   B C   1 
ATOM   2990 O O   . SER   B 1 98  ? -27.522 -24.162 -36.298 1.00 11.45 ?  1135 SER   B O   1 
ATOM   2991 C CB  . SER   B 1 98  ? -25.551 -23.496 -38.371 1.00 11.55 ?  1135 SER   B CB  1 
ATOM   2992 O OG  . SER   B 1 98  ? -25.504 -24.395 -39.464 1.00 15.19 ?  1135 SER   B OG  1 
ATOM   2993 N N   . HIS   B 1 99  ? -29.026 -24.103 -37.990 1.00 10.28 ?  1136 HIS   B N   1 
ATOM   2994 C CA  . HIS   B 1 99  ? -30.012 -24.967 -37.352 1.00 8.44  ?  1136 HIS   B CA  1 
ATOM   2995 C C   . HIS   B 1 99  ? -30.953 -25.467 -38.431 1.00 7.03  ?  1136 HIS   B C   1 
ATOM   2996 O O   . HIS   B 1 99  ? -31.294 -24.695 -39.337 1.00 6.19  ?  1136 HIS   B O   1 
ATOM   2997 C CB  . HIS   B 1 99  ? -30.798 -24.224 -36.268 1.00 8.88  ?  1136 HIS   B CB  1 
ATOM   2998 C CG  . HIS   B 1 99  ? -31.546 -25.118 -35.327 1.00 10.89 ?  1136 HIS   B CG  1 
ATOM   2999 N ND1 . HIS   B 1 99  ? -32.775 -25.662 -35.633 1.00 7.91  ?  1136 HIS   B ND1 1 
ATOM   3000 C CD2 . HIS   B 1 99  ? -31.245 -25.551 -34.080 1.00 10.98 ?  1136 HIS   B CD2 1 
ATOM   3001 C CE1 . HIS   B 1 99  ? -33.196 -26.396 -34.619 1.00 7.63  ?  1136 HIS   B CE1 1 
ATOM   3002 N NE2 . HIS   B 1 99  ? -32.286 -26.345 -33.663 1.00 9.69  ?  1136 HIS   B NE2 1 
ATOM   3003 N N   . PRO   B 1 100 ? -31.383 -26.729 -38.380 1.00 10.06 ?  1137 PRO   B N   1 
ATOM   3004 C CA  . PRO   B 1 100 ? -32.310 -27.218 -39.412 1.00 7.71  ?  1137 PRO   B CA  1 
ATOM   3005 C C   . PRO   B 1 100 ? -33.642 -26.489 -39.414 1.00 6.63  ?  1137 PRO   B C   1 
ATOM   3006 O O   . PRO   B 1 100 ? -34.279 -26.389 -40.470 1.00 7.73  ?  1137 PRO   B O   1 
ATOM   3007 C CB  . PRO   B 1 100 ? -32.472 -28.704 -39.059 1.00 6.06  ?  1137 PRO   B CB  1 
ATOM   3008 C CG  . PRO   B 1 100 ? -32.109 -28.795 -37.611 1.00 8.35  ?  1137 PRO   B CG  1 
ATOM   3009 C CD  . PRO   B 1 100 ? -31.033 -27.775 -37.405 1.00 6.95  ?  1137 PRO   B CD  1 
ATOM   3010 N N   . ASN   B 1 101 ? -34.078 -25.963 -38.270 1.00 7.78  ?  1138 ASN   B N   1 
ATOM   3011 C CA  . ASN   B 1 101 ? -35.347 -25.256 -38.160 1.00 8.03  ?  1138 ASN   B CA  1 
ATOM   3012 C C   . ASN   B 1 101 ? -35.176 -23.740 -38.159 1.00 9.43  ?  1138 ASN   B C   1 
ATOM   3013 O O   . ASN   B 1 101 ? -36.044 -23.023 -37.649 1.00 10.23 ?  1138 ASN   B O   1 
ATOM   3014 C CB  . ASN   B 1 101 ? -36.091 -25.706 -36.903 1.00 8.96  ?  1138 ASN   B CB  1 
ATOM   3015 C CG  . ASN   B 1 101 ? -36.447 -27.181 -36.934 1.00 8.34  ?  1138 ASN   B CG  1 
ATOM   3016 O OD1 . ASN   B 1 101 ? -36.291 -27.889 -35.940 1.00 9.52  ?  1138 ASN   B OD1 1 
ATOM   3017 N ND2 . ASN   B 1 101 ? -36.927 -27.650 -38.079 1.00 6.06  ?  1138 ASN   B ND2 1 
ATOM   3018 N N   . VAL   B 1 102 ? -34.076 -23.241 -38.717 1.00 10.27 ?  1139 VAL   B N   1 
ATOM   3019 C CA  . VAL   B 1 102 ? -33.813 -21.813 -38.838 1.00 12.82 ?  1139 VAL   B CA  1 
ATOM   3020 C C   . VAL   B 1 102 ? -33.433 -21.530 -40.283 1.00 15.04 ?  1139 VAL   B C   1 
ATOM   3021 O O   . VAL   B 1 102 ? -32.633 -22.266 -40.872 1.00 11.45 ?  1139 VAL   B O   1 
ATOM   3022 C CB  . VAL   B 1 102 ? -32.694 -21.352 -37.882 1.00 13.21 ?  1139 VAL   B CB  1 
ATOM   3023 C CG1 . VAL   B 1 102 ? -32.281 -19.918 -38.182 1.00 10.82 ?  1139 VAL   B CG1 1 
ATOM   3024 C CG2 . VAL   B 1 102 ? -33.139 -21.483 -36.433 1.00 10.82 ?  1139 VAL   B CG2 1 
ATOM   3025 N N   . LEU   B 1 103 ? -34.015 -20.481 -40.860 1.00 14.24 ?  1140 LEU   B N   1 
ATOM   3026 C CA  . LEU   B 1 103 ? -33.633 -20.086 -42.208 1.00 14.82 ?  1140 LEU   B CA  1 
ATOM   3027 C C   . LEU   B 1 103 ? -32.181 -19.626 -42.220 1.00 13.91 ?  1140 LEU   B C   1 
ATOM   3028 O O   . LEU   B 1 103 ? -31.717 -18.956 -41.295 1.00 14.87 ?  1140 LEU   B O   1 
ATOM   3029 C CB  . LEU   B 1 103 ? -34.543 -18.975 -42.730 1.00 13.27 ?  1140 LEU   B CB  1 
ATOM   3030 C CG  . LEU   B 1 103 ? -34.384 -18.731 -44.232 1.00 14.15 ?  1140 LEU   B CG  1 
ATOM   3031 C CD1 . LEU   B 1 103 ? -34.849 -19.948 -45.016 1.00 10.79 ?  1140 LEU   B CD1 1 
ATOM   3032 C CD2 . LEU   B 1 103 ? -35.125 -17.482 -44.682 1.00 11.08 ?  1140 LEU   B CD2 1 
ATOM   3033 N N   . SER   B 1 104 ? -31.460 -19.995 -43.272 1.00 13.01 ?  1141 SER   B N   1 
ATOM   3034 C CA  . SER   B 1 104 ? -30.033 -19.733 -43.362 1.00 14.25 ?  1141 SER   B CA  1 
ATOM   3035 C C   . SER   B 1 104 ? -29.742 -18.676 -44.420 1.00 16.55 ?  1141 SER   B C   1 
ATOM   3036 O O   . SER   B 1 104 ? -30.566 -18.397 -45.293 1.00 20.92 ?  1141 SER   B O   1 
ATOM   3037 C CB  . SER   B 1 104 ? -29.268 -21.023 -43.677 1.00 15.41 ?  1141 SER   B CB  1 
ATOM   3038 O OG  . SER   B 1 104 ? -29.268 -21.894 -42.558 1.00 22.23 ?  1141 SER   B OG  1 
ATOM   3039 N N   . LEU   B 1 105 ? -28.554 -18.078 -44.329 1.00 14.82 ?  1142 LEU   B N   1 
ATOM   3040 C CA  . LEU   B 1 105 ? -28.091 -17.097 -45.305 1.00 17.29 ?  1142 LEU   B CA  1 
ATOM   3041 C C   . LEU   B 1 105 ? -26.991 -17.731 -46.141 1.00 12.76 ?  1142 LEU   B C   1 
ATOM   3042 O O   . LEU   B 1 105 ? -25.935 -18.082 -45.606 1.00 13.52 ?  1142 LEU   B O   1 
ATOM   3043 C CB  . LEU   B 1 105 ? -27.552 -15.832 -44.638 1.00 16.77 ?  1142 LEU   B CB  1 
ATOM   3044 C CG  . LEU   B 1 105 ? -27.281 -14.767 -45.699 1.00 15.22 ?  1142 LEU   B CG  1 
ATOM   3045 C CD1 . LEU   B 1 105 ? -28.615 -14.266 -46.200 1.00 12.08 ?  1142 LEU   B CD1 1 
ATOM   3046 C CD2 . LEU   B 1 105 ? -26.429 -13.639 -45.190 1.00 14.42 ?  1142 LEU   B CD2 1 
ATOM   3047 N N   . LEU   B 1 106 ? -27.227 -17.853 -47.448 1.00 13.59 ?  1143 LEU   B N   1 
ATOM   3048 C CA  . LEU   B 1 106 ? -26.249 -18.461 -48.345 1.00 13.48 ?  1143 LEU   B CA  1 
ATOM   3049 C C   . LEU   B 1 106 ? -25.175 -17.482 -48.799 1.00 17.21 ?  1143 LEU   B C   1 
ATOM   3050 O O   . LEU   B 1 106 ? -23.992 -17.835 -48.836 1.00 22.79 ?  1143 LEU   B O   1 
ATOM   3051 C CB  . LEU   B 1 106 ? -26.944 -19.047 -49.574 1.00 15.71 ?  1143 LEU   B CB  1 
ATOM   3052 C CG  . LEU   B 1 106 ? -27.505 -20.462 -49.453 1.00 19.06 ?  1143 LEU   B CG  1 
ATOM   3053 C CD1 . LEU   B 1 106 ? -28.954 -20.424 -48.995 1.00 15.80 ?  1143 LEU   B CD1 1 
ATOM   3054 C CD2 . LEU   B 1 106 ? -27.372 -21.183 -50.778 1.00 17.92 ?  1143 LEU   B CD2 1 
ATOM   3055 N N   . GLY   B 1 107 ? -25.560 -16.270 -49.164 1.00 18.20 ?  1144 GLY   B N   1 
ATOM   3056 C CA  . GLY   B 1 107 ? -24.580 -15.258 -49.500 1.00 16.20 ?  1144 GLY   B CA  1 
ATOM   3057 C C   . GLY   B 1 107 ? -25.268 -13.958 -49.848 1.00 14.10 ?  1144 GLY   B C   1 
ATOM   3058 O O   . GLY   B 1 107 ? -26.500 -13.848 -49.805 1.00 14.86 ?  1144 GLY   B O   1 
ATOM   3059 N N   . ILE   B 1 108 ? -24.443 -12.972 -50.189 1.00 16.69 ?  1145 ILE   B N   1 
ATOM   3060 C CA  . ILE   B 1 108 ? -24.908 -11.657 -50.612 1.00 11.14 ?  1145 ILE   B CA  1 
ATOM   3061 C C   . ILE   B 1 108 ? -24.216 -11.324 -51.922 1.00 12.00 ?  1145 ILE   B C   1 
ATOM   3062 O O   . ILE   B 1 108 ? -22.982 -11.303 -51.986 1.00 13.11 ?  1145 ILE   B O   1 
ATOM   3063 C CB  . ILE   B 1 108 ? -24.624 -10.576 -49.558 1.00 11.97 ?  1145 ILE   B CB  1 
ATOM   3064 C CG1 . ILE   B 1 108 ? -25.276 -10.929 -48.227 1.00 11.36 ?  1145 ILE   B CG1 1 
ATOM   3065 C CG2 . ILE   B 1 108 ? -25.132 -9.227  -50.035 1.00 10.97 ?  1145 ILE   B CG2 1 
ATOM   3066 C CD1 . ILE   B 1 108 ? -24.907 -9.979  -47.133 1.00 12.61 ?  1145 ILE   B CD1 1 
ATOM   3067 N N   . CYS   B 1 109 ? -25.001 -11.064 -52.961 1.00 9.81  ?  1146 CYS   B N   1 
ATOM   3068 C CA  . CYS   B 1 109 ? -24.465 -10.727 -54.272 1.00 13.37 ?  1146 CYS   B CA  1 
ATOM   3069 C C   . CYS   B 1 109 ? -24.548 -9.222  -54.493 1.00 15.13 ?  1146 CYS   B C   1 
ATOM   3070 O O   . CYS   B 1 109 ? -25.566 -8.592  -54.190 1.00 14.44 ?  1146 CYS   B O   1 
ATOM   3071 C CB  . CYS   B 1 109 ? -25.220 -11.464 -55.379 1.00 14.46 ?  1146 CYS   B CB  1 
ATOM   3072 S SG  . CYS   B 1 109 ? -24.366 -11.487 -56.974 1.00 20.63 ?  1146 CYS   B SG  1 
ATOM   3073 N N   . LEU   B 1 110 ? -23.470 -8.651  -55.023 1.00 15.45 ?  1147 LEU   B N   1 
ATOM   3074 C CA  . LEU   B 1 110 ? -23.379 -7.205  -55.213 1.00 13.43 ?  1147 LEU   B CA  1 
ATOM   3075 C C   . LEU   B 1 110 ? -23.426 -6.834  -56.691 1.00 13.66 ?  1147 LEU   B C   1 
ATOM   3076 O O   . LEU   B 1 110 ? -23.649 -5.676  -57.045 1.00 14.86 ?  1147 LEU   B O   1 
ATOM   3077 C CB  . LEU   B 1 110 ? -22.097 -6.667  -54.575 1.00 19.63 ?  1147 LEU   B CB  1 
ATOM   3078 C CG  . LEU   B 1 110 ? -22.094 -6.617  -53.046 1.00 16.56 ?  1147 LEU   B CG  1 
ATOM   3079 C CD1 . LEU   B 1 110 ? -20.744 -6.157  -52.522 1.00 12.39 ?  1147 LEU   B CD1 1 
ATOM   3080 C CD2 . LEU   B 1 110 ? -23.207 -5.714  -52.538 1.00 10.91 ?  1147 LEU   B CD2 1 
ATOM   3081 N N   . SER   B 1 115 ? -29.491 -3.127  -55.624 1.00 27.84 ?  1152 SER   B N   1 
ATOM   3082 C CA  . SER   B 1 115 ? -28.172 -3.633  -55.999 1.00 22.22 ?  1152 SER   B CA  1 
ATOM   3083 C C   . SER   B 1 115 ? -27.568 -4.687  -55.045 1.00 20.01 ?  1152 SER   B C   1 
ATOM   3084 O O   . SER   B 1 115 ? -26.827 -5.556  -55.504 1.00 15.74 ?  1152 SER   B O   1 
ATOM   3085 C CB  . SER   B 1 115 ? -27.192 -2.466  -56.167 1.00 19.87 ?  1152 SER   B CB  1 
ATOM   3086 O OG  . SER   B 1 115 ? -27.349 -1.499  -55.144 1.00 23.42 ?  1152 SER   B OG  1 
ATOM   3087 N N   . PRO   B 1 116 ? -27.849 -4.625  -53.737 1.00 17.47 ?  1153 PRO   B N   1 
ATOM   3088 C CA  . PRO   B 1 116 ? -27.508 -5.777  -52.893 1.00 15.03 ?  1153 PRO   B CA  1 
ATOM   3089 C C   . PRO   B 1 116 ? -28.619 -6.814  -52.905 1.00 17.40 ?  1153 PRO   B C   1 
ATOM   3090 O O   . PRO   B 1 116 ? -29.810 -6.496  -52.861 1.00 15.71 ?  1153 PRO   B O   1 
ATOM   3091 C CB  . PRO   B 1 116 ? -27.334 -5.166  -51.494 1.00 13.11 ?  1153 PRO   B CB  1 
ATOM   3092 C CG  . PRO   B 1 116 ? -28.013 -3.863  -51.525 1.00 19.39 ?  1153 PRO   B CG  1 
ATOM   3093 C CD  . PRO   B 1 116 ? -28.351 -3.493  -52.935 1.00 22.19 ?  1153 PRO   B CD  1 
ATOM   3094 N N   . LEU   B 1 117 ? -28.212 -8.079  -52.975 1.00 17.77 ?  1154 LEU   B N   1 
ATOM   3095 C CA  . LEU   B 1 117 ? -29.138 -9.195  -53.120 1.00 14.24 ?  1154 LEU   B CA  1 
ATOM   3096 C C   . LEU   B 1 117 ? -28.891 -10.205 -52.012 1.00 12.17 ?  1154 LEU   B C   1 
ATOM   3097 O O   . LEU   B 1 117 ? -27.802 -10.782 -51.925 1.00 12.75 ?  1154 LEU   B O   1 
ATOM   3098 C CB  . LEU   B 1 117 ? -28.987 -9.860  -54.490 1.00 11.31 ?  1154 LEU   B CB  1 
ATOM   3099 C CG  . LEU   B 1 117 ? -29.278 -8.980  -55.706 1.00 11.57 ?  1154 LEU   B CG  1 
ATOM   3100 C CD1 . LEU   B 1 117 ? -29.138 -9.776  -56.995 1.00 9.05  ?  1154 LEU   B CD1 1 
ATOM   3101 C CD2 . LEU   B 1 117 ? -30.664 -8.368  -55.600 1.00 13.98 ?  1154 LEU   B CD2 1 
ATOM   3102 N N   . VAL   B 1 118 ? -29.897 -10.416 -51.174 1.00 17.19 ?  1155 VAL   B N   1 
ATOM   3103 C CA  . VAL   B 1 118 ? -29.861 -11.480 -50.179 1.00 16.06 ?  1155 VAL   B CA  1 
ATOM   3104 C C   . VAL   B 1 118 ? -30.144 -12.806 -50.871 1.00 16.76 ?  1155 VAL   B C   1 
ATOM   3105 O O   . VAL   B 1 118 ? -31.027 -12.897 -51.732 1.00 16.13 ?  1155 VAL   B O   1 
ATOM   3106 C CB  . VAL   B 1 118 ? -30.877 -11.195 -49.058 1.00 17.04 ?  1155 VAL   B CB  1 
ATOM   3107 C CG1 . VAL   B 1 118 ? -30.784 -12.241 -47.977 1.00 16.11 ?  1155 VAL   B CG1 1 
ATOM   3108 C CG2 . VAL   B 1 118 ? -30.645 -9.809  -48.476 1.00 17.05 ?  1155 VAL   B CG2 1 
ATOM   3109 N N   . VAL   B 1 119 ? -29.385 -13.838 -50.512 1.00 18.90 ?  1156 VAL   B N   1 
ATOM   3110 C CA  . VAL   B 1 119 ? -29.492 -15.156 -51.132 1.00 15.45 ?  1156 VAL   B CA  1 
ATOM   3111 C C   . VAL   B 1 119 ? -29.847 -16.159 -50.044 1.00 15.54 ?  1156 VAL   B C   1 
ATOM   3112 O O   . VAL   B 1 119 ? -29.067 -16.372 -49.107 1.00 16.03 ?  1156 VAL   B O   1 
ATOM   3113 C CB  . VAL   B 1 119 ? -28.195 -15.552 -51.854 1.00 14.18 ?  1156 VAL   B CB  1 
ATOM   3114 C CG1 . VAL   B 1 119 ? -28.386 -16.847 -52.623 1.00 13.88 ?  1156 VAL   B CG1 1 
ATOM   3115 C CG2 . VAL   B 1 119 ? -27.756 -14.432 -52.783 1.00 16.10 ?  1156 VAL   B CG2 1 
ATOM   3116 N N   . LEU   B 1 120 ? -31.015 -16.773 -50.172 1.00 13.29 ?  1157 LEU   B N   1 
ATOM   3117 C CA  . LEU   B 1 120 ? -31.631 -17.594 -49.143 1.00 15.82 ?  1157 LEU   B CA  1 
ATOM   3118 C C   . LEU   B 1 120 ? -32.047 -18.934 -49.728 1.00 12.55 ?  1157 LEU   B C   1 
ATOM   3119 O O   . LEU   B 1 120 ? -32.187 -19.068 -50.948 1.00 11.08 ?  1157 LEU   B O   1 
ATOM   3120 C CB  . LEU   B 1 120 ? -32.851 -16.869 -48.553 1.00 15.66 ?  1157 LEU   B CB  1 
ATOM   3121 C CG  . LEU   B 1 120 ? -32.567 -15.439 -48.092 1.00 14.14 ?  1157 LEU   B CG  1 
ATOM   3122 C CD1 . LEU   B 1 120 ? -33.818 -14.587 -48.149 1.00 15.27 ?  1157 LEU   B CD1 1 
ATOM   3123 C CD2 . LEU   B 1 120 ? -31.986 -15.443 -46.689 1.00 12.99 ?  1157 LEU   B CD2 1 
ATOM   3124 N N   . PRO   B 1 121 ? -32.250 -19.950 -48.887 1.00 13.41 ?  1158 PRO   B N   1 
ATOM   3125 C CA  . PRO   B 1 121 ? -32.639 -21.264 -49.413 1.00 14.79 ?  1158 PRO   B CA  1 
ATOM   3126 C C   . PRO   B 1 121 ? -34.011 -21.210 -50.065 1.00 18.51 ?  1158 PRO   B C   1 
ATOM   3127 O O   . PRO   B 1 121 ? -34.960 -20.651 -49.512 1.00 16.67 ?  1158 PRO   B O   1 
ATOM   3128 C CB  . PRO   B 1 121 ? -32.643 -22.161 -48.167 1.00 11.33 ?  1158 PRO   B CB  1 
ATOM   3129 C CG  . PRO   B 1 121 ? -31.848 -21.420 -47.146 1.00 13.91 ?  1158 PRO   B CG  1 
ATOM   3130 C CD  . PRO   B 1 121 ? -32.120 -19.978 -47.421 1.00 14.30 ?  1158 PRO   B CD  1 
ATOM   3131 N N   . TYR   B 1 122 ? -34.105 -21.791 -51.258 1.00 14.99 ?  1159 TYR   B N   1 
ATOM   3132 C CA  . TYR   B 1 122 ? -35.392 -21.915 -51.923 1.00 16.59 ?  1159 TYR   B CA  1 
ATOM   3133 C C   . TYR   B 1 122 ? -36.312 -22.797 -51.088 1.00 17.49 ?  1159 TYR   B C   1 
ATOM   3134 O O   . TYR   B 1 122 ? -35.906 -23.858 -50.606 1.00 16.34 ?  1159 TYR   B O   1 
ATOM   3135 C CB  . TYR   B 1 122 ? -35.200 -22.486 -53.330 1.00 15.85 ?  1159 TYR   B CB  1 
ATOM   3136 C CG  . TYR   B 1 122 ? -36.467 -22.617 -54.146 1.00 21.64 ?  1159 TYR   B CG  1 
ATOM   3137 C CD1 . TYR   B 1 122 ? -37.358 -23.657 -53.927 1.00 18.43 ?  1159 TYR   B CD1 1 
ATOM   3138 C CD2 . TYR   B 1 122 ? -36.752 -21.721 -55.165 1.00 22.16 ?  1159 TYR   B CD2 1 
ATOM   3139 C CE1 . TYR   B 1 122 ? -38.502 -23.782 -54.678 1.00 18.21 ?  1159 TYR   B CE1 1 
ATOM   3140 C CE2 . TYR   B 1 122 ? -37.905 -21.840 -55.918 1.00 19.17 ?  1159 TYR   B CE2 1 
ATOM   3141 C CZ  . TYR   B 1 122 ? -38.775 -22.876 -55.669 1.00 17.68 ?  1159 TYR   B CZ  1 
ATOM   3142 O OH  . TYR   B 1 122 ? -39.927 -23.018 -56.409 1.00 26.58 ?  1159 TYR   B OH  1 
ATOM   3143 N N   . MET   B 1 123 ? -37.550 -22.345 -50.905 1.00 14.87 ?  1160 MET   B N   1 
ATOM   3144 C CA  . MET   B 1 123 ? -38.530 -23.008 -50.046 1.00 14.29 ?  1160 MET   B CA  1 
ATOM   3145 C C   . MET   B 1 123 ? -39.745 -23.351 -50.903 1.00 17.38 ?  1160 MET   B C   1 
ATOM   3146 O O   . MET   B 1 123 ? -40.678 -22.553 -51.011 1.00 17.85 ?  1160 MET   B O   1 
ATOM   3147 C CB  . MET   B 1 123 ? -38.911 -22.112 -48.875 1.00 16.38 ?  1160 MET   B CB  1 
ATOM   3148 C CG  . MET   B 1 123 ? -37.752 -21.742 -47.972 1.00 14.25 ?  1160 MET   B CG  1 
ATOM   3149 S SD  . MET   B 1 123 ? -37.074 -23.160 -47.098 1.00 17.16 ?  1160 MET   B SD  1 
ATOM   3150 C CE  . MET   B 1 123 ? -37.343 -22.658 -45.406 1.00 7.97  ?  1160 MET   B CE  1 
ATOM   3151 N N   . LYS   B 1 124 ? -39.749 -24.552 -51.488 1.00 16.89 ?  1161 LYS   B N   1 
ATOM   3152 C CA  . LYS   B 1 124 ? -40.737 -24.871 -52.515 1.00 16.56 ?  1161 LYS   B CA  1 
ATOM   3153 C C   . LYS   B 1 124 ? -42.168 -24.891 -51.992 1.00 14.66 ?  1161 LYS   B C   1 
ATOM   3154 O O   . LYS   B 1 124 ? -43.104 -24.842 -52.798 1.00 13.33 ?  1161 LYS   B O   1 
ATOM   3155 C CB  . LYS   B 1 124 ? -40.402 -26.212 -53.172 1.00 13.15 ?  1161 LYS   B CB  1 
ATOM   3156 N N   . HIS   B 1 125 ? -42.372 -24.941 -50.676 1.00 15.39 ?  1162 HIS   B N   1 
ATOM   3157 C CA  . HIS   B 1 125 ? -43.714 -24.977 -50.112 1.00 14.49 ?  1162 HIS   B CA  1 
ATOM   3158 C C   . HIS   B 1 125 ? -44.131 -23.655 -49.478 1.00 14.62 ?  1162 HIS   B C   1 
ATOM   3159 O O   . HIS   B 1 125 ? -45.077 -23.627 -48.684 1.00 13.61 ?  1162 HIS   B O   1 
ATOM   3160 C CB  . HIS   B 1 125 ? -43.821 -26.121 -49.111 1.00 14.98 ?  1162 HIS   B CB  1 
ATOM   3161 C CG  . HIS   B 1 125 ? -43.885 -27.461 -49.764 1.00 19.66 ?  1162 HIS   B CG  1 
ATOM   3162 N ND1 . HIS   B 1 125 ? -43.140 -28.536 -49.333 1.00 23.22 ?  1162 HIS   B ND1 1 
ATOM   3163 C CD2 . HIS   B 1 125 ? -44.595 -27.896 -50.831 1.00 21.32 ?  1162 HIS   B CD2 1 
ATOM   3164 C CE1 . HIS   B 1 125 ? -43.386 -29.576 -50.109 1.00 19.38 ?  1162 HIS   B CE1 1 
ATOM   3165 N NE2 . HIS   B 1 125 ? -44.273 -29.217 -51.020 1.00 25.01 ?  1162 HIS   B NE2 1 
ATOM   3166 N N   . GLY   B 1 126 ? -43.460 -22.562 -49.827 1.00 17.28 ?  1163 GLY   B N   1 
ATOM   3167 C CA  . GLY   B 1 126 ? -43.951 -21.256 -49.428 1.00 17.48 ?  1163 GLY   B CA  1 
ATOM   3168 C C   . GLY   B 1 126 ? -43.925 -21.054 -47.927 1.00 14.51 ?  1163 GLY   B C   1 
ATOM   3169 O O   . GLY   B 1 126 ? -43.018 -21.516 -47.226 1.00 16.42 ?  1163 GLY   B O   1 
ATOM   3170 N N   . ASP   B 1 127 ? -44.937 -20.350 -47.424 1.00 11.87 ?  1164 ASP   B N   1 
ATOM   3171 C CA  . ASP   B 1 127 ? -45.040 -19.994 -46.017 1.00 11.48 ?  1164 ASP   B CA  1 
ATOM   3172 C C   . ASP   B 1 127 ? -45.945 -20.970 -45.271 1.00 13.19 ?  1164 ASP   B C   1 
ATOM   3173 O O   . ASP   B 1 127 ? -46.834 -21.604 -45.846 1.00 12.91 ?  1164 ASP   B O   1 
ATOM   3174 C CB  . ASP   B 1 127 ? -45.549 -18.552 -45.854 1.00 12.52 ?  1164 ASP   B CB  1 
ATOM   3175 C CG  . ASP   B 1 127 ? -46.921 -18.331 -46.463 1.00 14.10 ?  1164 ASP   B CG  1 
ATOM   3176 O OD1 . ASP   B 1 127 ? -46.998 -18.144 -47.694 1.00 13.12 ?  1164 ASP   B OD1 1 
ATOM   3177 O OD2 . ASP   B 1 127 ? -47.919 -18.314 -45.709 1.00 16.33 -1 1164 ASP   B OD2 1 
ATOM   3178 N N   . LEU   B 1 128 ? -45.696 -21.076 -43.963 1.00 14.67 ?  1165 LEU   B N   1 
ATOM   3179 C CA  . LEU   B 1 128 ? -46.390 -22.053 -43.129 1.00 13.69 ?  1165 LEU   B CA  1 
ATOM   3180 C C   . LEU   B 1 128 ? -47.900 -21.856 -43.158 1.00 16.97 ?  1165 LEU   B C   1 
ATOM   3181 O O   . LEU   B 1 128 ? -48.659 -22.831 -43.211 1.00 13.93 ?  1165 LEU   B O   1 
ATOM   3182 C CB  . LEU   B 1 128 ? -45.871 -21.958 -41.696 1.00 11.89 ?  1165 LEU   B CB  1 
ATOM   3183 C CG  . LEU   B 1 128 ? -46.676 -22.657 -40.611 1.00 19.11 ?  1165 LEU   B CG  1 
ATOM   3184 C CD1 . LEU   B 1 128 ? -46.626 -24.160 -40.826 1.00 15.35 ?  1165 LEU   B CD1 1 
ATOM   3185 C CD2 . LEU   B 1 128 ? -46.157 -22.264 -39.240 1.00 14.12 ?  1165 LEU   B CD2 1 
ATOM   3186 N N   . ARG   B 1 129 ? -48.360 -20.604 -43.123 1.00 17.89 ?  1166 ARG   B N   1 
ATOM   3187 C CA  . ARG   B 1 129 ? -49.795 -20.368 -43.024 1.00 17.27 ?  1166 ARG   B CA  1 
ATOM   3188 C C   . ARG   B 1 129 ? -50.497 -20.561 -44.362 1.00 16.28 ?  1166 ARG   B C   1 
ATOM   3189 O O   . ARG   B 1 129 ? -51.574 -21.166 -44.416 1.00 17.15 ?  1166 ARG   B O   1 
ATOM   3190 C CB  . ARG   B 1 129 ? -50.069 -18.969 -42.483 1.00 16.12 ?  1166 ARG   B CB  1 
ATOM   3191 C CG  . ARG   B 1 129 ? -51.542 -18.680 -42.337 1.00 17.86 ?  1166 ARG   B CG  1 
ATOM   3192 C CD  . ARG   B 1 129 ? -51.781 -17.324 -41.735 1.00 20.50 ?  1166 ARG   B CD  1 
ATOM   3193 N NE  . ARG   B 1 129 ? -53.207 -17.072 -41.581 1.00 24.35 ?  1166 ARG   B NE  1 
ATOM   3194 C CZ  . ARG   B 1 129 ? -53.718 -16.051 -40.910 1.00 23.40 ?  1166 ARG   B CZ  1 
ATOM   3195 N NH1 . ARG   B 1 129 ? -52.940 -15.169 -40.301 1.00 31.07 ?  1166 ARG   B NH1 1 
ATOM   3196 N NH2 . ARG   B 1 129 ? -55.038 -15.911 -40.847 1.00 26.89 ?  1166 ARG   B NH2 1 
ATOM   3197 N N   . ASN   B 1 130 ? -49.917 -20.050 -45.451 1.00 14.52 ?  1167 ASN   B N   1 
ATOM   3198 C CA  . ASN   B 1 130 ? -50.471 -20.339 -46.770 1.00 16.15 ?  1167 ASN   B CA  1 
ATOM   3199 C C   . ASN   B 1 130 ? -50.511 -21.835 -47.031 1.00 22.35 ?  1167 ASN   B C   1 
ATOM   3200 O O   . ASN   B 1 130 ? -51.333 -22.309 -47.823 1.00 21.89 ?  1167 ASN   B O   1 
ATOM   3201 C CB  . ASN   B 1 130 ? -49.652 -19.652 -47.860 1.00 15.16 ?  1167 ASN   B CB  1 
ATOM   3202 C CG  . ASN   B 1 130 ? -50.280 -18.364 -48.344 1.00 16.00 ?  1167 ASN   B CG  1 
ATOM   3203 O OD1 . ASN   B 1 130 ? -51.409 -18.033 -47.983 1.00 15.45 ?  1167 ASN   B OD1 1 
ATOM   3204 N ND2 . ASN   B 1 130 ? -49.546 -17.625 -49.168 1.00 21.59 ?  1167 ASN   B ND2 1 
ATOM   3205 N N   . PHE   B 1 131 ? -49.630 -22.591 -46.375 1.00 16.89 ?  1168 PHE   B N   1 
ATOM   3206 C CA  . PHE   B 1 131 ? -49.601 -24.034 -46.548 1.00 17.70 ?  1168 PHE   B CA  1 
ATOM   3207 C C   . PHE   B 1 131 ? -50.711 -24.730 -45.772 1.00 21.15 ?  1168 PHE   B C   1 
ATOM   3208 O O   . PHE   B 1 131 ? -51.140 -25.822 -46.162 1.00 19.58 ?  1168 PHE   B O   1 
ATOM   3209 C CB  . PHE   B 1 131 ? -48.241 -24.582 -46.125 1.00 16.11 ?  1168 PHE   B CB  1 
ATOM   3210 C CG  . PHE   B 1 131 ? -47.942 -25.930 -46.689 1.00 18.81 ?  1168 PHE   B CG  1 
ATOM   3211 C CD1 . PHE   B 1 131 ? -47.464 -26.066 -47.982 1.00 21.59 ?  1168 PHE   B CD1 1 
ATOM   3212 C CD2 . PHE   B 1 131 ? -48.161 -27.066 -45.937 1.00 20.29 ?  1168 PHE   B CD2 1 
ATOM   3213 C CE1 . PHE   B 1 131 ? -47.198 -27.314 -48.505 1.00 23.54 ?  1168 PHE   B CE1 1 
ATOM   3214 C CE2 . PHE   B 1 131 ? -47.900 -28.307 -46.453 1.00 23.82 ?  1168 PHE   B CE2 1 
ATOM   3215 C CZ  . PHE   B 1 131 ? -47.417 -28.437 -47.738 1.00 22.73 ?  1168 PHE   B CZ  1 
ATOM   3216 N N   . ILE   B 1 132 ? -51.184 -24.131 -44.680 1.00 19.06 ?  1169 ILE   B N   1 
ATOM   3217 C CA  . ILE   B 1 132 ? -52.304 -24.696 -43.938 1.00 17.34 ?  1169 ILE   B CA  1 
ATOM   3218 C C   . ILE   B 1 132 ? -53.641 -24.099 -44.372 1.00 19.49 ?  1169 ILE   B C   1 
ATOM   3219 O O   . ILE   B 1 132 ? -54.693 -24.688 -44.078 1.00 18.51 ?  1169 ILE   B O   1 
ATOM   3220 C CB  . ILE   B 1 132 ? -52.100 -24.536 -42.416 1.00 16.85 ?  1169 ILE   B CB  1 
ATOM   3221 C CG1 . ILE   B 1 132 ? -51.946 -23.064 -42.036 1.00 17.17 ?  1169 ILE   B CG1 1 
ATOM   3222 C CG2 . ILE   B 1 132 ? -50.870 -25.306 -41.973 1.00 13.38 ?  1169 ILE   B CG2 1 
ATOM   3223 C CD1 . ILE   B 1 132 ? -51.382 -22.843 -40.642 1.00 14.39 ?  1169 ILE   B CD1 1 
ATOM   3224 N N   . ARG   B 1 133 ? -53.632 -22.958 -45.067 1.00 23.68 ?  1170 ARG   B N   1 
ATOM   3225 C CA  . ARG   B 1 133 ? -54.843 -22.460 -45.708 1.00 17.68 ?  1170 ARG   B CA  1 
ATOM   3226 C C   . ARG   B 1 133 ? -55.189 -23.241 -46.966 1.00 16.22 ?  1170 ARG   B C   1 
ATOM   3227 O O   . ARG   B 1 133 ? -56.328 -23.160 -47.437 1.00 21.37 ?  1170 ARG   B O   1 
ATOM   3228 C CB  . ARG   B 1 133 ? -54.691 -20.985 -46.081 1.00 15.91 ?  1170 ARG   B CB  1 
ATOM   3229 C CG  . ARG   B 1 133 ? -54.608 -20.045 -44.909 1.00 16.70 ?  1170 ARG   B CG  1 
ATOM   3230 C CD  . ARG   B 1 133 ? -54.332 -18.613 -45.331 1.00 22.46 ?  1170 ARG   B CD  1 
ATOM   3231 N NE  . ARG   B 1 133 ? -55.447 -18.035 -46.072 1.00 23.78 ?  1170 ARG   B NE  1 
ATOM   3232 C CZ  . ARG   B 1 133 ? -56.595 -17.657 -45.527 1.00 26.25 ?  1170 ARG   B CZ  1 
ATOM   3233 N NH1 . ARG   B 1 133 ? -56.827 -17.800 -44.233 1.00 25.57 ?  1170 ARG   B NH1 1 
ATOM   3234 N NH2 . ARG   B 1 133 ? -57.536 -17.126 -46.302 1.00 27.23 ?  1170 ARG   B NH2 1 
ATOM   3235 N N   . ASN   B 1 134 ? -54.236 -23.979 -47.526 1.00 17.92 ?  1171 ASN   B N   1 
ATOM   3236 C CA  . ASN   B 1 134 ? -54.413 -24.583 -48.840 1.00 20.51 ?  1171 ASN   B CA  1 
ATOM   3237 C C   . ASN   B 1 134 ? -55.337 -25.790 -48.742 1.00 26.60 ?  1171 ASN   B C   1 
ATOM   3238 O O   . ASN   B 1 134 ? -55.036 -26.757 -48.035 1.00 25.52 ?  1171 ASN   B O   1 
ATOM   3239 C CB  . ASN   B 1 134 ? -53.059 -24.975 -49.420 1.00 18.56 ?  1171 ASN   B CB  1 
ATOM   3240 C CG  . ASN   B 1 134 ? -53.060 -24.992 -50.931 1.00 24.44 ?  1171 ASN   B CG  1 
ATOM   3241 O OD1 . ASN   B 1 134 ? -54.071 -25.314 -51.554 1.00 32.72 ?  1171 ASN   B OD1 1 
ATOM   3242 N ND2 . ASN   B 1 134 ? -51.930 -24.638 -51.532 1.00 24.07 ?  1171 ASN   B ND2 1 
ATOM   3243 N N   . GLU   B 1 135 ? -56.453 -25.734 -49.466 1.00 29.54 ?  1172 GLU   B N   1 
ATOM   3244 C CA  . GLU   B 1 135 ? -57.495 -26.751 -49.403 1.00 35.20 ?  1172 GLU   B CA  1 
ATOM   3245 C C   . GLU   B 1 135 ? -57.132 -28.052 -50.100 1.00 28.71 ?  1172 GLU   B C   1 
ATOM   3246 O O   . GLU   B 1 135 ? -57.784 -29.074 -49.849 1.00 31.33 ?  1172 GLU   B O   1 
ATOM   3247 C CB  . GLU   B 1 135 ? -58.780 -26.190 -49.995 1.00 32.10 ?  1172 GLU   B CB  1 
ATOM   3248 C CG  . GLU   B 1 135 ? -58.653 -25.572 -51.366 1.00 35.48 ?  1172 GLU   B CG  1 
ATOM   3249 C CD  . GLU   B 1 135 ? -59.464 -24.299 -51.479 1.00 53.73 ?  1172 GLU   B CD  1 
ATOM   3250 O OE1 . GLU   B 1 135 ? -59.156 -23.343 -50.746 1.00 49.92 ?  1172 GLU   B OE1 1 
ATOM   3251 O OE2 . GLU   B 1 135 ? -60.431 -24.266 -52.274 1.00 60.46 -1 1172 GLU   B OE2 1 
ATOM   3252 N N   . THR   B 1 136 ? -56.117 -28.054 -50.952 1.00 27.46 ?  1173 THR   B N   1 
ATOM   3253 C CA  . THR   B 1 136 ? -55.661 -29.303 -51.541 1.00 28.94 ?  1173 THR   B CA  1 
ATOM   3254 C C   . THR   B 1 136 ? -54.655 -30.028 -50.657 1.00 26.69 ?  1173 THR   B C   1 
ATOM   3255 O O   . THR   B 1 136 ? -54.252 -31.151 -50.985 1.00 32.30 ?  1173 THR   B O   1 
ATOM   3256 C CB  . THR   B 1 136 ? -55.064 -29.047 -52.933 1.00 34.01 ?  1173 THR   B CB  1 
ATOM   3257 O OG1 . THR   B 1 136 ? -54.844 -30.292 -53.610 1.00 30.65 ?  1173 THR   B OG1 1 
ATOM   3258 C CG2 . THR   B 1 136 ? -53.759 -28.288 -52.827 1.00 26.74 ?  1173 THR   B CG2 1 
ATOM   3259 N N   . HIS   B 1 137 ? -54.252 -29.416 -49.548 1.00 30.63 ?  1174 HIS   B N   1 
ATOM   3260 C CA  . HIS   B 1 137 ? -53.445 -30.065 -48.526 1.00 25.85 ?  1174 HIS   B CA  1 
ATOM   3261 C C   . HIS   B 1 137 ? -54.357 -30.550 -47.408 1.00 19.87 ?  1174 HIS   B C   1 
ATOM   3262 O O   . HIS   B 1 137 ? -55.328 -29.878 -47.049 1.00 17.39 ?  1174 HIS   B O   1 
ATOM   3263 C CB  . HIS   B 1 137 ? -52.391 -29.116 -47.945 1.00 27.78 ?  1174 HIS   B CB  1 
ATOM   3264 C CG  . HIS   B 1 137 ? -51.634 -28.330 -48.971 1.00 27.18 ?  1174 HIS   B CG  1 
ATOM   3265 N ND1 . HIS   B 1 137 ? -50.809 -27.279 -48.634 1.00 23.09 ?  1174 HIS   B ND1 1 
ATOM   3266 C CD2 . HIS   B 1 137 ? -51.561 -28.447 -50.318 1.00 29.79 ?  1174 HIS   B CD2 1 
ATOM   3267 C CE1 . HIS   B 1 137 ? -50.268 -26.777 -49.730 1.00 24.30 ?  1174 HIS   B CE1 1 
ATOM   3268 N NE2 . HIS   B 1 137 ? -50.711 -27.466 -50.766 1.00 26.60 ?  1174 HIS   B NE2 1 
ATOM   3269 N N   . ASN   B 1 138 ? -54.040 -31.717 -46.855 1.00 20.99 ?  1175 ASN   B N   1 
ATOM   3270 C CA  . ASN   B 1 138 ? -54.819 -32.313 -45.771 1.00 18.12 ?  1175 ASN   B CA  1 
ATOM   3271 C C   . ASN   B 1 138 ? -53.900 -32.674 -44.612 1.00 16.81 ?  1175 ASN   B C   1 
ATOM   3272 O O   . ASN   B 1 138 ? -53.593 -33.850 -44.385 1.00 23.81 ?  1175 ASN   B O   1 
ATOM   3273 C CB  . ASN   B 1 138 ? -55.587 -33.539 -46.264 1.00 16.97 ?  1175 ASN   B CB  1 
ATOM   3274 C CG  . ASN   B 1 138 ? -56.473 -33.229 -47.451 1.00 15.62 ?  1175 ASN   B CG  1 
ATOM   3275 O OD1 . ASN   B 1 138 ? -57.520 -32.596 -47.311 1.00 19.27 ?  1175 ASN   B OD1 1 
ATOM   3276 N ND2 . ASN   B 1 138 ? -56.056 -33.670 -48.631 1.00 12.56 ?  1175 ASN   B ND2 1 
ATOM   3277 N N   . PRO   B 1 139 ? -53.440 -31.681 -43.854 1.00 20.66 ?  1176 PRO   B N   1 
ATOM   3278 C CA  . PRO   B 1 139 ? -52.642 -31.983 -42.663 1.00 15.76 ?  1176 PRO   B CA  1 
ATOM   3279 C C   . PRO   B 1 139 ? -53.529 -32.404 -41.504 1.00 15.60 ?  1176 PRO   B C   1 
ATOM   3280 O O   . PRO   B 1 139 ? -54.616 -31.860 -41.295 1.00 19.84 ?  1176 PRO   B O   1 
ATOM   3281 C CB  . PRO   B 1 139 ? -51.934 -30.655 -42.370 1.00 18.37 ?  1176 PRO   B CB  1 
ATOM   3282 C CG  . PRO   B 1 139 ? -52.881 -29.624 -42.876 1.00 16.89 ?  1176 PRO   B CG  1 
ATOM   3283 C CD  . PRO   B 1 139 ? -53.582 -30.229 -44.069 1.00 15.89 ?  1176 PRO   B CD  1 
ATOM   3284 N N   . THR   B 1 140 ? -53.061 -33.397 -40.757 1.00 17.79 ?  1177 THR   B N   1 
ATOM   3285 C CA  . THR   B 1 140 ? -53.768 -33.806 -39.558 1.00 14.48 ?  1177 THR   B CA  1 
ATOM   3286 C C   . THR   B 1 140 ? -53.407 -32.880 -38.401 1.00 13.54 ?  1177 THR   B C   1 
ATOM   3287 O O   . THR   B 1 140 ? -52.505 -32.045 -38.495 1.00 15.53 ?  1177 THR   B O   1 
ATOM   3288 C CB  . THR   B 1 140 ? -53.443 -35.257 -39.202 1.00 16.75 ?  1177 THR   B CB  1 
ATOM   3289 O OG1 . THR   B 1 140 ? -52.052 -35.374 -38.878 1.00 20.59 ?  1177 THR   B OG1 1 
ATOM   3290 C CG2 . THR   B 1 140 ? -53.767 -36.176 -40.367 1.00 13.97 ?  1177 THR   B CG2 1 
ATOM   3291 N N   . VAL   B 1 141 ? -54.139 -33.030 -37.295 1.00 14.54 ?  1178 VAL   B N   1 
ATOM   3292 C CA  . VAL   B 1 141 ? -53.811 -32.278 -36.089 1.00 16.03 ?  1178 VAL   B CA  1 
ATOM   3293 C C   . VAL   B 1 141 ? -52.389 -32.588 -35.643 1.00 13.83 ?  1178 VAL   B C   1 
ATOM   3294 O O   . VAL   B 1 141 ? -51.672 -31.703 -35.160 1.00 13.73 ?  1178 VAL   B O   1 
ATOM   3295 C CB  . VAL   B 1 141 ? -54.845 -32.578 -34.984 1.00 13.61 ?  1178 VAL   B CB  1 
ATOM   3296 C CG1 . VAL   B 1 141 ? -54.254 -32.348 -33.600 1.00 19.05 ?  1178 VAL   B CG1 1 
ATOM   3297 C CG2 . VAL   B 1 141 ? -56.090 -31.728 -35.184 1.00 17.92 ?  1178 VAL   B CG2 1 
ATOM   3298 N N   . LYS   B 1 142 ? -51.944 -33.834 -35.828 1.00 16.07 ?  1179 LYS   B N   1 
ATOM   3299 C CA  . LYS   B 1 142 ? -50.574 -34.194 -35.480 1.00 18.88 ?  1179 LYS   B CA  1 
ATOM   3300 C C   . LYS   B 1 142 ? -49.568 -33.587 -36.452 1.00 13.62 ?  1179 LYS   B C   1 
ATOM   3301 O O   . LYS   B 1 142 ? -48.456 -33.230 -36.046 1.00 14.22 ?  1179 LYS   B O   1 
ATOM   3302 C CB  . LYS   B 1 142 ? -50.437 -35.719 -35.429 1.00 15.71 ?  1179 LYS   B CB  1 
ATOM   3303 C CG  . LYS   B 1 142 ? -49.059 -36.262 -35.781 1.00 13.28 ?  1179 LYS   B CG  1 
ATOM   3304 C CD  . LYS   B 1 142 ? -48.809 -37.595 -35.093 1.00 20.79 ?  1179 LYS   B CD  1 
ATOM   3305 C CE  . LYS   B 1 142 ? -47.479 -38.199 -35.510 1.00 17.66 ?  1179 LYS   B CE  1 
ATOM   3306 N NZ  . LYS   B 1 142 ? -47.437 -38.500 -36.968 1.00 15.44 ?  1179 LYS   B NZ  1 
ATOM   3307 N N   . ASP   B 1 143 ? -49.939 -33.451 -37.729 1.00 14.00 ?  1180 ASP   B N   1 
ATOM   3308 C CA  . ASP   B 1 143 ? -49.063 -32.781 -38.685 1.00 12.32 ?  1180 ASP   B CA  1 
ATOM   3309 C C   . ASP   B 1 143 ? -48.814 -31.331 -38.295 1.00 12.40 ?  1180 ASP   B C   1 
ATOM   3310 O O   . ASP   B 1 143 ? -47.727 -30.798 -38.546 1.00 14.34 ?  1180 ASP   B O   1 
ATOM   3311 C CB  . ASP   B 1 143 ? -49.663 -32.841 -40.090 1.00 14.79 ?  1180 ASP   B CB  1 
ATOM   3312 C CG  . ASP   B 1 143 ? -49.620 -34.230 -40.686 1.00 23.89 ?  1180 ASP   B CG  1 
ATOM   3313 O OD1 . ASP   B 1 143 ? -49.298 -35.186 -39.950 1.00 21.75 ?  1180 ASP   B OD1 1 
ATOM   3314 O OD2 . ASP   B 1 143 ? -49.904 -34.363 -41.895 1.00 28.68 -1 1180 ASP   B OD2 1 
ATOM   3315 N N   . LEU   B 1 144 ? -49.803 -30.680 -37.684 1.00 14.34 ?  1181 LEU   B N   1 
ATOM   3316 C CA  . LEU   B 1 144 ? -49.670 -29.272 -37.335 1.00 13.51 ?  1181 LEU   B CA  1 
ATOM   3317 C C   . LEU   B 1 144 ? -48.951 -29.076 -36.006 1.00 12.76 ?  1181 LEU   B C   1 
ATOM   3318 O O   . LEU   B 1 144 ? -48.299 -28.045 -35.809 1.00 9.12  ?  1181 LEU   B O   1 
ATOM   3319 C CB  . LEU   B 1 144 ? -51.052 -28.618 -37.303 1.00 9.09  ?  1181 LEU   B CB  1 
ATOM   3320 C CG  . LEU   B 1 144 ? -51.893 -28.871 -38.556 1.00 12.49 ?  1181 LEU   B CG  1 
ATOM   3321 C CD1 . LEU   B 1 144 ? -53.366 -28.588 -38.307 1.00 13.57 ?  1181 LEU   B CD1 1 
ATOM   3322 C CD2 . LEU   B 1 144 ? -51.376 -28.049 -39.723 1.00 7.84  ?  1181 LEU   B CD2 1 
ATOM   3323 N N   . ILE   B 1 145 ? -49.060 -30.038 -35.085 1.00 11.26 ?  1182 ILE   B N   1 
ATOM   3324 C CA  . ILE   B 1 145 ? -48.256 -29.974 -33.868 1.00 11.57 ?  1182 ILE   B CA  1 
ATOM   3325 C C   . ILE   B 1 145 ? -46.808 -30.327 -34.179 1.00 11.67 ?  1182 ILE   B C   1 
ATOM   3326 O O   . ILE   B 1 145 ? -45.887 -29.879 -33.483 1.00 13.47 ?  1182 ILE   B O   1 
ATOM   3327 C CB  . ILE   B 1 145 ? -48.845 -30.889 -32.777 1.00 10.77 ?  1182 ILE   B CB  1 
ATOM   3328 C CG1 . ILE   B 1 145 ? -50.336 -30.607 -32.595 1.00 15.17 ?  1182 ILE   B CG1 1 
ATOM   3329 C CG2 . ILE   B 1 145 ? -48.119 -30.690 -31.454 1.00 8.27  ?  1182 ILE   B CG2 1 
ATOM   3330 C CD1 . ILE   B 1 145 ? -51.048 -31.595 -31.692 1.00 9.14  ?  1182 ILE   B CD1 1 
ATOM   3331 N N   . GLY   B 1 146 ? -46.580 -31.124 -35.224 1.00 11.73 ?  1183 GLY   B N   1 
ATOM   3332 C CA  . GLY   B 1 146 ? -45.217 -31.384 -35.657 1.00 12.69 ?  1183 GLY   B CA  1 
ATOM   3333 C C   . GLY   B 1 146 ? -44.515 -30.128 -36.133 1.00 13.73 ?  1183 GLY   B C   1 
ATOM   3334 O O   . GLY   B 1 146 ? -43.341 -29.907 -35.826 1.00 14.03 ?  1183 GLY   B O   1 
ATOM   3335 N N   . PHE   B 1 147 ? -45.226 -29.285 -36.888 1.00 11.44 ?  1184 PHE   B N   1 
ATOM   3336 C CA  . PHE   B 1 147 ? -44.674 -27.988 -37.264 1.00 12.43 ?  1184 PHE   B CA  1 
ATOM   3337 C C   . PHE   B 1 147 ? -44.435 -27.119 -36.037 1.00 13.39 ?  1184 PHE   B C   1 
ATOM   3338 O O   . PHE   B 1 147 ? -43.466 -26.352 -35.989 1.00 12.07 ?  1184 PHE   B O   1 
ATOM   3339 C CB  . PHE   B 1 147 ? -45.608 -27.275 -38.241 1.00 14.65 ?  1184 PHE   B CB  1 
ATOM   3340 C CG  . PHE   B 1 147 ? -45.803 -28.001 -39.540 1.00 13.04 ?  1184 PHE   B CG  1 
ATOM   3341 C CD1 . PHE   B 1 147 ? -44.810 -28.822 -40.049 1.00 13.26 ?  1184 PHE   B CD1 1 
ATOM   3342 C CD2 . PHE   B 1 147 ? -46.974 -27.846 -40.263 1.00 12.34 ?  1184 PHE   B CD2 1 
ATOM   3343 C CE1 . PHE   B 1 147 ? -44.983 -29.480 -41.248 1.00 18.44 ?  1184 PHE   B CE1 1 
ATOM   3344 C CE2 . PHE   B 1 147 ? -47.154 -28.503 -41.463 1.00 20.20 ?  1184 PHE   B CE2 1 
ATOM   3345 C CZ  . PHE   B 1 147 ? -46.156 -29.321 -41.956 1.00 23.88 ?  1184 PHE   B CZ  1 
ATOM   3346 N N   . GLY   B 1 148 ? -45.314 -27.218 -35.038 1.00 11.62 ?  1185 GLY   B N   1 
ATOM   3347 C CA  . GLY   B 1 148 ? -45.103 -26.475 -33.808 1.00 14.21 ?  1185 GLY   B CA  1 
ATOM   3348 C C   . GLY   B 1 148 ? -43.848 -26.911 -33.078 1.00 13.38 ?  1185 GLY   B C   1 
ATOM   3349 O O   . GLY   B 1 148 ? -43.153 -26.091 -32.473 1.00 14.33 ?  1185 GLY   B O   1 
ATOM   3350 N N   . LEU   B 1 149 ? -43.539 -28.208 -33.129 1.00 13.61 ?  1186 LEU   B N   1 
ATOM   3351 C CA  . LEU   B 1 149 ? -42.311 -28.700 -32.515 1.00 15.08 ?  1186 LEU   B CA  1 
ATOM   3352 C C   . LEU   B 1 149 ? -41.083 -28.228 -33.283 1.00 12.42 ?  1186 LEU   B C   1 
ATOM   3353 O O   . LEU   B 1 149 ? -40.044 -27.931 -32.682 1.00 12.65 ?  1186 LEU   B O   1 
ATOM   3354 C CB  . LEU   B 1 149 ? -42.338 -30.226 -32.438 1.00 11.52 ?  1186 LEU   B CB  1 
ATOM   3355 C CG  . LEU   B 1 149 ? -41.206 -30.881 -31.646 1.00 13.16 ?  1186 LEU   B CG  1 
ATOM   3356 C CD1 . LEU   B 1 149 ? -41.053 -30.224 -30.282 1.00 9.13  ?  1186 LEU   B CD1 1 
ATOM   3357 C CD2 . LEU   B 1 149 ? -41.451 -32.376 -31.507 1.00 15.69 ?  1186 LEU   B CD2 1 
ATOM   3358 N N   . GLN   B 1 150 ? -41.183 -28.152 -34.611 1.00 12.80 ?  1187 GLN   B N   1 
ATOM   3359 C CA  . GLN   B 1 150 ? -40.047 -27.707 -35.409 1.00 9.81  ?  1187 GLN   B CA  1 
ATOM   3360 C C   . GLN   B 1 150 ? -39.778 -26.220 -35.210 1.00 10.73 ?  1187 GLN   B C   1 
ATOM   3361 O O   . GLN   B 1 150 ? -38.619 -25.807 -35.089 1.00 9.70  ?  1187 GLN   B O   1 
ATOM   3362 C CB  . GLN   B 1 150 ? -40.288 -28.018 -36.885 1.00 7.96  ?  1187 GLN   B CB  1 
ATOM   3363 C CG  . GLN   B 1 150 ? -40.351 -29.493 -37.226 1.00 11.50 ?  1187 GLN   B CG  1 
ATOM   3364 C CD  . GLN   B 1 150 ? -40.363 -29.733 -38.722 1.00 11.41 ?  1187 GLN   B CD  1 
ATOM   3365 O OE1 . GLN   B 1 150 ? -39.876 -28.910 -39.496 1.00 8.93  ?  1187 GLN   B OE1 1 
ATOM   3366 N NE2 . GLN   B 1 150 ? -40.924 -30.862 -39.138 1.00 13.52 ?  1187 GLN   B NE2 1 
ATOM   3367 N N   . VAL   B 1 151 ? -40.832 -25.399 -35.175 1.00 13.73 ?  1188 VAL   B N   1 
ATOM   3368 C CA  . VAL   B 1 151 ? -40.653 -23.975 -34.897 1.00 14.99 ?  1188 VAL   B CA  1 
ATOM   3369 C C   . VAL   B 1 151 ? -39.999 -23.784 -33.535 1.00 14.94 ?  1188 VAL   B C   1 
ATOM   3370 O O   . VAL   B 1 151 ? -39.065 -22.988 -33.380 1.00 13.76 ?  1188 VAL   B O   1 
ATOM   3371 C CB  . VAL   B 1 151 ? -41.998 -23.230 -34.977 1.00 15.37 ?  1188 VAL   B CB  1 
ATOM   3372 C CG1 . VAL   B 1 151 ? -41.830 -21.786 -34.524 1.00 18.38 ?  1188 VAL   B CG1 1 
ATOM   3373 C CG2 . VAL   B 1 151 ? -42.559 -23.276 -36.385 1.00 15.17 ?  1188 VAL   B CG2 1 
ATOM   3374 N N   . ALA   B 1 152 ? -40.475 -24.525 -32.531 1.00 12.28 ?  1189 ALA   B N   1 
ATOM   3375 C CA  . ALA   B 1 152 ? -39.961 -24.364 -31.174 1.00 12.32 ?  1189 ALA   B CA  1 
ATOM   3376 C C   . ALA   B 1 152 ? -38.468 -24.656 -31.103 1.00 11.59 ?  1189 ALA   B C   1 
ATOM   3377 O O   . ALA   B 1 152 ? -37.730 -23.972 -30.385 1.00 13.97 ?  1189 ALA   B O   1 
ATOM   3378 C CB  . ALA   B 1 152 ? -40.732 -25.267 -30.213 1.00 10.20 ?  1189 ALA   B CB  1 
ATOM   3379 N N   . LYS   B 1 153 ? -38.003 -25.665 -31.843 1.00 12.06 ?  1190 LYS   B N   1 
ATOM   3380 C CA  . LYS   B 1 153 ? -36.581 -25.995 -31.835 1.00 14.05 ?  1190 LYS   B CA  1 
ATOM   3381 C C   . LYS   B 1 153 ? -35.753 -24.857 -32.420 1.00 14.23 ?  1190 LYS   B C   1 
ATOM   3382 O O   . LYS   B 1 153 ? -34.777 -24.406 -31.809 1.00 13.55 ?  1190 LYS   B O   1 
ATOM   3383 C CB  . LYS   B 1 153 ? -36.338 -27.292 -32.607 1.00 10.52 ?  1190 LYS   B CB  1 
ATOM   3384 C CG  . LYS   B 1 153 ? -36.962 -28.521 -31.969 1.00 14.13 ?  1190 LYS   B CG  1 
ATOM   3385 C CD  . LYS   B 1 153 ? -37.107 -29.648 -32.979 1.00 14.08 ?  1190 LYS   B CD  1 
ATOM   3386 C CE  . LYS   B 1 153 ? -37.354 -30.981 -32.291 1.00 14.64 ?  1190 LYS   B CE  1 
ATOM   3387 N NZ  . LYS   B 1 153 ? -37.171 -32.125 -33.226 1.00 13.80 ?  1190 LYS   B NZ  1 
ATOM   3388 N N   . GLY   B 1 154 ? -36.129 -24.382 -33.609 1.00 12.81 ?  1191 GLY   B N   1 
ATOM   3389 C CA  . GLY   B 1 154 ? -35.441 -23.256 -34.216 1.00 10.04 ?  1191 GLY   B CA  1 
ATOM   3390 C C   . GLY   B 1 154 ? -35.545 -21.976 -33.416 1.00 12.24 ?  1191 GLY   B C   1 
ATOM   3391 O O   . GLY   B 1 154 ? -34.667 -21.114 -33.521 1.00 14.81 ?  1191 GLY   B O   1 
ATOM   3392 N N   . MET   B 1 155 ? -36.606 -21.828 -32.621 1.00 12.21 ?  1192 MET   B N   1 
ATOM   3393 C CA  . MET   B 1 155 ? -36.704 -20.691 -31.715 1.00 13.70 ?  1192 MET   B CA  1 
ATOM   3394 C C   . MET   B 1 155 ? -35.919 -20.930 -30.432 1.00 13.89 ?  1192 MET   B C   1 
ATOM   3395 O O   . MET   B 1 155 ? -35.362 -19.984 -29.864 1.00 12.87 ?  1192 MET   B O   1 
ATOM   3396 C CB  . MET   B 1 155 ? -38.171 -20.400 -31.397 1.00 11.93 ?  1192 MET   B CB  1 
ATOM   3397 C CG  . MET   B 1 155 ? -38.935 -19.734 -32.532 1.00 15.22 ?  1192 MET   B CG  1 
ATOM   3398 S SD  . MET   B 1 155 ? -38.235 -18.146 -33.024 1.00 14.92 ?  1192 MET   B SD  1 
ATOM   3399 C CE  . MET   B 1 155 ? -38.287 -17.263 -31.469 1.00 9.19  ?  1192 MET   B CE  1 
ATOM   3400 N N   . LYS   B 1 156 ? -35.867 -22.181 -29.968 1.00 13.07 ?  1193 LYS   B N   1 
ATOM   3401 C CA  . LYS   B 1 156 ? -35.006 -22.530 -28.842 1.00 14.54 ?  1193 LYS   B CA  1 
ATOM   3402 C C   . LYS   B 1 156 ? -33.544 -22.244 -29.164 1.00 15.11 ?  1193 LYS   B C   1 
ATOM   3403 O O   . LYS   B 1 156 ? -32.777 -21.816 -28.293 1.00 10.79 ?  1193 LYS   B O   1 
ATOM   3404 C CB  . LYS   B 1 156 ? -35.215 -24.002 -28.479 1.00 10.73 ?  1193 LYS   B CB  1 
ATOM   3405 C CG  . LYS   B 1 156 ? -34.188 -24.607 -27.541 1.00 12.48 ?  1193 LYS   B CG  1 
ATOM   3406 C CD  . LYS   B 1 156 ? -34.623 -26.004 -27.114 1.00 12.36 ?  1193 LYS   B CD  1 
ATOM   3407 C CE  . LYS   B 1 156 ? -33.519 -26.747 -26.384 1.00 11.04 ?  1193 LYS   B CE  1 
ATOM   3408 N NZ  . LYS   B 1 156 ? -32.369 -27.034 -27.282 1.00 9.44  ?  1193 LYS   B NZ  1 
ATOM   3409 N N   . TYR   B 1 157 ? -33.148 -22.461 -30.418 1.00 10.95 ?  1194 TYR   B N   1 
ATOM   3410 C CA  . TYR   B 1 157 ? -31.798 -22.119 -30.854 1.00 10.48 ?  1194 TYR   B CA  1 
ATOM   3411 C C   . TYR   B 1 157 ? -31.588 -20.616 -30.856 1.00 11.01 ?  1194 TYR   B C   1 
ATOM   3412 O O   . TYR   B 1 157 ? -30.617 -20.108 -30.283 1.00 14.30 ?  1194 TYR   B O   1 
ATOM   3413 C CB  . TYR   B 1 157 ? -31.557 -22.683 -32.251 1.00 11.02 ?  1194 TYR   B CB  1 
ATOM   3414 C CG  . TYR   B 1 157 ? -30.237 -22.304 -32.885 1.00 11.82 ?  1194 TYR   B CG  1 
ATOM   3415 C CD1 . TYR   B 1 157 ? -29.035 -22.485 -32.212 1.00 9.18  ?  1194 TYR   B CD1 1 
ATOM   3416 C CD2 . TYR   B 1 157 ? -30.194 -21.776 -34.166 1.00 14.01 ?  1194 TYR   B CD2 1 
ATOM   3417 C CE1 . TYR   B 1 157 ? -27.828 -22.150 -32.807 1.00 11.56 ?  1194 TYR   B CE1 1 
ATOM   3418 C CE2 . TYR   B 1 157 ? -28.995 -21.450 -34.770 1.00 12.32 ?  1194 TYR   B CE2 1 
ATOM   3419 C CZ  . TYR   B 1 157 ? -27.817 -21.635 -34.086 1.00 11.15 ?  1194 TYR   B CZ  1 
ATOM   3420 O OH  . TYR   B 1 157 ? -26.631 -21.291 -34.689 1.00 9.31  ?  1194 TYR   B OH  1 
ATOM   3421 N N   . LEU   B 1 158 ? -32.479 -19.888 -31.524 1.00 11.53 ?  1195 LEU   B N   1 
ATOM   3422 C CA  . LEU   B 1 158 ? -32.337 -18.442 -31.590 1.00 9.11  ?  1195 LEU   B CA  1 
ATOM   3423 C C   . LEU   B 1 158 ? -32.340 -17.820 -30.199 1.00 10.80 ?  1195 LEU   B C   1 
ATOM   3424 O O   . LEU   B 1 158 ? -31.624 -16.845 -29.948 1.00 12.53 ?  1195 LEU   B O   1 
ATOM   3425 C CB  . LEU   B 1 158 ? -33.452 -17.841 -32.442 1.00 8.63  ?  1195 LEU   B CB  1 
ATOM   3426 C CG  . LEU   B 1 158 ? -33.417 -18.053 -33.954 1.00 9.46  ?  1195 LEU   B CG  1 
ATOM   3427 C CD1 . LEU   B 1 158 ? -34.715 -17.547 -34.557 1.00 7.16  ?  1195 LEU   B CD1 1 
ATOM   3428 C CD2 . LEU   B 1 158 ? -32.218 -17.359 -34.576 1.00 10.36 ?  1195 LEU   B CD2 1 
ATOM   3429 N N   . ALA   B 1 159 ? -33.144 -18.360 -29.280 1.00 11.94 ?  1196 ALA   B N   1 
ATOM   3430 C CA  . ALA   B 1 159 ? -33.139 -17.837 -27.918 1.00 11.86 ?  1196 ALA   B CA  1 
ATOM   3431 C C   . ALA   B 1 159 ? -31.838 -18.167 -27.200 1.00 9.27  ?  1196 ALA   B C   1 
ATOM   3432 O O   . ALA   B 1 159 ? -31.401 -17.409 -26.327 1.00 8.40  ?  1196 ALA   B O   1 
ATOM   3433 C CB  . ALA   B 1 159 ? -34.332 -18.386 -27.135 1.00 8.06  ?  1196 ALA   B CB  1 
ATOM   3434 N N   . SER   B 1 160 ? -31.213 -19.296 -27.544 1.00 12.79 ?  1197 SER   B N   1 
ATOM   3435 C CA  . SER   B 1 160 ? -29.948 -19.667 -26.921 1.00 12.91 ?  1197 SER   B CA  1 
ATOM   3436 C C   . SER   B 1 160 ? -28.801 -18.841 -27.485 1.00 10.88 ?  1197 SER   B C   1 
ATOM   3437 O O   . SER   B 1 160 ? -27.891 -18.449 -26.746 1.00 9.48  ?  1197 SER   B O   1 
ATOM   3438 C CB  . SER   B 1 160 ? -29.685 -21.161 -27.110 1.00 11.23 ?  1197 SER   B CB  1 
ATOM   3439 O OG  . SER   B 1 160 ? -29.393 -21.458 -28.463 1.00 12.06 ?  1197 SER   B OG  1 
ATOM   3440 N N   . LYS   B 1 161 ? -28.832 -18.560 -28.785 1.00 9.05  ?  1198 LYS   B N   1 
ATOM   3441 C CA  . LYS   B 1 161 ? -27.954 -17.557 -29.367 1.00 11.47 ?  1198 LYS   B CA  1 
ATOM   3442 C C   . LYS   B 1 161 ? -28.385 -16.139 -29.007 1.00 10.87 ?  1198 LYS   B C   1 
ATOM   3443 O O   . LYS   B 1 161 ? -27.803 -15.176 -29.519 1.00 9.72  ?  1198 LYS   B O   1 
ATOM   3444 C CB  . LYS   B 1 161 ? -27.897 -17.723 -30.888 1.00 10.23 ?  1198 LYS   B CB  1 
ATOM   3445 C CG  . LYS   B 1 161 ? -26.850 -18.721 -31.364 1.00 13.76 ?  1198 LYS   B CG  1 
ATOM   3446 C CD  . LYS   B 1 161 ? -25.534 -18.546 -30.619 1.00 13.17 ?  1198 LYS   B CD  1 
ATOM   3447 C CE  . LYS   B 1 161 ? -24.373 -19.151 -31.390 1.00 10.85 ?  1198 LYS   B CE  1 
ATOM   3448 N NZ  . LYS   B 1 161 ? -24.097 -18.413 -32.651 1.00 10.48 ?  1198 LYS   B NZ  1 
ATOM   3449 N N   . LYS   B 1 162 ? -29.398 -16.006 -28.145 1.00 12.76 ?  1199 LYS   B N   1 
ATOM   3450 C CA  . LYS   B 1 162 ? -29.855 -14.724 -27.610 1.00 10.72 ?  1199 LYS   B CA  1 
ATOM   3451 C C   . LYS   B 1 162 ? -30.313 -13.777 -28.715 1.00 13.50 ?  1199 LYS   B C   1 
ATOM   3452 O O   . LYS   B 1 162 ? -30.228 -12.554 -28.577 1.00 21.50 ?  1199 LYS   B O   1 
ATOM   3453 C CB  . LYS   B 1 162 ? -28.776 -14.076 -26.737 1.00 12.42 ?  1199 LYS   B CB  1 
ATOM   3454 C CG  . LYS   B 1 162 ? -28.207 -15.041 -25.702 1.00 12.35 ?  1199 LYS   B CG  1 
ATOM   3455 C CD  . LYS   B 1 162 ? -27.204 -14.376 -24.777 1.00 14.74 ?  1199 LYS   B CD  1 
ATOM   3456 C CE  . LYS   B 1 162 ? -27.345 -14.907 -23.358 1.00 17.13 ?  1199 LYS   B CE  1 
ATOM   3457 N NZ  . LYS   B 1 162 ? -27.947 -13.903 -22.439 1.00 17.67 ?  1199 LYS   B NZ  1 
ATOM   3458 N N   . PHE   B 1 163 ? -30.806 -14.339 -29.816 1.00 14.95 ?  1200 PHE   B N   1 
ATOM   3459 C CA  . PHE   B 1 163 ? -31.420 -13.555 -30.875 1.00 14.36 ?  1200 PHE   B CA  1 
ATOM   3460 C C   . PHE   B 1 163 ? -32.909 -13.403 -30.602 1.00 13.64 ?  1200 PHE   B C   1 
ATOM   3461 O O   . PHE   B 1 163 ? -33.560 -14.323 -30.101 1.00 12.77 ?  1200 PHE   B O   1 
ATOM   3462 C CB  . PHE   B 1 163 ? -31.202 -14.205 -32.242 1.00 13.94 ?  1200 PHE   B CB  1 
ATOM   3463 C CG  . PHE   B 1 163 ? -31.680 -13.364 -33.394 1.00 15.00 ?  1200 PHE   B CG  1 
ATOM   3464 C CD1 . PHE   B 1 163 ? -30.859 -12.399 -33.952 1.00 11.18 ?  1200 PHE   B CD1 1 
ATOM   3465 C CD2 . PHE   B 1 163 ? -32.952 -13.539 -33.921 1.00 13.99 ?  1200 PHE   B CD2 1 
ATOM   3466 C CE1 . PHE   B 1 163 ? -31.295 -11.622 -35.013 1.00 17.25 ?  1200 PHE   B CE1 1 
ATOM   3467 C CE2 . PHE   B 1 163 ? -33.394 -12.764 -34.982 1.00 12.02 ?  1200 PHE   B CE2 1 
ATOM   3468 C CZ  . PHE   B 1 163 ? -32.563 -11.805 -35.528 1.00 16.94 ?  1200 PHE   B CZ  1 
ATOM   3469 N N   . VAL   B 1 164 ? -33.441 -12.235 -30.945 1.00 17.18 ?  1201 VAL   B N   1 
ATOM   3470 C CA  . VAL   B 1 164 ? -34.818 -11.860 -30.651 1.00 17.09 ?  1201 VAL   B CA  1 
ATOM   3471 C C   . VAL   B 1 164 ? -35.503 -11.607 -31.990 1.00 18.62 ?  1201 VAL   B C   1 
ATOM   3472 O O   . VAL   B 1 164 ? -35.181 -10.636 -32.687 1.00 16.19 ?  1201 VAL   B O   1 
ATOM   3473 C CB  . VAL   B 1 164 ? -34.880 -10.633 -29.730 1.00 15.29 ?  1201 VAL   B CB  1 
ATOM   3474 C CG1 . VAL   B 1 164 ? -36.281 -10.367 -29.266 1.00 16.67 ?  1201 VAL   B CG1 1 
ATOM   3475 C CG2 . VAL   B 1 164 ? -33.983 -10.846 -28.519 1.00 17.59 ?  1201 VAL   B CG2 1 
ATOM   3476 N N   . HIS   B 1 165 ? -36.434 -12.492 -32.357 1.00 12.64 ?  1202 HIS   B N   1 
ATOM   3477 C CA  . HIS   B 1 165 ? -37.002 -12.492 -33.705 1.00 14.32 ?  1202 HIS   B CA  1 
ATOM   3478 C C   . HIS   B 1 165 ? -37.914 -11.290 -33.930 1.00 13.41 ?  1202 HIS   B C   1 
ATOM   3479 O O   . HIS   B 1 165 ? -37.737 -10.536 -34.894 1.00 14.54 ?  1202 HIS   B O   1 
ATOM   3480 C CB  . HIS   B 1 165 ? -37.756 -13.805 -33.943 1.00 13.30 ?  1202 HIS   B CB  1 
ATOM   3481 C CG  . HIS   B 1 165 ? -38.128 -14.048 -35.373 1.00 13.69 ?  1202 HIS   B CG  1 
ATOM   3482 N ND1 . HIS   B 1 165 ? -39.254 -13.503 -35.951 1.00 13.17 ?  1202 HIS   B ND1 1 
ATOM   3483 C CD2 . HIS   B 1 165 ? -37.537 -14.796 -36.336 1.00 11.55 ?  1202 HIS   B CD2 1 
ATOM   3484 C CE1 . HIS   B 1 165 ? -39.336 -13.895 -37.209 1.00 13.17 ?  1202 HIS   B CE1 1 
ATOM   3485 N NE2 . HIS   B 1 165 ? -38.306 -14.682 -37.468 1.00 10.82 ?  1202 HIS   B NE2 1 
ATOM   3486 N N   . ARG   B 1 166 ? -38.912 -11.116 -33.061 1.00 12.14 ?  1203 ARG   B N   1 
ATOM   3487 C CA  . ARG   B 1 166 ? -39.873 -10.017 -32.974 1.00 16.09 ?  1203 ARG   B CA  1 
ATOM   3488 C C   . ARG   B 1 166 ? -41.064 -10.176 -33.916 1.00 14.38 ?  1203 ARG   B C   1 
ATOM   3489 O O   . ARG   B 1 166 ? -42.061 -9.478  -33.734 1.00 16.16 ?  1203 ARG   B O   1 
ATOM   3490 C CB  . ARG   B 1 166 ? -39.245 -8.628  -33.211 1.00 17.45 ?  1203 ARG   B CB  1 
ATOM   3491 C CG  . ARG   B 1 166 ? -38.183 -8.238  -32.200 1.00 20.19 ?  1203 ARG   B CG  1 
ATOM   3492 C CD  . ARG   B 1 166 ? -37.001 -7.571  -32.876 1.00 24.36 ?  1203 ARG   B CD  1 
ATOM   3493 N NE  . ARG   B 1 166 ? -37.177 -6.125  -32.943 1.00 31.39 ?  1203 ARG   B NE  1 
ATOM   3494 C CZ  . ARG   B 1 166 ? -36.604 -5.256  -32.121 1.00 39.67 ?  1203 ARG   B CZ  1 
ATOM   3495 N NH1 . ARG   B 1 166 ? -35.800 -5.649  -31.146 1.00 38.69 ?  1203 ARG   B NH1 1 
ATOM   3496 N NH2 . ARG   B 1 166 ? -36.846 -3.958  -32.281 1.00 33.18 ?  1203 ARG   B NH2 1 
ATOM   3497 N N   . ASP   B 1 167 ? -41.018 -11.068 -34.900 1.00 13.14 ?  1204 ASP   B N   1 
ATOM   3498 C CA  . ASP   B 1 167 ? -42.084 -11.153 -35.890 1.00 15.16 ?  1204 ASP   B CA  1 
ATOM   3499 C C   . ASP   B 1 167 ? -42.519 -12.597 -36.102 1.00 15.75 ?  1204 ASP   B C   1 
ATOM   3500 O O   . ASP   B 1 167 ? -42.860 -13.005 -37.217 1.00 12.60 ?  1204 ASP   B O   1 
ATOM   3501 C CB  . ASP   B 1 167 ? -41.643 -10.517 -37.205 1.00 10.29 ?  1204 ASP   B CB  1 
ATOM   3502 C CG  . ASP   B 1 167 ? -42.811 -10.102 -38.073 1.00 15.74 ?  1204 ASP   B CG  1 
ATOM   3503 O OD1 . ASP   B 1 167 ? -43.919 -9.916  -37.530 1.00 13.06 ?  1204 ASP   B OD1 1 
ATOM   3504 O OD2 . ASP   B 1 167 ? -42.619 -9.960  -39.300 1.00 20.84 -1 1204 ASP   B OD2 1 
ATOM   3505 N N   . LEU   B 1 168 ? -42.523 -13.393 -35.034 1.00 16.85 ?  1205 LEU   B N   1 
ATOM   3506 C CA  . LEU   B 1 168 ? -42.858 -14.809 -35.150 1.00 17.19 ?  1205 LEU   B CA  1 
ATOM   3507 C C   . LEU   B 1 168 ? -44.332 -14.981 -35.501 1.00 17.51 ?  1205 LEU   B C   1 
ATOM   3508 O O   . LEU   B 1 168 ? -45.215 -14.614 -34.717 1.00 14.97 ?  1205 LEU   B O   1 
ATOM   3509 C CB  . LEU   B 1 168 ? -42.526 -15.543 -33.853 1.00 18.71 ?  1205 LEU   B CB  1 
ATOM   3510 C CG  . LEU   B 1 168 ? -42.763 -17.054 -33.867 1.00 15.33 ?  1205 LEU   B CG  1 
ATOM   3511 C CD1 . LEU   B 1 168 ? -42.029 -17.695 -35.034 1.00 14.45 ?  1205 LEU   B CD1 1 
ATOM   3512 C CD2 . LEU   B 1 168 ? -42.324 -17.672 -32.552 1.00 12.76 ?  1205 LEU   B CD2 1 
ATOM   3513 N N   . ALA   B 1 169 ? -44.592 -15.539 -36.680 1.00 17.34 ?  1206 ALA   B N   1 
ATOM   3514 C CA  . ALA   B 1 169 ? -45.944 -15.827 -37.135 1.00 16.11 ?  1206 ALA   B CA  1 
ATOM   3515 C C   . ALA   B 1 169 ? -45.863 -16.893 -38.216 1.00 14.61 ?  1206 ALA   B C   1 
ATOM   3516 O O   . ALA   B 1 169 ? -44.805 -17.120 -38.809 1.00 16.43 ?  1206 ALA   B O   1 
ATOM   3517 C CB  . ALA   B 1 169 ? -46.649 -14.571 -37.657 1.00 15.19 ?  1206 ALA   B CB  1 
ATOM   3518 N N   . ALA   B 1 170 ? -47.000 -17.547 -38.465 1.00 15.22 ?  1207 ALA   B N   1 
ATOM   3519 C CA  . ALA   B 1 170 ? -47.028 -18.634 -39.439 1.00 14.64 ?  1207 ALA   B CA  1 
ATOM   3520 C C   . ALA   B 1 170 ? -46.702 -18.131 -40.840 1.00 14.93 ?  1207 ALA   B C   1 
ATOM   3521 O O   . ALA   B 1 170 ? -46.060 -18.835 -41.628 1.00 16.93 ?  1207 ALA   B O   1 
ATOM   3522 C CB  . ALA   B 1 170 ? -48.390 -19.324 -39.413 1.00 11.53 ?  1207 ALA   B CB  1 
ATOM   3523 N N   . ARG   B 1 171 ? -47.125 -16.909 -41.166 1.00 13.19 ?  1208 ARG   B N   1 
ATOM   3524 C CA  . ARG   B 1 171 ? -46.745 -16.305 -42.438 1.00 14.68 ?  1208 ARG   B CA  1 
ATOM   3525 C C   . ARG   B 1 171 ? -45.240 -16.096 -42.552 1.00 12.51 ?  1208 ARG   B C   1 
ATOM   3526 O O   . ARG   B 1 171 ? -44.735 -15.891 -43.661 1.00 11.67 ?  1208 ARG   B O   1 
ATOM   3527 C CB  . ARG   B 1 171 ? -47.462 -14.966 -42.608 1.00 13.02 ?  1208 ARG   B CB  1 
ATOM   3528 C CG  . ARG   B 1 171 ? -47.058 -13.954 -41.554 1.00 10.74 ?  1208 ARG   B CG  1 
ATOM   3529 C CD  . ARG   B 1 171 ? -47.807 -12.646 -41.674 1.00 12.44 ?  1208 ARG   B CD  1 
ATOM   3530 N NE  . ARG   B 1 171 ? -47.312 -11.683 -40.700 1.00 13.21 ?  1208 ARG   B NE  1 
ATOM   3531 C CZ  . ARG   B 1 171 ? -47.798 -11.545 -39.475 1.00 13.64 ?  1208 ARG   B CZ  1 
ATOM   3532 N NH1 . ARG   B 1 171 ? -48.825 -12.264 -39.056 1.00 14.63 ?  1208 ARG   B NH1 1 
ATOM   3533 N NH2 . ARG   B 1 171 ? -47.236 -10.667 -38.649 1.00 16.58 ?  1208 ARG   B NH2 1 
ATOM   3534 N N   . ASN   B 1 172 ? -44.515 -16.137 -41.435 1.00 9.38  ?  1209 ASN   B N   1 
ATOM   3535 C CA  . ASN   B 1 172 ? -43.088 -15.853 -41.413 1.00 12.45 ?  1209 ASN   B CA  1 
ATOM   3536 C C   . ASN   B 1 172 ? -42.229 -17.096 -41.223 1.00 12.11 ?  1209 ASN   B C   1 
ATOM   3537 O O   . ASN   B 1 172 ? -41.001 -16.980 -41.164 1.00 13.06 ?  1209 ASN   B O   1 
ATOM   3538 C CB  . ASN   B 1 172 ? -42.778 -14.828 -40.311 1.00 11.78 ?  1209 ASN   B CB  1 
ATOM   3539 C CG  . ASN   B 1 172 ? -43.283 -13.432 -40.649 1.00 11.61 ?  1209 ASN   B CG  1 
ATOM   3540 O OD1 . ASN   B 1 172 ? -43.375 -13.060 -41.818 1.00 10.99 ?  1209 ASN   B OD1 1 
ATOM   3541 N ND2 . ASN   B 1 172 ? -43.606 -12.654 -39.622 1.00 10.61 ?  1209 ASN   B ND2 1 
ATOM   3542 N N   . CYS   B 1 173 ? -42.833 -18.274 -41.113 1.00 12.14 ?  1210 CYS   B N   1 
ATOM   3543 C CA  . CYS   B 1 173 ? -42.113 -19.535 -41.009 1.00 14.09 ?  1210 CYS   B CA  1 
ATOM   3544 C C   . CYS   B 1 173 ? -42.335 -20.285 -42.313 1.00 11.32 ?  1210 CYS   B C   1 
ATOM   3545 O O   . CYS   B 1 173 ? -43.473 -20.375 -42.784 1.00 12.21 ?  1210 CYS   B O   1 
ATOM   3546 C CB  . CYS   B 1 173 ? -42.612 -20.360 -39.819 1.00 10.52 ?  1210 CYS   B CB  1 
ATOM   3547 S SG  . CYS   B 1 173 ? -42.135 -19.741 -38.190 1.00 15.50 ?  1210 CYS   B SG  1 
ATOM   3548 N N   . MET   B 1 174 ? -41.266 -20.800 -42.911 1.00 10.81 ?  1211 MET   B N   1 
ATOM   3549 C CA  . MET   B 1 174 ? -41.354 -21.320 -44.266 1.00 10.93 ?  1211 MET   B CA  1 
ATOM   3550 C C   . MET   B 1 174 ? -41.051 -22.815 -44.278 1.00 9.27  ?  1211 MET   B C   1 
ATOM   3551 O O   . MET   B 1 174 ? -40.594 -23.390 -43.286 1.00 11.28 ?  1211 MET   B O   1 
ATOM   3552 C CB  . MET   B 1 174 ? -40.400 -20.559 -45.184 1.00 9.73  ?  1211 MET   B CB  1 
ATOM   3553 C CG  . MET   B 1 174 ? -40.667 -19.064 -45.199 1.00 17.40 ?  1211 MET   B CG  1 
ATOM   3554 S SD  . MET   B 1 174 ? -39.977 -18.238 -46.634 1.00 22.84 ?  1211 MET   B SD  1 
ATOM   3555 C CE  . MET   B 1 174 ? -41.351 -18.347 -47.771 1.00 18.20 ?  1211 MET   B CE  1 
ATOM   3556 N N   . LEU   B 1 175 ? -41.328 -23.453 -45.417 1.00 8.28  ?  1212 LEU   B N   1 
ATOM   3557 C CA  . LEU   B 1 175 ? -41.255 -24.903 -45.562 1.00 11.75 ?  1212 LEU   B CA  1 
ATOM   3558 C C   . LEU   B 1 175 ? -40.447 -25.274 -46.795 1.00 12.91 ?  1212 LEU   B C   1 
ATOM   3559 O O   . LEU   B 1 175 ? -40.595 -24.654 -47.852 1.00 11.15 ?  1212 LEU   B O   1 
ATOM   3560 C CB  . LEU   B 1 175 ? -42.650 -25.522 -45.686 1.00 8.70  ?  1212 LEU   B CB  1 
ATOM   3561 C CG  . LEU   B 1 175 ? -43.382 -25.883 -44.397 1.00 12.50 ?  1212 LEU   B CG  1 
ATOM   3562 C CD1 . LEU   B 1 175 ? -44.070 -24.669 -43.811 1.00 13.03 ?  1212 LEU   B CD1 1 
ATOM   3563 C CD2 . LEU   B 1 175 ? -44.379 -27.005 -44.653 1.00 12.50 ?  1212 LEU   B CD2 1 
ATOM   3564 N N   . ASP   B 1 176 ? -39.621 -26.313 -46.668 1.00 14.60 ?  1213 ASP   B N   1 
ATOM   3565 C CA  . ASP   B 1 176 ? -38.811 -26.818 -47.767 1.00 15.92 ?  1213 ASP   B CA  1 
ATOM   3566 C C   . ASP   B 1 176 ? -39.405 -28.120 -48.312 1.00 15.29 ?  1213 ASP   B C   1 
ATOM   3567 O O   . ASP   B 1 176 ? -40.515 -28.522 -47.944 1.00 13.97 ?  1213 ASP   B O   1 
ATOM   3568 C CB  . ASP   B 1 176 ? -37.356 -26.987 -47.314 1.00 16.72 ?  1213 ASP   B CB  1 
ATOM   3569 C CG  . ASP   B 1 176 ? -37.151 -28.188 -46.400 1.00 15.25 ?  1213 ASP   B CG  1 
ATOM   3570 O OD1 . ASP   B 1 176 ? -38.116 -28.628 -45.741 1.00 16.39 ?  1213 ASP   B OD1 1 
ATOM   3571 O OD2 . ASP   B 1 176 ? -36.009 -28.685 -46.326 1.00 15.94 -1 1213 ASP   B OD2 1 
ATOM   3572 N N   . GLU   B 1 177 ? -38.835 -28.759 -49.309 1.00 16.49 ?  1214 GLU   B N   1 
ATOM   3573 C CA  . GLU   B 1 177 ? -39.306 -30.004 -49.926 1.00 19.53 ?  1214 GLU   B CA  1 
ATOM   3574 C C   . GLU   B 1 177 ? -39.602 -31.153 -49.027 1.00 17.24 ?  1214 GLU   B C   1 
ATOM   3575 O O   . GLU   B 1 177 ? -40.469 -31.915 -49.301 1.00 17.52 ?  1214 GLU   B O   1 
ATOM   3576 C CB  . GLU   B 1 177 ? -38.226 -30.490 -50.824 1.00 22.45 ?  1214 GLU   B CB  1 
ATOM   3577 C CG  . GLU   B 1 177 ? -37.600 -29.482 -51.720 1.00 26.72 ?  1214 GLU   B CG  1 
ATOM   3578 C CD  . GLU   B 1 177 ? -36.250 -29.947 -52.149 1.00 28.74 ?  1214 GLU   B CD  1 
ATOM   3579 O OE1 . GLU   B 1 177 ? -35.441 -30.229 -51.254 1.00 29.32 ?  1214 GLU   B OE1 1 
ATOM   3580 O OE2 . GLU   B 1 177 ? -36.023 -30.047 -53.365 1.00 32.35 -1 1214 GLU   B OE2 1 
ATOM   3581 N N   . LYS   B 1 178 ? -38.898 -31.221 -47.922 1.00 20.75 ?  1215 LYS   B N   1 
ATOM   3582 C CA  . LYS   B 1 178 ? -39.001 -32.281 -47.016 1.00 15.02 ?  1215 LYS   B CA  1 
ATOM   3583 C C   . LYS   B 1 178 ? -39.774 -31.876 -45.834 1.00 14.32 ?  1215 LYS   B C   1 
ATOM   3584 O O   . LYS   B 1 178 ? -39.636 -32.450 -44.780 1.00 15.82 ?  1215 LYS   B O   1 
ATOM   3585 C CB  . LYS   B 1 178 ? -37.585 -32.639 -46.682 1.00 12.51 ?  1215 LYS   B CB  1 
ATOM   3586 N N   . PHE   B 1 179 ? -40.540 -30.836 -45.987 1.00 14.70 ?  1216 PHE   B N   1 
ATOM   3587 C CA  . PHE   B 1 179 ? -41.430 -30.379 -44.931 1.00 17.20 ?  1216 PHE   B CA  1 
ATOM   3588 C C   . PHE   B 1 179 ? -40.783 -29.899 -43.655 1.00 12.33 ?  1216 PHE   B C   1 
ATOM   3589 O O   . PHE   B 1 179 ? -41.311 -30.018 -42.583 1.00 13.03 ?  1216 PHE   B O   1 
ATOM   3590 C CB  . PHE   B 1 179 ? -42.792 -31.234 -44.804 1.00 19.54 ?  1216 PHE   B CB  1 
ATOM   3591 C CG  . PHE   B 1 179 ? -43.442 -31.549 -46.103 1.00 15.83 ?  1216 PHE   B CG  1 
ATOM   3592 C CD1 . PHE   B 1 179 ? -43.041 -32.633 -46.852 1.00 21.04 ?  1216 PHE   B CD1 1 
ATOM   3593 C CD2 . PHE   B 1 179 ? -44.463 -30.773 -46.570 1.00 23.51 ?  1216 PHE   B CD2 1 
ATOM   3594 C CE1 . PHE   B 1 179 ? -43.631 -32.922 -48.058 1.00 24.79 ?  1216 PHE   B CE1 1 
ATOM   3595 C CE2 . PHE   B 1 179 ? -45.073 -31.066 -47.767 1.00 23.15 ?  1216 PHE   B CE2 1 
ATOM   3596 C CZ  . PHE   B 1 179 ? -44.655 -32.137 -48.516 1.00 23.32 ?  1216 PHE   B CZ  1 
ATOM   3597 N N   . THR   B 1 180 ? -39.641 -29.294 -43.825 1.00 14.85 ?  1217 THR   B N   1 
ATOM   3598 C CA  . THR   B 1 180 ? -38.962 -28.709 -42.688 1.00 15.31 ?  1217 THR   B CA  1 
ATOM   3599 C C   . THR   B 1 180 ? -39.381 -27.246 -42.558 1.00 13.69 ?  1217 THR   B C   1 
ATOM   3600 O O   . THR   B 1 180 ? -39.250 -26.462 -43.478 1.00 15.53 ?  1217 THR   B O   1 
ATOM   3601 C CB  . THR   B 1 180 ? -37.378 -28.875 -42.685 1.00 16.05 ?  1217 THR   B CB  1 
ATOM   3602 O OG1 . THR   B 1 180 ? -37.021 -30.220 -42.999 1.00 14.94 ?  1217 THR   B OG1 1 
ATOM   3603 C CG2 . THR   B 1 180 ? -36.772 -28.475 -41.366 1.00 11.85 ?  1217 THR   B CG2 1 
ATOM   3604 N N   . VAL   B 1 181 ? -39.946 -26.940 -41.420 1.00 11.49 ?  1218 VAL   B N   1 
ATOM   3605 C CA  . VAL   B 1 181 ? -40.242 -25.531 -41.213 1.00 10.71 ?  1218 VAL   B CA  1 
ATOM   3606 C C   . VAL   B 1 181 ? -38.989 -24.853 -40.685 1.00 12.82 ?  1218 VAL   B C   1 
ATOM   3607 O O   . VAL   B 1 181 ? -38.237 -25.424 -39.883 1.00 13.82 ?  1218 VAL   B O   1 
ATOM   3608 C CB  . VAL   B 1 181 ? -41.449 -25.329 -40.277 1.00 12.67 ?  1218 VAL   B CB  1 
ATOM   3609 C CG1 . VAL   B 1 181 ? -42.505 -26.383 -40.532 1.00 13.83 ?  1218 VAL   B CG1 1 
ATOM   3610 C CG2 . VAL   B 1 181 ? -41.031 -25.302 -38.823 1.00 12.00 ?  1218 VAL   B CG2 1 
ATOM   3611 N N   . LYS   B 1 182 ? -38.726 -23.651 -41.184 1.00 13.94 ?  1219 LYS   B N   1 
ATOM   3612 C CA  . LYS   B 1 182 ? -37.548 -22.885 -40.800 1.00 12.32 ?  1219 LYS   B CA  1 
ATOM   3613 C C   . LYS   B 1 182 ? -38.003 -21.472 -40.471 1.00 14.47 ?  1219 LYS   B C   1 
ATOM   3614 O O   . LYS   B 1 182 ? -38.473 -20.747 -41.354 1.00 12.20 ?  1219 LYS   B O   1 
ATOM   3615 C CB  . LYS   B 1 182 ? -36.494 -22.889 -41.909 1.00 11.77 ?  1219 LYS   B CB  1 
ATOM   3616 C CG  . LYS   B 1 182 ? -35.874 -24.259 -42.159 1.00 15.24 ?  1219 LYS   B CG  1 
ATOM   3617 C CD  . LYS   B 1 182 ? -34.851 -24.226 -43.282 1.00 11.37 ?  1219 LYS   B CD  1 
ATOM   3618 C CE  . LYS   B 1 182 ? -34.230 -25.599 -43.495 1.00 8.21  ?  1219 LYS   B CE  1 
ATOM   3619 N NZ  . LYS   B 1 182 ? -33.241 -25.592 -44.609 1.00 4.39  ?  1219 LYS   B NZ  1 
ATOM   3620 N N   . VAL   B 1 183 ? -37.890 -21.104 -39.196 1.00 11.93 ?  1220 VAL   B N   1 
ATOM   3621 C CA  . VAL   B 1 183 ? -38.203 -19.761 -38.723 1.00 13.20 ?  1220 VAL   B CA  1 
ATOM   3622 C C   . VAL   B 1 183 ? -37.472 -18.752 -39.597 1.00 14.61 ?  1220 VAL   B C   1 
ATOM   3623 O O   . VAL   B 1 183 ? -36.238 -18.758 -39.673 1.00 21.93 ?  1220 VAL   B O   1 
ATOM   3624 C CB  . VAL   B 1 183 ? -37.822 -19.599 -37.240 1.00 12.90 ?  1220 VAL   B CB  1 
ATOM   3625 C CG1 . VAL   B 1 183 ? -38.048 -18.171 -36.788 1.00 10.14 ?  1220 VAL   B CG1 1 
ATOM   3626 C CG2 . VAL   B 1 183 ? -38.615 -20.573 -36.379 1.00 10.96 ?  1220 VAL   B CG2 1 
ATOM   3627 N N   . ALA   B 1 184 ? -38.225 -17.892 -40.272 1.00 9.73  ?  1221 ALA   B N   1 
ATOM   3628 C CA  . ALA   B 1 184 ? -37.663 -16.997 -41.276 1.00 13.75 ?  1221 ALA   B CA  1 
ATOM   3629 C C   . ALA   B 1 184 ? -38.033 -15.556 -40.929 1.00 12.44 ?  1221 ALA   B C   1 
ATOM   3630 O O   . ALA   B 1 184 ? -38.364 -15.226 -39.783 1.00 11.82 ?  1221 ALA   B O   1 
ATOM   3631 C CB  . ALA   B 1 184 ? -38.143 -17.413 -42.673 1.00 11.29 ?  1221 ALA   B CB  1 
ATOM   3632 N N   . ASP   B 1 185 ? -37.970 -14.681 -41.931 1.00 9.89  ?  1222 ASP   B N   1 
ATOM   3633 C CA  . ASP   B 1 185 ? -38.288 -13.261 -41.789 1.00 13.10 ?  1222 ASP   B CA  1 
ATOM   3634 C C   . ASP   B 1 185 ? -37.490 -12.631 -40.646 1.00 12.13 ?  1222 ASP   B C   1 
ATOM   3635 O O   . ASP   B 1 185 ? -38.036 -12.053 -39.704 1.00 16.42 ?  1222 ASP   B O   1 
ATOM   3636 C CB  . ASP   B 1 185 ? -39.793 -13.055 -41.592 1.00 13.07 ?  1222 ASP   B CB  1 
ATOM   3637 C CG  . ASP   B 1 185 ? -40.188 -11.592 -41.607 1.00 15.99 ?  1222 ASP   B CG  1 
ATOM   3638 O OD1 . ASP   B 1 185 ? -39.507 -10.804 -42.293 1.00 19.75 ?  1222 ASP   B OD1 1 
ATOM   3639 O OD2 . ASP   B 1 185 ? -41.171 -11.229 -40.928 1.00 14.80 -1 1222 ASP   B OD2 1 
ATOM   3640 N N   . PHE   B 1 186 ? -36.170 -12.765 -40.737 1.00 16.00 ?  1223 PHE   B N   1 
ATOM   3641 C CA  . PHE   B 1 186 ? -35.288 -12.179 -39.740 1.00 16.08 ?  1223 PHE   B CA  1 
ATOM   3642 C C   . PHE   B 1 186 ? -33.938 -11.898 -40.378 1.00 15.56 ?  1223 PHE   B C   1 
ATOM   3643 O O   . PHE   B 1 186 ? -33.523 -12.581 -41.318 1.00 13.58 ?  1223 PHE   B O   1 
ATOM   3644 C CB  . PHE   B 1 186 ? -35.130 -13.087 -38.511 1.00 13.33 ?  1223 PHE   B CB  1 
ATOM   3645 C CG  . PHE   B 1 186 ? -34.220 -14.265 -38.730 1.00 16.45 ?  1223 PHE   B CG  1 
ATOM   3646 C CD1 . PHE   B 1 186 ? -34.707 -15.439 -39.279 1.00 14.56 ?  1223 PHE   B CD1 1 
ATOM   3647 C CD2 . PHE   B 1 186 ? -32.883 -14.206 -38.365 1.00 16.73 ?  1223 PHE   B CD2 1 
ATOM   3648 C CE1 . PHE   B 1 186 ? -33.875 -16.527 -39.475 1.00 15.90 ?  1223 PHE   B CE1 1 
ATOM   3649 C CE2 . PHE   B 1 186 ? -32.047 -15.290 -38.560 1.00 17.85 ?  1223 PHE   B CE2 1 
ATOM   3650 C CZ  . PHE   B 1 186 ? -32.544 -16.452 -39.115 1.00 14.93 ?  1223 PHE   B CZ  1 
ATOM   3651 N N   . GLY   B 1 187 ? -33.260 -10.884 -39.856 1.00 15.23 ?  1224 GLY   B N   1 
ATOM   3652 C CA  . GLY   B 1 187 ? -31.973 -10.511 -40.414 1.00 14.19 ?  1224 GLY   B CA  1 
ATOM   3653 C C   . GLY   B 1 187 ? -32.145 -9.912  -41.794 1.00 12.33 ?  1224 GLY   B C   1 
ATOM   3654 O O   . GLY   B 1 187 ? -32.968 -9.015  -42.009 1.00 15.93 ?  1224 GLY   B O   1 
ATOM   3655 N N   . LEU   B 1 188 ? -31.365 -10.412 -42.748 1.00 15.01 ?  1225 LEU   B N   1 
ATOM   3656 C CA  . LEU   B 1 188 ? -31.475 -9.966  -44.129 1.00 14.12 ?  1225 LEU   B CA  1 
ATOM   3657 C C   . LEU   B 1 188 ? -32.688 -10.547 -44.839 1.00 12.88 ?  1225 LEU   B C   1 
ATOM   3658 O O   . LEU   B 1 188 ? -32.897 -10.251 -46.020 1.00 18.73 ?  1225 LEU   B O   1 
ATOM   3659 C CB  . LEU   B 1 188 ? -30.199 -10.315 -44.894 1.00 14.12 ?  1225 LEU   B CB  1 
ATOM   3660 C CG  . LEU   B 1 188 ? -28.910 -9.943  -44.162 1.00 11.89 ?  1225 LEU   B CG  1 
ATOM   3661 C CD1 . LEU   B 1 188 ? -27.712 -10.313 -45.000 1.00 16.03 ?  1225 LEU   B CD1 1 
ATOM   3662 C CD2 . LEU   B 1 188 ? -28.892 -8.460  -43.827 1.00 12.11 ?  1225 LEU   B CD2 1 
ATOM   3663 N N   . ALA   B 1 189 ? -33.480 -11.368 -44.154 1.00 14.28 ?  1226 ALA   B N   1 
ATOM   3664 C CA  . ALA   B 1 189 ? -34.770 -11.820 -44.650 1.00 15.09 ?  1226 ALA   B CA  1 
ATOM   3665 C C   . ALA   B 1 189 ? -35.927 -11.054 -44.028 1.00 12.57 ?  1226 ALA   B C   1 
ATOM   3666 O O   . ALA   B 1 189 ? -37.086 -11.333 -44.352 1.00 12.64 ?  1226 ALA   B O   1 
ATOM   3667 C CB  . ALA   B 1 189 ? -34.942 -13.321 -44.392 1.00 12.09 ?  1226 ALA   B CB  1 
ATOM   3668 N N   . ARG   B 1 190 ? -35.639 -10.105 -43.139 1.00 12.48 ?  1227 ARG   B N   1 
ATOM   3669 C CA  . ARG   B 1 190 ? -36.691 -9.309  -42.523 1.00 10.00 ?  1227 ARG   B CA  1 
ATOM   3670 C C   . ARG   B 1 190 ? -37.383 -8.447  -43.570 1.00 11.02 ?  1227 ARG   B C   1 
ATOM   3671 O O   . ARG   B 1 190 ? -36.737 -7.886  -44.460 1.00 11.15 ?  1227 ARG   B O   1 
ATOM   3672 C CB  . ARG   B 1 190 ? -36.108 -8.432  -41.413 1.00 10.86 ?  1227 ARG   B CB  1 
ATOM   3673 N N   . ASP   B 1 191 ? -38.708 -8.353  -43.462 1.00 14.22 ?  1228 ASP   B N   1 
ATOM   3674 C CA  . ASP   B 1 191 ? -39.547 -7.585  -44.377 1.00 12.04 ?  1228 ASP   B CA  1 
ATOM   3675 C C   . ASP   B 1 191 ? -40.998 -7.730  -43.941 1.00 11.05 ?  1228 ASP   B C   1 
ATOM   3676 O O   . ASP   B 1 191 ? -41.335 -8.593  -43.126 1.00 12.02 ?  1228 ASP   B O   1 
ATOM   3677 C CB  . ASP   B 1 191 ? -39.394 -8.045  -45.828 1.00 11.66 ?  1228 ASP   B CB  1 
ATOM   3678 C CG  . ASP   B 1 191 ? -39.523 -6.907  -46.812 1.00 14.75 ?  1228 ASP   B CG  1 
ATOM   3679 O OD1 . ASP   B 1 191 ? -40.156 -5.891  -46.460 1.00 16.37 ?  1228 ASP   B OD1 1 
ATOM   3680 O OD2 . ASP   B 1 191 ? -38.994 -7.027  -47.936 1.00 14.35 -1 1228 ASP   B OD2 1 
ATOM   3681 N N   . MET   B 1 192 ? -41.854 -6.875  -44.497 1.00 11.35 ?  1229 MET   B N   1 
ATOM   3682 C CA  . MET   B 1 192 ? -43.299 -6.967  -44.290 1.00 14.51 ?  1229 MET   B CA  1 
ATOM   3683 C C   . MET   B 1 192 ? -43.861 -7.762  -45.459 1.00 18.75 ?  1229 MET   B C   1 
ATOM   3684 O O   . MET   B 1 192 ? -43.974 -7.246  -46.573 1.00 19.97 ?  1229 MET   B O   1 
ATOM   3685 C CB  . MET   B 1 192 ? -43.929 -5.581  -44.202 1.00 14.93 ?  1229 MET   B CB  1 
ATOM   3686 C CG  . MET   B 1 192 ? -44.151 -5.048  -42.787 1.00 17.28 ?  1229 MET   B CG  1 
ATOM   3687 S SD  . MET   B 1 192 ? -44.829 -3.370  -42.756 1.00 19.29 ?  1229 MET   B SD  1 
ATOM   3688 C CE  . MET   B 1 192 ? -45.374 -3.193  -44.450 1.00 15.58 ?  1229 MET   B CE  1 
ATOM   3689 N N   . TYR   B 1 193 ? -44.213 -9.025  -45.214 1.00 12.40 ?  1230 TYR   B N   1 
ATOM   3690 C CA  . TYR   B 1 193 ? -44.518 -9.935  -46.311 1.00 12.62 ?  1230 TYR   B CA  1 
ATOM   3691 C C   . TYR   B 1 193 ? -45.993 -9.957  -46.691 1.00 13.66 ?  1230 TYR   B C   1 
ATOM   3692 O O   . TYR   B 1 193 ? -46.322 -10.378 -47.805 1.00 13.98 ?  1230 TYR   B O   1 
ATOM   3693 C CB  . TYR   B 1 193 ? -44.008 -11.338 -45.969 1.00 14.00 ?  1230 TYR   B CB  1 
ATOM   3694 C CG  . TYR   B 1 193 ? -42.506 -11.424 -46.131 1.00 10.99 ?  1230 TYR   B CG  1 
ATOM   3695 C CD1 . TYR   B 1 193 ? -41.921 -11.290 -47.384 1.00 10.99 ?  1230 TYR   B CD1 1 
ATOM   3696 C CD2 . TYR   B 1 193 ? -41.670 -11.593 -45.035 1.00 7.76  ?  1230 TYR   B CD2 1 
ATOM   3697 C CE1 . TYR   B 1 193 ? -40.552 -11.346 -47.547 1.00 8.26  ?  1230 TYR   B CE1 1 
ATOM   3698 C CE2 . TYR   B 1 193 ? -40.296 -11.652 -45.188 1.00 8.44  ?  1230 TYR   B CE2 1 
ATOM   3699 C CZ  . TYR   B 1 193 ? -39.743 -11.528 -46.446 1.00 9.51  ?  1230 TYR   B CZ  1 
ATOM   3700 O OH  . TYR   B 1 193 ? -38.377 -11.585 -46.604 1.00 7.64  ?  1230 TYR   B OH  1 
ATOM   3701 N N   . ASP   B 1 194 ? -46.882 -9.509  -45.808 1.00 13.95 ?  1231 ASP   B N   1 
ATOM   3702 C CA  . ASP   B 1 194 ? -48.202 -9.045  -46.230 1.00 20.83 ?  1231 ASP   B CA  1 
ATOM   3703 C C   . ASP   B 1 194 ? -48.644 -7.973  -45.245 1.00 17.83 ?  1231 ASP   B C   1 
ATOM   3704 O O   . ASP   B 1 194 ? -48.786 -8.240  -44.047 1.00 13.87 ?  1231 ASP   B O   1 
ATOM   3705 C CB  . ASP   B 1 194 ? -49.226 -10.188 -46.337 1.00 20.11 ?  1231 ASP   B CB  1 
ATOM   3706 C CG  . ASP   B 1 194 ? -49.561 -10.819 -45.005 1.00 20.55 ?  1231 ASP   B CG  1 
ATOM   3707 O OD1 . ASP   B 1 194 ? -48.631 -11.283 -44.318 1.00 17.90 ?  1231 ASP   B OD1 1 
ATOM   3708 O OD2 . ASP   B 1 194 ? -50.760 -10.858 -44.653 1.00 21.89 -1 1231 ASP   B OD2 1 
ATOM   3709 N N   . LYS   B 1 195 ? -48.839 -6.756  -45.753 1.00 19.93 ?  1232 LYS   B N   1 
ATOM   3710 C CA  . LYS   B 1 195 ? -48.956 -5.561  -44.925 1.00 20.98 ?  1232 LYS   B CA  1 
ATOM   3711 C C   . LYS   B 1 195 ? -50.271 -5.465  -44.162 1.00 21.37 ?  1232 LYS   B C   1 
ATOM   3712 O O   . LYS   B 1 195 ? -50.430 -4.520  -43.380 1.00 22.79 ?  1232 LYS   B O   1 
ATOM   3713 C CB  . LYS   B 1 195 ? -48.780 -4.314  -45.794 1.00 17.22 ?  1232 LYS   B CB  1 
ATOM   3714 N N   . GLU   B 1 196 ? -51.207 -6.398  -44.356 1.00 16.08 ?  1233 GLU   B N   1 
ATOM   3715 C CA  . GLU   B 1 196 ? -52.506 -6.285  -43.701 1.00 18.41 ?  1233 GLU   B CA  1 
ATOM   3716 C C   . GLU   B 1 196 ? -52.388 -6.350  -42.182 1.00 17.61 ?  1233 GLU   B C   1 
ATOM   3717 O O   . GLU   B 1 196 ? -53.158 -5.692  -41.472 1.00 17.27 ?  1233 GLU   B O   1 
ATOM   3718 C CB  . GLU   B 1 196 ? -53.445 -7.383  -44.208 1.00 21.41 ?  1233 GLU   B CB  1 
ATOM   3719 C CG  . GLU   B 1 196 ? -54.710 -7.559  -43.380 1.00 17.54 ?  1233 GLU   B CG  1 
ATOM   3720 C CD  . GLU   B 1 196 ? -55.888 -8.032  -44.205 1.00 22.55 ?  1233 GLU   B CD  1 
ATOM   3721 O OE1 . GLU   B 1 196 ? -55.825 -7.928  -45.448 1.00 31.48 ?  1233 GLU   B OE1 1 
ATOM   3722 O OE2 . GLU   B 1 196 ? -56.879 -8.506  -43.611 1.00 27.34 -1 1233 GLU   B OE2 1 
ATOM   3723 N N   . TYR   B 1 197 ? -51.430 -7.115  -41.667 1.00 16.75 ?  1234 TYR   B N   1 
ATOM   3724 C CA  . TYR   B 1 197 ? -51.316 -7.368  -40.238 1.00 16.93 ?  1234 TYR   B CA  1 
ATOM   3725 C C   . TYR   B 1 197 ? -50.316 -6.451  -39.553 1.00 16.40 ?  1234 TYR   B C   1 
ATOM   3726 O O   . TYR   B 1 197 ? -49.951 -6.701  -38.399 1.00 17.31 ?  1234 TYR   B O   1 
ATOM   3727 C CB  . TYR   B 1 197 ? -50.929 -8.826  -40.001 1.00 18.38 ?  1234 TYR   B CB  1 
ATOM   3728 C CG  . TYR   B 1 197 ? -51.955 -9.793  -40.531 1.00 20.75 ?  1234 TYR   B CG  1 
ATOM   3729 C CD1 . TYR   B 1 197 ? -53.180 -9.943  -39.899 1.00 14.58 ?  1234 TYR   B CD1 1 
ATOM   3730 C CD2 . TYR   B 1 197 ? -51.709 -10.542 -41.674 1.00 18.02 ?  1234 TYR   B CD2 1 
ATOM   3731 C CE1 . TYR   B 1 197 ? -54.129 -10.822 -40.380 1.00 18.72 ?  1234 TYR   B CE1 1 
ATOM   3732 C CE2 . TYR   B 1 197 ? -52.654 -11.425 -42.165 1.00 23.54 ?  1234 TYR   B CE2 1 
ATOM   3733 C CZ  . TYR   B 1 197 ? -53.862 -11.561 -41.513 1.00 21.95 ?  1234 TYR   B CZ  1 
ATOM   3734 O OH  . TYR   B 1 197 ? -54.808 -12.436 -41.993 1.00 20.08 ?  1234 TYR   B OH  1 
ATOM   3735 N N   . TYR   B 1 198 ? -49.880 -5.394  -40.225 1.00 17.58 ?  1235 TYR   B N   1 
ATOM   3736 C CA  . TYR   B 1 198 ? -48.794 -4.552  -39.749 1.00 18.62 ?  1235 TYR   B CA  1 
ATOM   3737 C C   . TYR   B 1 198 ? -49.282 -3.119  -39.580 1.00 18.35 ?  1235 TYR   B C   1 
ATOM   3738 O O   . TYR   B 1 198 ? -49.999 -2.594  -40.441 1.00 17.14 ?  1235 TYR   B O   1 
ATOM   3739 C CB  . TYR   B 1 198 ? -47.627 -4.601  -40.727 1.00 18.02 ?  1235 TYR   B CB  1 
ATOM   3740 C CG  . TYR   B 1 198 ? -46.823 -5.872  -40.671 1.00 19.05 ?  1235 TYR   B CG  1 
ATOM   3741 C CD1 . TYR   B 1 198 ? -45.740 -5.996  -39.809 1.00 16.39 ?  1235 TYR   B CD1 1 
ATOM   3742 C CD2 . TYR   B 1 198 ? -47.131 -6.941  -41.500 1.00 18.90 ?  1235 TYR   B CD2 1 
ATOM   3743 C CE1 . TYR   B 1 198 ? -44.993 -7.143  -39.771 1.00 18.32 ?  1235 TYR   B CE1 1 
ATOM   3744 C CE2 . TYR   B 1 198 ? -46.388 -8.098  -41.470 1.00 20.18 ?  1235 TYR   B CE2 1 
ATOM   3745 C CZ  . TYR   B 1 198 ? -45.318 -8.194  -40.600 1.00 18.76 ?  1235 TYR   B CZ  1 
ATOM   3746 O OH  . TYR   B 1 198 ? -44.564 -9.343  -40.554 1.00 17.64 ?  1235 TYR   B OH  1 
ATOM   3747 N N   . SER   B 1 199 ? -48.893 -2.491  -38.474 1.00 18.83 ?  1236 SER   B N   1 
ATOM   3748 C CA  . SER   B 1 199 ? -49.241 -1.102  -38.195 1.00 19.57 ?  1236 SER   B CA  1 
ATOM   3749 C C   . SER   B 1 199 ? -47.954 -0.298  -38.078 1.00 19.58 ?  1236 SER   B C   1 
ATOM   3750 O O   . SER   B 1 199 ? -47.230 -0.417  -37.084 1.00 15.52 ?  1236 SER   B O   1 
ATOM   3751 C CB  . SER   B 1 199 ? -50.071 -0.985  -36.920 1.00 19.57 ?  1236 SER   B CB  1 
ATOM   3752 O OG  . SER   B 1 199 ? -50.146 0.366   -36.500 1.00 16.89 ?  1236 SER   B OG  1 
ATOM   3753 N N   . VAL   B 1 200 ? -47.671 0.526   -39.084 1.00 16.68 ?  1237 VAL   B N   1 
ATOM   3754 C CA  . VAL   B 1 200 ? -46.489 1.377   -39.036 1.00 15.59 ?  1237 VAL   B CA  1 
ATOM   3755 C C   . VAL   B 1 200 ? -46.658 2.403   -37.922 1.00 18.36 ?  1237 VAL   B C   1 
ATOM   3756 O O   . VAL   B 1 200 ? -47.634 3.162   -37.898 1.00 17.09 ?  1237 VAL   B O   1 
ATOM   3757 C CB  . VAL   B 1 200 ? -46.245 2.057   -40.388 1.00 18.37 ?  1237 VAL   B CB  1 
ATOM   3758 C CG1 . VAL   B 1 200 ? -44.824 2.580   -40.451 1.00 16.79 ?  1237 VAL   B CG1 1 
ATOM   3759 C CG2 . VAL   B 1 200 ? -46.516 1.085   -41.527 1.00 17.33 ?  1237 VAL   B CG2 1 
ATOM   3760 N N   . HIS   B 1 201 ? -45.710 2.423   -36.990 1.00 13.23 ?  1238 HIS   B N   1 
ATOM   3761 C CA  . HIS   B 1 201 ? -45.727 3.398   -35.911 1.00 18.44 ?  1238 HIS   B CA  1 
ATOM   3762 C C   . HIS   B 1 201 ? -45.388 4.782   -36.459 1.00 18.52 ?  1238 HIS   B C   1 
ATOM   3763 O O   . HIS   B 1 201 ? -44.675 4.916   -37.456 1.00 18.33 ?  1238 HIS   B O   1 
ATOM   3764 C CB  . HIS   B 1 201 ? -44.735 2.985   -34.826 1.00 13.54 ?  1238 HIS   B CB  1 
ATOM   3765 C CG  . HIS   B 1 201 ? -44.886 3.739   -33.545 1.00 18.49 ?  1238 HIS   B CG  1 
ATOM   3766 N ND1 . HIS   B 1 201 ? -44.093 4.816   -33.217 1.00 23.72 ?  1238 HIS   B ND1 1 
ATOM   3767 C CD2 . HIS   B 1 201 ? -45.737 3.567   -32.506 1.00 17.97 ?  1238 HIS   B CD2 1 
ATOM   3768 C CE1 . HIS   B 1 201 ? -44.449 5.277   -32.032 1.00 22.27 ?  1238 HIS   B CE1 1 
ATOM   3769 N NE2 . HIS   B 1 201 ? -45.445 4.537   -31.579 1.00 24.10 ?  1238 HIS   B NE2 1 
ATOM   3770 N N   . ASN   B 1 202 ? -45.913 5.824   -35.807 1.00 18.24 ?  1239 ASN   B N   1 
ATOM   3771 C CA  . ASN   B 1 202 ? -45.805 7.168   -36.369 1.00 20.01 ?  1239 ASN   B CA  1 
ATOM   3772 C C   . ASN   B 1 202 ? -44.528 7.911   -35.986 1.00 18.65 ?  1239 ASN   B C   1 
ATOM   3773 O O   . ASN   B 1 202 ? -44.132 8.829   -36.714 1.00 20.39 ?  1239 ASN   B O   1 
ATOM   3774 C CB  . ASN   B 1 202 ? -47.031 8.016   -35.991 1.00 12.16 ?  1239 ASN   B CB  1 
ATOM   3775 C CG  . ASN   B 1 202 ? -47.467 7.826   -34.547 1.00 16.74 ?  1239 ASN   B CG  1 
ATOM   3776 O OD1 . ASN   B 1 202 ? -46.648 7.591   -33.660 1.00 23.35 ?  1239 ASN   B OD1 1 
ATOM   3777 N ND2 . ASN   B 1 202 ? -48.770 7.938   -34.306 1.00 16.77 ?  1239 ASN   B ND2 1 
ATOM   3778 N N   . LYS   B 1 203 ? -43.861 7.549   -34.889 1.00 12.76 ?  1240 LYS   B N   1 
ATOM   3779 C CA  . LYS   B 1 203 ? -42.580 8.167   -34.540 1.00 21.88 ?  1240 LYS   B CA  1 
ATOM   3780 C C   . LYS   B 1 203 ? -41.397 7.277   -34.904 1.00 20.94 ?  1240 LYS   B C   1 
ATOM   3781 O O   . LYS   B 1 203 ? -40.530 7.677   -35.686 1.00 21.05 ?  1240 LYS   B O   1 
ATOM   3782 C CB  . LYS   B 1 203 ? -42.519 8.497   -33.048 1.00 26.14 ?  1240 LYS   B CB  1 
ATOM   3783 C CG  . LYS   B 1 203 ? -43.693 9.264   -32.541 1.00 25.53 ?  1240 LYS   B CG  1 
ATOM   3784 C CD  . LYS   B 1 203 ? -44.128 8.639   -31.275 1.00 31.15 ?  1240 LYS   B CD  1 
ATOM   3785 C CE  . LYS   B 1 203 ? -45.303 9.355   -30.758 1.00 42.13 ?  1240 LYS   B CE  1 
ATOM   3786 N NZ  . LYS   B 1 203 ? -46.191 8.289   -30.427 1.00 37.43 ?  1240 LYS   B NZ  1 
ATOM   3787 N N   . THR   B 1 204 ? -41.307 6.101   -34.295 1.00 21.29 ?  1241 THR   B N   1 
ATOM   3788 C CA  . THR   B 1 204 ? -40.433 5.076   -34.835 1.00 21.90 ?  1241 THR   B CA  1 
ATOM   3789 C C   . THR   B 1 204 ? -41.060 4.522   -36.109 1.00 17.24 ?  1241 THR   B C   1 
ATOM   3790 O O   . THR   B 1 204 ? -42.282 4.418   -36.226 1.00 26.31 ?  1241 THR   B O   1 
ATOM   3791 C CB  . THR   B 1 204 ? -40.211 3.957   -33.816 1.00 17.05 ?  1241 THR   B CB  1 
ATOM   3792 O OG1 . THR   B 1 204 ? -41.467 3.369   -33.462 1.00 19.58 ?  1241 THR   B OG1 1 
ATOM   3793 C CG2 . THR   B 1 204 ? -39.564 4.511   -32.558 1.00 27.99 ?  1241 THR   B CG2 1 
ATOM   3794 N N   . GLY   B 1 205 ? -40.218 4.163   -37.071 1.00 21.28 ?  1242 GLY   B N   1 
ATOM   3795 C CA  . GLY   B 1 205 ? -40.746 3.594   -38.298 1.00 22.58 ?  1242 GLY   B CA  1 
ATOM   3796 C C   . GLY   B 1 205 ? -41.345 2.222   -38.068 1.00 16.83 ?  1242 GLY   B C   1 
ATOM   3797 O O   . GLY   B 1 205 ? -41.838 1.577   -38.999 1.00 11.28 ?  1242 GLY   B O   1 
ATOM   3798 N N   . ALA   B 1 206 ? -41.325 1.787   -36.810 1.00 17.89 ?  1243 ALA   B N   1 
ATOM   3799 C CA  . ALA   B 1 206 ? -41.543 0.390   -36.468 1.00 15.76 ?  1243 ALA   B CA  1 
ATOM   3800 C C   . ALA   B 1 206 ? -42.736 -0.276  -37.130 1.00 17.04 ?  1243 ALA   B C   1 
ATOM   3801 O O   . ALA   B 1 206 ? -43.878 0.168   -36.978 1.00 17.13 ?  1243 ALA   B O   1 
ATOM   3802 C CB  . ALA   B 1 206 ? -41.644 0.277   -34.950 1.00 16.73 ?  1243 ALA   B CB  1 
ATOM   3803 N N   . LYS   B 1 207 ? -42.455 -1.348  -37.862 1.00 20.50 ?  1244 LYS   B N   1 
ATOM   3804 C CA  . LYS   B 1 207 ? -43.482 -2.160  -38.496 1.00 17.97 ?  1244 LYS   B CA  1 
ATOM   3805 C C   . LYS   B 1 207 ? -43.967 -3.207  -37.498 1.00 18.36 ?  1244 LYS   B C   1 
ATOM   3806 O O   . LYS   B 1 207 ? -43.176 -4.026  -37.014 1.00 22.18 ?  1244 LYS   B O   1 
ATOM   3807 C CB  . LYS   B 1 207 ? -42.910 -2.785  -39.765 1.00 17.52 ?  1244 LYS   B CB  1 
ATOM   3808 C CG  . LYS   B 1 207 ? -42.370 -1.720  -40.715 1.00 12.80 ?  1244 LYS   B CG  1 
ATOM   3809 C CD  . LYS   B 1 207 ? -41.466 -2.281  -41.796 1.00 20.25 ?  1244 LYS   B CD  1 
ATOM   3810 C CE  . LYS   B 1 207 ? -40.769 -1.147  -42.540 1.00 11.48 ?  1244 LYS   B CE  1 
ATOM   3811 N NZ  . LYS   B 1 207 ? -40.001 -1.602  -43.730 1.00 16.33 ?  1244 LYS   B NZ  1 
ATOM   3812 N N   . LEU   B 1 208 ? -45.263 -3.179  -37.191 1.00 19.68 ?  1245 LEU   B N   1 
ATOM   3813 C CA  . LEU   B 1 208 ? -45.777 -3.727  -35.939 1.00 20.07 ?  1245 LEU   B CA  1 
ATOM   3814 C C   . LEU   B 1 208 ? -46.808 -4.827  -36.163 1.00 21.60 ?  1245 LEU   B C   1 
ATOM   3815 O O   . LEU   B 1 208 ? -47.899 -4.550  -36.694 1.00 22.54 ?  1245 LEU   B O   1 
ATOM   3816 C CB  . LEU   B 1 208 ? -46.384 -2.599  -35.095 1.00 20.66 ?  1245 LEU   B CB  1 
ATOM   3817 C CG  . LEU   B 1 208 ? -45.452 -1.495  -34.578 1.00 24.84 ?  1245 LEU   B CG  1 
ATOM   3818 C CD1 . LEU   B 1 208 ? -46.243 -0.395  -33.870 1.00 17.08 ?  1245 LEU   B CD1 1 
ATOM   3819 C CD2 . LEU   B 1 208 ? -44.357 -2.035  -33.669 1.00 24.65 ?  1245 LEU   B CD2 1 
ATOM   3820 N N   . PRO   B 1 209 ? -46.519 -6.077  -35.768 1.00 19.68 ?  1246 PRO   B N   1 
ATOM   3821 C CA  . PRO   B 1 209 ? -47.542 -7.136  -35.803 1.00 19.73 ?  1246 PRO   B CA  1 
ATOM   3822 C C   . PRO   B 1 209 ? -48.428 -7.181  -34.560 1.00 19.83 ?  1246 PRO   B C   1 
ATOM   3823 O O   . PRO   B 1 209 ? -48.160 -7.949  -33.629 1.00 19.63 ?  1246 PRO   B O   1 
ATOM   3824 C CB  . PRO   B 1 209 ? -46.704 -8.411  -35.934 1.00 18.35 ?  1246 PRO   B CB  1 
ATOM   3825 C CG  . PRO   B 1 209 ? -45.389 -8.060  -35.251 1.00 17.41 ?  1246 PRO   B CG  1 
ATOM   3826 C CD  . PRO   B 1 209 ? -45.155 -6.613  -35.585 1.00 18.75 ?  1246 PRO   B CD  1 
ATOM   3827 N N   . VAL   B 1 210 ? -49.532 -6.424  -34.584 1.00 14.62 ?  1247 VAL   B N   1 
ATOM   3828 C CA  . VAL   B 1 210 ? -50.298 -6.107  -33.376 1.00 16.34 ?  1247 VAL   B CA  1 
ATOM   3829 C C   . VAL   B 1 210 ? -50.915 -7.357  -32.750 1.00 17.28 ?  1247 VAL   B C   1 
ATOM   3830 O O   . VAL   B 1 210 ? -51.031 -7.457  -31.522 1.00 13.62 ?  1247 VAL   B O   1 
ATOM   3831 C CB  . VAL   B 1 210 ? -51.375 -5.059  -33.713 1.00 18.37 ?  1247 VAL   B CB  1 
ATOM   3832 C CG1 . VAL   B 1 210 ? -51.995 -4.462  -32.447 1.00 19.57 ?  1247 VAL   B CG1 1 
ATOM   3833 C CG2 . VAL   B 1 210 ? -50.786 -3.975  -34.597 1.00 19.02 ?  1247 VAL   B CG2 1 
ATOM   3834 N N   . LYS   B 1 211 ? -51.348 -8.312  -33.570 1.00 17.18 ?  1248 LYS   B N   1 
ATOM   3835 C CA  . LYS   B 1 211 ? -52.067 -9.475  -33.058 1.00 17.09 ?  1248 LYS   B CA  1 
ATOM   3836 C C   . LYS   B 1 211 ? -51.158 -10.648 -32.712 1.00 19.73 ?  1248 LYS   B C   1 
ATOM   3837 O O   . LYS   B 1 211 ? -51.657 -11.701 -32.300 1.00 14.99 ?  1248 LYS   B O   1 
ATOM   3838 C CB  . LYS   B 1 211 ? -53.133 -9.923  -34.062 1.00 16.25 ?  1248 LYS   B CB  1 
ATOM   3839 C CG  . LYS   B 1 211 ? -54.452 -9.197  -33.883 1.00 20.52 ?  1248 LYS   B CG  1 
ATOM   3840 C CD  . LYS   B 1 211 ? -55.278 -9.191  -35.151 1.00 20.00 ?  1248 LYS   B CD  1 
ATOM   3841 C CE  . LYS   B 1 211 ? -56.532 -8.358  -34.962 1.00 21.21 ?  1248 LYS   B CE  1 
ATOM   3842 N NZ  . LYS   B 1 211 ? -57.079 -8.498  -33.585 1.00 22.98 ?  1248 LYS   B NZ  1 
ATOM   3843 N N   . TRP   B 1 212 ? -49.846 -10.498 -32.868 1.00 18.48 ?  1249 TRP   B N   1 
ATOM   3844 C CA  . TRP   B 1 212 ? -48.887 -11.486 -32.404 1.00 12.12 ?  1249 TRP   B CA  1 
ATOM   3845 C C   . TRP   B 1 212 ? -48.020 -10.950 -31.280 1.00 16.79 ?  1249 TRP   B C   1 
ATOM   3846 O O   . TRP   B 1 212 ? -47.189 -11.690 -30.746 1.00 14.32 ?  1249 TRP   B O   1 
ATOM   3847 C CB  . TRP   B 1 212 ? -48.007 -11.964 -33.565 1.00 11.15 ?  1249 TRP   B CB  1 
ATOM   3848 C CG  . TRP   B 1 212 ? -48.751 -12.807 -34.546 1.00 16.13 ?  1249 TRP   B CG  1 
ATOM   3849 C CD1 . TRP   B 1 212 ? -48.657 -14.160 -34.701 1.00 17.75 ?  1249 TRP   B CD1 1 
ATOM   3850 C CD2 . TRP   B 1 212 ? -49.718 -12.360 -35.503 1.00 18.74 ?  1249 TRP   B CD2 1 
ATOM   3851 N NE1 . TRP   B 1 212 ? -49.504 -14.582 -35.696 1.00 15.75 ?  1249 TRP   B NE1 1 
ATOM   3852 C CE2 . TRP   B 1 212 ? -50.166 -13.495 -36.205 1.00 24.58 ?  1249 TRP   B CE2 1 
ATOM   3853 C CE3 . TRP   B 1 212 ? -50.245 -11.109 -35.838 1.00 18.38 ?  1249 TRP   B CE3 1 
ATOM   3854 C CZ2 . TRP   B 1 212 ? -51.116 -13.416 -37.220 1.00 17.61 ?  1249 TRP   B CZ2 1 
ATOM   3855 C CZ3 . TRP   B 1 212 ? -51.189 -11.034 -36.842 1.00 18.23 ?  1249 TRP   B CZ3 1 
ATOM   3856 C CH2 . TRP   B 1 212 ? -51.615 -12.179 -37.522 1.00 16.30 ?  1249 TRP   B CH2 1 
ATOM   3857 N N   . MET   B 1 213 ? -48.207 -9.693  -30.895 1.00 15.51 ?  1250 MET   B N   1 
ATOM   3858 C CA  . MET   B 1 213 ? -47.337 -9.062  -29.920 1.00 15.77 ?  1250 MET   B CA  1 
ATOM   3859 C C   . MET   B 1 213 ? -47.722 -9.403  -28.494 1.00 14.41 ?  1250 MET   B C   1 
ATOM   3860 O O   . MET   B 1 213 ? -48.900 -9.564  -28.159 1.00 13.08 ?  1250 MET   B O   1 
ATOM   3861 C CB  . MET   B 1 213 ? -47.372 -7.550  -30.046 1.00 15.63 ?  1250 MET   B CB  1 
ATOM   3862 C CG  . MET   B 1 213 ? -46.546 -7.006  -31.136 1.00 18.81 ?  1250 MET   B CG  1 
ATOM   3863 S SD  . MET   B 1 213 ? -46.656 -5.236  -30.990 1.00 36.22 ?  1250 MET   B SD  1 
ATOM   3864 C CE  . MET   B 1 213 ? -46.161 -4.814  -32.611 1.00 20.18 ?  1250 MET   B CE  1 
ATOM   3865 N N   . ALA   B 1 214 ? -46.706 -9.462  -27.641 1.00 13.08 ?  1251 ALA   B N   1 
ATOM   3866 C CA  . ALA   B 1 214 ? -46.942 -9.512  -26.211 1.00 13.78 ?  1251 ALA   B CA  1 
ATOM   3867 C C   . ALA   B 1 214 ? -47.629 -8.233  -25.754 1.00 16.31 ?  1251 ALA   B C   1 
ATOM   3868 O O   . ALA   B 1 214 ? -47.517 -7.179  -26.388 1.00 14.69 ?  1251 ALA   B O   1 
ATOM   3869 C CB  . ALA   B 1 214 ? -45.627 -9.701  -25.461 1.00 13.97 ?  1251 ALA   B CB  1 
ATOM   3870 N N   . LEU   B 1 215 ? -48.355 -8.336  -24.642 1.00 16.59 ?  1252 LEU   B N   1 
ATOM   3871 C CA  . LEU   B 1 215 ? -49.056 -7.174  -24.109 1.00 18.50 ?  1252 LEU   B CA  1 
ATOM   3872 C C   . LEU   B 1 215 ? -48.074 -6.068  -23.742 1.00 17.63 ?  1252 LEU   B C   1 
ATOM   3873 O O   . LEU   B 1 215 ? -48.293 -4.894  -24.066 1.00 17.46 ?  1252 LEU   B O   1 
ATOM   3874 C CB  . LEU   B 1 215 ? -49.894 -7.584  -22.899 1.00 20.72 ?  1252 LEU   B CB  1 
ATOM   3875 C CG  . LEU   B 1 215 ? -50.512 -6.443  -22.092 1.00 20.44 ?  1252 LEU   B CG  1 
ATOM   3876 C CD1 . LEU   B 1 215 ? -51.528 -5.689  -22.932 1.00 19.45 ?  1252 LEU   B CD1 1 
ATOM   3877 C CD2 . LEU   B 1 215 ? -51.149 -6.979  -20.821 1.00 20.94 ?  1252 LEU   B CD2 1 
ATOM   3878 N N   . GLU   B 1 216 ? -46.975 -6.427  -23.073 1.00 18.74 ?  1253 GLU   B N   1 
ATOM   3879 C CA  . GLU   B 1 216 ? -45.976 -5.428  -22.710 1.00 21.31 ?  1253 GLU   B CA  1 
ATOM   3880 C C   . GLU   B 1 216 ? -45.338 -4.800  -23.943 1.00 21.38 ?  1253 GLU   B C   1 
ATOM   3881 O O   . GLU   B 1 216 ? -44.977 -3.619  -23.920 1.00 23.05 ?  1253 GLU   B O   1 
ATOM   3882 C CB  . GLU   B 1 216 ? -44.910 -6.051  -21.804 1.00 16.24 ?  1253 GLU   B CB  1 
ATOM   3883 C CG  . GLU   B 1 216 ? -43.935 -6.987  -22.505 1.00 17.99 ?  1253 GLU   B CG  1 
ATOM   3884 C CD  . GLU   B 1 216 ? -44.356 -8.443  -22.426 1.00 20.59 ?  1253 GLU   B CD  1 
ATOM   3885 O OE1 . GLU   B 1 216 ? -43.638 -9.299  -22.984 1.00 15.54 ?  1253 GLU   B OE1 1 
ATOM   3886 O OE2 . GLU   B 1 216 ? -45.404 -8.732  -21.810 1.00 21.86 -1 1253 GLU   B OE2 1 
ATOM   3887 N N   . SER   B 1 217 ? -45.203 -5.565  -25.031 1.00 16.68 ?  1254 SER   B N   1 
ATOM   3888 C CA  . SER   B 1 217 ? -44.685 -4.994  -26.270 1.00 18.15 ?  1254 SER   B CA  1 
ATOM   3889 C C   . SER   B 1 217 ? -45.631 -3.935  -26.819 1.00 18.84 ?  1254 SER   B C   1 
ATOM   3890 O O   . SER   B 1 217 ? -45.188 -2.894  -27.319 1.00 28.06 ?  1254 SER   B O   1 
ATOM   3891 C CB  . SER   B 1 217 ? -44.456 -6.098  -27.302 1.00 18.27 ?  1254 SER   B CB  1 
ATOM   3892 O OG  . SER   B 1 217 ? -43.166 -6.666  -27.159 1.00 14.61 ?  1254 SER   B OG  1 
ATOM   3893 N N   . LEU   B 1 218 ? -46.940 -4.179  -26.727 1.00 18.18 ?  1255 LEU   B N   1 
ATOM   3894 C CA  . LEU   B 1 218 ? -47.935 -3.202  -27.152 1.00 20.83 ?  1255 LEU   B CA  1 
ATOM   3895 C C   . LEU   B 1 218 ? -47.949 -1.952  -26.282 1.00 20.39 ?  1255 LEU   B C   1 
ATOM   3896 O O   . LEU   B 1 218 ? -48.607 -0.973  -26.648 1.00 17.38 ?  1255 LEU   B O   1 
ATOM   3897 C CB  . LEU   B 1 218 ? -49.327 -3.840  -27.154 1.00 16.89 ?  1255 LEU   B CB  1 
ATOM   3898 C CG  . LEU   B 1 218 ? -49.623 -4.878  -28.237 1.00 23.36 ?  1255 LEU   B CG  1 
ATOM   3899 C CD1 . LEU   B 1 218 ? -50.972 -5.523  -28.004 1.00 19.05 ?  1255 LEU   B CD1 1 
ATOM   3900 C CD2 . LEU   B 1 218 ? -49.599 -4.220  -29.598 1.00 22.12 ?  1255 LEU   B CD2 1 
ATOM   3901 N N   . GLN   B 1 219 ? -47.246 -1.960  -25.149 1.00 21.40 ?  1256 GLN   B N   1 
ATOM   3902 C CA  . GLN   B 1 219 ? -47.216 -0.828  -24.233 1.00 20.97 ?  1256 GLN   B CA  1 
ATOM   3903 C C   . GLN   B 1 219 ? -45.870 -0.126  -24.166 1.00 23.73 ?  1256 GLN   B C   1 
ATOM   3904 O O   . GLN   B 1 219 ? -45.830 1.071   -23.875 1.00 16.87 ?  1256 GLN   B O   1 
ATOM   3905 C CB  . GLN   B 1 219 ? -47.598 -1.280  -22.817 1.00 20.55 ?  1256 GLN   B CB  1 
ATOM   3906 C CG  . GLN   B 1 219 ? -49.055 -1.669  -22.648 1.00 21.59 ?  1256 GLN   B CG  1 
ATOM   3907 C CD  . GLN   B 1 219 ? -49.350 -2.215  -21.264 1.00 29.63 ?  1256 GLN   B CD  1 
ATOM   3908 O OE1 . GLN   B 1 219 ? -50.022 -1.570  -20.459 1.00 42.36 ?  1256 GLN   B OE1 1 
ATOM   3909 N NE2 . GLN   B 1 219 ? -48.846 -3.410  -20.978 1.00 26.98 ?  1256 GLN   B NE2 1 
ATOM   3910 N N   . THR   B 1 220 ? -44.768 -0.836  -24.420 1.00 23.76 ?  1257 THR   B N   1 
ATOM   3911 C CA  . THR   B 1 220 ? -43.434 -0.274  -24.271 1.00 22.76 ?  1257 THR   B CA  1 
ATOM   3912 C C   . THR   B 1 220 ? -42.620 -0.241  -25.555 1.00 19.57 ?  1257 THR   B C   1 
ATOM   3913 O O   . THR   B 1 220 ? -41.575 0.421   -25.577 1.00 18.75 ?  1257 THR   B O   1 
ATOM   3914 C CB  . THR   B 1 220 ? -42.632 -1.057  -23.218 1.00 18.36 ?  1257 THR   B CB  1 
ATOM   3915 O OG1 . THR   B 1 220 ? -42.033 -2.205  -23.833 1.00 23.58 ?  1257 THR   B OG1 1 
ATOM   3916 C CG2 . THR   B 1 220 ? -43.526 -1.501  -22.071 1.00 15.61 ?  1257 THR   B CG2 1 
ATOM   3917 N N   . GLN   B 1 221 ? -43.053 -0.933  -26.610 1.00 20.95 ?  1258 GLN   B N   1 
ATOM   3918 C CA  . GLN   B 1 221 ? -42.310 -1.063  -27.863 1.00 17.90 ?  1258 GLN   B CA  1 
ATOM   3919 C C   . GLN   B 1 221 ? -40.989 -1.805  -27.679 1.00 19.03 ?  1258 GLN   B C   1 
ATOM   3920 O O   . GLN   B 1 221 ? -40.073 -1.659  -28.495 1.00 18.71 ?  1258 GLN   B O   1 
ATOM   3921 C CB  . GLN   B 1 221 ? -42.061 0.302   -28.514 1.00 13.68 ?  1258 GLN   B CB  1 
ATOM   3922 C CG  . GLN   B 1 221 ? -42.940 0.580   -29.708 1.00 23.56 ?  1258 GLN   B CG  1 
ATOM   3923 C CD  . GLN   B 1 221 ? -42.260 0.254   -31.017 1.00 23.62 ?  1258 GLN   B CD  1 
ATOM   3924 O OE1 . GLN   B 1 221 ? -41.152 -0.285  -31.044 1.00 28.66 ?  1258 GLN   B OE1 1 
ATOM   3925 N NE2 . GLN   B 1 221 ? -42.922 0.581   -32.115 1.00 24.40 ?  1258 GLN   B NE2 1 
ATOM   3926 N N   . LYS   B 1 222 ? -40.872 -2.601  -26.620 1.00 21.49 ?  1259 LYS   B N   1 
ATOM   3927 C CA  . LYS   B 1 222 ? -39.683 -3.401  -26.358 1.00 20.57 ?  1259 LYS   B CA  1 
ATOM   3928 C C   . LYS   B 1 222 ? -40.028 -4.875  -26.517 1.00 17.86 ?  1259 LYS   B C   1 
ATOM   3929 O O   . LYS   B 1 222 ? -40.993 -5.359  -25.915 1.00 14.90 ?  1259 LYS   B O   1 
ATOM   3930 C CB  . LYS   B 1 222 ? -39.131 -3.135  -24.954 1.00 19.15 ?  1259 LYS   B CB  1 
ATOM   3931 C CG  . LYS   B 1 222 ? -38.976 -1.661  -24.588 1.00 24.53 ?  1259 LYS   B CG  1 
ATOM   3932 C CD  . LYS   B 1 222 ? -38.324 -0.856  -25.705 1.00 26.03 ?  1259 LYS   B CD  1 
ATOM   3933 C CE  . LYS   B 1 222 ? -36.852 -0.602  -25.429 1.00 30.64 ?  1259 LYS   B CE  1 
ATOM   3934 N NZ  . LYS   B 1 222 ? -36.168 -0.019  -26.618 1.00 27.27 ?  1259 LYS   B NZ  1 
ATOM   3935 N N   . PHE   B 1 223 ? -39.244 -5.580  -27.328 1.00 20.13 ?  1260 PHE   B N   1 
ATOM   3936 C CA  . PHE   B 1 223 ? -39.426 -7.005  -27.564 1.00 19.59 ?  1260 PHE   B CA  1 
ATOM   3937 C C   . PHE   B 1 223 ? -38.322 -7.794  -26.874 1.00 18.71 ?  1260 PHE   B C   1 
ATOM   3938 O O   . PHE   B 1 223 ? -37.149 -7.406  -26.916 1.00 16.87 ?  1260 PHE   B O   1 
ATOM   3939 C CB  . PHE   B 1 223 ? -39.414 -7.331  -29.059 1.00 19.57 ?  1260 PHE   B CB  1 
ATOM   3940 C CG  . PHE   B 1 223 ? -40.493 -6.645  -29.850 1.00 23.94 ?  1260 PHE   B CG  1 
ATOM   3941 C CD1 . PHE   B 1 223 ? -41.765 -7.186  -29.929 1.00 19.16 ?  1260 PHE   B CD1 1 
ATOM   3942 C CD2 . PHE   B 1 223 ? -40.226 -5.474  -30.538 1.00 22.56 ?  1260 PHE   B CD2 1 
ATOM   3943 C CE1 . PHE   B 1 223 ? -42.755 -6.562  -30.664 1.00 20.15 ?  1260 PHE   B CE1 1 
ATOM   3944 C CE2 . PHE   B 1 223 ? -41.211 -4.846  -31.275 1.00 21.09 ?  1260 PHE   B CE2 1 
ATOM   3945 C CZ  . PHE   B 1 223 ? -42.477 -5.391  -31.338 1.00 21.40 ?  1260 PHE   B CZ  1 
ATOM   3946 N N   . THR   B 1 224 ? -38.701 -8.902  -26.244 1.00 17.97 ?  1261 THR   B N   1 
ATOM   3947 C CA  . THR   B 1 224 ? -37.759 -9.848  -25.661 1.00 16.58 ?  1261 THR   B CA  1 
ATOM   3948 C C   . THR   B 1 224 ? -38.051 -11.237 -26.218 1.00 17.52 ?  1261 THR   B C   1 
ATOM   3949 O O   . THR   B 1 224 ? -38.976 -11.430 -27.014 1.00 15.88 ?  1261 THR   B O   1 
ATOM   3950 C CB  . THR   B 1 224 ? -37.839 -9.854  -24.128 1.00 15.83 ?  1261 THR   B CB  1 
ATOM   3951 O OG1 . THR   B 1 224 ? -39.063 -10.473 -23.712 1.00 19.97 ?  1261 THR   B OG1 1 
ATOM   3952 C CG2 . THR   B 1 224 ? -37.778 -8.437  -23.576 1.00 16.46 ?  1261 THR   B CG2 1 
ATOM   3953 N N   . THR   B 1 225 ? -37.247 -12.217 -25.799 1.00 12.59 ?  1262 THR   B N   1 
ATOM   3954 C CA  . THR   B 1 225 ? -37.534 -13.598 -26.170 1.00 16.08 ?  1262 THR   B CA  1 
ATOM   3955 C C   . THR   B 1 225 ? -38.812 -14.094 -25.510 1.00 14.05 ?  1262 THR   B C   1 
ATOM   3956 O O   . THR   B 1 225 ? -39.531 -14.915 -26.090 1.00 14.55 ?  1262 THR   B O   1 
ATOM   3957 C CB  . THR   B 1 225 ? -36.362 -14.507 -25.799 1.00 18.00 ?  1262 THR   B CB  1 
ATOM   3958 O OG1 . THR   B 1 225 ? -36.107 -14.412 -24.392 1.00 25.39 ?  1262 THR   B OG1 1 
ATOM   3959 C CG2 . THR   B 1 225 ? -35.111 -14.108 -26.567 1.00 14.61 ?  1262 THR   B CG2 1 
ATOM   3960 N N   . LYS   B 1 226 ? -39.111 -13.611 -24.302 1.00 13.75 ?  1263 LYS   B N   1 
ATOM   3961 C CA  . LYS   B 1 226 ? -40.364 -13.962 -23.647 1.00 13.69 ?  1263 LYS   B CA  1 
ATOM   3962 C C   . LYS   B 1 226 ? -41.570 -13.388 -24.375 1.00 14.07 ?  1263 LYS   B C   1 
ATOM   3963 O O   . LYS   B 1 226 ? -42.676 -13.920 -24.233 1.00 14.07 ?  1263 LYS   B O   1 
ATOM   3964 C CB  . LYS   B 1 226 ? -40.344 -13.487 -22.195 1.00 15.56 ?  1263 LYS   B CB  1 
ATOM   3965 C CG  . LYS   B 1 226 ? -39.290 -14.180 -21.354 1.00 13.01 ?  1263 LYS   B CG  1 
ATOM   3966 C CD  . LYS   B 1 226 ? -39.037 -13.441 -20.054 1.00 13.44 ?  1263 LYS   B CD  1 
ATOM   3967 C CE  . LYS   B 1 226 ? -38.208 -12.188 -20.279 1.00 14.97 ?  1263 LYS   B CE  1 
ATOM   3968 N NZ  . LYS   B 1 226 ? -37.129 -12.056 -19.260 1.00 15.53 ?  1263 LYS   B NZ  1 
ATOM   3969 N N   . SER   B 1 227 ? -41.386 -12.312 -25.141 1.00 18.22 ?  1264 SER   B N   1 
ATOM   3970 C CA  . SER   B 1 227 ? -42.425 -11.868 -26.058 1.00 14.56 ?  1264 SER   B CA  1 
ATOM   3971 C C   . SER   B 1 227 ? -42.444 -12.696 -27.336 1.00 14.27 ?  1264 SER   B C   1 
ATOM   3972 O O   . SER   B 1 227 ? -43.483 -12.768 -27.998 1.00 13.40 ?  1264 SER   B O   1 
ATOM   3973 C CB  . SER   B 1 227 ? -42.244 -10.384 -26.390 1.00 11.33 ?  1264 SER   B CB  1 
ATOM   3974 O OG  . SER   B 1 227 ? -41.117 -10.169 -27.218 1.00 11.07 ?  1264 SER   B OG  1 
ATOM   3975 N N   . ASP   B 1 228 ? -41.320 -13.319 -27.699 1.00 12.04 ?  1265 ASP   B N   1 
ATOM   3976 C CA  . ASP   B 1 228 ? -41.350 -14.306 -28.773 1.00 14.12 ?  1265 ASP   B CA  1 
ATOM   3977 C C   . ASP   B 1 228 ? -42.111 -15.554 -28.354 1.00 14.80 ?  1265 ASP   B C   1 
ATOM   3978 O O   . ASP   B 1 228 ? -42.709 -16.230 -29.199 1.00 16.31 ?  1265 ASP   B O   1 
ATOM   3979 C CB  . ASP   B 1 228 ? -39.930 -14.669 -29.203 1.00 11.67 ?  1265 ASP   B CB  1 
ATOM   3980 C CG  . ASP   B 1 228 ? -39.500 -13.930 -30.444 1.00 13.56 ?  1265 ASP   B CG  1 
ATOM   3981 O OD1 . ASP   B 1 228 ? -40.375 -13.339 -31.110 1.00 17.87 ?  1265 ASP   B OD1 1 
ATOM   3982 O OD2 . ASP   B 1 228 ? -38.288 -13.922 -30.753 1.00 12.94 -1 1265 ASP   B OD2 1 
ATOM   3983 N N   . VAL   B 1 229 ? -42.081 -15.881 -27.062 1.00 15.57 ?  1266 VAL   B N   1 
ATOM   3984 C CA  . VAL   B 1 229 ? -42.909 -16.965 -26.550 1.00 17.62 ?  1266 VAL   B CA  1 
ATOM   3985 C C   . VAL   B 1 229 ? -44.383 -16.605 -26.678 1.00 16.60 ?  1266 VAL   B C   1 
ATOM   3986 O O   . VAL   B 1 229 ? -45.223 -17.463 -26.975 1.00 13.53 ?  1266 VAL   B O   1 
ATOM   3987 C CB  . VAL   B 1 229 ? -42.516 -17.283 -25.095 1.00 15.89 ?  1266 VAL   B CB  1 
ATOM   3988 C CG1 . VAL   B 1 229 ? -43.507 -18.246 -24.464 1.00 20.12 ?  1266 VAL   B CG1 1 
ATOM   3989 C CG2 . VAL   B 1 229 ? -41.106 -17.847 -25.044 1.00 13.85 ?  1266 VAL   B CG2 1 
ATOM   3990 N N   . TRP   B 1 230 ? -44.720 -15.328 -26.472 1.00 13.70 ?  1267 TRP   B N   1 
ATOM   3991 C CA  . TRP   B 1 230 ? -46.090 -14.878 -26.704 1.00 11.75 ?  1267 TRP   B CA  1 
ATOM   3992 C C   . TRP   B 1 230 ? -46.509 -15.129 -28.148 1.00 10.57 ?  1267 TRP   B C   1 
ATOM   3993 O O   . TRP   B 1 230 ? -47.577 -15.694 -28.406 1.00 10.49 ?  1267 TRP   B O   1 
ATOM   3994 C CB  . TRP   B 1 230 ? -46.229 -13.394 -26.349 1.00 13.24 ?  1267 TRP   B CB  1 
ATOM   3995 C CG  . TRP   B 1 230 ? -47.628 -12.848 -26.520 1.00 9.34  ?  1267 TRP   B CG  1 
ATOM   3996 C CD1 . TRP   B 1 230 ? -48.291 -12.638 -27.696 1.00 10.16 ?  1267 TRP   B CD1 1 
ATOM   3997 C CD2 . TRP   B 1 230 ? -48.525 -12.438 -25.479 1.00 13.16 ?  1267 TRP   B CD2 1 
ATOM   3998 N NE1 . TRP   B 1 230 ? -49.544 -12.131 -27.452 1.00 9.56  ?  1267 TRP   B NE1 1 
ATOM   3999 C CE2 . TRP   B 1 230 ? -49.711 -11.996 -26.099 1.00 12.44 ?  1267 TRP   B CE2 1 
ATOM   4000 C CE3 . TRP   B 1 230 ? -48.438 -12.400 -24.084 1.00 14.84 ?  1267 TRP   B CE3 1 
ATOM   4001 C CZ2 . TRP   B 1 230 ? -50.802 -11.526 -25.372 1.00 10.63 ?  1267 TRP   B CZ2 1 
ATOM   4002 C CZ3 . TRP   B 1 230 ? -49.524 -11.932 -23.365 1.00 12.98 ?  1267 TRP   B CZ3 1 
ATOM   4003 C CH2 . TRP   B 1 230 ? -50.690 -11.502 -24.010 1.00 11.87 ?  1267 TRP   B CH2 1 
ATOM   4004 N N   . SER   B 1 231 ? -45.679 -14.715 -29.108 1.00 12.34 ?  1268 SER   B N   1 
ATOM   4005 C CA  . SER   B 1 231 ? -46.021 -14.918 -30.510 1.00 11.71 ?  1268 SER   B CA  1 
ATOM   4006 C C   . SER   B 1 231 ? -45.905 -16.370 -30.939 1.00 16.23 ?  1268 SER   B C   1 
ATOM   4007 O O   . SER   B 1 231 ? -46.368 -16.712 -32.033 1.00 17.13 ?  1268 SER   B O   1 
ATOM   4008 C CB  . SER   B 1 231 ? -45.126 -14.075 -31.412 1.00 14.08 ?  1268 SER   B CB  1 
ATOM   4009 O OG  . SER   B 1 231 ? -45.400 -12.694 -31.273 1.00 15.93 ?  1268 SER   B OG  1 
ATOM   4010 N N   . PHE   B 1 232 ? -45.276 -17.221 -30.130 1.00 13.07 ?  1269 PHE   B N   1 
ATOM   4011 C CA  . PHE   B 1 232 ? -45.230 -18.631 -30.485 1.00 15.79 ?  1269 PHE   B CA  1 
ATOM   4012 C C   . PHE   B 1 232 ? -46.543 -19.321 -30.154 1.00 15.45 ?  1269 PHE   B C   1 
ATOM   4013 O O   . PHE   B 1 232 ? -46.989 -20.200 -30.897 1.00 13.28 ?  1269 PHE   B O   1 
ATOM   4014 C CB  . PHE   B 1 232 ? -44.072 -19.332 -29.781 1.00 14.72 ?  1269 PHE   B CB  1 
ATOM   4015 C CG  . PHE   B 1 232 ? -43.990 -20.795 -30.094 1.00 14.37 ?  1269 PHE   B CG  1 
ATOM   4016 C CD1 . PHE   B 1 232 ? -43.729 -21.227 -31.383 1.00 16.96 ?  1269 PHE   B CD1 1 
ATOM   4017 C CD2 . PHE   B 1 232 ? -44.205 -21.739 -29.109 1.00 12.56 ?  1269 PHE   B CD2 1 
ATOM   4018 C CE1 . PHE   B 1 232 ? -43.666 -22.575 -31.676 1.00 14.63 ?  1269 PHE   B CE1 1 
ATOM   4019 C CE2 . PHE   B 1 232 ? -44.142 -23.084 -29.395 1.00 13.52 ?  1269 PHE   B CE2 1 
ATOM   4020 C CZ  . PHE   B 1 232 ? -43.873 -23.504 -30.680 1.00 14.13 ?  1269 PHE   B CZ  1 
ATOM   4021 N N   . GLY   B 1 233 ? -47.172 -18.936 -29.042 1.00 12.93 ?  1270 GLY   B N   1 
ATOM   4022 C CA  . GLY   B 1 233 ? -48.499 -19.442 -28.748 1.00 15.28 ?  1270 GLY   B CA  1 
ATOM   4023 C C   . GLY   B 1 233 ? -49.519 -19.034 -29.790 1.00 15.16 ?  1270 GLY   B C   1 
ATOM   4024 O O   . GLY   B 1 233 ? -50.463 -19.779 -30.066 1.00 16.98 ?  1270 GLY   B O   1 
ATOM   4025 N N   . VAL   B 1 234 ? -49.352 -17.847 -30.376 1.00 15.57 ?  1271 VAL   B N   1 
ATOM   4026 C CA  . VAL   B 1 234 ? -50.255 -17.410 -31.435 1.00 14.38 ?  1271 VAL   B CA  1 
ATOM   4027 C C   . VAL   B 1 234 ? -50.012 -18.216 -32.704 1.00 13.98 ?  1271 VAL   B C   1 
ATOM   4028 O O   . VAL   B 1 234 ? -50.954 -18.558 -33.429 1.00 13.92 ?  1271 VAL   B O   1 
ATOM   4029 C CB  . VAL   B 1 234 ? -50.098 -15.898 -31.684 1.00 12.12 ?  1271 VAL   B CB  1 
ATOM   4030 C CG1 . VAL   B 1 234 ? -51.116 -15.419 -32.706 1.00 12.17 ?  1271 VAL   B CG1 1 
ATOM   4031 C CG2 . VAL   B 1 234 ? -50.242 -15.129 -30.384 1.00 10.36 ?  1271 VAL   B CG2 1 
ATOM   4032 N N   . LEU   B 1 235 ? -48.746 -18.526 -32.996 1.00 15.34 ?  1272 LEU   B N   1 
ATOM   4033 C CA  . LEU   B 1 235 ? -48.440 -19.423 -34.106 1.00 16.07 ?  1272 LEU   B CA  1 
ATOM   4034 C C   . LEU   B 1 235 ? -49.089 -20.785 -33.898 1.00 14.07 ?  1272 LEU   B C   1 
ATOM   4035 O O   . LEU   B 1 235 ? -49.634 -21.373 -34.840 1.00 12.90 ?  1272 LEU   B O   1 
ATOM   4036 C CB  . LEU   B 1 235 ? -46.926 -19.570 -34.263 1.00 11.77 ?  1272 LEU   B CB  1 
ATOM   4037 C CG  . LEU   B 1 235 ? -46.416 -20.281 -35.519 1.00 15.11 ?  1272 LEU   B CG  1 
ATOM   4038 C CD1 . LEU   B 1 235 ? -45.164 -19.598 -36.033 1.00 14.24 ?  1272 LEU   B CD1 1 
ATOM   4039 C CD2 . LEU   B 1 235 ? -46.136 -21.749 -35.240 1.00 10.63 ?  1272 LEU   B CD2 1 
ATOM   4040 N N   . LEU   B 1 236 ? -49.033 -21.304 -32.669 1.00 13.72 ?  1273 LEU   B N   1 
ATOM   4041 C CA  . LEU   B 1 236 ? -49.732 -22.545 -32.354 1.00 13.41 ?  1273 LEU   B CA  1 
ATOM   4042 C C   . LEU   B 1 236 ? -51.228 -22.407 -32.602 1.00 14.53 ?  1273 LEU   B C   1 
ATOM   4043 O O   . LEU   B 1 236 ? -51.860 -23.313 -33.158 1.00 13.89 ?  1273 LEU   B O   1 
ATOM   4044 C CB  . LEU   B 1 236 ? -49.465 -22.943 -30.901 1.00 16.77 ?  1273 LEU   B CB  1 
ATOM   4045 C CG  . LEU   B 1 236 ? -48.085 -23.502 -30.551 1.00 14.10 ?  1273 LEU   B CG  1 
ATOM   4046 C CD1 . LEU   B 1 236 ? -47.971 -23.713 -29.050 1.00 12.72 ?  1273 LEU   B CD1 1 
ATOM   4047 C CD2 . LEU   B 1 236 ? -47.818 -24.798 -31.299 1.00 11.49 ?  1273 LEU   B CD2 1 
ATOM   4048 N N   . TRP   B 1 237 ? -51.815 -21.279 -32.188 1.00 14.07 ?  1274 TRP   B N   1 
ATOM   4049 C CA  . TRP   B 1 237 ? -53.234 -21.046 -32.444 1.00 12.59 ?  1274 TRP   B CA  1 
ATOM   4050 C C   . TRP   B 1 237 ? -53.529 -21.043 -33.936 1.00 11.69 ?  1274 TRP   B C   1 
ATOM   4051 O O   . TRP   B 1 237 ? -54.567 -21.553 -34.373 1.00 12.00 ?  1274 TRP   B O   1 
ATOM   4052 C CB  . TRP   B 1 237 ? -53.676 -19.730 -31.806 1.00 14.69 ?  1274 TRP   B CB  1 
ATOM   4053 C CG  . TRP   B 1 237 ? -55.171 -19.564 -31.730 1.00 14.06 ?  1274 TRP   B CG  1 
ATOM   4054 C CD1 . TRP   B 1 237 ? -55.974 -19.843 -30.662 1.00 11.48 ?  1274 TRP   B CD1 1 
ATOM   4055 C CD2 . TRP   B 1 237 ? -56.037 -19.076 -32.765 1.00 11.90 ?  1274 TRP   B CD2 1 
ATOM   4056 N NE1 . TRP   B 1 237 ? -57.284 -19.562 -30.967 1.00 12.12 ?  1274 TRP   B NE1 1 
ATOM   4057 C CE2 . TRP   B 1 237 ? -57.349 -19.089 -32.251 1.00 10.39 ?  1274 TRP   B CE2 1 
ATOM   4058 C CE3 . TRP   B 1 237 ? -55.829 -18.630 -34.074 1.00 13.11 ?  1274 TRP   B CE3 1 
ATOM   4059 C CZ2 . TRP   B 1 237 ? -58.448 -18.674 -33.001 1.00 8.27  ?  1274 TRP   B CZ2 1 
ATOM   4060 C CZ3 . TRP   B 1 237 ? -56.922 -18.219 -34.816 1.00 15.79 ?  1274 TRP   B CZ3 1 
ATOM   4061 C CH2 . TRP   B 1 237 ? -58.214 -18.245 -34.278 1.00 9.85  ?  1274 TRP   B CH2 1 
ATOM   4062 N N   . GLU   B 1 238 ? -52.636 -20.453 -34.731 1.00 14.84 ?  1275 GLU   B N   1 
ATOM   4063 C CA  . GLU   B 1 238 ? -52.765 -20.550 -36.178 1.00 14.58 ?  1275 GLU   B CA  1 
ATOM   4064 C C   . GLU   B 1 238 ? -52.757 -22.009 -36.619 1.00 16.41 ?  1275 GLU   B C   1 
ATOM   4065 O O   . GLU   B 1 238 ? -53.702 -22.476 -37.260 1.00 16.33 ?  1275 GLU   B O   1 
ATOM   4066 C CB  . GLU   B 1 238 ? -51.648 -19.748 -36.848 1.00 14.63 ?  1275 GLU   B CB  1 
ATOM   4067 C CG  . GLU   B 1 238 ? -51.748 -18.250 -36.564 1.00 14.19 ?  1275 GLU   B CG  1 
ATOM   4068 C CD  . GLU   B 1 238 ? -50.729 -17.431 -37.326 1.00 15.17 ?  1275 GLU   B CD  1 
ATOM   4069 O OE1 . GLU   B 1 238 ? -50.996 -17.090 -38.496 1.00 16.97 ?  1275 GLU   B OE1 1 
ATOM   4070 O OE2 . GLU   B 1 238 ? -49.663 -17.122 -36.753 1.00 17.56 -1 1275 GLU   B OE2 1 
ATOM   4071 N N   . LEU   B 1 239 ? -51.727 -22.762 -36.220 1.00 12.15 ?  1276 LEU   B N   1 
ATOM   4072 C CA  . LEU   B 1 239 ? -51.625 -24.168 -36.610 1.00 9.17  ?  1276 LEU   B CA  1 
ATOM   4073 C C   . LEU   B 1 239 ? -52.918 -24.927 -36.333 1.00 12.97 ?  1276 LEU   B C   1 
ATOM   4074 O O   . LEU   B 1 239 ? -53.421 -25.653 -37.196 1.00 10.90 ?  1276 LEU   B O   1 
ATOM   4075 C CB  . LEU   B 1 239 ? -50.456 -24.833 -35.881 1.00 12.86 ?  1276 LEU   B CB  1 
ATOM   4076 C CG  . LEU   B 1 239 ? -49.049 -24.426 -36.317 1.00 11.41 ?  1276 LEU   B CG  1 
ATOM   4077 C CD1 . LEU   B 1 239 ? -48.033 -24.847 -35.272 1.00 8.72  ?  1276 LEU   B CD1 1 
ATOM   4078 C CD2 . LEU   B 1 239 ? -48.710 -25.017 -37.675 1.00 11.24 ?  1276 LEU   B CD2 1 
ATOM   4079 N N   . MET   B 1 240 ? -53.488 -24.748 -35.140 1.00 13.38 ?  1277 MET   B N   1 
ATOM   4080 C CA  . MET   B 1 240 ? -54.657 -25.532 -34.755 1.00 11.41 ?  1277 MET   B CA  1 
ATOM   4081 C C   . MET   B 1 240 ? -55.930 -25.093 -35.469 1.00 14.70 ?  1277 MET   B C   1 
ATOM   4082 O O   . MET   B 1 240 ? -56.862 -25.896 -35.588 1.00 17.95 ?  1277 MET   B O   1 
ATOM   4083 C CB  . MET   B 1 240 ? -54.849 -25.471 -33.241 1.00 13.47 ?  1277 MET   B CB  1 
ATOM   4084 C CG  . MET   B 1 240 ? -53.795 -26.234 -32.435 1.00 14.95 ?  1277 MET   B CG  1 
ATOM   4085 S SD  . MET   B 1 240 ? -53.640 -27.987 -32.866 1.00 20.49 ?  1277 MET   B SD  1 
ATOM   4086 C CE  . MET   B 1 240 ? -52.330 -27.979 -34.092 1.00 11.96 ?  1277 MET   B CE  1 
ATOM   4087 N N   . THR   B 1 241 ? -55.998 -23.849 -35.933 1.00 16.15 ?  1278 THR   B N   1 
ATOM   4088 C CA  . THR   B 1 241 ? -57.086 -23.390 -36.786 1.00 17.41 ?  1278 THR   B CA  1 
ATOM   4089 C C   . THR   B 1 241 ? -56.676 -23.311 -38.248 1.00 16.22 ?  1278 THR   B C   1 
ATOM   4090 O O   . THR   B 1 241 ? -57.473 -22.859 -39.079 1.00 13.37 ?  1278 THR   B O   1 
ATOM   4091 C CB  . THR   B 1 241 ? -57.586 -22.019 -36.325 1.00 11.03 ?  1278 THR   B CB  1 
ATOM   4092 O OG1 . THR   B 1 241 ? -56.536 -21.055 -36.475 1.00 14.77 ?  1278 THR   B OG1 1 
ATOM   4093 C CG2 . THR   B 1 241 ? -58.015 -22.066 -34.872 1.00 12.74 ?  1278 THR   B CG2 1 
ATOM   4094 N N   . ARG   B 1 242 ? -55.455 -23.739 -38.572 1.00 14.18 ?  1279 ARG   B N   1 
ATOM   4095 C CA  . ARG   B 1 242 ? -54.861 -23.629 -39.909 1.00 18.46 ?  1279 ARG   B CA  1 
ATOM   4096 C C   . ARG   B 1 242 ? -54.739 -22.146 -40.243 1.00 15.26 ?  1279 ARG   B C   1 
ATOM   4097 O O   . ARG   B 1 242 ? -54.105 -21.408 -39.471 1.00 18.91 ?  1279 ARG   B O   1 
ATOM   4098 C CB  . ARG   B 1 242 ? -55.645 -24.499 -40.897 1.00 13.67 ?  1279 ARG   B CB  1 
ATOM   4099 C CG  . ARG   B 1 242 ? -55.441 -25.989 -40.635 1.00 18.90 ?  1279 ARG   B CG  1 
ATOM   4100 C CD  . ARG   B 1 242 ? -56.229 -26.891 -41.575 1.00 16.22 ?  1279 ARG   B CD  1 
ATOM   4101 N NE  . ARG   B 1 242 ? -55.648 -26.950 -42.911 1.00 15.66 ?  1279 ARG   B NE  1 
ATOM   4102 C CZ  . ARG   B 1 242 ? -56.211 -27.561 -43.944 1.00 17.84 ?  1279 ARG   B CZ  1 
ATOM   4103 N NH1 . ARG   B 1 242 ? -57.368 -28.193 -43.827 1.00 24.77 ?  1279 ARG   B NH1 1 
ATOM   4104 N NH2 . ARG   B 1 242 ? -55.596 -27.544 -45.124 1.00 17.50 ?  1279 ARG   B NH2 1 
ATOM   4105 N N   . GLY   B 1 243 ? -55.288 -21.658 -41.340 1.00 15.99 ?  1280 GLY   B N   1 
ATOM   4106 C CA  . GLY   B 1 243 ? -54.906 -20.294 -41.632 1.00 24.65 ?  1280 GLY   B CA  1 
ATOM   4107 C C   . GLY   B 1 243 ? -55.739 -19.196 -41.015 1.00 17.65 ?  1280 GLY   B C   1 
ATOM   4108 O O   . GLY   B 1 243 ? -55.686 -18.063 -41.498 1.00 19.34 ?  1280 GLY   B O   1 
ATOM   4109 N N   . ALA   B 1 244 ? -56.490 -19.479 -39.959 1.00 16.64 ?  1281 ALA   B N   1 
ATOM   4110 C CA  . ALA   B 1 244 ? -57.414 -18.488 -39.418 1.00 18.07 ?  1281 ALA   B CA  1 
ATOM   4111 C C   . ALA   B 1 244 ? -56.651 -17.335 -38.773 1.00 18.73 ?  1281 ALA   B C   1 
ATOM   4112 O O   . ALA   B 1 244 ? -55.786 -17.570 -37.921 1.00 16.35 ?  1281 ALA   B O   1 
ATOM   4113 C CB  . ALA   B 1 244 ? -58.353 -19.128 -38.401 1.00 16.75 ?  1281 ALA   B CB  1 
ATOM   4114 N N   . PRO   B 1 245 ? -56.929 -16.092 -39.155 1.00 16.88 ?  1282 PRO   B N   1 
ATOM   4115 C CA  . PRO   B 1 245 ? -56.288 -14.942 -38.500 1.00 15.84 ?  1282 PRO   B CA  1 
ATOM   4116 C C   . PRO   B 1 245 ? -56.738 -14.820 -37.056 1.00 16.02 ?  1282 PRO   B C   1 
ATOM   4117 O O   . PRO   B 1 245 ? -57.902 -15.103 -36.733 1.00 16.44 ?  1282 PRO   B O   1 
ATOM   4118 C CB  . PRO   B 1 245 ? -56.763 -13.739 -39.331 1.00 18.15 ?  1282 PRO   B CB  1 
ATOM   4119 C CG  . PRO   B 1 245 ? -57.856 -14.249 -40.215 1.00 22.42 ?  1282 PRO   B CG  1 
ATOM   4120 C CD  . PRO   B 1 245 ? -57.653 -15.713 -40.379 1.00 21.10 ?  1282 PRO   B CD  1 
ATOM   4121 N N   . PRO   B 1 246 ? -55.851 -14.395 -36.162 1.00 16.47 ?  1283 PRO   B N   1 
ATOM   4122 C CA  . PRO   B 1 246 ? -56.217 -14.282 -34.748 1.00 18.68 ?  1283 PRO   B CA  1 
ATOM   4123 C C   . PRO   B 1 246 ? -57.030 -13.030 -34.460 1.00 19.28 ?  1283 PRO   B C   1 
ATOM   4124 O O   . PRO   B 1 246 ? -56.869 -11.987 -35.099 1.00 17.84 ?  1283 PRO   B O   1 
ATOM   4125 C CB  . PRO   B 1 246 ? -54.858 -14.228 -34.042 1.00 18.43 ?  1283 PRO   B CB  1 
ATOM   4126 C CG  . PRO   B 1 246 ? -53.962 -13.590 -35.045 1.00 18.81 ?  1283 PRO   B CG  1 
ATOM   4127 C CD  . PRO   B 1 246 ? -54.434 -14.069 -36.395 1.00 17.32 ?  1283 PRO   B CD  1 
ATOM   4128 N N   . TYR   B 1 247 ? -57.901 -13.152 -33.461 1.00 19.06 ?  1284 TYR   B N   1 
ATOM   4129 C CA  . TYR   B 1 247 ? -58.847 -12.111 -33.088 1.00 21.40 ?  1284 TYR   B CA  1 
ATOM   4130 C C   . TYR   B 1 247 ? -59.578 -11.510 -34.288 1.00 22.34 ?  1284 TYR   B C   1 
ATOM   4131 O O   . TYR   B 1 247 ? -59.459 -10.316 -34.566 1.00 18.01 ?  1284 TYR   B O   1 
ATOM   4132 C CB  . TYR   B 1 247 ? -58.154 -10.999 -32.295 1.00 19.17 ?  1284 TYR   B CB  1 
ATOM   4133 C CG  . TYR   B 1 247 ? -57.110 -11.425 -31.290 1.00 13.27 ?  1284 TYR   B CG  1 
ATOM   4134 C CD1 . TYR   B 1 247 ? -55.778 -11.550 -31.657 1.00 12.68 ?  1284 TYR   B CD1 1 
ATOM   4135 C CD2 . TYR   B 1 247 ? -57.446 -11.642 -29.961 1.00 14.67 ?  1284 TYR   B CD2 1 
ATOM   4136 C CE1 . TYR   B 1 247 ? -54.815 -11.912 -30.737 1.00 10.80 ?  1284 TYR   B CE1 1 
ATOM   4137 C CE2 . TYR   B 1 247 ? -56.490 -12.004 -29.033 1.00 10.76 ?  1284 TYR   B CE2 1 
ATOM   4138 C CZ  . TYR   B 1 247 ? -55.176 -12.137 -29.427 1.00 9.61  ?  1284 TYR   B CZ  1 
ATOM   4139 O OH  . TYR   B 1 247 ? -54.220 -12.498 -28.506 1.00 12.06 ?  1284 TYR   B OH  1 
ATOM   4140 N N   . PRO   B 1 248 ? -60.354 -12.314 -35.027 1.00 28.69 ?  1285 PRO   B N   1 
ATOM   4141 C CA  . PRO   B 1 248 ? -61.233 -11.705 -36.036 1.00 32.55 ?  1285 PRO   B CA  1 
ATOM   4142 C C   . PRO   B 1 248 ? -62.287 -10.821 -35.402 1.00 30.60 ?  1285 PRO   B C   1 
ATOM   4143 O O   . PRO   B 1 248 ? -62.747 -9.857  -36.027 1.00 23.95 ?  1285 PRO   B O   1 
ATOM   4144 C CB  . PRO   B 1 248 ? -61.846 -12.918 -36.747 1.00 25.92 ?  1285 PRO   B CB  1 
ATOM   4145 C CG  . PRO   B 1 248 ? -61.826 -13.990 -35.718 1.00 25.61 ?  1285 PRO   B CG  1 
ATOM   4146 C CD  . PRO   B 1 248 ? -60.569 -13.768 -34.921 1.00 25.61 ?  1285 PRO   B CD  1 
ATOM   4147 N N   . ASP   B 1 249 ? -62.672 -11.132 -34.163 1.00 33.35 ?  1286 ASP   B N   1 
ATOM   4148 C CA  . ASP   B 1 249 ? -63.547 -10.259 -33.389 1.00 30.85 ?  1286 ASP   B CA  1 
ATOM   4149 C C   . ASP   B 1 249 ? -62.954 -8.864  -33.255 1.00 29.38 ?  1286 ASP   B C   1 
ATOM   4150 O O   . ASP   B 1 249 ? -63.614 -7.858  -33.541 1.00 28.39 ?  1286 ASP   B O   1 
ATOM   4151 C CB  . ASP   B 1 249 ? -63.765 -10.852 -31.995 1.00 35.72 ?  1286 ASP   B CB  1 
ATOM   4152 C CG  . ASP   B 1 249 ? -64.557 -12.137 -32.018 1.00 36.53 ?  1286 ASP   B CG  1 
ATOM   4153 O OD1 . ASP   B 1 249 ? -65.223 -12.414 -33.035 1.00 36.30 ?  1286 ASP   B OD1 1 
ATOM   4154 O OD2 . ASP   B 1 249 ? -64.501 -12.878 -31.013 1.00 47.52 -1 1286 ASP   B OD2 1 
ATOM   4155 N N   . VAL   B 1 250 ? -61.698 -8.792  -32.831 1.00 24.28 ?  1287 VAL   B N   1 
ATOM   4156 C CA  . VAL   B 1 250 ? -61.141 -7.592  -32.222 1.00 23.09 ?  1287 VAL   B CA  1 
ATOM   4157 C C   . VAL   B 1 250 ? -60.537 -6.691  -33.288 1.00 23.98 ?  1287 VAL   B C   1 
ATOM   4158 O O   . VAL   B 1 250 ? -59.805 -7.152  -34.173 1.00 24.73 ?  1287 VAL   B O   1 
ATOM   4159 C CB  . VAL   B 1 250 ? -60.099 -7.962  -31.155 1.00 21.58 ?  1287 VAL   B CB  1 
ATOM   4160 C CG1 . VAL   B 1 250 ? -59.493 -6.716  -30.548 1.00 24.49 ?  1287 VAL   B CG1 1 
ATOM   4161 C CG2 . VAL   B 1 250 ? -60.739 -8.823  -30.081 1.00 14.38 ?  1287 VAL   B CG2 1 
ATOM   4162 N N   . ASN   B 1 251 ? -60.847 -5.402  -33.196 1.00 17.69 ?  1288 ASN   B N   1 
ATOM   4163 C CA  . ASN   B 1 251 ? -60.258 -4.396  -34.062 1.00 17.15 ?  1288 ASN   B CA  1 
ATOM   4164 C C   . ASN   B 1 251 ? -58.765 -4.251  -33.770 1.00 23.68 ?  1288 ASN   B C   1 
ATOM   4165 O O   . ASN   B 1 251 ? -58.318 -4.389  -32.628 1.00 21.80 ?  1288 ASN   B O   1 
ATOM   4166 C CB  . ASN   B 1 251 ? -60.985 -3.067  -33.862 1.00 20.11 ?  1288 ASN   B CB  1 
ATOM   4167 C CG  . ASN   B 1 251 ? -60.158 -1.883  -34.276 1.00 23.83 ?  1288 ASN   B CG  1 
ATOM   4168 O OD1 . ASN   B 1 251 ? -59.607 -1.183  -33.433 1.00 29.66 ?  1288 ASN   B OD1 1 
ATOM   4169 N ND2 . ASN   B 1 251 ? -60.078 -1.639  -35.577 1.00 29.00 ?  1288 ASN   B ND2 1 
ATOM   4170 N N   . THR   B 1 252 ? -57.994 -3.958  -34.822 1.00 23.88 ?  1289 THR   B N   1 
ATOM   4171 C CA  . THR   B 1 252 ? -56.536 -4.032  -34.730 1.00 19.27 ?  1289 THR   B CA  1 
ATOM   4172 C C   . THR   B 1 252 ? -55.982 -3.053  -33.700 1.00 21.09 ?  1289 THR   B C   1 
ATOM   4173 O O   . THR   B 1 252 ? -55.255 -3.449  -32.781 1.00 16.80 ?  1289 THR   B O   1 
ATOM   4174 C CB  . THR   B 1 252 ? -55.907 -3.775  -36.098 1.00 18.39 ?  1289 THR   B CB  1 
ATOM   4175 O OG1 . THR   B 1 252 ? -56.371 -4.758  -37.032 1.00 22.50 ?  1289 THR   B OG1 1 
ATOM   4176 C CG2 . THR   B 1 252 ? -54.394 -3.855  -35.997 1.00 19.93 ?  1289 THR   B CG2 1 
ATOM   4177 N N   . PHE   B 1 253 ? -56.296 -1.767  -33.843 1.00 18.93 ?  1290 PHE   B N   1 
ATOM   4178 C CA  . PHE   B 1 253 ? -55.826 -0.781  -32.877 1.00 23.55 ?  1290 PHE   B CA  1 
ATOM   4179 C C   . PHE   B 1 253 ? -56.591 -0.838  -31.562 1.00 24.49 ?  1290 PHE   B C   1 
ATOM   4180 O O   . PHE   B 1 253 ? -56.237 -0.114  -30.625 1.00 28.14 ?  1290 PHE   B O   1 
ATOM   4181 C CB  . PHE   B 1 253 ? -55.900 0.630   -33.469 1.00 24.14 ?  1290 PHE   B CB  1 
ATOM   4182 C CG  . PHE   B 1 253 ? -57.210 0.952   -34.120 1.00 23.03 ?  1290 PHE   B CG  1 
ATOM   4183 C CD1 . PHE   B 1 253 ? -58.262 1.445   -33.376 1.00 21.20 ?  1290 PHE   B CD1 1 
ATOM   4184 C CD2 . PHE   B 1 253 ? -57.385 0.773   -35.481 1.00 21.18 ?  1290 PHE   B CD2 1 
ATOM   4185 C CE1 . PHE   B 1 253 ? -59.463 1.740   -33.978 1.00 22.31 ?  1290 PHE   B CE1 1 
ATOM   4186 C CE2 . PHE   B 1 253 ? -58.587 1.074   -36.084 1.00 18.83 ?  1290 PHE   B CE2 1 
ATOM   4187 C CZ  . PHE   B 1 253 ? -59.627 1.556   -35.329 1.00 21.98 ?  1290 PHE   B CZ  1 
ATOM   4188 N N   . ASP   B 1 254 ? -57.625 -1.673  -31.474 1.00 20.04 ?  1291 ASP   B N   1 
ATOM   4189 C CA  . ASP   B 1 254 ? -58.313 -1.962  -30.224 1.00 22.80 ?  1291 ASP   B CA  1 
ATOM   4190 C C   . ASP   B 1 254 ? -57.967 -3.357  -29.715 1.00 26.05 ?  1291 ASP   B C   1 
ATOM   4191 O O   . ASP   B 1 254 ? -58.803 -4.022  -29.101 1.00 17.51 ?  1291 ASP   B O   1 
ATOM   4192 C CB  . ASP   B 1 254 ? -59.825 -1.816  -30.393 1.00 19.57 ?  1291 ASP   B CB  1 
ATOM   4193 C CG  . ASP   B 1 254 ? -60.550 -1.632  -29.072 1.00 22.96 ?  1291 ASP   B CG  1 
ATOM   4194 O OD1 . ASP   B 1 254 ? -59.993 -0.972  -28.170 1.00 24.07 ?  1291 ASP   B OD1 1 
ATOM   4195 O OD2 . ASP   B 1 254 ? -61.676 -2.155  -28.934 1.00 22.53 -1 1291 ASP   B OD2 1 
ATOM   4196 N N   . ILE   B 1 255 ? -56.734 -3.813  -29.956 1.00 22.41 ?  1292 ILE   B N   1 
ATOM   4197 C CA  . ILE   B 1 255 ? -56.319 -5.144  -29.518 1.00 22.92 ?  1292 ILE   B CA  1 
ATOM   4198 C C   . ILE   B 1 255 ? -55.630 -5.138  -28.162 1.00 18.69 ?  1292 ILE   B C   1 
ATOM   4199 O O   . ILE   B 1 255 ? -55.409 -6.215  -27.587 1.00 20.21 ?  1292 ILE   B O   1 
ATOM   4200 C CB  . ILE   B 1 255 ? -55.381 -5.805  -30.549 1.00 15.95 ?  1292 ILE   B CB  1 
ATOM   4201 N N   . THR   B 1 256 ? -55.282 -3.966  -27.629 1.00 16.34 ?  1293 THR   B N   1 
ATOM   4202 C CA  . THR   B 1 256 ? -54.621 -3.908  -26.330 1.00 13.24 ?  1293 THR   B CA  1 
ATOM   4203 C C   . THR   B 1 256 ? -55.634 -3.918  -25.194 1.00 16.36 ?  1293 THR   B C   1 
ATOM   4204 O O   . THR   B 1 256 ? -55.469 -4.650  -24.212 1.00 16.26 ?  1293 THR   B O   1 
ATOM   4205 C CB  . THR   B 1 256 ? -53.739 -2.663  -26.245 1.00 11.43 ?  1293 THR   B CB  1 
ATOM   4206 O OG1 . THR   B 1 256 ? -53.055 -2.476  -27.490 1.00 12.69 ?  1293 THR   B OG1 1 
ATOM   4207 C CG2 . THR   B 1 256 ? -52.722 -2.810  -25.125 1.00 11.35 ?  1293 THR   B CG2 1 
ATOM   4208 N N   . VAL   B 1 257 ? -56.684 -3.098  -25.311 1.00 20.93 ?  1294 VAL   B N   1 
ATOM   4209 C CA  . VAL   B 1 257 ? -57.762 -3.104  -24.325 1.00 20.29 ?  1294 VAL   B CA  1 
ATOM   4210 C C   . VAL   B 1 257 ? -58.336 -4.504  -24.180 1.00 19.57 ?  1294 VAL   B C   1 
ATOM   4211 O O   . VAL   B 1 257 ? -58.730 -4.920  -23.087 1.00 14.35 ?  1294 VAL   B O   1 
ATOM   4212 C CB  . VAL   B 1 257 ? -58.855 -2.094  -24.723 1.00 23.14 ?  1294 VAL   B CB  1 
ATOM   4213 C CG1 . VAL   B 1 257 ? -59.746 -1.775  -23.533 1.00 28.63 ?  1294 VAL   B CG1 1 
ATOM   4214 C CG2 . VAL   B 1 257 ? -58.237 -0.834  -25.308 1.00 22.75 ?  1294 VAL   B CG2 1 
ATOM   4215 N N   . TYR   B 1 258 ? -58.396 -5.249  -25.289 1.00 23.12 ?  1295 TYR   B N   1 
ATOM   4216 C CA  . TYR   B 1 258 ? -58.879 -6.628  -25.264 1.00 19.68 ?  1295 TYR   B CA  1 
ATOM   4217 C C   . TYR   B 1 258 ? -57.923 -7.550  -24.521 1.00 22.87 ?  1295 TYR   B C   1 
ATOM   4218 O O   . TYR   B 1 258 ? -58.367 -8.509  -23.879 1.00 20.19 ?  1295 TYR   B O   1 
ATOM   4219 C CB  . TYR   B 1 258 ? -59.088 -7.133  -26.691 1.00 19.10 ?  1295 TYR   B CB  1 
ATOM   4220 C CG  . TYR   B 1 258 ? -59.655 -8.531  -26.788 1.00 20.05 ?  1295 TYR   B CG  1 
ATOM   4221 C CD1 . TYR   B 1 258 ? -60.999 -8.780  -26.533 1.00 16.87 ?  1295 TYR   B CD1 1 
ATOM   4222 C CD2 . TYR   B 1 258 ? -58.846 -9.604  -27.142 1.00 22.23 ?  1295 TYR   B CD2 1 
ATOM   4223 C CE1 . TYR   B 1 258 ? -61.519 -10.060 -26.626 1.00 21.09 ?  1295 TYR   B CE1 1 
ATOM   4224 C CE2 . TYR   B 1 258 ? -59.357 -10.885 -27.234 1.00 23.90 ?  1295 TYR   B CE2 1 
ATOM   4225 C CZ  . TYR   B 1 258 ? -60.692 -11.107 -26.976 1.00 22.92 ?  1295 TYR   B CZ  1 
ATOM   4226 O OH  . TYR   B 1 258 ? -61.201 -12.379 -27.065 1.00 24.32 ?  1295 TYR   B OH  1 
ATOM   4227 N N   . LEU   B 1 259 ? -56.621 -7.271  -24.571 1.00 20.77 ?  1296 LEU   B N   1 
ATOM   4228 C CA  . LEU   B 1 259 ? -55.677 -8.076  -23.804 1.00 20.93 ?  1296 LEU   B CA  1 
ATOM   4229 C C   . LEU   B 1 259 ? -55.696 -7.700  -22.325 1.00 19.53 ?  1296 LEU   B C   1 
ATOM   4230 O O   . LEU   B 1 259 ? -55.527 -8.568  -21.461 1.00 16.21 ?  1296 LEU   B O   1 
ATOM   4231 C CB  . LEU   B 1 259 ? -54.265 -7.930  -24.376 1.00 22.43 ?  1296 LEU   B CB  1 
ATOM   4232 C CG  . LEU   B 1 259 ? -54.028 -8.520  -25.769 1.00 21.56 ?  1296 LEU   B CG  1 
ATOM   4233 C CD1 . LEU   B 1 259 ? -52.627 -8.205  -26.275 1.00 17.74 ?  1296 LEU   B CD1 1 
ATOM   4234 C CD2 . LEU   B 1 259 ? -54.275 -10.019 -25.760 1.00 14.86 ?  1296 LEU   B CD2 1 
ATOM   4235 N N   . LEU   B 1 260 ? -55.926 -6.420  -22.010 1.00 19.25 ?  1297 LEU   B N   1 
ATOM   4236 C CA  . LEU   B 1 260 ? -55.727 -5.926  -20.648 1.00 17.36 ?  1297 LEU   B CA  1 
ATOM   4237 C C   . LEU   B 1 260 ? -56.849 -6.285  -19.678 1.00 20.63 ?  1297 LEU   B C   1 
ATOM   4238 O O   . LEU   B 1 260 ? -56.703 -6.025  -18.479 1.00 20.74 ?  1297 LEU   B O   1 
ATOM   4239 C CB  . LEU   B 1 260 ? -55.528 -4.405  -20.652 1.00 14.03 ?  1297 LEU   B CB  1 
ATOM   4240 C CG  . LEU   B 1 260 ? -54.136 -3.891  -21.032 1.00 16.50 ?  1297 LEU   B CG  1 
ATOM   4241 C CD1 . LEU   B 1 260 ? -54.224 -2.518  -21.674 1.00 16.68 ?  1297 LEU   B CD1 1 
ATOM   4242 C CD2 . LEU   B 1 260 ? -53.232 -3.861  -19.805 1.00 13.85 ?  1297 LEU   B CD2 1 
ATOM   4243 N N   . GLN   B 1 261 ? -57.962 -6.850  -20.146 1.00 26.50 ?  1298 GLN   B N   1 
ATOM   4244 C CA  . GLN   B 1 261 ? -58.993 -7.388  -19.263 1.00 21.16 ?  1298 GLN   B CA  1 
ATOM   4245 C C   . GLN   B 1 261 ? -58.947 -8.906  -19.189 1.00 27.39 ?  1298 GLN   B C   1 
ATOM   4246 O O   . GLN   B 1 261 ? -59.903 -9.529  -18.714 1.00 30.58 ?  1298 GLN   B O   1 
ATOM   4247 C CB  . GLN   B 1 261 ? -60.383 -6.925  -19.704 1.00 21.26 ?  1298 GLN   B CB  1 
ATOM   4248 N N   . GLY   B 1 262 ? -57.859 -9.508  -19.658 1.00 28.50 ?  1299 GLY   B N   1 
ATOM   4249 C CA  . GLY   B 1 262 ? -57.640 -10.930 -19.518 1.00 23.79 ?  1299 GLY   B CA  1 
ATOM   4250 C C   . GLY   B 1 262 ? -58.193 -11.798 -20.625 1.00 24.96 ?  1299 GLY   B C   1 
ATOM   4251 O O   . GLY   B 1 262 ? -58.239 -13.023 -20.460 1.00 21.22 ?  1299 GLY   B O   1 
ATOM   4252 N N   . ARG   B 1 263 ? -58.612 -11.215 -21.743 1.00 24.55 ?  1300 ARG   B N   1 
ATOM   4253 C CA  . ARG   B 1 263 ? -59.180 -12.001 -22.827 1.00 21.23 ?  1300 ARG   B CA  1 
ATOM   4254 C C   . ARG   B 1 263 ? -58.077 -12.561 -23.716 1.00 18.69 ?  1300 ARG   B C   1 
ATOM   4255 O O   . ARG   B 1 263 ? -57.117 -11.864 -24.057 1.00 18.22 ?  1300 ARG   B O   1 
ATOM   4256 C CB  . ARG   B 1 263 ? -60.146 -11.154 -23.652 1.00 17.38 ?  1300 ARG   B CB  1 
ATOM   4257 N N   . ARG   B 1 264 ? -58.222 -13.830 -24.089 1.00 20.12 ?  1301 ARG   B N   1 
ATOM   4258 C CA  . ARG   B 1 264 ? -57.239 -14.531 -24.901 1.00 17.95 ?  1301 ARG   B CA  1 
ATOM   4259 C C   . ARG   B 1 264 ? -57.942 -15.249 -26.044 1.00 13.44 ?  1301 ARG   B C   1 
ATOM   4260 O O   . ARG   B 1 264 ? -59.169 -15.372 -26.072 1.00 18.28 ?  1301 ARG   B O   1 
ATOM   4261 C CB  . ARG   B 1 264 ? -56.434 -15.532 -24.062 1.00 14.83 ?  1301 ARG   B CB  1 
ATOM   4262 C CG  . ARG   B 1 264 ? -55.550 -14.891 -23.008 1.00 13.84 ?  1301 ARG   B CG  1 
ATOM   4263 C CD  . ARG   B 1 264 ? -54.539 -13.956 -23.644 1.00 16.78 ?  1301 ARG   B CD  1 
ATOM   4264 N NE  . ARG   B 1 264 ? -53.590 -13.428 -22.672 1.00 21.01 ?  1301 ARG   B NE  1 
ATOM   4265 C CZ  . ARG   B 1 264 ? -53.781 -12.324 -21.964 1.00 17.97 ?  1301 ARG   B CZ  1 
ATOM   4266 N NH1 . ARG   B 1 264 ? -54.884 -11.605 -22.090 1.00 19.48 ?  1301 ARG   B NH1 1 
ATOM   4267 N NH2 . ARG   B 1 264 ? -52.840 -11.930 -21.111 1.00 12.89 ?  1301 ARG   B NH2 1 
ATOM   4268 N N   . LEU   B 1 265 ? -57.143 -15.722 -26.997 1.00 11.65 ?  1302 LEU   B N   1 
ATOM   4269 C CA  . LEU   B 1 265 ? -57.683 -16.517 -28.091 1.00 13.16 ?  1302 LEU   B CA  1 
ATOM   4270 C C   . LEU   B 1 265 ? -58.242 -17.831 -27.559 1.00 14.30 ?  1302 LEU   B C   1 
ATOM   4271 O O   . LEU   B 1 265 ? -57.688 -18.434 -26.636 1.00 14.93 ?  1302 LEU   B O   1 
ATOM   4272 C CB  . LEU   B 1 265 ? -56.601 -16.775 -29.140 1.00 11.88 ?  1302 LEU   B CB  1 
ATOM   4273 C CG  . LEU   B 1 265 ? -56.095 -15.518 -29.850 1.00 12.39 ?  1302 LEU   B CG  1 
ATOM   4274 C CD1 . LEU   B 1 265 ? -54.726 -15.745 -30.477 1.00 13.79 ?  1302 LEU   B CD1 1 
ATOM   4275 C CD2 . LEU   B 1 265 ? -57.100 -15.071 -30.896 1.00 13.36 ?  1302 LEU   B CD2 1 
ATOM   4276 N N   . LEU   B 1 266 ? -59.353 -18.269 -28.143 1.00 14.03 ?  1303 LEU   B N   1 
ATOM   4277 C CA  . LEU   B 1 266 ? -60.116 -19.390 -27.617 1.00 16.64 ?  1303 LEU   B CA  1 
ATOM   4278 C C   . LEU   B 1 266 ? -59.626 -20.713 -28.195 1.00 15.20 ?  1303 LEU   B C   1 
ATOM   4279 O O   . LEU   B 1 266 ? -59.012 -20.767 -29.263 1.00 17.93 ?  1303 LEU   B O   1 
ATOM   4280 C CB  . LEU   B 1 266 ? -61.603 -19.206 -27.915 1.00 11.36 ?  1303 LEU   B CB  1 
ATOM   4281 C CG  . LEU   B 1 266 ? -62.247 -17.981 -27.264 1.00 9.23  ?  1303 LEU   B CG  1 
ATOM   4282 C CD1 . LEU   B 1 266 ? -63.728 -17.912 -27.598 1.00 9.44  ?  1303 LEU   B CD1 1 
ATOM   4283 C CD2 . LEU   B 1 266 ? -62.032 -17.999 -25.758 1.00 7.74  ?  1303 LEU   B CD2 1 
ATOM   4284 N N   . GLN   B 1 267 ? -59.922 -21.786 -27.474 1.00 14.43 ?  1304 GLN   B N   1 
ATOM   4285 C CA  . GLN   B 1 267 ? -59.462 -23.116 -27.859 1.00 16.05 ?  1304 GLN   B CA  1 
ATOM   4286 C C   . GLN   B 1 267 ? -60.216 -23.623 -29.079 1.00 17.75 ?  1304 GLN   B C   1 
ATOM   4287 O O   . GLN   B 1 267 ? -61.438 -23.806 -29.008 1.00 17.81 ?  1304 GLN   B O   1 
ATOM   4288 C CB  . GLN   B 1 267 ? -59.647 -24.092 -26.706 1.00 13.03 ?  1304 GLN   B CB  1 
ATOM   4289 C CG  . GLN   B 1 267 ? -59.392 -25.537 -27.089 1.00 15.13 ?  1304 GLN   B CG  1 
ATOM   4290 C CD  . GLN   B 1 267 ? -59.267 -26.439 -25.884 1.00 11.85 ?  1304 GLN   B CD  1 
ATOM   4291 O OE1 . GLN   B 1 267 ? -59.881 -26.196 -24.845 1.00 9.70  ?  1304 GLN   B OE1 1 
ATOM   4292 N NE2 . GLN   B 1 267 ? -58.467 -27.490 -26.013 1.00 16.51 ?  1304 GLN   B NE2 1 
ATOM   4293 N N   . PRO   B 1 268 ? -59.545 -23.874 -30.198 1.00 15.67 ?  1305 PRO   B N   1 
ATOM   4294 C CA  . PRO   B 1 268 ? -60.224 -24.510 -31.330 1.00 19.50 ?  1305 PRO   B CA  1 
ATOM   4295 C C   . PRO   B 1 268 ? -60.560 -25.959 -31.017 1.00 19.14 ?  1305 PRO   B C   1 
ATOM   4296 O O   . PRO   B 1 268 ? -59.831 -26.653 -30.303 1.00 15.88 ?  1305 PRO   B O   1 
ATOM   4297 C CB  . PRO   B 1 268 ? -59.207 -24.401 -32.471 1.00 13.88 ?  1305 PRO   B CB  1 
ATOM   4298 C CG  . PRO   B 1 268 ? -57.892 -24.192 -31.810 1.00 15.59 ?  1305 PRO   B CG  1 
ATOM   4299 C CD  . PRO   B 1 268 ? -58.139 -23.542 -30.488 1.00 14.34 ?  1305 PRO   B CD  1 
ATOM   4300 N N   . GLU   B 1 269 ? -61.683 -26.417 -31.578 1.00 20.75 ?  1306 GLU   B N   1 
ATOM   4301 C CA  . GLU   B 1 269 ? -62.282 -27.690 -31.191 1.00 28.79 ?  1306 GLU   B CA  1 
ATOM   4302 C C   . GLU   B 1 269 ? -61.421 -28.902 -31.525 1.00 21.70 ?  1306 GLU   B C   1 
ATOM   4303 O O   . GLU   B 1 269 ? -61.762 -30.012 -31.102 1.00 29.87 ?  1306 GLU   B O   1 
ATOM   4304 C CB  . GLU   B 1 269 ? -63.655 -27.842 -31.850 1.00 26.77 ?  1306 GLU   B CB  1 
ATOM   4305 C CG  . GLU   B 1 269 ? -63.656 -27.616 -33.352 1.00 28.24 ?  1306 GLU   B CG  1 
ATOM   4306 C CD  . GLU   B 1 269 ? -64.924 -28.121 -34.015 1.00 31.66 ?  1306 GLU   B CD  1 
ATOM   4307 O OE1 . GLU   B 1 269 ? -65.232 -29.323 -33.874 1.00 34.12 ?  1306 GLU   B OE1 1 
ATOM   4308 O OE2 . GLU   B 1 269 ? -65.613 -27.316 -34.678 1.00 28.48 -1 1306 GLU   B OE2 1 
ATOM   4309 N N   . TYR   B 1 270 ? -60.329 -28.731 -32.267 1.00 20.47 ?  1307 TYR   B N   1 
ATOM   4310 C CA  . TYR   B 1 270 ? -59.422 -29.832 -32.563 1.00 24.75 ?  1307 TYR   B CA  1 
ATOM   4311 C C   . TYR   B 1 270 ? -58.044 -29.615 -31.958 1.00 22.71 ?  1307 TYR   B C   1 
ATOM   4312 O O   . TYR   B 1 270 ? -57.114 -30.369 -32.264 1.00 19.43 ?  1307 TYR   B O   1 
ATOM   4313 C CB  . TYR   B 1 270 ? -59.329 -30.043 -34.074 1.00 26.14 ?  1307 TYR   B CB  1 
ATOM   4314 C CG  . TYR   B 1 270 ? -60.664 -30.426 -34.655 1.00 28.33 ?  1307 TYR   B CG  1 
ATOM   4315 C CD1 . TYR   B 1 270 ? -61.190 -31.694 -34.451 1.00 21.95 ?  1307 TYR   B CD1 1 
ATOM   4316 C CD2 . TYR   B 1 270 ? -61.421 -29.508 -35.366 1.00 22.68 ?  1307 TYR   B CD2 1 
ATOM   4317 C CE1 . TYR   B 1 270 ? -62.420 -32.046 -34.964 1.00 25.16 ?  1307 TYR   B CE1 1 
ATOM   4318 C CE2 . TYR   B 1 270 ? -62.654 -29.849 -35.879 1.00 24.44 ?  1307 TYR   B CE2 1 
ATOM   4319 C CZ  . TYR   B 1 270 ? -63.149 -31.120 -35.678 1.00 24.60 ?  1307 TYR   B CZ  1 
ATOM   4320 O OH  . TYR   B 1 270 ? -64.378 -31.462 -36.193 1.00 14.65 ?  1307 TYR   B OH  1 
ATOM   4321 N N   . CYS   B 1 271 ? -57.887 -28.600 -31.119 1.00 22.75 ?  1308 CYS   B N   1 
ATOM   4322 C CA  . CYS   B 1 271 ? -56.692 -28.462 -30.308 1.00 19.57 ?  1308 CYS   B CA  1 
ATOM   4323 C C   . CYS   B 1 271 ? -56.862 -29.315 -29.058 1.00 16.32 ?  1308 CYS   B C   1 
ATOM   4324 O O   . CYS   B 1 271 ? -57.767 -29.037 -28.261 1.00 18.21 ?  1308 CYS   B O   1 
ATOM   4325 C CB  . CYS   B 1 271 ? -56.470 -27.007 -29.923 1.00 16.27 ?  1308 CYS   B CB  1 
ATOM   4326 S SG  . CYS   B 1 271 ? -54.979 -26.733 -28.938 1.00 21.42 ?  1308 CYS   B SG  1 
ATOM   4327 N N   . PRO   B 1 272 ? -56.058 -30.365 -28.858 1.00 14.50 ?  1309 PRO   B N   1 
ATOM   4328 C CA  . PRO   B 1 272 ? -56.156 -31.139 -27.610 1.00 16.51 ?  1309 PRO   B CA  1 
ATOM   4329 C C   . PRO   B 1 272 ? -55.965 -30.232 -26.404 1.00 15.69 ?  1309 PRO   B C   1 
ATOM   4330 O O   . PRO   B 1 272 ? -55.345 -29.166 -26.492 1.00 19.57 ?  1309 PRO   B O   1 
ATOM   4331 C CB  . PRO   B 1 272 ? -55.016 -32.158 -27.721 1.00 11.99 ?  1309 PRO   B CB  1 
ATOM   4332 C CG  . PRO   B 1 272 ? -54.750 -32.259 -29.212 1.00 12.46 ?  1309 PRO   B CG  1 
ATOM   4333 C CD  . PRO   B 1 272 ? -55.036 -30.899 -29.777 1.00 20.85 ?  1309 PRO   B CD  1 
ATOM   4334 N N   . ASP   B 1 273 ? -56.560 -30.651 -25.280 1.00 12.95 ?  1310 ASP   B N   1 
ATOM   4335 C CA  . ASP   B 1 273 ? -56.470 -29.900 -24.027 1.00 13.10 ?  1310 ASP   B CA  1 
ATOM   4336 C C   . ASP   B 1 273 ? -55.053 -29.592 -23.560 1.00 16.96 ?  1310 ASP   B C   1 
ATOM   4337 O O   . ASP   B 1 273 ? -54.837 -28.464 -23.054 1.00 18.67 ?  1310 ASP   B O   1 
ATOM   4338 C CB  . ASP   B 1 273 ? -57.292 -30.603 -22.919 1.00 15.40 ?  1310 ASP   B CB  1 
ATOM   4339 C CG  . ASP   B 1 273 ? -58.761 -30.346 -23.059 1.00 17.08 ?  1310 ASP   B CG  1 
ATOM   4340 O OD1 . ASP   B 1 273 ? -59.210 -29.964 -24.158 1.00 13.79 ?  1310 ASP   B OD1 1 
ATOM   4341 O OD2 . ASP   B 1 273 ? -59.438 -30.555 -22.043 1.00 22.15 -1 1310 ASP   B OD2 1 
ATOM   4342 N N   . PRO   B 1 274 ? -54.098 -30.514 -23.626 1.00 17.97 ?  1311 PRO   B N   1 
ATOM   4343 C CA  . PRO   B 1 274 ? -52.728 -30.173 -23.269 1.00 14.66 ?  1311 PRO   B CA  1 
ATOM   4344 C C   . PRO   B 1 274 ? -52.051 -29.051 -24.070 1.00 16.07 ?  1311 PRO   B C   1 
ATOM   4345 O O   . PRO   B 1 274 ? -51.378 -28.163 -23.509 1.00 14.77 ?  1311 PRO   B O   1 
ATOM   4346 C CB  . PRO   B 1 274 ? -51.997 -31.523 -23.505 1.00 12.70 ?  1311 PRO   B CB  1 
ATOM   4347 C CG  . PRO   B 1 274 ? -53.205 -32.520 -23.460 1.00 14.27 ?  1311 PRO   B CG  1 
ATOM   4348 C CD  . PRO   B 1 274 ? -54.028 -31.753 -24.347 1.00 16.47 ?  1311 PRO   B CD  1 
ATOM   4349 N N   . LEU   B 1 275 ? -52.280 -29.051 -25.382 1.00 14.07 ?  1312 LEU   B N   1 
ATOM   4350 C CA  . LEU   B 1 275 ? -51.712 -28.040 -26.254 1.00 11.47 ?  1312 LEU   B CA  1 
ATOM   4351 C C   . LEU   B 1 275 ? -52.327 -26.670 -26.020 1.00 18.93 ?  1312 LEU   B C   1 
ATOM   4352 O O   . LEU   B 1 275 ? -51.634 -25.661 -26.160 1.00 16.09 ?  1312 LEU   B O   1 
ATOM   4353 C CB  . LEU   B 1 275 ? -51.930 -28.487 -27.709 1.00 10.35 ?  1312 LEU   B CB  1 
ATOM   4354 C CG  . LEU   B 1 275 ? -51.213 -27.661 -28.747 1.00 12.31 ?  1312 LEU   B CG  1 
ATOM   4355 C CD1 . LEU   B 1 275 ? -49.737 -27.648 -28.411 1.00 9.67  ?  1312 LEU   B CD1 1 
ATOM   4356 C CD2 . LEU   B 1 275 ? -51.443 -28.211 -30.138 1.00 14.86 ?  1312 LEU   B CD2 1 
ATOM   4357 N N   . TYR   B 1 276 ? -53.616 -26.608 -25.677 1.00 17.27 ?  1313 TYR   B N   1 
ATOM   4358 C CA  . TYR   B 1 276 ? -54.228 -25.303 -25.457 1.00 17.98 ?  1313 TYR   B CA  1 
ATOM   4359 C C   . TYR   B 1 276 ? -53.739 -24.670 -24.160 1.00 18.37 ?  1313 TYR   B C   1 
ATOM   4360 O O   . TYR   B 1 276 ? -53.511 -23.455 -24.104 1.00 16.12 ?  1313 TYR   B O   1 
ATOM   4361 C CB  . TYR   B 1 276 ? -55.751 -25.399 -25.454 1.00 19.25 ?  1313 TYR   B CB  1 
ATOM   4362 C CG  . TYR   B 1 276 ? -56.394 -24.037 -25.334 1.00 17.26 ?  1313 TYR   B CG  1 
ATOM   4363 C CD1 . TYR   B 1 276 ? -56.178 -23.066 -26.304 1.00 18.23 ?  1313 TYR   B CD1 1 
ATOM   4364 C CD2 . TYR   B 1 276 ? -57.190 -23.709 -24.245 1.00 13.55 ?  1313 TYR   B CD2 1 
ATOM   4365 C CE1 . TYR   B 1 276 ? -56.745 -21.810 -26.201 1.00 15.03 ?  1313 TYR   B CE1 1 
ATOM   4366 C CE2 . TYR   B 1 276 ? -57.766 -22.455 -24.136 1.00 18.65 ?  1313 TYR   B CE2 1 
ATOM   4367 C CZ  . TYR   B 1 276 ? -57.540 -21.511 -25.117 1.00 17.17 ?  1313 TYR   B CZ  1 
ATOM   4368 O OH  . TYR   B 1 276 ? -58.111 -20.263 -25.011 1.00 20.01 ?  1313 TYR   B OH  1 
ATOM   4369 N N   . GLU   B 1 277 ? -53.579 -25.468 -23.101 1.00 19.61 ?  1314 GLU   B N   1 
ATOM   4370 C CA  . GLU   B 1 277 ? -53.037 -24.923 -21.860 1.00 17.99 ?  1314 GLU   B CA  1 
ATOM   4371 C C   . GLU   B 1 277 ? -51.591 -24.480 -22.037 1.00 20.41 ?  1314 GLU   B C   1 
ATOM   4372 O O   . GLU   B 1 277 ? -51.115 -23.607 -21.301 1.00 17.13 ?  1314 GLU   B O   1 
ATOM   4373 C CB  . GLU   B 1 277 ? -53.152 -25.946 -20.732 1.00 17.80 ?  1314 GLU   B CB  1 
ATOM   4374 N N   . VAL   B 1 278 ? -50.880 -25.069 -23.002 1.00 17.22 ?  1315 VAL   B N   1 
ATOM   4375 C CA  . VAL   B 1 278 ? -49.572 -24.549 -23.385 1.00 16.99 ?  1315 VAL   B CA  1 
ATOM   4376 C C   . VAL   B 1 278 ? -49.709 -23.134 -23.935 1.00 19.31 ?  1315 VAL   B C   1 
ATOM   4377 O O   . VAL   B 1 278 ? -48.895 -22.252 -23.634 1.00 15.93 ?  1315 VAL   B O   1 
ATOM   4378 C CB  . VAL   B 1 278 ? -48.899 -25.495 -24.399 1.00 19.12 ?  1315 VAL   B CB  1 
ATOM   4379 C CG1 . VAL   B 1 278 ? -47.762 -24.792 -25.119 1.00 19.86 ?  1315 VAL   B CG1 1 
ATOM   4380 C CG2 . VAL   B 1 278 ? -48.395 -26.752 -23.701 1.00 15.30 ?  1315 VAL   B CG2 1 
ATOM   4381 N N   . MET   B 1 279 ? -50.755 -22.888 -24.729 1.00 14.98 ?  1316 MET   B N   1 
ATOM   4382 C CA  . MET   B 1 279 ? -50.950 -21.563 -25.311 1.00 15.88 ?  1316 MET   B CA  1 
ATOM   4383 C C   . MET   B 1 279 ? -51.269 -20.533 -24.238 1.00 12.13 ?  1316 MET   B C   1 
ATOM   4384 O O   . MET   B 1 279 ? -50.725 -19.423 -24.253 1.00 12.75 ?  1316 MET   B O   1 
ATOM   4385 C CB  . MET   B 1 279 ? -52.086 -21.597 -26.324 1.00 15.09 ?  1316 MET   B CB  1 
ATOM   4386 C CG  . MET   B 1 279 ? -51.940 -22.643 -27.385 1.00 13.35 ?  1316 MET   B CG  1 
ATOM   4387 S SD  . MET   B 1 279 ? -53.438 -22.668 -28.372 1.00 23.14 ?  1316 MET   B SD  1 
ATOM   4388 C CE  . MET   B 1 279 ? -52.865 -23.461 -29.850 1.00 22.14 ?  1316 MET   B CE  1 
ATOM   4389 N N   . LEU   B 1 280 ? -52.172 -20.874 -23.315 1.00 14.18 ?  1317 LEU   B N   1 
ATOM   4390 C CA  . LEU   B 1 280 ? -52.530 -19.935 -22.259 1.00 14.02 ?  1317 LEU   B CA  1 
ATOM   4391 C C   . LEU   B 1 280 ? -51.336 -19.617 -21.373 1.00 15.85 ?  1317 LEU   B C   1 
ATOM   4392 O O   . LEU   B 1 280 ? -51.270 -18.532 -20.786 1.00 18.20 ?  1317 LEU   B O   1 
ATOM   4393 C CB  . LEU   B 1 280 ? -53.685 -20.490 -21.425 1.00 12.27 ?  1317 LEU   B CB  1 
ATOM   4394 C CG  . LEU   B 1 280 ? -55.012 -20.633 -22.173 1.00 15.39 ?  1317 LEU   B CG  1 
ATOM   4395 C CD1 . LEU   B 1 280 ? -56.107 -21.135 -21.245 1.00 11.41 ?  1317 LEU   B CD1 1 
ATOM   4396 C CD2 . LEU   B 1 280 ? -55.413 -19.316 -22.821 1.00 13.57 ?  1317 LEU   B CD2 1 
ATOM   4397 N N   . LYS   B 1 281 ? -50.383 -20.546 -21.268 1.00 18.02 ?  1318 LYS   B N   1 
ATOM   4398 C CA  . LYS   B 1 281 ? -49.141 -20.246 -20.567 1.00 15.45 ?  1318 LYS   B CA  1 
ATOM   4399 C C   . LYS   B 1 281 ? -48.269 -19.287 -21.366 1.00 12.82 ?  1318 LYS   B C   1 
ATOM   4400 O O   . LYS   B 1 281 ? -47.560 -18.464 -20.778 1.00 11.44 ?  1318 LYS   B O   1 
ATOM   4401 C CB  . LYS   B 1 281 ? -48.379 -21.538 -20.269 1.00 15.14 ?  1318 LYS   B CB  1 
ATOM   4402 N N   . CYS   B 1 282 ? -48.315 -19.371 -22.698 1.00 12.04 ?  1319 CYS   B N   1 
ATOM   4403 C CA  . CYS   B 1 282 ? -47.540 -18.481 -23.555 1.00 12.30 ?  1319 CYS   B CA  1 
ATOM   4404 C C   . CYS   B 1 282 ? -48.046 -17.046 -23.534 1.00 20.20 ?  1319 CYS   B C   1 
ATOM   4405 O O   . CYS   B 1 282 ? -47.330 -16.151 -23.996 1.00 17.02 ?  1319 CYS   B O   1 
ATOM   4406 C CB  . CYS   B 1 282 ? -47.543 -18.997 -24.995 1.00 12.07 ?  1319 CYS   B CB  1 
ATOM   4407 S SG  . CYS   B 1 282 ? -46.737 -20.596 -25.228 1.00 12.94 ?  1319 CYS   B SG  1 
ATOM   4408 N N   . TRP   B 1 283 ? -49.249 -16.804 -23.018 1.00 15.54 ?  1320 TRP   B N   1 
ATOM   4409 C CA  . TRP   B 1 283 ? -49.825 -15.466 -22.972 1.00 14.11 ?  1320 TRP   B CA  1 
ATOM   4410 C C   . TRP   B 1 283 ? -50.082 -15.012 -21.541 1.00 14.87 ?  1320 TRP   B C   1 
ATOM   4411 O O   . TRP   B 1 283 ? -50.983 -14.208 -21.292 1.00 13.68 ?  1320 TRP   B O   1 
ATOM   4412 C CB  . TRP   B 1 283 ? -51.113 -15.400 -23.787 1.00 13.68 ?  1320 TRP   B CB  1 
ATOM   4413 C CG  . TRP   B 1 283 ? -50.951 -15.848 -25.194 1.00 12.88 ?  1320 TRP   B CG  1 
ATOM   4414 C CD1 . TRP   B 1 283 ? -49.970 -15.479 -26.065 1.00 11.77 ?  1320 TRP   B CD1 1 
ATOM   4415 C CD2 . TRP   B 1 283 ? -51.806 -16.746 -25.905 1.00 13.16 ?  1320 TRP   B CD2 1 
ATOM   4416 N NE1 . TRP   B 1 283 ? -50.158 -16.097 -27.277 1.00 12.23 ?  1320 TRP   B NE1 1 
ATOM   4417 C CE2 . TRP   B 1 283 ? -51.280 -16.880 -27.204 1.00 11.07 ?  1320 TRP   B CE2 1 
ATOM   4418 C CE3 . TRP   B 1 283 ? -52.964 -17.453 -25.570 1.00 12.46 ?  1320 TRP   B CE3 1 
ATOM   4419 C CZ2 . TRP   B 1 283 ? -51.876 -17.688 -28.167 1.00 10.77 ?  1320 TRP   B CZ2 1 
ATOM   4420 C CZ3 . TRP   B 1 283 ? -53.552 -18.255 -26.527 1.00 11.56 ?  1320 TRP   B CZ3 1 
ATOM   4421 C CH2 . TRP   B 1 283 ? -53.006 -18.368 -27.810 1.00 11.86 ?  1320 TRP   B CH2 1 
ATOM   4422 N N   . HIS   B 1 284 ? -49.308 -15.527 -20.594 1.00 12.72 ?  1321 HIS   B N   1 
ATOM   4423 C CA  . HIS   B 1 284 ? -49.390 -15.029 -19.232 1.00 14.50 ?  1321 HIS   B CA  1 
ATOM   4424 C C   . HIS   B 1 284 ? -49.005 -13.551 -19.210 1.00 16.50 ?  1321 HIS   B C   1 
ATOM   4425 O O   . HIS   B 1 284 ? -48.056 -13.148 -19.892 1.00 14.55 ?  1321 HIS   B O   1 
ATOM   4426 C CB  . HIS   B 1 284 ? -48.469 -15.833 -18.313 1.00 13.17 ?  1321 HIS   B CB  1 
ATOM   4427 C CG  . HIS   B 1 284 ? -48.810 -15.722 -16.860 1.00 12.00 ?  1321 HIS   B CG  1 
ATOM   4428 N ND1 . HIS   B 1 284 ? -48.486 -14.618 -16.102 1.00 15.64 ?  1321 HIS   B ND1 1 
ATOM   4429 C CD2 . HIS   B 1 284 ? -49.442 -16.579 -16.024 1.00 12.37 ?  1321 HIS   B CD2 1 
ATOM   4430 C CE1 . HIS   B 1 284 ? -48.907 -14.798 -14.863 1.00 16.05 ?  1321 HIS   B CE1 1 
ATOM   4431 N NE2 . HIS   B 1 284 ? -49.490 -15.980 -14.789 1.00 14.75 ?  1321 HIS   B NE2 1 
ATOM   4432 N N   . PRO   B 1 285 ? -49.732 -12.712 -18.466 1.00 16.84 ?  1322 PRO   B N   1 
ATOM   4433 C CA  . PRO   B 1 285 ? -49.368 -11.286 -18.429 1.00 16.21 ?  1322 PRO   B CA  1 
ATOM   4434 C C   . PRO   B 1 285 ? -47.980 -11.042 -17.864 1.00 15.74 ?  1322 PRO   B C   1 
ATOM   4435 O O   . PRO   B 1 285 ? -47.262 -10.160 -18.352 1.00 17.47 ?  1322 PRO   B O   1 
ATOM   4436 C CB  . PRO   B 1 285 ? -50.466 -10.668 -17.551 1.00 13.76 ?  1322 PRO   B CB  1 
ATOM   4437 C CG  . PRO   B 1 285 ? -51.011 -11.809 -16.755 1.00 13.07 ?  1322 PRO   B CG  1 
ATOM   4438 C CD  . PRO   B 1 285 ? -50.927 -13.000 -17.657 1.00 19.31 ?  1322 PRO   B CD  1 
ATOM   4439 N N   . LYS   B 1 286 ? -47.579 -11.803 -16.849 1.00 14.42 ?  1323 LYS   B N   1 
ATOM   4440 C CA  . LYS   B 1 286 ? -46.229 -11.715 -16.304 1.00 14.45 ?  1323 LYS   B CA  1 
ATOM   4441 C C   . LYS   B 1 286 ? -45.293 -12.511 -17.206 1.00 17.91 ?  1323 LYS   B C   1 
ATOM   4442 O O   . LYS   B 1 286 ? -45.358 -13.744 -17.245 1.00 13.66 ?  1323 LYS   B O   1 
ATOM   4443 C CB  . LYS   B 1 286 ? -46.197 -12.233 -14.870 1.00 15.12 ?  1323 LYS   B CB  1 
ATOM   4444 C CG  . LYS   B 1 286 ? -47.083 -11.453 -13.912 1.00 10.39 ?  1323 LYS   B CG  1 
ATOM   4445 N N   . ALA   B 1 287 ? -44.418 -11.806 -17.928 1.00 14.02 ?  1324 ALA   B N   1 
ATOM   4446 C CA  . ALA   B 1 287 ? -43.583 -12.434 -18.946 1.00 16.58 ?  1324 ALA   B CA  1 
ATOM   4447 C C   . ALA   B 1 287 ? -42.591 -13.440 -18.377 1.00 21.83 ?  1324 ALA   B C   1 
ATOM   4448 O O   . ALA   B 1 287 ? -41.994 -14.197 -19.151 1.00 18.78 ?  1324 ALA   B O   1 
ATOM   4449 C CB  . ALA   B 1 287 ? -42.831 -11.363 -19.738 1.00 19.04 ?  1324 ALA   B CB  1 
ATOM   4450 N N   . GLU   B 1 288 ? -42.394 -13.470 -17.059 1.00 20.78 ?  1325 GLU   B N   1 
ATOM   4451 C CA  . GLU   B 1 288 ? -41.518 -14.460 -16.448 1.00 16.23 ?  1325 GLU   B CA  1 
ATOM   4452 C C   . GLU   B 1 288 ? -42.201 -15.806 -16.240 1.00 21.31 ?  1325 GLU   B C   1 
ATOM   4453 O O   . GLU   B 1 288 ? -41.511 -16.799 -15.985 1.00 24.77 ?  1325 GLU   B O   1 
ATOM   4454 C CB  . GLU   B 1 288 ? -40.990 -13.941 -15.109 1.00 15.78 ?  1325 GLU   B CB  1 
ATOM   4455 N N   . MET   B 1 289 ? -43.529 -15.863 -16.340 1.00 21.61 ?  1326 MET   B N   1 
ATOM   4456 C CA  . MET   B 1 289 ? -44.258 -17.113 -16.179 1.00 17.76 ?  1326 MET   B CA  1 
ATOM   4457 C C   . MET   B 1 289 ? -44.441 -17.866 -17.488 1.00 17.66 ?  1326 MET   B C   1 
ATOM   4458 O O   . MET   B 1 289 ? -44.730 -19.068 -17.458 1.00 15.81 ?  1326 MET   B O   1 
ATOM   4459 C CB  . MET   B 1 289 ? -45.628 -16.849 -15.548 1.00 17.26 ?  1326 MET   B CB  1 
ATOM   4460 C CG  . MET   B 1 289 ? -45.552 -16.155 -14.201 1.00 23.47 ?  1326 MET   B CG  1 
ATOM   4461 S SD  . MET   B 1 289 ? -44.621 -17.112 -12.990 1.00 32.21 ?  1326 MET   B SD  1 
ATOM   4462 C CE  . MET   B 1 289 ? -45.758 -17.110 -11.608 1.00 15.16 ?  1326 MET   B CE  1 
ATOM   4463 N N   . ARG   B 1 290 ? -44.290 -17.194 -18.623 1.00 17.72 ?  1327 ARG   B N   1 
ATOM   4464 C CA  . ARG   B 1 290 ? -44.292 -17.894 -19.896 1.00 17.80 ?  1327 ARG   B CA  1 
ATOM   4465 C C   . ARG   B 1 290 ? -43.096 -18.841 -19.957 1.00 22.51 ?  1327 ARG   B C   1 
ATOM   4466 O O   . ARG   B 1 290 ? -42.005 -18.493 -19.489 1.00 19.84 ?  1327 ARG   B O   1 
ATOM   4467 C CB  . ARG   B 1 290 ? -44.241 -16.903 -21.057 1.00 16.16 ?  1327 ARG   B CB  1 
ATOM   4468 C CG  . ARG   B 1 290 ? -45.563 -16.222 -21.332 1.00 18.01 ?  1327 ARG   B CG  1 
ATOM   4469 C CD  . ARG   B 1 290 ? -45.508 -14.743 -21.033 1.00 18.57 ?  1327 ARG   B CD  1 
ATOM   4470 N NE  . ARG   B 1 290 ? -45.146 -13.976 -22.217 1.00 21.86 ?  1327 ARG   B NE  1 
ATOM   4471 C CZ  . ARG   B 1 290 ? -45.211 -12.655 -22.299 1.00 18.98 ?  1327 ARG   B CZ  1 
ATOM   4472 N NH1 . ARG   B 1 290 ? -45.631 -11.919 -21.283 1.00 14.39 ?  1327 ARG   B NH1 1 
ATOM   4473 N NH2 . ARG   B 1 290 ? -44.844 -12.058 -23.428 1.00 20.95 ?  1327 ARG   B NH2 1 
ATOM   4474 N N   . PRO   B 1 291 ? -43.259 -20.033 -20.518 1.00 23.81 ?  1328 PRO   B N   1 
ATOM   4475 C CA  . PRO   B 1 291 ? -42.179 -21.021 -20.491 1.00 23.15 ?  1328 PRO   B CA  1 
ATOM   4476 C C   . PRO   B 1 291 ? -41.078 -20.676 -21.484 1.00 24.43 ?  1328 PRO   B C   1 
ATOM   4477 O O   . PRO   B 1 291 ? -41.236 -19.842 -22.377 1.00 21.83 ?  1328 PRO   B O   1 
ATOM   4478 C CB  . PRO   B 1 291 ? -42.889 -22.318 -20.885 1.00 21.48 ?  1328 PRO   B CB  1 
ATOM   4479 C CG  . PRO   B 1 291 ? -43.984 -21.861 -21.786 1.00 21.58 ?  1328 PRO   B CG  1 
ATOM   4480 C CD  . PRO   B 1 291 ? -44.444 -20.531 -21.239 1.00 20.22 ?  1328 PRO   B CD  1 
ATOM   4481 N N   . SER   B 1 292 ? -39.941 -21.338 -21.302 1.00 25.90 ?  1329 SER   B N   1 
ATOM   4482 C CA  . SER   B 1 292 ? -38.869 -21.244 -22.274 1.00 18.76 ?  1329 SER   B CA  1 
ATOM   4483 C C   . SER   B 1 292 ? -39.267 -21.966 -23.555 1.00 15.54 ?  1329 SER   B C   1 
ATOM   4484 O O   . SER   B 1 292 ? -40.147 -22.831 -23.561 1.00 15.68 ?  1329 SER   B O   1 
ATOM   4485 C CB  . SER   B 1 292 ? -37.583 -21.856 -21.720 1.00 26.54 ?  1329 SER   B CB  1 
ATOM   4486 O OG  . SER   B 1 292 ? -37.487 -21.669 -20.320 1.00 30.10 ?  1329 SER   B OG  1 
ATOM   4487 N N   . PHE   B 1 293 ? -38.611 -21.599 -24.657 1.00 16.46 ?  1330 PHE   B N   1 
ATOM   4488 C CA  . PHE   B 1 293 ? -38.707 -22.433 -25.848 1.00 15.36 ?  1330 PHE   B CA  1 
ATOM   4489 C C   . PHE   B 1 293 ? -38.145 -23.821 -25.575 1.00 19.09 ?  1330 PHE   B C   1 
ATOM   4490 O O   . PHE   B 1 293 ? -38.615 -24.809 -26.151 1.00 15.96 ?  1330 PHE   B O   1 
ATOM   4491 C CB  . PHE   B 1 293 ? -37.978 -21.779 -27.021 1.00 16.76 ?  1330 PHE   B CB  1 
ATOM   4492 C CG  . PHE   B 1 293 ? -38.594 -20.489 -27.479 1.00 18.12 ?  1330 PHE   B CG  1 
ATOM   4493 C CD1 . PHE   B 1 293 ? -39.725 -20.492 -28.278 1.00 14.53 ?  1330 PHE   B CD1 1 
ATOM   4494 C CD2 . PHE   B 1 293 ? -38.035 -19.272 -27.121 1.00 14.95 ?  1330 PHE   B CD2 1 
ATOM   4495 C CE1 . PHE   B 1 293 ? -40.291 -19.306 -28.706 1.00 16.59 ?  1330 PHE   B CE1 1 
ATOM   4496 C CE2 . PHE   B 1 293 ? -38.596 -18.084 -27.547 1.00 16.17 ?  1330 PHE   B CE2 1 
ATOM   4497 C CZ  . PHE   B 1 293 ? -39.727 -18.102 -28.340 1.00 19.16 ?  1330 PHE   B CZ  1 
ATOM   4498 N N   . SER   B 1 294 ? -37.145 -23.910 -24.694 1.00 19.88 ?  1331 SER   B N   1 
ATOM   4499 C CA  . SER   B 1 294 ? -36.669 -25.207 -24.225 1.00 18.06 ?  1331 SER   B CA  1 
ATOM   4500 C C   . SER   B 1 294 ? -37.787 -25.976 -23.534 1.00 18.26 ?  1331 SER   B C   1 
ATOM   4501 O O   . SER   B 1 294 ? -37.997 -27.165 -23.800 1.00 17.56 ?  1331 SER   B O   1 
ATOM   4502 C CB  . SER   B 1 294 ? -35.479 -25.013 -23.284 1.00 19.24 ?  1331 SER   B CB  1 
ATOM   4503 O OG  . SER   B 1 294 ? -34.871 -26.250 -22.960 1.00 11.54 ?  1331 SER   B OG  1 
ATOM   4504 N N   . GLU   B 1 295 ? -38.518 -25.309 -22.636 1.00 18.47 ?  1332 GLU   B N   1 
ATOM   4505 C CA  . GLU   B 1 295 ? -39.698 -25.928 -22.042 1.00 19.46 ?  1332 GLU   B CA  1 
ATOM   4506 C C   . GLU   B 1 295 ? -40.760 -26.212 -23.093 1.00 17.57 ?  1332 GLU   B C   1 
ATOM   4507 O O   . GLU   B 1 295 ? -41.477 -27.215 -22.999 1.00 16.70 ?  1332 GLU   B O   1 
ATOM   4508 C CB  . GLU   B 1 295 ? -40.276 -25.032 -20.948 1.00 21.24 ?  1332 GLU   B CB  1 
ATOM   4509 C CG  . GLU   B 1 295 ? -39.329 -24.754 -19.801 1.00 23.84 ?  1332 GLU   B CG  1 
ATOM   4510 C CD  . GLU   B 1 295 ? -39.879 -23.728 -18.830 1.00 28.36 ?  1332 GLU   B CD  1 
ATOM   4511 O OE1 . GLU   B 1 295 ? -40.957 -23.975 -18.248 1.00 20.67 ?  1332 GLU   B OE1 1 
ATOM   4512 O OE2 . GLU   B 1 295 ? -39.234 -22.673 -18.650 1.00 27.01 -1 1332 GLU   B OE2 1 
ATOM   4513 N N   . LEU   B 1 296 ? -40.875 -25.345 -24.099 1.00 15.60 ?  1333 LEU   B N   1 
ATOM   4514 C CA  . LEU   B 1 296 ? -41.887 -25.541 -25.129 1.00 16.76 ?  1333 LEU   B CA  1 
ATOM   4515 C C   . LEU   B 1 296 ? -41.522 -26.702 -26.045 1.00 13.12 ?  1333 LEU   B C   1 
ATOM   4516 O O   . LEU   B 1 296 ? -42.402 -27.439 -26.500 1.00 11.41 ?  1333 LEU   B O   1 
ATOM   4517 C CB  . LEU   B 1 296 ? -42.077 -24.248 -25.917 1.00 14.29 ?  1333 LEU   B CB  1 
ATOM   4518 C CG  . LEU   B 1 296 ? -42.949 -23.255 -25.144 1.00 15.81 ?  1333 LEU   B CG  1 
ATOM   4519 C CD1 . LEU   B 1 296 ? -43.125 -21.950 -25.896 1.00 15.66 ?  1333 LEU   B CD1 1 
ATOM   4520 C CD2 . LEU   B 1 296 ? -44.296 -23.881 -24.826 1.00 17.72 ?  1333 LEU   B CD2 1 
ATOM   4521 N N   . VAL   B 1 297 ? -40.229 -26.886 -26.322 1.00 15.80 ?  1334 VAL   B N   1 
ATOM   4522 C CA  . VAL   B 1 297 ? -39.796 -28.097 -27.011 1.00 14.19 ?  1334 VAL   B CA  1 
ATOM   4523 C C   . VAL   B 1 297 ? -40.145 -29.325 -26.180 1.00 15.05 ?  1334 VAL   B C   1 
ATOM   4524 O O   . VAL   B 1 297 ? -40.484 -30.382 -26.726 1.00 12.25 ?  1334 VAL   B O   1 
ATOM   4525 C CB  . VAL   B 1 297 ? -38.286 -28.024 -27.324 1.00 13.70 ?  1334 VAL   B CB  1 
ATOM   4526 C CG1 . VAL   B 1 297 ? -37.750 -29.380 -27.762 1.00 15.00 ?  1334 VAL   B CG1 1 
ATOM   4527 C CG2 . VAL   B 1 297 ? -38.015 -26.981 -28.397 1.00 12.36 ?  1334 VAL   B CG2 1 
ATOM   4528 N N   . SER   B 1 298 ? -40.112 -29.194 -24.852 1.00 12.79 ?  1335 SER   B N   1 
ATOM   4529 C CA  . SER   B 1 298 ? -40.341 -30.341 -23.980 1.00 10.53 ?  1335 SER   B CA  1 
ATOM   4530 C C   . SER   B 1 298 ? -41.813 -30.736 -23.947 1.00 13.71 ?  1335 SER   B C   1 
ATOM   4531 O O   . SER   B 1 298 ? -42.159 -31.899 -24.187 1.00 12.72 ?  1335 SER   B O   1 
ATOM   4532 C CB  . SER   B 1 298 ? -39.839 -30.027 -22.570 1.00 10.87 ?  1335 SER   B CB  1 
ATOM   4533 O OG  . SER   B 1 298 ? -38.428 -30.132 -22.498 1.00 22.34 ?  1335 SER   B OG  1 
ATOM   4534 N N   . ARG   B 1 299 ? -42.696 -29.782 -23.646 1.00 14.45 ?  1336 ARG   B N   1 
ATOM   4535 C CA  . ARG   B 1 299 ? -44.106 -30.115 -23.464 1.00 12.02 ?  1336 ARG   B CA  1 
ATOM   4536 C C   . ARG   B 1 299 ? -44.783 -30.443 -24.790 1.00 10.22 ?  1336 ARG   B C   1 
ATOM   4537 O O   . ARG   B 1 299 ? -45.628 -31.344 -24.852 1.00 11.87 ?  1336 ARG   B O   1 
ATOM   4538 C CB  . ARG   B 1 299 ? -44.830 -28.970 -22.756 1.00 13.28 ?  1336 ARG   B CB  1 
ATOM   4539 C CG  . ARG   B 1 299 ? -44.310 -28.679 -21.357 1.00 14.61 ?  1336 ARG   B CG  1 
ATOM   4540 C CD  . ARG   B 1 299 ? -45.405 -28.114 -20.464 1.00 24.14 ?  1336 ARG   B CD  1 
ATOM   4541 N NE  . ARG   B 1 299 ? -44.915 -27.789 -19.129 1.00 37.39 ?  1336 ARG   B NE  1 
ATOM   4542 C CZ  . ARG   B 1 299 ? -44.903 -28.633 -18.106 1.00 40.67 ?  1336 ARG   B CZ  1 
ATOM   4543 N NH1 . ARG   B 1 299 ? -45.351 -29.872 -18.226 1.00 24.53 ?  1336 ARG   B NH1 1 
ATOM   4544 N NH2 . ARG   B 1 299 ? -44.432 -28.222 -16.931 1.00 40.41 ?  1336 ARG   B NH2 1 
ATOM   4545 N N   . ILE   B 1 300 ? -44.428 -29.730 -25.861 1.00 8.96  ?  1337 ILE   B N   1 
ATOM   4546 C CA  . ILE   B 1 300 ? -45.067 -29.972 -27.152 1.00 8.78  ?  1337 ILE   B CA  1 
ATOM   4547 C C   . ILE   B 1 300 ? -44.665 -31.333 -27.706 1.00 11.13 ?  1337 ILE   B C   1 
ATOM   4548 O O   . ILE   B 1 300 ? -45.502 -32.070 -28.243 1.00 12.84 ?  1337 ILE   B O   1 
ATOM   4549 C CB  . ILE   B 1 300 ? -44.733 -28.841 -28.139 1.00 9.36  ?  1337 ILE   B CB  1 
ATOM   4550 C CG1 . ILE   B 1 300 ? -45.297 -27.512 -27.640 1.00 9.70  ?  1337 ILE   B CG1 1 
ATOM   4551 C CG2 . ILE   B 1 300 ? -45.270 -29.163 -29.525 1.00 6.96  ?  1337 ILE   B CG2 1 
ATOM   4552 C CD1 . ILE   B 1 300 ? -44.862 -26.332 -28.468 1.00 10.41 ?  1337 ILE   B CD1 1 
ATOM   4553 N N   . SER   B 1 301 ? -43.382 -31.688 -27.594 1.00 11.49 ?  1338 SER   B N   1 
ATOM   4554 C CA  . SER   B 1 301 ? -42.930 -32.982 -28.097 1.00 11.36 ?  1338 SER   B CA  1 
ATOM   4555 C C   . SER   B 1 301 ? -43.642 -34.131 -27.398 1.00 12.95 ?  1338 SER   B C   1 
ATOM   4556 O O   . SER   B 1 301 ? -43.925 -35.158 -28.026 1.00 12.93 ?  1338 SER   B O   1 
ATOM   4557 C CB  . SER   B 1 301 ? -41.416 -33.118 -27.935 1.00 9.88  ?  1338 SER   B CB  1 
ATOM   4558 O OG  . SER   B 1 301 ? -41.051 -33.204 -26.568 1.00 10.54 ?  1338 SER   B OG  1 
ATOM   4559 N N   . ALA   B 1 302 ? -43.943 -33.976 -26.107 1.00 9.76  ?  1339 ALA   B N   1 
ATOM   4560 C CA  . ALA   B 1 302 ? -44.715 -34.993 -25.401 1.00 13.74 ?  1339 ALA   B CA  1 
ATOM   4561 C C   . ALA   B 1 302 ? -46.087 -35.171 -26.037 1.00 14.80 ?  1339 ALA   B C   1 
ATOM   4562 O O   . ALA   B 1 302 ? -46.483 -36.289 -26.383 1.00 17.30 ?  1339 ALA   B O   1 
ATOM   4563 C CB  . ALA   B 1 302 ? -44.844 -34.621 -23.924 1.00 12.05 ?  1339 ALA   B CB  1 
ATOM   4564 N N   . ILE   B 1 303 ? -46.823 -34.069 -26.212 1.00 13.98 ?  1340 ILE   B N   1 
ATOM   4565 C CA  . ILE   B 1 303 ? -48.125 -34.127 -26.872 1.00 12.18 ?  1340 ILE   B CA  1 
ATOM   4566 C C   . ILE   B 1 303 ? -47.991 -34.731 -28.264 1.00 14.72 ?  1340 ILE   B C   1 
ATOM   4567 O O   . ILE   B 1 303 ? -48.862 -35.483 -28.720 1.00 20.47 ?  1340 ILE   B O   1 
ATOM   4568 C CB  . ILE   B 1 303 ? -48.753 -32.721 -26.922 1.00 11.95 ?  1340 ILE   B CB  1 
ATOM   4569 C CG1 . ILE   B 1 303 ? -49.067 -32.227 -25.509 1.00 16.21 ?  1340 ILE   B CG1 1 
ATOM   4570 C CG2 . ILE   B 1 303 ? -50.008 -32.714 -27.785 1.00 10.85 ?  1340 ILE   B CG2 1 
ATOM   4571 C CD1 . ILE   B 1 303 ? -49.035 -30.720 -25.375 1.00 10.75 ?  1340 ILE   B CD1 1 
ATOM   4572 N N   . PHE   B 1 304 ? -46.893 -34.421 -28.954 1.00 11.49 ?  1341 PHE   B N   1 
ATOM   4573 C CA  . PHE   B 1 304 ? -46.670 -34.966 -30.289 1.00 12.64 ?  1341 PHE   B CA  1 
ATOM   4574 C C   . PHE   B 1 304 ? -46.493 -36.479 -30.245 1.00 14.65 ?  1341 PHE   B C   1 
ATOM   4575 O O   . PHE   B 1 304 ? -47.183 -37.219 -30.957 1.00 19.26 ?  1341 PHE   B O   1 
ATOM   4576 C CB  . PHE   B 1 304 ? -45.448 -34.295 -30.919 1.00 11.18 ?  1341 PHE   B CB  1 
ATOM   4577 C CG  . PHE   B 1 304 ? -45.169 -34.733 -32.328 1.00 9.77  ?  1341 PHE   B CG  1 
ATOM   4578 C CD1 . PHE   B 1 304 ? -46.075 -34.476 -33.342 1.00 9.62  ?  1341 PHE   B CD1 1 
ATOM   4579 C CD2 . PHE   B 1 304 ? -43.990 -35.391 -32.639 1.00 8.56  ?  1341 PHE   B CD2 1 
ATOM   4580 C CE1 . PHE   B 1 304 ? -45.814 -34.873 -34.640 1.00 8.80  ?  1341 PHE   B CE1 1 
ATOM   4581 C CE2 . PHE   B 1 304 ? -43.724 -35.791 -33.934 1.00 7.22  ?  1341 PHE   B CE2 1 
ATOM   4582 C CZ  . PHE   B 1 304 ? -44.637 -35.531 -34.936 1.00 7.93  ?  1341 PHE   B CZ  1 
ATOM   4583 N N   . SER   B 1 305 ? -45.579 -36.960 -29.399 1.00 19.97 ?  1342 SER   B N   1 
ATOM   4584 C CA  . SER   B 1 305 ? -45.235 -38.377 -29.372 1.00 18.98 ?  1342 SER   B CA  1 
ATOM   4585 C C   . SER   B 1 305 ? -46.319 -39.252 -28.756 1.00 18.73 ?  1342 SER   B C   1 
ATOM   4586 O O   . SER   B 1 305 ? -46.181 -40.479 -28.781 1.00 22.36 ?  1342 SER   B O   1 
ATOM   4587 C CB  . SER   B 1 305 ? -43.920 -38.580 -28.617 1.00 16.98 ?  1342 SER   B CB  1 
ATOM   4588 O OG  . SER   B 1 305 ? -42.893 -37.764 -29.155 1.00 17.56 ?  1342 SER   B OG  1 
ATOM   4589 N N   . THR   B 1 306 ? -47.378 -38.668 -28.208 1.00 17.20 ?  1343 THR   B N   1 
ATOM   4590 C CA  . THR   B 1 306 ? -48.478 -39.428 -27.640 1.00 19.70 ?  1343 THR   B CA  1 
ATOM   4591 C C   . THR   B 1 306 ? -49.676 -39.393 -28.593 1.00 22.61 ?  1343 THR   B C   1 
ATOM   4592 O O   . THR   B 1 306 ? -49.525 -39.147 -29.795 1.00 24.48 ?  1343 THR   B O   1 
ATOM   4593 C CB  . THR   B 1 306 ? -48.825 -38.878 -26.252 1.00 16.99 ?  1343 THR   B CB  1 
ATOM   4594 O OG1 . THR   B 1 306 ? -49.225 -37.506 -26.365 1.00 17.07 ?  1343 THR   B OG1 1 
ATOM   4595 C CG2 . THR   B 1 306 ? -47.633 -38.992 -25.312 1.00 21.95 ?  1343 THR   B CG2 1 
ATOM   4596 N N   . PHE   B 1 307 ? -50.869 -39.641 -28.061 1.00 17.25 ?  1344 PHE   B N   1 
ATOM   4597 C CA  . PHE   B 1 307 ? -52.101 -39.587 -28.839 1.00 25.42 ?  1344 PHE   B CA  1 
ATOM   4598 C C   . PHE   B 1 307 ? -53.315 -39.580 -27.914 1.00 26.68 ?  1344 PHE   B C   1 
ATOM   4599 O O   . PHE   B 1 307 ? -54.426 -39.912 -28.326 1.00 22.84 ?  1344 PHE   B O   1 
ATOM   4600 C CB  . PHE   B 1 307 ? -52.185 -40.768 -29.810 1.00 29.40 ?  1344 PHE   B CB  1 
HETATM 4601 C CAA . A1L3A C 2 .   ? -13.638 -16.450 5.299   1.00 8.86  ?  1401 A1L3A A CAA 1 
HETATM 4602 C CAB . A1L3A C 2 .   ? -14.747 -16.329 4.578   1.00 9.44  ?  1401 A1L3A A CAB 1 
HETATM 4603 C CAC . A1L3A C 2 .   ? -15.948 -16.377 5.271   1.00 7.15  ?  1401 A1L3A A CAC 1 
HETATM 4604 C CAD . A1L3A C 2 .   ? -15.882 -16.545 6.648   1.00 7.52  ?  1401 A1L3A A CAD 1 
HETATM 4605 C CAI . A1L3A C 2 .   ? -12.476 -16.691 7.015   1.00 7.12  ?  1401 A1L3A A CAI 1 
HETATM 4606 C CAJ . A1L3A C 2 .   ? -12.013 -16.885 8.451   1.00 7.53  ?  1401 A1L3A A CAJ 1 
HETATM 4607 C CAM . A1L3A C 2 .   ? -13.876 -13.848 11.666  1.00 17.50 ?  1401 A1L3A A CAM 1 
HETATM 4608 C CAN . A1L3A C 2 .   ? -13.046 -14.307 10.745  1.00 15.24 ?  1401 A1L3A A CAN 1 
HETATM 4609 C CAO . A1L3A C 2 .   ? -13.021 -15.449 10.069  1.00 12.62 ?  1401 A1L3A A CAO 1 
HETATM 4610 C CAP . A1L3A C 2 .   ? -12.019 -15.678 9.142   1.00 11.37 ?  1401 A1L3A A CAP 1 
HETATM 4611 C CAQ . A1L3A C 2 .   ? -11.055 -14.695 8.947   1.00 9.88  ?  1401 A1L3A A CAQ 1 
HETATM 4612 C CAR . A1L3A C 2 .   ? -11.142 -13.522 9.687   1.00 11.60 ?  1401 A1L3A A CAR 1 
HETATM 4613 C CAS . A1L3A C 2 .   ? -12.133 -13.360 10.562  1.00 11.24 ?  1401 A1L3A A CAS 1 
HETATM 4614 C CAT . A1L3A C 2 .   ? -14.130 -11.826 13.027  1.00 14.11 ?  1401 A1L3A A CAT 1 
HETATM 4615 C CAZ . A1L3A C 2 .   ? -17.064 -16.775 8.678   1.00 9.63  ?  1401 A1L3A A CAZ 1 
HETATM 4616 C CBA . A1L3A C 2 .   ? -16.997 -16.605 7.368   1.00 9.68  ?  1401 A1L3A A CBA 1 
HETATM 4617 C CBB . A1L3A C 2 .   ? -18.225 -16.515 6.884   1.00 11.05 ?  1401 A1L3A A CBB 1 
HETATM 4618 C CBC . A1L3A C 2 .   ? -20.512 -16.582 7.857   1.00 9.32  ?  1401 A1L3A A CBC 1 
HETATM 4619 C CBD . A1L3A C 2 .   ? -21.238 -17.781 8.442   1.00 12.26 ?  1401 A1L3A A CBD 1 
HETATM 4620 C CBE . A1L3A C 2 .   ? -21.141 -17.612 6.934   1.00 8.84  ?  1401 A1L3A A CBE 1 
HETATM 4621 F FAU . A1L3A C 2 .   ? -10.046 -14.862 8.050   1.00 11.67 ?  1401 A1L3A A FAU 1 
HETATM 4622 F FAV . A1L3A C 2 .   ? -12.822 -17.714 9.062   1.00 9.44  ?  1401 A1L3A A FAV 1 
HETATM 4623 F FAW . A1L3A C 2 .   ? -10.822 -17.384 8.443   1.00 7.79  ?  1401 A1L3A A FAW 1 
HETATM 4624 N NAE . A1L3A C 2 .   ? -14.686 -16.656 7.244   1.00 9.50  ?  1401 A1L3A A NAE 1 
HETATM 4625 N NAF . A1L3A C 2 .   ? -13.730 -16.608 6.612   1.00 10.01 ?  1401 A1L3A A NAF 1 
HETATM 4626 N NAG . A1L3A C 2 .   ? -11.668 -16.591 5.969   1.00 8.48  ?  1401 A1L3A A NAG 1 
HETATM 4627 N NAH . A1L3A C 2 .   ? -12.341 -16.457 4.984   1.00 7.86  ?  1401 A1L3A A NAH 1 
HETATM 4628 N NAK . A1L3A C 2 .   ? -12.443 -12.359 11.385  1.00 14.72 ?  1401 A1L3A A NAK 1 
HETATM 4629 N NAL . A1L3A C 2 .   ? -13.443 -12.642 12.014  1.00 15.73 ?  1401 A1L3A A NAL 1 
HETATM 4630 N NAX . A1L3A C 2 .   ? -19.035 -16.631 7.935   1.00 12.22 ?  1401 A1L3A A NAX 1 
HETATM 4631 N NAY . A1L3A C 2 .   ? -18.364 -16.780 8.975   1.00 14.02 ?  1401 A1L3A A NAY 1 
HETATM 4632 C CAA . A1L3A D 2 .   ? -39.359 -14.970 -45.245 1.00 6.75  ?  1401 A1L3A B CAA 1 
HETATM 4633 C CAB . A1L3A D 2 .   ? -40.416 -15.046 -44.444 1.00 5.09  ?  1401 A1L3A B CAB 1 
HETATM 4634 C CAC . A1L3A D 2 .   ? -41.664 -15.028 -45.051 1.00 6.35  ?  1401 A1L3A B CAC 1 
HETATM 4635 C CAD . A1L3A D 2 .   ? -41.688 -14.932 -46.437 1.00 8.01  ?  1401 A1L3A B CAD 1 
HETATM 4636 C CAI . A1L3A D 2 .   ? -38.333 -14.825 -47.070 1.00 8.42  ?  1401 A1L3A B CAI 1 
HETATM 4637 C CAJ . A1L3A D 2 .   ? -38.020 -14.718 -48.561 1.00 9.73  ?  1401 A1L3A B CAJ 1 
HETATM 4638 C CAM . A1L3A D 2 .   ? -39.907 -17.934 -51.616 1.00 16.47 ?  1401 A1L3A B CAM 1 
HETATM 4639 C CAN . A1L3A D 2 .   ? -39.108 -17.431 -50.688 1.00 17.43 ?  1401 A1L3A B CAN 1 
HETATM 4640 C CAO . A1L3A D 2 .   ? -39.044 -16.230 -50.119 1.00 14.98 ?  1401 A1L3A B CAO 1 
HETATM 4641 C CAP . A1L3A D 2 .   ? -38.083 -15.975 -49.152 1.00 12.19 ?  1401 A1L3A B CAP 1 
HETATM 4642 C CAQ . A1L3A D 2 .   ? -37.206 -16.994 -48.803 1.00 10.36 ?  1401 A1L3A B CAQ 1 
HETATM 4643 C CAR . A1L3A D 2 .   ? -37.329 -18.225 -49.433 1.00 12.58 ?  1401 A1L3A B CAR 1 
HETATM 4644 C CAS . A1L3A D 2 .   ? -38.272 -18.409 -50.356 1.00 14.21 ?  1401 A1L3A B CAS 1 
HETATM 4645 C CAT . A1L3A D 2 .   ? -40.182 -20.101 -52.786 1.00 16.62 ?  1401 A1L3A B CAT 1 
HETATM 4646 C CAZ . A1L3A D 2 .   ? -42.956 -14.785 -48.413 1.00 8.28  ?  1401 A1L3A B CAZ 1 
HETATM 4647 C CBA . A1L3A D 2 .   ? -42.839 -14.906 -47.101 1.00 6.27  ?  1401 A1L3A B CBA 1 
HETATM 4648 C CBB . A1L3A D 2 .   ? -44.047 -14.994 -46.570 1.00 9.35  ?  1401 A1L3A B CBB 1 
HETATM 4649 C CBC . A1L3A D 2 .   ? -46.373 -14.981 -47.498 1.00 9.54  ?  1401 A1L3A B CBC 1 
HETATM 4650 C CBD . A1L3A D 2 .   ? -47.121 -13.880 -48.231 1.00 8.14  ?  1401 A1L3A B CBD 1 
HETATM 4651 C CBE . A1L3A D 2 .   ? -47.026 -13.856 -46.714 1.00 9.16  ?  1401 A1L3A B CBE 1 
HETATM 4652 F FAU . A1L3A D 2 .   ? -36.251 -16.805 -47.868 1.00 10.59 ?  1401 A1L3A B FAU 1 
HETATM 4653 F FAV . A1L3A D 2 .   ? -38.907 -13.938 -49.141 1.00 7.97  ?  1401 A1L3A B FAV 1 
HETATM 4654 F FAW . A1L3A D 2 .   ? -36.835 -14.214 -48.726 1.00 11.99 ?  1401 A1L3A B FAW 1 
HETATM 4655 N NAE . A1L3A D 2 .   ? -40.532 -14.864 -47.113 1.00 8.38  ?  1401 A1L3A B NAE 1 
HETATM 4656 N NAF . A1L3A D 2 .   ? -39.547 -14.882 -46.555 1.00 7.66  ?  1401 A1L3A B NAF 1 
HETATM 4657 N NAG . A1L3A D 2 .   ? -37.436 -14.876 -46.092 1.00 10.64 ?  1401 A1L3A B NAG 1 
HETATM 4658 N NAH . A1L3A D 2 .   ? -38.041 -14.960 -45.022 1.00 8.96  ?  1401 A1L3A B NAH 1 
HETATM 4659 N NAK . A1L3A D 2 .   ? -38.598 -19.467 -51.098 1.00 18.91 ?  1401 A1L3A B NAK 1 
HETATM 4660 N NAL . A1L3A D 2 .   ? -39.531 -19.194 -51.816 1.00 22.10 ?  1401 A1L3A B NAL 1 
HETATM 4661 N NAX . A1L3A D 2 .   ? -44.895 -14.921 -47.597 1.00 15.32 ?  1401 A1L3A B NAX 1 
HETATM 4662 N NAY . A1L3A D 2 .   ? -44.265 -14.802 -48.661 1.00 15.44 ?  1401 A1L3A B NAY 1 
HETATM 4663 O O   . HOH   E 3 .   ? -11.625 0.569   -3.873  1.00 18.95 ?  1501 HOH   A O   1 
HETATM 4664 O O   . HOH   E 3 .   ? -9.633  -9.170  -15.659 1.00 18.95 ?  1502 HOH   A O   1 
HETATM 4665 O O   . HOH   E 3 .   ? -23.363 -32.556 -0.650  1.00 18.95 ?  1503 HOH   A O   1 
HETATM 4666 O O   . HOH   E 3 .   ? 15.768  -26.859 26.517  1.00 18.95 ?  1504 HOH   A O   1 
HETATM 4667 O O   . HOH   E 3 .   ? -27.216 -14.560 -0.122  1.00 18.95 ?  1505 HOH   A O   1 
HETATM 4668 O O   . HOH   E 3 .   ? -15.471 -23.860 0.598   1.00 18.46 ?  1506 HOH   A O   1 
HETATM 4669 O O   . HOH   E 3 .   ? 18.770  -33.937 23.423  1.00 18.95 ?  1507 HOH   A O   1 
HETATM 4670 O O   . HOH   E 3 .   ? -16.194 -18.263 -7.048  1.00 18.95 ?  1508 HOH   A O   1 
HETATM 4671 O O   . HOH   E 3 .   ? -21.108 -9.890  8.633   1.00 18.46 ?  1509 HOH   A O   1 
HETATM 4672 O O   . HOH   E 3 .   ? -7.168  -9.164  -13.339 1.00 18.95 ?  1510 HOH   A O   1 
HETATM 4673 O O   . HOH   E 3 .   ? -31.560 -3.133  7.594   1.00 18.95 ?  1511 HOH   A O   1 
HETATM 4674 O O   . HOH   E 3 .   ? -15.119 -20.646 -10.256 1.00 18.95 ?  1512 HOH   A O   1 
HETATM 4675 O O   . HOH   E 3 .   ? 7.426   -17.925 20.433  1.00 18.95 ?  1513 HOH   A O   1 
HETATM 4676 O O   . HOH   E 3 .   ? 6.757   -30.352 -5.389  1.00 18.95 ?  1514 HOH   A O   1 
HETATM 4677 O O   . HOH   E 3 .   ? -12.238 -12.399 -21.508 1.00 18.95 ?  1515 HOH   A O   1 
HETATM 4678 O O   . HOH   E 3 .   ? -33.313 -15.560 -18.558 1.00 18.95 ?  1516 HOH   A O   1 
HETATM 4679 O O   . HOH   E 3 .   ? 8.356   -32.013 5.749   1.00 18.95 ?  1517 HOH   A O   1 
HETATM 4680 O O   . HOH   E 3 .   ? -25.521 -19.528 -10.269 1.00 18.95 ?  1518 HOH   A O   1 
HETATM 4681 O O   . HOH   E 3 .   ? -8.539  -35.685 8.188   1.00 18.95 ?  1519 HOH   A O   1 
HETATM 4682 O O   . HOH   E 3 .   ? -13.447 -11.798 19.619  1.00 18.95 ?  1520 HOH   A O   1 
HETATM 4683 O O   . HOH   E 3 .   ? -9.945  -16.181 -11.087 1.00 18.95 ?  1521 HOH   A O   1 
HETATM 4684 O O   . HOH   E 3 .   ? -33.607 -0.988  -19.596 1.00 18.95 ?  1522 HOH   A O   1 
HETATM 4685 O O   . HOH   E 3 .   ? 2.832   -13.242 3.344   1.00 18.46 ?  1523 HOH   A O   1 
HETATM 4686 O O   . HOH   E 3 .   ? -11.360 -12.722 -17.730 1.00 18.95 ?  1524 HOH   A O   1 
HETATM 4687 O O   . HOH   E 3 .   ? -18.380 -20.841 -7.228  1.00 18.95 ?  1525 HOH   A O   1 
HETATM 4688 O O   . HOH   E 3 .   ? -5.200  -5.137  21.139  1.00 18.46 ?  1526 HOH   A O   1 
HETATM 4689 O O   . HOH   E 3 .   ? -1.309  -4.495  -0.613  1.00 18.95 ?  1527 HOH   A O   1 
HETATM 4690 O O   . HOH   E 3 .   ? -8.445  -25.766 18.420  1.00 18.95 ?  1528 HOH   A O   1 
HETATM 4691 O O   . HOH   E 3 .   ? -7.951  -14.350 27.723  1.00 18.95 ?  1529 HOH   A O   1 
HETATM 4692 O O   . HOH   E 3 .   ? -11.141 -8.769  -22.315 1.00 18.95 ?  1530 HOH   A O   1 
HETATM 4693 O O   . HOH   E 3 .   ? -36.592 -1.667  -14.842 1.00 18.95 ?  1531 HOH   A O   1 
HETATM 4694 O O   . HOH   E 3 .   ? -39.295 -2.606  -1.214  1.00 18.46 ?  1532 HOH   A O   1 
HETATM 4695 O O   . HOH   E 3 .   ? -15.853 -25.358 -1.764  1.00 18.46 ?  1533 HOH   A O   1 
HETATM 4696 O O   . HOH   E 3 .   ? -35.708 -9.450  -14.998 1.00 18.46 ?  1534 HOH   A O   1 
HETATM 4697 O O   . HOH   E 3 .   ? -15.314 -11.067 -3.102  1.00 18.95 ?  1535 HOH   A O   1 
HETATM 4698 O O   . HOH   F 3 .   ? -40.621 -10.317 -29.150 1.00 18.95 ?  1501 HOH   B O   1 
HETATM 4699 O O   . HOH   F 3 .   ? -58.371 -4.116  -27.118 1.00 18.95 ?  1502 HOH   B O   1 
HETATM 4700 O O   . HOH   F 3 .   ? -51.350 -11.703 -30.146 1.00 18.95 ?  1503 HOH   B O   1 
HETATM 4701 O O   . HOH   F 3 .   ? -47.082 -21.794 -48.047 1.00 18.95 ?  1504 HOH   B O   1 
HETATM 4702 O O   . HOH   F 3 .   ? -51.141 -28.281 -21.200 1.00 18.95 ?  1505 HOH   B O   1 
HETATM 4703 O O   . HOH   F 3 .   ? -16.772 -9.794  -44.520 1.00 18.95 ?  1506 HOH   B O   1 
HETATM 4704 O O   . HOH   F 3 .   ? -44.055 -9.703  -42.826 1.00 18.95 ?  1507 HOH   B O   1 
HETATM 4705 O O   . HOH   F 3 .   ? -31.152 -24.908 -41.684 1.00 18.95 ?  1508 HOH   B O   1 
HETATM 4706 O O   . HOH   F 3 .   ? -18.541 0.551   -45.981 1.00 18.95 ?  1509 HOH   B O   1 
HETATM 4707 O O   . HOH   F 3 .   ? -41.421 2.204   -41.269 1.00 18.95 ?  1510 HOH   B O   1 
HETATM 4708 O O   . HOH   F 3 .   ? -43.694 7.775   -38.865 1.00 18.95 ?  1511 HOH   B O   1 
HETATM 4709 O O   . HOH   F 3 .   ? -42.563 -12.950 -32.224 1.00 18.95 ?  1512 HOH   B O   1 
HETATM 4710 O O   . HOH   F 3 .   ? -18.621 -12.724 -60.970 1.00 18.95 ?  1513 HOH   B O   1 
HETATM 4711 O O   . HOH   F 3 .   ? -51.395 -7.409  -36.489 1.00 18.95 ?  1514 HOH   B O   1 
HETATM 4712 O O   . HOH   F 3 .   ? -43.017 -15.109 -61.572 1.00 18.95 ?  1515 HOH   B O   1 
HETATM 4713 O O   . HOH   F 3 .   ? -40.475 8.002   -38.279 1.00 18.46 ?  1516 HOH   B O   1 
HETATM 4714 O O   . HOH   F 3 .   ? -49.219 -15.695 -39.812 1.00 18.95 ?  1517 HOH   B O   1 
HETATM 4715 O O   . HOH   F 3 .   ? -24.596 -22.605 -33.684 1.00 18.46 ?  1518 HOH   B O   1 
HETATM 4716 O O   . HOH   F 3 .   ? -32.626 -21.499 -25.669 1.00 18.95 ?  1519 HOH   B O   1 
HETATM 4717 O O   . HOH   F 3 .   ? -37.402 -26.659 -50.194 1.00 18.95 ?  1520 HOH   B O   1 
HETATM 4718 O O   . HOH   F 3 .   ? -18.280 -16.099 -55.954 1.00 18.95 ?  1521 HOH   B O   1 
HETATM 4719 O O   . HOH   F 3 .   ? -56.593 -31.952 -39.310 1.00 18.95 ?  1522 HOH   B O   1 
HETATM 4720 O O   . HOH   F 3 .   ? -23.989 1.227   -42.447 1.00 18.46 ?  1523 HOH   B O   1 
HETATM 4721 O O   . HOH   F 3 .   ? -26.301 0.255   -53.198 1.00 18.95 ?  1524 HOH   B O   1 
HETATM 4722 O O   . HOH   F 3 .   ? -44.268 -9.338  -29.074 1.00 18.95 ?  1525 HOH   B O   1 
HETATM 4723 O O   . HOH   F 3 .   ? -49.861 -16.254 -45.309 1.00 18.46 ?  1526 HOH   B O   1 
HETATM 4724 O O   . HOH   F 3 .   ? -25.403 0.703   -55.171 1.00 18.46 ?  1527 HOH   B O   1 
HETATM 4725 O O   . HOH   F 3 .   ? -41.941 -6.225  -38.546 1.00 18.95 ?  1528 HOH   B O   1 
HETATM 4726 O O   . HOH   F 3 .   ? -26.527 -18.548 -42.234 1.00 18.95 ?  1529 HOH   B O   1 
HETATM 4727 O O   . HOH   F 3 .   ? -39.646 -4.530  -43.277 1.00 18.95 ?  1530 HOH   B O   1 
HETATM 4728 O O   . HOH   F 3 .   ? -54.243 -14.912 -26.642 1.00 18.95 ?  1531 HOH   B O   1 
HETATM 4729 O O   . HOH   F 3 .   ? -29.433 -16.386 -21.261 1.00 18.95 ?  1532 HOH   B O   1 
HETATM 4730 O O   . HOH   F 3 .   ? -32.185 -9.420  -31.533 1.00 18.95 ?  1533 HOH   B O   1 
HETATM 4731 O O   . HOH   F 3 .   ? -23.788 1.338   -40.341 1.00 18.95 ?  1534 HOH   B O   1 
HETATM 4732 O O   . HOH   F 3 .   ? -45.747 -2.433  -40.343 1.00 18.95 ?  1535 HOH   B O   1 
HETATM 4733 O O   . HOH   F 3 .   ? -31.562 -5.334  -57.294 1.00 18.46 ?  1536 HOH   B O   1 
HETATM 4734 O O   . HOH   F 3 .   ? -32.582 -6.011  -59.226 1.00 18.46 ?  1537 HOH   B O   1 
# 
