data_8ZSE
# 
_entry.id   8ZSE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZSE         pdb_00008zse 10.2210/pdb8zse/pdb 
WWPDB D_1300048302 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZSE 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-05 
_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              shang_jinsai@gzlab.ac.cn 
_pdbx_contact_author.name_first         Jinsai 
_pdbx_contact_author.name_last          Shang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8164-1544 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lu, Y.'    1 0000-0002-9985-8546 
'Shang, J.' 2 0000-0001-8164-1544 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal Structure of SARS CoV-2 Papain-like Protease PLpro-C111S in Complex with GZNL-2002' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lu, Y.'    1 0000-0002-9985-8546 
primary 'Shang, J.' 2 0000-0001-8164-1544 
# 
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 'Papain-like protease nsp3'                                                      35712.484 2  3.4.19.12,3.4.22.- 
C111S ? ? 
2 non-polymer syn 'ZINC ION'                                                                       65.409    8  ?                  
?     ? ? 
3 non-polymer syn '2-methyl-5-(4-methylpiperazin-1-yl)-~{N}-(1-quinolin-4-ylcyclopropyl)benzamide' 400.516   2  ?                  
?     ? ? 
4 water       nat water                                                                            18.015    12 ?                  
?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Non-structural protein 3,nsp3,PL2-PRO,Papain-like proteinase,PL-PRO' 
# 
_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       
;GEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSF
LGRYMSALNHTKKWKYPQVNGLTSIKWADNNSYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTV
GELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQES
PFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GEVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSF
LGRYMSALNHTKKWKYPQVNGLTSIKWADNNSYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTV
GELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQES
PFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_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 'ZINC ION'                                                                       ZN    
3 '2-methyl-5-(4-methylpiperazin-1-yl)-~{N}-(1-quinolin-4-ylcyclopropyl)benzamide' A1L2A 
4 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   GLU n 
1 3   VAL n 
1 4   ARG n 
1 5   THR n 
1 6   ILE n 
1 7   LYS n 
1 8   VAL n 
1 9   PHE n 
1 10  THR n 
1 11  THR n 
1 12  VAL n 
1 13  ASP n 
1 14  ASN n 
1 15  ILE n 
1 16  ASN n 
1 17  LEU n 
1 18  HIS n 
1 19  THR n 
1 20  GLN n 
1 21  VAL n 
1 22  VAL n 
1 23  ASP n 
1 24  MET n 
1 25  SER n 
1 26  MET n 
1 27  THR n 
1 28  TYR n 
1 29  GLY n 
1 30  GLN n 
1 31  GLN n 
1 32  PHE n 
1 33  GLY n 
1 34  PRO n 
1 35  THR n 
1 36  TYR n 
1 37  LEU n 
1 38  ASP n 
1 39  GLY n 
1 40  ALA n 
1 41  ASP n 
1 42  VAL n 
1 43  THR n 
1 44  LYS n 
1 45  ILE n 
1 46  LYS n 
1 47  PRO n 
1 48  HIS n 
1 49  ASN n 
1 50  SER n 
1 51  HIS n 
1 52  GLU n 
1 53  GLY n 
1 54  LYS n 
1 55  THR n 
1 56  PHE n 
1 57  TYR n 
1 58  VAL n 
1 59  LEU n 
1 60  PRO n 
1 61  ASN n 
1 62  ASP n 
1 63  ASP n 
1 64  THR n 
1 65  LEU n 
1 66  ARG n 
1 67  VAL n 
1 68  GLU n 
1 69  ALA n 
1 70  PHE n 
1 71  GLU n 
1 72  TYR n 
1 73  TYR n 
1 74  HIS n 
1 75  THR n 
1 76  THR n 
1 77  ASP n 
1 78  PRO n 
1 79  SER n 
1 80  PHE n 
1 81  LEU n 
1 82  GLY n 
1 83  ARG n 
1 84  TYR n 
1 85  MET n 
1 86  SER n 
1 87  ALA n 
1 88  LEU n 
1 89  ASN n 
1 90  HIS n 
1 91  THR n 
1 92  LYS n 
1 93  LYS n 
1 94  TRP n 
1 95  LYS n 
1 96  TYR n 
1 97  PRO n 
1 98  GLN n 
1 99  VAL n 
1 100 ASN n 
1 101 GLY n 
1 102 LEU n 
1 103 THR n 
1 104 SER n 
1 105 ILE n 
1 106 LYS n 
1 107 TRP n 
1 108 ALA n 
1 109 ASP n 
1 110 ASN n 
1 111 ASN n 
1 112 SER n 
1 113 TYR n 
1 114 LEU n 
1 115 ALA n 
1 116 THR n 
1 117 ALA n 
1 118 LEU n 
1 119 LEU n 
1 120 THR n 
1 121 LEU n 
1 122 GLN n 
1 123 GLN n 
1 124 ILE n 
1 125 GLU n 
1 126 LEU n 
1 127 LYS n 
1 128 PHE n 
1 129 ASN n 
1 130 PRO n 
1 131 PRO n 
1 132 ALA n 
1 133 LEU n 
1 134 GLN n 
1 135 ASP n 
1 136 ALA n 
1 137 TYR n 
1 138 TYR n 
1 139 ARG n 
1 140 ALA n 
1 141 ARG n 
1 142 ALA n 
1 143 GLY n 
1 144 GLU n 
1 145 ALA n 
1 146 ALA n 
1 147 ASN n 
1 148 PHE n 
1 149 CYS n 
1 150 ALA n 
1 151 LEU n 
1 152 ILE n 
1 153 LEU n 
1 154 ALA n 
1 155 TYR n 
1 156 CYS n 
1 157 ASN n 
1 158 LYS n 
1 159 THR n 
1 160 VAL n 
1 161 GLY n 
1 162 GLU n 
1 163 LEU n 
1 164 GLY n 
1 165 ASP n 
1 166 VAL n 
1 167 ARG n 
1 168 GLU n 
1 169 THR n 
1 170 MET n 
1 171 SER n 
1 172 TYR n 
1 173 LEU n 
1 174 PHE n 
1 175 GLN n 
1 176 HIS n 
1 177 ALA n 
1 178 ASN n 
1 179 LEU n 
1 180 ASP n 
1 181 SER n 
1 182 CYS n 
1 183 LYS n 
1 184 ARG n 
1 185 VAL n 
1 186 LEU n 
1 187 ASN n 
1 188 VAL n 
1 189 VAL n 
1 190 CYS n 
1 191 LYS n 
1 192 THR n 
1 193 CYS n 
1 194 GLY n 
1 195 GLN n 
1 196 GLN n 
1 197 GLN n 
1 198 THR n 
1 199 THR n 
1 200 LEU n 
1 201 LYS n 
1 202 GLY n 
1 203 VAL n 
1 204 GLU n 
1 205 ALA n 
1 206 VAL n 
1 207 MET n 
1 208 TYR n 
1 209 MET n 
1 210 GLY n 
1 211 THR n 
1 212 LEU n 
1 213 SER n 
1 214 TYR n 
1 215 GLU n 
1 216 GLN n 
1 217 PHE n 
1 218 LYS n 
1 219 LYS n 
1 220 GLY n 
1 221 VAL n 
1 222 GLN n 
1 223 ILE n 
1 224 PRO n 
1 225 CYS n 
1 226 THR n 
1 227 CYS n 
1 228 GLY n 
1 229 LYS n 
1 230 GLN n 
1 231 ALA n 
1 232 THR n 
1 233 LYS n 
1 234 TYR n 
1 235 LEU n 
1 236 VAL n 
1 237 GLN n 
1 238 GLN n 
1 239 GLU n 
1 240 SER n 
1 241 PRO n 
1 242 PHE n 
1 243 VAL n 
1 244 MET n 
1 245 MET n 
1 246 SER n 
1 247 ALA n 
1 248 PRO n 
1 249 PRO n 
1 250 ALA n 
1 251 GLN n 
1 252 TYR n 
1 253 GLU n 
1 254 LEU n 
1 255 LYS n 
1 256 HIS n 
1 257 GLY n 
1 258 THR n 
1 259 PHE n 
1 260 THR n 
1 261 CYS n 
1 262 ALA n 
1 263 SER n 
1 264 GLU n 
1 265 TYR n 
1 266 THR n 
1 267 GLY n 
1 268 ASN n 
1 269 TYR n 
1 270 GLN n 
1 271 CYS n 
1 272 GLY n 
1 273 HIS n 
1 274 TYR n 
1 275 LYS n 
1 276 HIS n 
1 277 ILE n 
1 278 THR n 
1 279 SER n 
1 280 LYS n 
1 281 GLU n 
1 282 THR n 
1 283 LEU n 
1 284 TYR n 
1 285 CYS n 
1 286 ILE n 
1 287 ASP n 
1 288 GLY n 
1 289 ALA n 
1 290 LEU n 
1 291 LEU n 
1 292 THR n 
1 293 LYS n 
1 294 SER n 
1 295 SER n 
1 296 GLU n 
1 297 TYR n 
1 298 LYS n 
1 299 GLY n 
1 300 PRO n 
1 301 ILE n 
1 302 THR n 
1 303 ASP n 
1 304 VAL n 
1 305 PHE n 
1 306 TYR n 
1 307 LYS n 
1 308 GLU n 
1 309 ASN n 
1 310 SER n 
1 311 TYR n 
1 312 THR n 
1 313 THR n 
1 314 THR n 
1 315 ILE n 
1 316 LYS 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                   316 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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 
A1L2A non-polymer         . '2-methyl-5-(4-methylpiperazin-1-yl)-~{N}-(1-quinolin-4-ylcyclopropyl)benzamide' ? 'C25 H28 N4 O'   
400.516 
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 
ZN    non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'           
65.409  
# 
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   0   ?   ?   ?   A . n 
A 1 2   GLU 2   1   1   GLU GLU A . n 
A 1 3   VAL 3   2   2   VAL VAL A . n 
A 1 4   ARG 4   3   3   ARG ARG A . n 
A 1 5   THR 5   4   4   THR THR A . n 
A 1 6   ILE 6   5   5   ILE ILE A . n 
A 1 7   LYS 7   6   6   LYS LYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   PHE 9   8   8   PHE PHE A . n 
A 1 10  THR 10  9   9   THR THR A . n 
A 1 11  THR 11  10  10  THR THR A . n 
A 1 12  VAL 12  11  11  VAL VAL A . n 
A 1 13  ASP 13  12  12  ASP ASP A . n 
A 1 14  ASN 14  13  13  ASN ASN A . n 
A 1 15  ILE 15  14  14  ILE ILE A . n 
A 1 16  ASN 16  15  15  ASN ASN A . n 
A 1 17  LEU 17  16  16  LEU LEU A . n 
A 1 18  HIS 18  17  17  HIS HIS A . n 
A 1 19  THR 19  18  18  THR THR A . n 
A 1 20  GLN 20  19  19  GLN GLN A . n 
A 1 21  VAL 21  20  20  VAL VAL A . n 
A 1 22  VAL 22  21  21  VAL VAL A . n 
A 1 23  ASP 23  22  22  ASP ASP A . n 
A 1 24  MET 24  23  23  MET MET A . n 
A 1 25  SER 25  24  24  SER SER A . n 
A 1 26  MET 26  25  25  MET MET A . n 
A 1 27  THR 27  26  26  THR THR A . n 
A 1 28  TYR 28  27  27  TYR TYR A . n 
A 1 29  GLY 29  28  28  GLY GLY A . n 
A 1 30  GLN 30  29  29  GLN GLN A . n 
A 1 31  GLN 31  30  30  GLN GLN A . n 
A 1 32  PHE 32  31  31  PHE PHE A . n 
A 1 33  GLY 33  32  32  GLY GLY A . n 
A 1 34  PRO 34  33  33  PRO PRO A . n 
A 1 35  THR 35  34  34  THR THR A . n 
A 1 36  TYR 36  35  35  TYR TYR A . n 
A 1 37  LEU 37  36  36  LEU LEU A . n 
A 1 38  ASP 38  37  37  ASP ASP A . n 
A 1 39  GLY 39  38  38  GLY GLY A . n 
A 1 40  ALA 40  39  39  ALA ALA A . n 
A 1 41  ASP 41  40  40  ASP ASP A . n 
A 1 42  VAL 42  41  41  VAL VAL A . n 
A 1 43  THR 43  42  42  THR THR A . n 
A 1 44  LYS 44  43  43  LYS LYS A . n 
A 1 45  ILE 45  44  44  ILE ILE A . n 
A 1 46  LYS 46  45  45  LYS LYS A . n 
A 1 47  PRO 47  46  46  PRO PRO A . n 
A 1 48  HIS 48  47  47  HIS HIS A . n 
A 1 49  ASN 49  48  48  ASN ASN A . n 
A 1 50  SER 50  49  49  SER SER A . n 
A 1 51  HIS 51  50  50  HIS HIS A . n 
A 1 52  GLU 52  51  51  GLU GLU A . n 
A 1 53  GLY 53  52  52  GLY GLY A . n 
A 1 54  LYS 54  53  53  LYS LYS A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  PHE 56  55  55  PHE PHE A . n 
A 1 57  TYR 57  56  56  TYR TYR A . n 
A 1 58  VAL 58  57  57  VAL VAL A . n 
A 1 59  LEU 59  58  58  LEU LEU A . n 
A 1 60  PRO 60  59  59  PRO PRO A . n 
A 1 61  ASN 61  60  60  ASN ASN A . n 
A 1 62  ASP 62  61  61  ASP ASP A . n 
A 1 63  ASP 63  62  62  ASP ASP A . n 
A 1 64  THR 64  63  63  THR THR A . n 
A 1 65  LEU 65  64  64  LEU LEU A . n 
A 1 66  ARG 66  65  65  ARG ARG A . n 
A 1 67  VAL 67  66  66  VAL VAL A . n 
A 1 68  GLU 68  67  67  GLU GLU A . n 
A 1 69  ALA 69  68  68  ALA ALA A . n 
A 1 70  PHE 70  69  69  PHE PHE A . n 
A 1 71  GLU 71  70  70  GLU GLU A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  TYR 73  72  72  TYR TYR A . n 
A 1 74  HIS 74  73  73  HIS HIS A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  THR 76  75  75  THR THR A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  PRO 78  77  77  PRO PRO A . n 
A 1 79  SER 79  78  78  SER SER A . n 
A 1 80  PHE 80  79  79  PHE PHE A . n 
A 1 81  LEU 81  80  80  LEU LEU A . n 
A 1 82  GLY 82  81  81  GLY GLY A . n 
A 1 83  ARG 83  82  82  ARG ARG A . n 
A 1 84  TYR 84  83  83  TYR TYR A . n 
A 1 85  MET 85  84  84  MET MET A . n 
A 1 86  SER 86  85  85  SER SER A . n 
A 1 87  ALA 87  86  86  ALA ALA A . n 
A 1 88  LEU 88  87  87  LEU LEU A . n 
A 1 89  ASN 89  88  88  ASN ASN A . n 
A 1 90  HIS 90  89  89  HIS HIS A . n 
A 1 91  THR 91  90  90  THR THR A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  LYS 93  92  92  LYS LYS A . n 
A 1 94  TRP 94  93  93  TRP TRP A . n 
A 1 95  LYS 95  94  94  LYS LYS A . n 
A 1 96  TYR 96  95  95  TYR TYR A . n 
A 1 97  PRO 97  96  96  PRO PRO A . n 
A 1 98  GLN 98  97  97  GLN GLN A . n 
A 1 99  VAL 99  98  98  VAL VAL A . n 
A 1 100 ASN 100 99  99  ASN ASN A . n 
A 1 101 GLY 101 100 100 GLY GLY A . n 
A 1 102 LEU 102 101 101 LEU LEU A . n 
A 1 103 THR 103 102 102 THR THR A . n 
A 1 104 SER 104 103 103 SER SER A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 LYS 106 105 105 LYS LYS A . n 
A 1 107 TRP 107 106 106 TRP TRP A . n 
A 1 108 ALA 108 107 107 ALA ALA A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 ASN 110 109 109 ASN ASN A . n 
A 1 111 ASN 111 110 110 ASN ASN A . n 
A 1 112 SER 112 111 111 SER SER A . n 
A 1 113 TYR 113 112 112 TYR TYR A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 ALA 115 114 114 ALA ALA A . n 
A 1 116 THR 116 115 115 THR THR A . n 
A 1 117 ALA 117 116 116 ALA ALA A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 THR 120 119 119 THR THR A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 GLN 122 121 121 GLN GLN A . n 
A 1 123 GLN 123 122 122 GLN GLN A . n 
A 1 124 ILE 124 123 123 ILE ILE A . n 
A 1 125 GLU 125 124 124 GLU GLU A . n 
A 1 126 LEU 126 125 125 LEU LEU A . n 
A 1 127 LYS 127 126 126 LYS LYS A . n 
A 1 128 PHE 128 127 127 PHE PHE A . n 
A 1 129 ASN 129 128 128 ASN ASN A . n 
A 1 130 PRO 130 129 129 PRO PRO A . n 
A 1 131 PRO 131 130 130 PRO PRO A . n 
A 1 132 ALA 132 131 131 ALA ALA A . n 
A 1 133 LEU 133 132 132 LEU LEU A . n 
A 1 134 GLN 134 133 133 GLN GLN A . n 
A 1 135 ASP 135 134 134 ASP ASP A . n 
A 1 136 ALA 136 135 135 ALA ALA A . n 
A 1 137 TYR 137 136 136 TYR TYR A . n 
A 1 138 TYR 138 137 137 TYR TYR A . n 
A 1 139 ARG 139 138 138 ARG ARG A . n 
A 1 140 ALA 140 139 139 ALA ALA A . n 
A 1 141 ARG 141 140 140 ARG ARG A . n 
A 1 142 ALA 142 141 141 ALA ALA A . n 
A 1 143 GLY 143 142 142 GLY GLY A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 ALA 145 144 144 ALA ALA A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 ASN 147 146 146 ASN ASN A . n 
A 1 148 PHE 148 147 147 PHE PHE A . n 
A 1 149 CYS 149 148 148 CYS CYS A . n 
A 1 150 ALA 150 149 149 ALA ALA A . n 
A 1 151 LEU 151 150 150 LEU LEU A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 LEU 153 152 152 LEU LEU A . n 
A 1 154 ALA 154 153 153 ALA ALA A . n 
A 1 155 TYR 155 154 154 TYR TYR A . n 
A 1 156 CYS 156 155 155 CYS CYS A . n 
A 1 157 ASN 157 156 156 ASN ASN A . n 
A 1 158 LYS 158 157 157 LYS LYS A . n 
A 1 159 THR 159 158 158 THR THR A . n 
A 1 160 VAL 160 159 159 VAL VAL A . n 
A 1 161 GLY 161 160 160 GLY GLY A . n 
A 1 162 GLU 162 161 161 GLU GLU A . n 
A 1 163 LEU 163 162 162 LEU LEU A . n 
A 1 164 GLY 164 163 163 GLY GLY A . n 
A 1 165 ASP 165 164 164 ASP ASP A . n 
A 1 166 VAL 166 165 165 VAL VAL A . n 
A 1 167 ARG 167 166 166 ARG ARG A . n 
A 1 168 GLU 168 167 167 GLU GLU A . n 
A 1 169 THR 169 168 168 THR THR A . n 
A 1 170 MET 170 169 169 MET MET A . n 
A 1 171 SER 171 170 170 SER SER A . n 
A 1 172 TYR 172 171 171 TYR TYR A . n 
A 1 173 LEU 173 172 172 LEU LEU A . n 
A 1 174 PHE 174 173 173 PHE PHE A . n 
A 1 175 GLN 175 174 174 GLN GLN A . n 
A 1 176 HIS 176 175 175 HIS HIS A . n 
A 1 177 ALA 177 176 176 ALA ALA A . n 
A 1 178 ASN 178 177 177 ASN ASN A . n 
A 1 179 LEU 179 178 178 LEU LEU A . n 
A 1 180 ASP 180 179 179 ASP ASP A . n 
A 1 181 SER 181 180 180 SER SER A . n 
A 1 182 CYS 182 181 181 CYS CYS A . n 
A 1 183 LYS 183 182 182 LYS LYS A . n 
A 1 184 ARG 184 183 183 ARG ARG A . n 
A 1 185 VAL 185 184 184 VAL VAL A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 ASN 187 186 186 ASN ASN A . n 
A 1 188 VAL 188 187 187 VAL VAL A . n 
A 1 189 VAL 189 188 188 VAL VAL A . n 
A 1 190 CYS 190 189 189 CYS CYS A . n 
A 1 191 LYS 191 190 190 LYS LYS A . n 
A 1 192 THR 192 191 191 THR THR A . n 
A 1 193 CYS 193 192 192 CYS CYS A . n 
A 1 194 GLY 194 193 193 GLY GLY A . n 
A 1 195 GLN 195 194 194 GLN GLN A . n 
A 1 196 GLN 196 195 195 GLN GLN A . n 
A 1 197 GLN 197 196 196 GLN GLN A . n 
A 1 198 THR 198 197 197 THR THR A . n 
A 1 199 THR 199 198 198 THR THR A . n 
A 1 200 LEU 200 199 199 LEU LEU A . n 
A 1 201 LYS 201 200 200 LYS LYS A . n 
A 1 202 GLY 202 201 201 GLY GLY A . n 
A 1 203 VAL 203 202 202 VAL VAL A . n 
A 1 204 GLU 204 203 203 GLU GLU A . n 
A 1 205 ALA 205 204 204 ALA ALA A . n 
A 1 206 VAL 206 205 205 VAL VAL A . n 
A 1 207 MET 207 206 206 MET MET A . n 
A 1 208 TYR 208 207 207 TYR TYR A . n 
A 1 209 MET 209 208 208 MET MET A . n 
A 1 210 GLY 210 209 209 GLY GLY A . n 
A 1 211 THR 211 210 210 THR THR A . n 
A 1 212 LEU 212 211 211 LEU LEU A . n 
A 1 213 SER 213 212 212 SER SER A . n 
A 1 214 TYR 214 213 213 TYR TYR A . n 
A 1 215 GLU 215 214 214 GLU GLU A . n 
A 1 216 GLN 216 215 215 GLN GLN A . n 
A 1 217 PHE 217 216 216 PHE PHE A . n 
A 1 218 LYS 218 217 217 LYS LYS A . n 
A 1 219 LYS 219 218 218 LYS LYS A . n 
A 1 220 GLY 220 219 219 GLY GLY A . n 
A 1 221 VAL 221 220 220 VAL VAL A . n 
A 1 222 GLN 222 221 221 GLN GLN A . n 
A 1 223 ILE 223 222 222 ILE ILE A . n 
A 1 224 PRO 224 223 223 PRO PRO A . n 
A 1 225 CYS 225 224 224 CYS CYS A . n 
A 1 226 THR 226 225 225 THR THR A . n 
A 1 227 CYS 227 226 226 CYS CYS A . n 
A 1 228 GLY 228 227 227 GLY GLY A . n 
A 1 229 LYS 229 228 228 LYS LYS A . n 
A 1 230 GLN 230 229 229 GLN GLN A . n 
A 1 231 ALA 231 230 230 ALA ALA A . n 
A 1 232 THR 232 231 231 THR THR A . n 
A 1 233 LYS 233 232 232 LYS LYS A . n 
A 1 234 TYR 234 233 233 TYR TYR A . n 
A 1 235 LEU 235 234 234 LEU LEU A . n 
A 1 236 VAL 236 235 235 VAL VAL A . n 
A 1 237 GLN 237 236 236 GLN GLN A . n 
A 1 238 GLN 238 237 237 GLN GLN A . n 
A 1 239 GLU 239 238 238 GLU GLU A . n 
A 1 240 SER 240 239 239 SER SER A . n 
A 1 241 PRO 241 240 240 PRO PRO A . n 
A 1 242 PHE 242 241 241 PHE PHE A . n 
A 1 243 VAL 243 242 242 VAL VAL A . n 
A 1 244 MET 244 243 243 MET MET A . n 
A 1 245 MET 245 244 244 MET MET A . n 
A 1 246 SER 246 245 245 SER SER A . n 
A 1 247 ALA 247 246 246 ALA ALA A . n 
A 1 248 PRO 248 247 247 PRO PRO A . n 
A 1 249 PRO 249 248 248 PRO PRO A . n 
A 1 250 ALA 250 249 249 ALA ALA A . n 
A 1 251 GLN 251 250 250 GLN GLN A . n 
A 1 252 TYR 252 251 251 TYR TYR A . n 
A 1 253 GLU 253 252 252 GLU GLU A . n 
A 1 254 LEU 254 253 253 LEU LEU A . n 
A 1 255 LYS 255 254 254 LYS LYS A . n 
A 1 256 HIS 256 255 255 HIS HIS A . n 
A 1 257 GLY 257 256 256 GLY GLY A . n 
A 1 258 THR 258 257 257 THR THR A . n 
A 1 259 PHE 259 258 258 PHE PHE A . n 
A 1 260 THR 260 259 259 THR THR A . n 
A 1 261 CYS 261 260 260 CYS CYS A . n 
A 1 262 ALA 262 261 261 ALA ALA A . n 
A 1 263 SER 263 262 262 SER SER A . n 
A 1 264 GLU 264 263 263 GLU GLU A . n 
A 1 265 TYR 265 264 264 TYR TYR A . n 
A 1 266 THR 266 265 265 THR THR A . n 
A 1 267 GLY 267 266 266 GLY GLY A . n 
A 1 268 ASN 268 267 267 ASN ASN A . n 
A 1 269 TYR 269 268 268 TYR TYR A . n 
A 1 270 GLN 270 269 269 GLN GLN A . n 
A 1 271 CYS 271 270 270 CYS CYS A . n 
A 1 272 GLY 272 271 271 GLY GLY A . n 
A 1 273 HIS 273 272 272 HIS HIS A . n 
A 1 274 TYR 274 273 273 TYR TYR A . n 
A 1 275 LYS 275 274 274 LYS LYS A . n 
A 1 276 HIS 276 275 275 HIS HIS A . n 
A 1 277 ILE 277 276 276 ILE ILE A . n 
A 1 278 THR 278 277 277 THR THR A . n 
A 1 279 SER 279 278 278 SER SER A . n 
A 1 280 LYS 280 279 279 LYS LYS A . n 
A 1 281 GLU 281 280 280 GLU GLU A . n 
A 1 282 THR 282 281 281 THR THR A . n 
A 1 283 LEU 283 282 282 LEU LEU A . n 
A 1 284 TYR 284 283 283 TYR TYR A . n 
A 1 285 CYS 285 284 284 CYS CYS A . n 
A 1 286 ILE 286 285 285 ILE ILE A . n 
A 1 287 ASP 287 286 286 ASP ASP A . n 
A 1 288 GLY 288 287 287 GLY GLY A . n 
A 1 289 ALA 289 288 288 ALA ALA A . n 
A 1 290 LEU 290 289 289 LEU LEU A . n 
A 1 291 LEU 291 290 290 LEU LEU A . n 
A 1 292 THR 292 291 291 THR THR A . n 
A 1 293 LYS 293 292 292 LYS LYS A . n 
A 1 294 SER 294 293 293 SER SER A . n 
A 1 295 SER 295 294 294 SER SER A . n 
A 1 296 GLU 296 295 295 GLU GLU A . n 
A 1 297 TYR 297 296 296 TYR TYR A . n 
A 1 298 LYS 298 297 297 LYS LYS A . n 
A 1 299 GLY 299 298 298 GLY GLY A . n 
A 1 300 PRO 300 299 299 PRO PRO A . n 
A 1 301 ILE 301 300 300 ILE ILE A . n 
A 1 302 THR 302 301 301 THR THR A . n 
A 1 303 ASP 303 302 302 ASP ASP A . n 
A 1 304 VAL 304 303 303 VAL VAL A . n 
A 1 305 PHE 305 304 304 PHE PHE A . n 
A 1 306 TYR 306 305 305 TYR TYR A . n 
A 1 307 LYS 307 306 306 LYS LYS A . n 
A 1 308 GLU 308 307 307 GLU GLU A . n 
A 1 309 ASN 309 308 308 ASN ASN A . n 
A 1 310 SER 310 309 309 SER SER A . n 
A 1 311 TYR 311 310 310 TYR TYR A . n 
A 1 312 THR 312 311 311 THR THR A . n 
A 1 313 THR 313 312 312 THR THR A . n 
A 1 314 THR 314 313 313 THR THR A . n 
A 1 315 ILE 315 314 314 ILE ILE A . n 
A 1 316 LYS 316 315 315 LYS LYS A . n 
B 1 1   GLY 1   0   ?   ?   ?   B . n 
B 1 2   GLU 2   1   ?   ?   ?   B . n 
B 1 3   VAL 3   2   ?   ?   ?   B . n 
B 1 4   ARG 4   3   ?   ?   ?   B . n 
B 1 5   THR 5   4   ?   ?   ?   B . n 
B 1 6   ILE 6   5   ?   ?   ?   B . n 
B 1 7   LYS 7   6   ?   ?   ?   B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   PHE 9   8   8   PHE PHE B . n 
B 1 10  THR 10  9   9   THR THR B . n 
B 1 11  THR 11  10  10  THR THR B . n 
B 1 12  VAL 12  11  11  VAL VAL B . n 
B 1 13  ASP 13  12  12  ASP ASP B . n 
B 1 14  ASN 14  13  13  ASN ASN B . n 
B 1 15  ILE 15  14  14  ILE ILE B . n 
B 1 16  ASN 16  15  15  ASN ASN B . n 
B 1 17  LEU 17  16  16  LEU LEU B . n 
B 1 18  HIS 18  17  17  HIS HIS B . n 
B 1 19  THR 19  18  18  THR THR B . n 
B 1 20  GLN 20  19  19  GLN GLN B . n 
B 1 21  VAL 21  20  20  VAL VAL B . n 
B 1 22  VAL 22  21  21  VAL VAL B . n 
B 1 23  ASP 23  22  22  ASP ASP B . n 
B 1 24  MET 24  23  23  MET MET B . n 
B 1 25  SER 25  24  24  SER SER B . n 
B 1 26  MET 26  25  25  MET MET B . n 
B 1 27  THR 27  26  26  THR THR B . n 
B 1 28  TYR 28  27  27  TYR TYR B . n 
B 1 29  GLY 29  28  28  GLY GLY B . n 
B 1 30  GLN 30  29  29  GLN GLN B . n 
B 1 31  GLN 31  30  30  GLN GLN B . n 
B 1 32  PHE 32  31  31  PHE PHE B . n 
B 1 33  GLY 33  32  32  GLY GLY B . n 
B 1 34  PRO 34  33  33  PRO PRO B . n 
B 1 35  THR 35  34  34  THR THR B . n 
B 1 36  TYR 36  35  35  TYR TYR B . n 
B 1 37  LEU 37  36  36  LEU LEU B . n 
B 1 38  ASP 38  37  37  ASP ASP B . n 
B 1 39  GLY 39  38  38  GLY GLY B . n 
B 1 40  ALA 40  39  39  ALA ALA B . n 
B 1 41  ASP 41  40  40  ASP ASP B . n 
B 1 42  VAL 42  41  41  VAL VAL B . n 
B 1 43  THR 43  42  42  THR THR B . n 
B 1 44  LYS 44  43  43  LYS LYS B . n 
B 1 45  ILE 45  44  44  ILE ILE B . n 
B 1 46  LYS 46  45  45  LYS LYS B . n 
B 1 47  PRO 47  46  46  PRO PRO B . n 
B 1 48  HIS 48  47  47  HIS HIS B . n 
B 1 49  ASN 49  48  48  ASN ASN B . n 
B 1 50  SER 50  49  49  SER SER B . n 
B 1 51  HIS 51  50  50  HIS HIS B . n 
B 1 52  GLU 52  51  51  GLU GLU B . n 
B 1 53  GLY 53  52  52  GLY GLY B . n 
B 1 54  LYS 54  53  53  LYS LYS B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  PHE 56  55  55  PHE PHE B . n 
B 1 57  TYR 57  56  56  TYR TYR B . n 
B 1 58  VAL 58  57  57  VAL VAL B . n 
B 1 59  LEU 59  58  58  LEU LEU B . n 
B 1 60  PRO 60  59  59  PRO PRO B . n 
B 1 61  ASN 61  60  60  ASN ASN B . n 
B 1 62  ASP 62  61  61  ASP ASP B . n 
B 1 63  ASP 63  62  62  ASP ASP B . n 
B 1 64  THR 64  63  63  THR THR B . n 
B 1 65  LEU 65  64  64  LEU LEU B . n 
B 1 66  ARG 66  65  65  ARG ARG B . n 
B 1 67  VAL 67  66  66  VAL VAL B . n 
B 1 68  GLU 68  67  67  GLU GLU B . n 
B 1 69  ALA 69  68  68  ALA ALA B . n 
B 1 70  PHE 70  69  69  PHE PHE B . n 
B 1 71  GLU 71  70  70  GLU GLU B . n 
B 1 72  TYR 72  71  71  TYR TYR B . n 
B 1 73  TYR 73  72  72  TYR TYR B . n 
B 1 74  HIS 74  73  73  HIS HIS B . n 
B 1 75  THR 75  74  74  THR THR B . n 
B 1 76  THR 76  75  75  THR THR B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  PRO 78  77  77  PRO PRO B . n 
B 1 79  SER 79  78  78  SER SER B . n 
B 1 80  PHE 80  79  79  PHE PHE B . n 
B 1 81  LEU 81  80  80  LEU LEU B . n 
B 1 82  GLY 82  81  81  GLY GLY B . n 
B 1 83  ARG 83  82  82  ARG ARG B . n 
B 1 84  TYR 84  83  83  TYR TYR B . n 
B 1 85  MET 85  84  84  MET MET B . n 
B 1 86  SER 86  85  85  SER SER B . n 
B 1 87  ALA 87  86  86  ALA ALA B . n 
B 1 88  LEU 88  87  87  LEU LEU B . n 
B 1 89  ASN 89  88  88  ASN ASN B . n 
B 1 90  HIS 90  89  89  HIS HIS B . n 
B 1 91  THR 91  90  90  THR THR B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  LYS 93  92  92  LYS LYS B . n 
B 1 94  TRP 94  93  93  TRP TRP B . n 
B 1 95  LYS 95  94  94  LYS LYS B . n 
B 1 96  TYR 96  95  95  TYR TYR B . n 
B 1 97  PRO 97  96  96  PRO PRO B . n 
B 1 98  GLN 98  97  97  GLN GLN B . n 
B 1 99  VAL 99  98  98  VAL VAL B . n 
B 1 100 ASN 100 99  99  ASN ASN B . n 
B 1 101 GLY 101 100 100 GLY GLY B . n 
B 1 102 LEU 102 101 101 LEU LEU B . n 
B 1 103 THR 103 102 102 THR THR B . n 
B 1 104 SER 104 103 103 SER SER B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 LYS 106 105 105 LYS LYS B . n 
B 1 107 TRP 107 106 106 TRP TRP B . n 
B 1 108 ALA 108 107 107 ALA ALA B . n 
B 1 109 ASP 109 108 108 ASP ASP B . n 
B 1 110 ASN 110 109 109 ASN ASN B . n 
B 1 111 ASN 111 110 110 ASN ASN B . n 
B 1 112 SER 112 111 111 SER SER B . n 
B 1 113 TYR 113 112 112 TYR TYR B . n 
B 1 114 LEU 114 113 113 LEU LEU B . n 
B 1 115 ALA 115 114 114 ALA ALA B . n 
B 1 116 THR 116 115 115 THR THR B . n 
B 1 117 ALA 117 116 116 ALA ALA B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 LEU 119 118 118 LEU LEU B . n 
B 1 120 THR 120 119 119 THR THR B . n 
B 1 121 LEU 121 120 120 LEU LEU B . n 
B 1 122 GLN 122 121 121 GLN GLN B . n 
B 1 123 GLN 123 122 122 GLN GLN B . n 
B 1 124 ILE 124 123 123 ILE ILE B . n 
B 1 125 GLU 125 124 124 GLU GLU B . n 
B 1 126 LEU 126 125 125 LEU LEU B . n 
B 1 127 LYS 127 126 126 LYS LYS B . n 
B 1 128 PHE 128 127 127 PHE PHE B . n 
B 1 129 ASN 129 128 128 ASN ASN B . n 
B 1 130 PRO 130 129 129 PRO PRO B . n 
B 1 131 PRO 131 130 130 PRO PRO B . n 
B 1 132 ALA 132 131 131 ALA ALA B . n 
B 1 133 LEU 133 132 132 LEU LEU B . n 
B 1 134 GLN 134 133 133 GLN GLN B . n 
B 1 135 ASP 135 134 134 ASP ASP B . n 
B 1 136 ALA 136 135 135 ALA ALA B . n 
B 1 137 TYR 137 136 136 TYR TYR B . n 
B 1 138 TYR 138 137 137 TYR TYR B . n 
B 1 139 ARG 139 138 138 ARG ARG B . n 
B 1 140 ALA 140 139 139 ALA ALA B . n 
B 1 141 ARG 141 140 140 ARG ARG B . n 
B 1 142 ALA 142 141 141 ALA ALA B . n 
B 1 143 GLY 143 142 142 GLY GLY B . n 
B 1 144 GLU 144 143 143 GLU GLU B . n 
B 1 145 ALA 145 144 144 ALA ALA B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 ASN 147 146 146 ASN ASN B . n 
B 1 148 PHE 148 147 147 PHE PHE B . n 
B 1 149 CYS 149 148 148 CYS CYS B . n 
B 1 150 ALA 150 149 149 ALA ALA B . n 
B 1 151 LEU 151 150 150 LEU LEU B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 LEU 153 152 152 LEU LEU B . n 
B 1 154 ALA 154 153 153 ALA ALA B . n 
B 1 155 TYR 155 154 154 TYR TYR B . n 
B 1 156 CYS 156 155 155 CYS CYS B . n 
B 1 157 ASN 157 156 156 ASN ASN B . n 
B 1 158 LYS 158 157 157 LYS LYS B . n 
B 1 159 THR 159 158 158 THR THR B . n 
B 1 160 VAL 160 159 159 VAL VAL B . n 
B 1 161 GLY 161 160 160 GLY GLY B . n 
B 1 162 GLU 162 161 161 GLU GLU B . n 
B 1 163 LEU 163 162 162 LEU LEU B . n 
B 1 164 GLY 164 163 163 GLY GLY B . n 
B 1 165 ASP 165 164 164 ASP ASP B . n 
B 1 166 VAL 166 165 165 VAL VAL B . n 
B 1 167 ARG 167 166 166 ARG ARG B . n 
B 1 168 GLU 168 167 167 GLU GLU B . n 
B 1 169 THR 169 168 168 THR THR B . n 
B 1 170 MET 170 169 169 MET MET B . n 
B 1 171 SER 171 170 170 SER SER B . n 
B 1 172 TYR 172 171 171 TYR TYR B . n 
B 1 173 LEU 173 172 172 LEU LEU B . n 
B 1 174 PHE 174 173 173 PHE PHE B . n 
B 1 175 GLN 175 174 174 GLN GLN B . n 
B 1 176 HIS 176 175 175 HIS HIS B . n 
B 1 177 ALA 177 176 176 ALA ALA B . n 
B 1 178 ASN 178 177 177 ASN ASN B . n 
B 1 179 LEU 179 178 178 LEU LEU B . n 
B 1 180 ASP 180 179 179 ASP ASP B . n 
B 1 181 SER 181 180 180 SER SER B . n 
B 1 182 CYS 182 181 181 CYS CYS B . n 
B 1 183 LYS 183 182 182 LYS LYS B . n 
B 1 184 ARG 184 183 183 ARG ARG B . n 
B 1 185 VAL 185 184 184 VAL VAL B . n 
B 1 186 LEU 186 185 185 LEU LEU B . n 
B 1 187 ASN 187 186 186 ASN ASN B . n 
B 1 188 VAL 188 187 187 VAL VAL B . n 
B 1 189 VAL 189 188 188 VAL VAL B . n 
B 1 190 CYS 190 189 189 CYS CYS B . n 
B 1 191 LYS 191 190 190 LYS LYS B . n 
B 1 192 THR 192 191 191 THR THR B . n 
B 1 193 CYS 193 192 192 CYS CYS B . n 
B 1 194 GLY 194 193 193 GLY GLY B . n 
B 1 195 GLN 195 194 194 GLN GLN B . n 
B 1 196 GLN 196 195 195 GLN GLN B . n 
B 1 197 GLN 197 196 196 GLN GLN B . n 
B 1 198 THR 198 197 197 THR THR B . n 
B 1 199 THR 199 198 198 THR THR B . n 
B 1 200 LEU 200 199 199 LEU LEU B . n 
B 1 201 LYS 201 200 200 LYS LYS B . n 
B 1 202 GLY 202 201 201 GLY GLY B . n 
B 1 203 VAL 203 202 202 VAL VAL B . n 
B 1 204 GLU 204 203 203 GLU GLU B . n 
B 1 205 ALA 205 204 204 ALA ALA B . n 
B 1 206 VAL 206 205 205 VAL VAL B . n 
B 1 207 MET 207 206 206 MET MET B . n 
B 1 208 TYR 208 207 207 TYR TYR B . n 
B 1 209 MET 209 208 208 MET MET B . n 
B 1 210 GLY 210 209 209 GLY GLY B . n 
B 1 211 THR 211 210 210 THR THR B . n 
B 1 212 LEU 212 211 211 LEU LEU B . n 
B 1 213 SER 213 212 212 SER SER B . n 
B 1 214 TYR 214 213 213 TYR TYR B . n 
B 1 215 GLU 215 214 214 GLU GLU B . n 
B 1 216 GLN 216 215 215 GLN GLN B . n 
B 1 217 PHE 217 216 216 PHE PHE B . n 
B 1 218 LYS 218 217 217 LYS LYS B . n 
B 1 219 LYS 219 218 218 LYS LYS B . n 
B 1 220 GLY 220 219 219 GLY GLY B . n 
B 1 221 VAL 221 220 220 VAL VAL B . n 
B 1 222 GLN 222 221 221 GLN GLN B . n 
B 1 223 ILE 223 222 222 ILE ILE B . n 
B 1 224 PRO 224 223 223 PRO PRO B . n 
B 1 225 CYS 225 224 224 CYS CYS B . n 
B 1 226 THR 226 225 225 THR THR B . n 
B 1 227 CYS 227 226 226 CYS CYS B . n 
B 1 228 GLY 228 227 227 GLY GLY B . n 
B 1 229 LYS 229 228 228 LYS LYS B . n 
B 1 230 GLN 230 229 229 GLN GLN B . n 
B 1 231 ALA 231 230 230 ALA ALA B . n 
B 1 232 THR 232 231 231 THR THR B . n 
B 1 233 LYS 233 232 232 LYS LYS B . n 
B 1 234 TYR 234 233 233 TYR TYR B . n 
B 1 235 LEU 235 234 234 LEU LEU B . n 
B 1 236 VAL 236 235 235 VAL VAL B . n 
B 1 237 GLN 237 236 236 GLN GLN B . n 
B 1 238 GLN 238 237 237 GLN GLN B . n 
B 1 239 GLU 239 238 238 GLU GLU B . n 
B 1 240 SER 240 239 239 SER SER B . n 
B 1 241 PRO 241 240 240 PRO PRO B . n 
B 1 242 PHE 242 241 241 PHE PHE B . n 
B 1 243 VAL 243 242 242 VAL VAL B . n 
B 1 244 MET 244 243 243 MET MET B . n 
B 1 245 MET 245 244 244 MET MET B . n 
B 1 246 SER 246 245 245 SER SER B . n 
B 1 247 ALA 247 246 246 ALA ALA B . n 
B 1 248 PRO 248 247 247 PRO PRO B . n 
B 1 249 PRO 249 248 248 PRO PRO B . n 
B 1 250 ALA 250 249 249 ALA ALA B . n 
B 1 251 GLN 251 250 250 GLN GLN B . n 
B 1 252 TYR 252 251 251 TYR TYR B . n 
B 1 253 GLU 253 252 252 GLU GLU B . n 
B 1 254 LEU 254 253 253 LEU LEU B . n 
B 1 255 LYS 255 254 254 LYS LYS B . n 
B 1 256 HIS 256 255 255 HIS HIS B . n 
B 1 257 GLY 257 256 256 GLY GLY B . n 
B 1 258 THR 258 257 257 THR THR B . n 
B 1 259 PHE 259 258 258 PHE PHE B . n 
B 1 260 THR 260 259 259 THR THR B . n 
B 1 261 CYS 261 260 260 CYS CYS B . n 
B 1 262 ALA 262 261 261 ALA ALA B . n 
B 1 263 SER 263 262 262 SER SER B . n 
B 1 264 GLU 264 263 263 GLU GLU B . n 
B 1 265 TYR 265 264 264 TYR TYR B . n 
B 1 266 THR 266 265 265 THR THR B . n 
B 1 267 GLY 267 266 266 GLY GLY B . n 
B 1 268 ASN 268 267 267 ASN ASN B . n 
B 1 269 TYR 269 268 268 TYR TYR B . n 
B 1 270 GLN 270 269 269 GLN GLN B . n 
B 1 271 CYS 271 270 270 CYS CYS B . n 
B 1 272 GLY 272 271 271 GLY GLY B . n 
B 1 273 HIS 273 272 272 HIS HIS B . n 
B 1 274 TYR 274 273 273 TYR TYR B . n 
B 1 275 LYS 275 274 274 LYS LYS B . n 
B 1 276 HIS 276 275 275 HIS HIS B . n 
B 1 277 ILE 277 276 276 ILE ILE B . n 
B 1 278 THR 278 277 277 THR THR B . n 
B 1 279 SER 279 278 278 SER SER B . n 
B 1 280 LYS 280 279 279 LYS LYS B . n 
B 1 281 GLU 281 280 280 GLU GLU B . n 
B 1 282 THR 282 281 281 THR THR B . n 
B 1 283 LEU 283 282 282 LEU LEU B . n 
B 1 284 TYR 284 283 283 TYR TYR B . n 
B 1 285 CYS 285 284 284 CYS CYS B . n 
B 1 286 ILE 286 285 285 ILE ILE B . n 
B 1 287 ASP 287 286 286 ASP ASP B . n 
B 1 288 GLY 288 287 287 GLY GLY B . n 
B 1 289 ALA 289 288 288 ALA ALA B . n 
B 1 290 LEU 290 289 289 LEU LEU B . n 
B 1 291 LEU 291 290 290 LEU LEU B . n 
B 1 292 THR 292 291 291 THR THR B . n 
B 1 293 LYS 293 292 292 LYS LYS B . n 
B 1 294 SER 294 293 293 SER SER B . n 
B 1 295 SER 295 294 294 SER SER B . n 
B 1 296 GLU 296 295 295 GLU GLU B . n 
B 1 297 TYR 297 296 296 TYR TYR B . n 
B 1 298 LYS 298 297 297 LYS LYS B . n 
B 1 299 GLY 299 298 298 GLY GLY B . n 
B 1 300 PRO 300 299 299 PRO PRO B . n 
B 1 301 ILE 301 300 300 ILE ILE B . n 
B 1 302 THR 302 301 301 THR THR B . n 
B 1 303 ASP 303 302 302 ASP ASP B . n 
B 1 304 VAL 304 303 303 VAL VAL B . n 
B 1 305 PHE 305 304 304 PHE PHE B . n 
B 1 306 TYR 306 305 305 TYR TYR B . n 
B 1 307 LYS 307 306 306 LYS LYS B . n 
B 1 308 GLU 308 307 307 GLU GLU B . n 
B 1 309 ASN 309 308 308 ASN ASN B . n 
B 1 310 SER 310 309 309 SER SER B . n 
B 1 311 TYR 311 310 310 TYR TYR B . n 
B 1 312 THR 312 311 311 THR THR B . n 
B 1 313 THR 313 312 312 THR THR B . n 
B 1 314 THR 314 313 313 THR THR B . n 
B 1 315 ILE 315 314 314 ILE ILE B . n 
B 1 316 LYS 316 315 315 LYS LYS B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L2A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L2A 
_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 ZN    1 401 341 ZN    ZN  A . 
D 2 ZN    1 402 342 ZN    ZN  A . 
E 2 ZN    1 403 343 ZN    ZN  A . 
F 2 ZN    1 404 344 ZN    ZN  A . 
G 3 A1L2A 1 405 351 A1L2A 325 A . 
H 2 ZN    1 401 341 ZN    ZN  B . 
I 2 ZN    1 402 342 ZN    ZN  B . 
J 2 ZN    1 403 343 ZN    ZN  B . 
K 2 ZN    1 404 344 ZN    ZN  B . 
L 3 A1L2A 1 405 351 A1L2A 325 B . 
M 4 HOH   1 501 365 HOH   HOH A . 
M 4 HOH   2 502 363 HOH   HOH A . 
M 4 HOH   3 503 361 HOH   HOH A . 
M 4 HOH   4 504 361 HOH   HOH A . 
N 4 HOH   1 501 368 HOH   HOH B . 
N 4 HOH   2 502 366 HOH   HOH B . 
N 4 HOH   3 503 367 HOH   HOH B . 
N 4 HOH   4 504 364 HOH   HOH B . 
N 4 HOH   5 505 362 HOH   HOH B . 
N 4 HOH   6 506 362 HOH   HOH B . 
N 4 HOH   7 507 365 HOH   HOH B . 
N 4 HOH   8 508 363 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZSE 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     95.180 
_cell.length_a_esd                 ? 
_cell.length_b                     95.180 
_cell.length_b_esd                 ? 
_cell.length_c                     232.350 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8ZSE 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                91 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 2 2' 
_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                   8ZSE 
_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             3.68 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.61 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.05 M Zinc acetate dihydrate, 20% w/v Polyethylene glycol 3,350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZSE 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.8 
_reflns.d_resolution_low                               88.08 
_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                                     26015 
_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                           96.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.68 
_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                                0.093 
_reflns.pdbx_Rpim_I_all                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.975 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_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                                    2.8 
_reflns_shell.d_res_low                                     2.95 
_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                             3765 
_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                               3.1 
_reflns_shell.pdbx_chi_squared                              0.46 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.307 
_reflns_shell.pdbx_Rpim_I_all                               0.166 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.935 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.256 
_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                                 8ZSE 
_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                            2.80 
_refine.ls_d_res_low                             73.63 
_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                     25999 
_refine.ls_number_reflns_R_free                  1288 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.65 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2114 
_refine.ls_R_factor_R_free                       0.2571 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2089 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_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                      7CJM 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_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                 28.73 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.34 
_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                       2.80 
_refine_hist.d_res_low                        73.63 
_refine_hist.number_atoms_solvent             12 
_refine_hist.number_atoms_total               5031 
_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        4951 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.010  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.166  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.097 ? 707 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 767 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 884 ? 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' 2.80 2.91  . . 123 2720 97.00 . . . . 0.2723 . . . . . . . . . . . 0.3692 
'X-RAY DIFFRACTION' 2.91 3.04  . . 158 2729 97.00 . . . . 0.2698 . . . . . . . . . . . 0.3125 
'X-RAY DIFFRACTION' 3.04 3.21  . . 141 2726 97.00 . . . . 0.2584 . . . . . . . . . . . 0.3263 
'X-RAY DIFFRACTION' 3.21 3.41  . . 142 2728 96.00 . . . . 0.2404 . . . . . . . . . . . 0.3313 
'X-RAY DIFFRACTION' 3.41 3.67  . . 133 2730 96.00 . . . . 0.2304 . . . . . . . . . . . 0.2836 
'X-RAY DIFFRACTION' 3.67 4.04  . . 139 2708 96.00 . . . . 0.2082 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 4.04 4.62  . . 135 2789 96.00 . . . . 0.1704 . . . . . . . . . . . 0.2058 
'X-RAY DIFFRACTION' 4.62 5.82  . . 151 2738 94.00 . . . . 0.1760 . . . . . . . . . . . 0.2171 
'X-RAY DIFFRACTION' 5.82 73.63 . . 166 2843 92.00 . . . . 0.1991 . . . . . . . . . . . 0.2455 
# 
_struct.entry_id                     8ZSE 
_struct.title                        'Crystal Structure of SARS CoV-2 Papain-like Protease PLpro-C111S in Complex with GZNL-2002' 
_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        8ZSE 
_struct_keywords.text            'SARS CoV-2, PAPAIN-LIKE PROTEINASE, NSP3, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
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 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;EVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFL
GRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVG
ELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESP
FVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIK
;
_struct_ref.pdbx_align_begin           1564 
# 
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 8ZSE A 2 ? 316 ? P0DTD1 1564 ? 1878 ? 1 315 
2 1 8ZSE B 2 ? 316 ? P0DTD1 1564 ? 1878 ? 1 315 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZSE GLY A 1   ? UNP P0DTD1 ?   ?    'expression tag'      0   1 
1 8ZSE SER A 112 ? UNP P0DTD1 CYS 1674 'engineered mutation' 111 2 
2 8ZSE GLY B 1   ? UNP P0DTD1 ?   ?    'expression tag'      0   3 
2 8ZSE SER B 112 ? UNP P0DTD1 CYS 1674 'engineered mutation' 111 4 
# 
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,D,E,F,G,M 
2 1 B,H,I,J,K,L,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 27  ? GLY A 33  ? THR A 26  GLY A 32  1 ? 7  
HELX_P HELX_P2  AA2 HIS A 48  ? GLU A 52  ? HIS A 47  GLU A 51  5 ? 5  
HELX_P HELX_P3  AA3 ASP A 62  ? HIS A 74  ? ASP A 61  HIS A 73  1 ? 13 
HELX_P HELX_P4  AA4 SER A 79  ? LYS A 92  ? SER A 78  LYS A 91  1 ? 14 
HELX_P HELX_P5  AA5 ASN A 111 ? GLN A 122 ? ASN A 110 GLN A 121 1 ? 12 
HELX_P HELX_P6  AA6 PRO A 130 ? ALA A 142 ? PRO A 129 ALA A 141 1 ? 13 
HELX_P HELX_P7  AA7 ALA A 145 ? ASN A 157 ? ALA A 144 ASN A 156 1 ? 13 
HELX_P HELX_P8  AA8 ASP A 165 ? GLN A 175 ? ASP A 164 GLN A 174 1 ? 11 
HELX_P HELX_P9  AA9 VAL A 203 ? ALA A 205 ? VAL A 202 ALA A 204 5 ? 3  
HELX_P HELX_P10 AB1 SER A 213 ? GLY A 220 ? SER A 212 GLY A 219 1 ? 8  
HELX_P HELX_P11 AB2 THR B 27  ? PHE B 32  ? THR B 26  PHE B 31  1 ? 6  
HELX_P HELX_P12 AB3 ASP B 62  ? HIS B 74  ? ASP B 61  HIS B 73  1 ? 13 
HELX_P HELX_P13 AB4 SER B 79  ? LYS B 92  ? SER B 78  LYS B 91  1 ? 14 
HELX_P HELX_P14 AB5 ASN B 111 ? GLN B 122 ? ASN B 110 GLN B 121 1 ? 12 
HELX_P HELX_P15 AB6 PRO B 130 ? GLY B 143 ? PRO B 129 GLY B 142 1 ? 14 
HELX_P HELX_P16 AB7 ALA B 145 ? ASN B 157 ? ALA B 144 ASN B 156 1 ? 13 
HELX_P HELX_P17 AB8 ASP B 165 ? GLN B 175 ? ASP B 164 GLN B 174 1 ? 11 
HELX_P HELX_P18 AB9 GLY B 202 ? VAL B 206 ? GLY B 201 VAL B 205 1 ? 5  
HELX_P HELX_P19 AC1 SER B 213 ? GLY B 220 ? SER B 212 GLY B 219 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 63  OD1 ? ? ? 1_555 K ZN  .   ZN  ? ? A ASP 62  B ZN  404 8_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc2  metalc ? ? A HIS 74  ND1 ? ? ? 1_555 F ZN  .   ZN  ? ? A HIS 73  A ZN  404 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc3  metalc ? ? A HIS 90  ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 89  A ZN  403 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc4  metalc ? ? A ASP 109 OD2 ? ? ? 1_555 E ZN  .   ZN  ? ? A ASP 108 A ZN  403 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc5  metalc ? ? A HIS 176 ND1 ? ? ? 1_555 F ZN  .   ZN  ? ? A HIS 175 A ZN  404 1_555 ? ? ? ? ? ? ? 2.222 ? ? 
metalc6  metalc ? ? A CYS 190 SG  ? ? ? 1_555 C ZN  .   ZN  ? ? A CYS 189 A ZN  401 1_555 ? ? ? ? ? ? ? 2.550 ? ? 
metalc7  metalc ? ? A CYS 193 SG  ? ? ? 1_555 C ZN  .   ZN  ? ? A CYS 192 A ZN  401 1_555 ? ? ? ? ? ? ? 2.578 ? ? 
metalc8  metalc ? ? A CYS 225 SG  ? ? ? 1_555 C ZN  .   ZN  ? ? A CYS 224 A ZN  401 1_555 ? ? ? ? ? ? ? 2.601 ? ? 
metalc9  metalc ? ? A CYS 271 SG  ? ? ? 1_555 J ZN  .   ZN  ? ? A CYS 270 B ZN  403 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc10 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 B CYS 271 SG  ? ? A ZN  403 B CYS 270 1_555 ? ? ? ? ? ? ? 2.648 ? ? 
metalc11 metalc ? ? F ZN  .   ZN  ? ? ? 8_555 B ASP 63  OD1 ? ? A ZN  404 B ASP 62  1_555 ? ? ? ? ? ? ? 2.639 ? ? 
metalc12 metalc ? ? F ZN  .   ZN  ? ? ? 8_555 B ASP 63  OD2 ? ? A ZN  404 B ASP 62  1_555 ? ? ? ? ? ? ? 1.921 ? ? 
metalc13 metalc ? ? B HIS 74  ND1 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 73  B ZN  404 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc14 metalc ? ? B HIS 90  ND1 ? ? ? 1_555 J ZN  .   ZN  ? ? B HIS 89  B ZN  403 1_555 ? ? ? ? ? ? ? 2.012 ? ? 
metalc15 metalc ? ? B ASP 109 OD2 ? ? ? 1_555 J ZN  .   ZN  ? ? B ASP 108 B ZN  403 1_555 ? ? ? ? ? ? ? 2.148 ? ? 
metalc16 metalc ? ? B SER 112 OG  ? ? ? 1_555 I ZN  .   ZN  ? ? B SER 111 B ZN  402 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc17 metalc ? ? B HIS 176 ND1 ? ? ? 1_555 K ZN  .   ZN  ? ? B HIS 175 B ZN  404 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
metalc18 metalc ? ? B CYS 190 SG  ? ? ? 1_555 H ZN  .   ZN  ? ? B CYS 189 B ZN  401 1_555 ? ? ? ? ? ? ? 2.540 ? ? 
metalc19 metalc ? ? B CYS 193 SG  ? ? ? 1_555 H ZN  .   ZN  ? ? B CYS 192 B ZN  401 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc20 metalc ? ? B CYS 225 SG  ? ? ? 1_555 H ZN  .   ZN  ? ? B CYS 224 B ZN  401 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc21 metalc ? ? B CYS 227 SG  ? ? ? 1_555 H ZN  .   ZN  ? ? B CYS 226 B ZN  401 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc22 metalc ? ? B HIS 273 ND1 ? ? ? 1_555 I ZN  .   ZN  ? ? B HIS 272 B ZN  402 1_555 ? ? ? ? ? ? ? 2.527 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 63  ? A ASP 62  ? 1_555 ZN ? K ZN . ? B ZN 404 ? 8_555 ND1 ? B HIS 74  ? B HIS 73  ? 1_555 93.1  ? 
2  OD1 ? A ASP 63  ? A ASP 62  ? 1_555 ZN ? K ZN . ? B ZN 404 ? 8_555 ND1 ? B HIS 176 ? B HIS 175 ? 1_555 90.8  ? 
3  ND1 ? B HIS 74  ? B HIS 73  ? 1_555 ZN ? K ZN . ? B ZN 404 ? 8_555 ND1 ? B HIS 176 ? B HIS 175 ? 1_555 3.3   ? 
4  ND1 ? A HIS 74  ? A HIS 73  ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 ND1 ? A HIS 176 ? A HIS 175 ? 1_555 120.5 ? 
5  ND1 ? A HIS 74  ? A HIS 73  ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 OD1 ? B ASP 63  ? B ASP 62  ? 1_555 141.3 ? 
6  ND1 ? A HIS 176 ? A HIS 175 ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 OD1 ? B ASP 63  ? B ASP 62  ? 1_555 66.5  ? 
7  ND1 ? A HIS 74  ? A HIS 73  ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 OD2 ? B ASP 63  ? B ASP 62  ? 1_555 141.7 ? 
8  ND1 ? A HIS 176 ? A HIS 175 ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 OD2 ? B ASP 63  ? B ASP 62  ? 1_555 64.8  ? 
9  OD1 ? B ASP 63  ? B ASP 62  ? 1_555 ZN ? F ZN . ? A ZN 404 ? 1_555 OD2 ? B ASP 63  ? B ASP 62  ? 1_555 1.7   ? 
10 ND1 ? A HIS 90  ? A HIS 89  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 OD2 ? A ASP 109 ? A ASP 108 ? 1_555 114.2 ? 
11 ND1 ? A HIS 90  ? A HIS 89  ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 SG  ? B CYS 271 ? B CYS 270 ? 1_555 98.9  ? 
12 OD2 ? A ASP 109 ? A ASP 108 ? 1_555 ZN ? E ZN . ? A ZN 403 ? 1_555 SG  ? B CYS 271 ? B CYS 270 ? 1_555 98.9  ? 
13 SG  ? A CYS 190 ? A CYS 189 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 SG  ? A CYS 193 ? A CYS 192 ? 1_555 93.3  ? 
14 SG  ? A CYS 190 ? A CYS 189 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 SG  ? A CYS 225 ? A CYS 224 ? 1_555 98.1  ? 
15 SG  ? A CYS 193 ? A CYS 192 ? 1_555 ZN ? C ZN . ? A ZN 401 ? 1_555 SG  ? A CYS 225 ? A CYS 224 ? 1_555 91.5  ? 
16 SG  ? A CYS 271 ? A CYS 270 ? 1_555 ZN ? J ZN . ? B ZN 403 ? 1_555 ND1 ? B HIS 90  ? B HIS 89  ? 1_555 101.5 ? 
17 SG  ? A CYS 271 ? A CYS 270 ? 1_555 ZN ? J ZN . ? B ZN 403 ? 1_555 OD2 ? B ASP 109 ? B ASP 108 ? 1_555 102.3 ? 
18 ND1 ? B HIS 90  ? B HIS 89  ? 1_555 ZN ? J ZN . ? B ZN 403 ? 1_555 OD2 ? B ASP 109 ? B ASP 108 ? 1_555 95.8  ? 
19 OG  ? B SER 112 ? B SER 111 ? 1_555 ZN ? I ZN . ? B ZN 402 ? 1_555 ND1 ? B HIS 273 ? B HIS 272 ? 1_555 100.6 ? 
20 SG  ? B CYS 190 ? B CYS 189 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 193 ? B CYS 192 ? 1_555 106.7 ? 
21 SG  ? B CYS 190 ? B CYS 189 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 225 ? B CYS 224 ? 1_555 94.2  ? 
22 SG  ? B CYS 193 ? B CYS 192 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 225 ? B CYS 224 ? 1_555 102.6 ? 
23 SG  ? B CYS 190 ? B CYS 189 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 227 ? B CYS 226 ? 1_555 97.2  ? 
24 SG  ? B CYS 193 ? B CYS 192 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 227 ? B CYS 226 ? 1_555 141.5 ? 
25 SG  ? B CYS 225 ? B CYS 224 ? 1_555 ZN ? H ZN . ? B ZN 401 ? 1_555 SG  ? B CYS 227 ? B CYS 226 ? 1_555 105.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 2 ? 
AA7 ? 4 ? 
AA8 ? 4 ? 
AA9 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? 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 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AA9 5 6 ? anti-parallel 
AA9 6 7 ? 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 HIS A 18  ? ASP A 23  ? HIS A 17  ASP A 22  
AA1 2 THR A 5   ? THR A 11  ? THR A 4   THR A 10  
AA1 3 THR A 55  ? VAL A 58  ? THR A 54  VAL A 57  
AA1 4 THR A 35  ? LEU A 37  ? THR A 34  LEU A 36  
AA1 5 ALA A 40  ? ASP A 41  ? ALA A 39  ASP A 40  
AA2 1 GLY A 194 ? LYS A 201 ? GLY A 193 LYS A 200 
AA2 2 LYS A 183 ? CYS A 190 ? LYS A 182 CYS A 189 
AA2 3 GLN A 230 ? GLU A 239 ? GLN A 229 GLU A 238 
AA2 4 VAL A 221 ? PRO A 224 ? VAL A 220 PRO A 223 
AA3 1 GLY A 194 ? LYS A 201 ? GLY A 193 LYS A 200 
AA3 2 LYS A 183 ? CYS A 190 ? LYS A 182 CYS A 189 
AA3 3 GLN A 230 ? GLU A 239 ? GLN A 229 GLU A 238 
AA3 4 SER A 310 ? THR A 312 ? SER A 309 THR A 311 
AA4 1 MET A 207 ? MET A 209 ? MET A 206 MET A 208 
AA4 2 PHE A 242 ? LEU A 254 ? PHE A 241 LEU A 253 
AA4 3 TYR A 297 ? LYS A 307 ? TYR A 296 LYS A 306 
AA4 4 CYS A 261 ? THR A 266 ? CYS A 260 THR A 265 
AA4 5 HIS A 273 ? SER A 279 ? HIS A 272 SER A 278 
AA4 6 LEU A 283 ? ASP A 287 ? LEU A 282 ASP A 286 
AA4 7 LEU A 290 ? SER A 294 ? LEU A 289 SER A 293 
AA5 1 HIS B 18  ? THR B 19  ? HIS B 17  THR B 18  
AA5 2 PHE B 9   ? THR B 11  ? PHE B 8   THR B 10  
AA5 3 THR B 55  ? VAL B 58  ? THR B 54  VAL B 57  
AA5 4 THR B 35  ? LEU B 37  ? THR B 34  LEU B 36  
AA5 5 ALA B 40  ? ASP B 41  ? ALA B 39  ASP B 40  
AA6 1 GLN B 98  ? VAL B 99  ? GLN B 97  VAL B 98  
AA6 2 LEU B 102 ? THR B 103 ? LEU B 101 THR B 102 
AA7 1 GLY B 194 ? LYS B 201 ? GLY B 193 LYS B 200 
AA7 2 LYS B 183 ? CYS B 190 ? LYS B 182 CYS B 189 
AA7 3 GLN B 230 ? GLU B 239 ? GLN B 229 GLU B 238 
AA7 4 VAL B 221 ? PRO B 224 ? VAL B 220 PRO B 223 
AA8 1 GLY B 194 ? LYS B 201 ? GLY B 193 LYS B 200 
AA8 2 LYS B 183 ? CYS B 190 ? LYS B 182 CYS B 189 
AA8 3 GLN B 230 ? GLU B 239 ? GLN B 229 GLU B 238 
AA8 4 TYR B 311 ? THR B 312 ? TYR B 310 THR B 311 
AA9 1 MET B 207 ? MET B 209 ? MET B 206 MET B 208 
AA9 2 PHE B 242 ? LEU B 254 ? PHE B 241 LEU B 253 
AA9 3 TYR B 297 ? LYS B 307 ? TYR B 296 LYS B 306 
AA9 4 CYS B 261 ? THR B 266 ? CYS B 260 THR B 265 
AA9 5 HIS B 273 ? SER B 279 ? HIS B 272 SER B 278 
AA9 6 LEU B 283 ? ASP B 287 ? LEU B 282 ASP B 286 
AA9 7 LEU B 290 ? SER B 294 ? LEU B 289 SER B 293 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O HIS A 18  ? O HIS A 17  N THR A 10  ? N THR A 9   
AA1 2 3 N PHE A 9   ? N PHE A 8   O PHE A 56  ? O PHE A 55  
AA1 3 4 O TYR A 57  ? O TYR A 56  N TYR A 36  ? N TYR A 35  
AA1 4 5 N LEU A 37  ? N LEU A 36  O ALA A 40  ? O ALA A 39  
AA2 1 2 O GLY A 194 ? O GLY A 193 N CYS A 190 ? N CYS A 189 
AA2 2 3 N LYS A 183 ? N LYS A 182 O GLU A 239 ? O GLU A 238 
AA2 3 4 O LYS A 233 ? O LYS A 232 N VAL A 221 ? N VAL A 220 
AA3 1 2 O GLY A 194 ? O GLY A 193 N CYS A 190 ? N CYS A 189 
AA3 2 3 N LYS A 183 ? N LYS A 182 O GLU A 239 ? O GLU A 238 
AA3 3 4 N GLN A 238 ? N GLN A 237 O TYR A 311 ? O TYR A 310 
AA4 1 2 N TYR A 208 ? N TYR A 207 O SER A 246 ? O SER A 245 
AA4 2 3 N MET A 245 ? N MET A 244 O VAL A 304 ? O VAL A 303 
AA4 3 4 O PHE A 305 ? O PHE A 304 N CYS A 261 ? N CYS A 260 
AA4 4 5 N GLU A 264 ? N GLU A 263 O LYS A 275 ? O LYS A 274 
AA4 5 6 N HIS A 276 ? N HIS A 275 O ILE A 286 ? O ILE A 285 
AA4 6 7 N ASP A 287 ? N ASP A 286 O LEU A 290 ? O LEU A 289 
AA5 1 2 O HIS B 18  ? O HIS B 17  N THR B 10  ? N THR B 9   
AA5 2 3 N THR B 11  ? N THR B 10  O VAL B 58  ? O VAL B 57  
AA5 3 4 O TYR B 57  ? O TYR B 56  N TYR B 36  ? N TYR B 35  
AA5 4 5 N LEU B 37  ? N LEU B 36  O ALA B 40  ? O ALA B 39  
AA6 1 2 N VAL B 99  ? N VAL B 98  O LEU B 102 ? O LEU B 101 
AA7 1 2 O THR B 198 ? O THR B 197 N LEU B 186 ? N LEU B 185 
AA7 2 3 N VAL B 185 ? N VAL B 184 O VAL B 236 ? O VAL B 235 
AA7 3 4 O LYS B 233 ? O LYS B 232 N VAL B 221 ? N VAL B 220 
AA8 1 2 O THR B 198 ? O THR B 197 N LEU B 186 ? N LEU B 185 
AA8 2 3 N VAL B 185 ? N VAL B 184 O VAL B 236 ? O VAL B 235 
AA8 3 4 N GLN B 238 ? N GLN B 237 O TYR B 311 ? O TYR B 310 
AA9 1 2 N TYR B 208 ? N TYR B 207 O SER B 246 ? O SER B 245 
AA9 2 3 N MET B 245 ? N MET B 244 O VAL B 304 ? O VAL B 303 
AA9 3 4 O PHE B 305 ? O PHE B 304 N CYS B 261 ? N CYS B 260 
AA9 4 5 N GLU B 264 ? N GLU B 263 O LYS B 275 ? O LYS B 274 
AA9 5 6 N HIS B 276 ? N HIS B 275 O ILE B 286 ? O ILE B 285 
AA9 6 7 N ASP B 287 ? N ASP B 286 O LEU B 290 ? O LEU B 289 
# 
_pdbx_entry_details.entry_id                   8ZSE 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 14  ? ? -137.25 -41.40  
2  1 ASP A 40  ? ? -68.00  88.47   
3  1 PRO A 59  ? ? -69.52  84.37   
4  1 ASP A 108 ? ? 20.74   58.77   
5  1 VAL A 159 ? ? -39.08  136.52  
6  1 THR A 191 ? ? -89.26  -70.11  
7  1 HIS A 255 ? ? -31.29  115.21  
8  1 TYR A 268 ? ? -33.65  120.00  
9  1 LYS A 279 ? ? -114.54 -131.27 
10 1 ASN A 308 ? ? -127.94 -56.55  
11 1 ILE B 14  ? ? -137.96 -43.00  
12 1 MET B 23  ? ? 65.54   -1.11   
13 1 ASN B 109 ? ? 72.79   30.97   
14 1 GLU B 143 ? ? -107.87 71.02   
15 1 THR B 191 ? ? -97.60  -86.84  
16 1 CYS B 226 ? ? -66.72  6.69    
17 1 GLU B 238 ? ? -153.94 84.31   
18 1 GLN B 269 ? ? 74.20   -6.11   
19 1 LYS B 279 ? ? -127.44 -116.13 
20 1 SER B 293 ? ? -175.99 132.24  
21 1 ASN B 308 ? ? -131.11 -63.21  
22 1 SER B 309 ? ? -176.49 129.52  
# 
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 0 ? A GLY 1 
2 1 Y 1 B GLY 0 ? B GLY 1 
3 1 Y 1 B GLU 1 ? B GLU 2 
4 1 Y 1 B VAL 2 ? B VAL 3 
5 1 Y 1 B ARG 3 ? B ARG 4 
6 1 Y 1 B THR 4 ? B THR 5 
7 1 Y 1 B ILE 5 ? B ILE 6 
8 1 Y 1 B LYS 6 ? B LYS 7 
# 
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 
A1L2A C16  C  Y N 1   
A1L2A C17  C  Y N 2   
A1L2A C22  C  N N 3   
A1L2A C21  C  N N 4   
A1L2A N23  N  N N 5   
A1L2A C26  C  N N 6   
A1L2A C19  C  Y N 7   
A1L2A C18  C  Y N 8   
A1L2A C13  C  Y N 9   
A1L2A C11  C  Y N 10  
A1L2A C12  C  Y N 11  
A1L2A C14  C  Y N 12  
A1L2A C02  C  N N 13  
A1L2A C04  C  N N 14  
A1L2A C05  C  N N 15  
A1L2A C06  C  N N 16  
A1L2A C07  C  Y N 17  
A1L2A C08  C  Y N 18  
A1L2A C09  C  Y N 19  
A1L2A C15  C  Y N 20  
A1L2A C24  C  N N 21  
A1L2A C25  C  N N 22  
A1L2A C27  C  Y N 23  
A1L2A C28  C  Y N 24  
A1L2A C29  C  Y N 25  
A1L2A C30  C  N N 26  
A1L2A N03  N  N N 27  
A1L2A N10  N  Y N 28  
A1L2A N20  N  N N 29  
A1L2A O01  O  N N 30  
A1L2A H1   H  N N 31  
A1L2A H2   H  N N 32  
A1L2A H3   H  N N 33  
A1L2A H4   H  N N 34  
A1L2A H5   H  N N 35  
A1L2A H7   H  N N 36  
A1L2A H8   H  N N 37  
A1L2A H9   H  N N 38  
A1L2A H10  H  N N 39  
A1L2A H11  H  N N 40  
A1L2A H12  H  N N 41  
A1L2A H13  H  N N 42  
A1L2A H14  H  N N 43  
A1L2A H15  H  N N 44  
A1L2A H16  H  N N 45  
A1L2A H17  H  N N 46  
A1L2A H18  H  N N 47  
A1L2A H19  H  N N 48  
A1L2A H20  H  N N 49  
A1L2A H21  H  N N 50  
A1L2A H22  H  N N 51  
A1L2A H23  H  N N 52  
A1L2A H24  H  N N 53  
A1L2A H25  H  N N 54  
A1L2A H26  H  N N 55  
A1L2A H27  H  N N 56  
A1L2A H28  H  N N 57  
A1L2A H29  H  N N 58  
ALA   N    N  N N 59  
ALA   CA   C  N S 60  
ALA   C    C  N N 61  
ALA   O    O  N N 62  
ALA   CB   C  N N 63  
ALA   OXT  O  N N 64  
ALA   H    H  N N 65  
ALA   H2   H  N N 66  
ALA   HA   H  N N 67  
ALA   HB1  H  N N 68  
ALA   HB2  H  N N 69  
ALA   HB3  H  N N 70  
ALA   HXT  H  N N 71  
ARG   N    N  N N 72  
ARG   CA   C  N S 73  
ARG   C    C  N N 74  
ARG   O    O  N N 75  
ARG   CB   C  N N 76  
ARG   CG   C  N N 77  
ARG   CD   C  N N 78  
ARG   NE   N  N N 79  
ARG   CZ   C  N N 80  
ARG   NH1  N  N N 81  
ARG   NH2  N  N N 82  
ARG   OXT  O  N N 83  
ARG   H    H  N N 84  
ARG   H2   H  N N 85  
ARG   HA   H  N N 86  
ARG   HB2  H  N N 87  
ARG   HB3  H  N N 88  
ARG   HG2  H  N N 89  
ARG   HG3  H  N N 90  
ARG   HD2  H  N N 91  
ARG   HD3  H  N N 92  
ARG   HE   H  N N 93  
ARG   HH11 H  N N 94  
ARG   HH12 H  N N 95  
ARG   HH21 H  N N 96  
ARG   HH22 H  N N 97  
ARG   HXT  H  N N 98  
ASN   N    N  N N 99  
ASN   CA   C  N S 100 
ASN   C    C  N N 101 
ASN   O    O  N N 102 
ASN   CB   C  N N 103 
ASN   CG   C  N N 104 
ASN   OD1  O  N N 105 
ASN   ND2  N  N N 106 
ASN   OXT  O  N N 107 
ASN   H    H  N N 108 
ASN   H2   H  N N 109 
ASN   HA   H  N N 110 
ASN   HB2  H  N N 111 
ASN   HB3  H  N N 112 
ASN   HD21 H  N N 113 
ASN   HD22 H  N N 114 
ASN   HXT  H  N N 115 
ASP   N    N  N N 116 
ASP   CA   C  N S 117 
ASP   C    C  N N 118 
ASP   O    O  N N 119 
ASP   CB   C  N N 120 
ASP   CG   C  N N 121 
ASP   OD1  O  N N 122 
ASP   OD2  O  N N 123 
ASP   OXT  O  N N 124 
ASP   H    H  N N 125 
ASP   H2   H  N N 126 
ASP   HA   H  N N 127 
ASP   HB2  H  N N 128 
ASP   HB3  H  N N 129 
ASP   HD2  H  N N 130 
ASP   HXT  H  N N 131 
CYS   N    N  N N 132 
CYS   CA   C  N R 133 
CYS   C    C  N N 134 
CYS   O    O  N N 135 
CYS   CB   C  N N 136 
CYS   SG   S  N N 137 
CYS   OXT  O  N N 138 
CYS   H    H  N N 139 
CYS   H2   H  N N 140 
CYS   HA   H  N N 141 
CYS   HB2  H  N N 142 
CYS   HB3  H  N N 143 
CYS   HG   H  N N 144 
CYS   HXT  H  N N 145 
GLN   N    N  N N 146 
GLN   CA   C  N S 147 
GLN   C    C  N N 148 
GLN   O    O  N N 149 
GLN   CB   C  N N 150 
GLN   CG   C  N N 151 
GLN   CD   C  N N 152 
GLN   OE1  O  N N 153 
GLN   NE2  N  N N 154 
GLN   OXT  O  N N 155 
GLN   H    H  N N 156 
GLN   H2   H  N N 157 
GLN   HA   H  N N 158 
GLN   HB2  H  N N 159 
GLN   HB3  H  N N 160 
GLN   HG2  H  N N 161 
GLN   HG3  H  N N 162 
GLN   HE21 H  N N 163 
GLN   HE22 H  N N 164 
GLN   HXT  H  N N 165 
GLU   N    N  N N 166 
GLU   CA   C  N S 167 
GLU   C    C  N N 168 
GLU   O    O  N N 169 
GLU   CB   C  N N 170 
GLU   CG   C  N N 171 
GLU   CD   C  N N 172 
GLU   OE1  O  N N 173 
GLU   OE2  O  N N 174 
GLU   OXT  O  N N 175 
GLU   H    H  N N 176 
GLU   H2   H  N N 177 
GLU   HA   H  N N 178 
GLU   HB2  H  N N 179 
GLU   HB3  H  N N 180 
GLU   HG2  H  N N 181 
GLU   HG3  H  N N 182 
GLU   HE2  H  N N 183 
GLU   HXT  H  N N 184 
GLY   N    N  N N 185 
GLY   CA   C  N N 186 
GLY   C    C  N N 187 
GLY   O    O  N N 188 
GLY   OXT  O  N N 189 
GLY   H    H  N N 190 
GLY   H2   H  N N 191 
GLY   HA2  H  N N 192 
GLY   HA3  H  N N 193 
GLY   HXT  H  N N 194 
HIS   N    N  N N 195 
HIS   CA   C  N S 196 
HIS   C    C  N N 197 
HIS   O    O  N N 198 
HIS   CB   C  N N 199 
HIS   CG   C  Y N 200 
HIS   ND1  N  Y N 201 
HIS   CD2  C  Y N 202 
HIS   CE1  C  Y N 203 
HIS   NE2  N  Y N 204 
HIS   OXT  O  N N 205 
HIS   H    H  N N 206 
HIS   H2   H  N N 207 
HIS   HA   H  N N 208 
HIS   HB2  H  N N 209 
HIS   HB3  H  N N 210 
HIS   HD1  H  N N 211 
HIS   HD2  H  N N 212 
HIS   HE1  H  N N 213 
HIS   HE2  H  N N 214 
HIS   HXT  H  N N 215 
HOH   O    O  N N 216 
HOH   H1   H  N N 217 
HOH   H2   H  N N 218 
ILE   N    N  N N 219 
ILE   CA   C  N S 220 
ILE   C    C  N N 221 
ILE   O    O  N N 222 
ILE   CB   C  N S 223 
ILE   CG1  C  N N 224 
ILE   CG2  C  N N 225 
ILE   CD1  C  N N 226 
ILE   OXT  O  N N 227 
ILE   H    H  N N 228 
ILE   H2   H  N N 229 
ILE   HA   H  N N 230 
ILE   HB   H  N N 231 
ILE   HG12 H  N N 232 
ILE   HG13 H  N N 233 
ILE   HG21 H  N N 234 
ILE   HG22 H  N N 235 
ILE   HG23 H  N N 236 
ILE   HD11 H  N N 237 
ILE   HD12 H  N N 238 
ILE   HD13 H  N N 239 
ILE   HXT  H  N N 240 
LEU   N    N  N N 241 
LEU   CA   C  N S 242 
LEU   C    C  N N 243 
LEU   O    O  N N 244 
LEU   CB   C  N N 245 
LEU   CG   C  N N 246 
LEU   CD1  C  N N 247 
LEU   CD2  C  N N 248 
LEU   OXT  O  N N 249 
LEU   H    H  N N 250 
LEU   H2   H  N N 251 
LEU   HA   H  N N 252 
LEU   HB2  H  N N 253 
LEU   HB3  H  N N 254 
LEU   HG   H  N N 255 
LEU   HD11 H  N N 256 
LEU   HD12 H  N N 257 
LEU   HD13 H  N N 258 
LEU   HD21 H  N N 259 
LEU   HD22 H  N N 260 
LEU   HD23 H  N N 261 
LEU   HXT  H  N N 262 
LYS   N    N  N N 263 
LYS   CA   C  N S 264 
LYS   C    C  N N 265 
LYS   O    O  N N 266 
LYS   CB   C  N N 267 
LYS   CG   C  N N 268 
LYS   CD   C  N N 269 
LYS   CE   C  N N 270 
LYS   NZ   N  N N 271 
LYS   OXT  O  N N 272 
LYS   H    H  N N 273 
LYS   H2   H  N N 274 
LYS   HA   H  N N 275 
LYS   HB2  H  N N 276 
LYS   HB3  H  N N 277 
LYS   HG2  H  N N 278 
LYS   HG3  H  N N 279 
LYS   HD2  H  N N 280 
LYS   HD3  H  N N 281 
LYS   HE2  H  N N 282 
LYS   HE3  H  N N 283 
LYS   HZ1  H  N N 284 
LYS   HZ2  H  N N 285 
LYS   HZ3  H  N N 286 
LYS   HXT  H  N N 287 
MET   N    N  N N 288 
MET   CA   C  N S 289 
MET   C    C  N N 290 
MET   O    O  N N 291 
MET   CB   C  N N 292 
MET   CG   C  N N 293 
MET   SD   S  N N 294 
MET   CE   C  N N 295 
MET   OXT  O  N N 296 
MET   H    H  N N 297 
MET   H2   H  N N 298 
MET   HA   H  N N 299 
MET   HB2  H  N N 300 
MET   HB3  H  N N 301 
MET   HG2  H  N N 302 
MET   HG3  H  N N 303 
MET   HE1  H  N N 304 
MET   HE2  H  N N 305 
MET   HE3  H  N N 306 
MET   HXT  H  N N 307 
PHE   N    N  N N 308 
PHE   CA   C  N S 309 
PHE   C    C  N N 310 
PHE   O    O  N N 311 
PHE   CB   C  N N 312 
PHE   CG   C  Y N 313 
PHE   CD1  C  Y N 314 
PHE   CD2  C  Y N 315 
PHE   CE1  C  Y N 316 
PHE   CE2  C  Y N 317 
PHE   CZ   C  Y N 318 
PHE   OXT  O  N N 319 
PHE   H    H  N N 320 
PHE   H2   H  N N 321 
PHE   HA   H  N N 322 
PHE   HB2  H  N N 323 
PHE   HB3  H  N N 324 
PHE   HD1  H  N N 325 
PHE   HD2  H  N N 326 
PHE   HE1  H  N N 327 
PHE   HE2  H  N N 328 
PHE   HZ   H  N N 329 
PHE   HXT  H  N N 330 
PRO   N    N  N N 331 
PRO   CA   C  N S 332 
PRO   C    C  N N 333 
PRO   O    O  N N 334 
PRO   CB   C  N N 335 
PRO   CG   C  N N 336 
PRO   CD   C  N N 337 
PRO   OXT  O  N N 338 
PRO   H    H  N N 339 
PRO   HA   H  N N 340 
PRO   HB2  H  N N 341 
PRO   HB3  H  N N 342 
PRO   HG2  H  N N 343 
PRO   HG3  H  N N 344 
PRO   HD2  H  N N 345 
PRO   HD3  H  N N 346 
PRO   HXT  H  N N 347 
SER   N    N  N N 348 
SER   CA   C  N S 349 
SER   C    C  N N 350 
SER   O    O  N N 351 
SER   CB   C  N N 352 
SER   OG   O  N N 353 
SER   OXT  O  N N 354 
SER   H    H  N N 355 
SER   H2   H  N N 356 
SER   HA   H  N N 357 
SER   HB2  H  N N 358 
SER   HB3  H  N N 359 
SER   HG   H  N N 360 
SER   HXT  H  N N 361 
THR   N    N  N N 362 
THR   CA   C  N S 363 
THR   C    C  N N 364 
THR   O    O  N N 365 
THR   CB   C  N R 366 
THR   OG1  O  N N 367 
THR   CG2  C  N N 368 
THR   OXT  O  N N 369 
THR   H    H  N N 370 
THR   H2   H  N N 371 
THR   HA   H  N N 372 
THR   HB   H  N N 373 
THR   HG1  H  N N 374 
THR   HG21 H  N N 375 
THR   HG22 H  N N 376 
THR   HG23 H  N N 377 
THR   HXT  H  N N 378 
TRP   N    N  N N 379 
TRP   CA   C  N S 380 
TRP   C    C  N N 381 
TRP   O    O  N N 382 
TRP   CB   C  N N 383 
TRP   CG   C  Y N 384 
TRP   CD1  C  Y N 385 
TRP   CD2  C  Y N 386 
TRP   NE1  N  Y N 387 
TRP   CE2  C  Y N 388 
TRP   CE3  C  Y N 389 
TRP   CZ2  C  Y N 390 
TRP   CZ3  C  Y N 391 
TRP   CH2  C  Y N 392 
TRP   OXT  O  N N 393 
TRP   H    H  N N 394 
TRP   H2   H  N N 395 
TRP   HA   H  N N 396 
TRP   HB2  H  N N 397 
TRP   HB3  H  N N 398 
TRP   HD1  H  N N 399 
TRP   HE1  H  N N 400 
TRP   HE3  H  N N 401 
TRP   HZ2  H  N N 402 
TRP   HZ3  H  N N 403 
TRP   HH2  H  N N 404 
TRP   HXT  H  N N 405 
TYR   N    N  N N 406 
TYR   CA   C  N S 407 
TYR   C    C  N N 408 
TYR   O    O  N N 409 
TYR   CB   C  N N 410 
TYR   CG   C  Y N 411 
TYR   CD1  C  Y N 412 
TYR   CD2  C  Y N 413 
TYR   CE1  C  Y N 414 
TYR   CE2  C  Y N 415 
TYR   CZ   C  Y N 416 
TYR   OH   O  N N 417 
TYR   OXT  O  N N 418 
TYR   H    H  N N 419 
TYR   H2   H  N N 420 
TYR   HA   H  N N 421 
TYR   HB2  H  N N 422 
TYR   HB3  H  N N 423 
TYR   HD1  H  N N 424 
TYR   HD2  H  N N 425 
TYR   HE1  H  N N 426 
TYR   HE2  H  N N 427 
TYR   HH   H  N N 428 
TYR   HXT  H  N N 429 
VAL   N    N  N N 430 
VAL   CA   C  N S 431 
VAL   C    C  N N 432 
VAL   O    O  N N 433 
VAL   CB   C  N N 434 
VAL   CG1  C  N N 435 
VAL   CG2  C  N N 436 
VAL   OXT  O  N N 437 
VAL   H    H  N N 438 
VAL   H2   H  N N 439 
VAL   HA   H  N N 440 
VAL   HB   H  N N 441 
VAL   HG11 H  N N 442 
VAL   HG12 H  N N 443 
VAL   HG13 H  N N 444 
VAL   HG21 H  N N 445 
VAL   HG22 H  N N 446 
VAL   HG23 H  N N 447 
VAL   HXT  H  N N 448 
ZN    ZN   ZN N N 449 
# 
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 
A1L2A C05 C06  sing N N 1   
A1L2A C05 C04  sing N N 2   
A1L2A C06 C04  sing N N 3   
A1L2A C04 N03  sing N N 4   
A1L2A C04 C07  sing N N 5   
A1L2A N03 C02  sing N N 6   
A1L2A C22 C21  sing N N 7   
A1L2A C22 N23  sing N N 8   
A1L2A C28 C27  doub Y N 9   
A1L2A C28 C29  sing Y N 10  
A1L2A C27 C19  sing Y N 11  
A1L2A C24 N23  sing N N 12  
A1L2A C30 C29  sing N N 13  
A1L2A C29 C17  doub Y N 14  
A1L2A C21 N20  sing N N 15  
A1L2A C13 C14  doub Y N 16  
A1L2A C13 C12  sing Y N 17  
A1L2A C19 N20  sing N N 18  
A1L2A C19 C18  doub Y N 19  
A1L2A N20 C26  sing N N 20  
A1L2A C17 C18  sing Y N 21  
A1L2A C17 C02  sing N N 22  
A1L2A C02 O01  doub N N 23  
A1L2A C14 C15  sing Y N 24  
A1L2A N23 C25  sing N N 25  
A1L2A C25 C26  sing N N 26  
A1L2A C07 C12  doub Y N 27  
A1L2A C07 C08  sing Y N 28  
A1L2A C12 C11  sing Y N 29  
A1L2A C08 C09  doub Y N 30  
A1L2A C15 C16  doub Y N 31  
A1L2A C11 C16  sing Y N 32  
A1L2A C11 N10  doub Y N 33  
A1L2A C09 N10  sing Y N 34  
A1L2A C16 H1   sing N N 35  
A1L2A C22 H2   sing N N 36  
A1L2A C22 H3   sing N N 37  
A1L2A C21 H4   sing N N 38  
A1L2A C21 H5   sing N N 39  
A1L2A C26 H7   sing N N 40  
A1L2A C26 H8   sing N N 41  
A1L2A C18 H9   sing N N 42  
A1L2A C13 H10  sing N N 43  
A1L2A C14 H11  sing N N 44  
A1L2A C05 H12  sing N N 45  
A1L2A C05 H13  sing N N 46  
A1L2A C06 H14  sing N N 47  
A1L2A C06 H15  sing N N 48  
A1L2A C08 H16  sing N N 49  
A1L2A C09 H17  sing N N 50  
A1L2A C15 H18  sing N N 51  
A1L2A C24 H19  sing N N 52  
A1L2A C24 H20  sing N N 53  
A1L2A C24 H21  sing N N 54  
A1L2A C25 H22  sing N N 55  
A1L2A C25 H23  sing N N 56  
A1L2A C27 H24  sing N N 57  
A1L2A C28 H25  sing N N 58  
A1L2A C30 H26  sing N N 59  
A1L2A C30 H27  sing N N 60  
A1L2A C30 H28  sing N N 61  
A1L2A N03 H29  sing N N 62  
ALA   N   CA   sing N N 63  
ALA   N   H    sing N N 64  
ALA   N   H2   sing N N 65  
ALA   CA  C    sing N N 66  
ALA   CA  CB   sing N N 67  
ALA   CA  HA   sing N N 68  
ALA   C   O    doub N N 69  
ALA   C   OXT  sing N N 70  
ALA   CB  HB1  sing N N 71  
ALA   CB  HB2  sing N N 72  
ALA   CB  HB3  sing N N 73  
ALA   OXT HXT  sing N N 74  
ARG   N   CA   sing N N 75  
ARG   N   H    sing N N 76  
ARG   N   H2   sing N N 77  
ARG   CA  C    sing N N 78  
ARG   CA  CB   sing N N 79  
ARG   CA  HA   sing N N 80  
ARG   C   O    doub N N 81  
ARG   C   OXT  sing N N 82  
ARG   CB  CG   sing N N 83  
ARG   CB  HB2  sing N N 84  
ARG   CB  HB3  sing N N 85  
ARG   CG  CD   sing N N 86  
ARG   CG  HG2  sing N N 87  
ARG   CG  HG3  sing N N 88  
ARG   CD  NE   sing N N 89  
ARG   CD  HD2  sing N N 90  
ARG   CD  HD3  sing N N 91  
ARG   NE  CZ   sing N N 92  
ARG   NE  HE   sing N N 93  
ARG   CZ  NH1  sing N N 94  
ARG   CZ  NH2  doub N N 95  
ARG   NH1 HH11 sing N N 96  
ARG   NH1 HH12 sing N N 97  
ARG   NH2 HH21 sing N N 98  
ARG   NH2 HH22 sing N N 99  
ARG   OXT HXT  sing N N 100 
ASN   N   CA   sing N N 101 
ASN   N   H    sing N N 102 
ASN   N   H2   sing N N 103 
ASN   CA  C    sing N N 104 
ASN   CA  CB   sing N N 105 
ASN   CA  HA   sing N N 106 
ASN   C   O    doub N N 107 
ASN   C   OXT  sing N N 108 
ASN   CB  CG   sing N N 109 
ASN   CB  HB2  sing N N 110 
ASN   CB  HB3  sing N N 111 
ASN   CG  OD1  doub N N 112 
ASN   CG  ND2  sing N N 113 
ASN   ND2 HD21 sing N N 114 
ASN   ND2 HD22 sing N N 115 
ASN   OXT HXT  sing N N 116 
ASP   N   CA   sing N N 117 
ASP   N   H    sing N N 118 
ASP   N   H2   sing N N 119 
ASP   CA  C    sing N N 120 
ASP   CA  CB   sing N N 121 
ASP   CA  HA   sing N N 122 
ASP   C   O    doub N N 123 
ASP   C   OXT  sing N N 124 
ASP   CB  CG   sing N N 125 
ASP   CB  HB2  sing N N 126 
ASP   CB  HB3  sing N N 127 
ASP   CG  OD1  doub N N 128 
ASP   CG  OD2  sing N N 129 
ASP   OD2 HD2  sing N N 130 
ASP   OXT HXT  sing N N 131 
CYS   N   CA   sing N N 132 
CYS   N   H    sing N N 133 
CYS   N   H2   sing N N 134 
CYS   CA  C    sing N N 135 
CYS   CA  CB   sing N N 136 
CYS   CA  HA   sing N N 137 
CYS   C   O    doub N N 138 
CYS   C   OXT  sing N N 139 
CYS   CB  SG   sing N N 140 
CYS   CB  HB2  sing N N 141 
CYS   CB  HB3  sing N N 142 
CYS   SG  HG   sing N N 143 
CYS   OXT HXT  sing N N 144 
GLN   N   CA   sing N N 145 
GLN   N   H    sing N N 146 
GLN   N   H2   sing N N 147 
GLN   CA  C    sing N N 148 
GLN   CA  CB   sing N N 149 
GLN   CA  HA   sing N N 150 
GLN   C   O    doub N N 151 
GLN   C   OXT  sing N N 152 
GLN   CB  CG   sing N N 153 
GLN   CB  HB2  sing N N 154 
GLN   CB  HB3  sing N N 155 
GLN   CG  CD   sing N N 156 
GLN   CG  HG2  sing N N 157 
GLN   CG  HG3  sing N N 158 
GLN   CD  OE1  doub N N 159 
GLN   CD  NE2  sing N N 160 
GLN   NE2 HE21 sing N N 161 
GLN   NE2 HE22 sing N N 162 
GLN   OXT HXT  sing N N 163 
GLU   N   CA   sing N N 164 
GLU   N   H    sing N N 165 
GLU   N   H2   sing N N 166 
GLU   CA  C    sing N N 167 
GLU   CA  CB   sing N N 168 
GLU   CA  HA   sing N N 169 
GLU   C   O    doub N N 170 
GLU   C   OXT  sing N N 171 
GLU   CB  CG   sing N N 172 
GLU   CB  HB2  sing N N 173 
GLU   CB  HB3  sing N N 174 
GLU   CG  CD   sing N N 175 
GLU   CG  HG2  sing N N 176 
GLU   CG  HG3  sing N N 177 
GLU   CD  OE1  doub N N 178 
GLU   CD  OE2  sing N N 179 
GLU   OE2 HE2  sing N N 180 
GLU   OXT HXT  sing N N 181 
GLY   N   CA   sing N N 182 
GLY   N   H    sing N N 183 
GLY   N   H2   sing N N 184 
GLY   CA  C    sing N N 185 
GLY   CA  HA2  sing N N 186 
GLY   CA  HA3  sing N N 187 
GLY   C   O    doub N N 188 
GLY   C   OXT  sing N N 189 
GLY   OXT HXT  sing N N 190 
HIS   N   CA   sing N N 191 
HIS   N   H    sing N N 192 
HIS   N   H2   sing N N 193 
HIS   CA  C    sing N N 194 
HIS   CA  CB   sing N N 195 
HIS   CA  HA   sing N N 196 
HIS   C   O    doub N N 197 
HIS   C   OXT  sing N N 198 
HIS   CB  CG   sing N N 199 
HIS   CB  HB2  sing N N 200 
HIS   CB  HB3  sing N N 201 
HIS   CG  ND1  sing Y N 202 
HIS   CG  CD2  doub Y N 203 
HIS   ND1 CE1  doub Y N 204 
HIS   ND1 HD1  sing N N 205 
HIS   CD2 NE2  sing Y N 206 
HIS   CD2 HD2  sing N N 207 
HIS   CE1 NE2  sing Y N 208 
HIS   CE1 HE1  sing N N 209 
HIS   NE2 HE2  sing N N 210 
HIS   OXT HXT  sing N N 211 
HOH   O   H1   sing N N 212 
HOH   O   H2   sing N N 213 
ILE   N   CA   sing N N 214 
ILE   N   H    sing N N 215 
ILE   N   H2   sing N N 216 
ILE   CA  C    sing N N 217 
ILE   CA  CB   sing N N 218 
ILE   CA  HA   sing N N 219 
ILE   C   O    doub N N 220 
ILE   C   OXT  sing N N 221 
ILE   CB  CG1  sing N N 222 
ILE   CB  CG2  sing N N 223 
ILE   CB  HB   sing N N 224 
ILE   CG1 CD1  sing N N 225 
ILE   CG1 HG12 sing N N 226 
ILE   CG1 HG13 sing N N 227 
ILE   CG2 HG21 sing N N 228 
ILE   CG2 HG22 sing N N 229 
ILE   CG2 HG23 sing N N 230 
ILE   CD1 HD11 sing N N 231 
ILE   CD1 HD12 sing N N 232 
ILE   CD1 HD13 sing N N 233 
ILE   OXT HXT  sing N N 234 
LEU   N   CA   sing N N 235 
LEU   N   H    sing N N 236 
LEU   N   H2   sing N N 237 
LEU   CA  C    sing N N 238 
LEU   CA  CB   sing N N 239 
LEU   CA  HA   sing N N 240 
LEU   C   O    doub N N 241 
LEU   C   OXT  sing N N 242 
LEU   CB  CG   sing N N 243 
LEU   CB  HB2  sing N N 244 
LEU   CB  HB3  sing N N 245 
LEU   CG  CD1  sing N N 246 
LEU   CG  CD2  sing N N 247 
LEU   CG  HG   sing N N 248 
LEU   CD1 HD11 sing N N 249 
LEU   CD1 HD12 sing N N 250 
LEU   CD1 HD13 sing N N 251 
LEU   CD2 HD21 sing N N 252 
LEU   CD2 HD22 sing N N 253 
LEU   CD2 HD23 sing N N 254 
LEU   OXT HXT  sing N N 255 
LYS   N   CA   sing N N 256 
LYS   N   H    sing N N 257 
LYS   N   H2   sing N N 258 
LYS   CA  C    sing N N 259 
LYS   CA  CB   sing N N 260 
LYS   CA  HA   sing N N 261 
LYS   C   O    doub N N 262 
LYS   C   OXT  sing N N 263 
LYS   CB  CG   sing N N 264 
LYS   CB  HB2  sing N N 265 
LYS   CB  HB3  sing N N 266 
LYS   CG  CD   sing N N 267 
LYS   CG  HG2  sing N N 268 
LYS   CG  HG3  sing N N 269 
LYS   CD  CE   sing N N 270 
LYS   CD  HD2  sing N N 271 
LYS   CD  HD3  sing N N 272 
LYS   CE  NZ   sing N N 273 
LYS   CE  HE2  sing N N 274 
LYS   CE  HE3  sing N N 275 
LYS   NZ  HZ1  sing N N 276 
LYS   NZ  HZ2  sing N N 277 
LYS   NZ  HZ3  sing N N 278 
LYS   OXT HXT  sing N N 279 
MET   N   CA   sing N N 280 
MET   N   H    sing N N 281 
MET   N   H2   sing N N 282 
MET   CA  C    sing N N 283 
MET   CA  CB   sing N N 284 
MET   CA  HA   sing N N 285 
MET   C   O    doub N N 286 
MET   C   OXT  sing N N 287 
MET   CB  CG   sing N N 288 
MET   CB  HB2  sing N N 289 
MET   CB  HB3  sing N N 290 
MET   CG  SD   sing N N 291 
MET   CG  HG2  sing N N 292 
MET   CG  HG3  sing N N 293 
MET   SD  CE   sing N N 294 
MET   CE  HE1  sing N N 295 
MET   CE  HE2  sing N N 296 
MET   CE  HE3  sing N N 297 
MET   OXT HXT  sing N N 298 
PHE   N   CA   sing N N 299 
PHE   N   H    sing N N 300 
PHE   N   H2   sing N N 301 
PHE   CA  C    sing N N 302 
PHE   CA  CB   sing N N 303 
PHE   CA  HA   sing N N 304 
PHE   C   O    doub N N 305 
PHE   C   OXT  sing N N 306 
PHE   CB  CG   sing N N 307 
PHE   CB  HB2  sing N N 308 
PHE   CB  HB3  sing N N 309 
PHE   CG  CD1  doub Y N 310 
PHE   CG  CD2  sing Y N 311 
PHE   CD1 CE1  sing Y N 312 
PHE   CD1 HD1  sing N N 313 
PHE   CD2 CE2  doub Y N 314 
PHE   CD2 HD2  sing N N 315 
PHE   CE1 CZ   doub Y N 316 
PHE   CE1 HE1  sing N N 317 
PHE   CE2 CZ   sing Y N 318 
PHE   CE2 HE2  sing N N 319 
PHE   CZ  HZ   sing N N 320 
PHE   OXT HXT  sing N N 321 
PRO   N   CA   sing N N 322 
PRO   N   CD   sing N N 323 
PRO   N   H    sing N N 324 
PRO   CA  C    sing N N 325 
PRO   CA  CB   sing N N 326 
PRO   CA  HA   sing N N 327 
PRO   C   O    doub N N 328 
PRO   C   OXT  sing N N 329 
PRO   CB  CG   sing N N 330 
PRO   CB  HB2  sing N N 331 
PRO   CB  HB3  sing N N 332 
PRO   CG  CD   sing N N 333 
PRO   CG  HG2  sing N N 334 
PRO   CG  HG3  sing N N 335 
PRO   CD  HD2  sing N N 336 
PRO   CD  HD3  sing N N 337 
PRO   OXT HXT  sing N N 338 
SER   N   CA   sing N N 339 
SER   N   H    sing N N 340 
SER   N   H2   sing N N 341 
SER   CA  C    sing N N 342 
SER   CA  CB   sing N N 343 
SER   CA  HA   sing N N 344 
SER   C   O    doub N N 345 
SER   C   OXT  sing N N 346 
SER   CB  OG   sing N N 347 
SER   CB  HB2  sing N N 348 
SER   CB  HB3  sing N N 349 
SER   OG  HG   sing N N 350 
SER   OXT HXT  sing N N 351 
THR   N   CA   sing N N 352 
THR   N   H    sing N N 353 
THR   N   H2   sing N N 354 
THR   CA  C    sing N N 355 
THR   CA  CB   sing N N 356 
THR   CA  HA   sing N N 357 
THR   C   O    doub N N 358 
THR   C   OXT  sing N N 359 
THR   CB  OG1  sing N N 360 
THR   CB  CG2  sing N N 361 
THR   CB  HB   sing N N 362 
THR   OG1 HG1  sing N N 363 
THR   CG2 HG21 sing N N 364 
THR   CG2 HG22 sing N N 365 
THR   CG2 HG23 sing N N 366 
THR   OXT HXT  sing N N 367 
TRP   N   CA   sing N N 368 
TRP   N   H    sing N N 369 
TRP   N   H2   sing N N 370 
TRP   CA  C    sing N N 371 
TRP   CA  CB   sing N N 372 
TRP   CA  HA   sing N N 373 
TRP   C   O    doub N N 374 
TRP   C   OXT  sing N N 375 
TRP   CB  CG   sing N N 376 
TRP   CB  HB2  sing N N 377 
TRP   CB  HB3  sing N N 378 
TRP   CG  CD1  doub Y N 379 
TRP   CG  CD2  sing Y N 380 
TRP   CD1 NE1  sing Y N 381 
TRP   CD1 HD1  sing N N 382 
TRP   CD2 CE2  doub Y N 383 
TRP   CD2 CE3  sing Y N 384 
TRP   NE1 CE2  sing Y N 385 
TRP   NE1 HE1  sing N N 386 
TRP   CE2 CZ2  sing Y N 387 
TRP   CE3 CZ3  doub Y N 388 
TRP   CE3 HE3  sing N N 389 
TRP   CZ2 CH2  doub Y N 390 
TRP   CZ2 HZ2  sing N N 391 
TRP   CZ3 CH2  sing Y N 392 
TRP   CZ3 HZ3  sing N N 393 
TRP   CH2 HH2  sing N N 394 
TRP   OXT HXT  sing N N 395 
TYR   N   CA   sing N N 396 
TYR   N   H    sing N N 397 
TYR   N   H2   sing N N 398 
TYR   CA  C    sing N N 399 
TYR   CA  CB   sing N N 400 
TYR   CA  HA   sing N N 401 
TYR   C   O    doub N N 402 
TYR   C   OXT  sing N N 403 
TYR   CB  CG   sing N N 404 
TYR   CB  HB2  sing N N 405 
TYR   CB  HB3  sing N N 406 
TYR   CG  CD1  doub Y N 407 
TYR   CG  CD2  sing Y N 408 
TYR   CD1 CE1  sing Y N 409 
TYR   CD1 HD1  sing N N 410 
TYR   CD2 CE2  doub Y N 411 
TYR   CD2 HD2  sing N N 412 
TYR   CE1 CZ   doub Y N 413 
TYR   CE1 HE1  sing N N 414 
TYR   CE2 CZ   sing Y N 415 
TYR   CE2 HE2  sing N N 416 
TYR   CZ  OH   sing N N 417 
TYR   OH  HH   sing N N 418 
TYR   OXT HXT  sing N N 419 
VAL   N   CA   sing N N 420 
VAL   N   H    sing N N 421 
VAL   N   H2   sing N N 422 
VAL   CA  C    sing N N 423 
VAL   CA  CB   sing N N 424 
VAL   CA  HA   sing N N 425 
VAL   C   O    doub N N 426 
VAL   C   OXT  sing N N 427 
VAL   CB  CG1  sing N N 428 
VAL   CB  CG2  sing N N 429 
VAL   CB  HB   sing N N 430 
VAL   CG1 HG11 sing N N 431 
VAL   CG1 HG12 sing N N 432 
VAL   CG1 HG13 sing N N 433 
VAL   CG2 HG21 sing N N 434 
VAL   CG2 HG22 sing N N 435 
VAL   CG2 HG23 sing N N 436 
VAL   OXT HXT  sing N N 437 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Ministry of Science and Technology (MoST, China)'    China GZNL2023401008 1 
'Ministry of Science and Technology (MoST, China)'    China SRPG22-002     2 
'Ministry of Science and Technology (MoST, China)'    China SRPG22-003     3 
'National Natural Science Foundation of China (NSFC)' China 82170473       4 
# 
_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   7CJM 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZSE 
_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]   0.010506 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010506 
_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]   0.004304 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . GLU   A 1 2   ? -11.158 5.575   56.153 1.00 66.92  ?  1   GLU   A N   1 
ATOM   2    C  CA  . GLU   A 1 2   ? -11.095 5.630   54.689 1.00 70.47  ?  1   GLU   A CA  1 
ATOM   3    C  C   . GLU   A 1 2   ? -10.275 4.457   54.095 1.00 73.57  ?  1   GLU   A C   1 
ATOM   4    O  O   . GLU   A 1 2   ? -10.206 4.325   52.871 1.00 72.86  ?  1   GLU   A O   1 
ATOM   5    C  CB  . GLU   A 1 2   ? -10.520 6.980   54.201 1.00 61.94  ?  1   GLU   A CB  1 
ATOM   6    C  CG  . GLU   A 1 2   ? -10.858 7.297   52.753 1.00 62.74  ?  1   GLU   A CG  1 
ATOM   7    C  CD  . GLU   A 1 2   ? -9.783  8.083   52.004 1.00 70.39  ?  1   GLU   A CD  1 
ATOM   8    O  OE1 . GLU   A 1 2   ? -10.032 9.271   51.741 1.00 73.36  ?  1   GLU   A OE1 1 
ATOM   9    O  OE2 . GLU   A 1 2   ? -8.703  7.537   51.669 1.00 66.11  ?  1   GLU   A OE2 1 
ATOM   10   N  N   . VAL   A 1 3   ? -9.667  3.611   54.938 1.00 70.72  ?  2   VAL   A N   1 
ATOM   11   C  CA  . VAL   A 1 3   ? -9.037  2.359   54.491 1.00 72.29  ?  2   VAL   A CA  1 
ATOM   12   C  C   . VAL   A 1 3   ? -9.185  1.319   55.598 1.00 74.46  ?  2   VAL   A C   1 
ATOM   13   O  O   . VAL   A 1 3   ? -8.807  1.568   56.749 1.00 69.96  ?  2   VAL   A O   1 
ATOM   14   C  CB  . VAL   A 1 3   ? -7.537  2.504   54.124 1.00 70.24  ?  2   VAL   A CB  1 
ATOM   15   C  CG1 . VAL   A 1 3   ? -6.904  1.137   53.969 1.00 69.65  ?  2   VAL   A CG1 1 
ATOM   16   C  CG2 . VAL   A 1 3   ? -7.330  3.258   52.823 1.00 65.94  ?  2   VAL   A CG2 1 
ATOM   17   N  N   . ARG   A 1 4   ? -9.719  0.142   55.251 1.00 75.70  ?  3   ARG   A N   1 
ATOM   18   C  CA  . ARG   A 1 4   ? -9.768  -0.976  56.190 1.00 80.98  ?  3   ARG   A CA  1 
ATOM   19   C  C   . ARG   A 1 4   ? -8.693  -2.018  55.858 1.00 78.41  ?  3   ARG   A C   1 
ATOM   20   O  O   . ARG   A 1 4   ? -8.275  -2.177  54.706 1.00 75.69  ?  3   ARG   A O   1 
ATOM   21   C  CB  . ARG   A 1 4   ? -11.157 -1.631  56.226 1.00 77.40  ?  3   ARG   A CB  1 
ATOM   22   C  CG  . ARG   A 1 4   ? -12.015 -1.459  54.972 1.00 82.00  ?  3   ARG   A CG  1 
ATOM   23   C  CD  . ARG   A 1 4   ? -13.415 -2.068  55.172 1.00 82.76  ?  3   ARG   A CD  1 
ATOM   24   N  NE  . ARG   A 1 4   ? -13.367 -3.487  55.522 1.00 88.84  ?  3   ARG   A NE  1 
ATOM   25   C  CZ  . ARG   A 1 4   ? -13.900 -4.017  56.618 1.00 93.70  ?  3   ARG   A CZ  1 
ATOM   26   N  NH1 . ARG   A 1 4   ? -14.549 -3.278  57.503 1.00 95.58  ?  3   ARG   A NH1 1 
ATOM   27   N  NH2 . ARG   A 1 4   ? -13.766 -5.321  56.839 1.00 91.90  ?  3   ARG   A NH2 1 
ATOM   28   N  N   . THR   A 1 5   ? -8.210  -2.694  56.901 1.00 70.74  ?  4   THR   A N   1 
ATOM   29   C  CA  . THR   A 1 5   ? -7.060  -3.580  56.792 1.00 75.47  ?  4   THR   A CA  1 
ATOM   30   C  C   . THR   A 1 5   ? -7.246  -4.771  57.723 1.00 77.74  ?  4   THR   A C   1 
ATOM   31   O  O   . THR   A 1 5   ? -8.001  -4.706  58.699 1.00 78.03  ?  4   THR   A O   1 
ATOM   32   C  CB  . THR   A 1 5   ? -5.715  -2.875  57.135 1.00 75.57  ?  4   THR   A CB  1 
ATOM   33   O  OG1 . THR   A 1 5   ? -5.491  -2.905  58.556 1.00 74.98  ?  4   THR   A OG1 1 
ATOM   34   C  CG2 . THR   A 1 5   ? -5.640  -1.426  56.613 1.00 71.15  ?  4   THR   A CG2 1 
ATOM   35   N  N   . ILE   A 1 6   ? -6.531  -5.864  57.416 1.00 77.72  ?  5   ILE   A N   1 
ATOM   36   C  CA  . ILE   A 1 6   ? -6.502  -7.057  58.259 1.00 77.40  ?  5   ILE   A CA  1 
ATOM   37   C  C   . ILE   A 1 6   ? -5.077  -7.599  58.365 1.00 74.26  ?  5   ILE   A C   1 
ATOM   38   O  O   . ILE   A 1 6   ? -4.263  -7.457  57.446 1.00 71.51  ?  5   ILE   A O   1 
ATOM   39   C  CB  . ILE   A 1 6   ? -7.468  -8.150  57.743 1.00 77.65  ?  5   ILE   A CB  1 
ATOM   40   C  CG1 . ILE   A 1 6   ? -7.253  -8.420  56.253 1.00 71.85  ?  5   ILE   A CG1 1 
ATOM   41   C  CG2 . ILE   A 1 6   ? -8.918  -7.766  58.030 1.00 81.44  ?  5   ILE   A CG2 1 
ATOM   42   C  CD1 . ILE   A 1 6   ? -7.200  -9.898  55.906 1.00 73.73  ?  5   ILE   A CD1 1 
ATOM   43   N  N   . LYS   A 1 7   ? -4.779  -8.216  59.509 1.00 72.79  ?  6   LYS   A N   1 
ATOM   44   C  CA  . LYS   A 1 7   ? -3.470  -8.816  59.741 1.00 67.81  ?  6   LYS   A CA  1 
ATOM   45   C  C   . LYS   A 1 7   ? -3.389  -10.198 59.098 1.00 68.14  ?  6   LYS   A C   1 
ATOM   46   O  O   . LYS   A 1 7   ? -4.345  -10.975 59.140 1.00 76.39  ?  6   LYS   A O   1 
ATOM   47   C  CB  . LYS   A 1 7   ? -3.194  -8.922  61.245 1.00 66.85  ?  6   LYS   A CB  1 
ATOM   48   C  CG  . LYS   A 1 7   ? -2.240  -7.861  61.799 1.00 67.68  ?  6   LYS   A CG  1 
ATOM   49   C  CD  . LYS   A 1 7   ? -1.403  -8.417  62.966 1.00 73.16  ?  6   LYS   A CD  1 
ATOM   50   C  CE  . LYS   A 1 7   ? -1.162  -7.370  64.063 1.00 76.18  ?  6   LYS   A CE  1 
ATOM   51   N  NZ  . LYS   A 1 7   ? -0.275  -6.237  63.621 1.00 63.36  ?  6   LYS   A NZ  1 
ATOM   52   N  N   . VAL   A 1 8   ? -2.243  -10.498 58.484 1.00 60.58  ?  7   VAL   A N   1 
ATOM   53   C  CA  . VAL   A 1 8   ? -1.971  -11.798 57.878 1.00 58.06  ?  7   VAL   A CA  1 
ATOM   54   C  C   . VAL   A 1 8   ? -0.465  -12.008 57.956 1.00 58.85  ?  7   VAL   A C   1 
ATOM   55   O  O   . VAL   A 1 8   ? 0.302   -11.054 58.084 1.00 66.25  ?  7   VAL   A O   1 
ATOM   56   C  CB  . VAL   A 1 8   ? -2.458  -11.900 56.402 1.00 61.33  ?  7   VAL   A CB  1 
ATOM   57   C  CG1 . VAL   A 1 8   ? -3.965  -11.659 56.264 1.00 56.08  ?  7   VAL   A CG1 1 
ATOM   58   C  CG2 . VAL   A 1 8   ? -1.665  -10.964 55.478 1.00 54.47  ?  7   VAL   A CG2 1 
ATOM   59   N  N   . PHE   A 1 9   ? -0.027  -13.262 57.866 1.00 59.79  ?  8   PHE   A N   1 
ATOM   60   C  CA  . PHE   A 1 9   ? 1.400   -13.579 57.881 1.00 61.51  ?  8   PHE   A CA  1 
ATOM   61   C  C   . PHE   A 1 9   ? 1.839   -14.168 56.542 1.00 61.07  ?  8   PHE   A C   1 
ATOM   62   O  O   . PHE   A 1 9   ? 1.244   -15.138 56.064 1.00 68.92  ?  8   PHE   A O   1 
ATOM   63   C  CB  . PHE   A 1 9   ? 1.741   -14.552 59.011 1.00 55.52  ?  8   PHE   A CB  1 
ATOM   64   C  CG  . PHE   A 1 9   ? 1.179   -14.159 60.350 1.00 61.15  ?  8   PHE   A CG  1 
ATOM   65   C  CD1 . PHE   A 1 9   ? 1.739   -13.127 61.079 1.00 60.89  ?  8   PHE   A CD1 1 
ATOM   66   C  CD2 . PHE   A 1 9   ? 0.090   -14.833 60.890 1.00 67.20  ?  8   PHE   A CD2 1 
ATOM   67   C  CE1 . PHE   A 1 9   ? 1.222   -12.776 62.326 1.00 62.95  ?  8   PHE   A CE1 1 
ATOM   68   C  CE2 . PHE   A 1 9   ? -0.426  -14.490 62.142 1.00 59.96  ?  8   PHE   A CE2 1 
ATOM   69   C  CZ  . PHE   A 1 9   ? 0.141   -13.461 62.855 1.00 56.88  ?  8   PHE   A CZ  1 
ATOM   70   N  N   . THR   A 1 10  ? 2.881   -13.593 55.945 1.00 55.48  ?  9   THR   A N   1 
ATOM   71   C  CA  . THR   A 1 10  ? 3.523   -14.144 54.760 1.00 54.62  ?  9   THR   A CA  1 
ATOM   72   C  C   . THR   A 1 10  ? 4.794   -14.900 55.128 1.00 58.89  ?  9   THR   A C   1 
ATOM   73   O  O   . THR   A 1 10  ? 5.371   -14.718 56.205 1.00 61.90  ?  9   THR   A O   1 
ATOM   74   C  CB  . THR   A 1 10  ? 3.881   -13.052 53.762 1.00 50.51  ?  9   THR   A CB  1 
ATOM   75   O  OG1 . THR   A 1 10  ? 4.753   -12.107 54.396 1.00 55.48  ?  9   THR   A OG1 1 
ATOM   76   C  CG2 . THR   A 1 10  ? 2.650   -12.371 53.303 1.00 54.24  ?  9   THR   A CG2 1 
ATOM   77   N  N   . THR   A 1 11  ? 5.250   -15.723 54.189 1.00 52.11  ?  10  THR   A N   1 
ATOM   78   C  CA  . THR   A 1 11  ? 6.314   -16.677 54.449 1.00 51.40  ?  10  THR   A CA  1 
ATOM   79   C  C   . THR   A 1 11  ? 6.717   -17.309 53.128 1.00 51.93  ?  10  THR   A C   1 
ATOM   80   O  O   . THR   A 1 11  ? 5.915   -17.384 52.190 1.00 51.16  ?  10  THR   A O   1 
ATOM   81   C  CB  . THR   A 1 11  ? 5.865   -17.758 55.459 1.00 61.27  ?  10  THR   A CB  1 
ATOM   82   O  OG1 . THR   A 1 11  ? 6.988   -18.538 55.892 1.00 63.70  ?  10  THR   A OG1 1 
ATOM   83   C  CG2 . THR   A 1 11  ? 4.809   -18.678 54.862 1.00 59.14  ?  10  THR   A CG2 1 
ATOM   84   N  N   . VAL   A 1 12  ? 7.979   -17.715 53.049 1.00 47.19  ?  11  VAL   A N   1 
ATOM   85   C  CA  . VAL   A 1 12  ? 8.445   -18.559 51.966 1.00 44.94  ?  11  VAL   A CA  1 
ATOM   86   C  C   . VAL   A 1 12  ? 8.816   -19.941 52.459 1.00 56.22  ?  11  VAL   A C   1 
ATOM   87   O  O   . VAL   A 1 12  ? 9.131   -20.820 51.638 1.00 61.41  ?  11  VAL   A O   1 
ATOM   88   C  CB  . VAL   A 1 12  ? 9.613   -17.905 51.200 1.00 45.08  ?  11  VAL   A CB  1 
ATOM   89   C  CG1 . VAL   A 1 12  ? 9.282   -16.463 50.932 1.00 55.68  ?  11  VAL   A CG1 1 
ATOM   90   C  CG2 . VAL   A 1 12  ? 10.947  -18.010 51.934 1.00 46.58  ?  11  VAL   A CG2 1 
ATOM   91   N  N   . ASP   A 1 13  ? 8.737   -20.181 53.778 1.00 54.20  ?  12  ASP   A N   1 
ATOM   92   C  CA  . ASP   A 1 13  ? 9.066   -21.478 54.354 1.00 53.99  ?  12  ASP   A CA  1 
ATOM   93   C  C   . ASP   A 1 13  ? 8.086   -21.919 55.434 1.00 60.98  ?  12  ASP   A C   1 
ATOM   94   O  O   . ASP   A 1 13  ? 8.349   -22.929 56.095 1.00 66.08  ?  12  ASP   A O   1 
ATOM   95   C  CB  . ASP   A 1 13  ? 10.497  -21.512 54.965 1.00 56.11  ?  12  ASP   A CB  1 
ATOM   96   C  CG  . ASP   A 1 13  ? 10.820  -20.314 55.881 1.00 61.21  ?  12  ASP   A CG  1 
ATOM   97   O  OD1 . ASP   A 1 13  ? 9.922   -19.850 56.636 1.00 61.24  -1 12  ASP   A OD1 1 
ATOM   98   O  OD2 . ASP   A 1 13  ? 12.008  -19.881 55.884 1.00 59.39  ?  12  ASP   A OD2 1 
ATOM   99   N  N   . ASN   A 1 14  ? 6.986   -21.195 55.660 1.00 60.94  ?  13  ASN   A N   1 
ATOM   100  C  CA  . ASN   A 1 14  ? 6.019   -21.545 56.713 1.00 65.00  ?  13  ASN   A CA  1 
ATOM   101  C  C   . ASN   A 1 14  ? 6.700   -21.710 58.077 1.00 65.91  ?  13  ASN   A C   1 
ATOM   102  O  O   . ASN   A 1 14  ? 6.227   -22.448 58.948 1.00 66.74  ?  13  ASN   A O   1 
ATOM   103  C  CB  . ASN   A 1 14  ? 5.237   -22.813 56.342 1.00 64.62  ?  13  ASN   A CB  1 
ATOM   104  C  CG  . ASN   A 1 14  ? 3.844   -22.868 56.977 1.00 76.57  ?  13  ASN   A CG  1 
ATOM   105  O  OD1 . ASN   A 1 14  ? 3.654   -22.477 58.140 1.00 75.60  ?  13  ASN   A OD1 1 
ATOM   106  N  ND2 . ASN   A 1 14  ? 2.862   -23.359 56.212 1.00 68.28  ?  13  ASN   A ND2 1 
ATOM   107  N  N   . ILE   A 1 15  ? 7.821   -21.020 58.280 1.00 63.09  ?  14  ILE   A N   1 
ATOM   108  C  CA  . ILE   A 1 15  ? 8.597   -21.192 59.500 1.00 60.33  ?  14  ILE   A CA  1 
ATOM   109  C  C   . ILE   A 1 15  ? 9.064   -19.839 60.030 1.00 63.88  ?  14  ILE   A C   1 
ATOM   110  O  O   . ILE   A 1 15  ? 9.021   -19.592 61.241 1.00 67.83  ?  14  ILE   A O   1 
ATOM   111  C  CB  . ILE   A 1 15  ? 9.768   -22.157 59.246 1.00 70.15  ?  14  ILE   A CB  1 
ATOM   112  C  CG1 . ILE   A 1 15  ? 9.243   -23.611 59.233 1.00 73.07  ?  14  ILE   A CG1 1 
ATOM   113  C  CG2 . ILE   A 1 15  ? 10.918  -21.914 60.250 1.00 64.50  ?  14  ILE   A CG2 1 
ATOM   114  C  CD1 . ILE   A 1 15  ? 10.199  -24.648 58.584 1.00 72.06  ?  14  ILE   A CD1 1 
ATOM   115  N  N   . ASN   A 1 16  ? 9.503   -18.948 59.141 1.00 63.45  ?  15  ASN   A N   1 
ATOM   116  C  CA  . ASN   A 1 16  ? 9.675   -17.537 59.485 1.00 62.93  ?  15  ASN   A CA  1 
ATOM   117  C  C   . ASN   A 1 16  ? 8.437   -16.791 58.993 1.00 63.78  ?  15  ASN   A C   1 
ATOM   118  O  O   . ASN   A 1 16  ? 8.343   -16.424 57.816 1.00 59.05  ?  15  ASN   A O   1 
ATOM   119  C  CB  . ASN   A 1 16  ? 10.961  -16.959 58.899 1.00 59.43  ?  15  ASN   A CB  1 
ATOM   120  C  CG  . ASN   A 1 16  ? 12.147  -17.202 59.793 1.00 70.76  ?  15  ASN   A CG  1 
ATOM   121  O  OD1 . ASN   A 1 16  ? 12.352  -16.491 60.788 1.00 76.44  ?  15  ASN   A OD1 1 
ATOM   122  N  ND2 . ASN   A 1 16  ? 12.929  -18.229 59.466 1.00 68.37  ?  15  ASN   A ND2 1 
ATOM   123  N  N   . LEU   A 1 17  ? 7.479   -16.572 59.898 1.00 63.83  ?  16  LEU   A N   1 
ATOM   124  C  CA  . LEU   A 1 17  ? 6.292   -15.792 59.564 1.00 60.72  ?  16  LEU   A CA  1 
ATOM   125  C  C   . LEU   A 1 17  ? 6.574   -14.303 59.704 1.00 58.45  ?  16  LEU   A C   1 
ATOM   126  O  O   . LEU   A 1 17  ? 7.142   -13.859 60.709 1.00 57.96  ?  16  LEU   A O   1 
ATOM   127  C  CB  . LEU   A 1 17  ? 5.116   -16.190 60.447 1.00 55.43  ?  16  LEU   A CB  1 
ATOM   128  C  CG  . LEU   A 1 17  ? 4.890   -17.690 60.514 1.00 57.21  ?  16  LEU   A CG  1 
ATOM   129  C  CD1 . LEU   A 1 17  ? 3.609   -17.962 61.243 1.00 57.83  ?  16  LEU   A CD1 1 
ATOM   130  C  CD2 . LEU   A 1 17  ? 4.834   -18.250 59.115 1.00 62.67  ?  16  LEU   A CD2 1 
ATOM   131  N  N   . HIS   A 1 18  ? 6.167   -13.557 58.680 1.00 57.96  ?  17  HIS   A N   1 
ATOM   132  C  CA  . HIS   A 1 18  ? 6.365   -12.091 58.688 1.00 57.43  ?  17  HIS   A CA  1 
ATOM   133  C  C   . HIS   A 1 18  ? 5.002   -11.413 58.751 1.00 60.06  ?  17  HIS   A C   1 
ATOM   134  O  O   . HIS   A 1 18  ? 4.197   -11.581 57.827 1.00 63.22  ?  17  HIS   A O   1 
ATOM   135  C  CB  . HIS   A 1 18  ? 7.119   -11.648 57.438 1.00 47.46  ?  17  HIS   A CB  1 
ATOM   136  C  CG  . HIS   A 1 18  ? 8.311   -12.472 57.129 1.00 57.28  ?  17  HIS   A CG  1 
ATOM   137  N  ND1 . HIS   A 1 18  ? 8.230   -13.559 56.293 1.00 71.27  ?  17  HIS   A ND1 1 
ATOM   138  C  CD2 . HIS   A 1 18  ? 9.585   -12.385 57.515 1.00 57.15  ?  17  HIS   A CD2 1 
ATOM   139  C  CE1 . HIS   A 1 18  ? 9.426   -14.103 56.186 1.00 62.77  ?  17  HIS   A CE1 1 
ATOM   140  N  NE2 . HIS   A 1 18  ? 10.267  -13.409 56.921 1.00 65.85  ?  17  HIS   A NE2 1 
ATOM   141  N  N   . THR   A 1 19  ? 4.763   -10.660 59.817 1.00 58.69  ?  18  THR   A N   1 
ATOM   142  C  CA  . THR   A 1 19  ? 3.504   -9.924  59.958 1.00 59.46  ?  18  THR   A CA  1 
ATOM   143  C  C   . THR   A 1 19  ? 3.323   -8.880  58.860 1.00 61.99  ?  18  THR   A C   1 
ATOM   144  O  O   . THR   A 1 19  ? 4.231   -8.090  58.597 1.00 62.96  ?  18  THR   A O   1 
ATOM   145  C  CB  . THR   A 1 19  ? 3.450   -9.212  61.296 1.00 55.90  ?  18  THR   A CB  1 
ATOM   146  O  OG1 . THR   A 1 19  ? 3.581   -10.161 62.364 1.00 64.20  ?  18  THR   A OG1 1 
ATOM   147  C  CG2 . THR   A 1 19  ? 2.122   -8.492  61.407 1.00 62.58  ?  18  THR   A CG2 1 
ATOM   148  N  N   . GLN   A 1 20  ? 2.142   -8.862  58.227 1.00 60.11  ?  19  GLN   A N   1 
ATOM   149  C  CA  . GLN   A 1 20  ? 1.769   -7.793  57.304 1.00 59.19  ?  19  GLN   A CA  1 
ATOM   150  C  C   . GLN   A 1 20  ? 0.331   -7.363  57.557 1.00 60.05  ?  19  GLN   A C   1 
ATOM   151  O  O   . GLN   A 1 20  ? -0.445  -8.091  58.172 1.00 64.31  ?  19  GLN   A O   1 
ATOM   152  C  CB  . GLN   A 1 20  ? 1.914   -8.212  55.847 1.00 61.69  ?  19  GLN   A CB  1 
ATOM   153  C  CG  . GLN   A 1 20  ? 3.125   -9.055  55.568 1.00 62.21  ?  19  GLN   A CG  1 
ATOM   154  C  CD  . GLN   A 1 20  ? 4.330   -8.214  55.309 1.00 62.25  ?  19  GLN   A CD  1 
ATOM   155  O  OE1 . GLN   A 1 20  ? 4.239   -6.990  55.245 1.00 67.24  ?  19  GLN   A OE1 1 
ATOM   156  N  NE2 . GLN   A 1 20  ? 5.475   -8.858  55.153 1.00 67.20  ?  19  GLN   A NE2 1 
ATOM   157  N  N   . VAL   A 1 21  ? -0.013  -6.156  57.096 1.00 62.87  ?  20  VAL   A N   1 
ATOM   158  C  CA  . VAL   A 1 21  ? -1.394  -5.671  57.060 1.00 64.67  ?  20  VAL   A CA  1 
ATOM   159  C  C   . VAL   A 1 21  ? -1.779  -5.480  55.602 1.00 62.79  ?  20  VAL   A C   1 
ATOM   160  O  O   . VAL   A 1 21  ? -1.043  -4.846  54.838 1.00 61.43  ?  20  VAL   A O   1 
ATOM   161  C  CB  . VAL   A 1 21  ? -1.601  -4.357  57.845 1.00 60.82  ?  20  VAL   A CB  1 
ATOM   162  C  CG1 . VAL   A 1 21  ? -1.634  -4.614  59.348 1.00 57.71  ?  20  VAL   A CG1 1 
ATOM   163  C  CG2 . VAL   A 1 21  ? -0.545  -3.351  57.498 1.00 56.55  ?  20  VAL   A CG2 1 
ATOM   164  N  N   . VAL   A 1 22  ? -2.926  -6.028  55.217 1.00 68.42  ?  21  VAL   A N   1 
ATOM   165  C  CA  . VAL   A 1 22  ? -3.367  -6.009  53.827 1.00 71.53  ?  21  VAL   A CA  1 
ATOM   166  C  C   . VAL   A 1 22  ? -4.591  -5.112  53.690 1.00 75.37  ?  21  VAL   A C   1 
ATOM   167  O  O   . VAL   A 1 22  ? -5.421  -4.995  54.605 1.00 68.04  ?  21  VAL   A O   1 
ATOM   168  C  CB  . VAL   A 1 22  ? -3.681  -7.425  53.293 1.00 70.93  ?  21  VAL   A CB  1 
ATOM   169  C  CG1 . VAL   A 1 22  ? -2.397  -8.155  52.887 1.00 62.54  ?  21  VAL   A CG1 1 
ATOM   170  C  CG2 . VAL   A 1 22  ? -4.447  -8.217  54.334 1.00 66.90  ?  21  VAL   A CG2 1 
ATOM   171  N  N   . ASP   A 1 23  ? -4.707  -4.495  52.514 1.00 72.52  ?  22  ASP   A N   1 
ATOM   172  C  CA  . ASP   A 1 23  ? -5.794  -3.577  52.205 1.00 71.88  ?  22  ASP   A CA  1 
ATOM   173  C  C   . ASP   A 1 23  ? -6.922  -4.369  51.554 1.00 75.37  ?  22  ASP   A C   1 
ATOM   174  O  O   . ASP   A 1 23  ? -6.736  -4.947  50.476 1.00 75.73  ?  22  ASP   A O   1 
ATOM   175  C  CB  . ASP   A 1 23  ? -5.285  -2.463  51.288 1.00 76.71  ?  22  ASP   A CB  1 
ATOM   176  C  CG  . ASP   A 1 23  ? -6.393  -1.550  50.769 1.00 78.01  ?  22  ASP   A CG  1 
ATOM   177  O  OD1 . ASP   A 1 23  ? -7.520  -1.564  51.318 1.00 78.61  ?  22  ASP   A OD1 1 
ATOM   178  O  OD2 . ASP   A 1 23  ? -6.118  -0.805  49.801 1.00 75.13  -1 22  ASP   A OD2 1 
ATOM   179  N  N   . MET   A 1 24  ? -8.093  -4.389  52.204 1.00 77.30  ?  23  MET   A N   1 
ATOM   180  C  CA  . MET   A 1 24  ? -9.221  -5.207  51.758 1.00 71.45  ?  23  MET   A CA  1 
ATOM   181  C  C   . MET   A 1 24  ? -9.851  -4.721  50.471 1.00 64.06  ?  23  MET   A C   1 
ATOM   182  O  O   . MET   A 1 24  ? -10.799 -5.347  50.002 1.00 73.76  ?  23  MET   A O   1 
ATOM   183  C  CB  . MET   A 1 24  ? -10.278 -5.261  52.845 1.00 61.70  ?  23  MET   A CB  1 
ATOM   184  C  CG  . MET   A 1 24  ? -9.699  -5.598  54.159 1.00 67.17  ?  23  MET   A CG  1 
ATOM   185  S  SD  . MET   A 1 24  ? -10.967 -6.318  55.165 1.00 94.91  ?  23  MET   A SD  1 
ATOM   186  C  CE  . MET   A 1 24  ? -10.707 -8.053  54.794 1.00 85.57  ?  23  MET   A CE  1 
ATOM   187  N  N   . SER   A 1 25  ? -9.379  -3.626  49.899 1.00 69.45  ?  24  SER   A N   1 
ATOM   188  C  CA  . SER   A 1 25  ? -9.842  -3.181  48.598 1.00 72.86  ?  24  SER   A CA  1 
ATOM   189  C  C   . SER   A 1 25  ? -8.888  -3.573  47.475 1.00 77.14  ?  24  SER   A C   1 
ATOM   190  O  O   . SER   A 1 25  ? -9.240  -3.420  46.297 1.00 72.47  ?  24  SER   A O   1 
ATOM   191  C  CB  . SER   A 1 25  ? -10.032 -1.660  48.601 1.00 72.17  ?  24  SER   A CB  1 
ATOM   192  O  OG  . SER   A 1 25  ? -8.837  -1.002  48.213 1.00 72.99  ?  24  SER   A OG  1 
ATOM   193  N  N   . MET   A 1 26  ? -7.694  -4.064  47.808 1.00 77.72  ?  25  MET   A N   1 
ATOM   194  C  CA  . MET   A 1 26  ? -6.712  -4.484  46.818 1.00 80.18  ?  25  MET   A CA  1 
ATOM   195  C  C   . MET   A 1 26  ? -6.599  -6.004  46.781 1.00 74.03  ?  25  MET   A C   1 
ATOM   196  O  O   . MET   A 1 26  ? -6.954  -6.706  47.733 1.00 66.84  ?  25  MET   A O   1 
ATOM   197  C  CB  . MET   A 1 26  ? -5.331  -3.876  47.105 1.00 78.58  ?  25  MET   A CB  1 
ATOM   198  C  CG  . MET   A 1 26  ? -5.112  -2.444  46.611 1.00 75.08  ?  25  MET   A CG  1 
ATOM   199  S  SD  . MET   A 1 26  ? -4.047  -1.471  47.709 1.00 92.83  ?  25  MET   A SD  1 
ATOM   200  C  CE  . MET   A 1 26  ? -2.522  -1.468  46.758 1.00 66.93  ?  25  MET   A CE  1 
ATOM   201  N  N   . THR   A 1 27  ? -6.098  -6.512  45.660 1.00 71.38  ?  26  THR   A N   1 
ATOM   202  C  CA  . THR   A 1 27  ? -5.808  -7.934  45.598 1.00 74.17  ?  26  THR   A CA  1 
ATOM   203  C  C   . THR   A 1 27  ? -4.495  -8.226  46.303 1.00 73.25  ?  26  THR   A C   1 
ATOM   204  O  O   . THR   A 1 27  ? -3.616  -7.363  46.418 1.00 72.75  ?  26  THR   A O   1 
ATOM   205  C  CB  . THR   A 1 27  ? -5.702  -8.448  44.163 1.00 68.55  ?  26  THR   A CB  1 
ATOM   206  O  OG1 . THR   A 1 27  ? -4.771  -7.646  43.427 1.00 65.49  ?  26  THR   A OG1 1 
ATOM   207  C  CG2 . THR   A 1 27  ? -7.051  -8.426  43.496 1.00 69.05  ?  26  THR   A CG2 1 
ATOM   208  N  N   . TYR   A 1 28  ? -4.375  -9.467  46.774 1.00 70.68  ?  27  TYR   A N   1 
ATOM   209  C  CA  . TYR   A 1 28  ? -3.091  -9.971  47.225 1.00 61.17  ?  27  TYR   A CA  1 
ATOM   210  C  C   . TYR   A 1 28  ? -2.029  -9.770  46.163 1.00 60.77  ?  27  TYR   A C   1 
ATOM   211  O  O   . TYR   A 1 28  ? -0.855  -9.574  46.484 1.00 62.01  ?  27  TYR   A O   1 
ATOM   212  C  CB  . TYR   A 1 28  ? -3.235  -11.443 47.596 1.00 59.92  ?  27  TYR   A CB  1 
ATOM   213  C  CG  . TYR   A 1 28  ? -4.056  -11.653 48.859 1.00 60.01  ?  27  TYR   A CG  1 
ATOM   214  C  CD1 . TYR   A 1 28  ? -3.477  -11.489 50.107 1.00 54.17  ?  27  TYR   A CD1 1 
ATOM   215  C  CD2 . TYR   A 1 28  ? -5.395  -12.013 48.806 1.00 58.63  ?  27  TYR   A CD2 1 
ATOM   216  C  CE1 . TYR   A 1 28  ? -4.193  -11.673 51.268 1.00 55.97  ?  27  TYR   A CE1 1 
ATOM   217  C  CE2 . TYR   A 1 28  ? -6.128  -12.201 49.976 1.00 63.37  ?  27  TYR   A CE2 1 
ATOM   218  C  CZ  . TYR   A 1 28  ? -5.512  -12.027 51.208 1.00 59.49  ?  27  TYR   A CZ  1 
ATOM   219  O  OH  . TYR   A 1 28  ? -6.199  -12.199 52.391 1.00 56.47  ?  27  TYR   A OH  1 
ATOM   220  N  N   . GLY   A 1 29  ? -2.428  -9.765  44.894 1.00 68.28  ?  28  GLY   A N   1 
ATOM   221  C  CA  . GLY   A 1 29  ? -1.456  -9.609  43.827 1.00 65.44  ?  28  GLY   A CA  1 
ATOM   222  C  C   . GLY   A 1 29  ? -0.817  -8.234  43.823 1.00 68.93  ?  28  GLY   A C   1 
ATOM   223  O  O   . GLY   A 1 29  ? 0.411   -8.110  43.769 1.00 70.59  ?  28  GLY   A O   1 
ATOM   224  N  N   . GLN   A 1 30  ? -1.641  -7.177  43.873 1.00 69.23  ?  29  GLN   A N   1 
ATOM   225  C  CA  . GLN   A 1 30  ? -1.087  -5.824  43.842 1.00 69.44  ?  29  GLN   A CA  1 
ATOM   226  C  C   . GLN   A 1 30  ? -0.238  -5.542  45.071 1.00 70.78  ?  29  GLN   A C   1 
ATOM   227  O  O   . GLN   A 1 30  ? 0.712   -4.754  44.996 1.00 73.27  ?  29  GLN   A O   1 
ATOM   228  C  CB  . GLN   A 1 30  ? -2.191  -4.769  43.753 1.00 74.44  ?  29  GLN   A CB  1 
ATOM   229  C  CG  . GLN   A 1 30  ? -3.321  -5.053  42.784 1.00 73.06  ?  29  GLN   A CG  1 
ATOM   230  C  CD  . GLN   A 1 30  ? -4.584  -4.305  43.175 1.00 77.33  ?  29  GLN   A CD  1 
ATOM   231  O  OE1 . GLN   A 1 30  ? -5.693  -4.837  43.114 1.00 79.44  ?  29  GLN   A OE1 1 
ATOM   232  N  NE2 . GLN   A 1 30  ? -4.415  -3.052  43.574 1.00 79.32  ?  29  GLN   A NE2 1 
ATOM   233  N  N   . GLN   A 1 31  ? -0.569  -6.168  46.208 1.00 66.16  ?  30  GLN   A N   1 
ATOM   234  C  CA  . GLN   A 1 31  ? 0.156   -5.923  47.447 1.00 63.41  ?  30  GLN   A CA  1 
ATOM   235  C  C   . GLN   A 1 31  ? 1.410   -6.788  47.564 1.00 65.74  ?  30  GLN   A C   1 
ATOM   236  O  O   . GLN   A 1 31  ? 2.472   -6.290  47.955 1.00 67.85  ?  30  GLN   A O   1 
ATOM   237  C  CB  . GLN   A 1 31  ? -0.772  -6.153  48.639 1.00 61.41  ?  30  GLN   A CB  1 
ATOM   238  C  CG  . GLN   A 1 31  ? -1.784  -5.042  48.860 1.00 65.89  ?  30  GLN   A CG  1 
ATOM   239  C  CD  . GLN   A 1 31  ? -3.020  -5.511  49.621 1.00 74.76  ?  30  GLN   A CD  1 
ATOM   240  O  OE1 . GLN   A 1 31  ? -3.122  -5.377  50.846 1.00 69.78  ?  30  GLN   A OE1 1 
ATOM   241  N  NE2 . GLN   A 1 31  ? -3.966  -6.082  48.886 1.00 79.34  ?  30  GLN   A NE2 1 
ATOM   242  N  N   . PHE   A 1 32  ? 1.322   -8.076  47.225 1.00 64.08  ?  31  PHE   A N   1 
ATOM   243  C  CA  . PHE   A 1 32  ? 2.353   -9.029  47.615 1.00 56.41  ?  31  PHE   A CA  1 
ATOM   244  C  C   . PHE   A 1 32  ? 3.143   -9.615  46.460 1.00 57.17  ?  31  PHE   A C   1 
ATOM   245  O  O   . PHE   A 1 32  ? 4.178   -10.239 46.705 1.00 63.96  ?  31  PHE   A O   1 
ATOM   246  C  CB  . PHE   A 1 32  ? 1.737   -10.196 48.399 1.00 54.22  ?  31  PHE   A CB  1 
ATOM   247  C  CG  . PHE   A 1 32  ? 1.437   -9.882  49.833 1.00 48.35  ?  31  PHE   A CG  1 
ATOM   248  C  CD1 . PHE   A 1 32  ? 0.595   -10.707 50.573 1.00 50.39  ?  31  PHE   A CD1 1 
ATOM   249  C  CD2 . PHE   A 1 32  ? 1.991   -8.776  50.443 1.00 48.91  ?  31  PHE   A CD2 1 
ATOM   250  C  CE1 . PHE   A 1 32  ? 0.299   -10.429 51.913 1.00 56.63  ?  31  PHE   A CE1 1 
ATOM   251  C  CE2 . PHE   A 1 32  ? 1.710   -8.488  51.792 1.00 63.33  ?  31  PHE   A CE2 1 
ATOM   252  C  CZ  . PHE   A 1 32  ? 0.866   -9.319  52.530 1.00 54.94  ?  31  PHE   A CZ  1 
ATOM   253  N  N   . GLY   A 1 33  ? 2.700   -9.440  45.225 1.00 61.96  ?  32  GLY   A N   1 
ATOM   254  C  CA  . GLY   A 1 33  ? 3.123   -10.318 44.162 1.00 58.95  ?  32  GLY   A CA  1 
ATOM   255  C  C   . GLY   A 1 33  ? 2.303   -11.597 44.200 1.00 59.85  ?  32  GLY   A C   1 
ATOM   256  O  O   . GLY   A 1 33  ? 1.271   -11.683 44.880 1.00 59.75  ?  32  GLY   A O   1 
ATOM   257  N  N   . PRO   A 1 34  ? 2.730   -12.606 43.450 1.00 56.14  ?  33  PRO   A N   1 
ATOM   258  C  CA  . PRO   A 1 34  ? 2.058   -13.914 43.509 1.00 57.67  ?  33  PRO   A CA  1 
ATOM   259  C  C   . PRO   A 1 34  ? 1.878   -14.421 44.935 1.00 58.55  ?  33  PRO   A C   1 
ATOM   260  O  O   . PRO   A 1 34  ? 2.829   -14.477 45.728 1.00 61.94  ?  33  PRO   A O   1 
ATOM   261  C  CB  . PRO   A 1 34  ? 2.999   -14.813 42.706 1.00 56.93  ?  33  PRO   A CB  1 
ATOM   262  C  CG  . PRO   A 1 34  ? 3.567   -13.871 41.655 1.00 52.00  ?  33  PRO   A CG  1 
ATOM   263  C  CD  . PRO   A 1 34  ? 3.642   -12.498 42.299 1.00 51.42  ?  33  PRO   A CD  1 
ATOM   264  N  N   . THR   A 1 35  ? 0.643   -14.792 45.266 1.00 52.22  ?  34  THR   A N   1 
ATOM   265  C  CA  . THR   A 1 35  ? 0.313   -15.283 46.596 1.00 52.61  ?  34  THR   A CA  1 
ATOM   266  C  C   . THR   A 1 35  ? -0.455  -16.594 46.484 1.00 59.50  ?  34  THR   A C   1 
ATOM   267  O  O   . THR   A 1 35  ? -1.294  -16.760 45.594 1.00 61.30  ?  34  THR   A O   1 
ATOM   268  C  CB  . THR   A 1 35  ? -0.520  -14.247 47.382 1.00 55.94  ?  34  THR   A CB  1 
ATOM   269  O  OG1 . THR   A 1 35  ? 0.133   -12.976 47.331 1.00 58.39  ?  34  THR   A OG1 1 
ATOM   270  C  CG2 . THR   A 1 35  ? -0.711  -14.657 48.852 1.00 51.17  ?  34  THR   A CG2 1 
ATOM   271  N  N   . TYR   A 1 36  ? -0.164  -17.521 47.395 1.00 60.98  ?  35  TYR   A N   1 
ATOM   272  C  CA  . TYR   A 1 36  ? -0.888  -18.775 47.537 1.00 56.17  ?  35  TYR   A CA  1 
ATOM   273  C  C   . TYR   A 1 36  ? -1.384  -18.894 48.967 1.00 58.13  ?  35  TYR   A C   1 
ATOM   274  O  O   . TYR   A 1 36  ? -0.657  -18.558 49.903 1.00 63.41  ?  35  TYR   A O   1 
ATOM   275  C  CB  . TYR   A 1 36  ? 0.010   -19.968 47.212 1.00 54.17  ?  35  TYR   A CB  1 
ATOM   276  C  CG  . TYR   A 1 36  ? 0.596   -19.894 45.842 1.00 50.63  ?  35  TYR   A CG  1 
ATOM   277  C  CD1 . TYR   A 1 36  ? 1.800   -19.234 45.626 1.00 49.87  ?  35  TYR   A CD1 1 
ATOM   278  C  CD2 . TYR   A 1 36  ? -0.041  -20.492 44.756 1.00 53.71  ?  35  TYR   A CD2 1 
ATOM   279  C  CE1 . TYR   A 1 36  ? 2.339   -19.151 44.369 1.00 53.89  ?  35  TYR   A CE1 1 
ATOM   280  C  CE2 . TYR   A 1 36  ? 0.503   -20.425 43.488 1.00 47.44  ?  35  TYR   A CE2 1 
ATOM   281  C  CZ  . TYR   A 1 36  ? 1.684   -19.752 43.305 1.00 47.43  ?  35  TYR   A CZ  1 
ATOM   282  O  OH  . TYR   A 1 36  ? 2.231   -19.676 42.064 1.00 50.78  ?  35  TYR   A OH  1 
ATOM   283  N  N   . LEU   A 1 37  ? -2.622  -19.355 49.135 1.00 58.70  ?  36  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 37  ? -3.155  -19.746 50.440 1.00 58.66  ?  36  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 37  ? -3.535  -21.218 50.330 1.00 69.56  ?  36  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 37  ? -4.439  -21.578 49.562 1.00 69.93  ?  36  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 37  ? -4.341  -18.872 50.855 1.00 50.44  ?  36  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 37  ? -5.239  -19.269 52.039 1.00 55.24  ?  36  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 37  ? -4.539  -19.298 53.406 1.00 62.99  ?  36  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 37  ? -6.436  -18.350 52.104 1.00 45.93  ?  36  LEU   A CD2 1 
ATOM   291  N  N   . ASP   A 1 38  ? -2.798  -22.068 51.052 1.00 74.35  ?  37  ASP   A N   1 
ATOM   292  C  CA  . ASP   A 1 38  ? -3.027  -23.513 51.057 1.00 68.42  ?  37  ASP   A CA  1 
ATOM   293  C  C   . ASP   A 1 38  ? -2.971  -24.097 49.649 1.00 64.77  ?  37  ASP   A C   1 
ATOM   294  O  O   . ASP   A 1 38  ? -3.725  -25.003 49.296 1.00 70.56  ?  37  ASP   A O   1 
ATOM   295  C  CB  . ASP   A 1 38  ? -4.346  -23.832 51.750 1.00 69.08  ?  37  ASP   A CB  1 
ATOM   296  C  CG  . ASP   A 1 38  ? -4.376  -23.290 53.155 1.00 85.02  ?  37  ASP   A CG  1 
ATOM   297  O  OD1 . ASP   A 1 38  ? -5.355  -23.561 53.886 1.00 99.66  -1 37  ASP   A OD1 1 
ATOM   298  O  OD2 . ASP   A 1 38  ? -3.396  -22.590 53.525 1.00 79.82  ?  37  ASP   A OD2 1 
ATOM   299  N  N   . GLY   A 1 39  ? -2.059  -23.574 48.838 1.00 71.01  ?  38  GLY   A N   1 
ATOM   300  C  CA  . GLY   A 1 39  ? -1.904  -23.988 47.465 1.00 60.96  ?  38  GLY   A CA  1 
ATOM   301  C  C   . GLY   A 1 39  ? -2.704  -23.179 46.473 1.00 61.34  ?  38  GLY   A C   1 
ATOM   302  O  O   . GLY   A 1 39  ? -2.349  -23.151 45.286 1.00 64.21  ?  38  GLY   A O   1 
ATOM   303  N  N   . ALA   A 1 40  ? -3.760  -22.505 46.926 1.00 60.71  ?  39  ALA   A N   1 
ATOM   304  C  CA  . ALA   A 1 40  ? -4.655  -21.778 46.032 1.00 63.02  ?  39  ALA   A CA  1 
ATOM   305  C  C   . ALA   A 1 40  ? -4.035  -20.444 45.606 1.00 59.19  ?  39  ALA   A C   1 
ATOM   306  O  O   . ALA   A 1 40  ? -3.752  -19.593 46.447 1.00 67.76  ?  39  ALA   A O   1 
ATOM   307  C  CB  . ALA   A 1 40  ? -5.995  -21.557 46.730 1.00 60.74  ?  39  ALA   A CB  1 
ATOM   308  N  N   . ASP   A 1 41  ? -3.887  -20.261 44.286 1.00 54.72  ?  40  ASP   A N   1 
ATOM   309  C  CA  . ASP   A 1 41  ? -3.332  -18.987 43.742 1.00 57.36  ?  40  ASP   A CA  1 
ATOM   310  C  C   . ASP   A 1 41  ? -4.326  -17.852 43.991 1.00 66.13  ?  40  ASP   A C   1 
ATOM   311  O  O   . ASP   A 1 41  ? -5.169  -17.591 43.106 1.00 66.67  ?  40  ASP   A O   1 
ATOM   312  C  CB  . ASP   A 1 41  ? -2.942  -19.102 42.278 1.00 48.79  ?  40  ASP   A CB  1 
ATOM   313  C  CG  . ASP   A 1 41  ? -2.086  -17.955 41.761 1.00 63.45  ?  40  ASP   A CG  1 
ATOM   314  O  OD1 . ASP   A 1 41  ? -2.403  -17.430 40.674 1.00 78.31  ?  40  ASP   A OD1 1 
ATOM   315  O  OD2 . ASP   A 1 41  ? -1.117  -17.589 42.459 1.00 64.78  ?  40  ASP   A OD2 1 
ATOM   316  N  N   . VAL   A 1 42  ? -4.224  -17.203 45.146 1.00 55.95  ?  41  VAL   A N   1 
ATOM   317  C  CA  . VAL   A 1 42  ? -5.107  -16.097 45.535 1.00 57.93  ?  41  VAL   A CA  1 
ATOM   318  C  C   . VAL   A 1 42  ? -4.604  -14.755 45.001 1.00 59.93  ?  41  VAL   A C   1 
ATOM   319  O  O   . VAL   A 1 42  ? -5.050  -13.700 45.458 1.00 63.35  ?  41  VAL   A O   1 
ATOM   320  C  CB  . VAL   A 1 42  ? -5.273  -15.997 47.069 1.00 54.47  ?  41  VAL   A CB  1 
ATOM   321  C  CG1 . VAL   A 1 42  ? -5.984  -17.218 47.657 1.00 52.12  ?  41  VAL   A CG1 1 
ATOM   322  C  CG2 . VAL   A 1 42  ? -3.927  -15.781 47.750 1.00 54.85  ?  41  VAL   A CG2 1 
ATOM   323  N  N   . THR   A 1 43  ? -3.667  -14.772 44.051 1.00 58.78  ?  42  THR   A N   1 
ATOM   324  C  CA  . THR   A 1 43  ? -3.154  -13.519 43.491 1.00 65.48  ?  42  THR   A CA  1 
ATOM   325  C  C   . THR   A 1 43  ? -4.276  -12.579 43.048 1.00 72.50  ?  42  THR   A C   1 
ATOM   326  O  O   . THR   A 1 43  ? -4.330  -11.417 43.473 1.00 70.25  ?  42  THR   A O   1 
ATOM   327  C  CB  . THR   A 1 43  ? -2.207  -13.797 42.318 1.00 62.06  ?  42  THR   A CB  1 
ATOM   328  O  OG1 . THR   A 1 43  ? -1.269  -14.819 42.684 1.00 67.78  ?  42  THR   A OG1 1 
ATOM   329  C  CG2 . THR   A 1 43  ? -1.469  -12.558 41.932 1.00 61.19  ?  42  THR   A CG2 1 
ATOM   330  N  N   . LYS   A 1 44  ? -5.194  -13.066 42.208 1.00 76.44  ?  43  LYS   A N   1 
ATOM   331  C  CA  . LYS   A 1 44  ? -6.230  -12.221 41.622 1.00 70.67  ?  43  LYS   A CA  1 
ATOM   332  C  C   . LYS   A 1 44  ? -7.474  -12.062 42.523 1.00 71.59  ?  43  LYS   A C   1 
ATOM   333  O  O   . LYS   A 1 44  ? -8.542  -11.684 42.024 1.00 76.88  ?  43  LYS   A O   1 
ATOM   334  C  CB  . LYS   A 1 44  ? -6.625  -12.762 40.241 1.00 59.61  ?  43  LYS   A CB  1 
ATOM   335  C  CG  . LYS   A 1 44  ? -5.499  -12.705 39.181 1.00 75.15  ?  43  LYS   A CG  1 
ATOM   336  C  CD  . LYS   A 1 44  ? -5.360  -14.033 38.378 1.00 78.96  ?  43  LYS   A CD  1 
ATOM   337  C  CE  . LYS   A 1 44  ? -4.219  -14.947 38.938 1.00 71.92  ?  43  LYS   A CE  1 
ATOM   338  N  NZ  . LYS   A 1 44  ? -3.982  -16.232 38.184 1.00 60.86  ?  43  LYS   A NZ  1 
ATOM   339  N  N   . ILE   A 1 45  ? -7.361  -12.305 43.831 1.00 61.32  ?  44  ILE   A N   1 
ATOM   340  C  CA  . ILE   A 1 45  ? -8.489  -12.151 44.747 1.00 66.94  ?  44  ILE   A CA  1 
ATOM   341  C  C   . ILE   A 1 45  ? -8.125  -11.165 45.861 1.00 72.99  ?  44  ILE   A C   1 
ATOM   342  O  O   . ILE   A 1 45  ? -6.979  -11.119 46.325 1.00 74.87  ?  44  ILE   A O   1 
ATOM   343  C  CB  . ILE   A 1 45  ? -8.956  -13.511 45.326 1.00 68.78  ?  44  ILE   A CB  1 
ATOM   344  C  CG1 . ILE   A 1 45  ? -8.401  -13.758 46.733 1.00 67.16  ?  44  ILE   A CG1 1 
ATOM   345  C  CG2 . ILE   A 1 45  ? -8.594  -14.664 44.400 1.00 68.72  ?  44  ILE   A CG2 1 
ATOM   346  C  CD1 . ILE   A 1 45  ? -9.416  -14.327 47.700 1.00 72.89  ?  44  ILE   A CD1 1 
ATOM   347  N  N   . LYS   A 1 46  ? -9.114  -10.351 46.281 1.00 69.89  ?  45  LYS   A N   1 
ATOM   348  C  CA  . LYS   A 1 46  ? -8.970  -9.435  47.404 1.00 71.97  ?  45  LYS   A CA  1 
ATOM   349  C  C   . LYS   A 1 46  ? -9.270  -10.144 48.726 1.00 71.53  ?  45  LYS   A C   1 
ATOM   350  O  O   . LYS   A 1 46  ? -9.862  -11.231 48.747 1.00 69.47  ?  45  LYS   A O   1 
ATOM   351  C  CB  . LYS   A 1 46  ? -9.891  -8.233  47.206 1.00 68.73  ?  45  LYS   A CB  1 
ATOM   352  C  CG  . LYS   A 1 46  ? -9.851  -7.718  45.789 1.00 72.81  ?  45  LYS   A CG  1 
ATOM   353  C  CD  . LYS   A 1 46  ? -10.549 -6.370  45.618 1.00 81.23  ?  45  LYS   A CD  1 
ATOM   354  C  CE  . LYS   A 1 46  ? -11.840 -6.249  46.431 1.00 83.61  ?  45  LYS   A CE  1 
ATOM   355  N  NZ  . LYS   A 1 46  ? -12.665 -5.117  45.887 1.00 84.29  ?  45  LYS   A NZ  1 
ATOM   356  N  N   . PRO   A 1 47  ? -8.843  -9.567  49.864 1.00 68.27  ?  46  PRO   A N   1 
ATOM   357  C  CA  . PRO   A 1 47  ? -9.020  -10.263 51.143 1.00 72.35  ?  46  PRO   A CA  1 
ATOM   358  C  C   . PRO   A 1 47  ? -10.468 -10.417 51.562 1.00 71.31  ?  46  PRO   A C   1 
ATOM   359  O  O   . PRO   A 1 47  ? -11.100 -9.429  51.942 1.00 79.72  ?  46  PRO   A O   1 
ATOM   360  C  CB  . PRO   A 1 47  ? -8.254  -9.365  52.126 1.00 70.68  ?  46  PRO   A CB  1 
ATOM   361  C  CG  . PRO   A 1 47  ? -7.202  -8.734  51.272 1.00 63.89  ?  46  PRO   A CG  1 
ATOM   362  C  CD  . PRO   A 1 47  ? -7.977  -8.388  50.033 1.00 66.37  ?  46  PRO   A CD  1 
ATOM   363  N  N   . HIS   A 1 48  ? -11.011 -11.630 51.483 1.00 72.46  ?  47  HIS   A N   1 
ATOM   364  C  CA  . HIS   A 1 48  ? -12.219 -11.930 52.238 1.00 79.76  ?  47  HIS   A CA  1 
ATOM   365  C  C   . HIS   A 1 48  ? -11.883 -11.863 53.732 1.00 78.87  ?  47  HIS   A C   1 
ATOM   366  O  O   . HIS   A 1 48  ? -10.733 -12.047 54.145 1.00 70.37  ?  47  HIS   A O   1 
ATOM   367  C  CB  . HIS   A 1 48  ? -12.794 -13.309 51.853 1.00 81.61  ?  47  HIS   A CB  1 
ATOM   368  C  CG  . HIS   A 1 48  ? -13.308 -13.407 50.437 1.00 88.61  ?  47  HIS   A CG  1 
ATOM   369  N  ND1 . HIS   A 1 48  ? -12.741 -12.728 49.376 1.00 85.03  ?  47  HIS   A ND1 1 
ATOM   370  C  CD2 . HIS   A 1 48  ? -14.328 -14.134 49.909 1.00 94.76  ?  47  HIS   A CD2 1 
ATOM   371  C  CE1 . HIS   A 1 48  ? -13.396 -13.019 48.263 1.00 88.58  ?  47  HIS   A CE1 1 
ATOM   372  N  NE2 . HIS   A 1 48  ? -14.364 -13.869 48.558 1.00 90.02  ?  47  HIS   A NE2 1 
ATOM   373  N  N   . ASN   A 1 49  ? -12.893 -11.562 54.546 1.00 82.04  ?  48  ASN   A N   1 
ATOM   374  C  CA  . ASN   A 1 49  ? -12.638 -11.214 55.940 1.00 76.99  ?  48  ASN   A CA  1 
ATOM   375  C  C   . ASN   A 1 49  ? -12.174 -12.418 56.756 1.00 77.00  ?  48  ASN   A C   1 
ATOM   376  O  O   . ASN   A 1 49  ? -11.517 -12.236 57.790 1.00 75.99  ?  48  ASN   A O   1 
ATOM   377  C  CB  . ASN   A 1 49  ? -13.908 -10.569 56.515 1.00 79.94  ?  48  ASN   A CB  1 
ATOM   378  C  CG  . ASN   A 1 49  ? -13.862 -10.361 58.019 1.00 91.59  ?  48  ASN   A CG  1 
ATOM   379  O  OD1 . ASN   A 1 49  ? -14.907 -10.179 58.649 1.00 99.24  ?  48  ASN   A OD1 1 
ATOM   380  N  ND2 . ASN   A 1 49  ? -12.660 -10.358 58.603 1.00 94.28  ?  48  ASN   A ND2 1 
ATOM   381  N  N   . SER   A 1 50  ? -12.477 -13.639 56.302 1.00 79.77  ?  49  SER   A N   1 
ATOM   382  C  CA  . SER   A 1 50  ? -12.055 -14.860 56.985 1.00 73.79  ?  49  SER   A CA  1 
ATOM   383  C  C   . SER   A 1 50  ? -10.543 -15.025 57.028 1.00 73.29  ?  49  SER   A C   1 
ATOM   384  O  O   . SER   A 1 50  ? -10.053 -15.904 57.746 1.00 71.02  ?  49  SER   A O   1 
ATOM   385  C  CB  . SER   A 1 50  ? -12.673 -16.069 56.287 1.00 71.03  ?  49  SER   A CB  1 
ATOM   386  O  OG  . SER   A 1 50  ? -12.730 -15.846 54.882 1.00 78.14  ?  49  SER   A OG  1 
ATOM   387  N  N   . HIS   A 1 51  ? -9.799  -14.198 56.291 1.00 74.80  ?  50  HIS   A N   1 
ATOM   388  C  CA  . HIS   A 1 51  ? -8.365  -14.386 56.125 1.00 68.64  ?  50  HIS   A CA  1 
ATOM   389  C  C   . HIS   A 1 51  ? -7.532  -13.896 57.307 1.00 72.04  ?  50  HIS   A C   1 
ATOM   390  O  O   . HIS   A 1 51  ? -6.361  -14.281 57.398 1.00 71.35  ?  50  HIS   A O   1 
ATOM   391  C  CB  . HIS   A 1 51  ? -7.885  -13.682 54.856 1.00 65.04  ?  50  HIS   A CB  1 
ATOM   392  C  CG  . HIS   A 1 51  ? -8.339  -14.340 53.592 1.00 68.85  ?  50  HIS   A CG  1 
ATOM   393  N  ND1 . HIS   A 1 51  ? -8.447  -13.663 52.396 1.00 74.23  ?  50  HIS   A ND1 1 
ATOM   394  C  CD2 . HIS   A 1 51  ? -8.730  -15.610 53.339 1.00 66.97  ?  50  HIS   A CD2 1 
ATOM   395  C  CE1 . HIS   A 1 51  ? -8.876  -14.489 51.458 1.00 66.35  ?  50  HIS   A CE1 1 
ATOM   396  N  NE2 . HIS   A 1 51  ? -9.059  -15.676 52.006 1.00 67.07  ?  50  HIS   A NE2 1 
ATOM   397  N  N   . GLU   A 1 52  ? -8.076  -13.056 58.192 1.00 69.59  ?  51  GLU   A N   1 
ATOM   398  C  CA  . GLU   A 1 52  ? -7.311  -12.593 59.350 1.00 74.86  ?  51  GLU   A CA  1 
ATOM   399  C  C   . GLU   A 1 52  ? -6.551  -13.743 60.008 1.00 67.04  ?  51  GLU   A C   1 
ATOM   400  O  O   . GLU   A 1 52  ? -7.101  -14.824 60.229 1.00 68.72  ?  51  GLU   A O   1 
ATOM   401  C  CB  . GLU   A 1 52  ? -8.235  -11.912 60.377 1.00 76.32  ?  51  GLU   A CB  1 
ATOM   402  C  CG  . GLU   A 1 52  ? -7.530  -10.805 61.179 1.00 75.91  ?  51  GLU   A CG  1 
ATOM   403  C  CD  . GLU   A 1 52  ? -8.347  -10.278 62.346 1.00 83.01  ?  51  GLU   A CD  1 
ATOM   404  O  OE1 . GLU   A 1 52  ? -7.785  -10.122 63.465 1.00 72.71  ?  51  GLU   A OE1 1 
ATOM   405  O  OE2 . GLU   A 1 52  ? -9.553  -9.997  62.139 1.00 83.00  -1 51  GLU   A OE2 1 
ATOM   406  N  N   . GLY   A 1 53  ? -5.262  -13.520 60.263 1.00 63.39  ?  52  GLY   A N   1 
ATOM   407  C  CA  . GLY   A 1 53  ? -4.433  -14.476 60.968 1.00 68.90  ?  52  GLY   A CA  1 
ATOM   408  C  C   . GLY   A 1 53  ? -3.853  -15.596 60.129 1.00 72.01  ?  52  GLY   A C   1 
ATOM   409  O  O   . GLY   A 1 53  ? -2.882  -16.230 60.563 1.00 74.85  ?  52  GLY   A O   1 
ATOM   410  N  N   . LYS   A 1 54  ? -4.409  -15.861 58.946 1.00 68.29  ?  53  LYS   A N   1 
ATOM   411  C  CA  . LYS   A 1 54  ? -3.945  -16.931 58.077 1.00 66.60  ?  53  LYS   A CA  1 
ATOM   412  C  C   . LYS   A 1 54  ? -2.528  -16.652 57.564 1.00 68.48  ?  53  LYS   A C   1 
ATOM   413  O  O   . LYS   A 1 54  ? -2.041  -15.518 57.578 1.00 68.91  ?  53  LYS   A O   1 
ATOM   414  C  CB  . LYS   A 1 54  ? -4.895  -17.099 56.886 1.00 69.86  ?  53  LYS   A CB  1 
ATOM   415  C  CG  . LYS   A 1 54  ? -6.348  -17.560 57.185 1.00 67.75  ?  53  LYS   A CG  1 
ATOM   416  C  CD  . LYS   A 1 54  ? -6.496  -18.864 57.985 1.00 63.11  ?  53  LYS   A CD  1 
ATOM   417  C  CE  . LYS   A 1 54  ? -6.674  -18.571 59.489 1.00 86.36  ?  53  LYS   A CE  1 
ATOM   418  N  NZ  . LYS   A 1 54  ? -7.545  -19.540 60.236 1.00 86.18  ?  53  LYS   A NZ  1 
ATOM   419  N  N   . THR   A 1 55  ? -1.870  -17.707 57.086 1.00 66.93  ?  54  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 55  ? -0.515  -17.623 56.554 1.00 61.03  ?  54  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 55  ? -0.545  -17.805 55.041 1.00 60.83  ?  54  THR   A C   1 
ATOM   422  O  O   . THR   A 1 55  ? -1.238  -18.692 54.534 1.00 70.96  ?  54  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 55  ? 0.377   -18.678 57.212 1.00 59.24  ?  54  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 55  ? 0.553   -18.342 58.588 1.00 64.16  ?  54  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 55  ? 1.737   -18.730 56.556 1.00 65.95  ?  54  THR   A CG2 1 
ATOM   426  N  N   . PHE   A 1 56  ? 0.191   -16.973 54.318 1.00 56.14  ?  55  PHE   A N   1 
ATOM   427  C  CA  . PHE   A 1 56  ? 0.211   -17.034 52.863 1.00 60.39  ?  55  PHE   A CA  1 
ATOM   428  C  C   . PHE   A 1 56  ? 1.631   -17.252 52.358 1.00 63.11  ?  55  PHE   A C   1 
ATOM   429  O  O   . PHE   A 1 56  ? 2.600   -16.766 52.945 1.00 67.60  ?  55  PHE   A O   1 
ATOM   430  C  CB  . PHE   A 1 56  ? -0.320  -15.754 52.220 1.00 59.33  ?  55  PHE   A CB  1 
ATOM   431  C  CG  . PHE   A 1 56  ? -1.748  -15.433 52.554 1.00 61.38  ?  55  PHE   A CG  1 
ATOM   432  C  CD1 . PHE   A 1 56  ? -2.127  -15.125 53.854 1.00 56.18  ?  55  PHE   A CD1 1 
ATOM   433  C  CD2 . PHE   A 1 56  ? -2.709  -15.398 51.546 1.00 58.93  ?  55  PHE   A CD2 1 
ATOM   434  C  CE1 . PHE   A 1 56  ? -3.444  -14.815 54.153 1.00 58.42  ?  55  PHE   A CE1 1 
ATOM   435  C  CE2 . PHE   A 1 56  ? -4.023  -15.084 51.833 1.00 54.57  ?  55  PHE   A CE2 1 
ATOM   436  C  CZ  . PHE   A 1 56  ? -4.395  -14.791 53.140 1.00 59.48  ?  55  PHE   A CZ  1 
ATOM   437  N  N   . TYR   A 1 57  ? 1.757   -17.960 51.251 1.00 56.90  ?  56  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 3.057   -18.131 50.638 1.00 54.23  ?  56  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 3.235   -17.060 49.588 1.00 58.88  ?  56  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 2.283   -16.701 48.892 1.00 61.91  ?  56  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 3.196   -19.506 49.999 1.00 55.96  ?  56  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 3.678   -20.559 50.953 1.00 58.03  ?  56  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 4.893   -21.198 50.750 1.00 59.18  ?  56  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 2.916   -20.910 52.062 1.00 55.41  ?  56  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 5.326   -22.176 51.619 1.00 65.71  ?  56  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 3.331   -21.882 52.929 1.00 59.77  ?  56  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 4.536   -22.511 52.713 1.00 69.24  ?  56  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 4.951   -23.477 53.598 1.00 75.75  ?  56  TYR   A OH  1 
ATOM   449  N  N   . VAL   A 1 58  ? 4.461   -16.554 49.467 1.00 53.27  ?  57  VAL   A N   1 
ATOM   450  C  CA  . VAL   A 1 58  ? 4.763   -15.504 48.509 1.00 51.34  ?  57  VAL   A CA  1 
ATOM   451  C  C   . VAL   A 1 58  ? 6.051   -15.880 47.796 1.00 51.28  ?  57  VAL   A C   1 
ATOM   452  O  O   . VAL   A 1 58  ? 6.740   -16.828 48.173 1.00 50.83  ?  57  VAL   A O   1 
ATOM   453  C  CB  . VAL   A 1 58  ? 4.898   -14.118 49.180 1.00 54.88  ?  57  VAL   A CB  1 
ATOM   454  C  CG1 . VAL   A 1 58  ? 3.720   -13.834 50.114 1.00 51.74  ?  57  VAL   A CG1 1 
ATOM   455  C  CG2 . VAL   A 1 58  ? 6.209   -14.033 49.946 1.00 51.17  ?  57  VAL   A CG2 1 
ATOM   456  N  N   . LEU   A 1 59  ? 6.366   -15.129 46.748 1.00 50.29  ?  58  LEU   A N   1 
ATOM   457  C  CA  . LEU   A 1 59  ? 7.665   -15.305 46.133 1.00 47.84  ?  58  LEU   A CA  1 
ATOM   458  C  C   . LEU   A 1 59  ? 8.714   -14.464 46.866 1.00 60.52  ?  58  LEU   A C   1 
ATOM   459  O  O   . LEU   A 1 59  ? 8.395   -13.424 47.464 1.00 55.84  ?  58  LEU   A O   1 
ATOM   460  C  CB  . LEU   A 1 59  ? 7.632   -14.908 44.662 1.00 51.09  ?  58  LEU   A CB  1 
ATOM   461  C  CG  . LEU   A 1 59  ? 7.097   -15.877 43.608 1.00 53.88  ?  58  LEU   A CG  1 
ATOM   462  C  CD1 . LEU   A 1 59  ? 5.871   -16.635 44.103 1.00 54.89  ?  58  LEU   A CD1 1 
ATOM   463  C  CD2 . LEU   A 1 59  ? 6.755   -15.099 42.357 1.00 43.96  ?  58  LEU   A CD2 1 
ATOM   464  N  N   . PRO   A 1 60  ? 9.968   -14.918 46.858 1.00 56.73  ?  59  PRO   A N   1 
ATOM   465  C  CA  . PRO   A 1 60  ? 11.045  -14.136 47.467 1.00 58.58  ?  59  PRO   A CA  1 
ATOM   466  C  C   . PRO   A 1 60  ? 11.399  -12.860 46.719 1.00 61.74  ?  59  PRO   A C   1 
ATOM   467  O  O   . PRO   A 1 60  ? 12.366  -12.835 45.947 1.00 65.02  ?  59  PRO   A O   1 
ATOM   468  C  CB  . PRO   A 1 60  ? 12.220  -15.127 47.470 1.00 61.00  ?  59  PRO   A CB  1 
ATOM   469  C  CG  . PRO   A 1 60  ? 11.795  -16.258 46.566 1.00 51.17  ?  59  PRO   A CG  1 
ATOM   470  C  CD  . PRO   A 1 60  ? 10.342  -16.335 46.734 1.00 52.31  ?  59  PRO   A CD  1 
ATOM   471  N  N   . ASN   A 1 61  ? 10.662  -11.776 46.982 1.00 62.62  ?  60  ASN   A N   1 
ATOM   472  C  CA  . ASN   A 1 61  ? 10.943  -10.510 46.309 1.00 67.59  ?  60  ASN   A CA  1 
ATOM   473  C  C   . ASN   A 1 61  ? 12.174  -9.801  46.885 1.00 78.02  ?  60  ASN   A C   1 
ATOM   474  O  O   . ASN   A 1 61  ? 12.960  -9.228  46.121 1.00 84.28  ?  60  ASN   A O   1 
ATOM   475  C  CB  . ASN   A 1 61  ? 9.714   -9.601  46.374 1.00 60.35  ?  60  ASN   A CB  1 
ATOM   476  C  CG  . ASN   A 1 61  ? 9.040   -9.634  47.733 1.00 73.46  ?  60  ASN   A CG  1 
ATOM   477  O  OD1 . ASN   A 1 61  ? 9.710   -9.534  48.772 1.00 70.70  ?  60  ASN   A OD1 1 
ATOM   478  N  ND2 . ASN   A 1 61  ? 7.707   -9.810  47.741 1.00 76.31  ?  60  ASN   A ND2 1 
ATOM   479  N  N   . ASP   A 1 62  ? 12.383  -9.821  48.209 1.00 64.72  ?  61  ASP   A N   1 
ATOM   480  C  CA  . ASP   A 1 62  ? 13.532  -9.110  48.755 1.00 67.97  ?  61  ASP   A CA  1 
ATOM   481  C  C   . ASP   A 1 62  ? 14.737  -10.056 48.940 1.00 71.51  ?  61  ASP   A C   1 
ATOM   482  O  O   . ASP   A 1 62  ? 14.708  -11.226 48.562 1.00 70.02  ?  61  ASP   A O   1 
ATOM   483  C  CB  . ASP   A 1 62  ? 13.138  -8.399  50.050 1.00 67.28  ?  61  ASP   A CB  1 
ATOM   484  C  CG  . ASP   A 1 62  ? 12.718  -9.344  51.119 1.00 72.10  ?  61  ASP   A CG  1 
ATOM   485  O  OD1 . ASP   A 1 62  ? 13.586  -10.152 51.518 1.00 73.39  ?  61  ASP   A OD1 1 
ATOM   486  O  OD2 . ASP   A 1 62  ? 11.544  -9.267  51.580 1.00 75.97  -1 61  ASP   A OD2 1 
ATOM   487  N  N   . ASP   A 1 63  ? 15.836  -9.546  49.503 1.00 74.91  ?  62  ASP   A N   1 
ATOM   488  C  CA  . ASP   A 1 63  ? 16.996  -10.412 49.711 1.00 64.71  ?  62  ASP   A CA  1 
ATOM   489  C  C   . ASP   A 1 63  ? 16.899  -11.234 50.986 1.00 61.56  ?  62  ASP   A C   1 
ATOM   490  O  O   . ASP   A 1 63  ? 17.539  -12.280 51.079 1.00 60.87  ?  62  ASP   A O   1 
ATOM   491  C  CB  . ASP   A 1 63  ? 18.301  -9.617  49.758 1.00 66.87  ?  62  ASP   A CB  1 
ATOM   492  C  CG  . ASP   A 1 63  ? 19.522  -10.481 49.443 1.00 62.17  ?  62  ASP   A CG  1 
ATOM   493  O  OD1 . ASP   A 1 63  ? 19.504  -11.207 48.436 1.00 64.75  -1 62  ASP   A OD1 1 
ATOM   494  O  OD2 . ASP   A 1 63  ? 20.470  -10.505 50.249 1.00 56.48  ?  62  ASP   A OD2 1 
ATOM   495  N  N   . THR   A 1 64  ? 16.156  -10.781 51.992 1.00 64.59  ?  63  THR   A N   1 
ATOM   496  C  CA  . THR   A 1 64  ? 15.937  -11.633 53.159 1.00 60.66  ?  63  THR   A CA  1 
ATOM   497  C  C   . THR   A 1 64  ? 15.204  -12.907 52.770 1.00 58.42  ?  63  THR   A C   1 
ATOM   498  O  O   . THR   A 1 64  ? 15.637  -14.015 53.102 1.00 52.62  ?  63  THR   A O   1 
ATOM   499  C  CB  . THR   A 1 64  ? 15.153  -10.884 54.224 1.00 61.37  ?  63  THR   A CB  1 
ATOM   500  O  OG1 . THR   A 1 64  ? 15.918  -9.751  54.638 1.00 76.58  ?  63  THR   A OG1 1 
ATOM   501  C  CG2 . THR   A 1 64  ? 14.884  -11.794 55.422 1.00 63.36  ?  63  THR   A CG2 1 
ATOM   502  N  N   . LEU   A 1 65  ? 14.095  -12.761 52.045 1.00 60.88  ?  64  LEU   A N   1 
ATOM   503  C  CA  . LEU   A 1 65  ? 13.312  -13.911 51.617 1.00 57.85  ?  64  LEU   A CA  1 
ATOM   504  C  C   . LEU   A 1 65  ? 14.112  -14.837 50.706 1.00 49.26  ?  64  LEU   A C   1 
ATOM   505  O  O   . LEU   A 1 65  ? 14.023  -16.057 50.837 1.00 49.71  ?  64  LEU   A O   1 
ATOM   506  C  CB  . LEU   A 1 65  ? 12.033  -13.427 50.938 1.00 57.20  ?  64  LEU   A CB  1 
ATOM   507  C  CG  . LEU   A 1 65  ? 11.154  -12.674 51.938 1.00 54.32  ?  64  LEU   A CG  1 
ATOM   508  C  CD1 . LEU   A 1 65  ? 9.751   -12.558 51.426 1.00 50.99  ?  64  LEU   A CD1 1 
ATOM   509  C  CD2 . LEU   A 1 65  ? 11.173  -13.395 53.278 1.00 55.75  ?  64  LEU   A CD2 1 
ATOM   510  N  N   . ARG   A 1 66  ? 14.919  -14.288 49.799 1.00 52.94  ?  65  ARG   A N   1 
ATOM   511  C  CA  . ARG   A 1 66  ? 15.731  -15.149 48.934 1.00 53.55  ?  65  ARG   A CA  1 
ATOM   512  C  C   . ARG   A 1 66  ? 16.674  -16.019 49.751 1.00 51.84  ?  65  ARG   A C   1 
ATOM   513  O  O   . ARG   A 1 66  ? 16.964  -17.161 49.373 1.00 52.52  ?  65  ARG   A O   1 
ATOM   514  C  CB  . ARG   A 1 66  ? 16.545  -14.320 47.944 1.00 51.85  ?  65  ARG   A CB  1 
ATOM   515  C  CG  . ARG   A 1 66  ? 15.806  -13.937 46.696 1.00 47.87  ?  65  ARG   A CG  1 
ATOM   516  C  CD  . ARG   A 1 66  ? 16.804  -13.565 45.611 1.00 55.26  ?  65  ARG   A CD  1 
ATOM   517  N  NE  . ARG   A 1 66  ? 17.577  -12.363 45.912 1.00 64.97  ?  65  ARG   A NE  1 
ATOM   518  C  CZ  . ARG   A 1 66  ? 17.113  -11.121 45.834 1.00 68.68  ?  65  ARG   A CZ  1 
ATOM   519  N  NH1 . ARG   A 1 66  ? 15.878  -10.863 45.426 1.00 70.29  ?  65  ARG   A NH1 1 
ATOM   520  N  NH2 . ARG   A 1 66  ? 17.913  -10.111 46.167 1.00 68.41  ?  65  ARG   A NH2 1 
ATOM   521  N  N   . VAL   A 1 67  ? 17.181  -15.483 50.865 1.00 53.01  ?  66  VAL   A N   1 
ATOM   522  C  CA  . VAL   A 1 67  ? 17.966  -16.284 51.798 1.00 45.94  ?  66  VAL   A CA  1 
ATOM   523  C  C   . VAL   A 1 67  ? 17.049  -17.219 52.576 1.00 44.25  ?  66  VAL   A C   1 
ATOM   524  O  O   . VAL   A 1 67  ? 17.294  -18.424 52.644 1.00 42.49  ?  66  VAL   A O   1 
ATOM   525  C  CB  . VAL   A 1 67  ? 18.797  -15.373 52.730 1.00 43.12  ?  66  VAL   A CB  1 
ATOM   526  C  CG1 . VAL   A 1 67  ? 19.579  -16.201 53.763 1.00 38.18  ?  66  VAL   A CG1 1 
ATOM   527  C  CG2 . VAL   A 1 67  ? 19.773  -14.540 51.945 1.00 34.39  ?  66  VAL   A CG2 1 
ATOM   528  N  N   . GLU   A 1 68  ? 15.967  -16.680 53.140 1.00 42.93  ?  67  GLU   A N   1 
ATOM   529  C  CA  . GLU   A 1 68  ? 15.000  -17.535 53.879 1.00 41.25  ?  67  GLU   A CA  1 
ATOM   530  C  C   . GLU   A 1 68  ? 14.578  -18.722 53.000 1.00 50.17  ?  67  GLU   A C   1 
ATOM   531  O  O   . GLU   A 1 68  ? 14.322  -19.810 53.561 1.00 53.19  ?  67  GLU   A O   1 
ATOM   532  C  CB  . GLU   A 1 68  ? 13.769  -16.724 54.281 1.00 53.03  ?  67  GLU   A CB  1 
ATOM   533  C  CG  . GLU   A 1 68  ? 14.039  -15.760 55.430 1.00 50.60  ?  67  GLU   A CG  1 
ATOM   534  C  CD  . GLU   A 1 68  ? 12.790  -15.372 56.196 1.00 63.52  ?  67  GLU   A CD  1 
ATOM   535  O  OE1 . GLU   A 1 68  ? 11.685  -15.772 55.773 1.00 66.24  ?  67  GLU   A OE1 1 
ATOM   536  O  OE2 . GLU   A 1 68  ? 12.925  -14.669 57.219 1.00 43.23  -1 67  GLU   A OE2 1 
ATOM   537  N  N   . ALA   A 1 69  ? 14.517  -18.525 51.681 1.00 53.23  ?  68  ALA   A N   1 
ATOM   538  C  CA  . ALA   A 1 69  ? 14.056  -19.575 50.768 1.00 43.60  ?  68  ALA   A CA  1 
ATOM   539  C  C   . ALA   A 1 69  ? 15.162  -20.535 50.359 1.00 46.71  ?  68  ALA   A C   1 
ATOM   540  O  O   . ALA   A 1 69  ? 14.910  -21.737 50.185 1.00 46.92  ?  68  ALA   A O   1 
ATOM   541  C  CB  . ALA   A 1 69  ? 13.447  -18.973 49.510 1.00 43.50  ?  68  ALA   A CB  1 
ATOM   542  N  N   . PHE   A 1 70  ? 16.381  -20.037 50.148 1.00 47.01  ?  69  PHE   A N   1 
ATOM   543  C  CA  . PHE   A 1 70  ? 17.477  -20.966 49.893 1.00 43.21  ?  69  PHE   A CA  1 
ATOM   544  C  C   . PHE   A 1 70  ? 17.673  -21.902 51.079 1.00 44.16  ?  69  PHE   A C   1 
ATOM   545  O  O   . PHE   A 1 70  ? 17.795  -23.122 50.901 1.00 47.13  ?  69  PHE   A O   1 
ATOM   546  C  CB  . PHE   A 1 70  ? 18.790  -20.245 49.567 1.00 44.06  ?  69  PHE   A CB  1 
ATOM   547  C  CG  . PHE   A 1 70  ? 19.901  -21.204 49.235 1.00 47.32  ?  69  PHE   A CG  1 
ATOM   548  C  CD1 . PHE   A 1 70  ? 19.958  -21.808 47.971 1.00 47.81  ?  69  PHE   A CD1 1 
ATOM   549  C  CD2 . PHE   A 1 70  ? 20.823  -21.593 50.206 1.00 43.75  ?  69  PHE   A CD2 1 
ATOM   550  C  CE1 . PHE   A 1 70  ? 20.954  -22.729 47.663 1.00 47.02  ?  69  PHE   A CE1 1 
ATOM   551  C  CE2 . PHE   A 1 70  ? 21.814  -22.529 49.909 1.00 43.65  ?  69  PHE   A CE2 1 
ATOM   552  C  CZ  . PHE   A 1 70  ? 21.890  -23.093 48.631 1.00 42.15  ?  69  PHE   A CZ  1 
ATOM   553  N  N   . GLU   A 1 71  ? 17.669  -21.357 52.303 1.00 40.49  ?  70  GLU   A N   1 
ATOM   554  C  CA  . GLU   A 1 71  ? 17.838  -22.210 53.476 1.00 44.50  ?  70  GLU   A CA  1 
ATOM   555  C  C   . GLU   A 1 71  ? 16.764  -23.301 53.540 1.00 41.19  ?  70  GLU   A C   1 
ATOM   556  O  O   . GLU   A 1 71  ? 17.066  -24.442 53.878 1.00 42.08  ?  70  GLU   A O   1 
ATOM   557  C  CB  . GLU   A 1 71  ? 17.835  -21.389 54.771 1.00 45.74  ?  70  GLU   A CB  1 
ATOM   558  C  CG  . GLU   A 1 71  ? 18.599  -20.061 54.770 1.00 47.61  ?  70  GLU   A CG  1 
ATOM   559  C  CD  . GLU   A 1 71  ? 20.014  -20.141 55.337 1.00 64.20  ?  70  GLU   A CD  1 
ATOM   560  O  OE1 . GLU   A 1 71  ? 20.726  -21.122 55.003 1.00 64.34  ?  70  GLU   A OE1 1 
ATOM   561  O  OE2 . GLU   A 1 71  ? 20.408  -19.226 56.126 1.00 63.50  -1 70  GLU   A OE2 1 
ATOM   562  N  N   . TYR   A 1 72  ? 15.509  -22.986 53.206 1.00 47.96  ?  71  TYR   A N   1 
ATOM   563  C  CA  . TYR   A 1 72  ? 14.464  -24.010 53.324 1.00 43.86  ?  71  TYR   A CA  1 
ATOM   564  C  C   . TYR   A 1 72  ? 14.502  -25.035 52.196 1.00 43.86  ?  71  TYR   A C   1 
ATOM   565  O  O   . TYR   A 1 72  ? 14.230  -26.215 52.445 1.00 40.61  ?  71  TYR   A O   1 
ATOM   566  C  CB  . TYR   A 1 72  ? 13.073  -23.384 53.354 1.00 41.89  ?  71  TYR   A CB  1 
ATOM   567  C  CG  . TYR   A 1 72  ? 11.993  -24.322 53.845 1.00 44.46  ?  71  TYR   A CG  1 
ATOM   568  C  CD1 . TYR   A 1 72  ? 10.769  -24.433 53.182 1.00 49.19  ?  71  TYR   A CD1 1 
ATOM   569  C  CD2 . TYR   A 1 72  ? 12.181  -25.072 54.985 1.00 47.48  ?  71  TYR   A CD2 1 
ATOM   570  C  CE1 . TYR   A 1 72  ? 9.764   -25.281 53.645 1.00 45.42  ?  71  TYR   A CE1 1 
ATOM   571  C  CE2 . TYR   A 1 72  ? 11.199  -25.925 55.450 1.00 55.18  ?  71  TYR   A CE2 1 
ATOM   572  C  CZ  . TYR   A 1 72  ? 9.987   -26.036 54.785 1.00 53.96  ?  71  TYR   A CZ  1 
ATOM   573  O  OH  . TYR   A 1 72  ? 9.021   -26.912 55.304 1.00 55.09  ?  71  TYR   A OH  1 
ATOM   574  N  N   . TYR   A 1 73  ? 14.800  -24.604 50.944 1.00 44.24  ?  72  TYR   A N   1 
ATOM   575  C  CA  . TYR   A 1 73  ? 14.671  -25.455 49.754 1.00 42.18  ?  72  TYR   A CA  1 
ATOM   576  C  C   . TYR   A 1 73  ? 15.968  -25.734 49.010 1.00 42.59  ?  72  TYR   A C   1 
ATOM   577  O  O   . TYR   A 1 73  ? 15.970  -26.615 48.135 1.00 36.09  ?  72  TYR   A O   1 
ATOM   578  C  CB  . TYR   A 1 73  ? 13.726  -24.838 48.715 1.00 38.55  ?  72  TYR   A CB  1 
ATOM   579  C  CG  . TYR   A 1 73  ? 12.317  -24.533 49.121 1.00 41.01  ?  72  TYR   A CG  1 
ATOM   580  C  CD1 . TYR   A 1 73  ? 11.951  -23.249 49.462 1.00 41.42  ?  72  TYR   A CD1 1 
ATOM   581  C  CD2 . TYR   A 1 73  ? 11.327  -25.505 49.074 1.00 42.67  ?  72  TYR   A CD2 1 
ATOM   582  C  CE1 . TYR   A 1 73  ? 10.656  -22.948 49.792 1.00 44.90  ?  72  TYR   A CE1 1 
ATOM   583  C  CE2 . TYR   A 1 73  ? 10.023  -25.213 49.397 1.00 39.17  ?  72  TYR   A CE2 1 
ATOM   584  C  CZ  . TYR   A 1 73  ? 9.694   -23.929 49.749 1.00 45.36  ?  72  TYR   A CZ  1 
ATOM   585  O  OH  . TYR   A 1 73  ? 8.398   -23.598 50.072 1.00 57.60  ?  72  TYR   A OH  1 
ATOM   586  N  N   . HIS   A 1 74  ? 17.048  -24.984 49.283 1.00 44.66  ?  73  HIS   A N   1 
ATOM   587  C  CA  . HIS   A 1 74  ? 18.304  -25.075 48.518 1.00 43.62  ?  73  HIS   A CA  1 
ATOM   588  C  C   . HIS   A 1 74  ? 18.112  -24.669 47.062 1.00 46.10  ?  73  HIS   A C   1 
ATOM   589  O  O   . HIS   A 1 74  ? 18.724  -25.244 46.166 1.00 53.53  ?  73  HIS   A O   1 
ATOM   590  C  CB  . HIS   A 1 74  ? 18.908  -26.477 48.574 1.00 46.51  ?  73  HIS   A CB  1 
ATOM   591  C  CG  . HIS   A 1 74  ? 19.646  -26.767 49.839 1.00 45.54  ?  73  HIS   A CG  1 
ATOM   592  N  ND1 . HIS   A 1 74  ? 20.757  -27.582 49.877 1.00 44.43  ?  73  HIS   A ND1 1 
ATOM   593  C  CD2 . HIS   A 1 74  ? 19.435  -26.349 51.109 1.00 41.98  ?  73  HIS   A CD2 1 
ATOM   594  C  CE1 . HIS   A 1 74  ? 21.191  -27.664 51.119 1.00 46.57  ?  73  HIS   A CE1 1 
ATOM   595  N  NE2 . HIS   A 1 74  ? 20.415  -26.916 51.885 1.00 47.04  ?  73  HIS   A NE2 1 
ATOM   596  N  N   . THR   A 1 75  ? 17.253  -23.685 46.814 1.00 49.12  ?  74  THR   A N   1 
ATOM   597  C  CA  . THR   A 1 75  ? 17.046  -23.174 45.470 1.00 52.01  ?  74  THR   A CA  1 
ATOM   598  C  C   . THR   A 1 75  ? 17.169  -21.663 45.475 1.00 50.15  ?  74  THR   A C   1 
ATOM   599  O  O   . THR   A 1 75  ? 16.846  -21.004 46.464 1.00 52.44  ?  74  THR   A O   1 
ATOM   600  C  CB  . THR   A 1 75  ? 15.672  -23.557 44.883 1.00 53.45  ?  74  THR   A CB  1 
ATOM   601  O  OG1 . THR   A 1 75  ? 15.776  -23.578 43.453 1.00 57.22  ?  74  THR   A OG1 1 
ATOM   602  C  CG2 . THR   A 1 75  ? 14.614  -22.541 45.264 1.00 42.73  ?  74  THR   A CG2 1 
ATOM   603  N  N   . THR   A 1 76  ? 17.666  -21.122 44.364 1.00 57.85  ?  75  THR   A N   1 
ATOM   604  C  CA  . THR   A 1 76  ? 17.592  -19.690 44.109 1.00 57.52  ?  75  THR   A CA  1 
ATOM   605  C  C   . THR   A 1 76  ? 16.569  -19.349 43.046 1.00 61.08  ?  75  THR   A C   1 
ATOM   606  O  O   . THR   A 1 76  ? 16.027  -18.239 43.074 1.00 70.02  ?  75  THR   A O   1 
ATOM   607  C  CB  . THR   A 1 76  ? 18.944  -19.131 43.671 1.00 52.92  ?  75  THR   A CB  1 
ATOM   608  O  OG1 . THR   A 1 76  ? 19.052  -19.267 42.257 1.00 70.03  ?  75  THR   A OG1 1 
ATOM   609  C  CG2 . THR   A 1 76  ? 20.078  -19.893 44.326 1.00 58.34  ?  75  THR   A CG2 1 
ATOM   610  N  N   . ASP   A 1 77  ? 16.293  -20.307 42.116 1.00 58.81  ?  76  ASP   A N   1 
ATOM   611  C  CA  . ASP   A 1 77  ? 15.302  -20.295 41.037 1.00 51.00  ?  76  ASP   A CA  1 
ATOM   612  C  C   . ASP   A 1 77  ? 13.960  -19.743 41.499 1.00 56.27  ?  76  ASP   A C   1 
ATOM   613  O  O   . ASP   A 1 77  ? 13.289  -20.347 42.347 1.00 58.60  ?  76  ASP   A O   1 
ATOM   614  C  CB  . ASP   A 1 77  ? 15.115  -21.712 40.482 1.00 52.01  ?  76  ASP   A CB  1 
ATOM   615  C  CG  . ASP   A 1 77  ? 14.238  -21.759 39.212 1.00 60.88  ?  76  ASP   A CG  1 
ATOM   616  O  OD1 . ASP   A 1 77  ? 14.333  -22.787 38.479 1.00 55.01  ?  76  ASP   A OD1 1 
ATOM   617  O  OD2 . ASP   A 1 77  ? 13.462  -20.793 38.953 1.00 53.32  -1 76  ASP   A OD2 1 
ATOM   618  N  N   . PRO   A 1 78  ? 13.523  -18.601 40.966 1.00 62.97  ?  77  PRO   A N   1 
ATOM   619  C  CA  . PRO   A 1 78  ? 12.253  -18.020 41.443 1.00 59.96  ?  77  PRO   A CA  1 
ATOM   620  C  C   . PRO   A 1 78  ? 11.024  -18.742 40.929 1.00 57.54  ?  77  PRO   A C   1 
ATOM   621  O  O   . PRO   A 1 78  ? 9.939   -18.560 41.505 1.00 59.81  ?  77  PRO   A O   1 
ATOM   622  C  CB  . PRO   A 1 78  ? 12.312  -16.568 40.949 1.00 59.09  ?  77  PRO   A CB  1 
ATOM   623  C  CG  . PRO   A 1 78  ? 13.750  -16.368 40.426 1.00 57.70  ?  77  PRO   A CG  1 
ATOM   624  C  CD  . PRO   A 1 78  ? 14.256  -17.712 40.048 1.00 55.18  ?  77  PRO   A CD  1 
ATOM   625  N  N   . SER   A 1 79  ? 11.165  -19.575 39.892 1.00 54.91  ?  78  SER   A N   1 
ATOM   626  C  CA  . SER   A 1 79  ? 10.054  -20.396 39.415 1.00 59.28  ?  78  SER   A CA  1 
ATOM   627  C  C   . SER   A 1 79  ? 9.700   -21.531 40.373 1.00 60.53  ?  78  SER   A C   1 
ATOM   628  O  O   . SER   A 1 79  ? 8.601   -22.102 40.261 1.00 54.63  ?  78  SER   A O   1 
ATOM   629  C  CB  . SER   A 1 79  ? 10.398  -21.005 38.063 1.00 58.05  ?  78  SER   A CB  1 
ATOM   630  O  OG  . SER   A 1 79  ? 11.353  -22.040 38.234 1.00 62.86  ?  78  SER   A OG  1 
ATOM   631  N  N   . PHE   A 1 80  ? 10.613  -21.879 41.291 1.00 59.60  ?  79  PHE   A N   1 
ATOM   632  C  CA  . PHE   A 1 80  ? 10.417  -23.038 42.161 1.00 56.89  ?  79  PHE   A CA  1 
ATOM   633  C  C   . PHE   A 1 80  ? 9.066   -23.004 42.854 1.00 51.69  ?  79  PHE   A C   1 
ATOM   634  O  O   . PHE   A 1 80  ? 8.299   -23.971 42.790 1.00 50.15  ?  79  PHE   A O   1 
ATOM   635  C  CB  . PHE   A 1 80  ? 11.533  -23.120 43.201 1.00 50.78  ?  79  PHE   A CB  1 
ATOM   636  C  CG  . PHE   A 1 80  ? 11.571  -24.425 43.942 1.00 48.73  ?  79  PHE   A CG  1 
ATOM   637  C  CD1 . PHE   A 1 80  ? 12.387  -25.451 43.516 1.00 43.31  ?  79  PHE   A CD1 1 
ATOM   638  C  CD2 . PHE   A 1 80  ? 10.781  -24.621 45.082 1.00 49.77  ?  79  PHE   A CD2 1 
ATOM   639  C  CE1 . PHE   A 1 80  ? 12.424  -26.645 44.215 1.00 47.45  ?  79  PHE   A CE1 1 
ATOM   640  C  CE2 . PHE   A 1 80  ? 10.796  -25.810 45.773 1.00 38.36  ?  79  PHE   A CE2 1 
ATOM   641  C  CZ  . PHE   A 1 80  ? 11.622  -26.824 45.348 1.00 44.27  ?  79  PHE   A CZ  1 
ATOM   642  N  N   . LEU   A 1 81  ? 8.755   -21.908 43.539 1.00 49.93  ?  80  LEU   A N   1 
ATOM   643  C  CA  . LEU   A 1 81  ? 7.500   -21.880 44.278 1.00 51.04  ?  80  LEU   A CA  1 
ATOM   644  C  C   . LEU   A 1 81  ? 6.338   -22.246 43.359 1.00 54.77  ?  80  LEU   A C   1 
ATOM   645  O  O   . LEU   A 1 81  ? 5.523   -23.121 43.685 1.00 54.96  ?  80  LEU   A O   1 
ATOM   646  C  CB  . LEU   A 1 81  ? 7.311   -20.506 44.906 1.00 51.27  ?  80  LEU   A CB  1 
ATOM   647  C  CG  . LEU   A 1 81  ? 6.639   -20.499 46.260 1.00 59.99  ?  80  LEU   A CG  1 
ATOM   648  C  CD1 . LEU   A 1 81  ? 7.716   -20.845 47.362 1.00 74.70  ?  80  LEU   A CD1 1 
ATOM   649  C  CD2 . LEU   A 1 81  ? 5.983   -19.134 46.475 1.00 67.10  ?  80  LEU   A CD2 1 
ATOM   650  N  N   . GLY   A 1 82  ? 6.325   -21.673 42.149 1.00 49.23  ?  81  GLY   A N   1 
ATOM   651  C  CA  . GLY   A 1 82  ? 5.185   -21.848 41.269 1.00 42.61  ?  81  GLY   A CA  1 
ATOM   652  C  C   . GLY   A 1 82  ? 5.092   -23.252 40.704 1.00 50.68  ?  81  GLY   A C   1 
ATOM   653  O  O   . GLY   A 1 82  ? 4.013   -23.859 40.696 1.00 52.30  ?  81  GLY   A O   1 
ATOM   654  N  N   . ARG   A 1 83  ? 6.222   -23.792 40.225 1.00 46.02  ?  82  ARG   A N   1 
ATOM   655  C  CA  . ARG   A 1 83  ? 6.244   -25.179 39.767 1.00 38.05  ?  82  ARG   A CA  1 
ATOM   656  C  C   . ARG   A 1 83  ? 5.755   -26.117 40.864 1.00 44.50  ?  82  ARG   A C   1 
ATOM   657  O  O   . ARG   A 1 83  ? 4.876   -26.954 40.631 1.00 47.00  ?  82  ARG   A O   1 
ATOM   658  C  CB  . ARG   A 1 83  ? 7.648   -25.549 39.295 1.00 41.09  ?  82  ARG   A CB  1 
ATOM   659  C  CG  . ARG   A 1 83  ? 8.224   -24.533 38.292 1.00 50.66  ?  82  ARG   A CG  1 
ATOM   660  C  CD  . ARG   A 1 83  ? 9.422   -25.049 37.531 1.00 44.07  ?  82  ARG   A CD  1 
ATOM   661  N  NE  . ARG   A 1 83  ? 10.651  -24.929 38.310 1.00 55.47  ?  82  ARG   A NE  1 
ATOM   662  C  CZ  . ARG   A 1 83  ? 11.336  -25.971 38.764 1.00 54.85  ?  82  ARG   A CZ  1 
ATOM   663  N  NH1 . ARG   A 1 83  ? 10.904  -27.212 38.577 1.00 53.17  ?  82  ARG   A NH1 1 
ATOM   664  N  NH2 . ARG   A 1 83  ? 12.479  -25.765 39.424 1.00 53.54  ?  82  ARG   A NH2 1 
ATOM   665  N  N   . TYR   A 1 84  ? 6.283   -25.952 42.082 1.00 47.70  ?  83  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 5.855   -26.746 43.235 1.00 47.79  ?  83  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 4.354   -26.607 43.505 1.00 49.19  ?  83  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 3.641   -27.617 43.601 1.00 42.72  ?  83  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 6.687   -26.334 44.456 1.00 49.92  ?  83  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 6.234   -26.864 45.802 1.00 51.27  ?  83  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 5.743   -28.156 45.950 1.00 50.84  ?  83  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 6.315   -26.062 46.940 1.00 55.91  ?  83  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 5.324   -28.632 47.201 1.00 51.80  ?  83  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 5.903   -26.519 48.181 1.00 55.88  ?  83  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 5.409   -27.806 48.310 1.00 59.35  ?  83  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 5.008   -28.261 49.554 1.00 60.27  ?  83  TYR   A OH  1 
ATOM   677  N  N   . MET   A 1 85  ? 3.858   -25.362 43.648 1.00 50.61  ?  84  MET   A N   1 
ATOM   678  C  CA  . MET   A 1 85  ? 2.433   -25.135 43.933 1.00 47.24  ?  84  MET   A CA  1 
ATOM   679  C  C   . MET   A 1 85  ? 1.558   -25.770 42.866 1.00 46.86  ?  84  MET   A C   1 
ATOM   680  O  O   . MET   A 1 85  ? 0.430   -26.196 43.141 1.00 44.56  ?  84  MET   A O   1 
ATOM   681  C  CB  . MET   A 1 85  ? 2.150   -23.636 43.997 1.00 48.85  ?  84  MET   A CB  1 
ATOM   682  C  CG  . MET   A 1 85  ? 2.303   -22.965 45.364 1.00 57.84  ?  84  MET   A CG  1 
ATOM   683  S  SD  . MET   A 1 85  ? 1.863   -23.905 46.840 1.00 59.86  ?  84  MET   A SD  1 
ATOM   684  C  CE  . MET   A 1 85  ? 3.104   -23.273 47.957 1.00 64.31  ?  84  MET   A CE  1 
ATOM   685  N  N   . SER   A 1 86  ? 2.076   -25.822 41.639 1.00 52.24  ?  85  SER   A N   1 
ATOM   686  C  CA  . SER   A 1 86  ? 1.363   -26.402 40.511 1.00 51.08  ?  85  SER   A CA  1 
ATOM   687  C  C   . SER   A 1 86  ? 1.289   -27.918 40.623 1.00 52.41  ?  85  SER   A C   1 
ATOM   688  O  O   . SER   A 1 86  ? 0.230   -28.518 40.390 1.00 56.78  ?  85  SER   A O   1 
ATOM   689  C  CB  . SER   A 1 86  ? 2.061   -26.007 39.214 1.00 46.24  ?  85  SER   A CB  1 
ATOM   690  O  OG  . SER   A 1 86  ? 1.296   -26.428 38.104 1.00 59.31  ?  85  SER   A OG  1 
ATOM   691  N  N   . ALA   A 1 87  ? 2.414   -28.561 40.957 1.00 51.23  ?  86  ALA   A N   1 
ATOM   692  C  CA  . ALA   A 1 87  ? 2.386   -29.997 41.216 1.00 44.61  ?  86  ALA   A CA  1 
ATOM   693  C  C   . ALA   A 1 87  ? 1.485   -30.319 42.398 1.00 47.11  ?  86  ALA   A C   1 
ATOM   694  O  O   . ALA   A 1 87  ? 0.725   -31.297 42.355 1.00 46.44  ?  86  ALA   A O   1 
ATOM   695  C  CB  . ALA   A 1 87  ? 3.798   -30.521 41.461 1.00 41.76  ?  86  ALA   A CB  1 
ATOM   696  N  N   . LEU   A 1 88  ? 1.544   -29.500 43.460 1.00 41.89  ?  87  LEU   A N   1 
ATOM   697  C  CA  . LEU   A 1 88  ? 0.768   -29.812 44.654 1.00 43.69  ?  87  LEU   A CA  1 
ATOM   698  C  C   . LEU   A 1 88  ? -0.720  -29.860 44.352 1.00 47.66  ?  87  LEU   A C   1 
ATOM   699  O  O   . LEU   A 1 88  ? -1.457  -30.633 44.982 1.00 51.31  ?  87  LEU   A O   1 
ATOM   700  C  CB  . LEU   A 1 88  ? 1.043   -28.803 45.766 1.00 47.09  ?  87  LEU   A CB  1 
ATOM   701  C  CG  . LEU   A 1 88  ? 0.381   -29.146 47.107 1.00 48.22  ?  87  LEU   A CG  1 
ATOM   702  C  CD1 . LEU   A 1 88  ? 0.846   -30.504 47.581 1.00 49.78  ?  87  LEU   A CD1 1 
ATOM   703  C  CD2 . LEU   A 1 88  ? 0.679   -28.082 48.132 1.00 50.85  ?  87  LEU   A CD2 1 
ATOM   704  N  N   . ASN   A 1 89  ? -1.177  -29.056 43.392 1.00 50.99  ?  88  ASN   A N   1 
ATOM   705  C  CA  . ASN   A 1 89  ? -2.583  -29.088 43.027 1.00 45.54  ?  88  ASN   A CA  1 
ATOM   706  C  C   . ASN   A 1 89  ? -2.981  -30.467 42.563 1.00 47.08  ?  88  ASN   A C   1 
ATOM   707  O  O   . ASN   A 1 89  ? -4.120  -30.864 42.785 1.00 53.08  ?  88  ASN   A O   1 
ATOM   708  C  CB  . ASN   A 1 89  ? -2.884  -28.042 41.949 1.00 45.19  ?  88  ASN   A CB  1 
ATOM   709  C  CG  . ASN   A 1 89  ? -3.521  -26.784 42.511 1.00 55.91  ?  88  ASN   A CG  1 
ATOM   710  O  OD1 . ASN   A 1 89  ? -4.160  -26.809 43.562 1.00 72.38  ?  88  ASN   A OD1 1 
ATOM   711  N  ND2 . ASN   A 1 89  ? -3.292  -25.658 41.847 1.00 58.56  ?  88  ASN   A ND2 1 
ATOM   712  N  N   . HIS   A 1 90  ? -2.064  -31.217 41.926 1.00 47.86  ?  89  HIS   A N   1 
ATOM   713  C  CA  . HIS   A 1 90  ? -2.392  -32.590 41.541 1.00 43.26  ?  89  HIS   A CA  1 
ATOM   714  C  C   . HIS   A 1 90  ? -2.215  -33.552 42.703 1.00 47.97  ?  89  HIS   A C   1 
ATOM   715  O  O   . HIS   A 1 90  ? -3.111  -34.348 43.012 1.00 50.27  ?  89  HIS   A O   1 
ATOM   716  C  CB  . HIS   A 1 90  ? -1.514  -33.069 40.400 1.00 46.00  ?  89  HIS   A CB  1 
ATOM   717  C  CG  . HIS   A 1 90  ? -1.647  -32.277 39.148 1.00 49.71  ?  89  HIS   A CG  1 
ATOM   718  N  ND1 . HIS   A 1 90  ? -2.671  -32.476 38.247 1.00 50.73  ?  89  HIS   A ND1 1 
ATOM   719  C  CD2 . HIS   A 1 90  ? -0.863  -31.311 38.622 1.00 51.26  ?  89  HIS   A CD2 1 
ATOM   720  C  CE1 . HIS   A 1 90  ? -2.518  -31.658 37.223 1.00 51.85  ?  89  HIS   A CE1 1 
ATOM   721  N  NE2 . HIS   A 1 90  ? -1.426  -30.941 37.422 1.00 52.95  ?  89  HIS   A NE2 1 
ATOM   722  N  N   . THR   A 1 91  ? -1.047  -33.510 43.342 1.00 46.77  ?  90  THR   A N   1 
ATOM   723  C  CA  . THR   A 1 91  ? -0.717  -34.537 44.321 1.00 45.62  ?  90  THR   A CA  1 
ATOM   724  C  C   . THR   A 1 91  ? -1.631  -34.483 45.537 1.00 47.68  ?  90  THR   A C   1 
ATOM   725  O  O   . THR   A 1 91  ? -1.840  -35.525 46.176 1.00 50.09  ?  90  THR   A O   1 
ATOM   726  C  CB  . THR   A 1 91  ? 0.751   -34.423 44.725 1.00 44.34  ?  90  THR   A CB  1 
ATOM   727  O  OG1 . THR   A 1 91  ? 0.930   -33.287 45.589 1.00 41.34  ?  90  THR   A OG1 1 
ATOM   728  C  CG2 . THR   A 1 91  ? 1.596   -34.253 43.462 1.00 41.66  ?  90  THR   A CG2 1 
ATOM   729  N  N   . LYS   A 1 92  ? -2.203  -33.310 45.870 1.00 40.24  ?  91  LYS   A N   1 
ATOM   730  C  CA  . LYS   A 1 92  ? -3.168  -33.295 46.972 1.00 44.43  ?  91  LYS   A CA  1 
ATOM   731  C  C   . LYS   A 1 92  ? -4.385  -34.161 46.672 1.00 47.83  ?  91  LYS   A C   1 
ATOM   732  O  O   . LYS   A 1 92  ? -5.074  -34.574 47.609 1.00 47.65  ?  91  LYS   A O   1 
ATOM   733  C  CB  . LYS   A 1 92  ? -3.645  -31.877 47.318 1.00 48.94  ?  91  LYS   A CB  1 
ATOM   734  C  CG  . LYS   A 1 92  ? -2.657  -31.025 48.136 1.00 54.33  ?  91  LYS   A CG  1 
ATOM   735  C  CD  . LYS   A 1 92  ? -3.386  -30.077 49.125 1.00 57.74  ?  91  LYS   A CD  1 
ATOM   736  C  CE  . LYS   A 1 92  ? -2.564  -28.825 49.481 1.00 54.70  ?  91  LYS   A CE  1 
ATOM   737  N  NZ  . LYS   A 1 92  ? -2.953  -27.641 48.659 1.00 60.29  ?  91  LYS   A NZ  1 
ATOM   738  N  N   . LYS   A 1 93  ? -4.666  -34.456 45.393 1.00 50.97  ?  92  LYS   A N   1 
ATOM   739  C  CA  . LYS   A 1 93  ? -5.807  -35.299 45.028 1.00 50.54  ?  92  LYS   A CA  1 
ATOM   740  C  C   . LYS   A 1 93  ? -5.466  -36.780 44.913 1.00 52.76  ?  92  LYS   A C   1 
ATOM   741  O  O   . LYS   A 1 93  ? -6.380  -37.618 44.969 1.00 45.68  ?  92  LYS   A O   1 
ATOM   742  C  CB  . LYS   A 1 93  ? -6.428  -34.858 43.700 1.00 47.26  ?  92  LYS   A CB  1 
ATOM   743  C  CG  . LYS   A 1 93  ? -7.229  -33.564 43.751 1.00 60.89  ?  92  LYS   A CG  1 
ATOM   744  C  CD  . LYS   A 1 93  ? -6.335  -32.346 43.730 1.00 61.44  ?  92  LYS   A CD  1 
ATOM   745  C  CE  . LYS   A 1 93  ? -7.034  -31.078 43.158 1.00 66.36  ?  92  LYS   A CE  1 
ATOM   746  N  NZ  . LYS   A 1 93  ? -8.030  -30.445 44.085 1.00 73.41  ?  92  LYS   A NZ  1 
ATOM   747  N  N   . TRP   A 1 94  ? -4.196  -37.127 44.722 1.00 49.88  ?  93  TRP   A N   1 
ATOM   748  C  CA  . TRP   A 1 94  ? -3.817  -38.528 44.713 1.00 46.11  ?  93  TRP   A CA  1 
ATOM   749  C  C   . TRP   A 1 94  ? -4.112  -39.163 46.069 1.00 46.87  ?  93  TRP   A C   1 
ATOM   750  O  O   . TRP   A 1 94  ? -4.168  -38.494 47.111 1.00 45.46  ?  93  TRP   A O   1 
ATOM   751  C  CB  . TRP   A 1 94  ? -2.329  -38.697 44.397 1.00 42.75  ?  93  TRP   A CB  1 
ATOM   752  C  CG  . TRP   A 1 94  ? -1.936  -38.198 43.039 1.00 45.37  ?  93  TRP   A CG  1 
ATOM   753  C  CD1 . TRP   A 1 94  ? -2.769  -37.791 42.049 1.00 40.63  ?  93  TRP   A CD1 1 
ATOM   754  C  CD2 . TRP   A 1 94  ? -0.599  -38.057 42.524 1.00 40.92  ?  93  TRP   A CD2 1 
ATOM   755  N  NE1 . TRP   A 1 94  ? -2.038  -37.401 40.951 1.00 42.70  ?  93  TRP   A NE1 1 
ATOM   756  C  CE2 . TRP   A 1 94  ? -0.707  -37.559 41.217 1.00 37.54  ?  93  TRP   A CE2 1 
ATOM   757  C  CE3 . TRP   A 1 94  ? 0.672   -38.297 43.050 1.00 41.17  ?  93  TRP   A CE3 1 
ATOM   758  C  CZ2 . TRP   A 1 94  ? 0.397   -37.303 40.425 1.00 40.26  ?  93  TRP   A CZ2 1 
ATOM   759  C  CZ3 . TRP   A 1 94  ? 1.781   -38.032 42.262 1.00 45.19  ?  93  TRP   A CZ3 1 
ATOM   760  C  CH2 . TRP   A 1 94  ? 1.638   -37.543 40.965 1.00 43.66  ?  93  TRP   A CH2 1 
ATOM   761  N  N   . LYS   A 1 95  ? -4.281  -40.481 46.032 1.00 48.65  ?  94  LYS   A N   1 
ATOM   762  C  CA  . LYS   A 1 95  ? -4.378  -41.351 47.192 1.00 43.18  ?  94  LYS   A CA  1 
ATOM   763  C  C   . LYS   A 1 95  ? -3.021  -41.972 47.484 1.00 46.11  ?  94  LYS   A C   1 
ATOM   764  O  O   . LYS   A 1 95  ? -2.241  -42.260 46.569 1.00 49.99  ?  94  LYS   A O   1 
ATOM   765  C  CB  . LYS   A 1 95  ? -5.404  -42.449 46.952 1.00 45.95  ?  94  LYS   A CB  1 
ATOM   766  C  CG  . LYS   A 1 95  ? -6.751  -41.912 46.578 1.00 48.75  ?  94  LYS   A CG  1 
ATOM   767  C  CD  . LYS   A 1 95  ? -7.453  -41.410 47.815 1.00 50.21  ?  94  LYS   A CD  1 
ATOM   768  C  CE  . LYS   A 1 95  ? -8.151  -40.078 47.585 1.00 54.03  ?  94  LYS   A CE  1 
ATOM   769  N  NZ  . LYS   A 1 95  ? -8.955  -39.741 48.802 1.00 75.35  ?  94  LYS   A NZ  1 
ATOM   770  N  N   . TYR   A 1 96  ? -2.745  -42.181 48.774 1.00 43.91  ?  95  TYR   A N   1 
ATOM   771  C  CA  . TYR   A 1 96  ? -1.439  -42.635 49.250 1.00 37.33  ?  95  TYR   A CA  1 
ATOM   772  C  C   . TYR   A 1 96  ? -1.639  -43.760 50.252 1.00 44.56  ?  95  TYR   A C   1 
ATOM   773  O  O   . TYR   A 1 96  ? -1.410  -43.592 51.460 1.00 46.94  ?  95  TYR   A O   1 
ATOM   774  C  CB  . TYR   A 1 96  ? -0.666  -41.473 49.876 1.00 43.30  ?  95  TYR   A CB  1 
ATOM   775  C  CG  . TYR   A 1 96  ? -0.360  -40.339 48.930 1.00 38.05  ?  95  TYR   A CG  1 
ATOM   776  C  CD1 . TYR   A 1 96  ? 0.761   -40.378 48.102 1.00 39.57  ?  95  TYR   A CD1 1 
ATOM   777  C  CD2 . TYR   A 1 96  ? -1.204  -39.259 48.834 1.00 37.14  ?  95  TYR   A CD2 1 
ATOM   778  C  CE1 . TYR   A 1 96  ? 1.051   -39.344 47.239 1.00 37.29  ?  95  TYR   A CE1 1 
ATOM   779  C  CE2 . TYR   A 1 96  ? -0.937  -38.227 47.968 1.00 42.30  ?  95  TYR   A CE2 1 
ATOM   780  C  CZ  . TYR   A 1 96  ? 0.196   -38.273 47.177 1.00 42.01  ?  95  TYR   A CZ  1 
ATOM   781  O  OH  . TYR   A 1 96  ? 0.448   -37.232 46.319 1.00 48.57  ?  95  TYR   A OH  1 
ATOM   782  N  N   . PRO   A 1 97  ? -2.075  -44.927 49.789 1.00 45.38  ?  96  PRO   A N   1 
ATOM   783  C  CA  . PRO   A 1 97  ? -2.373  -46.020 50.720 1.00 41.56  ?  96  PRO   A CA  1 
ATOM   784  C  C   . PRO   A 1 97  ? -1.133  -46.552 51.433 1.00 41.04  ?  96  PRO   A C   1 
ATOM   785  O  O   . PRO   A 1 97  ? 0.022   -46.283 51.086 1.00 38.30  ?  96  PRO   A O   1 
ATOM   786  C  CB  . PRO   A 1 97  ? -2.978  -47.076 49.805 1.00 32.13  ?  96  PRO   A CB  1 
ATOM   787  C  CG  . PRO   A 1 97  ? -2.248  -46.866 48.544 1.00 40.96  ?  96  PRO   A CG  1 
ATOM   788  C  CD  . PRO   A 1 97  ? -2.284  -45.357 48.401 1.00 43.02  ?  96  PRO   A CD  1 
ATOM   789  N  N   . GLN   A 1 98  ? -1.413  -47.309 52.489 1.00 43.97  ?  97  GLN   A N   1 
ATOM   790  C  CA  . GLN   A 1 98  ? -0.429  -48.172 53.116 1.00 41.49  ?  97  GLN   A CA  1 
ATOM   791  C  C   . GLN   A 1 98  ? -0.499  -49.517 52.428 1.00 43.09  ?  97  GLN   A C   1 
ATOM   792  O  O   . GLN   A 1 98  ? -1.564  -50.145 52.386 1.00 47.34  ?  97  GLN   A O   1 
ATOM   793  C  CB  . GLN   A 1 98  ? -0.703  -48.334 54.603 1.00 45.15  ?  97  GLN   A CB  1 
ATOM   794  C  CG  . GLN   A 1 98  ? -0.536  -47.071 55.363 1.00 44.89  ?  97  GLN   A CG  1 
ATOM   795  C  CD  . GLN   A 1 98  ? 0.891   -46.676 55.418 1.00 53.71  ?  97  GLN   A CD  1 
ATOM   796  O  OE1 . GLN   A 1 98  ? 1.306   -45.711 54.748 1.00 44.52  ?  97  GLN   A OE1 1 
ATOM   797  N  NE2 . GLN   A 1 98  ? 1.689   -47.439 56.201 1.00 56.03  ?  97  GLN   A NE2 1 
ATOM   798  N  N   . VAL   A 1 99  ? 0.623   -49.951 51.883 1.00 39.82  ?  98  VAL   A N   1 
ATOM   799  C  CA  . VAL   A 1 99  ? 0.733   -51.247 51.245 1.00 38.38  ?  98  VAL   A CA  1 
ATOM   800  C  C   . VAL   A 1 99  ? 1.936   -51.907 51.876 1.00 41.93  ?  98  VAL   A C   1 
ATOM   801  O  O   . VAL   A 1 99  ? 3.062   -51.416 51.710 1.00 42.85  ?  98  VAL   A O   1 
ATOM   802  C  CB  . VAL   A 1 99  ? 0.932   -51.137 49.721 1.00 39.94  ?  98  VAL   A CB  1 
ATOM   803  C  CG1 . VAL   A 1 99  ? 1.035   -52.526 49.079 1.00 40.50  ?  98  VAL   A CG1 1 
ATOM   804  C  CG2 . VAL   A 1 99  ? -0.167  -50.334 49.090 1.00 41.16  ?  98  VAL   A CG2 1 
ATOM   805  N  N   . ASN   A 1 100 ? 1.713   -53.011 52.590 1.00 40.83  ?  99  ASN   A N   1 
ATOM   806  C  CA  . ASN   A 1 100 ? 2.826   -53.818 53.082 1.00 38.35  ?  99  ASN   A CA  1 
ATOM   807  C  C   . ASN   A 1 100 ? 3.699   -53.017 54.028 1.00 36.44  ?  99  ASN   A C   1 
ATOM   808  O  O   . ASN   A 1 100 ? 4.927   -53.157 54.024 1.00 37.33  ?  99  ASN   A O   1 
ATOM   809  C  CB  . ASN   A 1 100 ? 3.676   -54.355 51.921 1.00 42.99  ?  99  ASN   A CB  1 
ATOM   810  C  CG  . ASN   A 1 100 ? 4.670   -55.394 52.373 1.00 47.62  ?  99  ASN   A CG  1 
ATOM   811  O  OD1 . ASN   A 1 100 ? 5.856   -55.359 52.009 1.00 40.93  ?  99  ASN   A OD1 1 
ATOM   812  N  ND2 . ASN   A 1 100 ? 4.198   -56.311 53.224 1.00 50.88  ?  99  ASN   A ND2 1 
ATOM   813  N  N   . GLY   A 1 101 ? 3.079   -52.124 54.792 1.00 36.46  ?  100 GLY   A N   1 
ATOM   814  C  CA  . GLY   A 1 101 ? 3.830   -51.299 55.723 1.00 39.54  ?  100 GLY   A CA  1 
ATOM   815  C  C   . GLY   A 1 101 ? 4.695   -50.234 55.084 1.00 44.76  ?  100 GLY   A C   1 
ATOM   816  O  O   . GLY   A 1 101 ? 5.800   -49.974 55.569 1.00 61.61  ?  100 GLY   A O   1 
ATOM   817  N  N   . LEU   A 1 102 ? 4.222   -49.611 54.008 1.00 43.59  ?  101 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 102 ? 4.955   -48.593 53.266 1.00 41.79  ?  101 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 102 ? 3.923   -47.635 52.680 1.00 48.01  ?  101 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 102 ? 2.738   -47.983 52.551 1.00 47.18  ?  101 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 102 ? 5.815   -49.211 52.163 1.00 41.28  ?  101 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 102 ? 7.066   -50.029 52.510 1.00 38.53  ?  101 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 102 ? 7.531   -50.786 51.296 1.00 40.67  ?  101 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 102 ? 8.166   -49.132 52.955 1.00 40.14  ?  101 LEU   A CD2 1 
ATOM   825  N  N   . THR   A 1 103 ? 4.358   -46.408 52.367 1.00 44.45  ?  102 THR   A N   1 
ATOM   826  C  CA  . THR   A 1 103 ? 3.476   -45.420 51.749 1.00 47.76  ?  102 THR   A CA  1 
ATOM   827  C  C   . THR   A 1 103 ? 3.703   -45.457 50.254 1.00 44.58  ?  102 THR   A C   1 
ATOM   828  O  O   . THR   A 1 103 ? 4.815   -45.179 49.804 1.00 42.70  ?  102 THR   A O   1 
ATOM   829  C  CB  . THR   A 1 103 ? 3.713   -43.997 52.245 1.00 46.16  ?  102 THR   A CB  1 
ATOM   830  O  OG1 . THR   A 1 103 ? 3.424   -43.917 53.640 1.00 47.08  ?  102 THR   A OG1 1 
ATOM   831  C  CG2 . THR   A 1 103 ? 2.770   -43.059 51.503 1.00 42.09  ?  102 THR   A CG2 1 
ATOM   832  N  N   . SER   A 1 104 ? 2.656   -45.804 49.500 1.00 41.81  ?  103 SER   A N   1 
ATOM   833  C  CA  . SER   A 1 104 ? 2.652   -45.913 48.048 1.00 41.58  ?  103 SER   A CA  1 
ATOM   834  C  C   . SER   A 1 104 ? 1.798   -44.790 47.460 1.00 46.18  ?  103 SER   A C   1 
ATOM   835  O  O   . SER   A 1 104 ? 1.334   -43.889 48.182 1.00 49.70  ?  103 SER   A O   1 
ATOM   836  C  CB  . SER   A 1 104 ? 2.140   -47.297 47.648 1.00 44.22  ?  103 SER   A CB  1 
ATOM   837  O  OG  . SER   A 1 104 ? 2.332   -47.559 46.268 1.00 41.06  ?  103 SER   A OG  1 
ATOM   838  N  N   . ILE   A 1 105 ? 1.580   -44.833 46.142 1.00 41.36  ?  104 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 105 ? 0.679   -43.892 45.473 1.00 43.75  ?  104 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 105 ? -0.237  -44.679 44.555 1.00 44.78  ?  104 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 105 ? 0.236   -45.393 43.649 1.00 49.93  ?  104 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 105 ? 1.416   -42.816 44.657 1.00 39.07  ?  104 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 105 ? 2.735   -42.430 45.302 1.00 37.08  ?  104 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 105 ? 0.562   -41.605 44.587 1.00 39.67  ?  104 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 105 ? 3.643   -41.661 44.393 1.00 33.99  ?  104 ILE   A CD1 1 
ATOM   846  N  N   . LYS   A 1 106 ? -1.545  -44.521 44.751 1.00 39.62  ?  105 LYS   A N   1 
ATOM   847  C  CA  . LYS   A 1 106 ? -2.505  -45.089 43.812 1.00 42.47  ?  105 LYS   A CA  1 
ATOM   848  C  C   . LYS   A 1 106 ? -2.261  -44.501 42.430 1.00 48.94  ?  105 LYS   A C   1 
ATOM   849  O  O   . LYS   A 1 106 ? -2.077  -43.286 42.290 1.00 51.66  ?  105 LYS   A O   1 
ATOM   850  C  CB  . LYS   A 1 106 ? -3.921  -44.782 44.286 1.00 42.01  ?  105 LYS   A CB  1 
ATOM   851  C  CG  . LYS   A 1 106 ? -4.992  -45.104 43.272 1.00 52.70  ?  105 LYS   A CG  1 
ATOM   852  C  CD  . LYS   A 1 106 ? -6.380  -45.095 43.915 1.00 58.69  ?  105 LYS   A CD  1 
ATOM   853  C  CE  . LYS   A 1 106 ? -7.385  -45.858 43.062 1.00 65.49  ?  105 LYS   A CE  1 
ATOM   854  N  NZ  . LYS   A 1 106 ? -6.921  -47.258 42.742 1.00 72.64  ?  105 LYS   A NZ  1 
ATOM   855  N  N   . TRP   A 1 107 ? -2.288  -45.369 41.421 1.00 47.70  ?  106 TRP   A N   1 
ATOM   856  C  CA  . TRP   A 1 107 ? -1.945  -44.913 40.054 1.00 54.14  ?  106 TRP   A CA  1 
ATOM   857  C  C   . TRP   A 1 107 ? -2.726  -43.689 39.630 1.00 57.39  ?  106 TRP   A C   1 
ATOM   858  O  O   . TRP   A 1 107 ? -3.956  -43.655 39.809 1.00 50.87  ?  106 TRP   A O   1 
ATOM   859  C  CB  . TRP   A 1 107 ? -2.102  -46.008 38.994 1.00 45.88  ?  106 TRP   A CB  1 
ATOM   860  C  CG  . TRP   A 1 107 ? -1.404  -45.607 37.723 1.00 57.74  ?  106 TRP   A CG  1 
ATOM   861  C  CD1 . TRP   A 1 107 ? -0.084  -45.769 37.427 1.00 67.63  ?  106 TRP   A CD1 1 
ATOM   862  C  CD2 . TRP   A 1 107 ? -1.980  -44.898 36.605 1.00 59.46  ?  106 TRP   A CD2 1 
ATOM   863  N  NE1 . TRP   A 1 107 ? 0.198   -45.243 36.196 1.00 63.19  ?  106 TRP   A NE1 1 
ATOM   864  C  CE2 . TRP   A 1 107 ? -0.942  -44.697 35.671 1.00 63.77  ?  106 TRP   A CE2 1 
ATOM   865  C  CE3 . TRP   A 1 107 ? -3.260  -44.427 36.303 1.00 61.18  ?  106 TRP   A CE3 1 
ATOM   866  C  CZ2 . TRP   A 1 107 ? -1.152  -44.046 34.459 1.00 65.55  ?  106 TRP   A CZ2 1 
ATOM   867  C  CZ3 . TRP   A 1 107 ? -3.464  -43.778 35.108 1.00 55.95  ?  106 TRP   A CZ3 1 
ATOM   868  C  CH2 . TRP   A 1 107 ? -2.422  -43.588 34.202 1.00 67.59  ?  106 TRP   A CH2 1 
ATOM   869  N  N   . ALA   A 1 108 ? -2.009  -42.735 39.054 1.00 53.35  ?  107 ALA   A N   1 
ATOM   870  C  CA  . ALA   A 1 108 ? -2.603  -41.519 38.507 1.00 49.78  ?  107 ALA   A CA  1 
ATOM   871  C  C   . ALA   A 1 108 ? -1.552  -40.851 37.645 1.00 52.65  ?  107 ALA   A C   1 
ATOM   872  O  O   . ALA   A 1 108 ? -0.357  -41.114 37.793 1.00 52.55  ?  107 ALA   A O   1 
ATOM   873  C  CB  . ALA   A 1 108 ? -3.086  -40.551 39.600 1.00 39.47  ?  107 ALA   A CB  1 
ATOM   874  N  N   . ASP   A 1 109 ? -2.020  -39.971 36.748 1.00 52.38  ?  108 ASP   A N   1 
ATOM   875  C  CA  . ASP   A 1 109 ? -1.186  -39.086 35.930 1.00 46.14  ?  108 ASP   A CA  1 
ATOM   876  C  C   . ASP   A 1 109 ? 0.265   -39.519 35.766 1.00 52.38  ?  108 ASP   A C   1 
ATOM   877  O  O   . ASP   A 1 109 ? 1.177   -38.784 36.168 1.00 59.71  ?  108 ASP   A O   1 
ATOM   878  C  CB  . ASP   A 1 109 ? -1.158  -37.660 36.502 1.00 46.17  ?  108 ASP   A CB  1 
ATOM   879  C  CG  . ASP   A 1 109 ? -2.526  -37.096 36.837 1.00 48.94  ?  108 ASP   A CG  1 
ATOM   880  O  OD1 . ASP   A 1 109 ? -3.560  -37.701 36.487 1.00 61.08  ?  108 ASP   A OD1 1 
ATOM   881  O  OD2 . ASP   A 1 109 ? -2.548  -35.982 37.426 1.00 41.96  -1 108 ASP   A OD2 1 
ATOM   882  N  N   . ASN   A 1 110 ? 0.488   -40.711 35.223 1.00 47.62  ?  109 ASN   A N   1 
ATOM   883  C  CA  . ASN   A 1 110 ? 1.848   -41.170 34.889 1.00 54.48  ?  109 ASN   A CA  1 
ATOM   884  C  C   . ASN   A 1 110 ? 2.783   -41.300 36.100 1.00 52.14  ?  109 ASN   A C   1 
ATOM   885  O  O   . ASN   A 1 110 ? 4.004   -41.176 35.957 1.00 45.76  ?  109 ASN   A O   1 
ATOM   886  C  CB  . ASN   A 1 110 ? 2.498   -40.248 33.851 1.00 54.11  ?  109 ASN   A CB  1 
ATOM   887  C  CG  . ASN   A 1 110 ? 2.262   -40.711 32.443 1.00 56.23  ?  109 ASN   A CG  1 
ATOM   888  O  OD1 . ASN   A 1 110 ? 2.101   -39.905 31.536 1.00 55.87  ?  109 ASN   A OD1 1 
ATOM   889  N  ND2 . ASN   A 1 110 ? 2.278   -42.027 32.242 1.00 57.38  ?  109 ASN   A ND2 1 
ATOM   890  N  N   . ASN   A 1 111 ? 2.273   -41.570 37.309 1.00 51.65  ?  110 ASN   A N   1 
ATOM   891  C  CA  . ASN   A 1 111 ? 3.127   -41.480 38.490 1.00 49.92  ?  110 ASN   A CA  1 
ATOM   892  C  C   . ASN   A 1 111 ? 3.767   -42.816 38.926 1.00 50.21  ?  110 ASN   A C   1 
ATOM   893  O  O   . ASN   A 1 111 ? 4.298   -42.890 40.038 1.00 45.16  ?  110 ASN   A O   1 
ATOM   894  C  CB  . ASN   A 1 111 ? 2.358   -40.858 39.651 1.00 43.64  ?  110 ASN   A CB  1 
ATOM   895  C  CG  . ASN   A 1 111 ? 1.262   -41.739 40.153 1.00 49.80  ?  110 ASN   A CG  1 
ATOM   896  O  OD1 . ASN   A 1 111 ? 1.151   -42.907 39.764 1.00 49.11  ?  110 ASN   A OD1 1 
ATOM   897  N  ND2 . ASN   A 1 111 ? 0.417   -41.182 41.031 1.00 47.20  ?  110 ASN   A ND2 1 
ATOM   898  N  N   . SER   A 1 112 ? 3.773   -43.851 38.078 1.00 47.73  ?  111 SER   A N   1 
ATOM   899  C  CA  . SER   A 1 112 ? 4.430   -45.098 38.463 1.00 43.34  ?  111 SER   A CA  1 
ATOM   900  C  C   . SER   A 1 112 ? 5.849   -44.835 38.971 1.00 44.76  ?  111 SER   A C   1 
ATOM   901  O  O   . SER   A 1 112 ? 6.245   -45.344 40.031 1.00 46.95  ?  111 SER   A O   1 
ATOM   902  C  CB  . SER   A 1 112 ? 4.420   -46.111 37.293 1.00 48.43  ?  111 SER   A CB  1 
ATOM   903  O  OG  . SER   A 1 112 ? 5.364   -45.882 36.239 1.00 41.01  ?  111 SER   A OG  1 
ATOM   904  N  N   . TYR   A 1 113 ? 6.611   -43.992 38.265 1.00 39.00  ?  112 TYR   A N   1 
ATOM   905  C  CA  . TYR   A 1 113 ? 8.016   -43.817 38.627 1.00 37.91  ?  112 TYR   A CA  1 
ATOM   906  C  C   . TYR   A 1 113 ? 8.178   -43.095 39.969 1.00 42.68  ?  112 TYR   A C   1 
ATOM   907  O  O   . TYR   A 1 113 ? 9.205   -43.286 40.636 1.00 38.09  ?  112 TYR   A O   1 
ATOM   908  C  CB  . TYR   A 1 113 ? 8.781   -43.066 37.527 1.00 31.94  ?  112 TYR   A CB  1 
ATOM   909  C  CG  . TYR   A 1 113 ? 8.571   -41.571 37.588 1.00 38.58  ?  112 TYR   A CG  1 
ATOM   910  C  CD1 . TYR   A 1 113 ? 7.349   -41.014 37.213 1.00 42.67  ?  112 TYR   A CD1 1 
ATOM   911  C  CD2 . TYR   A 1 113 ? 9.565   -40.714 38.057 1.00 39.57  ?  112 TYR   A CD2 1 
ATOM   912  C  CE1 . TYR   A 1 113 ? 7.121   -39.667 37.276 1.00 39.19  ?  112 TYR   A CE1 1 
ATOM   913  C  CE2 . TYR   A 1 113 ? 9.340   -39.340 38.121 1.00 41.63  ?  112 TYR   A CE2 1 
ATOM   914  C  CZ  . TYR   A 1 113 ? 8.104   -38.829 37.723 1.00 40.55  ?  112 TYR   A CZ  1 
ATOM   915  O  OH  . TYR   A 1 113 ? 7.830   -37.478 37.777 1.00 43.84  ?  112 TYR   A OH  1 
ATOM   916  N  N   . LEU   A 1 114 ? 7.192   -42.270 40.386 1.00 39.27  ?  113 LEU   A N   1 
ATOM   917  C  CA  . LEU   A 1 114 ? 7.272   -41.613 41.701 1.00 39.44  ?  113 LEU   A CA  1 
ATOM   918  C  C   . LEU   A 1 114 ? 6.988   -42.592 42.839 1.00 41.12  ?  113 LEU   A C   1 
ATOM   919  O  O   . LEU   A 1 114 ? 7.610   -42.518 43.908 1.00 38.07  ?  113 LEU   A O   1 
ATOM   920  C  CB  . LEU   A 1 114 ? 6.288   -40.446 41.803 1.00 34.13  ?  113 LEU   A CB  1 
ATOM   921  C  CG  . LEU   A 1 114 ? 6.574   -39.191 40.991 1.00 40.54  ?  113 LEU   A CG  1 
ATOM   922  C  CD1 . LEU   A 1 114 ? 5.396   -38.246 41.082 1.00 45.61  ?  113 LEU   A CD1 1 
ATOM   923  C  CD2 . LEU   A 1 114 ? 7.837   -38.532 41.473 1.00 43.13  ?  113 LEU   A CD2 1 
ATOM   924  N  N   . ALA   A 1 115 ? 6.023   -43.491 42.637 1.00 39.94  ?  114 ALA   A N   1 
ATOM   925  C  CA  . ALA   A 1 115 ? 5.752   -44.524 43.623 1.00 42.78  ?  114 ALA   A CA  1 
ATOM   926  C  C   . ALA   A 1 115 ? 6.959   -45.454 43.806 1.00 44.29  ?  114 ALA   A C   1 
ATOM   927  O  O   . ALA   A 1 115 ? 7.328   -45.788 44.944 1.00 36.24  ?  114 ALA   A O   1 
ATOM   928  C  CB  . ALA   A 1 115 ? 4.492   -45.298 43.222 1.00 35.53  ?  114 ALA   A CB  1 
ATOM   929  N  N   . THR   A 1 116 ? 7.606   -45.878 42.712 1.00 33.91  ?  115 THR   A N   1 
ATOM   930  C  CA  . THR   A 1 116 ? 8.788   -46.708 42.925 1.00 39.70  ?  115 THR   A CA  1 
ATOM   931  C  C   . THR   A 1 116 ? 9.876   -45.909 43.648 1.00 40.79  ?  115 THR   A C   1 
ATOM   932  O  O   . THR   A 1 116 ? 10.614  -46.445 44.485 1.00 38.59  ?  115 THR   A O   1 
ATOM   933  C  CB  . THR   A 1 116 ? 9.269   -47.292 41.586 1.00 41.24  ?  115 THR   A CB  1 
ATOM   934  O  OG1 . THR   A 1 116 ? 8.290   -48.223 41.098 1.00 39.49  ?  115 THR   A OG1 1 
ATOM   935  C  CG2 . THR   A 1 116 ? 10.581  -48.036 41.727 1.00 36.99  ?  115 THR   A CG2 1 
ATOM   936  N  N   . ALA   A 1 117 ? 9.936   -44.608 43.400 1.00 44.11  ?  116 ALA   A N   1 
ATOM   937  C  CA  . ALA   A 1 117 ? 10.904  -43.786 44.105 1.00 38.40  ?  116 ALA   A CA  1 
ATOM   938  C  C   . ALA   A 1 117 ? 10.500  -43.583 45.561 1.00 40.14  ?  116 ALA   A C   1 
ATOM   939  O  O   . ALA   A 1 117 ? 11.347  -43.644 46.460 1.00 41.46  ?  116 ALA   A O   1 
ATOM   940  C  CB  . ALA   A 1 117 ? 11.078  -42.446 43.384 1.00 32.92  ?  116 ALA   A CB  1 
ATOM   941  N  N   . LEU   A 1 118 ? 9.214   -43.335 45.815 1.00 37.34  ?  117 LEU   A N   1 
ATOM   942  C  CA  . LEU   A 1 118 ? 8.767   -43.114 47.185 1.00 35.92  ?  117 LEU   A CA  1 
ATOM   943  C  C   . LEU   A 1 118 ? 9.022   -44.349 48.039 1.00 43.67  ?  117 LEU   A C   1 
ATOM   944  O  O   . LEU   A 1 118 ? 9.563   -44.253 49.148 1.00 46.85  ?  117 LEU   A O   1 
ATOM   945  C  CB  . LEU   A 1 118 ? 7.285   -42.766 47.183 1.00 34.84  ?  117 LEU   A CB  1 
ATOM   946  C  CG  . LEU   A 1 118 ? 6.669   -42.486 48.539 1.00 34.44  ?  117 LEU   A CG  1 
ATOM   947  C  CD1 . LEU   A 1 118 ? 7.400   -41.327 49.166 1.00 37.22  ?  117 LEU   A CD1 1 
ATOM   948  C  CD2 . LEU   A 1 118 ? 5.192   -42.154 48.337 1.00 35.82  ?  117 LEU   A CD2 1 
ATOM   949  N  N   . LEU   A 1 119 ? 8.645   -45.524 47.514 1.00 41.38  ?  118 LEU   A N   1 
ATOM   950  C  CA  . LEU   A 1 119 ? 8.855   -46.794 48.190 1.00 38.58  ?  118 LEU   A CA  1 
ATOM   951  C  C   . LEU   A 1 119 ? 10.330  -47.021 48.504 1.00 42.06  ?  118 LEU   A C   1 
ATOM   952  O  O   . LEU   A 1 119 ? 10.680  -47.524 49.580 1.00 42.14  ?  118 LEU   A O   1 
ATOM   953  C  CB  . LEU   A 1 119 ? 8.306   -47.918 47.311 1.00 37.78  ?  118 LEU   A CB  1 
ATOM   954  C  CG  . LEU   A 1 119 ? 6.784   -47.831 47.143 1.00 43.05  ?  118 LEU   A CG  1 
ATOM   955  C  CD1 . LEU   A 1 119 ? 6.230   -48.760 46.082 1.00 41.27  ?  118 LEU   A CD1 1 
ATOM   956  C  CD2 . LEU   A 1 119 ? 6.119   -48.084 48.456 1.00 41.32  ?  118 LEU   A CD2 1 
ATOM   957  N  N   . THR   A 1 120 ? 11.212  -46.664 47.579 1.00 39.20  ?  119 THR   A N   1 
ATOM   958  C  CA  . THR   A 1 120 ? 12.624  -46.940 47.800 1.00 37.35  ?  119 THR   A CA  1 
ATOM   959  C  C   . THR   A 1 120 ? 13.185  -46.034 48.880 1.00 38.94  ?  119 THR   A C   1 
ATOM   960  O  O   . THR   A 1 120 ? 14.042  -46.450 49.671 1.00 37.45  ?  119 THR   A O   1 
ATOM   961  C  CB  . THR   A 1 120 ? 13.386  -46.775 46.490 1.00 34.85  ?  119 THR   A CB  1 
ATOM   962  O  OG1 . THR   A 1 120 ? 12.722  -47.553 45.494 1.00 41.25  ?  119 THR   A OG1 1 
ATOM   963  C  CG2 . THR   A 1 120 ? 14.788  -47.276 46.617 1.00 27.64  ?  119 THR   A CG2 1 
ATOM   964  N  N   . LEU   A 1 121 ? 12.706  -44.790 48.937 1.00 41.28  ?  120 LEU   A N   1 
ATOM   965  C  CA  . LEU   A 1 121 ? 13.247  -43.861 49.921 1.00 42.08  ?  120 LEU   A CA  1 
ATOM   966  C  C   . LEU   A 1 121 ? 12.846  -44.257 51.342 1.00 44.00  ?  120 LEU   A C   1 
ATOM   967  O  O   . LEU   A 1 121 ? 13.572  -43.956 52.295 1.00 43.17  ?  120 LEU   A O   1 
ATOM   968  C  CB  . LEU   A 1 121 ? 12.801  -42.438 49.595 1.00 37.45  ?  120 LEU   A CB  1 
ATOM   969  C  CG  . LEU   A 1 121 ? 13.426  -41.866 48.321 1.00 41.57  ?  120 LEU   A CG  1 
ATOM   970  C  CD1 . LEU   A 1 121 ? 12.522  -40.814 47.640 1.00 42.09  ?  120 LEU   A CD1 1 
ATOM   971  C  CD2 . LEU   A 1 121 ? 14.764  -41.285 48.662 1.00 40.27  ?  120 LEU   A CD2 1 
ATOM   972  N  N   . GLN   A 1 122 ? 11.712  -44.943 51.504 1.00 41.75  ?  121 GLN   A N   1 
ATOM   973  C  CA  . GLN   A 1 122 ? 11.318  -45.431 52.820 1.00 44.46  ?  121 GLN   A CA  1 
ATOM   974  C  C   . GLN   A 1 122 ? 12.147  -46.621 53.284 1.00 45.96  ?  121 GLN   A C   1 
ATOM   975  O  O   . GLN   A 1 122 ? 11.943  -47.059 54.424 1.00 43.60  ?  121 GLN   A O   1 
ATOM   976  C  CB  . GLN   A 1 122 ? 9.834   -45.814 52.828 1.00 39.84  ?  121 GLN   A CB  1 
ATOM   977  C  CG  . GLN   A 1 122 ? 8.915   -44.633 52.698 1.00 38.16  ?  121 GLN   A CG  1 
ATOM   978  C  CD  . GLN   A 1 122 ? 7.488   -45.027 52.417 1.00 45.05  ?  121 GLN   A CD  1 
ATOM   979  O  OE1 . GLN   A 1 122 ? 6.700   -45.268 53.339 1.00 46.23  ?  121 GLN   A OE1 1 
ATOM   980  N  NE2 . GLN   A 1 122 ? 7.124   -45.060 51.128 1.00 49.93  ?  121 GLN   A NE2 1 
ATOM   981  N  N   . GLN   A 1 123 ? 13.066  -47.140 52.449 1.00 35.90  ?  122 GLN   A N   1 
ATOM   982  C  CA  . GLN   A 1 123 ? 13.846  -48.323 52.785 1.00 31.40  ?  122 GLN   A CA  1 
ATOM   983  C  C   . GLN   A 1 123 ? 15.362  -48.139 52.744 1.00 37.30  ?  122 GLN   A C   1 
ATOM   984  O  O   . GLN   A 1 123 ? 16.089  -49.120 52.952 1.00 39.94  ?  122 GLN   A O   1 
ATOM   985  C  CB  . GLN   A 1 123 ? 13.464  -49.469 51.854 1.00 31.68  ?  122 GLN   A CB  1 
ATOM   986  C  CG  . GLN   A 1 123 ? 11.979  -49.665 51.722 1.00 36.18  ?  122 GLN   A CG  1 
ATOM   987  C  CD  . GLN   A 1 123 ? 11.665  -50.904 50.934 1.00 39.73  ?  122 GLN   A CD  1 
ATOM   988  O  OE1 . GLN   A 1 123 ? 10.803  -50.887 50.057 1.00 44.56  ?  122 GLN   A OE1 1 
ATOM   989  N  NE2 . GLN   A 1 123 ? 12.388  -51.985 51.213 1.00 36.78  ?  122 GLN   A NE2 1 
ATOM   990  N  N   . ILE   A 1 124 ? 15.874  -46.937 52.487 1.00 33.73  ?  123 ILE   A N   1 
ATOM   991  C  CA  . ILE   A 1 124 ? 17.302  -46.704 52.616 1.00 31.23  ?  123 ILE   A CA  1 
ATOM   992  C  C   . ILE   A 1 124 ? 17.525  -45.533 53.570 1.00 38.87  ?  123 ILE   A C   1 
ATOM   993  O  O   . ILE   A 1 124 ? 16.600  -44.769 53.889 1.00 40.48  ?  123 ILE   A O   1 
ATOM   994  C  CB  . ILE   A 1 124 ? 17.982  -46.467 51.258 1.00 35.77  ?  123 ILE   A CB  1 
ATOM   995  C  CG1 . ILE   A 1 124 ? 17.223  -45.419 50.447 1.00 40.49  ?  123 ILE   A CG1 1 
ATOM   996  C  CG2 . ILE   A 1 124 ? 18.039  -47.765 50.496 1.00 35.88  ?  123 ILE   A CG2 1 
ATOM   997  C  CD1 . ILE   A 1 124 ? 17.912  -45.029 49.143 1.00 36.20  ?  123 ILE   A CD1 1 
ATOM   998  N  N   . GLU   A 1 125 ? 18.761  -45.438 54.081 1.00 33.25  ?  124 GLU   A N   1 
ATOM   999  C  CA  . GLU   A 1 125 ? 19.104  -44.432 55.077 1.00 41.01  ?  124 GLU   A CA  1 
ATOM   1000 C  C   . GLU   A 1 125 ? 19.497  -43.162 54.337 1.00 42.49  ?  124 GLU   A C   1 
ATOM   1001 O  O   . GLU   A 1 125 ? 20.478  -43.140 53.590 1.00 47.31  ?  124 GLU   A O   1 
ATOM   1002 C  CB  . GLU   A 1 125 ? 20.221  -44.893 56.032 1.00 43.01  ?  124 GLU   A CB  1 
ATOM   1003 C  CG  . GLU   A 1 125 ? 20.007  -44.436 57.515 1.00 55.71  ?  124 GLU   A CG  1 
ATOM   1004 C  CD  . GLU   A 1 125 ? 20.928  -45.160 58.559 1.00 89.64  ?  124 GLU   A CD  1 
ATOM   1005 O  OE1 . GLU   A 1 125 ? 21.560  -44.484 59.420 1.00 89.31  ?  124 GLU   A OE1 1 
ATOM   1006 O  OE2 . GLU   A 1 125 ? 21.033  -46.415 58.525 1.00 86.33  -1 124 GLU   A OE2 1 
ATOM   1007 N  N   . LEU   A 1 126 ? 18.728  -42.108 54.546 1.00 40.32  ?  125 LEU   A N   1 
ATOM   1008 C  CA  . LEU   A 1 126 ? 18.946  -40.878 53.817 1.00 43.91  ?  125 LEU   A CA  1 
ATOM   1009 C  C   . LEU   A 1 126 ? 18.563  -39.720 54.719 1.00 49.25  ?  125 LEU   A C   1 
ATOM   1010 O  O   . LEU   A 1 126 ? 17.460  -39.693 55.280 1.00 50.71  ?  125 LEU   A O   1 
ATOM   1011 C  CB  . LEU   A 1 126 ? 18.111  -40.854 52.530 1.00 42.70  ?  125 LEU   A CB  1 
ATOM   1012 C  CG  . LEU   A 1 126 ? 18.759  -40.286 51.266 1.00 43.93  ?  125 LEU   A CG  1 
ATOM   1013 C  CD1 . LEU   A 1 126 ? 20.206  -40.749 51.016 1.00 32.74  ?  125 LEU   A CD1 1 
ATOM   1014 C  CD2 . LEU   A 1 126 ? 17.866  -40.632 50.087 1.00 50.63  ?  125 LEU   A CD2 1 
ATOM   1015 N  N   . LYS   A 1 127 ? 19.483  -38.787 54.876 1.00 48.68  ?  126 LYS   A N   1 
ATOM   1016 C  CA  . LYS   A 1 127 ? 19.177  -37.475 55.419 1.00 51.97  ?  126 LYS   A CA  1 
ATOM   1017 C  C   . LYS   A 1 127 ? 19.289  -36.495 54.258 1.00 48.29  ?  126 LYS   A C   1 
ATOM   1018 O  O   . LYS   A 1 127 ? 20.310  -36.472 53.560 1.00 50.85  ?  126 LYS   A O   1 
ATOM   1019 C  CB  . LYS   A 1 127 ? 20.129  -37.118 56.569 1.00 54.22  ?  126 LYS   A CB  1 
ATOM   1020 C  CG  . LYS   A 1 127 ? 19.813  -35.802 57.304 1.00 55.86  ?  126 LYS   A CG  1 
ATOM   1021 C  CD  . LYS   A 1 127 ? 21.099  -35.052 57.717 1.00 65.37  ?  126 LYS   A CD  1 
ATOM   1022 C  CE  . LYS   A 1 127 ? 21.393  -33.849 56.782 1.00 62.83  ?  126 LYS   A CE  1 
ATOM   1023 N  NZ  . LYS   A 1 127 ? 22.810  -33.291 56.854 1.00 57.35  ?  126 LYS   A NZ  1 
ATOM   1024 N  N   . PHE   A 1 128 ? 18.222  -35.743 54.014 1.00 46.45  ?  127 PHE   A N   1 
ATOM   1025 C  CA  . PHE   A 1 128 ? 18.237  -34.649 53.052 1.00 46.60  ?  127 PHE   A CA  1 
ATOM   1026 C  C   . PHE   A 1 128 ? 18.658  -33.359 53.741 1.00 48.02  ?  127 PHE   A C   1 
ATOM   1027 O  O   . PHE   A 1 128 ? 18.245  -33.088 54.871 1.00 53.30  ?  127 PHE   A O   1 
ATOM   1028 C  CB  . PHE   A 1 128 ? 16.853  -34.439 52.453 1.00 45.07  ?  127 PHE   A CB  1 
ATOM   1029 C  CG  . PHE   A 1 128 ? 16.389  -35.545 51.581 1.00 42.13  ?  127 PHE   A CG  1 
ATOM   1030 C  CD1 . PHE   A 1 128 ? 17.103  -35.909 50.473 1.00 41.22  ?  127 PHE   A CD1 1 
ATOM   1031 C  CD2 . PHE   A 1 128 ? 15.208  -36.202 51.867 1.00 42.35  ?  127 PHE   A CD2 1 
ATOM   1032 C  CE1 . PHE   A 1 128 ? 16.648  -36.922 49.665 1.00 48.56  ?  127 PHE   A CE1 1 
ATOM   1033 C  CE2 . PHE   A 1 128 ? 14.748  -37.205 51.078 1.00 40.85  ?  127 PHE   A CE2 1 
ATOM   1034 C  CZ  . PHE   A 1 128 ? 15.465  -37.575 49.973 1.00 48.95  ?  127 PHE   A CZ  1 
ATOM   1035 N  N   . ASN   A 1 129 ? 19.431  -32.539 53.043 1.00 46.97  ?  128 ASN   A N   1 
ATOM   1036 C  CA  . ASN   A 1 129 ? 19.821  -31.259 53.627 1.00 41.84  ?  128 ASN   A CA  1 
ATOM   1037 C  C   . ASN   A 1 129 ? 18.721  -30.187 53.585 1.00 42.65  ?  128 ASN   A C   1 
ATOM   1038 O  O   . ASN   A 1 129 ? 18.502  -29.523 54.596 1.00 47.25  ?  128 ASN   A O   1 
ATOM   1039 C  CB  . ASN   A 1 129 ? 21.107  -30.771 52.962 1.00 44.07  ?  128 ASN   A CB  1 
ATOM   1040 C  CG  . ASN   A 1 129 ? 22.321  -31.609 53.377 1.00 49.12  ?  128 ASN   A CG  1 
ATOM   1041 O  OD1 . ASN   A 1 129 ? 22.463  -31.962 54.547 1.00 54.51  ?  128 ASN   A OD1 1 
ATOM   1042 N  ND2 . ASN   A 1 129 ? 23.177  -31.949 52.425 1.00 49.77  ?  128 ASN   A ND2 1 
ATOM   1043 N  N   . PRO   A 1 130 ? 17.989  -29.957 52.505 1.00 44.44  ?  129 PRO   A N   1 
ATOM   1044 C  CA  . PRO   A 1 130 ? 17.008  -28.888 52.555 1.00 42.51  ?  129 PRO   A CA  1 
ATOM   1045 C  C   . PRO   A 1 130 ? 15.898  -29.225 53.536 1.00 43.57  ?  129 PRO   A C   1 
ATOM   1046 O  O   . PRO   A 1 130 ? 15.179  -30.220 53.353 1.00 41.39  ?  129 PRO   A O   1 
ATOM   1047 C  CB  . PRO   A 1 130 ? 16.483  -28.818 51.109 1.00 42.45  ?  129 PRO   A CB  1 
ATOM   1048 C  CG  . PRO   A 1 130 ? 17.483  -29.532 50.290 1.00 41.33  ?  129 PRO   A CG  1 
ATOM   1049 C  CD  . PRO   A 1 130 ? 17.965  -30.618 51.188 1.00 45.58  ?  129 PRO   A CD  1 
ATOM   1050 N  N   . PRO   A 1 131 ? 15.712  -28.409 54.580 1.00 42.36  ?  130 PRO   A N   1 
ATOM   1051 C  CA  . PRO   A 1 131 ? 14.600  -28.639 55.513 1.00 38.57  ?  130 PRO   A CA  1 
ATOM   1052 C  C   . PRO   A 1 131 ? 13.258  -28.858 54.864 1.00 43.54  ?  130 PRO   A C   1 
ATOM   1053 O  O   . PRO   A 1 131 ? 12.409  -29.539 55.456 1.00 46.59  ?  130 PRO   A O   1 
ATOM   1054 C  CB  . PRO   A 1 131 ? 14.604  -27.359 56.347 1.00 33.33  ?  130 PRO   A CB  1 
ATOM   1055 C  CG  . PRO   A 1 131 ? 15.999  -26.996 56.391 1.00 31.53  ?  130 PRO   A CG  1 
ATOM   1056 C  CD  . PRO   A 1 131 ? 16.519  -27.262 55.011 1.00 39.28  ?  130 PRO   A CD  1 
ATOM   1057 N  N   . ALA   A 1 132 ? 13.021  -28.304 53.674 1.00 45.86  ?  131 ALA   A N   1 
ATOM   1058 C  CA  . ALA   A 1 132 ? 11.766  -28.584 52.987 1.00 43.20  ?  131 ALA   A CA  1 
ATOM   1059 C  C   . ALA   A 1 132 ? 11.668  -30.052 52.623 1.00 40.76  ?  131 ALA   A C   1 
ATOM   1060 O  O   . ALA   A 1 132 ? 10.588  -30.645 52.722 1.00 39.06  ?  131 ALA   A O   1 
ATOM   1061 C  CB  . ALA   A 1 132 ? 11.636  -27.727 51.732 1.00 46.85  ?  131 ALA   A CB  1 
ATOM   1062 N  N   . LEU   A 1 133 ? 12.789  -30.659 52.208 1.00 39.93  ?  132 LEU   A N   1 
ATOM   1063 C  CA  . LEU   A 1 133 ? 12.768  -32.069 51.811 1.00 40.53  ?  132 LEU   A CA  1 
ATOM   1064 C  C   . LEU   A 1 133 ? 12.591  -32.971 53.017 1.00 44.24  ?  132 LEU   A C   1 
ATOM   1065 O  O   . LEU   A 1 133 ? 11.755  -33.889 53.010 1.00 42.76  ?  132 LEU   A O   1 
ATOM   1066 C  CB  . LEU   A 1 133 ? 14.049  -32.451 51.078 1.00 38.64  ?  132 LEU   A CB  1 
ATOM   1067 C  CG  . LEU   A 1 133 ? 13.863  -32.422 49.568 1.00 40.73  ?  132 LEU   A CG  1 
ATOM   1068 C  CD1 . LEU   A 1 133 ? 15.094  -32.949 48.847 1.00 38.11  ?  132 LEU   A CD1 1 
ATOM   1069 C  CD2 . LEU   A 1 133 ? 12.603  -33.199 49.229 1.00 39.38  ?  132 LEU   A CD2 1 
ATOM   1070 N  N   . GLN   A 1 134 ? 13.360  -32.713 54.078 1.00 42.14  ?  133 GLN   A N   1 
ATOM   1071 C  CA  . GLN   A 1 134 ? 13.328  -33.633 55.195 1.00 41.86  ?  133 GLN   A CA  1 
ATOM   1072 C  C   . GLN   A 1 134 ? 11.991  -33.578 55.919 1.00 42.20  ?  133 GLN   A C   1 
ATOM   1073 O  O   . GLN   A 1 134 ? 11.475  -34.626 56.342 1.00 40.10  ?  133 GLN   A O   1 
ATOM   1074 C  CB  . GLN   A 1 134 ? 14.479  -33.371 56.148 1.00 42.18  ?  133 GLN   A CB  1 
ATOM   1075 C  CG  . GLN   A 1 134 ? 14.635  -34.561 57.074 1.00 40.47  ?  133 GLN   A CG  1 
ATOM   1076 C  CD  . GLN   A 1 134 ? 15.581  -35.578 56.510 1.00 45.38  ?  133 GLN   A CD  1 
ATOM   1077 O  OE1 . GLN   A 1 134 ? 16.760  -35.299 56.296 1.00 52.13  ?  133 GLN   A OE1 1 
ATOM   1078 N  NE2 . GLN   A 1 134 ? 15.065  -36.751 56.207 1.00 52.85  ?  133 GLN   A NE2 1 
ATOM   1079 N  N   . ASP   A 1 135 ? 11.399  -32.381 56.061 1.00 36.36  ?  134 ASP   A N   1 
ATOM   1080 C  CA  . ASP   A 1 135 ? 10.069  -32.326 56.668 1.00 41.23  ?  134 ASP   A CA  1 
ATOM   1081 C  C   . ASP   A 1 135 ? 9.052   -33.091 55.821 1.00 43.33  ?  134 ASP   A C   1 
ATOM   1082 O  O   . ASP   A 1 135 ? 8.212   -33.829 56.364 1.00 41.25  ?  134 ASP   A O   1 
ATOM   1083 C  CB  . ASP   A 1 135 ? 9.597   -30.881 56.876 1.00 37.91  ?  134 ASP   A CB  1 
ATOM   1084 C  CG  . ASP   A 1 135 ? 10.540  -30.057 57.729 1.00 50.35  ?  134 ASP   A CG  1 
ATOM   1085 O  OD1 . ASP   A 1 135 ? 11.389  -30.623 58.478 1.00 54.90  ?  134 ASP   A OD1 1 
ATOM   1086 O  OD2 . ASP   A 1 135 ? 10.416  -28.814 57.644 1.00 54.46  -1 134 ASP   A OD2 1 
ATOM   1087 N  N   . ALA   A 1 136 ? 9.110   -32.942 54.487 1.00 39.83  ?  135 ALA   A N   1 
ATOM   1088 C  CA  . ALA   A 1 136 ? 8.138   -33.660 53.669 1.00 42.87  ?  135 ALA   A CA  1 
ATOM   1089 C  C   . ALA   A 1 136 ? 8.455   -35.147 53.667 1.00 41.20  ?  135 ALA   A C   1 
ATOM   1090 O  O   . ALA   A 1 136 ? 7.538   -35.976 53.720 1.00 41.37  ?  135 ALA   A O   1 
ATOM   1091 C  CB  . ALA   A 1 136 ? 8.076   -33.097 52.244 1.00 36.41  ?  135 ALA   A CB  1 
ATOM   1092 N  N   . TYR   A 1 137 ? 9.748   -35.500 53.648 1.00 36.57  ?  136 TYR   A N   1 
ATOM   1093 C  CA  . TYR   A 1 137 ? 10.147  -36.896 53.826 1.00 43.23  ?  136 TYR   A CA  1 
ATOM   1094 C  C   . TYR   A 1 137 ? 9.461   -37.505 55.036 1.00 43.25  ?  136 TYR   A C   1 
ATOM   1095 O  O   . TYR   A 1 137 ? 8.757   -38.510 54.914 1.00 44.21  ?  136 TYR   A O   1 
ATOM   1096 C  CB  . TYR   A 1 137 ? 11.659  -37.001 53.999 1.00 51.03  ?  136 TYR   A CB  1 
ATOM   1097 C  CG  . TYR   A 1 137 ? 12.314  -38.362 53.729 1.00 49.45  ?  136 TYR   A CG  1 
ATOM   1098 C  CD1 . TYR   A 1 137 ? 11.625  -39.429 53.138 1.00 43.13  ?  136 TYR   A CD1 1 
ATOM   1099 C  CD2 . TYR   A 1 137 ? 13.660  -38.551 54.058 1.00 47.52  ?  136 TYR   A CD2 1 
ATOM   1100 C  CE1 . TYR   A 1 137 ? 12.289  -40.661 52.882 1.00 47.16  ?  136 TYR   A CE1 1 
ATOM   1101 C  CE2 . TYR   A 1 137 ? 14.322  -39.744 53.815 1.00 52.82  ?  136 TYR   A CE2 1 
ATOM   1102 C  CZ  . TYR   A 1 137 ? 13.650  -40.804 53.232 1.00 55.45  ?  136 TYR   A CZ  1 
ATOM   1103 O  OH  . TYR   A 1 137 ? 14.388  -41.973 53.024 1.00 46.32  ?  136 TYR   A OH  1 
ATOM   1104 N  N   . TYR   A 1 138 ? 9.660   -36.898 56.219 1.00 41.27  ?  137 TYR   A N   1 
ATOM   1105 C  CA  . TYR   A 1 138 ? 9.066   -37.441 57.440 1.00 36.16  ?  137 TYR   A CA  1 
ATOM   1106 C  C   . TYR   A 1 138 ? 7.572   -37.558 57.283 1.00 37.21  ?  137 TYR   A C   1 
ATOM   1107 O  O   . TYR   A 1 138 ? 7.000   -38.635 57.479 1.00 44.24  ?  137 TYR   A O   1 
ATOM   1108 C  CB  . TYR   A 1 138 ? 9.402   -36.582 58.664 1.00 36.56  ?  137 TYR   A CB  1 
ATOM   1109 C  CG  . TYR   A 1 138 ? 10.789  -36.816 59.204 1.00 35.14  ?  137 TYR   A CG  1 
ATOM   1110 C  CD1 . TYR   A 1 138 ? 11.224  -38.096 59.539 1.00 38.22  ?  137 TYR   A CD1 1 
ATOM   1111 C  CD2 . TYR   A 1 138 ? 11.676  -35.770 59.349 1.00 34.53  ?  137 TYR   A CD2 1 
ATOM   1112 C  CE1 . TYR   A 1 138 ? 12.498  -38.315 60.023 1.00 36.73  ?  137 TYR   A CE1 1 
ATOM   1113 C  CE2 . TYR   A 1 138 ? 12.941  -35.977 59.808 1.00 35.52  ?  137 TYR   A CE2 1 
ATOM   1114 C  CZ  . TYR   A 1 138 ? 13.354  -37.241 60.147 1.00 39.98  ?  137 TYR   A CZ  1 
ATOM   1115 O  OH  . TYR   A 1 138 ? 14.628  -37.428 60.618 1.00 40.77  ?  137 TYR   A OH  1 
ATOM   1116 N  N   . ARG   A 1 139 ? 6.924   -36.467 56.884 1.00 39.40  ?  138 ARG   A N   1 
ATOM   1117 C  CA  . ARG   A 1 139 ? 5.473   -36.475 56.811 1.00 41.14  ?  138 ARG   A CA  1 
ATOM   1118 C  C   . ARG   A 1 139 ? 4.982   -37.494 55.795 1.00 42.71  ?  138 ARG   A C   1 
ATOM   1119 O  O   . ARG   A 1 139 ? 3.894   -38.051 55.954 1.00 44.36  ?  138 ARG   A O   1 
ATOM   1120 C  CB  . ARG   A 1 139 ? 4.980   -35.072 56.482 1.00 48.56  ?  138 ARG   A CB  1 
ATOM   1121 C  CG  . ARG   A 1 139 ? 4.960   -34.111 57.674 1.00 45.32  ?  138 ARG   A CG  1 
ATOM   1122 C  CD  . ARG   A 1 139 ? 4.058   -32.926 57.338 1.00 60.51  ?  138 ARG   A CD  1 
ATOM   1123 N  NE  . ARG   A 1 139 ? 2.651   -33.312 57.322 1.00 68.32  ?  138 ARG   A NE  1 
ATOM   1124 C  CZ  . ARG   A 1 139 ? 1.885   -33.401 58.402 1.00 80.53  ?  138 ARG   A CZ  1 
ATOM   1125 N  NH1 . ARG   A 1 139 ? 2.343   -33.074 59.609 1.00 68.83  ?  138 ARG   A NH1 1 
ATOM   1126 N  NH2 . ARG   A 1 139 ? 0.627   -33.821 58.270 1.00 83.37  ?  138 ARG   A NH2 1 
ATOM   1127 N  N   . ALA   A 1 140 ? 5.787   -37.791 54.771 1.00 43.48  ?  139 ALA   A N   1 
ATOM   1128 C  CA  . ALA   A 1 140 ? 5.397   -38.834 53.828 1.00 44.38  ?  139 ALA   A CA  1 
ATOM   1129 C  C   . ALA   A 1 140 ? 5.480   -40.223 54.448 1.00 46.28  ?  139 ALA   A C   1 
ATOM   1130 O  O   . ALA   A 1 140 ? 4.678   -41.097 54.095 1.00 50.47  ?  139 ALA   A O   1 
ATOM   1131 C  CB  . ALA   A 1 140 ? 6.257   -38.780 52.573 1.00 37.56  ?  139 ALA   A CB  1 
ATOM   1132 N  N   . ARG   A 1 141 ? 6.451   -40.460 55.339 1.00 43.02  ?  140 ARG   A N   1 
ATOM   1133 C  CA  . ARG   A 1 141 ? 6.503   -41.741 56.030 1.00 44.50  ?  140 ARG   A CA  1 
ATOM   1134 C  C   . ARG   A 1 141 ? 5.201   -42.010 56.754 1.00 48.24  ?  140 ARG   A C   1 
ATOM   1135 O  O   . ARG   A 1 141 ? 4.760   -43.160 56.835 1.00 56.51  ?  140 ARG   A O   1 
ATOM   1136 C  CB  . ARG   A 1 141 ? 7.663   -41.788 57.026 1.00 44.07  ?  140 ARG   A CB  1 
ATOM   1137 C  CG  . ARG   A 1 141 ? 8.845   -42.597 56.546 1.00 50.71  ?  140 ARG   A CG  1 
ATOM   1138 C  CD  . ARG   A 1 141 ? 10.139  -42.356 57.354 1.00 55.77  ?  140 ARG   A CD  1 
ATOM   1139 N  NE  . ARG   A 1 141 ? 11.274  -43.044 56.740 1.00 56.39  ?  140 ARG   A NE  1 
ATOM   1140 C  CZ  . ARG   A 1 141 ? 11.373  -44.363 56.620 1.00 54.64  ?  140 ARG   A CZ  1 
ATOM   1141 N  NH1 . ARG   A 1 141 ? 10.434  -45.177 57.091 1.00 55.51  ?  140 ARG   A NH1 1 
ATOM   1142 N  NH2 . ARG   A 1 141 ? 12.420  -44.881 55.980 1.00 56.78  ?  140 ARG   A NH2 1 
ATOM   1143 N  N   . ALA   A 1 142 ? 4.559   -40.962 57.251 1.00 46.31  ?  141 ALA   A N   1 
ATOM   1144 C  CA  . ALA   A 1 142 ? 3.329   -41.079 58.011 1.00 43.00  ?  141 ALA   A CA  1 
ATOM   1145 C  C   . ALA   A 1 142 ? 2.073   -41.111 57.145 1.00 52.38  ?  141 ALA   A C   1 
ATOM   1146 O  O   . ALA   A 1 142 ? 0.975   -41.129 57.701 1.00 63.29  ?  141 ALA   A O   1 
ATOM   1147 C  CB  . ALA   A 1 142 ? 3.237   -39.917 59.006 1.00 37.98  ?  141 ALA   A CB  1 
ATOM   1148 N  N   . GLY   A 1 143 ? 2.188   -41.079 55.810 1.00 55.98  ?  142 GLY   A N   1 
ATOM   1149 C  CA  . GLY   A 1 143 ? 1.045   -41.157 54.913 1.00 50.83  ?  142 GLY   A CA  1 
ATOM   1150 C  C   . GLY   A 1 143 ? 0.711   -39.869 54.170 1.00 56.73  ?  142 GLY   A C   1 
ATOM   1151 O  O   . GLY   A 1 143 ? -0.012  -39.920 53.161 1.00 58.82  ?  142 GLY   A O   1 
ATOM   1152 N  N   . GLU   A 1 144 ? 1.206   -38.721 54.638 1.00 58.69  ?  143 GLU   A N   1 
ATOM   1153 C  CA  . GLU   A 1 144 ? 0.944   -37.422 54.008 1.00 51.56  ?  143 GLU   A CA  1 
ATOM   1154 C  C   . GLU   A 1 144 ? 2.055   -37.096 53.014 1.00 50.59  ?  143 GLU   A C   1 
ATOM   1155 O  O   . GLU   A 1 144 ? 2.911   -36.232 53.237 1.00 46.52  ?  143 GLU   A O   1 
ATOM   1156 C  CB  . GLU   A 1 144 ? 0.848   -36.345 55.067 1.00 55.51  ?  143 GLU   A CB  1 
ATOM   1157 C  CG  . GLU   A 1 144 ? 0.009   -36.770 56.196 1.00 59.99  ?  143 GLU   A CG  1 
ATOM   1158 C  CD  . GLU   A 1 144 ? -1.340  -36.185 56.079 1.00 70.64  ?  143 GLU   A CD  1 
ATOM   1159 O  OE1 . GLU   A 1 144 ? -1.432  -34.941 55.940 1.00 79.05  ?  143 GLU   A OE1 1 
ATOM   1160 O  OE2 . GLU   A 1 144 ? -2.303  -36.980 56.090 1.00 80.64  -1 143 GLU   A OE2 1 
ATOM   1161 N  N   . ALA   A 1 145 ? 2.020   -37.803 51.890 1.00 48.56  ?  144 ALA   A N   1 
ATOM   1162 C  CA  . ALA   A 1 145 ? 3.080   -37.724 50.901 1.00 39.15  ?  144 ALA   A CA  1 
ATOM   1163 C  C   . ALA   A 1 145 ? 2.862   -36.653 49.833 1.00 40.24  ?  144 ALA   A C   1 
ATOM   1164 O  O   . ALA   A 1 145 ? 3.746   -36.474 48.985 1.00 43.82  ?  144 ALA   A O   1 
ATOM   1165 C  CB  . ALA   A 1 145 ? 3.246   -39.086 50.231 1.00 34.87  ?  144 ALA   A CB  1 
ATOM   1166 N  N   . ALA   A 1 146 ? 1.726   -35.944 49.829 1.00 39.46  ?  145 ALA   A N   1 
ATOM   1167 C  CA  . ALA   A 1 146 ? 1.460   -34.980 48.760 1.00 38.17  ?  145 ALA   A CA  1 
ATOM   1168 C  C   . ALA   A 1 146 ? 2.602   -33.974 48.629 1.00 43.46  ?  145 ALA   A C   1 
ATOM   1169 O  O   . ALA   A 1 146 ? 3.198   -33.842 47.554 1.00 46.06  ?  145 ALA   A O   1 
ATOM   1170 C  CB  . ALA   A 1 146 ? 0.129   -34.266 48.985 1.00 36.50  ?  145 ALA   A CB  1 
ATOM   1171 N  N   . ASN   A 1 147 ? 2.966   -33.292 49.721 1.00 41.04  ?  146 ASN   A N   1 
ATOM   1172 C  CA  . ASN   A 1 147 ? 4.053   -32.320 49.604 1.00 40.19  ?  146 ASN   A CA  1 
ATOM   1173 C  C   . ASN   A 1 147 ? 5.354   -32.974 49.187 1.00 42.88  ?  146 ASN   A C   1 
ATOM   1174 O  O   . ASN   A 1 147 ? 6.136   -32.375 48.432 1.00 47.37  ?  146 ASN   A O   1 
ATOM   1175 C  CB  . ASN   A 1 147 ? 4.275   -31.548 50.893 1.00 38.59  ?  146 ASN   A CB  1 
ATOM   1176 C  CG  . ASN   A 1 147 ? 3.159   -30.613 51.188 1.00 50.79  ?  146 ASN   A CG  1 
ATOM   1177 O  OD1 . ASN   A 1 147 ? 2.006   -31.026 51.339 1.00 61.16  ?  146 ASN   A OD1 1 
ATOM   1178 N  ND2 . ASN   A 1 147 ? 3.473   -29.328 51.231 1.00 61.04  ?  146 ASN   A ND2 1 
ATOM   1179 N  N   . PHE   A 1 148 ? 5.624   -34.188 49.676 1.00 41.75  ?  147 PHE   A N   1 
ATOM   1180 C  CA  . PHE   A 1 148 ? 6.883   -34.822 49.314 1.00 37.25  ?  147 PHE   A CA  1 
ATOM   1181 C  C   . PHE   A 1 148 ? 6.957   -35.029 47.809 1.00 41.65  ?  147 PHE   A C   1 
ATOM   1182 O  O   . PHE   A 1 148 ? 7.949   -34.657 47.172 1.00 37.01  ?  147 PHE   A O   1 
ATOM   1183 C  CB  . PHE   A 1 148 ? 7.082   -36.140 50.061 1.00 33.05  ?  147 PHE   A CB  1 
ATOM   1184 C  CG  . PHE   A 1 148 ? 8.480   -36.696 49.913 1.00 34.60  ?  147 PHE   A CG  1 
ATOM   1185 C  CD1 . PHE   A 1 148 ? 9.579   -35.925 50.254 1.00 32.05  ?  147 PHE   A CD1 1 
ATOM   1186 C  CD2 . PHE   A 1 148 ? 8.698   -37.961 49.382 1.00 40.34  ?  147 PHE   A CD2 1 
ATOM   1187 C  CE1 . PHE   A 1 148 ? 10.855  -36.392 50.088 1.00 30.59  ?  147 PHE   A CE1 1 
ATOM   1188 C  CE2 . PHE   A 1 148 ? 9.997   -38.453 49.220 1.00 38.01  ?  147 PHE   A CE2 1 
ATOM   1189 C  CZ  . PHE   A 1 148 ? 11.070  -37.657 49.575 1.00 37.97  ?  147 PHE   A CZ  1 
ATOM   1190 N  N   . CYS   A 1 149 ? 5.887   -35.575 47.218 1.00 42.56  ?  148 CYS   A N   1 
ATOM   1191 C  CA  . CYS   A 1 149 ? 5.878   -35.814 45.780 1.00 40.68  ?  148 CYS   A CA  1 
ATOM   1192 C  C   . CYS   A 1 149 ? 5.930   -34.509 45.000 1.00 39.16  ?  148 CYS   A C   1 
ATOM   1193 O  O   . CYS   A 1 149 ? 6.585   -34.430 43.962 1.00 44.04  ?  148 CYS   A O   1 
ATOM   1194 C  CB  . CYS   A 1 149 ? 4.638   -36.606 45.386 1.00 46.69  ?  148 CYS   A CB  1 
ATOM   1195 S  SG  . CYS   A 1 149 ? 4.462   -38.187 46.200 1.00 42.36  ?  148 CYS   A SG  1 
ATOM   1196 N  N   . ALA   A 1 150 ? 5.250   -33.471 45.478 1.00 42.42  ?  149 ALA   A N   1 
ATOM   1197 C  CA  . ALA   A 1 150 ? 5.265   -32.205 44.750 1.00 42.81  ?  149 ALA   A CA  1 
ATOM   1198 C  C   . ALA   A 1 150 ? 6.664   -31.590 44.729 1.00 44.86  ?  149 ALA   A C   1 
ATOM   1199 O  O   . ALA   A 1 150 ? 7.096   -31.055 43.699 1.00 45.99  ?  149 ALA   A O   1 
ATOM   1200 C  CB  . ALA   A 1 150 ? 4.249   -31.246 45.357 1.00 43.94  ?  149 ALA   A CB  1 
ATOM   1201 N  N   . LEU   A 1 151 ? 7.399   -31.683 45.848 1.00 44.92  ?  150 LEU   A N   1 
ATOM   1202 C  CA  . LEU   A 1 151 ? 8.788   -31.214 45.886 1.00 44.35  ?  150 LEU   A CA  1 
ATOM   1203 C  C   . LEU   A 1 151 ? 9.692   -32.009 44.936 1.00 44.71  ?  150 LEU   A C   1 
ATOM   1204 O  O   . LEU   A 1 151 ? 10.609  -31.449 44.322 1.00 42.27  ?  150 LEU   A O   1 
ATOM   1205 C  CB  . LEU   A 1 151 ? 9.324   -31.296 47.317 1.00 38.46  ?  150 LEU   A CB  1 
ATOM   1206 C  CG  . LEU   A 1 151 ? 8.752   -30.260 48.301 1.00 47.17  ?  150 LEU   A CG  1 
ATOM   1207 C  CD1 . LEU   A 1 151 ? 9.379   -30.404 49.664 1.00 40.76  ?  150 LEU   A CD1 1 
ATOM   1208 C  CD2 . LEU   A 1 151 ? 8.940   -28.825 47.805 1.00 41.54  ?  150 LEU   A CD2 1 
ATOM   1209 N  N   . ILE   A 1 152 ? 9.477   -33.322 44.832 1.00 39.49  ?  151 ILE   A N   1 
ATOM   1210 C  CA  . ILE   A 1 152 ? 10.267  -34.132 43.910 1.00 42.52  ?  151 ILE   A CA  1 
ATOM   1211 C  C   . ILE   A 1 152 ? 10.058  -33.663 42.475 1.00 48.42  ?  151 ILE   A C   1 
ATOM   1212 O  O   . ILE   A 1 152 ? 11.026  -33.424 41.732 1.00 43.96  ?  151 ILE   A O   1 
ATOM   1213 C  CB  . ILE   A 1 152 ? 9.928   -35.621 44.112 1.00 47.99  ?  151 ILE   A CB  1 
ATOM   1214 C  CG1 . ILE   A 1 152 ? 10.035  -35.939 45.626 1.00 48.94  ?  151 ILE   A CG1 1 
ATOM   1215 C  CG2 . ILE   A 1 152 ? 10.633  -36.564 43.112 1.00 36.92  ?  151 ILE   A CG2 1 
ATOM   1216 C  CD1 . ILE   A 1 152 ? 10.089  -37.410 45.994 1.00 43.24  ?  151 ILE   A CD1 1 
ATOM   1217 N  N   . LEU   A 1 153 ? 8.790   -33.496 42.078 1.00 40.67  ?  152 LEU   A N   1 
ATOM   1218 C  CA  . LEU   A 1 153 ? 8.479   -32.919 40.781 1.00 40.96  ?  152 LEU   A CA  1 
ATOM   1219 C  C   . LEU   A 1 153 ? 9.209   -31.590 40.583 1.00 47.50  ?  152 LEU   A C   1 
ATOM   1220 O  O   . LEU   A 1 153 ? 9.854   -31.367 39.548 1.00 47.62  ?  152 LEU   A O   1 
ATOM   1221 C  CB  . LEU   A 1 153 ? 6.964   -32.759 40.655 1.00 41.34  ?  152 LEU   A CB  1 
ATOM   1222 C  CG  . LEU   A 1 153 ? 6.283   -34.116 40.494 1.00 45.17  ?  152 LEU   A CG  1 
ATOM   1223 C  CD1 . LEU   A 1 153 ? 4.751   -34.031 40.474 1.00 39.95  ?  152 LEU   A CD1 1 
ATOM   1224 C  CD2 . LEU   A 1 153 ? 6.840   -34.816 39.230 1.00 41.86  ?  152 LEU   A CD2 1 
ATOM   1225 N  N   . ALA   A 1 154 ? 9.154   -30.709 41.593 1.00 42.13  ?  153 ALA   A N   1 
ATOM   1226 C  CA  . ALA   A 1 154 ? 9.793   -29.407 41.466 1.00 37.37  ?  153 ALA   A CA  1 
ATOM   1227 C  C   . ALA   A 1 154 ? 11.312  -29.529 41.365 1.00 44.88  ?  153 ALA   A C   1 
ATOM   1228 O  O   . ALA   A 1 154 ? 11.941  -28.834 40.556 1.00 48.94  ?  153 ALA   A O   1 
ATOM   1229 C  CB  . ALA   A 1 154 ? 9.384   -28.523 42.631 1.00 41.19  ?  153 ALA   A CB  1 
ATOM   1230 N  N   . TYR   A 1 155 ? 11.929  -30.417 42.156 1.00 47.64  ?  154 TYR   A N   1 
ATOM   1231 C  CA  . TYR   A 1 155 ? 13.386  -30.539 42.092 1.00 48.19  ?  154 TYR   A CA  1 
ATOM   1232 C  C   . TYR   A 1 155 ? 13.844  -31.134 40.779 1.00 44.06  ?  154 TYR   A C   1 
ATOM   1233 O  O   . TYR   A 1 155 ? 14.985  -30.901 40.357 1.00 42.03  ?  154 TYR   A O   1 
ATOM   1234 C  CB  . TYR   A 1 155 ? 13.929  -31.395 43.235 1.00 45.00  ?  154 TYR   A CB  1 
ATOM   1235 C  CG  . TYR   A 1 155 ? 14.092  -30.631 44.513 1.00 44.30  ?  154 TYR   A CG  1 
ATOM   1236 C  CD1 . TYR   A 1 155 ? 13.187  -30.794 45.567 1.00 44.53  ?  154 TYR   A CD1 1 
ATOM   1237 C  CD2 . TYR   A 1 155 ? 15.124  -29.732 44.669 1.00 40.14  ?  154 TYR   A CD2 1 
ATOM   1238 C  CE1 . TYR   A 1 155 ? 13.314  -30.082 46.734 1.00 39.53  ?  154 TYR   A CE1 1 
ATOM   1239 C  CE2 . TYR   A 1 155 ? 15.261  -29.010 45.840 1.00 46.22  ?  154 TYR   A CE2 1 
ATOM   1240 C  CZ  . TYR   A 1 155 ? 14.347  -29.187 46.869 1.00 39.48  ?  154 TYR   A CZ  1 
ATOM   1241 O  OH  . TYR   A 1 155 ? 14.483  -28.468 48.036 1.00 38.96  ?  154 TYR   A OH  1 
ATOM   1242 N  N   . CYS   A 1 156 ? 12.985  -31.894 40.134 1.00 47.22  ?  155 CYS   A N   1 
ATOM   1243 C  CA  . CYS   A 1 156 ? 13.355  -32.593 38.919 1.00 54.37  ?  155 CYS   A CA  1 
ATOM   1244 C  C   . CYS   A 1 156 ? 13.049  -31.798 37.666 1.00 52.88  ?  155 CYS   A C   1 
ATOM   1245 O  O   . CYS   A 1 156 ? 13.412  -32.239 36.569 1.00 58.69  ?  155 CYS   A O   1 
ATOM   1246 C  CB  . CYS   A 1 156 ? 12.639  -33.936 38.870 1.00 52.48  ?  155 CYS   A CB  1 
ATOM   1247 S  SG  . CYS   A 1 156 ? 13.194  -35.034 40.169 1.00 41.37  ?  155 CYS   A SG  1 
ATOM   1248 N  N   . ASN   A 1 157 ? 12.431  -30.623 37.806 1.00 52.31  ?  156 ASN   A N   1 
ATOM   1249 C  CA  A ASN   A 1 157 ? 11.935  -29.836 36.680 0.56 51.69  ?  156 ASN   A CA  1 
ATOM   1250 C  CA  B ASN   A 1 157 ? 11.989  -29.853 36.649 0.44 52.67  ?  156 ASN   A CA  1 
ATOM   1251 C  C   . ASN   A 1 157 ? 11.094  -30.694 35.749 1.00 53.20  ?  156 ASN   A C   1 
ATOM   1252 O  O   . ASN   A 1 157 ? 11.006  -30.448 34.545 1.00 64.19  ?  156 ASN   A O   1 
ATOM   1253 C  CB  A ASN   A 1 157 ? 13.073  -29.151 35.929 0.56 49.53  ?  156 ASN   A CB  1 
ATOM   1254 C  CB  B ASN   A 1 157 ? 13.175  -29.290 35.844 0.44 49.34  ?  156 ASN   A CB  1 
ATOM   1255 C  CG  A ASN   A 1 157 ? 13.020  -27.655 36.072 0.56 48.20  ?  156 ASN   A CG  1 
ATOM   1256 C  CG  B ASN   A 1 157 ? 14.435  -29.106 36.683 0.44 49.25  ?  156 ASN   A CG  1 
ATOM   1257 O  OD1 A ASN   A 1 157 ? 11.975  -27.040 35.863 0.56 46.46  ?  156 ASN   A OD1 1 
ATOM   1258 O  OD1 B ASN   A 1 157 ? 15.348  -29.936 36.657 0.44 48.60  ?  156 ASN   A OD1 1 
ATOM   1259 N  ND2 A ASN   A 1 157 ? 14.138  -27.058 36.448 0.56 52.41  ?  156 ASN   A ND2 1 
ATOM   1260 N  ND2 B ASN   A 1 157 ? 14.498  -28.002 37.411 0.44 49.81  ?  156 ASN   A ND2 1 
ATOM   1261 N  N   . LYS   A 1 158 ? 10.485  -31.713 36.322 1.00 54.23  ?  157 LYS   A N   1 
ATOM   1262 C  CA  . LYS   A 1 158 ? 9.483   -32.550 35.698 1.00 54.31  ?  157 LYS   A CA  1 
ATOM   1263 C  C   . LYS   A 1 158 ? 8.136   -32.052 36.192 1.00 48.03  ?  157 LYS   A C   1 
ATOM   1264 O  O   . LYS   A 1 158 ? 8.047   -31.238 37.107 1.00 57.68  ?  157 LYS   A O   1 
ATOM   1265 C  CB  . LYS   A 1 158 ? 9.709   -34.034 36.052 1.00 53.05  ?  157 LYS   A CB  1 
ATOM   1266 C  CG  . LYS   A 1 158 ? 10.371  -34.871 34.956 1.00 51.59  ?  157 LYS   A CG  1 
ATOM   1267 C  CD  . LYS   A 1 158 ? 11.777  -34.371 34.634 1.00 56.77  ?  157 LYS   A CD  1 
ATOM   1268 C  CE  . LYS   A 1 158 ? 12.298  -34.982 33.321 1.00 70.22  ?  157 LYS   A CE  1 
ATOM   1269 N  NZ  . LYS   A 1 158 ? 13.770  -34.750 33.098 1.00 71.88  ?  157 LYS   A NZ  1 
ATOM   1270 N  N   . THR   A 1 159 ? 7.086   -32.521 35.560 1.00 46.74  ?  158 THR   A N   1 
ATOM   1271 C  CA  . THR   A 1 159 ? 5.747   -32.019 35.804 1.00 42.83  ?  158 THR   A CA  1 
ATOM   1272 C  C   . THR   A 1 159 ? 4.842   -33.235 35.751 1.00 49.82  ?  158 THR   A C   1 
ATOM   1273 O  O   . THR   A 1 159 ? 5.162   -34.218 35.069 1.00 51.95  ?  158 THR   A O   1 
ATOM   1274 C  CB  . THR   A 1 159 ? 5.346   -30.914 34.757 1.00 46.00  ?  158 THR   A CB  1 
ATOM   1275 O  OG1 . THR   A 1 159 ? 4.063   -31.180 34.173 1.00 37.05  ?  158 THR   A OG1 1 
ATOM   1276 C  CG2 . THR   A 1 159 ? 6.371   -30.815 33.614 1.00 50.13  ?  158 THR   A CG2 1 
ATOM   1277 N  N   . VAL   A 1 160 ? 3.759   -33.204 36.534 1.00 46.53  ?  159 VAL   A N   1 
ATOM   1278 C  CA  . VAL   A 1 160 ? 2.728   -34.232 36.447 1.00 45.76  ?  159 VAL   A CA  1 
ATOM   1279 C  C   . VAL   A 1 160 ? 2.516   -34.604 34.980 1.00 49.98  ?  159 VAL   A C   1 
ATOM   1280 O  O   . VAL   A 1 160 ? 2.537   -33.733 34.108 1.00 56.48  ?  159 VAL   A O   1 
ATOM   1281 C  CB  . VAL   A 1 160 ? 1.432   -33.743 37.108 1.00 46.41  ?  159 VAL   A CB  1 
ATOM   1282 C  CG1 . VAL   A 1 160 ? 0.270   -34.544 36.638 1.00 53.41  ?  159 VAL   A CG1 1 
ATOM   1283 C  CG2 . VAL   A 1 160 ? 1.543   -33.859 38.605 1.00 47.49  ?  159 VAL   A CG2 1 
ATOM   1284 N  N   . GLY   A 1 161 ? 2.400   -35.902 34.685 1.00 48.55  ?  160 GLY   A N   1 
ATOM   1285 C  CA  . GLY   A 1 161 ? 2.148   -36.371 33.340 1.00 57.98  ?  160 GLY   A CA  1 
ATOM   1286 C  C   . GLY   A 1 161 ? 3.374   -36.621 32.479 1.00 60.69  ?  160 GLY   A C   1 
ATOM   1287 O  O   . GLY   A 1 161 ? 3.256   -37.241 31.415 1.00 70.32  ?  160 GLY   A O   1 
ATOM   1288 N  N   . GLU   A 1 162 ? 4.526   -36.102 32.857 1.00 54.60  ?  161 GLU   A N   1 
ATOM   1289 C  CA  . GLU   A 1 162 ? 5.773   -36.583 32.291 1.00 53.25  ?  161 GLU   A CA  1 
ATOM   1290 C  C   . GLU   A 1 162 ? 6.030   -37.973 32.868 1.00 51.69  ?  161 GLU   A C   1 
ATOM   1291 O  O   . GLU   A 1 162 ? 5.773   -38.219 34.051 1.00 56.95  ?  161 GLU   A O   1 
ATOM   1292 C  CB  . GLU   A 1 162 ? 6.895   -35.596 32.656 1.00 55.85  ?  161 GLU   A CB  1 
ATOM   1293 C  CG  . GLU   A 1 162 ? 7.896   -35.253 31.575 1.00 62.58  ?  161 GLU   A CG  1 
ATOM   1294 C  CD  . GLU   A 1 162 ? 8.590   -33.910 31.828 1.00 70.75  ?  161 GLU   A CD  1 
ATOM   1295 O  OE1 . GLU   A 1 162 ? 8.024   -33.073 32.587 1.00 56.00  ?  161 GLU   A OE1 1 
ATOM   1296 O  OE2 . GLU   A 1 162 ? 9.698   -33.697 31.256 1.00 76.39  -1 161 GLU   A OE2 1 
ATOM   1297 N  N   . LEU   A 1 163 ? 6.484   -38.905 32.041 1.00 53.13  ?  162 LEU   A N   1 
ATOM   1298 C  CA  . LEU   A 1 163 ? 6.887   -40.206 32.563 1.00 50.48  ?  162 LEU   A CA  1 
ATOM   1299 C  C   . LEU   A 1 163 ? 8.352   -40.117 32.980 1.00 49.35  ?  162 LEU   A C   1 
ATOM   1300 O  O   . LEU   A 1 163 ? 9.197   -39.629 32.221 1.00 52.09  ?  162 LEU   A O   1 
ATOM   1301 C  CB  . LEU   A 1 163 ? 6.674   -41.320 31.536 1.00 54.71  ?  162 LEU   A CB  1 
ATOM   1302 C  CG  . LEU   A 1 163 ? 6.523   -42.732 32.124 1.00 65.20  ?  162 LEU   A CG  1 
ATOM   1303 C  CD1 . LEU   A 1 163 ? 7.796   -43.369 32.696 1.00 55.74  ?  162 LEU   A CD1 1 
ATOM   1304 C  CD2 . LEU   A 1 163 ? 5.506   -42.639 33.223 1.00 61.63  ?  162 LEU   A CD2 1 
ATOM   1305 N  N   . GLY   A 1 164 ? 8.648   -40.551 34.192 1.00 42.60  ?  163 GLY   A N   1 
ATOM   1306 C  CA  . GLY   A 1 164 ? 9.944   -40.305 34.776 1.00 39.81  ?  163 GLY   A CA  1 
ATOM   1307 C  C   . GLY   A 1 164 ? 10.833  -41.525 34.750 1.00 38.36  ?  163 GLY   A C   1 
ATOM   1308 O  O   . GLY   A 1 164 ? 10.422  -42.636 34.450 1.00 43.49  ?  163 GLY   A O   1 
ATOM   1309 N  N   . ASP   A 1 165 ? 12.093  -41.295 35.054 1.00 39.26  ?  164 ASP   A N   1 
ATOM   1310 C  CA  . ASP   A 1 165 ? 13.072  -42.371 35.164 1.00 43.12  ?  164 ASP   A CA  1 
ATOM   1311 C  C   . ASP   A 1 165 ? 13.526  -42.446 36.631 1.00 42.37  ?  164 ASP   A C   1 
ATOM   1312 O  O   . ASP   A 1 165 ? 13.995  -41.451 37.200 1.00 37.70  ?  164 ASP   A O   1 
ATOM   1313 C  CB  . ASP   A 1 165 ? 14.214  -42.110 34.182 1.00 37.82  ?  164 ASP   A CB  1 
ATOM   1314 C  CG  . ASP   A 1 165 ? 15.436  -42.924 34.476 1.00 45.14  ?  164 ASP   A CG  1 
ATOM   1315 O  OD1 . ASP   A 1 165 ? 16.070  -42.623 35.523 1.00 47.94  ?  164 ASP   A OD1 1 
ATOM   1316 O  OD2 . ASP   A 1 165 ? 15.803  -43.813 33.647 1.00 45.15  -1 164 ASP   A OD2 1 
ATOM   1317 N  N   . VAL   A 1 166 ? 13.352  -43.614 37.253 1.00 42.81  ?  165 VAL   A N   1 
ATOM   1318 C  CA  . VAL   A 1 166 ? 13.541  -43.705 38.704 1.00 44.51  ?  165 VAL   A CA  1 
ATOM   1319 C  C   . VAL   A 1 166 ? 14.988  -43.404 39.081 1.00 44.04  ?  165 VAL   A C   1 
ATOM   1320 O  O   . VAL   A 1 166 ? 15.245  -42.713 40.075 1.00 37.53  ?  165 VAL   A O   1 
ATOM   1321 C  CB  . VAL   A 1 166 ? 13.096  -45.083 39.231 1.00 39.26  ?  165 VAL   A CB  1 
ATOM   1322 C  CG1 . VAL   A 1 166 ? 13.727  -45.359 40.576 1.00 36.82  ?  165 VAL   A CG1 1 
ATOM   1323 C  CG2 . VAL   A 1 166 ? 11.576  -45.151 39.301 1.00 37.15  ?  165 VAL   A CG2 1 
ATOM   1324 N  N   . ARG   A 1 167 ? 15.956  -43.892 38.279 1.00 40.08  ?  166 ARG   A N   1 
ATOM   1325 C  CA  . ARG   A 1 167 ? 17.360  -43.637 38.604 1.00 39.49  ?  166 ARG   A CA  1 
ATOM   1326 C  C   . ARG   A 1 167 ? 17.668  -42.153 38.580 1.00 39.56  ?  166 ARG   A C   1 
ATOM   1327 O  O   . ARG   A 1 167 ? 18.337  -41.633 39.466 1.00 38.02  ?  166 ARG   A O   1 
ATOM   1328 C  CB  . ARG   A 1 167 ? 18.295  -44.362 37.641 1.00 35.44  ?  166 ARG   A CB  1 
ATOM   1329 C  CG  . ARG   A 1 167 ? 19.722  -44.253 38.093 1.00 33.59  ?  166 ARG   A CG  1 
ATOM   1330 C  CD  . ARG   A 1 167 ? 20.727  -44.827 37.121 1.00 43.49  ?  166 ARG   A CD  1 
ATOM   1331 N  NE  . ARG   A 1 167 ? 20.562  -44.309 35.768 1.00 57.56  ?  166 ARG   A NE  1 
ATOM   1332 C  CZ  . ARG   A 1 167 ? 21.568  -43.932 34.987 1.00 52.92  ?  166 ARG   A CZ  1 
ATOM   1333 N  NH1 . ARG   A 1 167 ? 22.828  -44.003 35.397 1.00 58.09  ?  166 ARG   A NH1 1 
ATOM   1334 N  NH2 . ARG   A 1 167 ? 21.304  -43.461 33.773 1.00 38.39  ?  166 ARG   A NH2 1 
ATOM   1335 N  N   . GLU   A 1 168 ? 17.193  -41.456 37.561 1.00 49.16  ?  167 GLU   A N   1 
ATOM   1336 C  CA  . GLU   A 1 168 ? 17.484  -40.040 37.458 1.00 43.08  ?  167 GLU   A CA  1 
ATOM   1337 C  C   . GLU   A 1 168 ? 16.757  -39.251 38.535 1.00 42.73  ?  167 GLU   A C   1 
ATOM   1338 O  O   . GLU   A 1 168 ? 17.300  -38.277 39.064 1.00 45.80  ?  167 GLU   A O   1 
ATOM   1339 C  CB  . GLU   A 1 168 ? 17.113  -39.562 36.063 1.00 40.14  ?  167 GLU   A CB  1 
ATOM   1340 C  CG  . GLU   A 1 168 ? 18.280  -39.613 35.104 1.00 38.62  ?  167 GLU   A CG  1 
ATOM   1341 C  CD  . GLU   A 1 168 ? 17.876  -39.209 33.702 1.00 47.05  ?  167 GLU   A CD  1 
ATOM   1342 O  OE1 . GLU   A 1 168 ? 18.308  -39.938 32.781 1.00 38.74  ?  167 GLU   A OE1 1 
ATOM   1343 O  OE2 . GLU   A 1 168 ? 17.124  -38.186 33.537 1.00 45.59  -1 167 GLU   A OE2 1 
ATOM   1344 N  N   . THR   A 1 169 ? 15.530  -39.663 38.872 1.00 39.83  ?  168 THR   A N   1 
ATOM   1345 C  CA  . THR   A 1 169 ? 14.799  -39.039 39.967 1.00 36.77  ?  168 THR   A CA  1 
ATOM   1346 C  C   . THR   A 1 169 ? 15.592  -39.111 41.258 1.00 47.27  ?  168 THR   A C   1 
ATOM   1347 O  O   . THR   A 1 169 ? 15.686  -38.119 41.995 1.00 50.55  ?  168 THR   A O   1 
ATOM   1348 C  CB  . THR   A 1 169 ? 13.448  -39.718 40.155 1.00 39.89  ?  168 THR   A CB  1 
ATOM   1349 O  OG1 . THR   A 1 169 ? 12.669  -39.614 38.942 1.00 43.84  ?  168 THR   A OG1 1 
ATOM   1350 C  CG2 . THR   A 1 169 ? 12.702  -39.103 41.365 1.00 30.22  ?  168 THR   A CG2 1 
ATOM   1351 N  N   . MET   A 1 170 ? 16.175  -40.279 41.550 1.00 46.77  ?  169 MET   A N   1 
ATOM   1352 C  CA  . MET   A 1 170 ? 17.009  -40.402 42.737 1.00 41.38  ?  169 MET   A CA  1 
ATOM   1353 C  C   . MET   A 1 170 ? 18.244  -39.529 42.633 1.00 43.25  ?  169 MET   A C   1 
ATOM   1354 O  O   . MET   A 1 170 ? 18.677  -38.927 43.630 1.00 47.42  ?  169 MET   A O   1 
ATOM   1355 C  CB  . MET   A 1 170 ? 17.431  -41.847 42.961 1.00 37.17  ?  169 MET   A CB  1 
ATOM   1356 C  CG  . MET   A 1 170 ? 16.313  -42.871 42.990 1.00 39.68  ?  169 MET   A CG  1 
ATOM   1357 S  SD  . MET   A 1 170 ? 15.563  -42.861 44.615 1.00 46.42  ?  169 MET   A SD  1 
ATOM   1358 C  CE  . MET   A 1 170 ? 14.143  -43.814 44.304 1.00 48.59  ?  169 MET   A CE  1 
ATOM   1359 N  N   . SER   A 1 171 ? 18.843  -39.457 41.448 1.00 41.36  ?  170 SER   A N   1 
ATOM   1360 C  CA  . SER   A 1 171 ? 20.085  -38.711 41.368 1.00 45.76  ?  170 SER   A CA  1 
ATOM   1361 C  C   . SER   A 1 171 ? 19.837  -37.219 41.570 1.00 45.95  ?  170 SER   A C   1 
ATOM   1362 O  O   . SER   A 1 171 ? 20.662  -36.538 42.181 1.00 44.52  ?  170 SER   A O   1 
ATOM   1363 C  CB  . SER   A 1 171 ? 20.784  -38.995 40.051 1.00 45.44  ?  170 SER   A CB  1 
ATOM   1364 O  OG  . SER   A 1 171 ? 22.001  -38.270 39.992 1.00 59.79  ?  170 SER   A OG  1 
ATOM   1365 N  N   . TYR   A 1 172 ? 18.691  -36.709 41.109 1.00 45.87  ?  171 TYR   A N   1 
ATOM   1366 C  CA  . TYR   A 1 172 ? 18.289  -35.343 41.442 1.00 44.51  ?  171 TYR   A CA  1 
ATOM   1367 C  C   . TYR   A 1 172 ? 18.216  -35.148 42.959 1.00 48.98  ?  171 TYR   A C   1 
ATOM   1368 O  O   . TYR   A 1 172 ? 18.673  -34.128 43.494 1.00 49.51  ?  171 TYR   A O   1 
ATOM   1369 C  CB  . TYR   A 1 172 ? 16.934  -35.017 40.783 1.00 46.67  ?  171 TYR   A CB  1 
ATOM   1370 C  CG  . TYR   A 1 172 ? 17.000  -34.413 39.375 1.00 55.98  ?  171 TYR   A CG  1 
ATOM   1371 C  CD1 . TYR   A 1 172 ? 17.641  -33.196 39.150 1.00 49.55  ?  171 TYR   A CD1 1 
ATOM   1372 C  CD2 . TYR   A 1 172 ? 16.395  -35.054 38.272 1.00 60.30  ?  171 TYR   A CD2 1 
ATOM   1373 C  CE1 . TYR   A 1 172 ? 17.713  -32.639 37.880 1.00 59.89  ?  171 TYR   A CE1 1 
ATOM   1374 C  CE2 . TYR   A 1 172 ? 16.455  -34.496 36.977 1.00 56.79  ?  171 TYR   A CE2 1 
ATOM   1375 C  CZ  . TYR   A 1 172 ? 17.119  -33.280 36.795 1.00 67.66  ?  171 TYR   A CZ  1 
ATOM   1376 O  OH  . TYR   A 1 172 ? 17.206  -32.676 35.548 1.00 66.64  ?  171 TYR   A OH  1 
ATOM   1377 N  N   . LEU   A 1 173 ? 17.663  -36.127 43.674 1.00 49.04  ?  172 LEU   A N   1 
ATOM   1378 C  CA  . LEU   A 1 173 ? 17.453  -35.972 45.109 1.00 47.40  ?  172 LEU   A CA  1 
ATOM   1379 C  C   . LEU   A 1 173 ? 18.739  -36.153 45.907 1.00 52.19  ?  172 LEU   A C   1 
ATOM   1380 O  O   . LEU   A 1 173 ? 18.965  -35.423 46.878 1.00 51.61  ?  172 LEU   A O   1 
ATOM   1381 C  CB  . LEU   A 1 173 ? 16.403  -36.962 45.583 1.00 42.86  ?  172 LEU   A CB  1 
ATOM   1382 C  CG  . LEU   A 1 173 ? 15.103  -36.719 44.838 1.00 46.23  ?  172 LEU   A CG  1 
ATOM   1383 C  CD1 . LEU   A 1 173 ? 14.165  -37.897 45.036 1.00 41.10  ?  172 LEU   A CD1 1 
ATOM   1384 C  CD2 . LEU   A 1 173 ? 14.471  -35.397 45.285 1.00 37.43  ?  172 LEU   A CD2 1 
ATOM   1385 N  N   . PHE   A 1 174 ? 19.589  -37.117 45.531 1.00 48.30  ?  173 PHE   A N   1 
ATOM   1386 C  CA  . PHE   A 1 174 ? 20.798  -37.348 46.311 1.00 43.46  ?  173 PHE   A CA  1 
ATOM   1387 C  C   . PHE   A 1 174 ? 21.722  -36.137 46.320 1.00 47.83  ?  173 PHE   A C   1 
ATOM   1388 O  O   . PHE   A 1 174 ? 22.587  -36.034 47.195 1.00 55.67  ?  173 PHE   A O   1 
ATOM   1389 C  CB  . PHE   A 1 174 ? 21.559  -38.559 45.772 1.00 48.36  ?  173 PHE   A CB  1 
ATOM   1390 C  CG  . PHE   A 1 174 ? 20.875  -39.884 46.014 1.00 46.79  ?  173 PHE   A CG  1 
ATOM   1391 C  CD1 . PHE   A 1 174 ? 19.829  -40.002 46.915 1.00 40.95  ?  173 PHE   A CD1 1 
ATOM   1392 C  CD2 . PHE   A 1 174 ? 21.301  -41.024 45.341 1.00 41.65  ?  173 PHE   A CD2 1 
ATOM   1393 C  CE1 . PHE   A 1 174 ? 19.216  -41.232 47.122 1.00 38.83  ?  173 PHE   A CE1 1 
ATOM   1394 C  CE2 . PHE   A 1 174 ? 20.697  -42.244 45.556 1.00 40.57  ?  173 PHE   A CE2 1 
ATOM   1395 C  CZ  . PHE   A 1 174 ? 19.658  -42.353 46.445 1.00 40.62  ?  173 PHE   A CZ  1 
ATOM   1396 N  N   . GLN   A 1 175 ? 21.570  -35.218 45.365 1.00 54.69  ?  174 GLN   A N   1 
ATOM   1397 C  CA  . GLN   A 1 175 ? 22.444  -34.050 45.309 1.00 52.86  ?  174 GLN   A CA  1 
ATOM   1398 C  C   . GLN   A 1 175 ? 22.235  -33.142 46.499 1.00 48.43  ?  174 GLN   A C   1 
ATOM   1399 O  O   . GLN   A 1 175 ? 23.114  -32.333 46.805 1.00 51.85  ?  174 GLN   A O   1 
ATOM   1400 C  CB  . GLN   A 1 175 ? 22.207  -33.264 44.019 1.00 53.84  ?  174 GLN   A CB  1 
ATOM   1401 C  CG  . GLN   A 1 175 ? 22.369  -34.102 42.790 1.00 50.49  ?  174 GLN   A CG  1 
ATOM   1402 C  CD  . GLN   A 1 175 ? 23.819  -34.402 42.488 1.00 59.99  ?  174 GLN   A CD  1 
ATOM   1403 O  OE1 . GLN   A 1 175 ? 24.735  -33.779 43.061 1.00 63.77  ?  174 GLN   A OE1 1 
ATOM   1404 N  NE2 . GLN   A 1 175 ? 24.047  -35.379 41.599 1.00 55.79  ?  174 GLN   A NE2 1 
ATOM   1405 N  N   . HIS   A 1 176 ? 21.078  -33.254 47.151 1.00 47.80  ?  175 HIS   A N   1 
ATOM   1406 C  CA  . HIS   A 1 176 ? 20.744  -32.520 48.360 1.00 48.82  ?  175 HIS   A CA  1 
ATOM   1407 C  C   . HIS   A 1 176 ? 20.607  -33.452 49.553 1.00 50.23  ?  175 HIS   A C   1 
ATOM   1408 O  O   . HIS   A 1 176 ? 20.000  -33.080 50.564 1.00 49.59  ?  175 HIS   A O   1 
ATOM   1409 C  CB  . HIS   A 1 176 ? 19.461  -31.708 48.152 1.00 53.37  ?  175 HIS   A CB  1 
ATOM   1410 C  CG  . HIS   A 1 176 ? 19.483  -30.863 46.918 1.00 56.95  ?  175 HIS   A CG  1 
ATOM   1411 N  ND1 . HIS   A 1 176 ? 20.203  -29.688 46.834 1.00 59.39  ?  175 HIS   A ND1 1 
ATOM   1412 C  CD2 . HIS   A 1 176 ? 18.919  -31.049 45.699 1.00 53.92  ?  175 HIS   A CD2 1 
ATOM   1413 C  CE1 . HIS   A 1 176 ? 20.073  -29.182 45.621 1.00 58.30  ?  175 HIS   A CE1 1 
ATOM   1414 N  NE2 . HIS   A 1 176 ? 19.296  -29.987 44.914 1.00 55.04  ?  175 HIS   A NE2 1 
ATOM   1415 N  N   . ALA   A 1 177 ? 21.139  -34.666 49.451 1.00 51.68  ?  176 ALA   A N   1 
ATOM   1416 C  CA  . ALA   A 1 177 ? 21.267  -35.539 50.606 1.00 49.86  ?  176 ALA   A CA  1 
ATOM   1417 C  C   . ALA   A 1 177 ? 22.667  -35.394 51.187 1.00 51.66  ?  176 ALA   A C   1 
ATOM   1418 O  O   . ALA   A 1 177 ? 23.606  -34.979 50.504 1.00 53.41  ?  176 ALA   A O   1 
ATOM   1419 C  CB  . ALA   A 1 177 ? 20.993  -36.994 50.241 1.00 40.44  ?  176 ALA   A CB  1 
ATOM   1420 N  N   . ASN   A 1 178 ? 22.786  -35.709 52.474 1.00 52.40  ?  177 ASN   A N   1 
ATOM   1421 C  CA  . ASN   A 1 178 ? 24.075  -35.690 53.159 1.00 53.96  ?  177 ASN   A CA  1 
ATOM   1422 C  C   . ASN   A 1 178 ? 24.733  -37.033 52.927 1.00 59.02  ?  177 ASN   A C   1 
ATOM   1423 O  O   . ASN   A 1 178 ? 24.579  -37.963 53.722 1.00 53.79  ?  177 ASN   A O   1 
ATOM   1424 C  CB  . ASN   A 1 178 ? 23.919  -35.445 54.650 1.00 59.71  ?  177 ASN   A CB  1 
ATOM   1425 C  CG  . ASN   A 1 178 ? 25.232  -35.039 55.309 1.00 64.75  ?  177 ASN   A CG  1 
ATOM   1426 O  OD1 . ASN   A 1 178 ? 25.410  -33.885 55.701 1.00 68.14  ?  177 ASN   A OD1 1 
ATOM   1427 N  ND2 . ASN   A 1 178 ? 26.175  -35.970 55.379 1.00 67.62  ?  177 ASN   A ND2 1 
ATOM   1428 N  N   . LEU   A 1 179 ? 25.452  -37.150 51.814 1.00 53.11  ?  178 LEU   A N   1 
ATOM   1429 C  CA  . LEU   A 1 179 ? 26.289  -38.313 51.576 1.00 50.68  ?  178 LEU   A CA  1 
ATOM   1430 C  C   . LEU   A 1 179 ? 27.757  -37.957 51.720 1.00 59.90  ?  178 LEU   A C   1 
ATOM   1431 O  O   . LEU   A 1 179 ? 28.629  -38.671 51.212 1.00 58.84  ?  178 LEU   A O   1 
ATOM   1432 C  CB  . LEU   A 1 179 ? 26.003  -38.920 50.208 1.00 47.81  ?  178 LEU   A CB  1 
ATOM   1433 C  CG  . LEU   A 1 179 ? 24.568  -38.878 49.709 1.00 47.16  ?  178 LEU   A CG  1 
ATOM   1434 C  CD1 . LEU   A 1 179 ? 24.627  -39.032 48.241 1.00 53.60  ?  178 LEU   A CD1 1 
ATOM   1435 C  CD2 . LEU   A 1 179 ? 23.741  -39.983 50.284 1.00 48.34  ?  178 LEU   A CD2 1 
ATOM   1436 N  N   . ASP   A 1 180 ? 28.041  -36.886 52.465 1.00 71.81  ?  179 ASP   A N   1 
ATOM   1437 C  CA  . ASP   A 1 180 ? 29.374  -36.302 52.555 1.00 72.98  ?  179 ASP   A CA  1 
ATOM   1438 C  C   . ASP   A 1 180 ? 30.400  -37.218 53.233 1.00 68.47  ?  179 ASP   A C   1 
ATOM   1439 O  O   . ASP   A 1 180 ? 31.603  -36.963 53.110 1.00 74.81  ?  179 ASP   A O   1 
ATOM   1440 C  CB  . ASP   A 1 180 ? 29.232  -34.927 53.236 1.00 65.48  ?  179 ASP   A CB  1 
ATOM   1441 C  CG  . ASP   A 1 180 ? 28.436  -33.897 52.344 1.00 85.50  ?  179 ASP   A CG  1 
ATOM   1442 O  OD1 . ASP   A 1 180 ? 28.255  -34.121 51.102 1.00 76.54  ?  179 ASP   A OD1 1 
ATOM   1443 O  OD2 . ASP   A 1 180 ? 27.936  -32.883 52.899 1.00 83.94  -1 179 ASP   A OD2 1 
ATOM   1444 N  N   . SER   A 1 181 ? 29.976  -38.300 53.888 1.00 65.19  ?  180 SER   A N   1 
ATOM   1445 C  CA  . SER   A 1 181 ? 30.910  -39.299 54.399 1.00 64.43  ?  180 SER   A CA  1 
ATOM   1446 C  C   . SER   A 1 181 ? 30.819  -40.624 53.636 1.00 66.67  ?  180 SER   A C   1 
ATOM   1447 O  O   . SER   A 1 181 ? 31.208  -41.673 54.171 1.00 65.31  ?  180 SER   A O   1 
ATOM   1448 C  CB  . SER   A 1 181 ? 30.678  -39.547 55.891 1.00 64.13  ?  180 SER   A CB  1 
ATOM   1449 O  OG  . SER   A 1 181 ? 29.444  -40.203 56.098 1.00 63.62  ?  180 SER   A OG  1 
ATOM   1450 N  N   . CYS   A 1 182 ? 30.286  -40.610 52.412 1.00 55.72  ?  181 CYS   A N   1 
ATOM   1451 C  CA  . CYS   A 1 182 ? 30.235  -41.812 51.593 1.00 54.90  ?  181 CYS   A CA  1 
ATOM   1452 C  C   . CYS   A 1 182 ? 31.469  -41.869 50.713 1.00 57.42  ?  181 CYS   A C   1 
ATOM   1453 O  O   . CYS   A 1 182 ? 31.827  -40.878 50.073 1.00 59.84  ?  181 CYS   A O   1 
ATOM   1454 C  CB  . CYS   A 1 182 ? 28.974  -41.845 50.739 1.00 51.27  ?  181 CYS   A CB  1 
ATOM   1455 S  SG  . CYS   A 1 182 ? 27.517  -42.091 51.755 1.00 49.73  ?  181 CYS   A SG  1 
ATOM   1456 N  N   . LYS   A 1 183 ? 32.126  -43.020 50.692 1.00 54.54  ?  182 LYS   A N   1 
ATOM   1457 C  CA  . LYS   A 1 183 ? 33.406  -43.130 50.021 1.00 52.26  ?  182 LYS   A CA  1 
ATOM   1458 C  C   . LYS   A 1 183 ? 33.408  -44.430 49.257 1.00 50.92  ?  182 LYS   A C   1 
ATOM   1459 O  O   . LYS   A 1 183 ? 32.938  -45.444 49.776 1.00 52.25  ?  182 LYS   A O   1 
ATOM   1460 C  CB  . LYS   A 1 183 ? 34.558  -43.084 51.025 1.00 57.30  ?  182 LYS   A CB  1 
ATOM   1461 C  CG  . LYS   A 1 183 ? 35.946  -43.033 50.419 1.00 58.51  ?  182 LYS   A CG  1 
ATOM   1462 C  CD  . LYS   A 1 183 ? 36.971  -42.676 51.493 1.00 68.12  ?  182 LYS   A CD  1 
ATOM   1463 C  CE  . LYS   A 1 183 ? 37.871  -43.862 51.847 1.00 72.15  ?  182 LYS   A CE  1 
ATOM   1464 N  NZ  . LYS   A 1 183 ? 38.927  -43.469 52.819 1.00 77.17  ?  182 LYS   A NZ  1 
ATOM   1465 N  N   . ARG   A 1 184 ? 33.882  -44.380 48.014 1.00 53.30  ?  183 ARG   A N   1 
ATOM   1466 C  CA  . ARG   A 1 184 ? 34.043  -45.552 47.164 1.00 51.99  ?  183 ARG   A CA  1 
ATOM   1467 C  C   . ARG   A 1 184 ? 35.434  -45.516 46.550 1.00 56.38  ?  183 ARG   A C   1 
ATOM   1468 O  O   . ARG   A 1 184 ? 35.838  -44.511 45.962 1.00 58.72  ?  183 ARG   A O   1 
ATOM   1469 C  CB  . ARG   A 1 184 ? 32.990  -45.627 46.054 1.00 43.84  ?  183 ARG   A CB  1 
ATOM   1470 C  CG  . ARG   A 1 184 ? 33.423  -46.552 44.921 1.00 47.14  ?  183 ARG   A CG  1 
ATOM   1471 C  CD  . ARG   A 1 184 ? 32.302  -46.938 43.977 1.00 45.96  ?  183 ARG   A CD  1 
ATOM   1472 N  NE  . ARG   A 1 184 ? 31.167  -47.521 44.679 1.00 48.42  ?  183 ARG   A NE  1 
ATOM   1473 C  CZ  . ARG   A 1 184 ? 29.927  -47.537 44.215 1.00 45.90  ?  183 ARG   A CZ  1 
ATOM   1474 N  NH1 . ARG   A 1 184 ? 29.621  -47.007 43.047 1.00 56.58  ?  183 ARG   A NH1 1 
ATOM   1475 N  NH2 . ARG   A 1 184 ? 28.968  -48.086 44.949 1.00 50.96  ?  183 ARG   A NH2 1 
ATOM   1476 N  N   . VAL   A 1 185 ? 36.174  -46.596 46.710 1.00 55.99  ?  184 VAL   A N   1 
ATOM   1477 C  CA  . VAL   A 1 185 ? 37.497  -46.728 46.135 1.00 52.70  ?  184 VAL   A CA  1 
ATOM   1478 C  C   . VAL   A 1 185 ? 37.412  -47.936 45.243 1.00 53.44  ?  184 VAL   A C   1 
ATOM   1479 O  O   . VAL   A 1 185 ? 36.990  -49.008 45.689 1.00 58.01  ?  184 VAL   A O   1 
ATOM   1480 C  CB  . VAL   A 1 185 ? 38.593  -46.906 47.203 1.00 55.57  ?  184 VAL   A CB  1 
ATOM   1481 C  CG1 . VAL   A 1 185 ? 39.958  -47.011 46.547 1.00 55.29  ?  184 VAL   A CG1 1 
ATOM   1482 C  CG2 . VAL   A 1 185 ? 38.569  -45.764 48.214 1.00 50.69  ?  184 VAL   A CG2 1 
ATOM   1483 N  N   . LEU   A 1 186 ? 37.762  -47.767 43.984 1.00 58.83  ?  185 LEU   A N   1 
ATOM   1484 C  CA  . LEU   A 1 186 ? 37.758  -48.896 43.080 1.00 61.57  ?  185 LEU   A CA  1 
ATOM   1485 C  C   . LEU   A 1 186 ? 39.050  -48.936 42.278 1.00 65.46  ?  185 LEU   A C   1 
ATOM   1486 O  O   . LEU   A 1 186 ? 39.788  -47.955 42.178 1.00 64.36  ?  185 LEU   A O   1 
ATOM   1487 C  CB  . LEU   A 1 186 ? 36.522  -48.878 42.191 1.00 57.36  ?  185 LEU   A CB  1 
ATOM   1488 C  CG  . LEU   A 1 186 ? 36.309  -47.632 41.374 1.00 59.18  ?  185 LEU   A CG  1 
ATOM   1489 C  CD1 . LEU   A 1 186 ? 36.857  -47.857 40.001 1.00 71.55  ?  185 LEU   A CD1 1 
ATOM   1490 C  CD2 . LEU   A 1 186 ? 34.823  -47.415 41.288 1.00 53.81  ?  185 LEU   A CD2 1 
ATOM   1491 N  N   . ASN   A 1 187 ? 39.333  -50.121 41.755 1.00 67.47  ?  186 ASN   A N   1 
ATOM   1492 C  CA  . ASN   A 1 187 ? 40.595  -50.442 41.114 1.00 67.47  ?  186 ASN   A CA  1 
ATOM   1493 C  C   . ASN   A 1 187 ? 40.273  -50.924 39.717 1.00 66.40  ?  186 ASN   A C   1 
ATOM   1494 O  O   . ASN   A 1 187 ? 39.416  -51.796 39.547 1.00 70.58  ?  186 ASN   A O   1 
ATOM   1495 C  CB  . ASN   A 1 187 ? 41.335  -51.534 41.894 1.00 73.96  ?  186 ASN   A CB  1 
ATOM   1496 C  CG  . ASN   A 1 187 ? 42.842  -51.382 41.845 1.00 79.00  ?  186 ASN   A CG  1 
ATOM   1497 O  OD1 . ASN   A 1 187 ? 43.430  -50.626 42.628 1.00 82.95  ?  186 ASN   A OD1 1 
ATOM   1498 N  ND2 . ASN   A 1 187 ? 43.480  -52.123 40.941 1.00 78.31  ?  186 ASN   A ND2 1 
ATOM   1499 N  N   . VAL   A 1 188 ? 40.928  -50.355 38.718 1.00 68.60  ?  187 VAL   A N   1 
ATOM   1500 C  CA  . VAL   A 1 188 ? 40.730  -50.794 37.343 1.00 76.68  ?  187 VAL   A CA  1 
ATOM   1501 C  C   . VAL   A 1 188 ? 42.064  -51.298 36.810 1.00 73.60  ?  187 VAL   A C   1 
ATOM   1502 O  O   . VAL   A 1 188 ? 43.106  -50.663 37.021 1.00 69.04  ?  187 VAL   A O   1 
ATOM   1503 C  CB  . VAL   A 1 188 ? 40.114  -49.686 36.464 1.00 63.89  ?  187 VAL   A CB  1 
ATOM   1504 C  CG1 . VAL   A 1 188 ? 40.832  -48.356 36.671 1.00 73.70  ?  187 VAL   A CG1 1 
ATOM   1505 C  CG2 . VAL   A 1 188 ? 40.102  -50.113 35.030 1.00 48.58  ?  187 VAL   A CG2 1 
ATOM   1506 N  N   . VAL   A 1 189 ? 42.027  -52.460 36.158 1.00 73.23  ?  188 VAL   A N   1 
ATOM   1507 C  CA  . VAL   A 1 189 ? 43.204  -53.273 35.884 1.00 71.81  ?  188 VAL   A CA  1 
ATOM   1508 C  C   . VAL   A 1 189 ? 43.188  -53.634 34.407 1.00 71.29  ?  188 VAL   A C   1 
ATOM   1509 O  O   . VAL   A 1 189 ? 42.216  -54.226 33.925 1.00 70.11  ?  188 VAL   A O   1 
ATOM   1510 C  CB  . VAL   A 1 189 ? 43.227  -54.542 36.755 1.00 72.50  ?  188 VAL   A CB  1 
ATOM   1511 C  CG1 . VAL   A 1 189 ? 44.107  -55.605 36.127 1.00 70.25  ?  188 VAL   A CG1 1 
ATOM   1512 C  CG2 . VAL   A 1 189 ? 43.681  -54.215 38.180 1.00 67.72  ?  188 VAL   A CG2 1 
ATOM   1513 N  N   . CYS   A 1 190 ? 44.253  -53.263 33.692 1.00 79.19  ?  189 CYS   A N   1 
ATOM   1514 C  CA  . CYS   A 1 190 ? 44.411  -53.513 32.262 1.00 83.01  ?  189 CYS   A CA  1 
ATOM   1515 C  C   . CYS   A 1 190 ? 45.545  -54.500 32.021 1.00 84.73  ?  189 CYS   A C   1 
ATOM   1516 O  O   . CYS   A 1 190 ? 46.597  -54.422 32.669 1.00 78.16  ?  189 CYS   A O   1 
ATOM   1517 C  CB  . CYS   A 1 190 ? 44.705  -52.216 31.500 1.00 80.74  ?  189 CYS   A CB  1 
ATOM   1518 S  SG  . CYS   A 1 190 ? 44.659  -52.367 29.695 1.00 81.74  ?  189 CYS   A SG  1 
ATOM   1519 N  N   . LYS   A 1 191 ? 45.329  -55.426 31.078 1.00 85.90  ?  190 LYS   A N   1 
ATOM   1520 C  CA  . LYS   A 1 191 ? 46.393  -56.361 30.718 1.00 90.37  ?  190 LYS   A CA  1 
ATOM   1521 C  C   . LYS   A 1 191 ? 47.626  -55.603 30.243 1.00 89.71  ?  190 LYS   A C   1 
ATOM   1522 O  O   . LYS   A 1 191 ? 48.761  -55.978 30.567 1.00 85.86  ?  190 LYS   A O   1 
ATOM   1523 C  CB  . LYS   A 1 191 ? 45.904  -57.344 29.646 1.00 91.66  ?  190 LYS   A CB  1 
ATOM   1524 C  CG  . LYS   A 1 191 ? 44.907  -56.744 28.653 1.00 100.40 ?  190 LYS   A CG  1 
ATOM   1525 C  CD  . LYS   A 1 191 ? 43.460  -57.155 28.946 1.00 96.23  ?  190 LYS   A CD  1 
ATOM   1526 C  CE  . LYS   A 1 191 ? 43.079  -58.458 28.258 1.00 90.52  ?  190 LYS   A CE  1 
ATOM   1527 N  NZ  . LYS   A 1 191 ? 41.706  -58.342 27.694 1.00 93.94  ?  190 LYS   A NZ  1 
ATOM   1528 N  N   . THR   A 1 192 ? 47.410  -54.494 29.522 1.00 88.62  ?  191 THR   A N   1 
ATOM   1529 C  CA  . THR   A 1 192 ? 48.491  -53.649 28.998 1.00 83.33  ?  191 THR   A CA  1 
ATOM   1530 C  C   . THR   A 1 192 ? 48.900  -52.560 29.995 1.00 85.35  ?  191 THR   A C   1 
ATOM   1531 O  O   . THR   A 1 192 ? 49.986  -52.625 30.579 1.00 81.45  ?  191 THR   A O   1 
ATOM   1532 C  CB  . THR   A 1 192 ? 48.048  -53.053 27.660 1.00 80.43  ?  191 THR   A CB  1 
ATOM   1533 O  OG1 . THR   A 1 192 ? 47.961  -54.098 26.687 1.00 86.17  ?  191 THR   A OG1 1 
ATOM   1534 C  CG2 . THR   A 1 192 ? 49.042  -52.014 27.174 1.00 77.78  ?  191 THR   A CG2 1 
ATOM   1535 N  N   . CYS   A 1 193 ? 48.026  -51.559 30.214 1.00 84.60  ?  192 CYS   A N   1 
ATOM   1536 C  CA  . CYS   A 1 193 ? 48.435  -50.342 30.928 1.00 84.87  ?  192 CYS   A CA  1 
ATOM   1537 C  C   . CYS   A 1 193 ? 48.806  -50.596 32.385 1.00 84.60  ?  192 CYS   A C   1 
ATOM   1538 O  O   . CYS   A 1 193 ? 49.660  -49.886 32.932 1.00 81.27  ?  192 CYS   A O   1 
ATOM   1539 C  CB  . CYS   A 1 193 ? 47.337  -49.273 30.904 1.00 86.99  ?  192 CYS   A CB  1 
ATOM   1540 S  SG  . CYS   A 1 193 ? 46.337  -49.048 29.420 1.00 79.79  ?  192 CYS   A SG  1 
ATOM   1541 N  N   . GLY   A 1 194 ? 48.145  -51.547 33.047 1.00 84.97  ?  193 GLY   A N   1 
ATOM   1542 C  CA  . GLY   A 1 194 ? 48.370  -51.806 34.455 1.00 84.87  ?  193 GLY   A CA  1 
ATOM   1543 C  C   . GLY   A 1 194 ? 47.134  -51.510 35.292 1.00 80.57  ?  193 GLY   A C   1 
ATOM   1544 O  O   . GLY   A 1 194 ? 45.998  -51.601 34.810 1.00 77.03  ?  193 GLY   A O   1 
ATOM   1545 N  N   . GLN   A 1 195 ? 47.371  -51.153 36.552 1.00 76.59  ?  194 GLN   A N   1 
ATOM   1546 C  CA  . GLN   A 1 195 ? 46.303  -50.909 37.511 1.00 79.92  ?  194 GLN   A CA  1 
ATOM   1547 C  C   . GLN   A 1 195 ? 46.296  -49.450 37.961 1.00 82.61  ?  194 GLN   A C   1 
ATOM   1548 O  O   . GLN   A 1 195 ? 47.349  -48.847 38.183 1.00 86.76  ?  194 GLN   A O   1 
ATOM   1549 C  CB  . GLN   A 1 195 ? 46.414  -51.892 38.717 1.00 84.48  ?  194 GLN   A CB  1 
ATOM   1550 C  CG  . GLN   A 1 195 ? 47.824  -52.368 39.131 1.00 89.80  ?  194 GLN   A CG  1 
ATOM   1551 C  CD  . GLN   A 1 195 ? 48.714  -51.278 39.737 1.00 102.78 ?  194 GLN   A CD  1 
ATOM   1552 O  OE1 . GLN   A 1 195 ? 48.229  -50.251 40.225 1.00 102.68 ?  194 GLN   A OE1 1 
ATOM   1553 N  NE2 . GLN   A 1 195 ? 50.033  -51.506 39.706 1.00 97.13  ?  194 GLN   A NE2 1 
ATOM   1554 N  N   . GLN   A 1 196 ? 45.102  -48.867 38.057 1.00 80.87  ?  195 GLN   A N   1 
ATOM   1555 C  CA  . GLN   A 1 196 ? 44.943  -47.507 38.562 1.00 80.71  ?  195 GLN   A CA  1 
ATOM   1556 C  C   . GLN   A 1 196 ? 43.832  -47.473 39.595 1.00 80.25  ?  195 GLN   A C   1 
ATOM   1557 O  O   . GLN   A 1 196 ? 42.696  -47.860 39.299 1.00 82.62  ?  195 GLN   A O   1 
ATOM   1558 C  CB  . GLN   A 1 196 ? 44.627  -46.512 37.448 1.00 87.03  ?  195 GLN   A CB  1 
ATOM   1559 C  CG  . GLN   A 1 196 ? 44.417  -45.098 37.984 1.00 84.63  ?  195 GLN   A CG  1 
ATOM   1560 C  CD  . GLN   A 1 196 ? 44.432  -44.060 36.891 1.00 93.72  ?  195 GLN   A CD  1 
ATOM   1561 O  OE1 . GLN   A 1 196 ? 44.461  -44.393 35.700 1.00 98.43  ?  195 GLN   A OE1 1 
ATOM   1562 N  NE2 . GLN   A 1 196 ? 44.427  -42.791 37.282 1.00 94.02  ?  195 GLN   A NE2 1 
ATOM   1563 N  N   . GLN   A 1 197 ? 44.155  -46.993 40.793 1.00 77.22  ?  196 GLN   A N   1 
ATOM   1564 C  CA  . GLN   A 1 197 ? 43.141  -46.781 41.810 1.00 72.88  ?  196 GLN   A CA  1 
ATOM   1565 C  C   . GLN   A 1 197 ? 42.444  -45.450 41.579 1.00 73.06  ?  196 GLN   A C   1 
ATOM   1566 O  O   . GLN   A 1 197 ? 43.065  -44.457 41.192 1.00 78.39  ?  196 GLN   A O   1 
ATOM   1567 C  CB  . GLN   A 1 197 ? 43.753  -46.832 43.209 1.00 76.83  ?  196 GLN   A CB  1 
ATOM   1568 C  CG  . GLN   A 1 197 ? 42.769  -47.233 44.311 1.00 78.88  ?  196 GLN   A CG  1 
ATOM   1569 C  CD  . GLN   A 1 197 ? 43.439  -47.445 45.666 1.00 74.54  ?  196 GLN   A CD  1 
ATOM   1570 O  OE1 . GLN   A 1 197 ? 43.741  -46.488 46.384 1.00 65.57  ?  196 GLN   A OE1 1 
ATOM   1571 N  NE2 . GLN   A 1 197 ? 43.627  -48.707 46.040 1.00 80.08  ?  196 GLN   A NE2 1 
ATOM   1572 N  N   . THR   A 1 198 ? 41.139  -45.446 41.807 1.00 74.80  ?  197 THR   A N   1 
ATOM   1573 C  CA  . THR   A 1 198 ? 40.290  -44.289 41.587 1.00 67.09  ?  197 THR   A CA  1 
ATOM   1574 C  C   . THR   A 1 198 ? 39.340  -44.204 42.769 1.00 63.35  ?  197 THR   A C   1 
ATOM   1575 O  O   . THR   A 1 198 ? 38.657  -45.178 43.097 1.00 62.16  ?  197 THR   A O   1 
ATOM   1576 C  CB  . THR   A 1 198 ? 39.530  -44.419 40.267 1.00 66.28  ?  197 THR   A CB  1 
ATOM   1577 O  OG1 . THR   A 1 198 ? 40.481  -44.610 39.214 1.00 79.48  ?  197 THR   A OG1 1 
ATOM   1578 C  CG2 . THR   A 1 198 ? 38.720  -43.164 39.984 1.00 59.34  ?  197 THR   A CG2 1 
ATOM   1579 N  N   . THR   A 1 199 ? 39.313  -43.052 43.416 1.00 63.65  ?  198 THR   A N   1 
ATOM   1580 C  CA  . THR   A 1 199 ? 38.634  -42.883 44.695 1.00 61.33  ?  198 THR   A CA  1 
ATOM   1581 C  C   . THR   A 1 199 ? 37.610  -41.752 44.583 1.00 59.50  ?  198 THR   A C   1 
ATOM   1582 O  O   . THR   A 1 199 ? 37.974  -40.588 44.397 1.00 67.86  ?  198 THR   A O   1 
ATOM   1583 C  CB  . THR   A 1 199 ? 39.674  -42.641 45.794 1.00 57.45  ?  198 THR   A CB  1 
ATOM   1584 O  OG1 . THR   A 1 199 ? 39.034  -42.227 47.000 1.00 62.73  ?  198 THR   A OG1 1 
ATOM   1585 C  CG2 . THR   A 1 199 ? 40.721  -41.627 45.359 1.00 72.18  ?  198 THR   A CG2 1 
ATOM   1586 N  N   . LEU   A 1 200 ? 36.325  -42.087 44.666 1.00 61.08  ?  199 LEU   A N   1 
ATOM   1587 C  CA  . LEU   A 1 200 ? 35.270  -41.092 44.517 1.00 61.39  ?  199 LEU   A CA  1 
ATOM   1588 C  C   . LEU   A 1 200 ? 34.347  -41.085 45.742 1.00 59.47  ?  199 LEU   A C   1 
ATOM   1589 O  O   . LEU   A 1 200 ? 34.460  -41.913 46.652 1.00 59.43  ?  199 LEU   A O   1 
ATOM   1590 C  CB  . LEU   A 1 200 ? 34.506  -41.310 43.203 1.00 58.50  ?  199 LEU   A CB  1 
ATOM   1591 C  CG  . LEU   A 1 200 ? 34.328  -42.712 42.668 1.00 51.75  ?  199 LEU   A CG  1 
ATOM   1592 C  CD1 . LEU   A 1 200 ? 33.271  -43.301 43.519 1.00 57.88  ?  199 LEU   A CD1 1 
ATOM   1593 C  CD2 . LEU   A 1 200 ? 33.870  -42.675 41.233 1.00 46.39  ?  199 LEU   A CD2 1 
ATOM   1594 N  N   . LYS   A 1 201 ? 33.464  -40.091 45.812 1.00 58.93  ?  200 LYS   A N   1 
ATOM   1595 C  CA  . LYS   A 1 201 ? 32.807  -39.804 47.079 1.00 56.08  ?  200 LYS   A CA  1 
ATOM   1596 C  C   . LYS   A 1 201 ? 31.460  -39.135 46.812 1.00 58.56  ?  200 LYS   A C   1 
ATOM   1597 O  O   . LYS   A 1 201 ? 31.082  -38.879 45.663 1.00 57.47  ?  200 LYS   A O   1 
ATOM   1598 C  CB  . LYS   A 1 201 ? 33.736  -38.984 47.982 1.00 46.55  ?  200 LYS   A CB  1 
ATOM   1599 C  CG  . LYS   A 1 201 ? 33.694  -37.508 47.761 1.00 62.81  ?  200 LYS   A CG  1 
ATOM   1600 C  CD  . LYS   A 1 201 ? 34.026  -36.732 49.051 1.00 77.53  ?  200 LYS   A CD  1 
ATOM   1601 C  CE  . LYS   A 1 201 ? 33.352  -35.337 49.104 1.00 76.92  ?  200 LYS   A CE  1 
ATOM   1602 N  NZ  . LYS   A 1 201 ? 31.845  -35.409 49.123 1.00 75.90  ?  200 LYS   A NZ  1 
ATOM   1603 N  N   . GLY   A 1 202 ? 30.707  -38.917 47.890 1.00 55.89  ?  201 GLY   A N   1 
ATOM   1604 C  CA  . GLY   A 1 202 ? 29.349  -38.403 47.796 1.00 51.25  ?  201 GLY   A CA  1 
ATOM   1605 C  C   . GLY   A 1 202 ? 28.486  -39.242 46.884 1.00 53.76  ?  201 GLY   A C   1 
ATOM   1606 O  O   . GLY   A 1 202 ? 28.687  -40.451 46.737 1.00 57.92  ?  201 GLY   A O   1 
ATOM   1607 N  N   . VAL   A 1 203 ? 27.522  -38.583 46.241 1.00 54.47  ?  202 VAL   A N   1 
ATOM   1608 C  CA  . VAL   A 1 203 ? 26.622  -39.154 45.236 1.00 51.90  ?  202 VAL   A CA  1 
ATOM   1609 C  C   . VAL   A 1 203 ? 27.301  -40.124 44.270 1.00 52.17  ?  202 VAL   A C   1 
ATOM   1610 O  O   . VAL   A 1 203 ? 26.663  -41.046 43.754 1.00 51.25  ?  202 VAL   A O   1 
ATOM   1611 C  CB  . VAL   A 1 203 ? 25.951  -38.015 44.445 1.00 57.65  ?  202 VAL   A CB  1 
ATOM   1612 C  CG1 . VAL   A 1 203 ? 24.675  -38.486 43.803 1.00 53.79  ?  202 VAL   A CG1 1 
ATOM   1613 C  CG2 . VAL   A 1 203 ? 25.679  -36.826 45.359 1.00 58.99  ?  202 VAL   A CG2 1 
ATOM   1614 N  N   . GLU   A 1 204 ? 28.585  -39.923 43.987 1.00 53.50  ?  203 GLU   A N   1 
ATOM   1615 C  CA  . GLU   A 1 204 ? 29.246  -40.836 43.064 1.00 59.20  ?  203 GLU   A CA  1 
ATOM   1616 C  C   . GLU   A 1 204 ? 29.693  -42.120 43.746 1.00 58.53  ?  203 GLU   A C   1 
ATOM   1617 O  O   . GLU   A 1 204 ? 29.973  -43.111 43.056 1.00 57.58  ?  203 GLU   A O   1 
ATOM   1618 C  CB  . GLU   A 1 204 ? 30.444  -40.146 42.400 1.00 66.63  ?  203 GLU   A CB  1 
ATOM   1619 C  CG  . GLU   A 1 204 ? 30.098  -39.254 41.203 1.00 64.30  ?  203 GLU   A CG  1 
ATOM   1620 C  CD  . GLU   A 1 204 ? 31.199  -39.245 40.160 1.00 81.31  ?  203 GLU   A CD  1 
ATOM   1621 O  OE1 . GLU   A 1 204 ? 31.304  -40.220 39.362 1.00 80.48  ?  203 GLU   A OE1 1 
ATOM   1622 O  OE2 . GLU   A 1 204 ? 31.988  -38.272 40.171 1.00 77.69  -1 203 GLU   A OE2 1 
ATOM   1623 N  N   . ALA   A 1 205 ? 29.754  -42.122 45.083 1.00 55.76  ?  204 ALA   A N   1 
ATOM   1624 C  CA  . ALA   A 1 205 ? 30.212  -43.283 45.828 1.00 50.08  ?  204 ALA   A CA  1 
ATOM   1625 C  C   . ALA   A 1 205 ? 29.140  -44.346 45.981 1.00 53.70  ?  204 ALA   A C   1 
ATOM   1626 O  O   . ALA   A 1 205 ? 29.481  -45.501 46.246 1.00 57.70  ?  204 ALA   A O   1 
ATOM   1627 C  CB  . ALA   A 1 205 ? 30.701  -42.864 47.216 1.00 47.40  ?  204 ALA   A CB  1 
ATOM   1628 N  N   . VAL   A 1 206 ? 27.863  -43.992 45.840 1.00 50.80  ?  205 VAL   A N   1 
ATOM   1629 C  CA  . VAL   A 1 206 ? 26.767  -44.891 46.172 1.00 47.93  ?  205 VAL   A CA  1 
ATOM   1630 C  C   . VAL   A 1 206 ? 25.908  -45.243 44.975 1.00 49.56  ?  205 VAL   A C   1 
ATOM   1631 O  O   . VAL   A 1 206 ? 24.887  -45.919 45.155 1.00 43.63  ?  205 VAL   A O   1 
ATOM   1632 C  CB  . VAL   A 1 206 ? 25.876  -44.316 47.293 1.00 50.56  ?  205 VAL   A CB  1 
ATOM   1633 C  CG1 . VAL   A 1 206 ? 26.726  -43.819 48.469 1.00 47.22  ?  205 VAL   A CG1 1 
ATOM   1634 C  CG2 . VAL   A 1 206 ? 24.959  -43.225 46.752 1.00 43.59  ?  205 VAL   A CG2 1 
ATOM   1635 N  N   . MET   A 1 207 ? 26.288  -44.801 43.756 1.00 50.84  ?  206 MET   A N   1 
ATOM   1636 C  CA  . MET   A 1 207 ? 25.514  -44.971 42.519 1.00 41.35  ?  206 MET   A CA  1 
ATOM   1637 C  C   . MET   A 1 207 ? 26.404  -45.550 41.425 1.00 41.84  ?  206 MET   A C   1 
ATOM   1638 O  O   . MET   A 1 207 ? 27.513  -45.052 41.179 1.00 42.17  ?  206 MET   A O   1 
ATOM   1639 C  CB  . MET   A 1 207 ? 24.921  -43.636 42.049 1.00 40.27  ?  206 MET   A CB  1 
ATOM   1640 C  CG  . MET   A 1 207 ? 23.463  -43.428 42.429 1.00 52.98  ?  206 MET   A CG  1 
ATOM   1641 S  SD  . MET   A 1 207 ? 22.539  -42.266 41.377 1.00 51.92  ?  206 MET   A SD  1 
ATOM   1642 C  CE  . MET   A 1 207 ? 23.335  -40.800 41.948 1.00 54.77  ?  206 MET   A CE  1 
ATOM   1643 N  N   . TYR   A 1 208 ? 25.937  -46.611 40.780 1.00 38.92  ?  207 TYR   A N   1 
ATOM   1644 C  CA  . TYR   A 1 208 ? 26.682  -47.194 39.674 1.00 37.15  ?  207 TYR   A CA  1 
ATOM   1645 C  C   . TYR   A 1 208 ? 25.710  -47.588 38.578 1.00 40.38  ?  207 TYR   A C   1 
ATOM   1646 O  O   . TYR   A 1 208 ? 24.579  -48.015 38.842 1.00 40.77  ?  207 TYR   A O   1 
ATOM   1647 C  CB  . TYR   A 1 208 ? 27.524  -48.415 40.088 1.00 41.03  ?  207 TYR   A CB  1 
ATOM   1648 C  CG  . TYR   A 1 208 ? 28.421  -48.900 38.983 1.00 47.31  ?  207 TYR   A CG  1 
ATOM   1649 C  CD1 . TYR   A 1 208 ? 29.663  -48.301 38.746 1.00 49.73  ?  207 TYR   A CD1 1 
ATOM   1650 C  CD2 . TYR   A 1 208 ? 28.022  -49.935 38.141 1.00 51.43  ?  207 TYR   A CD2 1 
ATOM   1651 C  CE1 . TYR   A 1 208 ? 30.480  -48.728 37.693 1.00 48.60  ?  207 TYR   A CE1 1 
ATOM   1652 C  CE2 . TYR   A 1 208 ? 28.829  -50.361 37.086 1.00 53.33  ?  207 TYR   A CE2 1 
ATOM   1653 C  CZ  . TYR   A 1 208 ? 30.053  -49.752 36.866 1.00 50.38  ?  207 TYR   A CZ  1 
ATOM   1654 O  OH  . TYR   A 1 208 ? 30.841  -50.181 35.819 1.00 50.48  ?  207 TYR   A OH  1 
ATOM   1655 N  N   . MET   A 1 209 ? 26.156  -47.415 37.341 1.00 46.27  ?  208 MET   A N   1 
ATOM   1656 C  CA  . MET   A 1 209 ? 25.370  -47.773 36.172 1.00 49.69  ?  208 MET   A CA  1 
ATOM   1657 C  C   . MET   A 1 209 ? 26.205  -48.681 35.292 1.00 49.50  ?  208 MET   A C   1 
ATOM   1658 O  O   . MET   A 1 209 ? 27.242  -48.250 34.780 1.00 55.11  ?  208 MET   A O   1 
ATOM   1659 C  CB  . MET   A 1 209 ? 24.947  -46.530 35.396 1.00 44.48  ?  208 MET   A CB  1 
ATOM   1660 C  CG  . MET   A 1 209 ? 24.321  -46.850 34.081 1.00 43.61  ?  208 MET   A CG  1 
ATOM   1661 S  SD  . MET   A 1 209 ? 22.640  -47.401 34.347 1.00 55.80  ?  208 MET   A SD  1 
ATOM   1662 C  CE  . MET   A 1 209 ? 21.913  -47.035 32.741 1.00 49.17  ?  208 MET   A CE  1 
ATOM   1663 N  N   . GLY   A 1 210 ? 25.756  -49.927 35.122 1.00 48.20  ?  209 GLY   A N   1 
ATOM   1664 C  CA  . GLY   A 1 210 ? 26.423  -50.892 34.270 1.00 45.84  ?  209 GLY   A CA  1 
ATOM   1665 C  C   . GLY   A 1 210 ? 26.094  -52.327 34.628 1.00 57.44  ?  209 GLY   A C   1 
ATOM   1666 O  O   . GLY   A 1 210 ? 25.893  -53.154 33.731 1.00 52.15  ?  209 GLY   A O   1 
ATOM   1667 N  N   . THR   A 1 211 ? 26.036  -52.631 35.939 1.00 60.80  ?  210 THR   A N   1 
ATOM   1668 C  CA  . THR   A 1 211 ? 25.708  -53.958 36.467 1.00 55.57  ?  210 THR   A CA  1 
ATOM   1669 C  C   . THR   A 1 211 ? 24.710  -53.867 37.612 1.00 52.36  ?  210 THR   A C   1 
ATOM   1670 O  O   . THR   A 1 211 ? 24.712  -52.905 38.385 1.00 54.98  ?  210 THR   A O   1 
ATOM   1671 C  CB  . THR   A 1 211 ? 26.950  -54.713 36.973 1.00 55.98  ?  210 THR   A CB  1 
ATOM   1672 O  OG1 . THR   A 1 211 ? 26.542  -55.950 37.574 1.00 50.79  ?  210 THR   A OG1 1 
ATOM   1673 C  CG2 . THR   A 1 211 ? 27.747  -53.883 37.960 1.00 56.73  ?  210 THR   A CG2 1 
ATOM   1674 N  N   . LEU   A 1 212 ? 23.862  -54.893 37.724 1.00 48.50  ?  211 LEU   A N   1 
ATOM   1675 C  CA  . LEU   A 1 212 ? 22.905  -54.955 38.824 1.00 46.85  ?  211 LEU   A CA  1 
ATOM   1676 C  C   . LEU   A 1 212 ? 23.438  -55.699 40.032 1.00 50.36  ?  211 LEU   A C   1 
ATOM   1677 O  O   . LEU   A 1 212 ? 22.980  -55.453 41.155 1.00 45.64  ?  211 LEU   A O   1 
ATOM   1678 C  CB  . LEU   A 1 212 ? 21.619  -55.665 38.403 1.00 40.97  ?  211 LEU   A CB  1 
ATOM   1679 C  CG  . LEU   A 1 212 ? 20.704  -55.062 37.381 1.00 34.71  ?  211 LEU   A CG  1 
ATOM   1680 C  CD1 . LEU   A 1 212 ? 19.522  -56.011 37.251 1.00 34.59  ?  211 LEU   A CD1 1 
ATOM   1681 C  CD2 . LEU   A 1 212 ? 20.289  -53.696 37.846 1.00 35.64  ?  211 LEU   A CD2 1 
ATOM   1682 N  N   . SER   A 1 213 ? 24.343  -56.651 39.817 1.00 53.37  ?  212 SER   A N   1 
ATOM   1683 C  CA  . SER   A 1 213 ? 24.848  -57.475 40.906 1.00 54.34  ?  212 SER   A CA  1 
ATOM   1684 C  C   . SER   A 1 213 ? 25.868  -56.691 41.715 1.00 49.95  ?  212 SER   A C   1 
ATOM   1685 O  O   . SER   A 1 213 ? 26.918  -56.309 41.202 1.00 51.36  ?  212 SER   A O   1 
ATOM   1686 C  CB  . SER   A 1 213 ? 25.484  -58.752 40.362 1.00 52.94  ?  212 SER   A CB  1 
ATOM   1687 O  OG  . SER   A 1 213 ? 25.789  -59.655 41.416 1.00 53.91  ?  212 SER   A OG  1 
ATOM   1688 N  N   . TYR   A 1 214 ? 25.575  -56.458 42.980 1.00 52.87  ?  213 TYR   A N   1 
ATOM   1689 C  CA  . TYR   A 1 214 ? 26.620  -55.893 43.813 1.00 53.46  ?  213 TYR   A CA  1 
ATOM   1690 C  C   . TYR   A 1 214 ? 27.736  -56.901 44.026 1.00 54.32  ?  213 TYR   A C   1 
ATOM   1691 O  O   . TYR   A 1 214 ? 28.874  -56.502 44.300 1.00 51.00  ?  213 TYR   A O   1 
ATOM   1692 C  CB  . TYR   A 1 214 ? 26.015  -55.430 45.146 1.00 49.41  ?  213 TYR   A CB  1 
ATOM   1693 C  CG  . TYR   A 1 214 ? 26.932  -54.637 46.038 1.00 46.69  ?  213 TYR   A CG  1 
ATOM   1694 C  CD1 . TYR   A 1 214 ? 26.893  -54.802 47.418 1.00 45.04  ?  213 TYR   A CD1 1 
ATOM   1695 C  CD2 . TYR   A 1 214 ? 27.813  -53.701 45.515 1.00 48.57  ?  213 TYR   A CD2 1 
ATOM   1696 C  CE1 . TYR   A 1 214 ? 27.702  -54.069 48.255 1.00 46.88  ?  213 TYR   A CE1 1 
ATOM   1697 C  CE2 . TYR   A 1 214 ? 28.640  -52.949 46.352 1.00 52.14  ?  213 TYR   A CE2 1 
ATOM   1698 C  CZ  . TYR   A 1 214 ? 28.578  -53.138 47.732 1.00 53.89  ?  213 TYR   A CZ  1 
ATOM   1699 O  OH  . TYR   A 1 214 ? 29.379  -52.413 48.600 1.00 52.47  ?  213 TYR   A OH  1 
ATOM   1700 N  N   . GLU   A 1 215 ? 27.419  -58.203 43.885 1.00 60.22  ?  214 GLU   A N   1 
ATOM   1701 C  CA  . GLU   A 1 215 ? 28.440  -59.240 43.975 1.00 61.77  ?  214 GLU   A CA  1 
ATOM   1702 C  C   . GLU   A 1 215 ? 29.395  -59.159 42.800 1.00 56.79  ?  214 GLU   A C   1 
ATOM   1703 O  O   . GLU   A 1 215 ? 30.617  -59.132 42.990 1.00 56.30  ?  214 GLU   A O   1 
ATOM   1704 C  CB  . GLU   A 1 215 ? 27.804  -60.630 44.041 1.00 65.78  ?  214 GLU   A CB  1 
ATOM   1705 C  CG  . GLU   A 1 215 ? 27.558  -61.201 45.456 1.00 73.72  ?  214 GLU   A CG  1 
ATOM   1706 C  CD  . GLU   A 1 215 ? 26.323  -62.118 45.516 1.00 88.86  ?  214 GLU   A CD  1 
ATOM   1707 O  OE1 . GLU   A 1 215 ? 25.602  -62.088 46.546 1.00 82.44  ?  214 GLU   A OE1 1 
ATOM   1708 O  OE2 . GLU   A 1 215 ? 26.066  -62.855 44.526 1.00 87.78  -1 214 GLU   A OE2 1 
ATOM   1709 N  N   . GLN   A 1 216 ? 28.847  -59.123 41.577 1.00 55.16  ?  215 GLN   A N   1 
ATOM   1710 C  CA  . GLN   A 1 216 ? 29.655  -58.902 40.375 1.00 54.07  ?  215 GLN   A CA  1 
ATOM   1711 C  C   . GLN   A 1 216 ? 30.606  -57.720 40.529 1.00 58.14  ?  215 GLN   A C   1 
ATOM   1712 O  O   . GLN   A 1 216 ? 31.735  -57.754 40.033 1.00 61.49  ?  215 GLN   A O   1 
ATOM   1713 C  CB  . GLN   A 1 216 ? 28.746  -58.666 39.168 1.00 50.91  ?  215 GLN   A CB  1 
ATOM   1714 C  CG  . GLN   A 1 216 ? 29.438  -58.849 37.853 1.00 64.73  ?  215 GLN   A CG  1 
ATOM   1715 C  CD  . GLN   A 1 216 ? 30.280  -60.123 37.787 1.00 73.45  ?  215 GLN   A CD  1 
ATOM   1716 O  OE1 . GLN   A 1 216 ? 29.778  -61.228 38.015 1.00 75.23  ?  215 GLN   A OE1 1 
ATOM   1717 N  NE2 . GLN   A 1 216 ? 31.577  -59.968 37.502 1.00 69.06  ?  215 GLN   A NE2 1 
ATOM   1718 N  N   . PHE   A 1 217 ? 30.165  -56.661 41.210 1.00 58.92  ?  216 PHE   A N   1 
ATOM   1719 C  CA  . PHE   A 1 217 ? 30.962  -55.444 41.305 1.00 56.93  ?  216 PHE   A CA  1 
ATOM   1720 C  C   . PHE   A 1 217 ? 32.213  -55.661 42.159 1.00 58.11  ?  216 PHE   A C   1 
ATOM   1721 O  O   . PHE   A 1 217 ? 33.258  -55.052 41.888 1.00 58.22  ?  216 PHE   A O   1 
ATOM   1722 C  CB  . PHE   A 1 217 ? 30.069  -54.311 41.841 1.00 55.07  ?  216 PHE   A CB  1 
ATOM   1723 C  CG  . PHE   A 1 217 ? 30.613  -52.925 41.620 1.00 52.40  ?  216 PHE   A CG  1 
ATOM   1724 C  CD1 . PHE   A 1 217 ? 31.281  -52.598 40.454 1.00 53.84  ?  216 PHE   A CD1 1 
ATOM   1725 C  CD2 . PHE   A 1 217 ? 30.397  -51.930 42.553 1.00 53.77  ?  216 PHE   A CD2 1 
ATOM   1726 C  CE1 . PHE   A 1 217 ? 31.766  -51.313 40.246 1.00 51.01  ?  216 PHE   A CE1 1 
ATOM   1727 C  CE2 . PHE   A 1 217 ? 30.876  -50.635 42.347 1.00 55.72  ?  216 PHE   A CE2 1 
ATOM   1728 C  CZ  . PHE   A 1 217 ? 31.562  -50.331 41.188 1.00 51.39  ?  216 PHE   A CZ  1 
ATOM   1729 N  N   . LYS   A 1 218 ? 32.136  -56.529 43.180 1.00 58.73  ?  217 LYS   A N   1 
ATOM   1730 C  CA  . LYS   A 1 218 ? 33.318  -56.835 43.988 1.00 59.14  ?  217 LYS   A CA  1 
ATOM   1731 C  C   . LYS   A 1 218 ? 34.217  -57.862 43.314 1.00 57.63  ?  217 LYS   A C   1 
ATOM   1732 O  O   . LYS   A 1 218 ? 35.426  -57.883 43.566 1.00 59.51  ?  217 LYS   A O   1 
ATOM   1733 C  CB  . LYS   A 1 218 ? 32.923  -57.353 45.375 1.00 59.16  ?  217 LYS   A CB  1 
ATOM   1734 C  CG  . LYS   A 1 218 ? 32.040  -56.438 46.222 1.00 60.59  ?  217 LYS   A CG  1 
ATOM   1735 C  CD  . LYS   A 1 218 ? 31.263  -57.260 47.235 1.00 54.22  ?  217 LYS   A CD  1 
ATOM   1736 C  CE  . LYS   A 1 218 ? 30.539  -56.403 48.236 1.00 52.93  ?  217 LYS   A CE  1 
ATOM   1737 N  NZ  . LYS   A 1 218 ? 29.460  -57.174 48.897 1.00 51.50  ?  217 LYS   A NZ  1 
ATOM   1738 N  N   . LYS   A 1 219 ? 33.644  -58.718 42.468 1.00 53.81  ?  218 LYS   A N   1 
ATOM   1739 C  CA  . LYS   A 1 219 ? 34.449  -59.695 41.745 1.00 64.92  ?  218 LYS   A CA  1 
ATOM   1740 C  C   . LYS   A 1 219 ? 35.222  -59.026 40.608 1.00 67.75  ?  218 LYS   A C   1 
ATOM   1741 O  O   . LYS   A 1 219 ? 36.420  -59.280 40.423 1.00 67.64  ?  218 LYS   A O   1 
ATOM   1742 C  CB  . LYS   A 1 219 ? 33.550  -60.827 41.219 1.00 60.51  ?  218 LYS   A CB  1 
ATOM   1743 C  CG  . LYS   A 1 219 ? 33.093  -61.831 42.301 1.00 65.91  ?  218 LYS   A CG  1 
ATOM   1744 C  CD  . LYS   A 1 219 ? 33.308  -63.275 41.875 1.00 77.99  ?  218 LYS   A CD  1 
ATOM   1745 C  CE  . LYS   A 1 219 ? 34.735  -63.740 42.150 1.00 81.30  ?  218 LYS   A CE  1 
ATOM   1746 N  NZ  . LYS   A 1 219 ? 35.139  -64.862 41.244 1.00 81.81  ?  218 LYS   A NZ  1 
ATOM   1747 N  N   . GLY   A 1 220 ? 34.565  -58.144 39.863 1.00 62.49  ?  219 GLY   A N   1 
ATOM   1748 C  CA  . GLY   A 1 220 ? 35.172  -57.436 38.753 1.00 61.56  ?  219 GLY   A CA  1 
ATOM   1749 C  C   . GLY   A 1 220 ? 34.204  -57.350 37.593 1.00 58.17  ?  219 GLY   A C   1 
ATOM   1750 O  O   . GLY   A 1 220 ? 33.476  -58.310 37.331 1.00 58.83  ?  219 GLY   A O   1 
ATOM   1751 N  N   . VAL   A 1 221 ? 34.153  -56.207 36.916 1.00 59.58  ?  220 VAL   A N   1 
ATOM   1752 C  CA  . VAL   A 1 221 ? 33.260  -56.008 35.775 1.00 68.01  ?  220 VAL   A CA  1 
ATOM   1753 C  C   . VAL   A 1 221 ? 34.077  -55.479 34.608 1.00 62.33  ?  220 VAL   A C   1 
ATOM   1754 O  O   . VAL   A 1 221 ? 35.000  -54.679 34.798 1.00 63.00  ?  220 VAL   A O   1 
ATOM   1755 C  CB  . VAL   A 1 221 ? 32.090  -55.047 36.090 1.00 63.09  ?  220 VAL   A CB  1 
ATOM   1756 C  CG1 . VAL   A 1 221 ? 30.949  -55.284 35.124 1.00 69.35  ?  220 VAL   A CG1 1 
ATOM   1757 C  CG2 . VAL   A 1 221 ? 31.591  -55.260 37.496 1.00 65.45  ?  220 VAL   A CG2 1 
ATOM   1758 N  N   . GLN   A 1 222 ? 33.732  -55.930 33.402 1.00 65.64  ?  221 GLN   A N   1 
ATOM   1759 C  CA  . GLN   A 1 222 ? 34.459  -55.575 32.188 1.00 63.08  ?  221 GLN   A CA  1 
ATOM   1760 C  C   . GLN   A 1 222 ? 34.081  -54.175 31.719 1.00 61.47  ?  221 GLN   A C   1 
ATOM   1761 O  O   . GLN   A 1 222 ? 32.903  -53.877 31.496 1.00 61.33  ?  221 GLN   A O   1 
ATOM   1762 C  CB  . GLN   A 1 222 ? 34.175  -56.602 31.096 1.00 59.56  ?  221 GLN   A CB  1 
ATOM   1763 C  CG  . GLN   A 1 222 ? 34.617  -57.971 31.482 1.00 63.75  ?  221 GLN   A CG  1 
ATOM   1764 C  CD  . GLN   A 1 222 ? 36.104  -57.992 31.756 1.00 73.66  ?  221 GLN   A CD  1 
ATOM   1765 O  OE1 . GLN   A 1 222 ? 36.558  -58.313 32.859 1.00 65.66  ?  221 GLN   A OE1 1 
ATOM   1766 N  NE2 . GLN   A 1 222 ? 36.884  -57.648 30.733 1.00 82.73  ?  221 GLN   A NE2 1 
ATOM   1767 N  N   . ILE   A 1 223 ? 35.086  -53.331 31.541 1.00 59.75  ?  222 ILE   A N   1 
ATOM   1768 C  CA  . ILE   A 1 223 ? 34.894  -51.989 30.999 1.00 73.48  ?  222 ILE   A CA  1 
ATOM   1769 C  C   . ILE   A 1 223 ? 35.937  -51.774 29.904 1.00 77.76  ?  222 ILE   A C   1 
ATOM   1770 O  O   . ILE   A 1 223 ? 37.089  -52.198 30.072 1.00 74.77  ?  222 ILE   A O   1 
ATOM   1771 C  CB  . ILE   A 1 223 ? 35.015  -50.924 32.102 1.00 73.83  ?  222 ILE   A CB  1 
ATOM   1772 C  CG1 . ILE   A 1 223 ? 36.219  -51.231 33.002 1.00 70.23  ?  222 ILE   A CG1 1 
ATOM   1773 C  CG2 . ILE   A 1 223 ? 33.758  -50.906 32.960 1.00 63.34  ?  222 ILE   A CG2 1 
ATOM   1774 C  CD1 . ILE   A 1 223 ? 36.909  -50.017 33.539 1.00 58.96  ?  222 ILE   A CD1 1 
ATOM   1775 N  N   . PRO   A 1 224 ? 35.595  -51.141 28.774 1.00 87.70  ?  223 PRO   A N   1 
ATOM   1776 C  CA  . PRO   A 1 224 ? 36.634  -50.787 27.791 1.00 88.31  ?  223 PRO   A CA  1 
ATOM   1777 C  C   . PRO   A 1 224 ? 37.689  -49.842 28.370 1.00 86.85  ?  223 PRO   A C   1 
ATOM   1778 O  O   . PRO   A 1 224 ? 37.435  -49.066 29.303 1.00 77.43  ?  223 PRO   A O   1 
ATOM   1779 C  CB  . PRO   A 1 224 ? 35.850  -50.126 26.651 1.00 79.58  ?  223 PRO   A CB  1 
ATOM   1780 C  CG  . PRO   A 1 224 ? 34.448  -49.953 27.116 1.00 76.05  ?  223 PRO   A CG  1 
ATOM   1781 C  CD  . PRO   A 1 224 ? 34.233  -50.782 28.339 1.00 77.57  ?  223 PRO   A CD  1 
ATOM   1782 N  N   . CYS   A 1 225 ? 38.898  -49.937 27.810 1.00 83.91  ?  224 CYS   A N   1 
ATOM   1783 C  CA  . CYS   A 1 225 ? 40.030  -49.103 28.194 1.00 81.37  ?  224 CYS   A CA  1 
ATOM   1784 C  C   . CYS   A 1 225 ? 40.338  -48.134 27.063 1.00 83.78  ?  224 CYS   A C   1 
ATOM   1785 O  O   . CYS   A 1 225 ? 40.341  -48.521 25.889 1.00 87.84  ?  224 CYS   A O   1 
ATOM   1786 C  CB  . CYS   A 1 225 ? 41.268  -49.953 28.510 1.00 79.35  ?  224 CYS   A CB  1 
ATOM   1787 S  SG  . CYS   A 1 225 ? 42.627  -49.067 29.363 1.00 79.66  ?  224 CYS   A SG  1 
ATOM   1788 N  N   . THR   A 1 226 ? 40.578  -46.868 27.419 1.00 88.91  ?  225 THR   A N   1 
ATOM   1789 C  CA  . THR   A 1 226 ? 40.940  -45.876 26.407 1.00 85.87  ?  225 THR   A CA  1 
ATOM   1790 C  C   . THR   A 1 226 ? 42.102  -46.374 25.578 1.00 91.51  ?  225 THR   A C   1 
ATOM   1791 O  O   . THR   A 1 226 ? 42.105  -46.240 24.349 1.00 95.73  ?  225 THR   A O   1 
ATOM   1792 C  CB  . THR   A 1 226 ? 41.320  -44.537 27.045 1.00 86.26  ?  225 THR   A CB  1 
ATOM   1793 O  OG1 . THR   A 1 226 ? 42.318  -44.740 28.063 1.00 86.10  ?  225 THR   A OG1 1 
ATOM   1794 C  CG2 . THR   A 1 226 ? 40.088  -43.853 27.635 1.00 85.39  ?  225 THR   A CG2 1 
ATOM   1795 N  N   . CYS   A 1 227 ? 43.092  -46.978 26.236 1.00 88.09  ?  226 CYS   A N   1 
ATOM   1796 C  CA  . CYS   A 1 227 ? 44.250  -47.481 25.520 1.00 92.30  ?  226 CYS   A CA  1 
ATOM   1797 C  C   . CYS   A 1 227 ? 43.878  -48.600 24.547 1.00 94.96  ?  226 CYS   A C   1 
ATOM   1798 O  O   . CYS   A 1 227 ? 44.677  -48.929 23.663 1.00 99.32  ?  226 CYS   A O   1 
ATOM   1799 C  CB  . CYS   A 1 227 ? 45.304  -47.940 26.523 1.00 91.02  ?  226 CYS   A CB  1 
ATOM   1800 S  SG  . CYS   A 1 227 ? 46.017  -46.585 27.521 1.00 84.95  ?  226 CYS   A SG  1 
ATOM   1801 N  N   . GLY   A 1 228 ? 42.686  -49.181 24.669 1.00 87.58  ?  227 GLY   A N   1 
ATOM   1802 C  CA  . GLY   A 1 228 ? 42.184  -49.996 23.581 1.00 92.22  ?  227 GLY   A CA  1 
ATOM   1803 C  C   . GLY   A 1 228 ? 41.705  -51.391 23.923 1.00 97.51  ?  227 GLY   A C   1 
ATOM   1804 O  O   . GLY   A 1 228 ? 40.788  -51.909 23.276 1.00 93.94  ?  227 GLY   A O   1 
ATOM   1805 N  N   . LYS   A 1 229 ? 42.317  -52.024 24.915 1.00 95.98  ?  228 LYS   A N   1 
ATOM   1806 C  CA  . LYS   A 1 229 ? 41.924  -53.380 25.268 1.00 96.94  ?  228 LYS   A CA  1 
ATOM   1807 C  C   . LYS   A 1 229 ? 40.662  -53.333 26.129 1.00 94.04  ?  228 LYS   A C   1 
ATOM   1808 O  O   . LYS   A 1 229 ? 40.051  -52.279 26.328 1.00 91.85  ?  228 LYS   A O   1 
ATOM   1809 C  CB  . LYS   A 1 229 ? 43.080  -54.105 25.957 1.00 102.66 ?  228 LYS   A CB  1 
ATOM   1810 C  CG  . LYS   A 1 229 ? 43.772  -55.144 25.067 1.00 104.97 ?  228 LYS   A CG  1 
ATOM   1811 C  CD  . LYS   A 1 229 ? 43.057  -56.501 25.127 1.00 109.97 ?  228 LYS   A CD  1 
ATOM   1812 C  CE  . LYS   A 1 229 ? 43.430  -57.405 23.952 1.00 106.83 ?  228 LYS   A CE  1 
ATOM   1813 N  NZ  . LYS   A 1 229 ? 44.882  -57.749 23.938 1.00 98.77  ?  228 LYS   A NZ  1 
ATOM   1814 N  N   . GLN   A 1 230 ? 40.249  -54.487 26.641 1.00 93.11  ?  229 GLN   A N   1 
ATOM   1815 C  CA  . GLN   A 1 230 ? 39.134  -54.574 27.571 1.00 86.04  ?  229 GLN   A CA  1 
ATOM   1816 C  C   . GLN   A 1 230 ? 39.675  -54.693 28.991 1.00 83.20  ?  229 GLN   A C   1 
ATOM   1817 O  O   . GLN   A 1 230 ? 40.515  -55.555 29.270 1.00 89.19  ?  229 GLN   A O   1 
ATOM   1818 C  CB  . GLN   A 1 230 ? 38.246  -55.768 27.228 1.00 90.23  ?  229 GLN   A CB  1 
ATOM   1819 C  CG  . GLN   A 1 230 ? 37.359  -55.528 26.028 1.00 91.95  ?  229 GLN   A CG  1 
ATOM   1820 C  CD  . GLN   A 1 230 ? 36.014  -54.964 26.422 1.00 90.34  ?  229 GLN   A CD  1 
ATOM   1821 O  OE1 . GLN   A 1 230 ? 35.214  -55.637 27.081 1.00 86.93  ?  229 GLN   A OE1 1 
ATOM   1822 N  NE2 . GLN   A 1 230 ? 35.760  -53.713 26.036 1.00 88.46  ?  229 GLN   A NE2 1 
ATOM   1823 N  N   . ALA   A 1 231 ? 39.197  -53.831 29.883 1.00 81.19  ?  230 ALA   A N   1 
ATOM   1824 C  CA  . ALA   A 1 231 ? 39.691  -53.762 31.253 1.00 78.64  ?  230 ALA   A CA  1 
ATOM   1825 C  C   . ALA   A 1 231 ? 38.649  -54.267 32.252 1.00 68.38  ?  230 ALA   A C   1 
ATOM   1826 O  O   . ALA   A 1 231 ? 37.494  -54.546 31.913 1.00 62.46  ?  230 ALA   A O   1 
ATOM   1827 C  CB  . ALA   A 1 231 ? 40.117  -52.330 31.603 1.00 73.76  ?  230 ALA   A CB  1 
ATOM   1828 N  N   . THR   A 1 232 ? 39.086  -54.367 33.508 1.00 62.73  ?  231 THR   A N   1 
ATOM   1829 C  CA  . THR   A 1 232 ? 38.303  -54.958 34.588 1.00 65.09  ?  231 THR   A CA  1 
ATOM   1830 C  C   . THR   A 1 232 ? 38.294  -54.012 35.788 1.00 68.57  ?  231 THR   A C   1 
ATOM   1831 O  O   . THR   A 1 232 ? 39.357  -53.647 36.307 1.00 68.95  ?  231 THR   A O   1 
ATOM   1832 C  CB  . THR   A 1 232 ? 38.871  -56.335 34.966 1.00 64.34  ?  231 THR   A CB  1 
ATOM   1833 O  OG1 . THR   A 1 232 ? 38.837  -57.186 33.817 1.00 69.27  ?  231 THR   A OG1 1 
ATOM   1834 C  CG2 . THR   A 1 232 ? 38.054  -56.987 36.053 1.00 64.21  ?  231 THR   A CG2 1 
ATOM   1835 N  N   . LYS   A 1 233 ? 37.096  -53.624 36.230 1.00 65.28  ?  232 LYS   A N   1 
ATOM   1836 C  CA  . LYS   A 1 233 ? 36.906  -52.679 37.328 1.00 66.71  ?  232 LYS   A CA  1 
ATOM   1837 C  C   . LYS   A 1 233 ? 36.234  -53.393 38.498 1.00 68.54  ?  232 LYS   A C   1 
ATOM   1838 O  O   . LYS   A 1 233 ? 35.218  -54.076 38.304 1.00 64.84  ?  232 LYS   A O   1 
ATOM   1839 C  CB  . LYS   A 1 233 ? 36.058  -51.485 36.855 1.00 61.72  ?  232 LYS   A CB  1 
ATOM   1840 C  CG  . LYS   A 1 233 ? 35.619  -50.536 37.955 1.00 61.88  ?  232 LYS   A CG  1 
ATOM   1841 C  CD  . LYS   A 1 233 ? 35.021  -49.209 37.441 1.00 60.98  ?  232 LYS   A CD  1 
ATOM   1842 C  CE  . LYS   A 1 233 ? 34.125  -49.335 36.210 1.00 64.04  ?  232 LYS   A CE  1 
ATOM   1843 N  NZ  . LYS   A 1 233 ? 33.668  -47.987 35.748 1.00 56.69  ?  232 LYS   A NZ  1 
ATOM   1844 N  N   . TYR   A 1 234 ? 36.794  -53.249 39.706 1.00 61.00  ?  233 TYR   A N   1 
ATOM   1845 C  CA  . TYR   A 1 234 ? 36.211  -53.884 40.885 1.00 60.50  ?  233 TYR   A CA  1 
ATOM   1846 C  C   . TYR   A 1 234 ? 36.262  -52.939 42.081 1.00 59.60  ?  233 TYR   A C   1 
ATOM   1847 O  O   . TYR   A 1 234 ? 37.002  -51.954 42.098 1.00 58.77  ?  233 TYR   A O   1 
ATOM   1848 C  CB  . TYR   A 1 234 ? 36.887  -55.239 41.219 1.00 60.79  ?  233 TYR   A CB  1 
ATOM   1849 C  CG  . TYR   A 1 234 ? 38.342  -55.193 41.682 1.00 68.21  ?  233 TYR   A CG  1 
ATOM   1850 C  CD1 . TYR   A 1 234 ? 39.386  -55.265 40.756 1.00 62.84  ?  233 TYR   A CD1 1 
ATOM   1851 C  CD2 . TYR   A 1 234 ? 38.675  -55.118 43.050 1.00 65.51  ?  233 TYR   A CD2 1 
ATOM   1852 C  CE1 . TYR   A 1 234 ? 40.720  -55.231 41.167 1.00 67.06  ?  233 TYR   A CE1 1 
ATOM   1853 C  CE2 . TYR   A 1 234 ? 40.017  -55.092 43.471 1.00 65.39  ?  233 TYR   A CE2 1 
ATOM   1854 C  CZ  . TYR   A 1 234 ? 41.031  -55.146 42.516 1.00 67.26  ?  233 TYR   A CZ  1 
ATOM   1855 O  OH  . TYR   A 1 234 ? 42.355  -55.100 42.882 1.00 61.28  ?  233 TYR   A OH  1 
ATOM   1856 N  N   . LEU   A 1 235 ? 35.448  -53.254 43.086 1.00 59.91  ?  234 LEU   A N   1 
ATOM   1857 C  CA  . LEU   A 1 235 ? 35.303  -52.426 44.279 1.00 62.76  ?  234 LEU   A CA  1 
ATOM   1858 C  C   . LEU   A 1 235 ? 36.302  -52.853 45.350 1.00 62.15  ?  234 LEU   A C   1 
ATOM   1859 O  O   . LEU   A 1 235 ? 36.362  -54.033 45.711 1.00 69.06  ?  234 LEU   A O   1 
ATOM   1860 C  CB  . LEU   A 1 235 ? 33.875  -52.537 44.819 1.00 55.64  ?  234 LEU   A CB  1 
ATOM   1861 C  CG  . LEU   A 1 235 ? 33.578  -51.651 46.019 1.00 58.90  ?  234 LEU   A CG  1 
ATOM   1862 C  CD1 . LEU   A 1 235 ? 33.926  -50.205 45.714 1.00 52.57  ?  234 LEU   A CD1 1 
ATOM   1863 C  CD2 . LEU   A 1 235 ? 32.114  -51.784 46.415 1.00 57.44  ?  234 LEU   A CD2 1 
ATOM   1864 N  N   . VAL   A 1 236 ? 37.084  -51.904 45.861 1.00 55.98  ?  235 VAL   A N   1 
ATOM   1865 C  CA  . VAL   A 1 236 ? 38.080  -52.220 46.871 1.00 57.77  ?  235 VAL   A CA  1 
ATOM   1866 C  C   . VAL   A 1 236 ? 37.702  -51.689 48.247 1.00 57.98  ?  235 VAL   A C   1 
ATOM   1867 O  O   . VAL   A 1 236 ? 38.052  -52.318 49.249 1.00 58.24  ?  235 VAL   A O   1 
ATOM   1868 C  CB  . VAL   A 1 236 ? 39.500  -51.739 46.474 1.00 59.26  ?  235 VAL   A CB  1 
ATOM   1869 C  CG1 . VAL   A 1 236 ? 39.667  -51.672 44.973 1.00 57.86  ?  235 VAL   A CG1 1 
ATOM   1870 C  CG2 . VAL   A 1 236 ? 39.855  -50.414 47.119 1.00 50.11  ?  235 VAL   A CG2 1 
ATOM   1871 N  N   . GLN   A 1 237 ? 37.013  -50.549 48.332 1.00 62.67  ?  236 GLN   A N   1 
ATOM   1872 C  CA  . GLN   A 1 237 ? 36.445  -50.085 49.591 1.00 60.59  ?  236 GLN   A CA  1 
ATOM   1873 C  C   . GLN   A 1 237 ? 35.126  -49.373 49.335 1.00 56.93  ?  236 GLN   A C   1 
ATOM   1874 O  O   . GLN   A 1 237 ? 34.915  -48.765 48.279 1.00 55.47  ?  236 GLN   A O   1 
ATOM   1875 C  CB  . GLN   A 1 237 ? 37.374  -49.149 50.369 1.00 57.65  ?  236 GLN   A CB  1 
ATOM   1876 C  CG  . GLN   A 1 237 ? 37.216  -49.355 51.870 1.00 65.65  ?  236 GLN   A CG  1 
ATOM   1877 C  CD  . GLN   A 1 237 ? 38.354  -48.779 52.688 1.00 80.17  ?  236 GLN   A CD  1 
ATOM   1878 O  OE1 . GLN   A 1 237 ? 38.752  -49.359 53.710 1.00 79.89  ?  236 GLN   A OE1 1 
ATOM   1879 N  NE2 . GLN   A 1 237 ? 38.874  -47.622 52.261 1.00 81.29  ?  236 GLN   A NE2 1 
ATOM   1880 N  N   . GLN   A 1 238 ? 34.244  -49.447 50.325 1.00 52.52  ?  237 GLN   A N   1 
ATOM   1881 C  CA  . GLN   A 1 238 ? 32.951  -48.785 50.242 1.00 51.32  ?  237 GLN   A CA  1 
ATOM   1882 C  C   . GLN   A 1 238 ? 32.502  -48.503 51.664 1.00 54.59  ?  237 GLN   A C   1 
ATOM   1883 O  O   . GLN   A 1 238 ? 32.251  -49.442 52.419 1.00 60.65  ?  237 GLN   A O   1 
ATOM   1884 C  CB  . GLN   A 1 238 ? 31.940  -49.655 49.499 1.00 55.60  ?  237 GLN   A CB  1 
ATOM   1885 C  CG  . GLN   A 1 238 ? 30.504  -49.151 49.543 1.00 55.46  ?  237 GLN   A CG  1 
ATOM   1886 C  CD  . GLN   A 1 238 ? 30.232  -48.093 48.490 1.00 53.40  ?  237 GLN   A CD  1 
ATOM   1887 O  OE1 . GLN   A 1 238 ? 30.756  -48.152 47.384 1.00 50.58  ?  237 GLN   A OE1 1 
ATOM   1888 N  NE2 . GLN   A 1 238 ? 29.418  -47.110 48.839 1.00 55.51  ?  237 GLN   A NE2 1 
ATOM   1889 N  N   . GLU   A 1 239 ? 32.448  -47.226 52.040 1.00 53.41  ?  238 GLU   A N   1 
ATOM   1890 C  CA  . GLU   A 1 239 ? 31.764  -46.788 53.250 1.00 48.63  ?  238 GLU   A CA  1 
ATOM   1891 C  C   . GLU   A 1 239 ? 30.546  -46.013 52.773 1.00 52.53  ?  238 GLU   A C   1 
ATOM   1892 O  O   . GLU   A 1 239 ? 30.688  -44.961 52.142 1.00 58.07  ?  238 GLU   A O   1 
ATOM   1893 C  CB  . GLU   A 1 239 ? 32.639  -45.907 54.145 1.00 58.38  ?  238 GLU   A CB  1 
ATOM   1894 C  CG  . GLU   A 1 239 ? 34.161  -46.043 53.976 1.00 69.29  ?  238 GLU   A CG  1 
ATOM   1895 C  CD  . GLU   A 1 239 ? 34.941  -45.320 55.084 1.00 82.35  ?  238 GLU   A CD  1 
ATOM   1896 O  OE1 . GLU   A 1 239 ? 34.484  -44.250 55.568 1.00 77.76  ?  238 GLU   A OE1 1 
ATOM   1897 O  OE2 . GLU   A 1 239 ? 36.031  -45.816 55.448 1.00 88.56  -1 238 GLU   A OE2 1 
ATOM   1898 N  N   . SER   A 1 240 ? 29.359  -46.540 53.053 1.00 54.27  ?  239 SER   A N   1 
ATOM   1899 C  CA  . SER   A 1 240 ? 28.073  -45.903 52.775 1.00 49.55  ?  239 SER   A CA  1 
ATOM   1900 C  C   . SER   A 1 240 ? 27.000  -46.834 53.314 1.00 42.64  ?  239 SER   A C   1 
ATOM   1901 O  O   . SER   A 1 240 ? 27.235  -48.041 53.419 1.00 44.93  ?  239 SER   A O   1 
ATOM   1902 C  CB  . SER   A 1 240 ? 27.893  -45.625 51.271 1.00 53.33  ?  239 SER   A CB  1 
ATOM   1903 O  OG  . SER   A 1 240 ? 27.553  -46.782 50.510 1.00 42.28  ?  239 SER   A OG  1 
ATOM   1904 N  N   . PRO   A 1 241 ? 25.825  -46.328 53.676 1.00 42.94  ?  240 PRO   A N   1 
ATOM   1905 C  CA  . PRO   A 1 241 ? 24.794  -47.211 54.258 1.00 46.89  ?  240 PRO   A CA  1 
ATOM   1906 C  C   . PRO   A 1 241 ? 24.003  -48.041 53.249 1.00 50.01  ?  240 PRO   A C   1 
ATOM   1907 O  O   . PRO   A 1 241 ? 23.416  -49.053 53.657 1.00 56.81  ?  240 PRO   A O   1 
ATOM   1908 C  CB  . PRO   A 1 241 ? 23.875  -46.237 55.001 1.00 43.90  ?  240 PRO   A CB  1 
ATOM   1909 C  CG  . PRO   A 1 241 ? 24.033  -44.976 54.285 1.00 48.44  ?  240 PRO   A CG  1 
ATOM   1910 C  CD  . PRO   A 1 241 ? 25.450  -44.917 53.750 1.00 45.40  ?  240 PRO   A CD  1 
ATOM   1911 N  N   . PHE   A 1 242 ? 23.959  -47.652 51.969 1.00 45.87  ?  241 PHE   A N   1 
ATOM   1912 C  CA  . PHE   A 1 242 ? 23.370  -48.436 50.888 1.00 42.28  ?  241 PHE   A CA  1 
ATOM   1913 C  C   . PHE   A 1 242 ? 24.224  -48.247 49.643 1.00 45.73  ?  241 PHE   A C   1 
ATOM   1914 O  O   . PHE   A 1 242 ? 25.204  -47.492 49.649 1.00 44.62  ?  241 PHE   A O   1 
ATOM   1915 C  CB  . PHE   A 1 242 ? 21.927  -48.020 50.587 1.00 40.73  ?  241 PHE   A CB  1 
ATOM   1916 C  CG  . PHE   A 1 242 ? 21.823  -46.661 49.978 1.00 42.91  ?  241 PHE   A CG  1 
ATOM   1917 C  CD1 . PHE   A 1 242 ? 21.788  -45.525 50.787 1.00 45.28  ?  241 PHE   A CD1 1 
ATOM   1918 C  CD2 . PHE   A 1 242 ? 21.817  -46.499 48.602 1.00 46.50  ?  241 PHE   A CD2 1 
ATOM   1919 C  CE1 . PHE   A 1 242 ? 21.718  -44.257 50.226 1.00 46.37  ?  241 PHE   A CE1 1 
ATOM   1920 C  CE2 . PHE   A 1 242 ? 21.757  -45.220 48.025 1.00 43.91  ?  241 PHE   A CE2 1 
ATOM   1921 C  CZ  . PHE   A 1 242 ? 21.710  -44.109 48.827 1.00 43.49  ?  241 PHE   A CZ  1 
ATOM   1922 N  N   . VAL   A 1 243 ? 23.848  -48.945 48.571 1.00 42.52  ?  242 VAL   A N   1 
ATOM   1923 C  CA  . VAL   A 1 243 ? 24.389  -48.719 47.234 1.00 45.37  ?  242 VAL   A CA  1 
ATOM   1924 C  C   . VAL   A 1 243 ? 23.271  -48.968 46.226 1.00 46.89  ?  242 VAL   A C   1 
ATOM   1925 O  O   . VAL   A 1 243 ? 22.469  -49.899 46.390 1.00 44.36  ?  242 VAL   A O   1 
ATOM   1926 C  CB  . VAL   A 1 243 ? 25.607  -49.611 46.903 1.00 43.09  ?  242 VAL   A CB  1 
ATOM   1927 C  CG1 . VAL   A 1 243 ? 26.813  -49.260 47.754 1.00 42.52  ?  242 VAL   A CG1 1 
ATOM   1928 C  CG2 . VAL   A 1 243 ? 25.264  -51.069 47.017 1.00 42.68  ?  242 VAL   A CG2 1 
ATOM   1929 N  N   . MET   A 1 244 ? 23.202  -48.106 45.202 1.00 45.03  ?  243 MET   A N   1 
ATOM   1930 C  CA  . MET   A 1 244 ? 22.318  -48.273 44.056 1.00 34.47  ?  243 MET   A CA  1 
ATOM   1931 C  C   . MET   A 1 244 ? 23.113  -48.857 42.890 1.00 38.99  ?  243 MET   A C   1 
ATOM   1932 O  O   . MET   A 1 244 ? 24.111  -48.267 42.450 1.00 39.21  ?  243 MET   A O   1 
ATOM   1933 C  CB  . MET   A 1 244 ? 21.713  -46.949 43.632 1.00 35.98  ?  243 MET   A CB  1 
ATOM   1934 C  CG  . MET   A 1 244 ? 20.471  -47.128 42.786 1.00 41.74  ?  243 MET   A CG  1 
ATOM   1935 S  SD  . MET   A 1 244 ? 19.813  -45.509 42.347 1.00 42.61  ?  243 MET   A SD  1 
ATOM   1936 C  CE  . MET   A 1 244 ? 18.453  -45.959 41.262 1.00 43.90  ?  243 MET   A CE  1 
ATOM   1937 N  N   . MET   A 1 245 ? 22.686  -50.020 42.407 1.00 39.89  ?  244 MET   A N   1 
ATOM   1938 C  CA  . MET   A 1 245 ? 23.250  -50.648 41.218 1.00 43.56  ?  244 MET   A CA  1 
ATOM   1939 C  C   . MET   A 1 245 ? 22.197  -50.576 40.122 1.00 45.28  ?  244 MET   A C   1 
ATOM   1940 O  O   . MET   A 1 245 ? 21.081  -51.092 40.292 1.00 43.01  ?  244 MET   A O   1 
ATOM   1941 C  CB  . MET   A 1 245 ? 23.643  -52.106 41.478 1.00 44.62  ?  244 MET   A CB  1 
ATOM   1942 C  CG  . MET   A 1 245 ? 24.539  -52.386 42.670 1.00 40.10  ?  244 MET   A CG  1 
ATOM   1943 S  SD  . MET   A 1 245 ? 26.108  -51.517 42.632 1.00 51.70  ?  244 MET   A SD  1 
ATOM   1944 C  CE  . MET   A 1 245 ? 26.832  -52.236 41.141 1.00 46.22  ?  244 MET   A CE  1 
ATOM   1945 N  N   . SER   A 1 246 ? 22.535  -49.913 39.021 1.00 44.02  ?  245 SER   A N   1 
ATOM   1946 C  CA  . SER   A 1 246 ? 21.609  -49.744 37.915 1.00 44.33  ?  245 SER   A CA  1 
ATOM   1947 C  C   . SER   A 1 246 ? 22.222  -50.317 36.647 1.00 44.62  ?  245 SER   A C   1 
ATOM   1948 O  O   . SER   A 1 246 ? 23.443  -50.433 36.517 1.00 45.36  ?  245 SER   A O   1 
ATOM   1949 C  CB  . SER   A 1 246 ? 21.263  -48.270 37.681 1.00 46.53  ?  245 SER   A CB  1 
ATOM   1950 O  OG  . SER   A 1 246 ? 20.648  -47.664 38.799 1.00 46.87  ?  245 SER   A OG  1 
ATOM   1951 N  N   . ALA   A 1 247 ? 21.352  -50.654 35.708 1.00 41.51  ?  246 ALA   A N   1 
ATOM   1952 C  CA  . ALA   A 1 247 ? 21.714  -51.129 34.383 1.00 46.29  ?  246 ALA   A CA  1 
ATOM   1953 C  C   . ALA   A 1 247 ? 20.439  -51.113 33.551 1.00 46.15  ?  246 ALA   A C   1 
ATOM   1954 O  O   . ALA   A 1 247 ? 19.330  -51.144 34.115 1.00 42.30  ?  246 ALA   A O   1 
ATOM   1955 C  CB  . ALA   A 1 247 ? 22.343  -52.524 34.439 1.00 43.67  ?  246 ALA   A CB  1 
ATOM   1956 N  N   . PRO   A 1 248 ? 20.548  -50.982 32.231 1.00 47.35  ?  247 PRO   A N   1 
ATOM   1957 C  CA  . PRO   A 1 248 ? 19.355  -50.975 31.401 1.00 44.33  ?  247 PRO   A CA  1 
ATOM   1958 C  C   . PRO   A 1 248 ? 18.540  -52.234 31.616 1.00 41.36  ?  247 PRO   A C   1 
ATOM   1959 O  O   . PRO   A 1 248 ? 19.100  -53.322 31.839 1.00 44.37  ?  247 PRO   A O   1 
ATOM   1960 C  CB  . PRO   A 1 248 ? 19.918  -50.908 29.974 1.00 43.04  ?  247 PRO   A CB  1 
ATOM   1961 C  CG  . PRO   A 1 248 ? 21.387  -50.593 30.114 1.00 39.92  ?  247 PRO   A CG  1 
ATOM   1962 C  CD  . PRO   A 1 248 ? 21.673  -50.322 31.553 1.00 44.11  ?  247 PRO   A CD  1 
ATOM   1963 N  N   . PRO   A 1 249 ? 17.186  -52.130 31.541 1.00 41.72  ?  248 PRO   A N   1 
ATOM   1964 C  CA  . PRO   A 1 249 ? 16.305  -53.290 31.777 1.00 39.56  ?  248 PRO   A CA  1 
ATOM   1965 C  C   . PRO   A 1 249 ? 16.777  -54.583 31.130 1.00 46.13  ?  248 PRO   A C   1 
ATOM   1966 O  O   . PRO   A 1 249 ? 17.158  -54.609 29.958 1.00 56.88  ?  248 PRO   A O   1 
ATOM   1967 C  CB  . PRO   A 1 249 ? 14.969  -52.850 31.163 1.00 40.36  ?  248 PRO   A CB  1 
ATOM   1968 C  CG  . PRO   A 1 249 ? 15.009  -51.362 31.153 1.00 40.95  ?  248 PRO   A CG  1 
ATOM   1969 C  CD  . PRO   A 1 249 ? 16.438  -50.909 31.199 1.00 41.26  ?  248 PRO   A CD  1 
ATOM   1970 N  N   . ALA   A 1 250 ? 16.744  -55.666 31.889 1.00 47.95  ?  249 ALA   A N   1 
ATOM   1971 C  CA  . ALA   A 1 250 ? 17.047  -56.986 31.364 1.00 48.29  ?  249 ALA   A CA  1 
ATOM   1972 C  C   . ALA   A 1 250 ? 16.465  -57.997 32.338 1.00 55.11  ?  249 ALA   A C   1 
ATOM   1973 O  O   . ALA   A 1 250 ? 16.203  -57.670 33.503 1.00 52.81  ?  249 ALA   A O   1 
ATOM   1974 C  CB  . ALA   A 1 250 ? 18.555  -57.181 31.189 1.00 40.67  ?  249 ALA   A CB  1 
ATOM   1975 N  N   . GLN   A 1 251 ? 16.237  -59.222 31.855 1.00 53.39  ?  250 GLN   A N   1 
ATOM   1976 C  CA  . GLN   A 1 251 ? 15.739  -60.257 32.755 1.00 52.08  ?  250 GLN   A CA  1 
ATOM   1977 C  C   . GLN   A 1 251 ? 16.782  -60.538 33.833 1.00 52.68  ?  250 GLN   A C   1 
ATOM   1978 O  O   . GLN   A 1 251 ? 17.975  -60.680 33.535 1.00 56.00  ?  250 GLN   A O   1 
ATOM   1979 C  CB  . GLN   A 1 251 ? 15.402  -61.535 31.992 1.00 44.33  ?  250 GLN   A CB  1 
ATOM   1980 C  CG  . GLN   A 1 251 ? 14.291  -61.371 31.003 1.00 40.60  ?  250 GLN   A CG  1 
ATOM   1981 C  CD  . GLN   A 1 251 ? 12.917  -61.305 31.637 1.00 51.81  ?  250 GLN   A CD  1 
ATOM   1982 O  OE1 . GLN   A 1 251 ? 12.546  -62.153 32.482 1.00 56.68  ?  250 GLN   A OE1 1 
ATOM   1983 N  NE2 . GLN   A 1 251 ? 12.128  -60.308 31.216 1.00 43.72  ?  250 GLN   A NE2 1 
ATOM   1984 N  N   . TYR   A 1 252 ? 16.336  -60.597 35.087 1.00 48.98  ?  251 TYR   A N   1 
ATOM   1985 C  CA  . TYR   A 1 252 ? 17.244  -60.765 36.217 1.00 51.58  ?  251 TYR   A CA  1 
ATOM   1986 C  C   . TYR   A 1 252 ? 16.501  -61.501 37.327 1.00 49.73  ?  251 TYR   A C   1 
ATOM   1987 O  O   . TYR   A 1 252 ? 15.288  -61.326 37.492 1.00 47.02  ?  251 TYR   A O   1 
ATOM   1988 C  CB  . TYR   A 1 252 ? 17.755  -59.400 36.685 1.00 45.02  ?  251 TYR   A CB  1 
ATOM   1989 C  CG  . TYR   A 1 252 ? 18.829  -59.399 37.737 1.00 44.28  ?  251 TYR   A CG  1 
ATOM   1990 C  CD1 . TYR   A 1 252 ? 18.539  -59.050 39.063 1.00 40.99  ?  251 TYR   A CD1 1 
ATOM   1991 C  CD2 . TYR   A 1 252 ? 20.143  -59.678 37.408 1.00 43.02  ?  251 TYR   A CD2 1 
ATOM   1992 C  CE1 . TYR   A 1 252 ? 19.529  -59.018 40.020 1.00 35.34  ?  251 TYR   A CE1 1 
ATOM   1993 C  CE2 . TYR   A 1 252 ? 21.146  -59.651 38.375 1.00 39.70  ?  251 TYR   A CE2 1 
ATOM   1994 C  CZ  . TYR   A 1 252 ? 20.830  -59.324 39.667 1.00 39.92  ?  251 TYR   A CZ  1 
ATOM   1995 O  OH  . TYR   A 1 252 ? 21.841  -59.292 40.605 1.00 53.50  ?  251 TYR   A OH  1 
ATOM   1996 N  N   . GLU   A 1 253 ? 17.206  -62.362 38.051 1.00 43.16  ?  252 GLU   A N   1 
ATOM   1997 C  CA  . GLU   A 1 253 ? 16.559  -63.107 39.119 1.00 53.43  ?  252 GLU   A CA  1 
ATOM   1998 C  C   . GLU   A 1 253 ? 16.853  -62.446 40.458 1.00 50.75  ?  252 GLU   A C   1 
ATOM   1999 O  O   . GLU   A 1 253 ? 17.983  -62.017 40.717 1.00 46.48  ?  252 GLU   A O   1 
ATOM   2000 C  CB  . GLU   A 1 253 ? 16.993  -64.575 39.158 1.00 60.91  ?  252 GLU   A CB  1 
ATOM   2001 C  CG  . GLU   A 1 253 ? 15.981  -65.422 39.944 1.00 73.21  ?  252 GLU   A CG  1 
ATOM   2002 C  CD  . GLU   A 1 253 ? 16.337  -66.894 40.044 1.00 79.91  ?  252 GLU   A CD  1 
ATOM   2003 O  OE1 . GLU   A 1 253 ? 17.438  -67.267 39.582 1.00 78.96  ?  252 GLU   A OE1 1 
ATOM   2004 O  OE2 . GLU   A 1 253 ? 15.516  -67.662 40.613 1.00 79.07  -1 252 GLU   A OE2 1 
ATOM   2005 N  N   . LEU   A 1 254 ? 15.824  -62.370 41.302 1.00 50.00  ?  253 LEU   A N   1 
ATOM   2006 C  CA  . LEU   A 1 254 ? 15.902  -61.741 42.614 1.00 51.19  ?  253 LEU   A CA  1 
ATOM   2007 C  C   . LEU   A 1 254 ? 15.581  -62.779 43.683 1.00 51.03  ?  253 LEU   A C   1 
ATOM   2008 O  O   . LEU   A 1 254 ? 14.485  -63.351 43.686 1.00 52.59  ?  253 LEU   A O   1 
ATOM   2009 C  CB  . LEU   A 1 254 ? 14.931  -60.568 42.711 1.00 50.05  ?  253 LEU   A CB  1 
ATOM   2010 C  CG  . LEU   A 1 254 ? 15.265  -59.290 41.961 1.00 42.61  ?  253 LEU   A CG  1 
ATOM   2011 C  CD1 . LEU   A 1 254 ? 14.125  -58.304 42.158 1.00 42.70  ?  253 LEU   A CD1 1 
ATOM   2012 C  CD2 . LEU   A 1 254 ? 16.574  -58.724 42.424 1.00 38.25  ?  253 LEU   A CD2 1 
ATOM   2013 N  N   . LYS   A 1 255 ? 16.532  -63.011 44.586 1.00 52.96  ?  254 LYS   A N   1 
ATOM   2014 C  CA  . LYS   A 1 255 ? 16.448  -64.051 45.607 1.00 54.33  ?  254 LYS   A CA  1 
ATOM   2015 C  C   . LYS   A 1 255 ? 16.187  -63.423 46.974 1.00 53.95  ?  254 LYS   A C   1 
ATOM   2016 O  O   . LYS   A 1 255 ? 16.994  -62.608 47.450 1.00 47.75  ?  254 LYS   A O   1 
ATOM   2017 C  CB  . LYS   A 1 255 ? 17.731  -64.884 45.638 1.00 48.97  ?  254 LYS   A CB  1 
ATOM   2018 C  CG  . LYS   A 1 255 ? 17.510  -66.346 45.313 1.00 57.25  ?  254 LYS   A CG  1 
ATOM   2019 C  CD  . LYS   A 1 255 ? 17.671  -66.604 43.830 1.00 70.72  ?  254 LYS   A CD  1 
ATOM   2020 C  CE  . LYS   A 1 255 ? 17.832  -68.102 43.545 1.00 81.76  ?  254 LYS   A CE  1 
ATOM   2021 N  NZ  . LYS   A 1 255 ? 18.307  -68.383 42.145 1.00 72.93  ?  254 LYS   A NZ  1 
ATOM   2022 N  N   . HIS   A 1 256 ? 15.059  -63.815 47.593 1.00 53.77  ?  255 HIS   A N   1 
ATOM   2023 C  CA  . HIS   A 1 256 ? 14.651  -63.473 48.956 1.00 48.63  ?  255 HIS   A CA  1 
ATOM   2024 C  C   . HIS   A 1 256 ? 15.870  -63.298 49.847 1.00 50.87  ?  255 HIS   A C   1 
ATOM   2025 O  O   . HIS   A 1 256 ? 16.668  -64.228 50.007 1.00 53.93  ?  255 HIS   A O   1 
ATOM   2026 C  CB  . HIS   A 1 256 ? 13.674  -64.554 49.463 1.00 53.08  ?  255 HIS   A CB  1 
ATOM   2027 C  CG  . HIS   A 1 256 ? 13.689  -64.812 50.947 1.00 61.28  ?  255 HIS   A CG  1 
ATOM   2028 N  ND1 . HIS   A 1 256 ? 13.076  -63.967 51.856 1.00 56.92  ?  255 HIS   A ND1 1 
ATOM   2029 C  CD2 . HIS   A 1 256 ? 14.107  -65.895 51.660 1.00 58.45  ?  255 HIS   A CD2 1 
ATOM   2030 C  CE1 . HIS   A 1 256 ? 13.187  -64.482 53.072 1.00 62.37  ?  255 HIS   A CE1 1 
ATOM   2031 N  NE2 . HIS   A 1 256 ? 13.803  -65.652 52.982 1.00 71.88  ?  255 HIS   A NE2 1 
ATOM   2032 N  N   . GLY   A 1 257 ? 16.079  -62.077 50.337 1.00 47.15  ?  256 GLY   A N   1 
ATOM   2033 C  CA  . GLY   A 1 257 ? 17.118  -61.801 51.302 1.00 35.82  ?  256 GLY   A CA  1 
ATOM   2034 C  C   . GLY   A 1 257 ? 18.487  -61.438 50.762 1.00 45.82  ?  256 GLY   A C   1 
ATOM   2035 O  O   . GLY   A 1 257 ? 19.403  -61.215 51.562 1.00 58.16  ?  256 GLY   A O   1 
ATOM   2036 N  N   . THR   A 1 258 ? 18.686  -61.364 49.452 1.00 46.20  ?  257 THR   A N   1 
ATOM   2037 C  CA  . THR   A 1 258 ? 19.996  -60.980 48.931 1.00 44.49  ?  257 THR   A CA  1 
ATOM   2038 C  C   . THR   A 1 258 ? 20.091  -59.512 48.533 1.00 39.77  ?  257 THR   A C   1 
ATOM   2039 O  O   . THR   A 1 258 ? 21.118  -59.113 47.966 1.00 40.90  ?  257 THR   A O   1 
ATOM   2040 C  CB  . THR   A 1 258 ? 20.353  -61.839 47.725 1.00 40.62  ?  257 THR   A CB  1 
ATOM   2041 O  OG1 . THR   A 1 258 ? 19.379  -61.608 46.691 1.00 54.44  ?  257 THR   A OG1 1 
ATOM   2042 C  CG2 . THR   A 1 258 ? 20.328  -63.278 48.118 1.00 34.00  ?  257 THR   A CG2 1 
ATOM   2043 N  N   . PHE   A 1 259 ? 19.063  -58.712 48.831 1.00 34.99  ?  258 PHE   A N   1 
ATOM   2044 C  CA  . PHE   A 1 259 ? 18.907  -57.337 48.364 1.00 37.81  ?  258 PHE   A CA  1 
ATOM   2045 C  C   . PHE   A 1 259 ? 17.788  -56.677 49.177 1.00 38.34  ?  258 PHE   A C   1 
ATOM   2046 O  O   . PHE   A 1 259 ? 16.969  -57.357 49.799 1.00 39.26  ?  258 PHE   A O   1 
ATOM   2047 C  CB  . PHE   A 1 259 ? 18.582  -57.288 46.853 1.00 35.46  ?  258 PHE   A CB  1 
ATOM   2048 C  CG  . PHE   A 1 259 ? 17.162  -57.703 46.514 1.00 34.87  ?  258 PHE   A CG  1 
ATOM   2049 C  CD1 . PHE   A 1 259 ? 16.807  -59.043 46.448 1.00 37.81  ?  258 PHE   A CD1 1 
ATOM   2050 C  CD2 . PHE   A 1 259 ? 16.176  -56.751 46.311 1.00 33.21  ?  258 PHE   A CD2 1 
ATOM   2051 C  CE1 . PHE   A 1 259 ? 15.498  -59.428 46.149 1.00 36.77  ?  258 PHE   A CE1 1 
ATOM   2052 C  CE2 . PHE   A 1 259 ? 14.876  -57.125 46.016 1.00 39.51  ?  258 PHE   A CE2 1 
ATOM   2053 C  CZ  . PHE   A 1 259 ? 14.538  -58.479 45.934 1.00 38.93  ?  258 PHE   A CZ  1 
ATOM   2054 N  N   . THR   A 1 260 ? 17.731  -55.345 49.129 1.00 34.76  ?  259 THR   A N   1 
ATOM   2055 C  CA  . THR   A 1 260 ? 16.667  -54.590 49.786 1.00 35.64  ?  259 THR   A CA  1 
ATOM   2056 C  C   . THR   A 1 260 ? 15.407  -54.452 48.926 1.00 38.14  ?  259 THR   A C   1 
ATOM   2057 O  O   . THR   A 1 260 ? 14.316  -54.855 49.345 1.00 37.21  ?  259 THR   A O   1 
ATOM   2058 C  CB  . THR   A 1 260 ? 17.195  -53.209 50.184 1.00 38.50  ?  259 THR   A CB  1 
ATOM   2059 O  OG1 . THR   A 1 260 ? 18.354  -53.375 51.001 1.00 41.52  ?  259 THR   A OG1 1 
ATOM   2060 C  CG2 . THR   A 1 260 ? 16.169  -52.436 50.941 1.00 28.77  ?  259 THR   A CG2 1 
ATOM   2061 N  N   . CYS   A 1 261 ? 15.532  -53.862 47.738 1.00 41.74  ?  260 CYS   A N   1 
ATOM   2062 C  CA  . CYS   A 1 261 ? 14.381  -53.587 46.881 1.00 42.46  ?  260 CYS   A CA  1 
ATOM   2063 C  C   . CYS   A 1 261 ? 14.910  -53.246 45.494 1.00 39.96  ?  260 CYS   A C   1 
ATOM   2064 O  O   . CYS   A 1 261 ? 16.108  -53.007 45.322 1.00 45.82  ?  260 CYS   A O   1 
ATOM   2065 C  CB  . CYS   A 1 261 ? 13.520  -52.449 47.449 1.00 43.97  ?  260 CYS   A CB  1 
ATOM   2066 S  SG  . CYS   A 1 261 ? 14.400  -50.865 47.574 1.00 37.68  ?  260 CYS   A SG  1 
ATOM   2067 N  N   . ALA   A 1 262 ? 14.003  -53.201 44.507 1.00 40.64  ?  261 ALA   A N   1 
ATOM   2068 C  CA  . ALA   A 1 262 ? 14.399  -53.094 43.099 1.00 43.08  ?  261 ALA   A CA  1 
ATOM   2069 C  C   . ALA   A 1 262 ? 13.307  -52.435 42.257 1.00 43.25  ?  261 ALA   A C   1 
ATOM   2070 O  O   . ALA   A 1 262 ? 12.119  -52.520 42.576 1.00 46.70  ?  261 ALA   A O   1 
ATOM   2071 C  CB  . ALA   A 1 262 ? 14.725  -54.472 42.499 1.00 37.85  ?  261 ALA   A CB  1 
ATOM   2072 N  N   . SER   A 1 263 ? 13.712  -51.801 41.153 1.00 45.68  ?  262 SER   A N   1 
ATOM   2073 C  CA  . SER   A 1 263 ? 12.764  -51.231 40.192 1.00 45.34  ?  262 SER   A CA  1 
ATOM   2074 C  C   . SER   A 1 263 ? 12.574  -52.207 39.041 1.00 45.59  ?  262 SER   A C   1 
ATOM   2075 O  O   . SER   A 1 263 ? 13.534  -52.524 38.316 1.00 42.58  ?  262 SER   A O   1 
ATOM   2076 C  CB  . SER   A 1 263 ? 13.236  -49.880 39.645 1.00 44.19  ?  262 SER   A CB  1 
ATOM   2077 O  OG  . SER   A 1 263 ? 13.596  -48.953 40.669 1.00 49.35  ?  262 SER   A OG  1 
ATOM   2078 N  N   . GLU   A 1 264 ? 11.350  -52.697 38.887 1.00 44.03  ?  263 GLU   A N   1 
ATOM   2079 C  CA  . GLU   A 1 264 ? 10.972  -53.495 37.733 1.00 40.27  ?  263 GLU   A CA  1 
ATOM   2080 C  C   . GLU   A 1 264 ? 10.386  -52.551 36.710 1.00 47.55  ?  263 GLU   A C   1 
ATOM   2081 O  O   . GLU   A 1 264 ? 9.426   -51.830 37.012 1.00 49.55  ?  263 GLU   A O   1 
ATOM   2082 C  CB  . GLU   A 1 264 ? 9.949   -54.570 38.079 1.00 46.51  ?  263 GLU   A CB  1 
ATOM   2083 C  CG  . GLU   A 1 264 ? 9.377   -55.218 36.835 1.00 44.00  ?  263 GLU   A CG  1 
ATOM   2084 C  CD  . GLU   A 1 264 ? 7.971   -55.774 37.021 1.00 50.75  ?  263 GLU   A CD  1 
ATOM   2085 O  OE1 . GLU   A 1 264 ? 7.833   -56.915 37.541 1.00 45.25  ?  263 GLU   A OE1 1 
ATOM   2086 O  OE2 . GLU   A 1 264 ? 7.012   -55.074 36.620 1.00 57.98  -1 263 GLU   A OE2 1 
ATOM   2087 N  N   . TYR   A 1 265 ? 10.952  -52.559 35.502 1.00 47.96  ?  264 TYR   A N   1 
ATOM   2088 C  CA  . TYR   A 1 265 ? 10.523  -51.696 34.414 1.00 41.86  ?  264 TYR   A CA  1 
ATOM   2089 C  C   . TYR   A 1 265 ? 10.202  -52.581 33.226 1.00 41.93  ?  264 TYR   A C   1 
ATOM   2090 O  O   . TYR   A 1 265 ? 11.017  -53.427 32.845 1.00 44.22  ?  264 TYR   A O   1 
ATOM   2091 C  CB  . TYR   A 1 265 ? 11.613  -50.695 34.045 1.00 45.32  ?  264 TYR   A CB  1 
ATOM   2092 C  CG  . TYR   A 1 265 ? 11.231  -49.746 32.930 1.00 46.69  ?  264 TYR   A CG  1 
ATOM   2093 C  CD1 . TYR   A 1 265 ? 10.427  -48.642 33.179 1.00 43.18  ?  264 TYR   A CD1 1 
ATOM   2094 C  CD2 . TYR   A 1 265 ? 11.652  -49.968 31.636 1.00 44.36  ?  264 TYR   A CD2 1 
ATOM   2095 C  CE1 . TYR   A 1 265 ? 10.057  -47.791 32.179 1.00 45.46  ?  264 TYR   A CE1 1 
ATOM   2096 C  CE2 . TYR   A 1 265 ? 11.288  -49.122 30.622 1.00 46.06  ?  264 TYR   A CE2 1 
ATOM   2097 C  CZ  . TYR   A 1 265 ? 10.490  -48.031 30.893 1.00 49.05  ?  264 TYR   A CZ  1 
ATOM   2098 O  OH  . TYR   A 1 265 ? 10.137  -47.159 29.878 1.00 46.04  ?  264 TYR   A OH  1 
ATOM   2099 N  N   . THR   A 1 266 ? 9.012   -52.390 32.663 1.00 43.48  ?  265 THR   A N   1 
ATOM   2100 C  CA  . THR   A 1 266 ? 8.514   -53.155 31.526 1.00 43.92  ?  265 THR   A CA  1 
ATOM   2101 C  C   . THR   A 1 266 ? 8.084   -52.173 30.442 1.00 51.88  ?  265 THR   A C   1 
ATOM   2102 O  O   . THR   A 1 266 ? 7.388   -51.194 30.741 1.00 46.18  ?  265 THR   A O   1 
ATOM   2103 C  CB  . THR   A 1 266 ? 7.331   -54.036 31.951 1.00 43.76  ?  265 THR   A CB  1 
ATOM   2104 O  OG1 . THR   A 1 266 ? 7.822   -55.216 32.614 1.00 54.63  ?  265 THR   A OG1 1 
ATOM   2105 C  CG2 . THR   A 1 266 ? 6.478   -54.445 30.778 1.00 24.58  ?  265 THR   A CG2 1 
ATOM   2106 N  N   . GLY   A 1 267 ? 8.504   -52.429 29.189 1.00 46.70  ?  266 GLY   A N   1 
ATOM   2107 C  CA  . GLY   A 1 267 ? 8.207   -51.539 28.079 1.00 45.64  ?  266 GLY   A CA  1 
ATOM   2108 C  C   . GLY   A 1 267 ? 9.432   -50.971 27.381 1.00 46.02  ?  266 GLY   A C   1 
ATOM   2109 O  O   . GLY   A 1 267 ? 10.554  -51.464 27.554 1.00 41.76  ?  266 GLY   A O   1 
ATOM   2110 N  N   . ASN   A 1 268 ? 9.233   -49.941 26.569 1.00 48.10  ?  267 ASN   A N   1 
ATOM   2111 C  CA  . ASN   A 1 268 ? 10.339  -49.347 25.830 1.00 53.95  ?  267 ASN   A CA  1 
ATOM   2112 C  C   . ASN   A 1 268 ? 10.856  -48.109 26.546 1.00 49.20  ?  267 ASN   A C   1 
ATOM   2113 O  O   . ASN   A 1 268 ? 10.146  -47.494 27.344 1.00 53.69  ?  267 ASN   A O   1 
ATOM   2114 C  CB  . ASN   A 1 268 ? 9.922   -48.989 24.401 1.00 45.85  ?  267 ASN   A CB  1 
ATOM   2115 C  CG  . ASN   A 1 268 ? 9.607   -50.214 23.576 1.00 57.66  ?  267 ASN   A CG  1 
ATOM   2116 O  OD1 . ASN   A 1 268 ? 10.363  -51.191 23.603 1.00 51.86  ?  267 ASN   A OD1 1 
ATOM   2117 N  ND2 . ASN   A 1 268 ? 8.486   -50.179 22.835 1.00 64.00  ?  267 ASN   A ND2 1 
ATOM   2118 N  N   . TYR   A 1 269 ? 12.113  -47.761 26.251 1.00 46.18  ?  268 TYR   A N   1 
ATOM   2119 C  CA  . TYR   A 1 269 ? 12.719  -46.504 26.664 1.00 41.07  ?  268 TYR   A CA  1 
ATOM   2120 C  C   . TYR   A 1 269 ? 11.660  -45.429 26.674 1.00 43.71  ?  268 TYR   A C   1 
ATOM   2121 O  O   . TYR   A 1 269 ? 10.983  -45.230 25.672 1.00 48.30  ?  268 TYR   A O   1 
ATOM   2122 C  CB  . TYR   A 1 269 ? 13.852  -46.123 25.717 1.00 40.38  ?  268 TYR   A CB  1 
ATOM   2123 C  CG  . TYR   A 1 269 ? 14.770  -45.011 26.200 1.00 53.26  ?  268 TYR   A CG  1 
ATOM   2124 C  CD1 . TYR   A 1 269 ? 15.554  -45.175 27.340 1.00 51.23  ?  268 TYR   A CD1 1 
ATOM   2125 C  CD2 . TYR   A 1 269 ? 14.888  -43.812 25.490 1.00 47.83  ?  268 TYR   A CD2 1 
ATOM   2126 C  CE1 . TYR   A 1 269 ? 16.398  -44.176 27.765 1.00 47.43  ?  268 TYR   A CE1 1 
ATOM   2127 C  CE2 . TYR   A 1 269 ? 15.732  -42.806 25.919 1.00 44.36  ?  268 TYR   A CE2 1 
ATOM   2128 C  CZ  . TYR   A 1 269 ? 16.483  -43.000 27.051 1.00 47.73  ?  268 TYR   A CZ  1 
ATOM   2129 O  OH  . TYR   A 1 269 ? 17.331  -42.026 27.496 1.00 52.77  ?  268 TYR   A OH  1 
ATOM   2130 N  N   . GLN   A 1 270 ? 11.418  -44.816 27.824 1.00 47.90  ?  269 GLN   A N   1 
ATOM   2131 C  CA  . GLN   A 1 270 ? 10.620  -43.599 27.941 1.00 47.20  ?  269 GLN   A CA  1 
ATOM   2132 C  C   . GLN   A 1 270 ? 9.099   -43.781 27.809 1.00 46.43  ?  269 GLN   A C   1 
ATOM   2133 O  O   . GLN   A 1 270 ? 8.374   -42.782 27.941 1.00 51.43  ?  269 GLN   A O   1 
ATOM   2134 C  CB  . GLN   A 1 270 ? 11.092  -42.535 26.935 1.00 47.22  ?  269 GLN   A CB  1 
ATOM   2135 C  CG  . GLN   A 1 270 ? 12.522  -42.091 27.218 1.00 49.51  ?  269 GLN   A CG  1 
ATOM   2136 C  CD  . GLN   A 1 270 ? 12.936  -40.839 26.472 1.00 56.20  ?  269 GLN   A CD  1 
ATOM   2137 O  OE1 . GLN   A 1 270 ? 13.443  -39.898 27.094 1.00 55.64  ?  269 GLN   A OE1 1 
ATOM   2138 N  NE2 . GLN   A 1 270 ? 12.759  -40.825 25.140 1.00 50.48  ?  269 GLN   A NE2 1 
ATOM   2139 N  N   . CYS   A 1 271 ? 8.572   -45.000 27.605 1.00 43.78  ?  270 CYS   A N   1 
ATOM   2140 C  CA  . CYS   A 1 271 ? 7.126   -45.188 27.690 1.00 39.28  ?  270 CYS   A CA  1 
ATOM   2141 C  C   . CYS   A 1 271 ? 6.699   -46.430 28.468 1.00 42.12  ?  270 CYS   A C   1 
ATOM   2142 O  O   . CYS   A 1 271 ? 5.502   -46.733 28.508 1.00 48.70  ?  270 CYS   A O   1 
ATOM   2143 C  CB  . CYS   A 1 271 ? 6.493   -45.235 26.305 1.00 47.16  ?  270 CYS   A CB  1 
ATOM   2144 S  SG  . CYS   A 1 271 ? 7.103   -46.637 25.322 1.00 63.69  ?  270 CYS   A SG  1 
ATOM   2145 N  N   . GLY   A 1 272 ? 7.614   -47.132 29.128 1.00 45.86  ?  271 GLY   A N   1 
ATOM   2146 C  CA  . GLY   A 1 272 ? 7.242   -48.267 29.959 1.00 49.07  ?  271 GLY   A CA  1 
ATOM   2147 C  C   . GLY   A 1 272 ? 6.647   -47.911 31.328 1.00 42.50  ?  271 GLY   A C   1 
ATOM   2148 O  O   . GLY   A 1 272 ? 6.506   -46.755 31.711 1.00 46.80  ?  271 GLY   A O   1 
ATOM   2149 N  N   . HIS   A 1 273 ? 6.275   -48.957 32.057 1.00 40.84  ?  272 HIS   A N   1 
ATOM   2150 C  CA  . HIS   A 1 273 ? 5.704   -48.906 33.395 1.00 41.30  ?  272 HIS   A CA  1 
ATOM   2151 C  C   . HIS   A 1 273 ? 6.742   -49.412 34.382 1.00 43.90  ?  272 HIS   A C   1 
ATOM   2152 O  O   . HIS   A 1 273 ? 7.638   -50.185 34.020 1.00 40.69  ?  272 HIS   A O   1 
ATOM   2153 C  CB  . HIS   A 1 273 ? 4.449   -49.789 33.496 1.00 40.24  ?  272 HIS   A CB  1 
ATOM   2154 C  CG  . HIS   A 1 273 ? 3.547   -49.497 34.664 1.00 53.31  ?  272 HIS   A CG  1 
ATOM   2155 N  ND1 . HIS   A 1 273 ? 3.044   -48.240 34.945 1.00 64.51  ?  272 HIS   A ND1 1 
ATOM   2156 C  CD2 . HIS   A 1 273 ? 3.071   -50.316 35.642 1.00 54.65  ?  272 HIS   A CD2 1 
ATOM   2157 C  CE1 . HIS   A 1 273 ? 2.277   -48.305 36.025 1.00 58.26  ?  272 HIS   A CE1 1 
ATOM   2158 N  NE2 . HIS   A 1 273 ? 2.287   -49.552 36.473 1.00 49.68  ?  272 HIS   A NE2 1 
ATOM   2159 N  N   . TYR   A 1 274 ? 6.625   -48.953 35.632 1.00 51.51  ?  273 TYR   A N   1 
ATOM   2160 C  CA  . TYR   A 1 274 ? 7.425   -49.441 36.751 1.00 46.26  ?  273 TYR   A CA  1 
ATOM   2161 C  C   . TYR   A 1 274 ? 6.533   -50.177 37.732 1.00 42.47  ?  273 TYR   A C   1 
ATOM   2162 O  O   . TYR   A 1 274 ? 5.341   -49.877 37.858 1.00 47.81  ?  273 TYR   A O   1 
ATOM   2163 C  CB  . TYR   A 1 274 ? 8.105   -48.314 37.525 1.00 40.34  ?  273 TYR   A CB  1 
ATOM   2164 C  CG  . TYR   A 1 274 ? 9.356   -47.690 36.939 1.00 39.93  ?  273 TYR   A CG  1 
ATOM   2165 C  CD1 . TYR   A 1 274 ? 10.589  -48.282 37.120 1.00 38.41  ?  273 TYR   A CD1 1 
ATOM   2166 C  CD2 . TYR   A 1 274 ? 9.314   -46.456 36.271 1.00 38.81  ?  273 TYR   A CD2 1 
ATOM   2167 C  CE1 . TYR   A 1 274 ? 11.740  -47.700 36.637 1.00 37.42  ?  273 TYR   A CE1 1 
ATOM   2168 C  CE2 . TYR   A 1 274 ? 10.476  -45.859 35.788 1.00 32.52  ?  273 TYR   A CE2 1 
ATOM   2169 C  CZ  . TYR   A 1 274 ? 11.682  -46.489 35.983 1.00 34.91  ?  273 TYR   A CZ  1 
ATOM   2170 O  OH  . TYR   A 1 274 ? 12.856  -45.937 35.526 1.00 36.26  ?  273 TYR   A OH  1 
ATOM   2171 N  N   . LYS   A 1 275 ? 7.130   -51.135 38.433 1.00 43.27  ?  274 LYS   A N   1 
ATOM   2172 C  CA  . LYS   A 1 275 ? 6.578   -51.699 39.662 1.00 44.68  ?  274 LYS   A CA  1 
ATOM   2173 C  C   . LYS   A 1 275 ? 7.720   -51.848 40.666 1.00 43.22  ?  274 LYS   A C   1 
ATOM   2174 O  O   . LYS   A 1 275 ? 8.900   -51.853 40.294 1.00 43.64  ?  274 LYS   A O   1 
ATOM   2175 C  CB  . LYS   A 1 275 ? 5.901   -53.053 39.423 1.00 39.36  ?  274 LYS   A CB  1 
ATOM   2176 C  CG  . LYS   A 1 275 ? 4.663   -53.010 38.594 1.00 43.65  ?  274 LYS   A CG  1 
ATOM   2177 C  CD  . LYS   A 1 275 ? 4.608   -54.263 37.744 1.00 46.30  ?  274 LYS   A CD  1 
ATOM   2178 C  CE  . LYS   A 1 275 ? 3.206   -54.684 37.389 1.00 46.13  ?  274 LYS   A CE  1 
ATOM   2179 N  NZ  . LYS   A 1 275 ? 3.298   -56.066 36.838 1.00 55.79  ?  274 LYS   A NZ  1 
ATOM   2180 N  N   . HIS   A 1 276 ? 7.378   -52.003 41.943 1.00 39.83  ?  275 HIS   A N   1 
ATOM   2181 C  CA  . HIS   A 1 276 ? 8.378   -52.058 43.008 1.00 41.78  ?  275 HIS   A CA  1 
ATOM   2182 C  C   . HIS   A 1 276 ? 8.455   -53.467 43.589 1.00 38.02  ?  275 HIS   A C   1 
ATOM   2183 O  O   . HIS   A 1 276 ? 7.436   -54.034 43.992 1.00 41.07  ?  275 HIS   A O   1 
ATOM   2184 C  CB  . HIS   A 1 276 ? 8.037   -51.041 44.100 1.00 44.52  ?  275 HIS   A CB  1 
ATOM   2185 C  CG  . HIS   A 1 276 ? 9.085   -50.904 45.150 1.00 47.32  ?  275 HIS   A CG  1 
ATOM   2186 N  ND1 . HIS   A 1 276 ? 10.277  -50.242 44.928 1.00 45.94  ?  275 HIS   A ND1 1 
ATOM   2187 C  CD2 . HIS   A 1 276 ? 9.115   -51.324 46.439 1.00 40.40  ?  275 HIS   A CD2 1 
ATOM   2188 C  CE1 . HIS   A 1 276 ? 11.006  -50.281 46.033 1.00 45.46  ?  275 HIS   A CE1 1 
ATOM   2189 N  NE2 . HIS   A 1 276 ? 10.326  -50.933 46.963 1.00 44.77  ?  275 HIS   A NE2 1 
ATOM   2190 N  N   . ILE   A 1 277 ? 9.652   -54.037 43.620 1.00 37.13  ?  276 ILE   A N   1 
ATOM   2191 C  CA  . ILE   A 1 277 ? 9.885   -55.337 44.247 1.00 45.60  ?  276 ILE   A CA  1 
ATOM   2192 C  C   . ILE   A 1 277 ? 10.680  -55.117 45.526 1.00 47.42  ?  276 ILE   A C   1 
ATOM   2193 O  O   . ILE   A 1 277 ? 11.708  -54.423 45.521 1.00 43.20  ?  276 ILE   A O   1 
ATOM   2194 C  CB  . ILE   A 1 277 ? 10.628  -56.319 43.328 1.00 47.31  ?  276 ILE   A CB  1 
ATOM   2195 C  CG1 . ILE   A 1 277 ? 10.032  -56.287 41.919 1.00 48.29  ?  276 ILE   A CG1 1 
ATOM   2196 C  CG2 . ILE   A 1 277 ? 10.605  -57.721 43.955 1.00 40.24  ?  276 ILE   A CG2 1 
ATOM   2197 C  CD1 . ILE   A 1 277 ? 8.575   -56.735 41.893 1.00 46.76  ?  276 ILE   A CD1 1 
ATOM   2198 N  N   . THR   A 1 278 ? 10.206  -55.706 46.616 1.00 42.72  ?  277 THR   A N   1 
ATOM   2199 C  CA  . THR   A 1 278 ? 10.846  -55.546 47.908 1.00 49.53  ?  277 THR   A CA  1 
ATOM   2200 C  C   . THR   A 1 278 ? 10.961  -56.905 48.595 1.00 46.36  ?  277 THR   A C   1 
ATOM   2201 O  O   . THR   A 1 278 ? 10.054  -57.742 48.504 1.00 47.74  ?  277 THR   A O   1 
ATOM   2202 C  CB  . THR   A 1 278 ? 10.071  -54.513 48.761 1.00 44.96  ?  277 THR   A CB  1 
ATOM   2203 O  OG1 . THR   A 1 278 ? 10.787  -54.275 49.972 1.00 45.24  ?  277 THR   A OG1 1 
ATOM   2204 C  CG2 . THR   A 1 278 ? 8.656   -54.978 49.068 1.00 42.12  ?  277 THR   A CG2 1 
ATOM   2205 N  N   . SER   A 1 279 ? 12.096  -57.136 49.244 1.00 42.94  ?  278 SER   A N   1 
ATOM   2206 C  CA  . SER   A 1 279 ? 12.384  -58.413 49.886 1.00 43.28  ?  278 SER   A CA  1 
ATOM   2207 C  C   . SER   A 1 279 ? 12.066  -58.295 51.368 1.00 43.91  ?  278 SER   A C   1 
ATOM   2208 O  O   . SER   A 1 279 ? 12.788  -57.615 52.103 1.00 41.89  ?  278 SER   A O   1 
ATOM   2209 C  CB  . SER   A 1 279 ? 13.842  -58.815 49.699 1.00 38.93  ?  278 SER   A CB  1 
ATOM   2210 O  OG  . SER   A 1 279 ? 14.100  -60.021 50.402 1.00 45.54  ?  278 SER   A OG  1 
ATOM   2211 N  N   . LYS   A 1 280 ? 11.008  -58.965 51.806 1.00 40.04  ?  279 LYS   A N   1 
ATOM   2212 C  CA  . LYS   A 1 280 ? 10.642  -59.025 53.220 1.00 43.50  ?  279 LYS   A CA  1 
ATOM   2213 C  C   . LYS   A 1 280 ? 10.788  -60.469 53.709 1.00 41.99  ?  279 LYS   A C   1 
ATOM   2214 O  O   . LYS   A 1 280 ? 11.850  -61.062 53.487 1.00 44.97  ?  279 LYS   A O   1 
ATOM   2215 C  CB  . LYS   A 1 280 ? 9.256   -58.424 53.422 1.00 43.99  ?  279 LYS   A CB  1 
ATOM   2216 C  CG  . LYS   A 1 280 ? 9.116   -57.062 52.818 1.00 41.98  ?  279 LYS   A CG  1 
ATOM   2217 C  CD  . LYS   A 1 280 ? 9.943   -56.048 53.588 1.00 34.83  ?  279 LYS   A CD  1 
ATOM   2218 C  CE  . LYS   A 1 280 ? 9.378   -54.664 53.389 1.00 40.08  ?  279 LYS   A CE  1 
ATOM   2219 N  NZ  . LYS   A 1 280 ? 7.908   -54.684 53.618 1.00 53.31  ?  279 LYS   A NZ  1 
ATOM   2220 N  N   . GLU   A 1 281 ? 9.797   -61.035 54.396 1.00 41.49  ?  280 GLU   A N   1 
ATOM   2221 C  CA  . GLU   A 1 281 ? 9.797   -62.470 54.664 1.00 48.96  ?  280 GLU   A CA  1 
ATOM   2222 C  C   . GLU   A 1 281 ? 9.719   -63.268 53.363 1.00 55.39  ?  280 GLU   A C   1 
ATOM   2223 O  O   . GLU   A 1 281 ? 10.234  -64.392 53.280 1.00 59.48  ?  280 GLU   A O   1 
ATOM   2224 C  CB  . GLU   A 1 281 ? 8.624   -62.797 55.581 1.00 42.22  ?  280 GLU   A CB  1 
ATOM   2225 C  CG  . GLU   A 1 281 ? 7.307   -62.842 54.834 1.00 48.22  ?  280 GLU   A CG  1 
ATOM   2226 C  CD  . GLU   A 1 281 ? 6.538   -61.523 54.834 1.00 56.33  ?  280 GLU   A CD  1 
ATOM   2227 O  OE1 . GLU   A 1 281 ? 7.163   -60.431 54.949 1.00 53.92  ?  280 GLU   A OE1 1 
ATOM   2228 O  OE2 . GLU   A 1 281 ? 5.295   -61.581 54.677 1.00 56.49  -1 280 GLU   A OE2 1 
ATOM   2229 N  N   . THR   A 1 282 ? 9.086   -62.691 52.340 1.00 53.35  ?  281 THR   A N   1 
ATOM   2230 C  CA  . THR   A 1 282 ? 9.001   -63.221 50.994 1.00 50.95  ?  281 THR   A CA  1 
ATOM   2231 C  C   . THR   A 1 282 ? 9.171   -62.037 50.052 1.00 49.46  ?  281 THR   A C   1 
ATOM   2232 O  O   . THR   A 1 282 ? 9.325   -60.897 50.498 1.00 46.26  ?  281 THR   A O   1 
ATOM   2233 C  CB  . THR   A 1 282 ? 7.669   -63.962 50.782 1.00 50.66  ?  281 THR   A CB  1 
ATOM   2234 O  OG1 . THR   A 1 282 ? 7.758   -64.851 49.659 1.00 52.42  ?  281 THR   A OG1 1 
ATOM   2235 C  CG2 . THR   A 1 282 ? 6.526   -62.984 50.566 1.00 50.14  ?  281 THR   A CG2 1 
ATOM   2236 N  N   . LEU   A 1 283 ? 9.154   -62.297 48.744 1.00 50.98  ?  282 LEU   A N   1 
ATOM   2237 C  CA  . LEU   A 1 283 ? 9.218   -61.217 47.772 1.00 45.87  ?  282 LEU   A CA  1 
ATOM   2238 C  C   . LEU   A 1 283 ? 7.839   -60.586 47.615 1.00 54.27  ?  282 LEU   A C   1 
ATOM   2239 O  O   . LEU   A 1 283 ? 6.827   -61.299 47.521 1.00 54.15  ?  282 LEU   A O   1 
ATOM   2240 C  CB  . LEU   A 1 283 ? 9.722   -61.721 46.422 1.00 48.13  ?  282 LEU   A CB  1 
ATOM   2241 C  CG  . LEU   A 1 283 ? 11.099  -62.385 46.415 1.00 53.19  ?  282 LEU   A CG  1 
ATOM   2242 C  CD1 . LEU   A 1 283 ? 11.610  -62.448 45.002 1.00 47.61  ?  282 LEU   A CD1 1 
ATOM   2243 C  CD2 . LEU   A 1 283 ? 12.065  -61.639 47.292 1.00 47.52  ?  282 LEU   A CD2 1 
ATOM   2244 N  N   . TYR   A 1 284 ? 7.798   -59.247 47.597 1.00 45.43  ?  283 TYR   A N   1 
ATOM   2245 C  CA  . TYR   A 1 284 ? 6.557   -58.508 47.401 1.00 47.40  ?  283 TYR   A CA  1 
ATOM   2246 C  C   . TYR   A 1 284 ? 6.693   -57.583 46.205 1.00 45.57  ?  283 TYR   A C   1 
ATOM   2247 O  O   . TYR   A 1 284 ? 7.780   -57.078 45.891 1.00 43.48  ?  283 TYR   A O   1 
ATOM   2248 C  CB  . TYR   A 1 284 ? 6.156   -57.655 48.628 1.00 52.93  ?  283 TYR   A CB  1 
ATOM   2249 C  CG  . TYR   A 1 284 ? 5.508   -58.441 49.742 1.00 52.09  ?  283 TYR   A CG  1 
ATOM   2250 C  CD1 . TYR   A 1 284 ? 4.217   -58.934 49.610 1.00 51.40  ?  283 TYR   A CD1 1 
ATOM   2251 C  CD2 . TYR   A 1 284 ? 6.194   -58.703 50.910 1.00 44.73  ?  283 TYR   A CD2 1 
ATOM   2252 C  CE1 . TYR   A 1 284 ? 3.635   -59.658 50.604 1.00 49.28  ?  283 TYR   A CE1 1 
ATOM   2253 C  CE2 . TYR   A 1 284 ? 5.623   -59.439 51.899 1.00 52.22  ?  283 TYR   A CE2 1 
ATOM   2254 C  CZ  . TYR   A 1 284 ? 4.341   -59.913 51.747 1.00 51.20  ?  283 TYR   A CZ  1 
ATOM   2255 O  OH  . TYR   A 1 284 ? 3.760   -60.632 52.761 1.00 48.95  ?  283 TYR   A OH  1 
ATOM   2256 N  N   . CYS   A 1 285 ? 5.562   -57.343 45.562 1.00 41.97  ?  284 CYS   A N   1 
ATOM   2257 C  CA  . CYS   A 1 285 ? 5.504   -56.524 44.366 1.00 40.86  ?  284 CYS   A CA  1 
ATOM   2258 C  C   . CYS   A 1 285 ? 4.438   -55.485 44.624 1.00 40.65  ?  284 CYS   A C   1 
ATOM   2259 O  O   . CYS   A 1 285 ? 3.261   -55.828 44.770 1.00 48.15  ?  284 CYS   A O   1 
ATOM   2260 C  CB  . CYS   A 1 285 ? 5.180   -57.363 43.134 1.00 38.72  ?  284 CYS   A CB  1 
ATOM   2261 S  SG  . CYS   A 1 285 ? 5.145   -56.413 41.587 1.00 54.13  ?  284 CYS   A SG  1 
ATOM   2262 N  N   . ILE   A 1 286 ? 4.847   -54.232 44.731 1.00 37.17  ?  285 ILE   A N   1 
ATOM   2263 C  CA  . ILE   A 1 286 ? 3.920   -53.122 44.916 1.00 44.20  ?  285 ILE   A CA  1 
ATOM   2264 C  C   . ILE   A 1 286 ? 3.761   -52.440 43.562 1.00 46.75  ?  285 ILE   A C   1 
ATOM   2265 O  O   . ILE   A 1 286 ? 4.757   -52.080 42.920 1.00 47.68  ?  285 ILE   A O   1 
ATOM   2266 C  CB  . ILE   A 1 286 ? 4.419   -52.142 45.995 1.00 41.05  ?  285 ILE   A CB  1 
ATOM   2267 C  CG1 . ILE   A 1 286 ? 4.996   -52.904 47.193 1.00 38.67  ?  285 ILE   A CG1 1 
ATOM   2268 C  CG2 . ILE   A 1 286 ? 3.298   -51.238 46.458 1.00 39.65  ?  285 ILE   A CG2 1 
ATOM   2269 C  CD1 . ILE   A 1 286 ? 5.303   -52.031 48.375 1.00 43.06  ?  285 ILE   A CD1 1 
ATOM   2270 N  N   . ASP   A 1 287 ? 2.520   -52.337 43.092 1.00 40.37  ?  286 ASP   A N   1 
ATOM   2271 C  CA  . ASP   A 1 287 ? 2.171   -51.580 41.901 1.00 39.16  ?  286 ASP   A CA  1 
ATOM   2272 C  C   . ASP   A 1 287 ? 1.107   -50.589 42.363 1.00 46.58  ?  286 ASP   A C   1 
ATOM   2273 O  O   . ASP   A 1 287 ? -0.086  -50.907 42.349 1.00 48.23  ?  286 ASP   A O   1 
ATOM   2274 C  CB  . ASP   A 1 287 ? 1.667   -52.462 40.777 1.00 41.32  ?  286 ASP   A CB  1 
ATOM   2275 C  CG  . ASP   A 1 287 ? 1.465   -51.684 39.471 1.00 59.42  ?  286 ASP   A CG  1 
ATOM   2276 O  OD1 . ASP   A 1 287 ? 1.806   -50.467 39.465 1.00 61.26  ?  286 ASP   A OD1 1 
ATOM   2277 O  OD2 . ASP   A 1 287 ? 0.972   -52.274 38.461 1.00 61.42  -1 286 ASP   A OD2 1 
ATOM   2278 N  N   . GLY   A 1 288 ? 1.545   -49.399 42.791 1.00 39.54  ?  287 GLY   A N   1 
ATOM   2279 C  CA  . GLY   A 1 288 ? 0.642   -48.393 43.319 1.00 36.66  ?  287 GLY   A CA  1 
ATOM   2280 C  C   . GLY   A 1 288 ? -0.124  -48.904 44.523 1.00 45.64  ?  287 GLY   A C   1 
ATOM   2281 O  O   . GLY   A 1 288 ? 0.461   -49.159 45.589 1.00 43.57  ?  287 GLY   A O   1 
ATOM   2282 N  N   . ALA   A 1 289 ? -1.435  -49.087 44.358 1.00 44.00  ?  288 ALA   A N   1 
ATOM   2283 C  CA  . ALA   A 1 289 ? -2.266  -49.675 45.398 1.00 45.07  ?  288 ALA   A CA  1 
ATOM   2284 C  C   . ALA   A 1 289 ? -2.283  -51.204 45.375 1.00 48.69  ?  288 ALA   A C   1 
ATOM   2285 O  O   . ALA   A 1 289 ? -2.839  -51.807 46.300 1.00 53.70  ?  288 ALA   A O   1 
ATOM   2286 C  CB  . ALA   A 1 289 ? -3.698  -49.149 45.287 1.00 40.97  ?  288 ALA   A CB  1 
ATOM   2287 N  N   . LEU   A 1 290 ? -1.667  -51.847 44.382 1.00 41.21  ?  289 LEU   A N   1 
ATOM   2288 C  CA  . LEU   A 1 290 ? -1.707  -53.298 44.245 1.00 45.01  ?  289 LEU   A CA  1 
ATOM   2289 C  C   . LEU   A 1 290 ? -0.421  -53.981 44.715 1.00 50.39  ?  289 LEU   A C   1 
ATOM   2290 O  O   . LEU   A 1 290 ? 0.691   -53.502 44.458 1.00 47.07  ?  289 LEU   A O   1 
ATOM   2291 C  CB  . LEU   A 1 290 ? -1.980  -53.675 42.795 1.00 48.70  ?  289 LEU   A CB  1 
ATOM   2292 C  CG  . LEU   A 1 290 ? -3.105  -52.821 42.220 1.00 53.95  ?  289 LEU   A CG  1 
ATOM   2293 C  CD1 . LEU   A 1 290 ? -3.218  -53.058 40.714 1.00 43.75  ?  289 LEU   A CD1 1 
ATOM   2294 C  CD2 . LEU   A 1 290 ? -4.426  -53.088 42.958 1.00 46.44  ?  289 LEU   A CD2 1 
ATOM   2295 N  N   . LEU   A 1 291 ? -0.589  -55.143 45.359 1.00 49.93  ?  290 LEU   A N   1 
ATOM   2296 C  CA  . LEU   A 1 291 ? 0.484   -55.931 45.952 1.00 47.35  ?  290 LEU   A CA  1 
ATOM   2297 C  C   . LEU   A 1 291 ? 0.357   -57.389 45.517 1.00 49.33  ?  290 LEU   A C   1 
ATOM   2298 O  O   . LEU   A 1 291 ? -0.755  -57.887 45.351 1.00 54.63  ?  290 LEU   A O   1 
ATOM   2299 C  CB  . LEU   A 1 291 ? 0.408   -55.809 47.485 1.00 49.95  ?  290 LEU   A CB  1 
ATOM   2300 C  CG  . LEU   A 1 291 ? 1.279   -56.585 48.476 1.00 47.17  ?  290 LEU   A CG  1 
ATOM   2301 C  CD1 . LEU   A 1 291 ? 2.680   -56.053 48.525 1.00 47.42  ?  290 LEU   A CD1 1 
ATOM   2302 C  CD2 . LEU   A 1 291 ? 0.634   -56.446 49.815 1.00 38.57  ?  290 LEU   A CD2 1 
ATOM   2303 N  N   . THR   A 1 292 ? 1.489   -58.079 45.311 1.00 46.82  ?  291 THR   A N   1 
ATOM   2304 C  CA  . THR   A 1 292 ? 1.469   -59.532 45.103 1.00 46.89  ?  291 THR   A CA  1 
ATOM   2305 C  C   . THR   A 1 292 ? 2.695   -60.166 45.758 1.00 46.77  ?  291 THR   A C   1 
ATOM   2306 O  O   . THR   A 1 292 ? 3.690   -59.491 46.025 1.00 53.42  ?  291 THR   A O   1 
ATOM   2307 C  CB  . THR   A 1 292 ? 1.401   -59.937 43.609 1.00 48.39  ?  291 THR   A CB  1 
ATOM   2308 O  OG1 . THR   A 1 292 ? 2.618   -59.593 42.927 1.00 56.95  ?  291 THR   A OG1 1 
ATOM   2309 C  CG2 . THR   A 1 292 ? 0.222   -59.307 42.900 1.00 37.18  ?  291 THR   A CG2 1 
ATOM   2310 N  N   . LYS   A 1 293 ? 2.610   -61.471 46.050 1.00 48.51  ?  292 LYS   A N   1 
ATOM   2311 C  CA  . LYS   A 1 293 ? 3.668   -62.193 46.755 1.00 49.00  ?  292 LYS   A CA  1 
ATOM   2312 C  C   . LYS   A 1 293 ? 4.195   -63.330 45.893 1.00 49.87  ?  292 LYS   A C   1 
ATOM   2313 O  O   . LYS   A 1 293 ? 3.436   -63.945 45.140 1.00 55.52  ?  292 LYS   A O   1 
ATOM   2314 C  CB  . LYS   A 1 293 ? 3.185   -62.824 48.081 1.00 54.59  ?  292 LYS   A CB  1 
ATOM   2315 C  CG  . LYS   A 1 293 ? 2.014   -62.179 48.782 1.00 55.56  ?  292 LYS   A CG  1 
ATOM   2316 C  CD  . LYS   A 1 293 ? 1.783   -62.814 50.167 1.00 61.41  ?  292 LYS   A CD  1 
ATOM   2317 C  CE  . LYS   A 1 293 ? 1.565   -64.321 50.082 1.00 64.57  ?  292 LYS   A CE  1 
ATOM   2318 N  NZ  . LYS   A 1 293 ? 1.833   -64.991 51.392 1.00 72.96  ?  292 LYS   A NZ  1 
ATOM   2319 N  N   . SER   A 1 294 ? 5.483   -63.649 46.040 1.00 45.27  ?  293 SER   A N   1 
ATOM   2320 C  CA  . SER   A 1 294 ? 5.988   -64.879 45.437 1.00 52.67  ?  293 SER   A CA  1 
ATOM   2321 C  C   . SER   A 1 294 ? 7.253   -65.337 46.149 1.00 57.91  ?  293 SER   A C   1 
ATOM   2322 O  O   . SER   A 1 294 ? 7.970   -64.548 46.770 1.00 57.31  ?  293 SER   A O   1 
ATOM   2323 C  CB  . SER   A 1 294 ? 6.265   -64.717 43.943 1.00 50.44  ?  293 SER   A CB  1 
ATOM   2324 O  OG  . SER   A 1 294 ? 6.872   -63.478 43.679 1.00 46.96  ?  293 SER   A OG  1 
ATOM   2325 N  N   . SER   A 1 295 ? 7.511   -66.641 46.037 1.00 64.90  ?  294 SER   A N   1 
ATOM   2326 C  CA  . SER   A 1 295 ? 8.728   -67.230 46.583 1.00 63.83  ?  294 SER   A CA  1 
ATOM   2327 C  C   . SER   A 1 295 ? 9.961   -66.679 45.878 1.00 66.76  ?  294 SER   A C   1 
ATOM   2328 O  O   . SER   A 1 295 ? 10.880  -66.151 46.520 1.00 68.70  ?  294 SER   A O   1 
ATOM   2329 C  CB  . SER   A 1 295 ? 8.662   -68.759 46.453 1.00 75.75  ?  294 SER   A CB  1 
ATOM   2330 O  OG  . SER   A 1 295 ? 7.494   -69.196 45.746 1.00 75.29  ?  294 SER   A OG  1 
ATOM   2331 N  N   . GLU   A 1 296 ? 9.995   -66.791 44.546 1.00 68.94  ?  295 GLU   A N   1 
ATOM   2332 C  CA  . GLU   A 1 296 ? 11.082  -66.291 43.707 1.00 65.95  ?  295 GLU   A CA  1 
ATOM   2333 C  C   . GLU   A 1 296 ? 10.553  -65.229 42.750 1.00 60.84  ?  295 GLU   A C   1 
ATOM   2334 O  O   . GLU   A 1 296 ? 9.340   -65.038 42.600 1.00 59.11  ?  295 GLU   A O   1 
ATOM   2335 C  CB  . GLU   A 1 296 ? 11.747  -67.429 42.911 1.00 64.72  ?  295 GLU   A CB  1 
ATOM   2336 C  CG  . GLU   A 1 296 ? 13.120  -67.893 43.417 1.00 77.66  ?  295 GLU   A CG  1 
ATOM   2337 C  CD  . GLU   A 1 296 ? 13.029  -69.008 44.467 1.00 85.76  ?  295 GLU   A CD  1 
ATOM   2338 O  OE1 . GLU   A 1 296 ? 11.985  -69.704 44.505 1.00 80.78  ?  295 GLU   A OE1 1 
ATOM   2339 O  OE2 . GLU   A 1 296 ? 14.008  -69.202 45.236 1.00 84.10  -1 295 GLU   A OE2 1 
ATOM   2340 N  N   . TYR   A 1 297 ? 11.481  -64.533 42.093 1.00 51.83  ?  296 TYR   A N   1 
ATOM   2341 C  CA  . TYR   A 1 297 ? 11.121  -63.523 41.107 1.00 44.90  ?  296 TYR   A CA  1 
ATOM   2342 C  C   . TYR   A 1 297 ? 12.131  -63.592 39.975 1.00 53.82  ?  296 TYR   A C   1 
ATOM   2343 O  O   . TYR   A 1 297 ? 13.345  -63.583 40.225 1.00 56.85  ?  296 TYR   A O   1 
ATOM   2344 C  CB  . TYR   A 1 297 ? 11.140  -62.110 41.689 1.00 49.56  ?  296 TYR   A CB  1 
ATOM   2345 C  CG  . TYR   A 1 297 ? 10.809  -61.036 40.676 1.00 49.56  ?  296 TYR   A CG  1 
ATOM   2346 C  CD1 . TYR   A 1 297 ? 11.823  -60.426 39.920 1.00 47.77  ?  296 TYR   A CD1 1 
ATOM   2347 C  CD2 . TYR   A 1 297 ? 9.496   -60.566 40.528 1.00 44.95  ?  296 TYR   A CD2 1 
ATOM   2348 C  CE1 . TYR   A 1 297 ? 11.522  -59.437 38.982 1.00 47.80  ?  296 TYR   A CE1 1 
ATOM   2349 C  CE2 . TYR   A 1 297 ? 9.184   -59.564 39.599 1.00 46.75  ?  296 TYR   A CE2 1 
ATOM   2350 C  CZ  . TYR   A 1 297 ? 10.193  -59.002 38.832 1.00 52.65  ?  296 TYR   A CZ  1 
ATOM   2351 O  OH  . TYR   A 1 297 ? 9.846   -58.010 37.937 1.00 50.31  ?  296 TYR   A OH  1 
ATOM   2352 N  N   . LYS   A 1 298 ? 11.635  -63.610 38.738 1.00 48.94  ?  297 LYS   A N   1 
ATOM   2353 C  CA  . LYS   A 1 298 ? 12.478  -63.498 37.551 1.00 47.64  ?  297 LYS   A CA  1 
ATOM   2354 C  C   . LYS   A 1 298 ? 11.770  -62.527 36.616 1.00 46.38  ?  297 LYS   A C   1 
ATOM   2355 O  O   . LYS   A 1 298 ? 10.550  -62.629 36.431 1.00 49.44  ?  297 LYS   A O   1 
ATOM   2356 C  CB  . LYS   A 1 298 ? 12.705  -64.882 36.913 1.00 55.08  ?  297 LYS   A CB  1 
ATOM   2357 C  CG  . LYS   A 1 298 ? 13.984  -65.058 36.094 1.00 58.99  ?  297 LYS   A CG  1 
ATOM   2358 C  CD  . LYS   A 1 298 ? 13.630  -64.896 34.624 1.00 62.29  ?  297 LYS   A CD  1 
ATOM   2359 C  CE  . LYS   A 1 298 ? 14.836  -64.692 33.737 1.00 57.11  ?  297 LYS   A CE  1 
ATOM   2360 N  NZ  . LYS   A 1 298 ? 14.290  -64.570 32.349 1.00 61.76  ?  297 LYS   A NZ  1 
ATOM   2361 N  N   . GLY   A 1 299 ? 12.495  -61.534 36.100 1.00 39.78  ?  298 GLY   A N   1 
ATOM   2362 C  CA  . GLY   A 1 299 ? 11.827  -60.417 35.461 1.00 42.37  ?  298 GLY   A CA  1 
ATOM   2363 C  C   . GLY   A 1 299 ? 12.739  -59.272 35.039 1.00 46.46  ?  298 GLY   A C   1 
ATOM   2364 O  O   . GLY   A 1 299 ? 13.964  -59.316 35.233 1.00 44.64  ?  298 GLY   A O   1 
ATOM   2365 N  N   . PRO   A 1 300 ? 12.134  -58.200 34.436 1.00 42.00  ?  299 PRO   A N   1 
ATOM   2366 C  CA  . PRO   A 1 300 ? 12.924  -57.082 33.895 1.00 44.46  ?  299 PRO   A CA  1 
ATOM   2367 C  C   . PRO   A 1 300 ? 13.247  -56.008 34.925 1.00 45.61  ?  299 PRO   A C   1 
ATOM   2368 O  O   . PRO   A 1 300 ? 12.396  -55.167 35.237 1.00 45.54  ?  299 PRO   A O   1 
ATOM   2369 C  CB  . PRO   A 1 300 ? 12.012  -56.521 32.796 1.00 39.30  ?  299 PRO   A CB  1 
ATOM   2370 C  CG  . PRO   A 1 300 ? 10.636  -56.807 33.256 1.00 35.23  ?  299 PRO   A CG  1 
ATOM   2371 C  CD  . PRO   A 1 300 ? 10.694  -58.009 34.193 1.00 40.92  ?  299 PRO   A CD  1 
ATOM   2372 N  N   . ILE   A 1 301 ? 14.485  -56.007 35.410 1.00 41.53  ?  300 ILE   A N   1 
ATOM   2373 C  CA  . ILE   A 1 301 ? 14.940  -55.173 36.518 1.00 43.07  ?  300 ILE   A CA  1 
ATOM   2374 C  C   . ILE   A 1 301 ? 15.920  -54.140 35.985 1.00 40.18  ?  300 ILE   A C   1 
ATOM   2375 O  O   . ILE   A 1 301 ? 16.785  -54.467 35.170 1.00 46.71  ?  300 ILE   A O   1 
ATOM   2376 C  CB  . ILE   A 1 301 ? 15.603  -56.047 37.612 1.00 44.44  ?  300 ILE   A CB  1 
ATOM   2377 C  CG1 . ILE   A 1 301 ? 14.573  -56.971 38.291 1.00 47.52  ?  300 ILE   A CG1 1 
ATOM   2378 C  CG2 . ILE   A 1 301 ? 16.350  -55.213 38.630 1.00 42.98  ?  300 ILE   A CG2 1 
ATOM   2379 C  CD1 . ILE   A 1 301 ? 13.238  -56.324 38.571 1.00 39.24  ?  300 ILE   A CD1 1 
ATOM   2380 N  N   . THR   A 1 302 ? 15.814  -52.897 36.457 1.00 46.29  ?  301 THR   A N   1 
ATOM   2381 C  CA  . THR   A 1 302 ? 16.784  -51.877 36.060 1.00 43.81  ?  301 THR   A CA  1 
ATOM   2382 C  C   . THR   A 1 302 ? 17.535  -51.186 37.207 1.00 43.65  ?  301 THR   A C   1 
ATOM   2383 O  O   . THR   A 1 302 ? 18.643  -50.699 36.963 1.00 45.15  ?  301 THR   A O   1 
ATOM   2384 C  CB  . THR   A 1 302 ? 16.110  -50.809 35.182 1.00 41.93  ?  301 THR   A CB  1 
ATOM   2385 O  OG1 . THR   A 1 302 ? 17.006  -49.708 35.025 1.00 46.61  ?  301 THR   A OG1 1 
ATOM   2386 C  CG2 . THR   A 1 302 ? 14.782  -50.337 35.797 1.00 38.85  ?  301 THR   A CG2 1 
ATOM   2387 N  N   . ASP   A 1 303 ? 16.993  -51.125 38.438 1.00 44.84  ?  302 ASP   A N   1 
ATOM   2388 C  CA  . ASP   A 1 303 ? 17.803  -50.789 39.616 1.00 50.25  ?  302 ASP   A CA  1 
ATOM   2389 C  C   . ASP   A 1 303 ? 17.587  -51.779 40.763 1.00 46.94  ?  302 ASP   A C   1 
ATOM   2390 O  O   . ASP   A 1 303 ? 16.461  -52.225 41.014 1.00 42.46  ?  302 ASP   A O   1 
ATOM   2391 C  CB  . ASP   A 1 303 ? 17.512  -49.394 40.195 1.00 50.07  ?  302 ASP   A CB  1 
ATOM   2392 C  CG  . ASP   A 1 303 ? 17.029  -48.413 39.175 1.00 48.90  ?  302 ASP   A CG  1 
ATOM   2393 O  OD1 . ASP   A 1 303 ? 17.844  -47.907 38.351 1.00 48.75  -1 302 ASP   A OD1 1 
ATOM   2394 O  OD2 . ASP   A 1 303 ? 15.813  -48.139 39.235 1.00 51.51  ?  302 ASP   A OD2 1 
ATOM   2395 N  N   . VAL   A 1 304 ? 18.671  -52.069 41.488 1.00 44.83  ?  303 VAL   A N   1 
ATOM   2396 C  CA  . VAL   A 1 304 ? 18.651  -52.892 42.693 1.00 41.75  ?  303 VAL   A CA  1 
ATOM   2397 C  C   . VAL   A 1 304 ? 19.428  -52.152 43.767 1.00 45.92  ?  303 VAL   A C   1 
ATOM   2398 O  O   . VAL   A 1 304 ? 20.591  -51.783 43.541 1.00 40.75  ?  303 VAL   A O   1 
ATOM   2399 C  CB  . VAL   A 1 304 ? 19.294  -54.278 42.488 1.00 45.31  ?  303 VAL   A CB  1 
ATOM   2400 C  CG1 . VAL   A 1 304 ? 19.248  -55.046 43.787 1.00 40.26  ?  303 VAL   A CG1 1 
ATOM   2401 C  CG2 . VAL   A 1 304 ? 18.643  -55.066 41.316 1.00 40.34  ?  303 VAL   A CG2 1 
ATOM   2402 N  N   . PHE   A 1 305 ? 18.800  -51.968 44.935 1.00 39.96  ?  304 PHE   A N   1 
ATOM   2403 C  CA  . PHE   A 1 305 ? 19.409  -51.320 46.089 1.00 40.76  ?  304 PHE   A CA  1 
ATOM   2404 C  C   . PHE   A 1 305 ? 19.863  -52.371 47.094 1.00 45.87  ?  304 PHE   A C   1 
ATOM   2405 O  O   . PHE   A 1 305 ? 19.177  -53.377 47.303 1.00 44.36  ?  304 PHE   A O   1 
ATOM   2406 C  CB  . PHE   A 1 305 ? 18.415  -50.377 46.760 1.00 43.44  ?  304 PHE   A CB  1 
ATOM   2407 C  CG  . PHE   A 1 305 ? 17.963  -49.272 45.875 1.00 48.96  ?  304 PHE   A CG  1 
ATOM   2408 C  CD1 . PHE   A 1 305 ? 16.992  -49.502 44.896 1.00 47.06  ?  304 PHE   A CD1 1 
ATOM   2409 C  CD2 . PHE   A 1 305 ? 18.510  -48.002 46.000 1.00 42.05  ?  304 PHE   A CD2 1 
ATOM   2410 C  CE1 . PHE   A 1 305 ? 16.597  -48.493 44.066 1.00 40.35  ?  304 PHE   A CE1 1 
ATOM   2411 C  CE2 . PHE   A 1 305 ? 18.108  -46.981 45.161 1.00 37.93  ?  304 PHE   A CE2 1 
ATOM   2412 C  CZ  . PHE   A 1 305 ? 17.161  -47.222 44.205 1.00 40.06  ?  304 PHE   A CZ  1 
ATOM   2413 N  N   . TYR   A 1 306 ? 21.012  -52.130 47.724 1.00 43.75  ?  305 TYR   A N   1 
ATOM   2414 C  CA  . TYR   A 1 306 ? 21.574  -53.049 48.707 1.00 44.13  ?  305 TYR   A CA  1 
ATOM   2415 C  C   . TYR   A 1 306 ? 21.901  -52.295 49.988 1.00 48.38  ?  305 TYR   A C   1 
ATOM   2416 O  O   . TYR   A 1 306 ? 21.983  -51.061 49.997 1.00 47.97  ?  305 TYR   A O   1 
ATOM   2417 C  CB  . TYR   A 1 306 ? 22.834  -53.716 48.176 1.00 40.99  ?  305 TYR   A CB  1 
ATOM   2418 C  CG  . TYR   A 1 306 ? 22.618  -54.504 46.900 1.00 47.50  ?  305 TYR   A CG  1 
ATOM   2419 C  CD1 . TYR   A 1 306 ? 22.243  -55.849 46.938 1.00 41.29  ?  305 TYR   A CD1 1 
ATOM   2420 C  CD2 . TYR   A 1 306 ? 22.787  -53.906 45.651 1.00 44.62  ?  305 TYR   A CD2 1 
ATOM   2421 C  CE1 . TYR   A 1 306 ? 22.057  -56.572 45.768 1.00 43.92  ?  305 TYR   A CE1 1 
ATOM   2422 C  CE2 . TYR   A 1 306 ? 22.591  -54.625 44.476 1.00 43.09  ?  305 TYR   A CE2 1 
ATOM   2423 C  CZ  . TYR   A 1 306 ? 22.230  -55.954 44.535 1.00 46.45  ?  305 TYR   A CZ  1 
ATOM   2424 O  OH  . TYR   A 1 306 ? 22.019  -56.661 43.356 1.00 51.45  ?  305 TYR   A OH  1 
ATOM   2425 N  N   . LYS   A 1 307 ? 22.100  -53.034 51.083 1.00 48.42  ?  306 LYS   A N   1 
ATOM   2426 C  CA  . LYS   A 1 307 ? 22.607  -52.429 52.313 1.00 45.29  ?  306 LYS   A CA  1 
ATOM   2427 C  C   . LYS   A 1 307 ? 24.112  -52.608 52.425 1.00 43.35  ?  306 LYS   A C   1 
ATOM   2428 O  O   . LYS   A 1 307 ? 24.667  -53.635 52.022 1.00 44.28  ?  306 LYS   A O   1 
ATOM   2429 C  CB  . LYS   A 1 307 ? 21.923  -53.020 53.546 1.00 43.18  ?  306 LYS   A CB  1 
ATOM   2430 C  CG  . LYS   A 1 307 ? 20.429  -52.849 53.506 1.00 48.34  ?  306 LYS   A CG  1 
ATOM   2431 C  CD  . LYS   A 1 307 ? 19.829  -52.618 54.858 1.00 52.62  ?  306 LYS   A CD  1 
ATOM   2432 C  CE  . LYS   A 1 307 ? 18.663  -51.645 54.785 1.00 55.06  ?  306 LYS   A CE  1 
ATOM   2433 N  NZ  . LYS   A 1 307 ? 17.362  -52.365 54.749 1.00 56.82  ?  306 LYS   A NZ  1 
ATOM   2434 N  N   . GLU   A 1 308 ? 24.780  -51.586 52.958 1.00 45.34  ?  307 GLU   A N   1 
ATOM   2435 C  CA  . GLU   A 1 308 ? 26.203  -51.676 53.273 1.00 49.08  ?  307 GLU   A CA  1 
ATOM   2436 C  C   . GLU   A 1 308 ? 26.439  -50.953 54.592 1.00 51.44  ?  307 GLU   A C   1 
ATOM   2437 O  O   . GLU   A 1 308 ? 25.580  -50.196 55.058 1.00 49.26  ?  307 GLU   A O   1 
ATOM   2438 C  CB  . GLU   A 1 308 ? 27.073  -51.087 52.143 1.00 49.15  ?  307 GLU   A CB  1 
ATOM   2439 C  CG  . GLU   A 1 308 ? 28.575  -51.357 52.268 1.00 57.53  ?  307 GLU   A CG  1 
ATOM   2440 C  CD  . GLU   A 1 308 ? 28.944  -52.821 51.939 1.00 73.13  ?  307 GLU   A CD  1 
ATOM   2441 O  OE1 . GLU   A 1 308 ? 29.030  -53.176 50.727 1.00 63.33  ?  307 GLU   A OE1 1 
ATOM   2442 O  OE2 . GLU   A 1 308 ? 29.188  -53.603 52.901 1.00 79.86  -1 307 GLU   A OE2 1 
ATOM   2443 N  N   . ASN   A 1 309 ? 27.594  -51.216 55.215 1.00 59.37  ?  308 ASN   A N   1 
ATOM   2444 C  CA  . ASN   A 1 309 ? 28.135  -50.320 56.236 1.00 52.41  ?  308 ASN   A CA  1 
ATOM   2445 C  C   . ASN   A 1 309 ? 29.577  -49.973 55.895 1.00 52.25  ?  308 ASN   A C   1 
ATOM   2446 O  O   . ASN   A 1 309 ? 29.882  -48.791 55.717 1.00 51.63  ?  308 ASN   A O   1 
ATOM   2447 C  CB  . ASN   A 1 309 ? 28.015  -50.893 57.665 1.00 51.20  ?  308 ASN   A CB  1 
ATOM   2448 C  CG  . ASN   A 1 309 ? 28.834  -50.050 58.735 1.00 70.71  ?  308 ASN   A CG  1 
ATOM   2449 O  OD1 . ASN   A 1 309 ? 28.327  -49.064 59.311 1.00 55.44  ?  308 ASN   A OD1 1 
ATOM   2450 N  ND2 . ASN   A 1 309 ? 30.068  -50.502 59.042 1.00 69.41  ?  308 ASN   A ND2 1 
ATOM   2451 N  N   . SER   A 1 310 ? 30.457  -50.969 55.736 1.00 58.31  ?  309 SER   A N   1 
ATOM   2452 C  CA  . SER   A 1 310 ? 31.866  -50.737 55.411 1.00 55.22  ?  309 SER   A CA  1 
ATOM   2453 C  C   . SER   A 1 310 ? 32.434  -52.014 54.799 1.00 57.93  ?  309 SER   A C   1 
ATOM   2454 O  O   . SER   A 1 310 ? 32.581  -53.014 55.499 1.00 62.29  ?  309 SER   A O   1 
ATOM   2455 C  CB  . SER   A 1 310 ? 32.650  -50.338 56.646 1.00 51.35  ?  309 SER   A CB  1 
ATOM   2456 O  OG  . SER   A 1 310 ? 34.004  -50.099 56.298 1.00 66.86  ?  309 SER   A OG  1 
ATOM   2457 N  N   . TYR   A 1 311 ? 32.768  -51.977 53.512 1.00 56.14  ?  310 TYR   A N   1 
ATOM   2458 C  CA  . TYR   A 1 311 ? 33.314  -53.129 52.821 1.00 50.95  ?  310 TYR   A CA  1 
ATOM   2459 C  C   . TYR   A 1 311 ? 34.770  -52.889 52.447 1.00 58.84  ?  310 TYR   A C   1 
ATOM   2460 O  O   . TYR   A 1 311 ? 35.196  -51.755 52.205 1.00 59.41  ?  310 TYR   A O   1 
ATOM   2461 C  CB  . TYR   A 1 311 ? 32.507  -53.453 51.567 1.00 52.75  ?  310 TYR   A CB  1 
ATOM   2462 C  CG  . TYR   A 1 311 ? 33.187  -54.408 50.605 1.00 56.59  ?  310 TYR   A CG  1 
ATOM   2463 C  CD1 . TYR   A 1 311 ? 33.978  -53.933 49.567 1.00 62.58  ?  310 TYR   A CD1 1 
ATOM   2464 C  CD2 . TYR   A 1 311 ? 33.017  -55.781 50.712 1.00 55.03  ?  310 TYR   A CD2 1 
ATOM   2465 C  CE1 . TYR   A 1 311 ? 34.599  -54.803 48.668 1.00 65.80  ?  310 TYR   A CE1 1 
ATOM   2466 C  CE2 . TYR   A 1 311 ? 33.625  -56.659 49.818 1.00 55.82  ?  310 TYR   A CE2 1 
ATOM   2467 C  CZ  . TYR   A 1 311 ? 34.419  -56.170 48.798 1.00 64.38  ?  310 TYR   A CZ  1 
ATOM   2468 O  OH  . TYR   A 1 311 ? 35.033  -57.036 47.901 1.00 62.76  ?  310 TYR   A OH  1 
ATOM   2469 N  N   . THR   A 1 312 ? 35.533  -53.982 52.417 1.00 61.19  ?  311 THR   A N   1 
ATOM   2470 C  CA  . THR   A 1 312 ? 36.903  -53.986 51.935 1.00 57.78  ?  311 THR   A CA  1 
ATOM   2471 C  C   . THR   A 1 312 ? 37.178  -55.291 51.210 1.00 62.19  ?  311 THR   A C   1 
ATOM   2472 O  O   . THR   A 1 312 ? 37.002  -56.365 51.791 1.00 71.32  ?  311 THR   A O   1 
ATOM   2473 C  CB  . THR   A 1 312 ? 37.897  -53.812 53.076 1.00 52.49  ?  311 THR   A CB  1 
ATOM   2474 O  OG1 . THR   A 1 312 ? 37.703  -52.526 53.687 1.00 57.23  ?  311 THR   A OG1 1 
ATOM   2475 C  CG2 . THR   A 1 312 ? 39.321  -53.952 52.542 1.00 52.73  ?  311 THR   A CG2 1 
ATOM   2476 N  N   . THR   A 1 313 ? 37.617  -55.190 49.953 1.00 60.70  ?  312 THR   A N   1 
ATOM   2477 C  CA  . THR   A 1 313 ? 37.968  -56.356 49.155 1.00 65.36  ?  312 THR   A CA  1 
ATOM   2478 C  C   . THR   A 1 313 ? 39.067  -57.163 49.844 1.00 71.82  ?  312 THR   A C   1 
ATOM   2479 O  O   . THR   A 1 313 ? 39.804  -56.665 50.705 1.00 76.68  ?  312 THR   A O   1 
ATOM   2480 C  CB  . THR   A 1 313 ? 38.441  -55.926 47.758 1.00 66.23  ?  312 THR   A CB  1 
ATOM   2481 O  OG1 . THR   A 1 313 ? 38.167  -56.954 46.797 1.00 64.78  ?  312 THR   A OG1 1 
ATOM   2482 C  CG2 . THR   A 1 313 ? 39.935  -55.632 47.755 1.00 55.06  ?  312 THR   A CG2 1 
ATOM   2483 N  N   . THR   A 1 314 ? 39.160  -58.436 49.472 1.00 75.27  ?  313 THR   A N   1 
ATOM   2484 C  CA  . THR   A 1 314 ? 40.303  -59.255 49.852 1.00 75.00  ?  313 THR   A CA  1 
ATOM   2485 C  C   . THR   A 1 314 ? 41.287  -59.446 48.709 1.00 82.24  ?  313 THR   A C   1 
ATOM   2486 O  O   . THR   A 1 314 ? 42.376  -59.981 48.947 1.00 89.06  ?  313 THR   A O   1 
ATOM   2487 C  CB  . THR   A 1 314 ? 39.853  -60.637 50.338 1.00 78.27  ?  313 THR   A CB  1 
ATOM   2488 O  OG1 . THR   A 1 314 ? 39.432  -61.427 49.212 1.00 79.90  ?  313 THR   A OG1 1 
ATOM   2489 C  CG2 . THR   A 1 314 ? 38.716  -60.510 51.355 1.00 70.09  ?  313 THR   A CG2 1 
ATOM   2490 N  N   . ILE   A 1 315 ? 40.913  -59.044 47.483 1.00 77.48  ?  314 ILE   A N   1 
ATOM   2491 C  CA  . ILE   A 1 315 ? 41.781  -59.168 46.310 1.00 76.40  ?  314 ILE   A CA  1 
ATOM   2492 C  C   . ILE   A 1 315 ? 43.097  -58.444 46.567 1.00 80.55  ?  314 ILE   A C   1 
ATOM   2493 O  O   . ILE   A 1 315 ? 43.121  -57.237 46.843 1.00 82.12  ?  314 ILE   A O   1 
ATOM   2494 C  CB  . ILE   A 1 315 ? 41.081  -58.622 45.057 1.00 71.19  ?  314 ILE   A CB  1 
ATOM   2495 C  CG1 . ILE   A 1 315 ? 39.658  -59.185 44.950 1.00 65.13  ?  314 ILE   A CG1 1 
ATOM   2496 C  CG2 . ILE   A 1 315 ? 41.924  -58.888 43.801 1.00 68.09  ?  314 ILE   A CG2 1 
ATOM   2497 C  CD1 . ILE   A 1 315 ? 39.096  -59.145 43.568 1.00 63.93  ?  314 ILE   A CD1 1 
ATOM   2498 N  N   . LYS   A 1 316 ? 44.203  -59.180 46.479 1.00 85.92  ?  315 LYS   A N   1 
ATOM   2499 C  CA  . LYS   A 1 316 ? 45.533  -58.587 46.637 1.00 88.61  ?  315 LYS   A CA  1 
ATOM   2500 C  C   . LYS   A 1 316 ? 46.136  -58.242 45.270 1.00 86.96  ?  315 LYS   A C   1 
ATOM   2501 O  O   . LYS   A 1 316 ? 45.444  -58.279 44.236 1.00 80.27  ?  315 LYS   A O   1 
ATOM   2502 C  CB  . LYS   A 1 316 ? 46.457  -59.535 47.420 1.00 88.97  ?  315 LYS   A CB  1 
ATOM   2503 C  CG  . LYS   A 1 316 ? 45.942  -59.876 48.827 1.00 86.27  ?  315 LYS   A CG  1 
ATOM   2504 C  CD  . LYS   A 1 316 ? 46.318  -61.286 49.288 1.00 89.48  ?  315 LYS   A CD  1 
ATOM   2505 C  CE  . LYS   A 1 316 ? 45.141  -62.260 49.129 1.00 91.33  ?  315 LYS   A CE  1 
ATOM   2506 N  NZ  . LYS   A 1 316 ? 44.076  -62.110 50.188 1.00 83.21  ?  315 LYS   A NZ  1 
ATOM   2507 N  N   . VAL   B 1 8   ? 29.684  -46.012 4.212  1.00 90.37  ?  7   VAL   B N   1 
ATOM   2508 C  CA  . VAL   B 1 8   ? 30.578  -45.403 3.232  1.00 98.72  ?  7   VAL   B CA  1 
ATOM   2509 C  C   . VAL   B 1 8   ? 29.927  -44.118 2.660  1.00 97.51  ?  7   VAL   B C   1 
ATOM   2510 O  O   . VAL   B 1 8   ? 30.500  -43.461 1.786  1.00 98.02  ?  7   VAL   B O   1 
ATOM   2511 C  CB  . VAL   B 1 8   ? 30.964  -46.438 2.114  1.00 99.90  ?  7   VAL   B CB  1 
ATOM   2512 C  CG1 . VAL   B 1 8   ? 32.304  -46.105 1.452  1.00 88.00  ?  7   VAL   B CG1 1 
ATOM   2513 C  CG2 . VAL   B 1 8   ? 31.015  -47.853 2.688  1.00 99.72  ?  7   VAL   B CG2 1 
ATOM   2514 N  N   . PHE   B 1 9   ? 28.733  -43.767 3.166  1.00 98.54  ?  8   PHE   B N   1 
ATOM   2515 C  CA  . PHE   B 1 9   ? 28.045  -42.498 2.887  1.00 97.54  ?  8   PHE   B CA  1 
ATOM   2516 C  C   . PHE   B 1 9   ? 27.413  -41.939 4.163  1.00 93.20  ?  8   PHE   B C   1 
ATOM   2517 O  O   . PHE   B 1 9   ? 26.637  -42.633 4.831  1.00 88.14  ?  8   PHE   B O   1 
ATOM   2518 C  CB  . PHE   B 1 9   ? 26.917  -42.643 1.849  1.00 95.72  ?  8   PHE   B CB  1 
ATOM   2519 C  CG  . PHE   B 1 9   ? 27.368  -42.904 0.434  1.00 100.27 ?  8   PHE   B CG  1 
ATOM   2520 C  CD1 . PHE   B 1 9   ? 27.181  -41.940 -0.549 1.00 96.57  ?  8   PHE   B CD1 1 
ATOM   2521 C  CD2 . PHE   B 1 9   ? 27.901  -44.132 0.064  1.00 104.22 ?  8   PHE   B CD2 1 
ATOM   2522 C  CE1 . PHE   B 1 9   ? 27.550  -42.186 -1.870 1.00 94.57  ?  8   PHE   B CE1 1 
ATOM   2523 C  CE2 . PHE   B 1 9   ? 28.281  -44.377 -1.254 1.00 100.89 ?  8   PHE   B CE2 1 
ATOM   2524 C  CZ  . PHE   B 1 9   ? 28.105  -43.400 -2.219 1.00 90.71  ?  8   PHE   B CZ  1 
ATOM   2525 N  N   . THR   B 1 10  ? 27.692  -40.673 4.469  1.00 91.64  ?  9   THR   B N   1 
ATOM   2526 C  CA  . THR   B 1 10  ? 27.095  -39.984 5.607  1.00 81.31  ?  9   THR   B CA  1 
ATOM   2527 C  C   . THR   B 1 10  ? 26.156  -38.872 5.150  1.00 79.65  ?  9   THR   B C   1 
ATOM   2528 O  O   . THR   B 1 10  ? 26.272  -38.343 4.038  1.00 80.36  ?  9   THR   B O   1 
ATOM   2529 C  CB  . THR   B 1 10  ? 28.174  -39.399 6.515  1.00 77.57  ?  9   THR   B CB  1 
ATOM   2530 O  OG1 . THR   B 1 10  ? 28.798  -38.292 5.862  1.00 81.21  ?  9   THR   B OG1 1 
ATOM   2531 C  CG2 . THR   B 1 10  ? 29.198  -40.423 6.798  1.00 81.53  ?  9   THR   B CG2 1 
ATOM   2532 N  N   . THR   B 1 11  ? 25.222  -38.505 6.032  1.00 77.14  ?  10  THR   B N   1 
ATOM   2533 C  CA  . THR   B 1 11  ? 24.261  -37.467 5.678  1.00 73.40  ?  10  THR   B CA  1 
ATOM   2534 C  C   . THR   B 1 11  ? 23.678  -36.818 6.928  1.00 70.07  ?  10  THR   B C   1 
ATOM   2535 O  O   . THR   B 1 11  ? 23.726  -37.379 8.030  1.00 69.08  ?  10  THR   B O   1 
ATOM   2536 C  CB  . THR   B 1 11  ? 23.135  -38.025 4.806  1.00 68.98  ?  10  THR   B CB  1 
ATOM   2537 O  OG1 . THR   B 1 11  ? 22.635  -36.974 3.976  1.00 74.39  ?  10  THR   B OG1 1 
ATOM   2538 C  CG2 . THR   B 1 11  ? 22.000  -38.562 5.668  1.00 64.12  ?  10  THR   B CG2 1 
ATOM   2539 N  N   . VAL   B 1 12  ? 23.139  -35.614 6.738  1.00 65.42  ?  11  VAL   B N   1 
ATOM   2540 C  CA  . VAL   B 1 12  ? 22.220  -35.018 7.700  1.00 61.56  ?  11  VAL   B CA  1 
ATOM   2541 C  C   . VAL   B 1 12  ? 20.828  -34.805 7.124  1.00 59.86  ?  11  VAL   B C   1 
ATOM   2542 O  O   . VAL   B 1 12  ? 19.891  -34.537 7.893  1.00 62.61  ?  11  VAL   B O   1 
ATOM   2543 C  CB  . VAL   B 1 12  ? 22.765  -33.690 8.278  1.00 60.07  ?  11  VAL   B CB  1 
ATOM   2544 C  CG1 . VAL   B 1 12  ? 23.863  -33.974 9.291  1.00 64.87  ?  11  VAL   B CG1 1 
ATOM   2545 C  CG2 . VAL   B 1 12  ? 23.247  -32.740 7.200  1.00 60.76  ?  11  VAL   B CG2 1 
ATOM   2546 N  N   . ASP   B 1 13  ? 20.648  -34.959 5.807  1.00 66.81  ?  12  ASP   B N   1 
ATOM   2547 C  CA  . ASP   B 1 13  ? 19.369  -34.719 5.142  1.00 69.93  ?  12  ASP   B CA  1 
ATOM   2548 C  C   . ASP   B 1 13  ? 18.912  -35.828 4.197  1.00 71.45  ?  12  ASP   B C   1 
ATOM   2549 O  O   . ASP   B 1 13  ? 17.791  -35.737 3.686  1.00 74.63  ?  12  ASP   B O   1 
ATOM   2550 C  CB  . ASP   B 1 13  ? 19.403  -33.397 4.341  1.00 65.30  ?  12  ASP   B CB  1 
ATOM   2551 C  CG  . ASP   B 1 13  ? 20.708  -33.190 3.556  1.00 71.32  ?  12  ASP   B CG  1 
ATOM   2552 O  OD1 . ASP   B 1 13  ? 21.543  -34.129 3.475  1.00 73.56  ?  12  ASP   B OD1 1 
ATOM   2553 O  OD2 . ASP   B 1 13  ? 20.896  -32.063 3.022  1.00 68.27  -1 12  ASP   B OD2 1 
ATOM   2554 N  N   . ASN   B 1 14  ? 19.727  -36.856 3.945  1.00 68.22  ?  13  ASN   B N   1 
ATOM   2555 C  CA  . ASN   B 1 14  ? 19.416  -37.910 2.973  1.00 73.43  ?  13  ASN   B CA  1 
ATOM   2556 C  C   . ASN   B 1 14  ? 19.245  -37.347 1.564  1.00 79.28  ?  13  ASN   B C   1 
ATOM   2557 O  O   . ASN   B 1 14  ? 18.486  -37.875 0.749  1.00 75.79  ?  13  ASN   B O   1 
ATOM   2558 C  CB  . ASN   B 1 14  ? 18.175  -38.708 3.385  1.00 76.50  ?  13  ASN   B CB  1 
ATOM   2559 C  CG  . ASN   B 1 14  ? 18.098  -40.070 2.707  1.00 85.05  ?  13  ASN   B CG  1 
ATOM   2560 O  OD1 . ASN   B 1 14  ? 18.834  -40.341 1.752  1.00 81.45  ?  13  ASN   B OD1 1 
ATOM   2561 N  ND2 . ASN   B 1 14  ? 17.231  -40.947 3.219  1.00 82.12  ?  13  ASN   B ND2 1 
ATOM   2562 N  N   . ILE   B 1 15  ? 19.959  -36.270 1.266  1.00 75.76  ?  14  ILE   B N   1 
ATOM   2563 C  CA  . ILE   B 1 15  ? 19.791  -35.552 0.014  1.00 68.87  ?  14  ILE   B CA  1 
ATOM   2564 C  C   . ILE   B 1 15  ? 21.175  -35.192 -0.491 1.00 71.85  ?  14  ILE   B C   1 
ATOM   2565 O  O   . ILE   B 1 15  ? 21.465  -35.321 -1.686 1.00 75.49  ?  14  ILE   B O   1 
ATOM   2566 C  CB  . ILE   B 1 15  ? 18.916  -34.300 0.220  1.00 71.49  ?  14  ILE   B CB  1 
ATOM   2567 C  CG1 . ILE   B 1 15  ? 17.503  -34.708 0.684  1.00 73.04  ?  14  ILE   B CG1 1 
ATOM   2568 C  CG2 . ILE   B 1 15  ? 18.953  -33.403 -1.019 1.00 63.33  ?  14  ILE   B CG2 1 
ATOM   2569 C  CD1 . ILE   B 1 15  ? 16.468  -33.583 0.717  1.00 72.16  ?  14  ILE   B CD1 1 
ATOM   2570 N  N   . ASN   B 1 16  ? 22.031  -34.735 0.427  1.00 73.41  ?  15  ASN   B N   1 
ATOM   2571 C  CA  . ASN   B 1 16  ? 23.427  -34.391 0.156  1.00 72.52  ?  15  ASN   B CA  1 
ATOM   2572 C  C   . ASN   B 1 16  ? 24.294  -35.393 0.912  1.00 69.98  ?  15  ASN   B C   1 
ATOM   2573 O  O   . ASN   B 1 16  ? 24.611  -35.204 2.086  1.00 78.39  ?  15  ASN   B O   1 
ATOM   2574 C  CB  . ASN   B 1 16  ? 23.732  -32.945 0.554  1.00 66.65  ?  15  ASN   B CB  1 
ATOM   2575 C  CG  . ASN   B 1 16  ? 23.830  -32.032 -0.642 1.00 74.83  ?  15  ASN   B CG  1 
ATOM   2576 O  OD1 . ASN   B 1 16  ? 24.684  -32.218 -1.513 1.00 75.54  ?  15  ASN   B OD1 1 
ATOM   2577 N  ND2 . ASN   B 1 16  ? 22.938  -31.055 -0.711 1.00 74.72  ?  15  ASN   B ND2 1 
ATOM   2578 N  N   . LEU   B 1 17  ? 24.655  -36.479 0.240  1.00 77.12  ?  16  LEU   B N   1 
ATOM   2579 C  CA  . LEU   B 1 17  ? 25.501  -37.501 0.839  1.00 81.92  ?  16  LEU   B CA  1 
ATOM   2580 C  C   . LEU   B 1 17  ? 26.963  -37.123 0.656  1.00 82.17  ?  16  LEU   B C   1 
ATOM   2581 O  O   . LEU   B 1 17  ? 27.409  -36.861 -0.463 1.00 78.69  ?  16  LEU   B O   1 
ATOM   2582 C  CB  . LEU   B 1 17  ? 25.231  -38.870 0.225  1.00 74.69  ?  16  LEU   B CB  1 
ATOM   2583 C  CG  . LEU   B 1 17  ? 23.805  -39.088 -0.267 1.00 71.41  ?  16  LEU   B CG  1 
ATOM   2584 C  CD1 . LEU   B 1 17  ? 23.762  -40.363 -1.070 1.00 75.82  ?  16  LEU   B CD1 1 
ATOM   2585 C  CD2 . LEU   B 1 17  ? 22.815  -39.129 0.895  1.00 75.88  ?  16  LEU   B CD2 1 
ATOM   2586 N  N   . HIS   B 1 18  ? 27.666  -37.026 1.791  1.00 77.06  ?  17  HIS   B N   1 
ATOM   2587 C  CA  . HIS   B 1 18  ? 29.129  -36.778 1.763  1.00 80.31  ?  17  HIS   B CA  1 
ATOM   2588 C  C   . HIS   B 1 18  ? 29.741  -38.148 2.036  1.00 84.75  ?  17  HIS   B C   1 
ATOM   2589 O  O   . HIS   B 1 18  ? 29.530  -38.692 3.143  1.00 89.24  ?  17  HIS   B O   1 
ATOM   2590 C  CB  . HIS   B 1 18  ? 29.525  -35.718 2.793  1.00 81.80  ?  17  HIS   B CB  1 
ATOM   2591 C  CG  . HIS   B 1 18  ? 28.750  -34.447 2.688  1.00 85.76  ?  17  HIS   B CG  1 
ATOM   2592 N  ND1 . HIS   B 1 18  ? 28.688  -33.538 3.722  1.00 82.99  ?  17  HIS   B ND1 1 
ATOM   2593 C  CD2 . HIS   B 1 18  ? 28.018  -33.925 1.693  1.00 89.46  ?  17  HIS   B CD2 1 
ATOM   2594 C  CE1 . HIS   B 1 18  ? 27.940  -32.509 3.354  1.00 68.33  ?  17  HIS   B CE1 1 
ATOM   2595 N  NE2 . HIS   B 1 18  ? 27.521  -32.724 2.126  1.00 69.03  ?  17  HIS   B NE2 1 
ATOM   2596 N  N   . THR   B 1 19  ? 30.463  -38.702 1.066  1.00 91.34  ?  18  THR   B N   1 
ATOM   2597 C  CA  . THR   B 1 19  ? 30.932  -40.083 1.211  1.00 98.81  ?  18  THR   B CA  1 
ATOM   2598 C  C   . THR   B 1 19  ? 32.155  -40.151 2.119  1.00 93.96  ?  18  THR   B C   1 
ATOM   2599 O  O   . THR   B 1 19  ? 32.926  -39.193 2.234  1.00 90.12  ?  18  THR   B O   1 
ATOM   2600 C  CB  . THR   B 1 19  ? 31.289  -40.719 -0.146 1.00 97.31  ?  18  THR   B CB  1 
ATOM   2601 O  OG1 . THR   B 1 19  ? 32.540  -40.204 -0.629 1.00 83.56  ?  18  THR   B OG1 1 
ATOM   2602 C  CG2 . THR   B 1 19  ? 30.222  -40.417 -1.175 1.00 93.48  ?  18  THR   B CG2 1 
ATOM   2603 N  N   . GLN   B 1 20  ? 32.339  -41.310 2.755  1.00 91.15  ?  19  GLN   B N   1 
ATOM   2604 C  CA  . GLN   B 1 20  ? 33.385  -41.489 3.750  1.00 99.61  ?  19  GLN   B CA  1 
ATOM   2605 C  C   . GLN   B 1 20  ? 33.972  -42.892 3.639  1.00 105.54 ?  19  GLN   B C   1 
ATOM   2606 O  O   . GLN   B 1 20  ? 33.406  -43.780 2.997  1.00 103.02 ?  19  GLN   B O   1 
ATOM   2607 C  CB  . GLN   B 1 20  ? 32.849  -41.244 5.170  1.00 94.79  ?  19  GLN   B CB  1 
ATOM   2608 C  CG  . GLN   B 1 20  ? 32.409  -39.810 5.454  1.00 84.42  ?  19  GLN   B CG  1 
ATOM   2609 C  CD  . GLN   B 1 20  ? 33.545  -38.826 5.344  1.00 87.11  ?  19  GLN   B CD  1 
ATOM   2610 O  OE1 . GLN   B 1 20  ? 34.614  -39.032 5.923  1.00 91.20  ?  19  GLN   B OE1 1 
ATOM   2611 N  NE2 . GLN   B 1 20  ? 33.320  -37.736 4.614  1.00 87.03  ?  19  GLN   B NE2 1 
ATOM   2612 N  N   . VAL   B 1 21  ? 35.121  -43.087 4.287  1.00 114.21 ?  20  VAL   B N   1 
ATOM   2613 C  CA  . VAL   B 1 21  ? 35.803  -44.376 4.342  1.00 122.65 ?  20  VAL   B CA  1 
ATOM   2614 C  C   . VAL   B 1 21  ? 35.686  -44.936 5.756  1.00 125.06 ?  20  VAL   B C   1 
ATOM   2615 O  O   . VAL   B 1 21  ? 35.741  -44.190 6.742  1.00 121.97 ?  20  VAL   B O   1 
ATOM   2616 C  CB  . VAL   B 1 21  ? 37.278  -44.244 3.913  1.00 125.65 ?  20  VAL   B CB  1 
ATOM   2617 C  CG1 . VAL   B 1 21  ? 37.361  -43.741 2.482  1.00 121.62 ?  20  VAL   B CG1 1 
ATOM   2618 C  CG2 . VAL   B 1 21  ? 38.030  -43.311 4.852  1.00 138.56 ?  20  VAL   B CG2 1 
ATOM   2619 N  N   . VAL   B 1 22  ? 35.517  -46.251 5.857  1.00 125.41 ?  21  VAL   B N   1 
ATOM   2620 C  CA  . VAL   B 1 22  ? 35.207  -46.894 7.126  1.00 121.50 ?  21  VAL   B CA  1 
ATOM   2621 C  C   . VAL   B 1 22  ? 36.293  -47.915 7.443  1.00 123.96 ?  21  VAL   B C   1 
ATOM   2622 O  O   . VAL   B 1 22  ? 36.598  -48.786 6.619  1.00 123.28 ?  21  VAL   B O   1 
ATOM   2623 C  CB  . VAL   B 1 22  ? 33.810  -47.542 7.097  1.00 122.46 ?  21  VAL   B CB  1 
ATOM   2624 C  CG1 . VAL   B 1 22  ? 33.649  -48.481 5.884  1.00 120.40 ?  21  VAL   B CG1 1 
ATOM   2625 C  CG2 . VAL   B 1 22  ? 33.526  -48.236 8.402  1.00 111.89 ?  21  VAL   B CG2 1 
ATOM   2626 N  N   . ASP   B 1 23  ? 36.872  -47.805 8.644  1.00 124.31 ?  22  ASP   B N   1 
ATOM   2627 C  CA  . ASP   B 1 23  ? 37.995  -48.654 9.034  1.00 125.72 ?  22  ASP   B CA  1 
ATOM   2628 C  C   . ASP   B 1 23  ? 37.627  -50.127 9.152  1.00 131.72 ?  22  ASP   B C   1 
ATOM   2629 O  O   . ASP   B 1 23  ? 38.530  -50.971 9.193  1.00 133.75 ?  22  ASP   B O   1 
ATOM   2630 C  CB  . ASP   B 1 23  ? 38.582  -48.191 10.367 1.00 121.41 ?  22  ASP   B CB  1 
ATOM   2631 C  CG  . ASP   B 1 23  ? 39.962  -48.768 10.624 1.00 121.83 ?  22  ASP   B CG  1 
ATOM   2632 O  OD1 . ASP   B 1 23  ? 40.797  -48.760 9.696  1.00 128.73 ?  22  ASP   B OD1 1 
ATOM   2633 O  OD2 . ASP   B 1 23  ? 40.206  -49.255 11.746 1.00 118.96 ?  22  ASP   B OD2 1 
ATOM   2634 N  N   . MET   B 1 24  ? 36.336  -50.452 9.244  1.00 129.70 ?  23  MET   B N   1 
ATOM   2635 C  CA  . MET   B 1 24  ? 35.871  -51.825 9.428  1.00 127.42 ?  23  MET   B CA  1 
ATOM   2636 C  C   . MET   B 1 24  ? 36.307  -52.383 10.788 1.00 123.03 ?  23  MET   B C   1 
ATOM   2637 O  O   . MET   B 1 24  ? 35.940  -53.505 11.152 1.00 121.25 ?  23  MET   B O   1 
ATOM   2638 C  CB  . MET   B 1 24  ? 36.338  -52.711 8.260  1.00 133.13 ?  23  MET   B CB  1 
ATOM   2639 C  CG  . MET   B 1 24  ? 35.750  -54.104 8.253  1.00 148.33 ?  23  MET   B CG  1 
ATOM   2640 S  SD  . MET   B 1 24  ? 34.407  -54.334 7.092  1.00 213.38 ?  23  MET   B SD  1 
ATOM   2641 C  CE  . MET   B 1 24  ? 33.731  -55.866 7.716  1.00 129.91 ?  23  MET   B CE  1 
ATOM   2642 N  N   . SER   B 1 25  ? 37.039  -51.590 11.579 1.00 119.36 ?  24  SER   B N   1 
ATOM   2643 C  CA  . SER   B 1 25  ? 37.540  -52.044 12.869 1.00 116.80 ?  24  SER   B CA  1 
ATOM   2644 C  C   . SER   B 1 25  ? 37.351  -51.056 14.014 1.00 117.26 ?  24  SER   B C   1 
ATOM   2645 O  O   . SER   B 1 25  ? 37.654  -51.416 15.159 1.00 113.59 ?  24  SER   B O   1 
ATOM   2646 C  CB  . SER   B 1 25  ? 39.033  -52.393 12.777 1.00 120.61 ?  24  SER   B CB  1 
ATOM   2647 O  OG  . SER   B 1 25  ? 39.711  -51.505 11.908 1.00 118.17 ?  24  SER   B OG  1 
ATOM   2648 N  N   . MET   B 1 26  ? 36.895  -49.830 13.756 1.00 112.55 ?  25  MET   B N   1 
ATOM   2649 C  CA  . MET   B 1 26  ? 36.468  -48.924 14.813 1.00 108.66 ?  25  MET   B CA  1 
ATOM   2650 C  C   . MET   B 1 26  ? 34.965  -48.701 14.717 1.00 108.43 ?  25  MET   B C   1 
ATOM   2651 O  O   . MET   B 1 26  ? 34.414  -48.640 13.614 1.00 108.06 ?  25  MET   B O   1 
ATOM   2652 C  CB  . MET   B 1 26  ? 37.191  -47.571 14.758 1.00 101.16 ?  25  MET   B CB  1 
ATOM   2653 C  CG  . MET   B 1 26  ? 38.696  -47.657 14.711 1.00 105.24 ?  25  MET   B CG  1 
ATOM   2654 S  SD  . MET   B 1 26  ? 39.454  -46.340 13.739 1.00 113.22 ?  25  MET   B SD  1 
ATOM   2655 C  CE  . MET   B 1 26  ? 39.479  -44.986 14.921 1.00 76.85  ?  25  MET   B CE  1 
ATOM   2656 N  N   . THR   B 1 27  ? 34.310  -48.586 15.877 1.00 104.05 ?  26  THR   B N   1 
ATOM   2657 C  CA  . THR   B 1 27  ? 32.877  -48.317 15.923 1.00 100.59 ?  26  THR   B CA  1 
ATOM   2658 C  C   . THR   B 1 27  ? 32.558  -47.007 15.217 1.00 95.03  ?  26  THR   B C   1 
ATOM   2659 O  O   . THR   B 1 27  ? 33.373  -46.078 15.194 1.00 97.13  ?  26  THR   B O   1 
ATOM   2660 C  CB  . THR   B 1 27  ? 32.378  -48.249 17.375 1.00 98.36  ?  26  THR   B CB  1 
ATOM   2661 O  OG1 . THR   B 1 27  ? 32.567  -46.926 17.906 1.00 90.63  ?  26  THR   B OG1 1 
ATOM   2662 C  CG2 . THR   B 1 27  ? 33.105  -49.252 18.253 1.00 99.36  ?  26  THR   B CG2 1 
ATOM   2663 N  N   . TYR   B 1 28  ? 31.350  -46.934 14.646 1.00 90.31  ?  27  TYR   B N   1 
ATOM   2664 C  CA  . TYR   B 1 28  ? 30.918  -45.706 13.976 1.00 85.81  ?  27  TYR   B CA  1 
ATOM   2665 C  C   . TYR   B 1 28  ? 31.064  -44.489 14.877 1.00 85.27  ?  27  TYR   B C   1 
ATOM   2666 O  O   . TYR   B 1 28  ? 31.522  -43.432 14.430 1.00 82.98  ?  27  TYR   B O   1 
ATOM   2667 C  CB  . TYR   B 1 28  ? 29.474  -45.834 13.509 1.00 77.56  ?  27  TYR   B CB  1 
ATOM   2668 C  CG  . TYR   B 1 28  ? 29.324  -46.785 12.371 1.00 74.86  ?  27  TYR   B CG  1 
ATOM   2669 C  CD1 . TYR   B 1 28  ? 28.875  -48.076 12.578 1.00 84.25  ?  27  TYR   B CD1 1 
ATOM   2670 C  CD2 . TYR   B 1 28  ? 29.651  -46.400 11.085 1.00 84.84  ?  27  TYR   B CD2 1 
ATOM   2671 C  CE1 . TYR   B 1 28  ? 28.739  -48.958 11.525 1.00 92.27  ?  27  TYR   B CE1 1 
ATOM   2672 C  CE2 . TYR   B 1 28  ? 29.524  -47.270 10.025 1.00 87.68  ?  27  TYR   B CE2 1 
ATOM   2673 C  CZ  . TYR   B 1 28  ? 29.067  -48.545 10.250 1.00 90.51  ?  27  TYR   B CZ  1 
ATOM   2674 O  OH  . TYR   B 1 28  ? 28.944  -49.407 9.192  1.00 95.98  ?  27  TYR   B OH  1 
ATOM   2675 N  N   . GLY   B 1 29  ? 30.691  -44.622 16.153 1.00 88.02  ?  28  GLY   B N   1 
ATOM   2676 C  CA  . GLY   B 1 29  ? 30.835  -43.534 17.105 1.00 83.41  ?  28  GLY   B CA  1 
ATOM   2677 C  C   . GLY   B 1 29  ? 32.238  -42.985 17.210 1.00 82.57  ?  28  GLY   B C   1 
ATOM   2678 O  O   . GLY   B 1 29  ? 32.410  -41.807 17.538 1.00 83.29  ?  28  GLY   B O   1 
ATOM   2679 N  N   . GLN   B 1 30  ? 33.250  -43.805 16.934 1.00 85.00  ?  29  GLN   B N   1 
ATOM   2680 C  CA  . GLN   B 1 30  ? 34.618  -43.305 16.988 1.00 91.43  ?  29  GLN   B CA  1 
ATOM   2681 C  C   . GLN   B 1 30  ? 34.913  -42.381 15.817 1.00 93.11  ?  29  GLN   B C   1 
ATOM   2682 O  O   . GLN   B 1 30  ? 35.564  -41.341 15.984 1.00 90.80  ?  29  GLN   B O   1 
ATOM   2683 C  CB  . GLN   B 1 30  ? 35.604  -44.468 17.000 1.00 93.93  ?  29  GLN   B CB  1 
ATOM   2684 C  CG  . GLN   B 1 30  ? 35.393  -45.449 18.123 1.00 97.12  ?  29  GLN   B CG  1 
ATOM   2685 C  CD  . GLN   B 1 30  ? 36.667  -46.179 18.459 1.00 100.14 ?  29  GLN   B CD  1 
ATOM   2686 O  OE1 . GLN   B 1 30  ? 37.001  -47.190 17.840 1.00 100.44 ?  29  GLN   B OE1 1 
ATOM   2687 N  NE2 . GLN   B 1 30  ? 37.409  -45.650 19.429 1.00 96.08  ?  29  GLN   B NE2 1 
ATOM   2688 N  N   . GLN   B 1 31  ? 34.424  -42.739 14.629 1.00 92.68  ?  30  GLN   B N   1 
ATOM   2689 C  CA  . GLN   B 1 31  ? 34.772  -42.057 13.391 1.00 88.46  ?  30  GLN   B CA  1 
ATOM   2690 C  C   . GLN   B 1 31  ? 33.778  -40.945 13.038 1.00 84.11  ?  30  GLN   B C   1 
ATOM   2691 O  O   . GLN   B 1 31  ? 34.186  -39.806 12.800 1.00 81.07  ?  30  GLN   B O   1 
ATOM   2692 C  CB  . GLN   B 1 31  ? 34.902  -43.104 12.271 1.00 85.08  ?  30  GLN   B CB  1 
ATOM   2693 C  CG  . GLN   B 1 31  ? 35.841  -44.271 12.659 1.00 89.67  ?  30  GLN   B CG  1 
ATOM   2694 C  CD  . GLN   B 1 31  ? 36.043  -45.314 11.560 1.00 100.42 ?  30  GLN   B CD  1 
ATOM   2695 O  OE1 . GLN   B 1 31  ? 36.952  -45.192 10.739 1.00 104.13 ?  30  GLN   B OE1 1 
ATOM   2696 N  NE2 . GLN   B 1 31  ? 35.229  -46.367 11.574 1.00 97.30  ?  30  GLN   B NE2 1 
ATOM   2697 N  N   . PHE   B 1 32  ? 32.473  -41.238 13.043 1.00 89.00  ?  31  PHE   B N   1 
ATOM   2698 C  CA  . PHE   B 1 32  ? 31.465  -40.279 12.593 1.00 77.64  ?  31  PHE   B CA  1 
ATOM   2699 C  C   . PHE   B 1 32  ? 30.871  -39.428 13.707 1.00 78.78  ?  31  PHE   B C   1 
ATOM   2700 O  O   . PHE   B 1 32  ? 30.351  -38.343 13.425 1.00 81.08  ?  31  PHE   B O   1 
ATOM   2701 C  CB  . PHE   B 1 32  ? 30.316  -41.003 11.903 1.00 68.53  ?  31  PHE   B CB  1 
ATOM   2702 C  CG  . PHE   B 1 32  ? 30.667  -41.551 10.565 1.00 78.82  ?  31  PHE   B CG  1 
ATOM   2703 C  CD1 . PHE   B 1 32  ? 29.870  -42.520 9.974  1.00 82.90  ?  31  PHE   B CD1 1 
ATOM   2704 C  CD2 . PHE   B 1 32  ? 31.785  -41.098 9.890  1.00 78.30  ?  31  PHE   B CD2 1 
ATOM   2705 C  CE1 . PHE   B 1 32  ? 30.182  -43.029 8.735  1.00 89.22  ?  31  PHE   B CE1 1 
ATOM   2706 C  CE2 . PHE   B 1 32  ? 32.103  -41.595 8.648  1.00 84.84  ?  31  PHE   B CE2 1 
ATOM   2707 C  CZ  . PHE   B 1 32  ? 31.308  -42.571 8.070  1.00 93.39  ?  31  PHE   B CZ  1 
ATOM   2708 N  N   . GLY   B 1 33  ? 30.926  -39.884 14.953 1.00 79.45  ?  32  GLY   B N   1 
ATOM   2709 C  CA  . GLY   B 1 33  ? 30.113  -39.316 16.005 1.00 75.40  ?  32  GLY   B CA  1 
ATOM   2710 C  C   . GLY   B 1 33  ? 28.860  -40.150 16.197 1.00 74.55  ?  32  GLY   B C   1 
ATOM   2711 O  O   . GLY   B 1 33  ? 28.746  -41.258 15.662 1.00 76.60  ?  32  GLY   B O   1 
ATOM   2712 N  N   . PRO   B 1 34  ? 27.902  -39.651 16.975 1.00 75.59  ?  33  PRO   B N   1 
ATOM   2713 C  CA  . PRO   B 1 34  ? 26.607  -40.343 17.081 1.00 68.48  ?  33  PRO   B CA  1 
ATOM   2714 C  C   . PRO   B 1 34  ? 25.967  -40.564 15.718 1.00 65.53  ?  33  PRO   B C   1 
ATOM   2715 O  O   . PRO   B 1 34  ? 25.613  -39.597 15.041 1.00 71.25  ?  33  PRO   B O   1 
ATOM   2716 C  CB  . PRO   B 1 34  ? 25.781  -39.390 17.950 1.00 62.99  ?  33  PRO   B CB  1 
ATOM   2717 C  CG  . PRO   B 1 34  ? 26.802  -38.706 18.793 1.00 63.08  ?  33  PRO   B CG  1 
ATOM   2718 C  CD  . PRO   B 1 34  ? 27.987  -38.500 17.891 1.00 74.25  ?  33  PRO   B CD  1 
ATOM   2719 N  N   . THR   B 1 35  ? 25.818  -41.825 15.309 1.00 67.18  ?  34  THR   B N   1 
ATOM   2720 C  CA  . THR   B 1 35  ? 25.455  -42.202 13.945 1.00 69.71  ?  34  THR   B CA  1 
ATOM   2721 C  C   . THR   B 1 35  ? 24.215  -43.084 13.949 1.00 70.92  ?  34  THR   B C   1 
ATOM   2722 O  O   . THR   B 1 35  ? 24.061  -43.940 14.824 1.00 75.33  ?  34  THR   B O   1 
ATOM   2723 C  CB  . THR   B 1 35  ? 26.597  -42.961 13.265 1.00 69.82  ?  34  THR   B CB  1 
ATOM   2724 O  OG1 . THR   B 1 35  ? 27.827  -42.288 13.526 1.00 76.09  ?  34  THR   B OG1 1 
ATOM   2725 C  CG2 . THR   B 1 35  ? 26.384  -43.054 11.768 1.00 69.94  ?  34  THR   B CG2 1 
ATOM   2726 N  N   . TYR   B 1 36  ? 23.342  -42.901 12.958 1.00 69.71  ?  35  TYR   B N   1 
ATOM   2727 C  CA  . TYR   B 1 36  ? 22.092  -43.644 12.906 1.00 70.00  ?  35  TYR   B CA  1 
ATOM   2728 C  C   . TYR   B 1 36  ? 21.961  -44.402 11.590 1.00 76.87  ?  35  TYR   B C   1 
ATOM   2729 O  O   . TYR   B 1 36  ? 22.414  -43.942 10.537 1.00 77.70  ?  35  TYR   B O   1 
ATOM   2730 C  CB  . TYR   B 1 36  ? 20.904  -42.709 13.114 1.00 61.93  ?  35  TYR   B CB  1 
ATOM   2731 C  CG  . TYR   B 1 36  ? 20.910  -42.084 14.479 1.00 62.14  ?  35  TYR   B CG  1 
ATOM   2732 C  CD1 . TYR   B 1 36  ? 20.362  -42.742 15.575 1.00 71.21  ?  35  TYR   B CD1 1 
ATOM   2733 C  CD2 . TYR   B 1 36  ? 21.526  -40.858 14.694 1.00 57.53  ?  35  TYR   B CD2 1 
ATOM   2734 C  CE1 . TYR   B 1 36  ? 20.397  -42.169 16.849 1.00 64.44  ?  35  TYR   B CE1 1 
ATOM   2735 C  CE2 . TYR   B 1 36  ? 21.574  -40.289 15.943 1.00 58.57  ?  35  TYR   B CE2 1 
ATOM   2736 C  CZ  . TYR   B 1 36  ? 21.002  -40.951 17.017 1.00 61.93  ?  35  TYR   B CZ  1 
ATOM   2737 O  OH  . TYR   B 1 36  ? 21.034  -40.387 18.262 1.00 67.97  ?  35  TYR   B OH  1 
ATOM   2738 N  N   . LEU   B 1 37  ? 21.409  -45.613 11.687 1.00 77.31  ?  36  LEU   B N   1 
ATOM   2739 C  CA  . LEU   B 1 37  ? 20.894  -46.379 10.554 1.00 82.86  ?  36  LEU   B CA  1 
ATOM   2740 C  C   . LEU   B 1 37  ? 19.438  -46.730 10.789 1.00 87.35  ?  36  LEU   B C   1 
ATOM   2741 O  O   . LEU   B 1 37  ? 19.130  -47.610 11.599 1.00 84.35  ?  36  LEU   B O   1 
ATOM   2742 C  CB  . LEU   B 1 37  ? 21.736  -47.621 10.259 1.00 81.53  ?  36  LEU   B CB  1 
ATOM   2743 C  CG  . LEU   B 1 37  ? 21.424  -48.211 8.859  1.00 87.76  ?  36  LEU   B CG  1 
ATOM   2744 C  CD1 . LEU   B 1 37  ? 21.678  -47.351 7.634  1.00 84.71  ?  36  LEU   B CD1 1 
ATOM   2745 C  CD2 . LEU   B 1 37  ? 22.288  -49.485 8.750  1.00 89.65  ?  36  LEU   B CD2 1 
ATOM   2746 N  N   . ASP   B 1 38  ? 18.564  -46.043 10.045 1.00 87.42  ?  37  ASP   B N   1 
ATOM   2747 C  CA  . ASP   B 1 38  ? 17.121  -46.220 10.018 1.00 76.37  ?  37  ASP   B CA  1 
ATOM   2748 C  C   . ASP   B 1 38  ? 16.460  -45.899 11.347 1.00 84.33  ?  37  ASP   B C   1 
ATOM   2749 O  O   . ASP   B 1 38  ? 15.291  -46.256 11.544 1.00 87.75  ?  37  ASP   B O   1 
ATOM   2750 C  CB  . ASP   B 1 38  ? 16.761  -47.638 9.587  1.00 76.80  ?  37  ASP   B CB  1 
ATOM   2751 C  CG  . ASP   B 1 38  ? 17.384  -48.002 8.259  1.00 94.03  ?  37  ASP   B CG  1 
ATOM   2752 O  OD1 . ASP   B 1 38  ? 16.883  -48.949 7.609  1.00 103.06 -1 37  ASP   B OD1 1 
ATOM   2753 O  OD2 . ASP   B 1 38  ? 18.377  -47.341 7.867  1.00 91.19  ?  37  ASP   B OD2 1 
ATOM   2754 N  N   . GLY   B 1 39  ? 17.156  -45.208 12.251 1.00 75.70  ?  38  GLY   B N   1 
ATOM   2755 C  CA  . GLY   B 1 39  ? 16.695  -45.006 13.610 1.00 76.82  ?  38  GLY   B CA  1 
ATOM   2756 C  C   . GLY   B 1 39  ? 17.469  -45.815 14.623 1.00 82.68  ?  38  GLY   B C   1 
ATOM   2757 O  O   . GLY   B 1 39  ? 17.365  -45.549 15.834 1.00 77.83  ?  38  GLY   B O   1 
ATOM   2758 N  N   . ALA   B 1 40  ? 18.248  -46.794 14.157 1.00 86.82  ?  39  ALA   B N   1 
ATOM   2759 C  CA  . ALA   B 1 40  ? 19.090  -47.617 15.017 1.00 87.53  ?  39  ALA   B CA  1 
ATOM   2760 C  C   . ALA   B 1 40  ? 20.363  -46.854 15.363 1.00 80.31  ?  39  ALA   B C   1 
ATOM   2761 O  O   . ALA   B 1 40  ? 21.113  -46.440 14.468 1.00 78.96  ?  39  ALA   B O   1 
ATOM   2762 C  CB  . ALA   B 1 40  ? 19.421  -48.936 14.319 1.00 75.88  ?  39  ALA   B CB  1 
ATOM   2763 N  N   . ASP   B 1 41  ? 20.635  -46.696 16.662 1.00 69.08  ?  40  ASP   B N   1 
ATOM   2764 C  CA  . ASP   B 1 41  ? 21.879  -45.999 17.097 1.00 73.27  ?  40  ASP   B CA  1 
ATOM   2765 C  C   . ASP   B 1 41  ? 23.087  -46.912 16.861 1.00 82.56  ?  40  ASP   B C   1 
ATOM   2766 O  O   . ASP   B 1 41  ? 23.403  -47.720 17.760 1.00 85.74  ?  40  ASP   B O   1 
ATOM   2767 C  CB  . ASP   B 1 41  ? 21.784  -45.506 18.532 1.00 67.09  ?  40  ASP   B CB  1 
ATOM   2768 C  CG  . ASP   B 1 41  ? 22.523  -44.205 18.809 1.00 76.82  ?  40  ASP   B CG  1 
ATOM   2769 O  OD1 . ASP   B 1 41  ? 23.090  -43.639 17.851 1.00 70.34  -1 40  ASP   B OD1 1 
ATOM   2770 O  OD2 . ASP   B 1 41  ? 22.525  -43.769 19.978 1.00 79.20  ?  40  ASP   B OD2 1 
ATOM   2771 N  N   . VAL   B 1 42  ? 23.739  -46.780 15.704 1.00 76.11  ?  41  VAL   B N   1 
ATOM   2772 C  CA  . VAL   B 1 42  ? 24.895  -47.603 15.362 1.00 75.75  ?  41  VAL   B CA  1 
ATOM   2773 C  C   . VAL   B 1 42  ? 26.192  -47.002 15.901 1.00 75.04  ?  41  VAL   B C   1 
ATOM   2774 O  O   . VAL   B 1 42  ? 27.276  -47.359 15.446 1.00 79.45  ?  41  VAL   B O   1 
ATOM   2775 C  CB  . VAL   B 1 42  ? 24.987  -47.847 13.849 1.00 83.40  ?  41  VAL   B CB  1 
ATOM   2776 C  CG1 . VAL   B 1 42  ? 23.681  -48.402 13.330 1.00 83.07  ?  41  VAL   B CG1 1 
ATOM   2777 C  CG2 . VAL   B 1 42  ? 25.378  -46.570 13.089 1.00 78.15  ?  41  VAL   B CG2 1 
ATOM   2778 N  N   . THR   B 1 43  ? 26.087  -46.100 16.874 1.00 71.42  ?  42  THR   B N   1 
ATOM   2779 C  CA  . THR   B 1 43  ? 27.263  -45.471 17.467 1.00 80.07  ?  42  THR   B CA  1 
ATOM   2780 C  C   . THR   B 1 43  ? 28.204  -46.484 18.104 1.00 85.20  ?  42  THR   B C   1 
ATOM   2781 O  O   . THR   B 1 43  ? 29.419  -46.444 17.877 1.00 89.51  ?  42  THR   B O   1 
ATOM   2782 C  CB  . THR   B 1 43  ? 26.820  -44.445 18.505 1.00 77.23  ?  42  THR   B CB  1 
ATOM   2783 O  OG1 . THR   B 1 43  ? 25.613  -43.838 18.044 1.00 75.56  ?  42  THR   B OG1 1 
ATOM   2784 C  CG2 . THR   B 1 43  ? 27.864  -43.384 18.707 1.00 73.84  ?  42  THR   B CG2 1 
ATOM   2785 N  N   . LYS   B 1 44  ? 27.664  -47.392 18.928 1.00 84.30  ?  43  LYS   B N   1 
ATOM   2786 C  CA  . LYS   B 1 44  ? 28.495  -48.323 19.680 1.00 84.73  ?  43  LYS   B CA  1 
ATOM   2787 C  C   . LYS   B 1 44  ? 28.766  -49.628 18.937 1.00 86.54  ?  43  LYS   B C   1 
ATOM   2788 O  O   . LYS   B 1 44  ? 29.544  -50.447 19.438 1.00 88.29  ?  43  LYS   B O   1 
ATOM   2789 C  CB  . LYS   B 1 44  ? 27.867  -48.612 21.058 1.00 79.14  ?  43  LYS   B CB  1 
ATOM   2790 C  CG  . LYS   B 1 44  ? 26.707  -49.624 21.042 1.00 87.99  ?  43  LYS   B CG  1 
ATOM   2791 C  CD  . LYS   B 1 44  ? 26.583  -50.432 22.344 1.00 83.75  ?  43  LYS   B CD  1 
ATOM   2792 C  CE  . LYS   B 1 44  ? 27.538  -51.634 22.398 1.00 81.50  ?  43  LYS   B CE  1 
ATOM   2793 N  NZ  . LYS   B 1 44  ? 27.373  -52.576 21.247 1.00 90.40  ?  43  LYS   B NZ  1 
ATOM   2794 N  N   . ILE   B 1 45  ? 28.161  -49.846 17.757 1.00 82.68  ?  44  ILE   B N   1 
ATOM   2795 C  CA  . ILE   B 1 45  ? 28.435  -51.054 16.983 1.00 93.78  ?  44  ILE   B CA  1 
ATOM   2796 C  C   . ILE   B 1 45  ? 29.547  -50.775 15.971 1.00 97.76  ?  44  ILE   B C   1 
ATOM   2797 O  O   . ILE   B 1 45  ? 29.890  -49.627 15.666 1.00 93.74  ?  44  ILE   B O   1 
ATOM   2798 C  CB  . ILE   B 1 45  ? 27.167  -51.635 16.295 1.00 91.01  ?  44  ILE   B CB  1 
ATOM   2799 C  CG1 . ILE   B 1 45  ? 27.168  -53.180 16.357 1.00 102.00 ?  44  ILE   B CG1 1 
ATOM   2800 C  CG2 . ILE   B 1 45  ? 27.062  -51.191 14.848 1.00 82.11  ?  44  ILE   B CG2 1 
ATOM   2801 C  CD1 . ILE   B 1 45  ? 26.962  -53.805 17.767 1.00 94.09  ?  44  ILE   B CD1 1 
ATOM   2802 N  N   . LYS   B 1 46  ? 30.156  -51.863 15.471 1.00 103.13 ?  45  LYS   B N   1 
ATOM   2803 C  CA  . LYS   B 1 46  ? 31.304  -51.916 14.587 1.00 102.61 ?  45  LYS   B CA  1 
ATOM   2804 C  C   . LYS   B 1 46  ? 30.848  -52.113 13.145 1.00 101.26 ?  45  LYS   B C   1 
ATOM   2805 O  O   . LYS   B 1 46  ? 29.770  -52.662 12.897 1.00 103.17 ?  45  LYS   B O   1 
ATOM   2806 C  CB  . LYS   B 1 46  ? 32.237  -53.064 14.994 1.00 107.05 ?  45  LYS   B CB  1 
ATOM   2807 C  CG  . LYS   B 1 46  ? 33.732  -52.803 14.802 1.00 108.08 ?  45  LYS   B CG  1 
ATOM   2808 C  CD  . LYS   B 1 46  ? 34.565  -53.536 15.854 1.00 108.03 ?  45  LYS   B CD  1 
ATOM   2809 C  CE  . LYS   B 1 46  ? 34.630  -52.803 17.183 1.00 102.94 ?  45  LYS   B CE  1 
ATOM   2810 N  NZ  . LYS   B 1 46  ? 35.164  -51.434 17.013 1.00 105.03 ?  45  LYS   B NZ  1 
ATOM   2811 N  N   . PRO   B 1 47  ? 31.638  -51.638 12.182 1.00 103.97 ?  46  PRO   B N   1 
ATOM   2812 C  CA  . PRO   B 1 47  ? 31.259  -51.771 10.764 1.00 105.22 ?  46  PRO   B CA  1 
ATOM   2813 C  C   . PRO   B 1 47  ? 31.206  -53.206 10.266 1.00 106.62 ?  46  PRO   B C   1 
ATOM   2814 O  O   . PRO   B 1 47  ? 32.243  -53.842 10.059 1.00 110.77 ?  46  PRO   B O   1 
ATOM   2815 C  CB  . PRO   B 1 47  ? 32.346  -50.977 10.025 1.00 108.51 ?  46  PRO   B CB  1 
ATOM   2816 C  CG  . PRO   B 1 47  ? 33.249  -50.405 11.071 1.00 108.34 ?  46  PRO   B CG  1 
ATOM   2817 C  CD  . PRO   B 1 47  ? 32.669  -50.618 12.406 1.00 102.74 ?  46  PRO   B CD  1 
ATOM   2818 N  N   . HIS   B 1 48  ? 29.995  -53.717 10.063 1.00 106.68 ?  47  HIS   B N   1 
ATOM   2819 C  CA  . HIS   B 1 48  ? 29.804  -55.043 9.505  1.00 109.69 ?  47  HIS   B CA  1 
ATOM   2820 C  C   . HIS   B 1 48  ? 29.999  -54.996 7.991  1.00 111.82 ?  47  HIS   B C   1 
ATOM   2821 O  O   . HIS   B 1 48  ? 30.161  -53.930 7.397  1.00 111.19 ?  47  HIS   B O   1 
ATOM   2822 C  CB  . HIS   B 1 48  ? 28.415  -55.587 9.867  1.00 108.44 ?  47  HIS   B CB  1 
ATOM   2823 C  CG  . HIS   B 1 48  ? 28.257  -55.949 11.315 1.00 109.36 ?  47  HIS   B CG  1 
ATOM   2824 N  ND1 . HIS   B 1 48  ? 27.407  -56.946 11.746 1.00 112.47 ?  47  HIS   B ND1 1 
ATOM   2825 C  CD2 . HIS   B 1 48  ? 28.840  -55.446 12.431 1.00 113.85 ?  47  HIS   B CD2 1 
ATOM   2826 C  CE1 . HIS   B 1 48  ? 27.474  -57.043 13.064 1.00 115.49 ?  47  HIS   B CE1 1 
ATOM   2827 N  NE2 . HIS   B 1 48  ? 28.336  -56.144 13.505 1.00 117.72 ?  47  HIS   B NE2 1 
ATOM   2828 N  N   . ASN   B 1 49  ? 30.004  -56.175 7.362  1.00 120.20 ?  48  ASN   B N   1 
ATOM   2829 C  CA  . ASN   B 1 49  ? 30.107  -56.240 5.905  1.00 123.00 ?  48  ASN   B CA  1 
ATOM   2830 C  C   . ASN   B 1 49  ? 28.790  -55.911 5.208  1.00 119.31 ?  48  ASN   B C   1 
ATOM   2831 O  O   . ASN   B 1 49  ? 28.803  -55.599 4.010  1.00 113.35 ?  48  ASN   B O   1 
ATOM   2832 C  CB  . ASN   B 1 49  ? 30.616  -57.620 5.454  1.00 117.80 ?  48  ASN   B CB  1 
ATOM   2833 C  CG  . ASN   B 1 49  ? 32.144  -57.703 5.418  1.00 124.51 ?  48  ASN   B CG  1 
ATOM   2834 O  OD1 . ASN   B 1 49  ? 32.754  -58.516 6.112  1.00 121.73 ?  48  ASN   B OD1 1 
ATOM   2835 N  ND2 . ASN   B 1 49  ? 32.764  -56.867 4.589  1.00 122.91 ?  48  ASN   B ND2 1 
ATOM   2836 N  N   . SER   B 1 50  ? 27.663  -55.958 5.933  1.00 119.91 ?  49  SER   B N   1 
ATOM   2837 C  CA  . SER   B 1 50  ? 26.386  -55.503 5.380  1.00 115.53 ?  49  SER   B CA  1 
ATOM   2838 C  C   . SER   B 1 50  ? 26.400  -54.008 5.076  1.00 115.07 ?  49  SER   B C   1 
ATOM   2839 O  O   . SER   B 1 50  ? 25.684  -53.547 4.177  1.00 111.72 ?  49  SER   B O   1 
ATOM   2840 C  CB  . SER   B 1 50  ? 25.248  -55.819 6.353  1.00 112.62 ?  49  SER   B CB  1 
ATOM   2841 O  OG  . SER   B 1 50  ? 24.711  -57.105 6.116  1.00 108.72 ?  49  SER   B OG  1 
ATOM   2842 N  N   . HIS   B 1 51  ? 27.202  -53.240 5.815  1.00 116.57 ?  50  HIS   B N   1 
ATOM   2843 C  CA  . HIS   B 1 51  ? 27.295  -51.786 5.672  1.00 108.41 ?  50  HIS   B CA  1 
ATOM   2844 C  C   . HIS   B 1 51  ? 28.376  -51.474 4.643  1.00 111.57 ?  50  HIS   B C   1 
ATOM   2845 O  O   . HIS   B 1 51  ? 29.561  -51.357 4.970  1.00 108.48 ?  50  HIS   B O   1 
ATOM   2846 C  CB  . HIS   B 1 51  ? 27.612  -51.140 7.014  1.00 102.96 ?  50  HIS   B CB  1 
ATOM   2847 C  CG  . HIS   B 1 51  ? 26.865  -51.731 8.174  1.00 103.94 ?  50  HIS   B CG  1 
ATOM   2848 N  ND1 . HIS   B 1 51  ? 27.335  -51.662 9.469  1.00 99.85  ?  50  HIS   B ND1 1 
ATOM   2849 C  CD2 . HIS   B 1 51  ? 25.678  -52.380 8.238  1.00 101.82 ?  50  HIS   B CD2 1 
ATOM   2850 C  CE1 . HIS   B 1 51  ? 26.476  -52.255 10.278 1.00 103.38 ?  50  HIS   B CE1 1 
ATOM   2851 N  NE2 . HIS   B 1 51  ? 25.460  -52.697 9.557  1.00 98.07  ?  50  HIS   B NE2 1 
ATOM   2852 N  N   . GLU   B 1 52  ? 27.965  -51.341 3.382  1.00 108.27 ?  51  GLU   B N   1 
ATOM   2853 C  CA  . GLU   B 1 52  ? 28.883  -51.008 2.296  1.00 104.09 ?  51  GLU   B CA  1 
ATOM   2854 C  C   . GLU   B 1 52  ? 28.086  -50.286 1.222  1.00 108.77 ?  51  GLU   B C   1 
ATOM   2855 O  O   . GLU   B 1 52  ? 27.115  -50.843 0.699  1.00 111.27 ?  51  GLU   B O   1 
ATOM   2856 C  CB  . GLU   B 1 52  ? 29.552  -52.254 1.726  1.00 109.24 ?  51  GLU   B CB  1 
ATOM   2857 C  CG  . GLU   B 1 52  ? 30.064  -52.087 0.297  1.00 115.98 ?  51  GLU   B CG  1 
ATOM   2858 C  CD  . GLU   B 1 52  ? 31.433  -51.419 0.221  1.00 114.03 ?  51  GLU   B CD  1 
ATOM   2859 O  OE1 . GLU   B 1 52  ? 32.294  -51.915 -0.535 1.00 109.27 ?  51  GLU   B OE1 1 
ATOM   2860 O  OE2 . GLU   B 1 52  ? 31.646  -50.399 0.919  1.00 117.57 -1 51  GLU   B OE2 1 
ATOM   2861 N  N   . GLY   B 1 53  ? 28.496  -49.061 0.884  1.00 108.01 ?  52  GLY   B N   1 
ATOM   2862 C  CA  . GLY   B 1 53  ? 27.696  -48.215 0.024  1.00 103.52 ?  52  GLY   B CA  1 
ATOM   2863 C  C   . GLY   B 1 53  ? 26.385  -47.776 0.638  1.00 106.65 ?  52  GLY   B C   1 
ATOM   2864 O  O   . GLY   B 1 53  ? 25.518  -47.263 -0.083 1.00 104.88 ?  52  GLY   B O   1 
ATOM   2865 N  N   . LYS   B 1 54  ? 26.209  -47.977 1.947  1.00 107.55 ?  53  LYS   B N   1 
ATOM   2866 C  CA  . LYS   B 1 54  ? 24.997  -47.621 2.668  1.00 104.61 ?  53  LYS   B CA  1 
ATOM   2867 C  C   . LYS   B 1 54  ? 25.086  -46.172 3.137  1.00 100.05 ?  53  LYS   B C   1 
ATOM   2868 O  O   . LYS   B 1 54  ? 26.148  -45.540 3.065  1.00 97.15  ?  53  LYS   B O   1 
ATOM   2869 C  CB  . LYS   B 1 54  ? 24.786  -48.576 3.843  1.00 96.32  ?  53  LYS   B CB  1 
ATOM   2870 C  CG  . LYS   B 1 54  ? 24.730  -50.037 3.433  1.00 102.15 ?  53  LYS   B CG  1 
ATOM   2871 C  CD  . LYS   B 1 54  ? 23.349  -50.653 3.561  1.00 99.66  ?  53  LYS   B CD  1 
ATOM   2872 C  CE  . LYS   B 1 54  ? 23.102  -51.158 4.972  1.00 102.19 ?  53  LYS   B CE  1 
ATOM   2873 N  NZ  . LYS   B 1 54  ? 21.656  -51.099 5.298  1.00 96.14  ?  53  LYS   B NZ  1 
ATOM   2874 N  N   . THR   B 1 55  ? 23.957  -45.642 3.632  1.00 101.64 ?  54  THR   B N   1 
ATOM   2875 C  CA  . THR   B 1 55  ? 23.863  -44.249 4.053  1.00 94.06  ?  54  THR   B CA  1 
ATOM   2876 C  C   . THR   B 1 55  ? 23.419  -44.165 5.507  1.00 88.26  ?  54  THR   B C   1 
ATOM   2877 O  O   . THR   B 1 55  ? 22.389  -44.732 5.880  1.00 79.26  ?  54  THR   B O   1 
ATOM   2878 C  CB  . THR   B 1 55  ? 22.909  -43.463 3.167  1.00 83.79  ?  54  THR   B CB  1 
ATOM   2879 O  OG1 . THR   B 1 55  ? 23.232  -43.678 1.789  1.00 87.69  ?  54  THR   B OG1 1 
ATOM   2880 C  CG2 . THR   B 1 55  ? 23.023  -41.989 3.472  1.00 84.71  ?  54  THR   B CG2 1 
ATOM   2881 N  N   . PHE   B 1 56  ? 24.209  -43.456 6.315  1.00 87.66  ?  55  PHE   B N   1 
ATOM   2882 C  CA  . PHE   B 1 56  ? 23.944  -43.202 7.724  1.00 86.40  ?  55  PHE   B CA  1 
ATOM   2883 C  C   . PHE   B 1 56  ? 23.666  -41.717 7.957  1.00 80.62  ?  55  PHE   B C   1 
ATOM   2884 O  O   . PHE   B 1 56  ? 24.320  -40.859 7.356  1.00 80.93  ?  55  PHE   B O   1 
ATOM   2885 C  CB  . PHE   B 1 56  ? 25.147  -43.626 8.578  1.00 84.50  ?  55  PHE   B CB  1 
ATOM   2886 C  CG  . PHE   B 1 56  ? 25.641  -45.010 8.317  1.00 87.90  ?  55  PHE   B CG  1 
ATOM   2887 C  CD1 . PHE   B 1 56  ? 26.921  -45.209 7.784  1.00 93.03  ?  55  PHE   B CD1 1 
ATOM   2888 C  CD2 . PHE   B 1 56  ? 24.891  -46.117 8.721  1.00 88.44  ?  55  PHE   B CD2 1 
ATOM   2889 C  CE1 . PHE   B 1 56  ? 27.416  -46.464 7.579  1.00 96.09  ?  55  PHE   B CE1 1 
ATOM   2890 C  CE2 . PHE   B 1 56  ? 25.381  -47.411 8.521  1.00 88.09  ?  55  PHE   B CE2 1 
ATOM   2891 C  CZ  . PHE   B 1 56  ? 26.662  -47.601 7.941  1.00 85.77  ?  55  PHE   B CZ  1 
ATOM   2892 N  N   . TYR   B 1 57  ? 22.685  -41.415 8.816  1.00 76.78  ?  56  TYR   B N   1 
ATOM   2893 C  CA  . TYR   B 1 57  ? 22.531  -40.070 9.370  1.00 74.42  ?  56  TYR   B CA  1 
ATOM   2894 C  C   . TYR   B 1 57  ? 23.531  -39.835 10.492 1.00 68.74  ?  56  TYR   B C   1 
ATOM   2895 O  O   . TYR   B 1 57  ? 23.615  -40.629 11.430 1.00 70.64  ?  56  TYR   B O   1 
ATOM   2896 C  CB  . TYR   B 1 57  ? 21.126  -39.849 9.929  1.00 70.44  ?  56  TYR   B CB  1 
ATOM   2897 C  CG  . TYR   B 1 57  ? 20.054  -39.731 8.893  1.00 77.52  ?  56  TYR   B CG  1 
ATOM   2898 C  CD1 . TYR   B 1 57  ? 19.746  -40.803 8.066  1.00 76.99  ?  56  TYR   B CD1 1 
ATOM   2899 C  CD2 . TYR   B 1 57  ? 19.344  -38.542 8.737  1.00 77.15  ?  56  TYR   B CD2 1 
ATOM   2900 C  CE1 . TYR   B 1 57  ? 18.754  -40.701 7.118  1.00 86.10  ?  56  TYR   B CE1 1 
ATOM   2901 C  CE2 . TYR   B 1 57  ? 18.345  -38.426 7.783  1.00 78.41  ?  56  TYR   B CE2 1 
ATOM   2902 C  CZ  . TYR   B 1 57  ? 18.057  -39.509 6.978  1.00 85.02  ?  56  TYR   B CZ  1 
ATOM   2903 O  OH  . TYR   B 1 57  ? 17.069  -39.410 6.034  1.00 84.87  ?  56  TYR   B OH  1 
ATOM   2904 N  N   . VAL   B 1 58  ? 24.251  -38.722 10.425 1.00 66.35  ?  57  VAL   B N   1 
ATOM   2905 C  CA  . VAL   B 1 58  ? 25.157  -38.358 11.510 1.00 67.79  ?  57  VAL   B CA  1 
ATOM   2906 C  C   . VAL   B 1 58  ? 24.736  -37.014 12.076 1.00 63.23  ?  57  VAL   B C   1 
ATOM   2907 O  O   . VAL   B 1 58  ? 23.809  -36.379 11.564 1.00 65.55  ?  57  VAL   B O   1 
ATOM   2908 C  CB  . VAL   B 1 58  ? 26.621  -38.310 11.035 1.00 73.68  ?  57  VAL   B CB  1 
ATOM   2909 C  CG1 . VAL   B 1 58  ? 27.116  -39.712 10.716 1.00 71.51  ?  57  VAL   B CG1 1 
ATOM   2910 C  CG2 . VAL   B 1 58  ? 26.778  -37.374 9.822  1.00 63.61  ?  57  VAL   B CG2 1 
ATOM   2911 N  N   . LEU   B 1 59  ? 25.413  -36.568 13.123 1.00 66.22  ?  58  LEU   B N   1 
ATOM   2912 C  CA  . LEU   B 1 59  ? 25.208  -35.216 13.614 1.00 65.42  ?  58  LEU   B CA  1 
ATOM   2913 C  C   . LEU   B 1 59  ? 25.954  -34.205 12.740 1.00 68.02  ?  58  LEU   B C   1 
ATOM   2914 O  O   . LEU   B 1 59  ? 26.928  -34.555 12.062 1.00 69.18  ?  58  LEU   B O   1 
ATOM   2915 C  CB  . LEU   B 1 59  ? 25.681  -35.102 15.054 1.00 63.73  ?  58  LEU   B CB  1 
ATOM   2916 C  CG  . LEU   B 1 59  ? 24.926  -35.942 16.094 1.00 69.24  ?  58  LEU   B CG  1 
ATOM   2917 C  CD1 . LEU   B 1 59  ? 24.865  -35.255 17.464 1.00 52.54  ?  58  LEU   B CD1 1 
ATOM   2918 C  CD2 . LEU   B 1 59  ? 23.509  -36.260 15.604 1.00 67.69  ?  58  LEU   B CD2 1 
ATOM   2919 N  N   . PRO   B 1 60  ? 25.487  -32.957 12.700 1.00 65.63  ?  59  PRO   B N   1 
ATOM   2920 C  CA  . PRO   B 1 60  ? 26.247  -31.907 12.005 1.00 70.20  ?  59  PRO   B CA  1 
ATOM   2921 C  C   . PRO   B 1 60  ? 27.453  -31.411 12.796 1.00 69.64  ?  59  PRO   B C   1 
ATOM   2922 O  O   . PRO   B 1 60  ? 27.313  -30.594 13.712 1.00 67.21  ?  59  PRO   B O   1 
ATOM   2923 C  CB  . PRO   B 1 60  ? 25.206  -30.796 11.800 1.00 61.79  ?  59  PRO   B CB  1 
ATOM   2924 C  CG  . PRO   B 1 60  ? 24.148  -31.075 12.787 1.00 64.83  ?  59  PRO   B CG  1 
ATOM   2925 C  CD  . PRO   B 1 60  ? 24.103  -32.550 12.978 1.00 59.64  ?  59  PRO   B CD  1 
ATOM   2926 N  N   . ASN   B 1 61  ? 28.643  -31.898 12.424 1.00 71.44  ?  60  ASN   B N   1 
ATOM   2927 C  CA  . ASN   B 1 61  ? 29.922  -31.544 13.040 1.00 69.27  ?  60  ASN   B CA  1 
ATOM   2928 C  C   . ASN   B 1 61  ? 30.682  -30.431 12.314 1.00 69.96  ?  60  ASN   B C   1 
ATOM   2929 O  O   . ASN   B 1 61  ? 31.367  -29.641 12.974 1.00 73.65  ?  60  ASN   B O   1 
ATOM   2930 C  CB  . ASN   B 1 61  ? 30.813  -32.797 13.156 1.00 68.78  ?  60  ASN   B CB  1 
ATOM   2931 C  CG  . ASN   B 1 61  ? 30.805  -33.678 11.887 1.00 79.92  ?  60  ASN   B CG  1 
ATOM   2932 O  OD1 . ASN   B 1 61  ? 30.751  -33.189 10.752 1.00 81.35  ?  60  ASN   B OD1 1 
ATOM   2933 N  ND2 . ASN   B 1 61  ? 30.838  -34.996 12.093 1.00 77.34  ?  60  ASN   B ND2 1 
ATOM   2934 N  N   . ASP   B 1 62  ? 30.572  -30.335 10.988 1.00 72.08  ?  61  ASP   B N   1 
ATOM   2935 C  CA  . ASP   B 1 62  ? 31.228  -29.291 10.211 1.00 68.79  ?  61  ASP   B CA  1 
ATOM   2936 C  C   . ASP   B 1 62  ? 30.425  -28.006 10.259 1.00 64.19  ?  61  ASP   B C   1 
ATOM   2937 O  O   . ASP   B 1 62  ? 29.333  -27.931 10.836 1.00 58.54  ?  61  ASP   B O   1 
ATOM   2938 C  CB  . ASP   B 1 62  ? 31.325  -29.667 8.740  1.00 64.60  ?  61  ASP   B CB  1 
ATOM   2939 C  CG  . ASP   B 1 62  ? 31.519  -31.113 8.537  1.00 75.28  ?  61  ASP   B CG  1 
ATOM   2940 O  OD1 . ASP   B 1 62  ? 30.666  -31.697 7.850  1.00 76.65  -1 61  ASP   B OD1 1 
ATOM   2941 O  OD2 . ASP   B 1 62  ? 32.516  -31.668 9.049  1.00 90.07  ?  61  ASP   B OD2 1 
ATOM   2942 N  N   . ASP   B 1 63  ? 30.945  -27.004 9.557  1.00 56.33  ?  62  ASP   B N   1 
ATOM   2943 C  CA  . ASP   B 1 63  ? 30.079  -25.921 9.147  1.00 55.49  ?  62  ASP   B CA  1 
ATOM   2944 C  C   . ASP   B 1 63  ? 29.246  -26.284 7.923  1.00 58.24  ?  62  ASP   B C   1 
ATOM   2945 O  O   . ASP   B 1 63  ? 28.110  -25.812 7.795  1.00 59.01  ?  62  ASP   B O   1 
ATOM   2946 C  CB  . ASP   B 1 63  ? 30.884  -24.659 8.877  1.00 47.35  ?  62  ASP   B CB  1 
ATOM   2947 C  CG  . ASP   B 1 63  ? 30.007  -23.427 8.882  1.00 54.80  ?  62  ASP   B CG  1 
ATOM   2948 O  OD1 . ASP   B 1 63  ? 30.309  -22.489 8.130  1.00 57.39  ?  62  ASP   B OD1 1 
ATOM   2949 O  OD2 . ASP   B 1 63  ? 28.991  -23.398 9.626  1.00 57.74  -1 62  ASP   B OD2 1 
ATOM   2950 N  N   . THR   B 1 64  ? 29.779  -27.101 7.011  1.00 60.43  ?  63  THR   B N   1 
ATOM   2951 C  CA  . THR   B 1 64  ? 28.986  -27.497 5.851  1.00 60.45  ?  63  THR   B CA  1 
ATOM   2952 C  C   . THR   B 1 64  ? 27.777  -28.314 6.287  1.00 57.26  ?  63  THR   B C   1 
ATOM   2953 O  O   . THR   B 1 64  ? 26.655  -28.073 5.829  1.00 54.19  ?  63  THR   B O   1 
ATOM   2954 C  CB  . THR   B 1 64  ? 29.854  -28.272 4.847  1.00 63.92  ?  63  THR   B CB  1 
ATOM   2955 O  OG1 . THR   B 1 64  ? 30.661  -27.343 4.104  1.00 67.98  ?  63  THR   B OG1 1 
ATOM   2956 C  CG2 . THR   B 1 64  ? 28.995  -29.110 3.878  1.00 54.77  ?  63  THR   B CG2 1 
ATOM   2957 N  N   . LEU   B 1 65  ? 27.983  -29.250 7.210  1.00 56.89  ?  64  LEU   B N   1 
ATOM   2958 C  CA  . LEU   B 1 65  ? 26.874  -30.052 7.703  1.00 58.30  ?  64  LEU   B CA  1 
ATOM   2959 C  C   . LEU   B 1 65  ? 25.853  -29.190 8.424  1.00 53.97  ?  64  LEU   B C   1 
ATOM   2960 O  O   . LEU   B 1 65  ? 24.639  -29.401 8.294  1.00 51.52  ?  64  LEU   B O   1 
ATOM   2961 C  CB  . LEU   B 1 65  ? 27.403  -31.135 8.634  1.00 61.95  ?  64  LEU   B CB  1 
ATOM   2962 C  CG  . LEU   B 1 65  ? 27.819  -32.385 7.878  1.00 60.56  ?  64  LEU   B CG  1 
ATOM   2963 C  CD1 . LEU   B 1 65  ? 27.981  -33.492 8.888  1.00 63.40  ?  64  LEU   B CD1 1 
ATOM   2964 C  CD2 . LEU   B 1 65  ? 26.817  -32.731 6.747  1.00 50.61  ?  64  LEU   B CD2 1 
ATOM   2965 N  N   . ARG   B 1 66  ? 26.328  -28.222 9.203  1.00 54.26  ?  65  ARG   B N   1 
ATOM   2966 C  CA  . ARG   B 1 66  ? 25.418  -27.300 9.865  1.00 52.57  ?  65  ARG   B CA  1 
ATOM   2967 C  C   . ARG   B 1 66  ? 24.499  -26.623 8.852  1.00 53.14  ?  65  ARG   B C   1 
ATOM   2968 O  O   . ARG   B 1 66  ? 23.271  -26.609 9.028  1.00 47.80  ?  65  ARG   B O   1 
ATOM   2969 C  CB  . ARG   B 1 66  ? 26.224  -26.267 10.650 1.00 56.58  ?  65  ARG   B CB  1 
ATOM   2970 C  CG  . ARG   B 1 66  ? 26.648  -26.722 12.030 1.00 53.06  ?  65  ARG   B CG  1 
ATOM   2971 C  CD  . ARG   B 1 66  ? 27.320  -25.581 12.781 1.00 49.09  ?  65  ARG   B CD  1 
ATOM   2972 N  NE  . ARG   B 1 66  ? 28.633  -25.996 13.262 1.00 53.98  ?  65  ARG   B NE  1 
ATOM   2973 C  CZ  . ARG   B 1 66  ? 29.786  -25.530 12.802 1.00 52.51  ?  65  ARG   B CZ  1 
ATOM   2974 N  NH1 . ARG   B 1 66  ? 30.943  -26.002 13.236 1.00 60.27  ?  65  ARG   B NH1 1 
ATOM   2975 N  NH2 . ARG   B 1 66  ? 29.779  -24.562 11.890 1.00 52.07  ?  65  ARG   B NH2 1 
ATOM   2976 N  N   . VAL   B 1 67  ? 25.083  -26.076 7.770  1.00 47.73  ?  66  VAL   B N   1 
ATOM   2977 C  CA  . VAL   B 1 67  ? 24.296  -25.400 6.739  1.00 42.68  ?  66  VAL   B CA  1 
ATOM   2978 C  C   . VAL   B 1 67  ? 23.244  -26.336 6.153  1.00 47.11  ?  66  VAL   B C   1 
ATOM   2979 O  O   . VAL   B 1 67  ? 22.077  -25.959 6.031  1.00 47.62  ?  66  VAL   B O   1 
ATOM   2980 C  CB  . VAL   B 1 67  ? 25.197  -24.835 5.624  1.00 43.40  ?  66  VAL   B CB  1 
ATOM   2981 C  CG1 . VAL   B 1 67  ? 24.339  -24.147 4.571  1.00 33.38  ?  66  VAL   B CG1 1 
ATOM   2982 C  CG2 . VAL   B 1 67  ? 26.169  -23.857 6.160  1.00 41.50  ?  66  VAL   B CG2 1 
ATOM   2983 N  N   . GLU   B 1 68  ? 23.667  -27.536 5.751  1.00 45.21  ?  67  GLU   B N   1 
ATOM   2984 C  CA  . GLU   B 1 68  ? 22.711  -28.515 5.172  1.00 48.22  ?  67  GLU   B CA  1 
ATOM   2985 C  C   . GLU   B 1 68  ? 21.599  -28.767 6.196  1.00 50.14  ?  67  GLU   B C   1 
ATOM   2986 O  O   . GLU   B 1 68  ? 20.409  -28.653 5.829  1.00 43.28  ?  67  GLU   B O   1 
ATOM   2987 C  CB  . GLU   B 1 68  ? 23.421  -29.821 4.829  1.00 48.27  ?  67  GLU   B CB  1 
ATOM   2988 C  CG  . GLU   B 1 68  ? 24.649  -29.611 3.952  1.00 47.91  ?  67  GLU   B CG  1 
ATOM   2989 C  CD  . GLU   B 1 68  ? 24.993  -30.812 3.097  1.00 63.11  ?  67  GLU   B CD  1 
ATOM   2990 O  OE1 . GLU   B 1 68  ? 24.777  -31.952 3.560  1.00 68.00  ?  67  GLU   B OE1 1 
ATOM   2991 O  OE2 . GLU   B 1 68  ? 25.479  -30.598 1.966  1.00 66.75  -1 67  GLU   B OE2 1 
ATOM   2992 N  N   . ALA   B 1 69  ? 21.984  -29.093 7.431  1.00 49.90  ?  68  ALA   B N   1 
ATOM   2993 C  CA  . ALA   B 1 69  ? 21.002  -29.345 8.491  1.00 48.66  ?  68  ALA   B CA  1 
ATOM   2994 C  C   . ALA   B 1 69  ? 19.977  -28.223 8.567  1.00 47.34  ?  68  ALA   B C   1 
ATOM   2995 O  O   . ALA   B 1 69  ? 18.770  -28.471 8.580  1.00 48.77  ?  68  ALA   B O   1 
ATOM   2996 C  CB  . ALA   B 1 69  ? 21.690  -29.506 9.848  1.00 46.29  ?  68  ALA   B CB  1 
ATOM   2997 N  N   . PHE   B 1 70  ? 20.441  -26.971 8.602  1.00 47.07  ?  69  PHE   B N   1 
ATOM   2998 C  CA  . PHE   B 1 70  ? 19.502  -25.864 8.703  1.00 45.12  ?  69  PHE   B CA  1 
ATOM   2999 C  C   . PHE   B 1 70  ? 18.543  -25.824 7.517  1.00 47.28  ?  69  PHE   B C   1 
ATOM   3000 O  O   . PHE   B 1 70  ? 17.341  -25.607 7.700  1.00 50.99  ?  69  PHE   B O   1 
ATOM   3001 C  CB  . PHE   B 1 70  ? 20.239  -24.537 8.829  1.00 44.68  ?  69  PHE   B CB  1 
ATOM   3002 C  CG  . PHE   B 1 70  ? 19.312  -23.359 8.922  1.00 48.73  ?  69  PHE   B CG  1 
ATOM   3003 C  CD1 . PHE   B 1 70  ? 18.843  -22.926 10.149 1.00 49.07  ?  69  PHE   B CD1 1 
ATOM   3004 C  CD2 . PHE   B 1 70  ? 18.871  -22.703 7.776  1.00 49.19  ?  69  PHE   B CD2 1 
ATOM   3005 C  CE1 . PHE   B 1 70  ? 17.969  -21.844 10.232 1.00 49.98  ?  69  PHE   B CE1 1 
ATOM   3006 C  CE2 . PHE   B 1 70  ? 17.994  -21.623 7.859  1.00 45.09  ?  69  PHE   B CE2 1 
ATOM   3007 C  CZ  . PHE   B 1 70  ? 17.543  -21.203 9.085  1.00 45.40  ?  69  PHE   B CZ  1 
ATOM   3008 N  N   . GLU   B 1 71  ? 19.050  -26.013 6.294  1.00 48.03  ?  70  GLU   B N   1 
ATOM   3009 C  CA  . GLU   B 1 71  ? 18.194  -25.882 5.118  1.00 42.83  ?  70  GLU   B CA  1 
ATOM   3010 C  C   . GLU   B 1 71  ? 17.108  -26.948 5.113  1.00 43.73  ?  70  GLU   B C   1 
ATOM   3011 O  O   . GLU   B 1 71  ? 15.971  -26.685 4.704  1.00 43.75  ?  70  GLU   B O   1 
ATOM   3012 C  CB  . GLU   B 1 71  ? 19.035  -25.956 3.849  1.00 42.31  ?  70  GLU   B CB  1 
ATOM   3013 C  CG  . GLU   B 1 71  ? 20.114  -24.902 3.822  1.00 53.89  ?  70  GLU   B CG  1 
ATOM   3014 C  CD  . GLU   B 1 71  ? 19.999  -23.904 2.681  1.00 67.93  ?  70  GLU   B CD  1 
ATOM   3015 O  OE1 . GLU   B 1 71  ? 20.938  -23.904 1.833  1.00 67.60  ?  70  GLU   B OE1 1 
ATOM   3016 O  OE2 . GLU   B 1 71  ? 18.993  -23.122 2.649  1.00 61.72  -1 70  GLU   B OE2 1 
ATOM   3017 N  N   . TYR   B 1 72  ? 17.426  -28.146 5.610  1.00 44.39  ?  71  TYR   B N   1 
ATOM   3018 C  CA  . TYR   B 1 72  ? 16.443  -29.224 5.663  1.00 46.55  ?  71  TYR   B CA  1 
ATOM   3019 C  C   . TYR   B 1 72  ? 15.448  -29.042 6.817  1.00 49.58  ?  71  TYR   B C   1 
ATOM   3020 O  O   . TYR   B 1 72  ? 14.226  -29.156 6.611  1.00 48.85  ?  71  TYR   B O   1 
ATOM   3021 C  CB  . TYR   B 1 72  ? 17.179  -30.572 5.752  1.00 44.97  ?  71  TYR   B CB  1 
ATOM   3022 C  CG  . TYR   B 1 72  ? 16.370  -31.783 5.330  1.00 52.54  ?  71  TYR   B CG  1 
ATOM   3023 C  CD1 . TYR   B 1 72  ? 16.435  -32.980 6.049  1.00 58.50  ?  71  TYR   B CD1 1 
ATOM   3024 C  CD2 . TYR   B 1 72  ? 15.511  -31.723 4.241  1.00 57.94  ?  71  TYR   B CD2 1 
ATOM   3025 C  CE1 . TYR   B 1 72  ? 15.697  -34.097 5.668  1.00 60.92  ?  71  TYR   B CE1 1 
ATOM   3026 C  CE2 . TYR   B 1 72  ? 14.762  -32.831 3.855  1.00 65.21  ?  71  TYR   B CE2 1 
ATOM   3027 C  CZ  . TYR   B 1 72  ? 14.857  -34.017 4.575  1.00 67.99  ?  71  TYR   B CZ  1 
ATOM   3028 O  OH  . TYR   B 1 72  ? 14.109  -35.124 4.201  1.00 73.69  ?  71  TYR   B OH  1 
ATOM   3029 N  N   . TYR   B 1 73  ? 15.949  -28.728 8.028  1.00 41.05  ?  72  TYR   B N   1 
ATOM   3030 C  CA  . TYR   B 1 73  ? 15.143  -28.718 9.245  1.00 44.55  ?  72  TYR   B CA  1 
ATOM   3031 C  C   . TYR   B 1 73  ? 14.828  -27.342 9.810  1.00 43.05  ?  72  TYR   B C   1 
ATOM   3032 O  O   . TYR   B 1 73  ? 13.957  -27.255 10.682 1.00 40.80  ?  72  TYR   B O   1 
ATOM   3033 C  CB  . TYR   B 1 73  ? 15.831  -29.503 10.376 1.00 48.42  ?  72  TYR   B CB  1 
ATOM   3034 C  CG  . TYR   B 1 73  ? 16.077  -30.955 10.089 1.00 43.94  ?  72  TYR   B CG  1 
ATOM   3035 C  CD1 . TYR   B 1 73  ? 15.020  -31.852 10.026 1.00 42.99  ?  72  TYR   B CD1 1 
ATOM   3036 C  CD2 . TYR   B 1 73  ? 17.361  -31.437 9.913  1.00 40.28  ?  72  TYR   B CD2 1 
ATOM   3037 C  CE1 . TYR   B 1 73  ? 15.230  -33.184 9.770  1.00 46.44  ?  72  TYR   B CE1 1 
ATOM   3038 C  CE2 . TYR   B 1 73  ? 17.582  -32.781 9.646  1.00 53.89  ?  72  TYR   B CE2 1 
ATOM   3039 C  CZ  . TYR   B 1 73  ? 16.505  -33.652 9.574  1.00 51.05  ?  72  TYR   B CZ  1 
ATOM   3040 O  OH  . TYR   B 1 73  ? 16.707  -34.990 9.304  1.00 60.39  ?  72  TYR   B OH  1 
ATOM   3041 N  N   . HIS   B 1 74  ? 15.519  -26.284 9.370  1.00 42.20  ?  73  HIS   B N   1 
ATOM   3042 C  CA  . HIS   B 1 74  ? 15.455  -24.959 9.994  1.00 47.09  ?  73  HIS   B CA  1 
ATOM   3043 C  C   . HIS   B 1 74  ? 15.917  -24.983 11.442 1.00 51.40  ?  73  HIS   B C   1 
ATOM   3044 O  O   . HIS   B 1 74  ? 15.489  -24.149 12.250 1.00 46.25  ?  73  HIS   B O   1 
ATOM   3045 C  CB  . HIS   B 1 74  ? 14.052  -24.354 9.951  1.00 49.51  ?  73  HIS   B CB  1 
ATOM   3046 C  CG  . HIS   B 1 74  ? 13.689  -23.735 8.643  1.00 46.00  ?  73  HIS   B CG  1 
ATOM   3047 N  ND1 . HIS   B 1 74  ? 12.872  -22.629 8.552  1.00 51.82  ?  73  HIS   B ND1 1 
ATOM   3048 C  CD2 . HIS   B 1 74  ? 14.002  -24.077 7.375  1.00 43.81  ?  73  HIS   B CD2 1 
ATOM   3049 C  CE1 . HIS   B 1 74  ? 12.703  -22.309 7.284  1.00 43.84  ?  73  HIS   B CE1 1 
ATOM   3050 N  NE2 . HIS   B 1 74  ? 13.375  -23.174 6.548  1.00 47.30  ?  73  HIS   B NE2 1 
ATOM   3051 N  N   . THR   B 1 75  ? 16.771  -25.931 11.806 1.00 50.99  ?  74  THR   B N   1 
ATOM   3052 C  CA  . THR   B 1 75  ? 17.341  -25.954 13.138 1.00 53.89  ?  74  THR   B CA  1 
ATOM   3053 C  C   . THR   B 1 75  ? 18.835  -25.694 13.081 1.00 60.39  ?  74  THR   B C   1 
ATOM   3054 O  O   . THR   B 1 75  ? 19.499  -25.965 12.072 1.00 53.01  ?  74  THR   B O   1 
ATOM   3055 C  CB  . THR   B 1 75  ? 17.091  -27.291 13.846 1.00 58.28  ?  74  THR   B CB  1 
ATOM   3056 O  OG1 . THR   B 1 75  ? 17.199  -27.076 15.256 1.00 67.59  ?  74  THR   B OG1 1 
ATOM   3057 C  CG2 . THR   B 1 75  ? 18.116  -28.363 13.418 1.00 53.57  ?  74  THR   B CG2 1 
ATOM   3058 N  N   . THR   B 1 76  ? 19.348  -25.148 14.183 1.00 67.25  ?  75  THR   B N   1 
ATOM   3059 C  CA  . THR   B 1 76  ? 20.773  -25.151 14.463 1.00 66.40  ?  75  THR   B CA  1 
ATOM   3060 C  C   . THR   B 1 76  ? 21.140  -26.021 15.654 1.00 61.01  ?  75  THR   B C   1 
ATOM   3061 O  O   . THR   B 1 76  ? 22.298  -26.432 15.756 1.00 65.10  ?  75  THR   B O   1 
ATOM   3062 C  CB  . THR   B 1 76  ? 21.280  -23.721 14.697 1.00 61.84  ?  75  THR   B CB  1 
ATOM   3063 O  OG1 . THR   B 1 76  ? 20.195  -22.897 15.145 1.00 62.02  ?  75  THR   B OG1 1 
ATOM   3064 C  CG2 . THR   B 1 76  ? 21.877  -23.153 13.408 1.00 63.53  ?  75  THR   B CG2 1 
ATOM   3065 N  N   . ASP   B 1 77  ? 20.187  -26.337 16.522 1.00 59.71  ?  76  ASP   B N   1 
ATOM   3066 C  CA  . ASP   B 1 77  ? 20.422  -27.198 17.673 1.00 59.13  ?  76  ASP   B CA  1 
ATOM   3067 C  C   . ASP   B 1 77  ? 21.040  -28.529 17.234 1.00 56.62  ?  76  ASP   B C   1 
ATOM   3068 O  O   . ASP   B 1 77  ? 20.423  -29.269 16.455 1.00 63.24  ?  76  ASP   B O   1 
ATOM   3069 C  CB  . ASP   B 1 77  ? 19.103  -27.414 18.412 1.00 61.52  ?  76  ASP   B CB  1 
ATOM   3070 C  CG  . ASP   B 1 77  ? 19.124  -28.609 19.372 1.00 67.14  ?  76  ASP   B CG  1 
ATOM   3071 O  OD1 . ASP   B 1 77  ? 20.174  -29.255 19.588 1.00 62.75  ?  76  ASP   B OD1 1 
ATOM   3072 O  OD2 . ASP   B 1 77  ? 18.051  -28.888 19.953 1.00 71.63  -1 76  ASP   B OD2 1 
ATOM   3073 N  N   . PRO   B 1 78  ? 22.232  -28.871 17.724 1.00 54.24  ?  77  PRO   B N   1 
ATOM   3074 C  CA  . PRO   B 1 78  ? 22.914  -30.088 17.243 1.00 54.76  ?  77  PRO   B CA  1 
ATOM   3075 C  C   . PRO   B 1 78  ? 22.265  -31.388 17.667 1.00 57.07  ?  77  PRO   B C   1 
ATOM   3076 O  O   . PRO   B 1 78  ? 22.589  -32.427 17.081 1.00 62.47  ?  77  PRO   B O   1 
ATOM   3077 C  CB  . PRO   B 1 78  ? 24.322  -29.966 17.840 1.00 50.03  ?  77  PRO   B CB  1 
ATOM   3078 C  CG  . PRO   B 1 78  ? 24.487  -28.524 18.180 1.00 52.24  ?  77  PRO   B CG  1 
ATOM   3079 C  CD  . PRO   B 1 78  ? 23.128  -27.982 18.484 1.00 58.51  ?  77  PRO   B CD  1 
ATOM   3080 N  N   . SER   B 1 79  ? 21.382  -31.376 18.664 1.00 56.47  ?  78  SER   B N   1 
ATOM   3081 C  CA  . SER   B 1 79  ? 20.750  -32.589 19.166 1.00 49.68  ?  78  SER   B CA  1 
ATOM   3082 C  C   . SER   B 1 79  ? 19.477  -32.956 18.426 1.00 57.03  ?  78  SER   B C   1 
ATOM   3083 O  O   . SER   B 1 79  ? 18.958  -34.059 18.649 1.00 50.28  ?  78  SER   B O   1 
ATOM   3084 C  CB  . SER   B 1 79  ? 20.396  -32.424 20.643 1.00 59.08  ?  78  SER   B CB  1 
ATOM   3085 O  OG  . SER   B 1 79  ? 19.285  -31.555 20.785 1.00 57.32  ?  78  SER   B OG  1 
ATOM   3086 N  N   . PHE   B 1 80  ? 18.964  -32.053 17.574 1.00 61.38  ?  79  PHE   B N   1 
ATOM   3087 C  CA  . PHE   B 1 80  ? 17.648  -32.220 16.958 1.00 58.53  ?  79  PHE   B CA  1 
ATOM   3088 C  C   . PHE   B 1 80  ? 17.466  -33.626 16.394 1.00 56.81  ?  79  PHE   B C   1 
ATOM   3089 O  O   . PHE   B 1 80  ? 16.477  -34.308 16.698 1.00 54.03  ?  79  PHE   B O   1 
ATOM   3090 C  CB  . PHE   B 1 80  ? 17.452  -31.162 15.866 1.00 55.82  ?  79  PHE   B CB  1 
ATOM   3091 C  CG  . PHE   B 1 80  ? 16.086  -31.182 15.217 1.00 52.18  ?  79  PHE   B CG  1 
ATOM   3092 C  CD1 . PHE   B 1 80  ? 15.122  -30.236 15.562 1.00 51.12  ?  79  PHE   B CD1 1 
ATOM   3093 C  CD2 . PHE   B 1 80  ? 15.775  -32.124 14.239 1.00 44.12  ?  79  PHE   B CD2 1 
ATOM   3094 C  CE1 . PHE   B 1 80  ? 13.851  -30.243 14.947 1.00 49.83  ?  79  PHE   B CE1 1 
ATOM   3095 C  CE2 . PHE   B 1 80  ? 14.517  -32.141 13.628 1.00 42.92  ?  79  PHE   B CE2 1 
ATOM   3096 C  CZ  . PHE   B 1 80  ? 13.553  -31.200 13.982 1.00 43.23  ?  79  PHE   B CZ  1 
ATOM   3097 N  N   . LEU   B 1 81  ? 18.417  -34.071 15.568 1.00 52.04  ?  80  LEU   B N   1 
ATOM   3098 C  CA  . LEU   B 1 81  ? 18.368  -35.427 15.030 1.00 51.64  ?  80  LEU   B CA  1 
ATOM   3099 C  C   . LEU   B 1 81  ? 18.212  -36.455 16.147 1.00 53.76  ?  80  LEU   B C   1 
ATOM   3100 O  O   . LEU   B 1 81  ? 17.417  -37.396 16.031 1.00 55.42  ?  80  LEU   B O   1 
ATOM   3101 C  CB  . LEU   B 1 81  ? 19.635  -35.715 14.223 1.00 52.61  ?  80  LEU   B CB  1 
ATOM   3102 C  CG  . LEU   B 1 81  ? 20.156  -34.600 13.310 1.00 66.79  ?  80  LEU   B CG  1 
ATOM   3103 C  CD1 . LEU   B 1 81  ? 21.075  -33.635 14.103 1.00 66.31  ?  80  LEU   B CD1 1 
ATOM   3104 C  CD2 . LEU   B 1 81  ? 20.906  -35.178 12.095 1.00 63.61  ?  80  LEU   B CD2 1 
ATOM   3105 N  N   . GLY   B 1 82  ? 18.956  -36.285 17.244 1.00 56.37  ?  81  GLY   B N   1 
ATOM   3106 C  CA  . GLY   B 1 82  ? 18.874  -37.235 18.343 1.00 47.51  ?  81  GLY   B CA  1 
ATOM   3107 C  C   . GLY   B 1 82  ? 17.482  -37.313 18.937 1.00 56.58  ?  81  GLY   B C   1 
ATOM   3108 O  O   . GLY   B 1 82  ? 16.906  -38.400 19.056 1.00 56.43  ?  81  GLY   B O   1 
ATOM   3109 N  N   . ARG   B 1 83  ? 16.920  -36.158 19.326 1.00 57.63  ?  82  ARG   B N   1 
ATOM   3110 C  CA  . ARG   B 1 83  ? 15.550  -36.133 19.833 1.00 54.49  ?  82  ARG   B CA  1 
ATOM   3111 C  C   . ARG   B 1 83  ? 14.597  -36.798 18.844 1.00 56.86  ?  82  ARG   B C   1 
ATOM   3112 O  O   . ARG   B 1 83  ? 13.777  -37.650 19.219 1.00 57.46  ?  82  ARG   B O   1 
ATOM   3113 C  CB  . ARG   B 1 83  ? 15.127  -34.694 20.107 1.00 51.54  ?  82  ARG   B CB  1 
ATOM   3114 C  CG  . ARG   B 1 83  ? 15.872  -34.057 21.238 1.00 46.20  ?  82  ARG   B CG  1 
ATOM   3115 C  CD  . ARG   B 1 83  ? 16.474  -32.737 20.822 1.00 54.41  ?  82  ARG   B CD  1 
ATOM   3116 N  NE  . ARG   B 1 83  ? 15.546  -31.797 20.197 1.00 49.26  ?  82  ARG   B NE  1 
ATOM   3117 C  CZ  . ARG   B 1 83  ? 15.528  -30.498 20.470 1.00 60.78  ?  82  ARG   B CZ  1 
ATOM   3118 N  NH1 . ARG   B 1 83  ? 16.270  -29.987 21.442 1.00 71.56  ?  82  ARG   B NH1 1 
ATOM   3119 N  NH2 . ARG   B 1 83  ? 14.743  -29.688 19.760 1.00 60.22  ?  82  ARG   B NH2 1 
ATOM   3120 N  N   . TYR   B 1 84  ? 14.747  -36.447 17.563 1.00 50.98  ?  83  TYR   B N   1 
ATOM   3121 C  CA  . TYR   B 1 84  ? 13.914  -36.970 16.483 1.00 54.76  ?  83  TYR   B CA  1 
ATOM   3122 C  C   . TYR   B 1 84  ? 13.970  -38.497 16.390 1.00 54.82  ?  83  TYR   B C   1 
ATOM   3123 O  O   . TYR   B 1 84  ? 12.936  -39.169 16.274 1.00 51.96  ?  83  TYR   B O   1 
ATOM   3124 C  CB  . TYR   B 1 84  ? 14.380  -36.331 15.174 1.00 51.82  ?  83  TYR   B CB  1 
ATOM   3125 C  CG  . TYR   B 1 84  ? 13.821  -36.938 13.919 1.00 55.46  ?  83  TYR   B CG  1 
ATOM   3126 C  CD1 . TYR   B 1 84  ? 12.455  -36.925 13.671 1.00 55.85  ?  83  TYR   B CD1 1 
ATOM   3127 C  CD2 . TYR   B 1 84  ? 14.660  -37.477 12.950 1.00 58.88  ?  83  TYR   B CD2 1 
ATOM   3128 C  CE1 . TYR   B 1 84  ? 11.930  -37.461 12.504 1.00 57.71  ?  83  TYR   B CE1 1 
ATOM   3129 C  CE2 . TYR   B 1 84  ? 14.146  -38.007 11.774 1.00 57.79  ?  83  TYR   B CE2 1 
ATOM   3130 C  CZ  . TYR   B 1 84  ? 12.781  -38.004 11.556 1.00 62.32  ?  83  TYR   B CZ  1 
ATOM   3131 O  OH  . TYR   B 1 84  ? 12.253  -38.544 10.392 1.00 61.24  ?  83  TYR   B OH  1 
ATOM   3132 N  N   . MET   B 1 85  ? 15.176  -39.063 16.395 1.00 55.71  ?  84  MET   B N   1 
ATOM   3133 C  CA  . MET   B 1 85  ? 15.316  -40.503 16.215 1.00 54.14  ?  84  MET   B CA  1 
ATOM   3134 C  C   . MET   B 1 85  ? 14.839  -41.275 17.436 1.00 53.44  ?  84  MET   B C   1 
ATOM   3135 O  O   . MET   B 1 85  ? 14.584  -42.480 17.338 1.00 53.97  ?  84  MET   B O   1 
ATOM   3136 C  CB  . MET   B 1 85  ? 16.774  -40.838 15.888 1.00 54.44  ?  84  MET   B CB  1 
ATOM   3137 C  CG  . MET   B 1 85  ? 17.192  -40.324 14.505 1.00 65.01  ?  84  MET   B CG  1 
ATOM   3138 S  SD  . MET   B 1 85  ? 16.901  -41.500 13.168 1.00 68.78  ?  84  MET   B SD  1 
ATOM   3139 C  CE  . MET   B 1 85  ? 16.235  -40.484 11.872 1.00 65.47  ?  84  MET   B CE  1 
ATOM   3140 N  N   . SER   B 1 86  ? 14.712  -40.609 18.587 1.00 59.13  ?  85  SER   B N   1 
ATOM   3141 C  CA  . SER   B 1 86  ? 14.136  -41.259 19.759 1.00 54.34  ?  85  SER   B CA  1 
ATOM   3142 C  C   . SER   B 1 86  ? 12.623  -41.308 19.659 1.00 55.01  ?  85  SER   B C   1 
ATOM   3143 O  O   . SER   B 1 86  ? 12.013  -42.362 19.883 1.00 56.02  ?  85  SER   B O   1 
ATOM   3144 C  CB  . SER   B 1 86  ? 14.568  -40.539 21.021 1.00 51.72  ?  85  SER   B CB  1 
ATOM   3145 O  OG  . SER   B 1 86  ? 15.975  -40.424 21.033 1.00 69.13  ?  85  SER   B OG  1 
ATOM   3146 N  N   . ALA   B 1 87  ? 11.999  -40.179 19.306 1.00 47.31  ?  86  ALA   B N   1 
ATOM   3147 C  CA  . ALA   B 1 87  ? 10.568  -40.209 19.065 1.00 39.08  ?  86  ALA   B CA  1 
ATOM   3148 C  C   . ALA   B 1 87  ? 10.239  -41.196 17.956 1.00 49.24  ?  86  ALA   B C   1 
ATOM   3149 O  O   . ALA   B 1 87  ? 9.310   -42.000 18.091 1.00 48.65  ?  86  ALA   B O   1 
ATOM   3150 C  CB  . ALA   B 1 87  ? 10.067  -38.809 18.735 1.00 42.31  ?  86  ALA   B CB  1 
ATOM   3151 N  N   . LEU   B 1 88  ? 11.033  -41.192 16.873 1.00 55.60  ?  87  LEU   B N   1 
ATOM   3152 C  CA  . LEU   B 1 88  ? 10.735  -42.038 15.721 1.00 49.40  ?  87  LEU   B CA  1 
ATOM   3153 C  C   . LEU   B 1 88  ? 10.698  -43.521 16.085 1.00 53.62  ?  87  LEU   B C   1 
ATOM   3154 O  O   . LEU   B 1 88  ? 9.913   -44.272 15.496 1.00 55.99  ?  87  LEU   B O   1 
ATOM   3155 C  CB  . LEU   B 1 88  ? 11.734  -41.781 14.589 1.00 50.95  ?  87  LEU   B CB  1 
ATOM   3156 C  CG  . LEU   B 1 88  ? 11.420  -42.530 13.273 1.00 53.30  ?  87  LEU   B CG  1 
ATOM   3157 C  CD1 . LEU   B 1 88  ? 10.040  -42.171 12.727 1.00 54.23  ?  87  LEU   B CD1 1 
ATOM   3158 C  CD2 . LEU   B 1 88  ? 12.482  -42.287 12.221 1.00 48.98  ?  87  LEU   B CD2 1 
ATOM   3159 N  N   . ASN   B 1 89  ? 11.514  -43.969 17.053 1.00 55.58  ?  88  ASN   B N   1 
ATOM   3160 C  CA  . ASN   B 1 89  ? 11.428  -45.369 17.480 1.00 53.08  ?  88  ASN   B CA  1 
ATOM   3161 C  C   . ASN   B 1 89  ? 10.045  -45.709 18.019 1.00 51.92  ?  88  ASN   B C   1 
ATOM   3162 O  O   . ASN   B 1 89  ? 9.562   -46.830 17.827 1.00 55.03  ?  88  ASN   B O   1 
ATOM   3163 C  CB  . ASN   B 1 89  ? 12.490  -45.681 18.532 1.00 50.77  ?  88  ASN   B CB  1 
ATOM   3164 C  CG  . ASN   B 1 89  ? 13.802  -46.108 17.921 1.00 58.76  ?  88  ASN   B CG  1 
ATOM   3165 O  OD1 . ASN   B 1 89  ? 13.829  -46.874 16.962 1.00 71.67  ?  88  ASN   B OD1 1 
ATOM   3166 N  ND2 . ASN   B 1 89  ? 14.903  -45.607 18.462 1.00 64.86  ?  88  ASN   B ND2 1 
ATOM   3167 N  N   . HIS   B 1 90  ? 9.389   -44.753 18.669 1.00 48.72  ?  89  HIS   B N   1 
ATOM   3168 C  CA  . HIS   B 1 90  ? 8.034   -44.966 19.157 1.00 46.27  ?  89  HIS   B CA  1 
ATOM   3169 C  C   . HIS   B 1 90  ? 7.030   -44.839 18.021 1.00 53.98  ?  89  HIS   B C   1 
ATOM   3170 O  O   . HIS   B 1 90  ? 6.207   -45.739 17.804 1.00 53.55  ?  89  HIS   B O   1 
ATOM   3171 C  CB  . HIS   B 1 90  ? 7.700   -43.938 20.231 1.00 49.19  ?  89  HIS   B CB  1 
ATOM   3172 C  CG  . HIS   B 1 90  ? 8.483   -44.092 21.495 1.00 54.08  ?  89  HIS   B CG  1 
ATOM   3173 N  ND1 . HIS   B 1 90  ? 8.039   -44.836 22.571 1.00 59.83  ?  89  HIS   B ND1 1 
ATOM   3174 C  CD2 . HIS   B 1 90  ? 9.687   -43.592 21.854 1.00 46.36  ?  89  HIS   B CD2 1 
ATOM   3175 C  CE1 . HIS   B 1 90  ? 8.934   -44.779 23.538 1.00 49.88  ?  89  HIS   B CE1 1 
ATOM   3176 N  NE2 . HIS   B 1 90  ? 9.944   -44.035 23.126 1.00 47.15  ?  89  HIS   B NE2 1 
ATOM   3177 N  N   . THR   B 1 91  ? 7.095   -43.722 17.276 1.00 50.23  ?  90  THR   B N   1 
ATOM   3178 C  CA  . THR   B 1 91  ? 6.043   -43.409 16.313 1.00 44.25  ?  90  THR   B CA  1 
ATOM   3179 C  C   . THR   B 1 91  ? 6.050   -44.362 15.120 1.00 52.60  ?  90  THR   B C   1 
ATOM   3180 O  O   . THR   B 1 91  ? 4.986   -44.624 14.541 1.00 56.14  ?  90  THR   B O   1 
ATOM   3181 C  CB  . THR   B 1 91  ? 6.172   -41.963 15.847 1.00 45.58  ?  90  THR   B CB  1 
ATOM   3182 O  OG1 . THR   B 1 91  ? 7.245   -41.852 14.893 1.00 47.41  ?  90  THR   B OG1 1 
ATOM   3183 C  CG2 . THR   B 1 91  ? 6.404   -41.022 17.065 1.00 39.50  ?  90  THR   B CG2 1 
ATOM   3184 N  N   . LYS   B 1 92  ? 7.223   -44.890 14.736 1.00 51.78  ?  91  LYS   B N   1 
ATOM   3185 C  CA  . LYS   B 1 92  ? 7.274   -45.957 13.739 1.00 46.60  ?  91  LYS   B CA  1 
ATOM   3186 C  C   . LYS   B 1 92  ? 6.378   -47.126 14.124 1.00 50.86  ?  91  LYS   B C   1 
ATOM   3187 O  O   . LYS   B 1 92  ? 5.857   -47.824 13.247 1.00 61.00  ?  91  LYS   B O   1 
ATOM   3188 C  CB  . LYS   B 1 92  ? 8.713   -46.454 13.551 1.00 48.92  ?  91  LYS   B CB  1 
ATOM   3189 C  CG  . LYS   B 1 92  ? 9.540   -45.630 12.540 1.00 60.79  ?  91  LYS   B CG  1 
ATOM   3190 C  CD  . LYS   B 1 92  ? 10.411  -46.501 11.612 1.00 64.77  ?  91  LYS   B CD  1 
ATOM   3191 C  CE  . LYS   B 1 92  ? 11.896  -46.089 11.681 1.00 63.69  ?  91  LYS   B CE  1 
ATOM   3192 N  NZ  . LYS   B 1 92  ? 12.807  -47.143 11.143 1.00 68.21  ?  91  LYS   B NZ  1 
ATOM   3193 N  N   . LYS   B 1 93  ? 6.188   -47.359 15.426 1.00 56.44  ?  92  LYS   B N   1 
ATOM   3194 C  CA  . LYS   B 1 93  ? 5.420   -48.493 15.929 1.00 53.73  ?  92  LYS   B CA  1 
ATOM   3195 C  C   . LYS   B 1 93  ? 3.974   -48.138 16.244 1.00 51.92  ?  92  LYS   B C   1 
ATOM   3196 O  O   . LYS   B 1 93  ? 3.175   -49.047 16.487 1.00 51.94  ?  92  LYS   B O   1 
ATOM   3197 C  CB  . LYS   B 1 93  ? 6.082   -49.062 17.191 1.00 57.37  ?  92  LYS   B CB  1 
ATOM   3198 C  CG  . LYS   B 1 93  ? 7.453   -49.707 16.982 1.00 60.21  ?  92  LYS   B CG  1 
ATOM   3199 C  CD  . LYS   B 1 93  ? 7.848   -50.550 18.209 1.00 63.28  ?  92  LYS   B CD  1 
ATOM   3200 C  CE  . LYS   B 1 93  ? 9.358   -50.630 18.394 1.00 58.55  ?  92  LYS   B CE  1 
ATOM   3201 N  NZ  . LYS   B 1 93  ? 9.798   -49.724 19.505 1.00 70.14  ?  92  LYS   B NZ  1 
ATOM   3202 N  N   . TRP   B 1 94  ? 3.631   -46.847 16.253 1.00 53.10  ?  93  TRP   B N   1 
ATOM   3203 C  CA  . TRP   B 1 94  ? 2.262   -46.390 16.451 1.00 51.62  ?  93  TRP   B CA  1 
ATOM   3204 C  C   . TRP   B 1 94  ? 1.381   -46.800 15.266 1.00 51.20  ?  93  TRP   B C   1 
ATOM   3205 O  O   . TRP   B 1 94  ? 1.859   -47.125 14.179 1.00 51.31  ?  93  TRP   B O   1 
ATOM   3206 C  CB  . TRP   B 1 94  ? 2.227   -44.862 16.632 1.00 50.50  ?  93  TRP   B CB  1 
ATOM   3207 C  CG  . TRP   B 1 94  ? 2.675   -44.371 18.002 1.00 50.33  ?  93  TRP   B CG  1 
ATOM   3208 C  CD1 . TRP   B 1 94  ? 3.021   -45.143 19.058 1.00 47.53  ?  93  TRP   B CD1 1 
ATOM   3209 C  CD2 . TRP   B 1 94  ? 2.828   -43.002 18.442 1.00 47.52  ?  93  TRP   B CD2 1 
ATOM   3210 N  NE1 . TRP   B 1 94  ? 3.379   -44.362 20.125 1.00 47.64  ?  93  TRP   B NE1 1 
ATOM   3211 C  CE2 . TRP   B 1 94  ? 3.271   -43.044 19.776 1.00 48.04  ?  93  TRP   B CE2 1 
ATOM   3212 C  CE3 . TRP   B 1 94  ? 2.630   -41.753 17.839 1.00 46.90  ?  93  TRP   B CE3 1 
ATOM   3213 C  CZ2 . TRP   B 1 94  ? 3.521   -41.887 20.527 1.00 47.17  ?  93  TRP   B CZ2 1 
ATOM   3214 C  CZ3 . TRP   B 1 94  ? 2.882   -40.596 18.586 1.00 48.59  ?  93  TRP   B CZ3 1 
ATOM   3215 C  CH2 . TRP   B 1 94  ? 3.324   -40.676 19.913 1.00 46.92  ?  93  TRP   B CH2 1 
ATOM   3216 N  N   . LYS   B 1 95  ? 0.073   -46.763 15.482 1.00 54.18  ?  94  LYS   B N   1 
ATOM   3217 C  CA  . LYS   B 1 95  ? -0.902  -47.063 14.443 1.00 56.64  ?  94  LYS   B CA  1 
ATOM   3218 C  C   . LYS   B 1 95  ? -1.656  -45.794 14.041 1.00 55.09  ?  94  LYS   B C   1 
ATOM   3219 O  O   . LYS   B 1 95  ? -2.065  -44.996 14.902 1.00 49.51  ?  94  LYS   B O   1 
ATOM   3220 C  CB  . LYS   B 1 95  ? -1.889  -48.144 14.911 1.00 54.91  ?  94  LYS   B CB  1 
ATOM   3221 C  CG  . LYS   B 1 95  ? -1.280  -49.537 15.086 1.00 56.84  ?  94  LYS   B CG  1 
ATOM   3222 C  CD  . LYS   B 1 95  ? -0.233  -49.856 14.024 1.00 58.51  ?  94  LYS   B CD  1 
ATOM   3223 C  CE  . LYS   B 1 95  ? -0.223  -51.356 13.623 1.00 67.55  ?  94  LYS   B CE  1 
ATOM   3224 N  NZ  . LYS   B 1 95  ? -0.773  -52.279 14.684 1.00 63.59  ?  94  LYS   B NZ  1 
ATOM   3225 N  N   . TYR   B 1 96  ? -1.860  -45.638 12.725 1.00 50.72  ?  95  TYR   B N   1 
ATOM   3226 C  CA  . TYR   B 1 96  ? -2.414  -44.433 12.103 1.00 55.21  ?  95  TYR   B CA  1 
ATOM   3227 C  C   . TYR   B 1 96  ? -3.649  -44.782 11.267 1.00 57.94  ?  95  TYR   B C   1 
ATOM   3228 O  O   . TYR   B 1 96  ? -3.612  -44.753 10.027 1.00 57.90  ?  95  TYR   B O   1 
ATOM   3229 C  CB  . TYR   B 1 96  ? -1.350  -43.740 11.244 1.00 51.87  ?  95  TYR   B CB  1 
ATOM   3230 C  CG  . TYR   B 1 96  ? -0.110  -43.357 12.031 1.00 55.13  ?  95  TYR   B CG  1 
ATOM   3231 C  CD1 . TYR   B 1 96  ? -0.033  -42.135 12.710 1.00 51.35  ?  95  TYR   B CD1 1 
ATOM   3232 C  CD2 . TYR   B 1 96  ? 0.963   -44.231 12.145 1.00 52.92  ?  95  TYR   B CD2 1 
ATOM   3233 C  CE1 . TYR   B 1 96  ? 1.087   -41.795 13.450 1.00 45.06  ?  95  TYR   B CE1 1 
ATOM   3234 C  CE2 . TYR   B 1 96  ? 2.086   -43.892 12.886 1.00 50.45  ?  95  TYR   B CE2 1 
ATOM   3235 C  CZ  . TYR   B 1 96  ? 2.138   -42.677 13.531 1.00 47.97  ?  95  TYR   B CZ  1 
ATOM   3236 O  OH  . TYR   B 1 96  ? 3.256   -42.344 14.255 1.00 50.74  ?  95  TYR   B OH  1 
ATOM   3237 N  N   . PRO   B 1 97  ? -4.768  -45.091 11.911 1.00 57.66  ?  96  PRO   B N   1 
ATOM   3238 C  CA  . PRO   B 1 97  ? -5.967  -45.479 11.153 1.00 58.53  ?  96  PRO   B CA  1 
ATOM   3239 C  C   . PRO   B 1 97  ? -6.589  -44.298 10.420 1.00 58.47  ?  96  PRO   B C   1 
ATOM   3240 O  O   . PRO   B 1 97  ? -6.369  -43.133 10.757 1.00 58.66  ?  96  PRO   B O   1 
ATOM   3241 C  CB  . PRO   B 1 97  ? -6.912  -46.001 12.238 1.00 56.60  ?  96  PRO   B CB  1 
ATOM   3242 C  CG  . PRO   B 1 97  ? -6.529  -45.186 13.460 1.00 54.56  ?  96  PRO   B CG  1 
ATOM   3243 C  CD  . PRO   B 1 97  ? -5.026  -44.996 13.360 1.00 51.77  ?  96  PRO   B CD  1 
ATOM   3244 N  N   . GLN   B 1 98  ? -7.395  -44.619 9.406  1.00 59.72  ?  97  GLN   B N   1 
ATOM   3245 C  CA  . GLN   B 1 98  ? -8.227  -43.627 8.739  1.00 54.51  ?  97  GLN   B CA  1 
ATOM   3246 C  C   . GLN   B 1 98  ? -9.553  -43.502 9.472  1.00 53.09  ?  97  GLN   B C   1 
ATOM   3247 O  O   . GLN   B 1 98  ? -10.196 -44.508 9.776  1.00 64.16  ?  97  GLN   B O   1 
ATOM   3248 C  CB  . GLN   B 1 98  ? -8.468  -44.007 7.281  1.00 51.98  ?  97  GLN   B CB  1 
ATOM   3249 C  CG  . GLN   B 1 98  ? -7.236  -43.921 6.405  1.00 49.05  ?  97  GLN   B CG  1 
ATOM   3250 C  CD  . GLN   B 1 98  ? -6.720  -42.498 6.277  1.00 55.59  ?  97  GLN   B CD  1 
ATOM   3251 O  OE1 . GLN   B 1 98  ? -5.568  -42.226 6.601  1.00 60.76  ?  97  GLN   B OE1 1 
ATOM   3252 N  NE2 . GLN   B 1 98  ? -7.575  -41.580 5.831  1.00 53.55  ?  97  GLN   B NE2 1 
ATOM   3253 N  N   . VAL   B 1 99  ? -9.955  -42.272 9.762  1.00 50.16  ?  98  VAL   B N   1 
ATOM   3254 C  CA  . VAL   B 1 99  ? -11.145 -41.997 10.558 1.00 49.76  ?  98  VAL   B CA  1 
ATOM   3255 C  C   . VAL   B 1 99  ? -11.779 -40.752 9.957  1.00 60.12  ?  98  VAL   B C   1 
ATOM   3256 O  O   . VAL   B 1 99  ? -11.146 -39.686 9.939  1.00 58.35  ?  98  VAL   B O   1 
ATOM   3257 C  CB  . VAL   B 1 99  ? -10.823 -41.764 12.052 1.00 56.82  ?  98  VAL   B CB  1 
ATOM   3258 C  CG1 . VAL   B 1 99  ? -12.102 -41.654 12.883 1.00 58.84  ?  98  VAL   B CG1 1 
ATOM   3259 C  CG2 . VAL   B 1 99  ? -9.885  -42.851 12.633 1.00 52.05  ?  98  VAL   B CG2 1 
ATOM   3260 N  N   . ASN   B 1 100 ? -13.023 -40.880 9.468  1.00 61.67  ?  99  ASN   B N   1 
ATOM   3261 C  CA  . ASN   B 1 100 ? -13.654 -39.847 8.633  1.00 51.56  ?  99  ASN   B CA  1 
ATOM   3262 C  C   . ASN   B 1 100 ? -12.756 -39.454 7.461  1.00 49.02  ?  99  ASN   B C   1 
ATOM   3263 O  O   . ASN   B 1 100 ? -12.695 -38.290 7.049  1.00 50.91  ?  99  ASN   B O   1 
ATOM   3264 C  CB  . ASN   B 1 100 ? -14.021 -38.614 9.451  1.00 56.79  ?  99  ASN   B CB  1 
ATOM   3265 C  CG  . ASN   B 1 100 ? -15.501 -38.335 9.439  1.00 72.79  ?  99  ASN   B CG  1 
ATOM   3266 O  OD1 . ASN   B 1 100 ? -16.225 -38.780 8.543  1.00 76.14  ?  99  ASN   B OD1 1 
ATOM   3267 N  ND2 . ASN   B 1 100 ? -15.962 -37.569 10.417 1.00 70.61  ?  99  ASN   B ND2 1 
ATOM   3268 N  N   . GLY   B 1 101 ? -12.020 -40.416 6.927  1.00 43.45  ?  100 GLY   B N   1 
ATOM   3269 C  CA  . GLY   B 1 101 ? -11.090 -40.076 5.873  1.00 51.19  ?  100 GLY   B CA  1 
ATOM   3270 C  C   . GLY   B 1 101 ? -9.979  -39.119 6.250  1.00 53.03  ?  100 GLY   B C   1 
ATOM   3271 O  O   . GLY   B 1 101 ? -9.434  -38.458 5.362  1.00 55.94  ?  100 GLY   B O   1 
ATOM   3272 N  N   . LEU   B 1 102 ? -9.625  -39.022 7.539  1.00 54.38  ?  101 LEU   B N   1 
ATOM   3273 C  CA  . LEU   B 1 102 ? -8.438  -38.309 7.997  1.00 46.02  ?  101 LEU   B CA  1 
ATOM   3274 C  C   . LEU   B 1 102 ? -7.514  -39.276 8.730  1.00 57.72  ?  101 LEU   B C   1 
ATOM   3275 O  O   . LEU   B 1 102 ? -7.976  -40.232 9.372  1.00 58.50  ?  101 LEU   B O   1 
ATOM   3276 C  CB  . LEU   B 1 102 ? -8.803  -37.168 8.919  1.00 47.31  ?  101 LEU   B CB  1 
ATOM   3277 C  CG  . LEU   B 1 102 ? -9.727  -36.048 8.438  1.00 49.84  ?  101 LEU   B CG  1 
ATOM   3278 C  CD1 . LEU   B 1 102 ? -10.641 -35.603 9.566  1.00 45.52  ?  101 LEU   B CD1 1 
ATOM   3279 C  CD2 . LEU   B 1 102 ? -8.927  -34.871 7.905  1.00 43.90  ?  101 LEU   B CD2 1 
ATOM   3280 N  N   . THR   B 1 103 ? -6.201  -39.032 8.638  1.00 54.92  ?  102 THR   B N   1 
ATOM   3281 C  CA  . THR   B 1 103 ? -5.248  -39.852 9.386  1.00 49.53  ?  102 THR   B CA  1 
ATOM   3282 C  C   . THR   B 1 103 ? -5.278  -39.489 10.865 1.00 50.57  ?  102 THR   B C   1 
ATOM   3283 O  O   . THR   B 1 103 ? -5.166  -38.314 11.224 1.00 53.02  ?  102 THR   B O   1 
ATOM   3284 C  CB  . THR   B 1 103 ? -3.829  -39.664 8.873  1.00 48.83  ?  102 THR   B CB  1 
ATOM   3285 O  OG1 . THR   B 1 103 ? -3.781  -39.842 7.453  1.00 50.13  ?  102 THR   B OG1 1 
ATOM   3286 C  CG2 . THR   B 1 103 ? -2.921  -40.674 9.529  1.00 47.19  ?  102 THR   B CG2 1 
ATOM   3287 N  N   . SER   B 1 104 ? -5.402  -40.494 11.724 1.00 50.72  ?  103 SER   B N   1 
ATOM   3288 C  CA  . SER   B 1 104 ? -5.435  -40.320 13.171 1.00 49.14  ?  103 SER   B CA  1 
ATOM   3289 C  C   . SER   B 1 104 ? -4.284  -41.100 13.803 1.00 53.82  ?  103 SER   B C   1 
ATOM   3290 O  O   . SER   B 1 104 ? -3.395  -41.612 13.099 1.00 52.20  ?  103 SER   B O   1 
ATOM   3291 C  CB  . SER   B 1 104 ? -6.776  -40.776 13.739 1.00 50.88  ?  103 SER   B CB  1 
ATOM   3292 O  OG  . SER   B 1 104 ? -7.032  -40.125 14.954 1.00 47.13  ?  103 SER   B OG  1 
ATOM   3293 N  N   . ILE   B 1 105 ? -4.300  -41.198 15.142 1.00 44.71  ?  104 ILE   B N   1 
ATOM   3294 C  CA  . ILE   B 1 105 ? -3.386  -42.077 15.872 1.00 45.11  ?  104 ILE   B CA  1 
ATOM   3295 C  C   . ILE   B 1 105 ? -4.176  -42.855 16.925 1.00 53.70  ?  104 ILE   B C   1 
ATOM   3296 O  O   . ILE   B 1 105 ? -4.940  -42.264 17.703 1.00 57.16  ?  104 ILE   B O   1 
ATOM   3297 C  CB  . ILE   B 1 105 ? -2.213  -41.307 16.525 1.00 42.75  ?  104 ILE   B CB  1 
ATOM   3298 C  CG1 . ILE   B 1 105 ? -1.697  -40.198 15.615 1.00 48.74  ?  104 ILE   B CG1 1 
ATOM   3299 C  CG2 . ILE   B 1 105 ? -1.061  -42.237 16.822 1.00 42.63  ?  104 ILE   B CG2 1 
ATOM   3300 C  CD1 . ILE   B 1 105 ? -0.754  -39.243 16.279 1.00 43.60  ?  104 ILE   B CD1 1 
ATOM   3301 N  N   . LYS   B 1 106 ? -4.000  -44.180 16.941 1.00 50.60  ?  105 LYS   B N   1 
ATOM   3302 C  CA  . LYS   B 1 106 ? -4.545  -44.994 18.021 1.00 49.30  ?  105 LYS   B CA  1 
ATOM   3303 C  C   . LYS   B 1 106 ? -3.824  -44.620 19.311 1.00 52.41  ?  105 LYS   B C   1 
ATOM   3304 O  O   . LYS   B 1 106 ? -2.624  -44.339 19.295 1.00 52.67  ?  105 LYS   B O   1 
ATOM   3305 C  CB  . LYS   B 1 106 ? -4.376  -46.482 17.684 1.00 47.23  ?  105 LYS   B CB  1 
ATOM   3306 C  CG  . LYS   B 1 106 ? -4.543  -47.464 18.820 1.00 56.05  ?  105 LYS   B CG  1 
ATOM   3307 C  CD  . LYS   B 1 106 ? -4.670  -48.909 18.289 1.00 57.73  ?  105 LYS   B CD  1 
ATOM   3308 C  CE  . LYS   B 1 106 ? -4.190  -49.965 19.309 1.00 57.53  ?  105 LYS   B CE  1 
ATOM   3309 N  NZ  . LYS   B 1 106 ? -2.713  -50.246 19.217 1.00 62.41  ?  105 LYS   B NZ  1 
ATOM   3310 N  N   . TRP   B 1 107 ? -4.561  -44.561 20.422 1.00 55.16  ?  106 TRP   B N   1 
ATOM   3311 C  CA  . TRP   B 1 107 ? -3.963  -44.121 21.677 1.00 54.29  ?  106 TRP   B CA  1 
ATOM   3312 C  C   . TRP   B 1 107 ? -2.677  -44.877 21.986 1.00 58.35  ?  106 TRP   B C   1 
ATOM   3313 O  O   . TRP   B 1 107 ? -2.646  -46.111 21.989 1.00 65.62  ?  106 TRP   B O   1 
ATOM   3314 C  CB  . TRP   B 1 107 ? -4.922  -44.288 22.858 1.00 60.35  ?  106 TRP   B CB  1 
ATOM   3315 C  CG  . TRP   B 1 107 ? -4.219  -43.837 24.139 1.00 66.03  ?  106 TRP   B CG  1 
ATOM   3316 C  CD1 . TRP   B 1 107 ? -4.191  -42.565 24.655 1.00 63.84  ?  106 TRP   B CD1 1 
ATOM   3317 C  CD2 . TRP   B 1 107 ? -3.396  -44.638 25.011 1.00 68.70  ?  106 TRP   B CD2 1 
ATOM   3318 N  NE1 . TRP   B 1 107 ? -3.425  -42.527 25.797 1.00 70.15  ?  106 TRP   B NE1 1 
ATOM   3319 C  CE2 . TRP   B 1 107 ? -2.923  -43.781 26.041 1.00 72.77  ?  106 TRP   B CE2 1 
ATOM   3320 C  CE3 . TRP   B 1 107 ? -3.023  -45.998 25.032 1.00 69.15  ?  106 TRP   B CE3 1 
ATOM   3321 C  CZ2 . TRP   B 1 107 ? -2.096  -44.239 27.087 1.00 70.94  ?  106 TRP   B CZ2 1 
ATOM   3322 C  CZ3 . TRP   B 1 107 ? -2.196  -46.454 26.071 1.00 70.86  ?  106 TRP   B CZ3 1 
ATOM   3323 C  CH2 . TRP   B 1 107 ? -1.745  -45.571 27.086 1.00 71.92  ?  106 TRP   B CH2 1 
ATOM   3324 N  N   . ALA   B 1 108 ? -1.621  -44.118 22.266 1.00 49.50  ?  107 ALA   B N   1 
ATOM   3325 C  CA  . ALA   B 1 108 ? -0.369  -44.647 22.771 1.00 50.78  ?  107 ALA   B CA  1 
ATOM   3326 C  C   . ALA   B 1 108 ? 0.325   -43.531 23.533 1.00 55.05  ?  107 ALA   B C   1 
ATOM   3327 O  O   . ALA   B 1 108 ? 0.128   -42.352 23.227 1.00 54.57  ?  107 ALA   B O   1 
ATOM   3328 C  CB  . ALA   B 1 108 ? 0.539   -45.154 21.651 1.00 41.78  ?  107 ALA   B CB  1 
ATOM   3329 N  N   . ASP   B 1 109 ? 1.097   -43.910 24.555 1.00 44.40  ?  108 ASP   B N   1 
ATOM   3330 C  CA  . ASP   B 1 109 ? 2.136   -43.049 25.105 1.00 43.01  ?  108 ASP   B CA  1 
ATOM   3331 C  C   . ASP   B 1 109 ? 1.739   -41.576 25.263 1.00 50.36  ?  108 ASP   B C   1 
ATOM   3332 O  O   . ASP   B 1 109 ? 2.579   -40.701 25.016 1.00 54.01  ?  108 ASP   B O   1 
ATOM   3333 C  CB  . ASP   B 1 109 ? 3.388   -43.064 24.208 1.00 43.46  ?  108 ASP   B CB  1 
ATOM   3334 C  CG  . ASP   B 1 109 ? 3.948   -44.462 23.908 1.00 46.30  ?  108 ASP   B CG  1 
ATOM   3335 O  OD1 . ASP   B 1 109 ? 3.328   -45.504 24.213 1.00 53.97  ?  108 ASP   B OD1 1 
ATOM   3336 O  OD2 . ASP   B 1 109 ? 5.071   -44.506 23.356 1.00 38.92  -1 108 ASP   B OD2 1 
ATOM   3337 N  N   . ASN   B 1 110 ? 0.480   -41.266 25.598 1.00 46.06  ?  109 ASN   B N   1 
ATOM   3338 C  CA  . ASN   B 1 110 ? 0.035   -39.876 25.810 1.00 50.56  ?  109 ASN   B CA  1 
ATOM   3339 C  C   . ASN   B 1 110 ? -0.092  -39.059 24.519 1.00 51.94  ?  109 ASN   B C   1 
ATOM   3340 O  O   . ASN   B 1 110 ? 0.093   -37.833 24.543 1.00 47.69  ?  109 ASN   B O   1 
ATOM   3341 C  CB  . ASN   B 1 110 ? 0.973   -39.098 26.751 1.00 53.05  ?  109 ASN   B CB  1 
ATOM   3342 C  CG  . ASN   B 1 110 ? 0.742   -39.397 28.199 1.00 53.38  ?  109 ASN   B CG  1 
ATOM   3343 O  OD1 . ASN   B 1 110 ? 1.698   -39.648 28.918 1.00 53.54  ?  109 ASN   B OD1 1 
ATOM   3344 N  ND2 . ASN   B 1 110 ? -0.520  -39.368 28.647 1.00 51.46  ?  109 ASN   B ND2 1 
ATOM   3345 N  N   . ASN   B 1 111 ? -0.423  -39.667 23.379 1.00 53.42  ?  110 ASN   B N   1 
ATOM   3346 C  CA  . ASN   B 1 111 ? -0.450  -38.895 22.140 1.00 47.09  ?  110 ASN   B CA  1 
ATOM   3347 C  C   . ASN   B 1 111 ? -1.793  -38.235 21.839 1.00 43.98  ?  110 ASN   B C   1 
ATOM   3348 O  O   . ASN   B 1 111 ? -1.958  -37.726 20.731 1.00 44.25  ?  110 ASN   B O   1 
ATOM   3349 C  CB  . ASN   B 1 111 ? -0.056  -39.765 20.958 1.00 46.02  ?  110 ASN   B CB  1 
ATOM   3350 C  CG  . ASN   B 1 111 ? -0.901  -40.988 20.869 1.00 52.61  ?  110 ASN   B CG  1 
ATOM   3351 O  OD1 . ASN   B 1 111 ? -1.897  -41.110 21.590 1.00 47.52  ?  110 ASN   B OD1 1 
ATOM   3352 N  ND2 . ASN   B 1 111 ? -0.513  -41.923 19.995 1.00 52.92  ?  110 ASN   B ND2 1 
ATOM   3353 N  N   . SER   B 1 112 ? -2.735  -38.191 22.787 1.00 42.98  ?  111 SER   B N   1 
ATOM   3354 C  CA  . SER   B 1 112 ? -4.011  -37.535 22.508 1.00 44.87  ?  111 SER   B CA  1 
ATOM   3355 C  C   . SER   B 1 112 ? -3.786  -36.174 21.847 1.00 47.74  ?  111 SER   B C   1 
ATOM   3356 O  O   . SER   B 1 112 ? -4.319  -35.906 20.763 1.00 49.44  ?  111 SER   B O   1 
ATOM   3357 C  CB  . SER   B 1 112 ? -4.871  -37.394 23.782 1.00 46.40  ?  111 SER   B CB  1 
ATOM   3358 O  OG  . SER   B 1 112 ? -4.264  -36.651 24.845 1.00 45.83  ?  111 SER   B OG  1 
ATOM   3359 N  N   . TYR   B 1 113 ? -2.946  -35.326 22.455 1.00 44.51  ?  112 TYR   B N   1 
ATOM   3360 C  CA  . TYR   B 1 113 ? -2.736  -33.980 21.928 1.00 45.57  ?  112 TYR   B CA  1 
ATOM   3361 C  C   . TYR   B 1 113 ? -2.079  -34.025 20.548 1.00 49.04  ?  112 TYR   B C   1 
ATOM   3362 O  O   . TYR   B 1 113 ? -2.252  -33.100 19.740 1.00 40.39  ?  112 TYR   B O   1 
ATOM   3363 C  CB  . TYR   B 1 113 ? -1.891  -33.149 22.904 1.00 42.45  ?  112 TYR   B CB  1 
ATOM   3364 C  CG  . TYR   B 1 113 ? -0.384  -33.393 22.758 1.00 46.25  ?  112 TYR   B CG  1 
ATOM   3365 C  CD1 . TYR   B 1 113 ? 0.207   -34.569 23.234 1.00 47.72  ?  112 TYR   B CD1 1 
ATOM   3366 C  CD2 . TYR   B 1 113 ? 0.440   -32.456 22.136 1.00 39.81  ?  112 TYR   B CD2 1 
ATOM   3367 C  CE1 . TYR   B 1 113 ? 1.569   -34.802 23.090 1.00 44.65  ?  112 TYR   B CE1 1 
ATOM   3368 C  CE2 . TYR   B 1 113 ? 1.794   -32.679 21.982 1.00 38.56  ?  112 TYR   B CE2 1 
ATOM   3369 C  CZ  . TYR   B 1 113 ? 2.357   -33.852 22.467 1.00 44.63  ?  112 TYR   B CZ  1 
ATOM   3370 O  OH  . TYR   B 1 113 ? 3.711   -34.077 22.308 1.00 45.83  ?  112 TYR   B OH  1 
ATOM   3371 N  N   . LEU   B 1 114 ? -1.343  -35.098 20.246 1.00 45.48  ?  113 LEU   B N   1 
ATOM   3372 C  CA  . LEU   B 1 114 ? -0.697  -35.181 18.939 1.00 45.87  ?  113 LEU   B CA  1 
ATOM   3373 C  C   . LEU   B 1 114 ? -1.703  -35.579 17.849 1.00 43.89  ?  113 LEU   B C   1 
ATOM   3374 O  O   . LEU   B 1 114 ? -1.668  -35.037 16.740 1.00 42.07  ?  113 LEU   B O   1 
ATOM   3375 C  CB  . LEU   B 1 114 ? 0.478   -36.166 19.012 1.00 43.72  ?  113 LEU   B CB  1 
ATOM   3376 C  CG  . LEU   B 1 114 ? 1.840   -35.606 19.454 1.00 40.21  ?  113 LEU   B CG  1 
ATOM   3377 C  CD1 . LEU   B 1 114 ? 2.925   -36.672 19.480 1.00 47.32  ?  113 LEU   B CD1 1 
ATOM   3378 C  CD2 . LEU   B 1 114 ? 2.284   -34.465 18.594 1.00 39.53  ?  113 LEU   B CD2 1 
ATOM   3379 N  N   . ALA   B 1 115 ? -2.637  -36.489 18.161 1.00 47.72  ?  114 ALA   B N   1 
ATOM   3380 C  CA  . ALA   B 1 115 ? -3.669  -36.878 17.200 1.00 44.85  ?  114 ALA   B CA  1 
ATOM   3381 C  C   . ALA   B 1 115 ? -4.642  -35.733 16.900 1.00 44.48  ?  114 ALA   B C   1 
ATOM   3382 O  O   . ALA   B 1 115 ? -5.057  -35.571 15.751 1.00 48.04  ?  114 ALA   B O   1 
ATOM   3383 C  CB  . ALA   B 1 115 ? -4.417  -38.113 17.698 1.00 35.52  ?  114 ALA   B CB  1 
ATOM   3384 N  N   . THR   B 1 116 ? -5.015  -34.923 17.901 1.00 40.60  ?  115 THR   B N   1 
ATOM   3385 C  CA  . THR   B 1 116 ? -5.859  -33.754 17.629 1.00 45.74  ?  115 THR   B CA  1 
ATOM   3386 C  C   . THR   B 1 116 ? -5.137  -32.728 16.754 1.00 48.25  ?  115 THR   B C   1 
ATOM   3387 O  O   . THR   B 1 116 ? -5.771  -31.967 16.010 1.00 47.92  ?  115 THR   B O   1 
ATOM   3388 C  CB  . THR   B 1 116 ? -6.278  -33.101 18.948 1.00 49.97  ?  115 THR   B CB  1 
ATOM   3389 O  OG1 . THR   B 1 116 ? -6.944  -34.072 19.756 1.00 55.44  ?  115 THR   B OG1 1 
ATOM   3390 C  CG2 . THR   B 1 116 ? -7.198  -31.882 18.726 1.00 45.59  ?  115 THR   B CG2 1 
ATOM   3391 N  N   . ALA   B 1 117 ? -3.814  -32.682 16.844 1.00 44.90  ?  116 ALA   B N   1 
ATOM   3392 C  CA  . ALA   B 1 117 ? -3.051  -31.747 16.044 1.00 40.76  ?  116 ALA   B CA  1 
ATOM   3393 C  C   . ALA   B 1 117 ? -2.813  -32.270 14.637 1.00 45.55  ?  116 ALA   B C   1 
ATOM   3394 O  O   . ALA   B 1 117 ? -2.721  -31.470 13.695 1.00 47.31  ?  116 ALA   B O   1 
ATOM   3395 C  CB  . ALA   B 1 117 ? -1.725  -31.457 16.726 1.00 32.48  ?  116 ALA   B CB  1 
ATOM   3396 N  N   . LEU   B 1 118 ? -2.673  -33.589 14.475 1.00 40.53  ?  117 LEU   B N   1 
ATOM   3397 C  CA  . LEU   B 1 118 ? -2.652  -34.166 13.134 1.00 41.12  ?  117 LEU   B CA  1 
ATOM   3398 C  C   . LEU   B 1 118 ? -3.967  -33.905 12.415 1.00 51.16  ?  117 LEU   B C   1 
ATOM   3399 O  O   . LEU   B 1 118 ? -3.993  -33.363 11.297 1.00 50.22  ?  117 LEU   B O   1 
ATOM   3400 C  CB  . LEU   B 1 118 ? -2.412  -35.661 13.213 1.00 38.72  ?  117 LEU   B CB  1 
ATOM   3401 C  CG  . LEU   B 1 118 ? -1.755  -36.281 11.998 1.00 39.81  ?  117 LEU   B CG  1 
ATOM   3402 C  CD1 . LEU   B 1 118 ? -0.511  -35.546 11.679 1.00 39.68  ?  117 LEU   B CD1 1 
ATOM   3403 C  CD2 . LEU   B 1 118 ? -1.426  -37.708 12.345 1.00 47.08  ?  117 LEU   B CD2 1 
ATOM   3404 N  N   . LEU   B 1 119 ? -5.073  -34.281 13.062 1.00 46.09  ?  118 LEU   B N   1 
ATOM   3405 C  CA  . LEU   B 1 119 ? -6.390  -34.145 12.469 1.00 47.66  ?  118 LEU   B CA  1 
ATOM   3406 C  C   . LEU   B 1 119 ? -6.665  -32.706 12.055 1.00 52.06  ?  118 LEU   B C   1 
ATOM   3407 O  O   . LEU   B 1 119 ? -7.263  -32.450 11.001 1.00 48.51  ?  118 LEU   B O   1 
ATOM   3408 C  CB  . LEU   B 1 119 ? -7.421  -34.641 13.473 1.00 50.46  ?  118 LEU   B CB  1 
ATOM   3409 C  CG  . LEU   B 1 119 ? -7.295  -36.142 13.729 1.00 49.46  ?  118 LEU   B CG  1 
ATOM   3410 C  CD1 . LEU   B 1 119 ? -8.157  -36.529 14.918 1.00 46.43  ?  118 LEU   B CD1 1 
ATOM   3411 C  CD2 . LEU   B 1 119 ? -7.668  -36.940 12.485 1.00 49.10  ?  118 LEU   B CD2 1 
ATOM   3412 N  N   . THR   B 1 120 ? -6.223  -31.752 12.872 1.00 54.21  ?  119 THR   B N   1 
ATOM   3413 C  CA  . THR   B 1 120 ? -6.422  -30.330 12.596 1.00 51.48  ?  119 THR   B CA  1 
ATOM   3414 C  C   . THR   B 1 120 ? -5.571  -29.879 11.407 1.00 46.10  ?  119 THR   B C   1 
ATOM   3415 O  O   . THR   B 1 120 ? -5.995  -29.043 10.603 1.00 48.54  ?  119 THR   B O   1 
ATOM   3416 C  CB  . THR   B 1 120 ? -6.081  -29.514 13.857 1.00 44.38  ?  119 THR   B CB  1 
ATOM   3417 O  OG1 . THR   B 1 120 ? -7.114  -29.690 14.822 1.00 51.98  ?  119 THR   B OG1 1 
ATOM   3418 C  CG2 . THR   B 1 120 ? -6.013  -28.028 13.536 1.00 39.06  ?  119 THR   B CG2 1 
ATOM   3419 N  N   . LEU   B 1 121 ? -4.358  -30.430 11.279 1.00 39.50  ?  120 LEU   B N   1 
ATOM   3420 C  CA  . LEU   B 1 121 ? -3.428  -29.934 10.278 1.00 46.48  ?  120 LEU   B CA  1 
ATOM   3421 C  C   . LEU   B 1 121 ? -3.801  -30.394 8.877  1.00 52.02  ?  120 LEU   B C   1 
ATOM   3422 O  O   . LEU   B 1 121 ? -3.267  -29.863 7.894  1.00 43.42  ?  120 LEU   B O   1 
ATOM   3423 C  CB  . LEU   B 1 121 ? -2.007  -30.365 10.633 1.00 45.73  ?  120 LEU   B CB  1 
ATOM   3424 C  CG  . LEU   B 1 121 ? -1.318  -29.427 11.627 1.00 48.84  ?  120 LEU   B CG  1 
ATOM   3425 C  CD1 . LEU   B 1 121 ? -0.088  -30.123 12.207 1.00 33.73  ?  120 LEU   B CD1 1 
ATOM   3426 C  CD2 . LEU   B 1 121 ? -0.959  -28.073 10.937 1.00 47.55  ?  120 LEU   B CD2 1 
ATOM   3427 N  N   . GLN   B 1 122 ? -4.707  -31.372 8.776  1.00 52.19  ?  121 GLN   B N   1 
ATOM   3428 C  CA  . GLN   B 1 122 ? -5.232  -31.844 7.513  1.00 45.40  ?  121 GLN   B CA  1 
ATOM   3429 C  C   . GLN   B 1 122 ? -6.488  -31.101 7.101  1.00 49.51  ?  121 GLN   B C   1 
ATOM   3430 O  O   . GLN   B 1 122 ? -6.949  -31.294 5.973  1.00 48.60  ?  121 GLN   B O   1 
ATOM   3431 C  CB  . GLN   B 1 122 ? -5.542  -33.349 7.598  1.00 47.89  ?  121 GLN   B CB  1 
ATOM   3432 C  CG  . GLN   B 1 122 ? -4.356  -34.203 8.033  1.00 50.91  ?  121 GLN   B CG  1 
ATOM   3433 C  CD  . GLN   B 1 122 ? -4.747  -35.620 8.412  1.00 56.60  ?  121 GLN   B CD  1 
ATOM   3434 O  OE1 . GLN   B 1 122 ? -4.994  -36.455 7.549  1.00 63.29  ?  121 GLN   B OE1 1 
ATOM   3435 N  NE2 . GLN   B 1 122 ? -4.841  -35.887 9.720  1.00 52.32  ?  121 GLN   B NE2 1 
ATOM   3436 N  N   . GLN   B 1 123 ? -7.041  -30.247 7.983  1.00 44.79  ?  122 GLN   B N   1 
ATOM   3437 C  CA  . GLN   B 1 123 ? -8.253  -29.487 7.698  1.00 43.57  ?  122 GLN   B CA  1 
ATOM   3438 C  C   . GLN   B 1 123 ? -8.047  -27.983 7.609  1.00 46.18  ?  122 GLN   B C   1 
ATOM   3439 O  O   . GLN   B 1 123 ? -9.028  -27.251 7.452  1.00 52.52  ?  122 GLN   B O   1 
ATOM   3440 C  CB  . GLN   B 1 123 ? -9.316  -29.755 8.762  1.00 39.78  ?  122 GLN   B CB  1 
ATOM   3441 C  CG  . GLN   B 1 123 ? -9.695  -31.202 8.881  1.00 44.13  ?  122 GLN   B CG  1 
ATOM   3442 C  CD  . GLN   B 1 123 ? -10.660 -31.430 10.024 1.00 48.04  ?  122 GLN   B CD  1 
ATOM   3443 O  OE1 . GLN   B 1 123 ? -11.733 -30.840 10.067 1.00 46.36  ?  122 GLN   B OE1 1 
ATOM   3444 N  NE2 . GLN   B 1 123 ? -10.248 -32.243 10.996 1.00 54.69  ?  122 GLN   B NE2 1 
ATOM   3445 N  N   . ILE   B 1 124 ? -6.829  -27.488 7.765  1.00 44.75  ?  123 ILE   B N   1 
ATOM   3446 C  CA  . ILE   B 1 124 ? -6.564  -26.065 7.624  1.00 39.70  ?  123 ILE   B CA  1 
ATOM   3447 C  C   . ILE   B 1 124 ? -5.485  -25.948 6.560  1.00 47.29  ?  123 ILE   B C   1 
ATOM   3448 O  O   . ILE   B 1 124 ? -4.663  -26.857 6.387  1.00 46.66  ?  123 ILE   B O   1 
ATOM   3449 C  CB  . ILE   B 1 124 ? -6.139  -25.401 8.965  1.00 47.34  ?  123 ILE   B CB  1 
ATOM   3450 C  CG1 . ILE   B 1 124 ? -5.002  -26.176 9.636  1.00 45.38  ?  123 ILE   B CG1 1 
ATOM   3451 C  CG2 . ILE   B 1 124 ? -7.310  -25.311 9.970  1.00 39.35  ?  123 ILE   B CG2 1 
ATOM   3452 C  CD1 . ILE   B 1 124 ? -4.005  -25.272 10.324 1.00 41.69  ?  123 ILE   B CD1 1 
ATOM   3453 N  N   . GLU   B 1 125 ? -5.523  -24.862 5.798  1.00 49.77  ?  124 GLU   B N   1 
ATOM   3454 C  CA  . GLU   B 1 125 ? -4.611  -24.702 4.674  1.00 51.88  ?  124 GLU   B CA  1 
ATOM   3455 C  C   . GLU   B 1 125 ? -3.296  -24.127 5.187  1.00 53.19  ?  124 GLU   B C   1 
ATOM   3456 O  O   . GLU   B 1 125 ? -3.286  -23.111 5.894  1.00 49.44  ?  124 GLU   B O   1 
ATOM   3457 C  CB  . GLU   B 1 125 ? -5.227  -23.801 3.596  1.00 61.17  ?  124 GLU   B CB  1 
ATOM   3458 C  CG  . GLU   B 1 125 ? -5.754  -24.531 2.308  1.00 74.45  ?  124 GLU   B CG  1 
ATOM   3459 C  CD  . GLU   B 1 125 ? -4.972  -25.819 1.904  1.00 80.17  ?  124 GLU   B CD  1 
ATOM   3460 O  OE1 . GLU   B 1 125 ? -5.585  -26.926 1.870  1.00 71.42  ?  124 GLU   B OE1 1 
ATOM   3461 O  OE2 . GLU   B 1 125 ? -3.750  -25.722 1.590  1.00 80.81  -1 124 GLU   B OE2 1 
ATOM   3462 N  N   . LEU   B 1 126 ? -2.186  -24.762 4.817  1.00 49.30  ?  125 LEU   B N   1 
ATOM   3463 C  CA  . LEU   B 1 126 ? -0.950  -24.400 5.482  1.00 39.71  ?  125 LEU   B CA  1 
ATOM   3464 C  C   . LEU   B 1 126 ? 0.254   -24.982 4.741  1.00 49.90  ?  125 LEU   B C   1 
ATOM   3465 O  O   . LEU   B 1 126 ? 0.193   -26.100 4.220  1.00 48.90  ?  125 LEU   B O   1 
ATOM   3466 C  CB  . LEU   B 1 126 ? -1.004  -24.897 6.921  1.00 39.59  ?  125 LEU   B CB  1 
ATOM   3467 C  CG  . LEU   B 1 126 ? 0.219   -24.528 7.725  1.00 44.49  ?  125 LEU   B CG  1 
ATOM   3468 C  CD1 . LEU   B 1 126 ? -0.170  -23.755 8.959  1.00 46.69  ?  125 LEU   B CD1 1 
ATOM   3469 C  CD2 . LEU   B 1 126 ? 0.874   -25.814 8.072  1.00 47.12  ?  125 LEU   B CD2 1 
ATOM   3470 N  N   . LYS   B 1 127 ? 1.347   -24.218 4.706  1.00 52.00  ?  126 LYS   B N   1 
ATOM   3471 C  CA  . LYS   B 1 127 ? 2.577   -24.627 4.041  1.00 50.52  ?  126 LYS   B CA  1 
ATOM   3472 C  C   . LYS   B 1 127 ? 3.756   -24.533 5.011  1.00 55.86  ?  126 LYS   B C   1 
ATOM   3473 O  O   . LYS   B 1 127 ? 3.932   -23.508 5.675  1.00 56.47  ?  126 LYS   B O   1 
ATOM   3474 C  CB  . LYS   B 1 127 ? 2.821   -23.748 2.824  1.00 54.44  ?  126 LYS   B CB  1 
ATOM   3475 C  CG  . LYS   B 1 127 ? 3.789   -24.336 1.826  1.00 62.01  ?  126 LYS   B CG  1 
ATOM   3476 C  CD  . LYS   B 1 127 ? 5.162   -23.720 2.019  1.00 63.30  ?  126 LYS   B CD  1 
ATOM   3477 C  CE  . LYS   B 1 127 ? 6.267   -24.620 1.493  1.00 62.08  ?  126 LYS   B CE  1 
ATOM   3478 N  NZ  . LYS   B 1 127 ? 7.563   -23.873 1.550  1.00 68.43  ?  126 LYS   B NZ  1 
ATOM   3479 N  N   . PHE   B 1 128 ? 4.569   -25.591 5.082  1.00 52.99  ?  127 PHE   B N   1 
ATOM   3480 C  CA  . PHE   B 1 128 ? 5.715   -25.659 5.985  1.00 51.60  ?  127 PHE   B CA  1 
ATOM   3481 C  C   . PHE   B 1 128 ? 6.996   -25.381 5.210  1.00 49.98  ?  127 PHE   B C   1 
ATOM   3482 O  O   . PHE   B 1 128 ? 7.287   -26.064 4.228  1.00 48.87  ?  127 PHE   B O   1 
ATOM   3483 C  CB  . PHE   B 1 128 ? 5.830   -27.032 6.671  1.00 47.62  ?  127 PHE   B CB  1 
ATOM   3484 C  CG  . PHE   B 1 128 ? 4.839   -27.249 7.760  1.00 41.09  ?  127 PHE   B CG  1 
ATOM   3485 C  CD1 . PHE   B 1 128 ? 3.888   -28.269 7.654  1.00 42.71  ?  127 PHE   B CD1 1 
ATOM   3486 C  CD2 . PHE   B 1 128 ? 4.828   -26.427 8.873  1.00 42.52  ?  127 PHE   B CD2 1 
ATOM   3487 C  CE1 . PHE   B 1 128 ? 2.936   -28.477 8.629  1.00 35.78  ?  127 PHE   B CE1 1 
ATOM   3488 C  CE2 . PHE   B 1 128 ? 3.884   -26.616 9.877  1.00 41.92  ?  127 PHE   B CE2 1 
ATOM   3489 C  CZ  . PHE   B 1 128 ? 2.942   -27.654 9.758  1.00 47.28  ?  127 PHE   B CZ  1 
ATOM   3490 N  N   . ASN   B 1 129 ? 7.784   -24.420 5.691  1.00 50.92  ?  128 ASN   B N   1 
ATOM   3491 C  CA  . ASN   B 1 129 ? 9.012   -24.018 5.017  1.00 45.35  ?  128 ASN   B CA  1 
ATOM   3492 C  C   . ASN   B 1 129 ? 10.166  -25.021 5.137  1.00 47.08  ?  128 ASN   B C   1 
ATOM   3493 O  O   . ASN   B 1 129 ? 10.990  -25.097 4.227  1.00 51.84  ?  128 ASN   B O   1 
ATOM   3494 C  CB  . ASN   B 1 129 ? 9.458   -22.652 5.536  1.00 46.81  ?  128 ASN   B CB  1 
ATOM   3495 C  CG  . ASN   B 1 129 ? 8.580   -21.536 5.030  1.00 57.92  ?  128 ASN   B CG  1 
ATOM   3496 O  OD1 . ASN   B 1 129 ? 8.606   -21.208 3.833  1.00 65.57  ?  128 ASN   B OD1 1 
ATOM   3497 N  ND2 . ASN   B 1 129 ? 7.813   -20.915 5.939  1.00 53.44  ?  128 ASN   B ND2 1 
ATOM   3498 N  N   . PRO   B 1 130 ? 10.332  -25.773 6.217  1.00 50.11  ?  129 PRO   B N   1 
ATOM   3499 C  CA  . PRO   B 1 130 ? 11.398  -26.775 6.203  1.00 48.08  ?  129 PRO   B CA  1 
ATOM   3500 C  C   . PRO   B 1 130 ? 11.011  -27.958 5.334  1.00 50.87  ?  129 PRO   B C   1 
ATOM   3501 O  O   . PRO   B 1 130 ? 9.969   -28.599 5.551  1.00 46.77  ?  129 PRO   B O   1 
ATOM   3502 C  CB  . PRO   B 1 130 ? 11.549  -27.167 7.682  1.00 46.26  ?  129 PRO   B CB  1 
ATOM   3503 C  CG  . PRO   B 1 130 ? 11.006  -25.975 8.449  1.00 45.54  ?  129 PRO   B CG  1 
ATOM   3504 C  CD  . PRO   B 1 130 ? 9.878   -25.484 7.598  1.00 50.69  ?  129 PRO   B CD  1 
ATOM   3505 N  N   . PRO   B 1 131 ? 11.805  -28.246 4.302  1.00 51.64  ?  130 PRO   B N   1 
ATOM   3506 C  CA  . PRO   B 1 131 ? 11.560  -29.433 3.478  1.00 48.85  ?  130 PRO   B CA  1 
ATOM   3507 C  C   . PRO   B 1 131 ? 11.210  -30.682 4.270  1.00 53.06  ?  130 PRO   B C   1 
ATOM   3508 O  O   . PRO   B 1 131 ? 10.189  -31.319 3.979  1.00 52.56  ?  130 PRO   B O   1 
ATOM   3509 C  CB  . PRO   B 1 131 ? 12.887  -29.612 2.725  1.00 40.65  ?  130 PRO   B CB  1 
ATOM   3510 C  CG  . PRO   B 1 131 ? 13.414  -28.255 2.577  1.00 34.62  ?  130 PRO   B CG  1 
ATOM   3511 C  CD  . PRO   B 1 131 ? 12.909  -27.431 3.762  1.00 52.77  ?  130 PRO   B CD  1 
ATOM   3512 N  N   . ALA   B 1 132 ? 12.027  -31.048 5.266  1.00 54.05  ?  131 ALA   B N   1 
ATOM   3513 C  CA  . ALA   B 1 132 ? 11.757  -32.287 5.994  1.00 50.36  ?  131 ALA   B CA  1 
ATOM   3514 C  C   . ALA   B 1 132 ? 10.379  -32.246 6.650  1.00 42.32  ?  131 ALA   B C   1 
ATOM   3515 O  O   . ALA   B 1 132 ? 9.646   -33.239 6.636  1.00 43.00  ?  131 ALA   B O   1 
ATOM   3516 C  CB  . ALA   B 1 132 ? 12.852  -32.541 7.026  1.00 49.22  ?  131 ALA   B CB  1 
ATOM   3517 N  N   . LEU   B 1 133 ? 9.991   -31.090 7.183  1.00 40.69  ?  132 LEU   B N   1 
ATOM   3518 C  CA  . LEU   B 1 133 ? 8.658   -30.935 7.761  1.00 43.37  ?  132 LEU   B CA  1 
ATOM   3519 C  C   . LEU   B 1 133 ? 7.563   -31.115 6.711  1.00 45.69  ?  132 LEU   B C   1 
ATOM   3520 O  O   . LEU   B 1 133 ? 6.573   -31.828 6.938  1.00 37.87  ?  132 LEU   B O   1 
ATOM   3521 C  CB  . LEU   B 1 133 ? 8.549   -29.560 8.403  1.00 43.08  ?  132 LEU   B CB  1 
ATOM   3522 C  CG  . LEU   B 1 133 ? 7.491   -29.444 9.466  1.00 42.24  ?  132 LEU   B CG  1 
ATOM   3523 C  CD1 . LEU   B 1 133 ? 7.502   -30.709 10.307 1.00 40.20  ?  132 LEU   B CD1 1 
ATOM   3524 C  CD2 . LEU   B 1 133 ? 7.773   -28.205 10.285 1.00 40.37  ?  132 LEU   B CD2 1 
ATOM   3525 N  N   . GLN   B 1 134 ? 7.733   -30.468 5.545  1.00 49.83  ?  133 GLN   B N   1 
ATOM   3526 C  CA  . GLN   B 1 134 ? 6.740   -30.549 4.477  1.00 42.20  ?  133 GLN   B CA  1 
ATOM   3527 C  C   . GLN   B 1 134 ? 6.655   -31.955 3.870  1.00 43.69  ?  133 GLN   B C   1 
ATOM   3528 O  O   . GLN   B 1 134 ? 5.547   -32.472 3.675  1.00 41.35  ?  133 GLN   B O   1 
ATOM   3529 C  CB  . GLN   B 1 134 ? 7.047   -29.507 3.411  1.00 46.79  ?  133 GLN   B CB  1 
ATOM   3530 C  CG  . GLN   B 1 134 ? 5.956   -29.399 2.341  1.00 47.60  ?  133 GLN   B CG  1 
ATOM   3531 C  CD  . GLN   B 1 134 ? 4.674   -28.776 2.877  1.00 50.54  ?  133 GLN   B CD  1 
ATOM   3532 O  OE1 . GLN   B 1 134 ? 4.603   -28.342 4.033  1.00 51.10  ?  133 GLN   B OE1 1 
ATOM   3533 N  NE2 . GLN   B 1 134 ? 3.644   -28.763 2.050  1.00 52.10  ?  133 GLN   B NE2 1 
ATOM   3534 N  N   . ASP   B 1 135 ? 7.798   -32.599 3.571  1.00 41.05  ?  134 ASP   B N   1 
ATOM   3535 C  CA  . ASP   B 1 135 ? 7.756   -34.001 3.138  1.00 42.59  ?  134 ASP   B CA  1 
ATOM   3536 C  C   . ASP   B 1 135 ? 6.955   -34.864 4.111  1.00 50.87  ?  134 ASP   B C   1 
ATOM   3537 O  O   . ASP   B 1 135 ? 6.117   -35.671 3.688  1.00 54.32  ?  134 ASP   B O   1 
ATOM   3538 C  CB  . ASP   B 1 135 ? 9.156   -34.597 2.989  1.00 34.18  ?  134 ASP   B CB  1 
ATOM   3539 C  CG  . ASP   B 1 135 ? 10.068  -33.761 2.120  1.00 56.60  ?  134 ASP   B CG  1 
ATOM   3540 O  OD1 . ASP   B 1 135 ? 9.589   -32.736 1.556  1.00 62.99  ?  134 ASP   B OD1 1 
ATOM   3541 O  OD2 . ASP   B 1 135 ? 11.268  -34.141 1.988  1.00 60.20  -1 134 ASP   B OD2 1 
ATOM   3542 N  N   . ALA   B 1 136 ? 7.200   -34.714 5.424  1.00 46.02  ?  135 ALA   B N   1 
ATOM   3543 C  CA  . ALA   B 1 136 ? 6.483   -35.530 6.391  1.00 40.85  ?  135 ALA   B CA  1 
ATOM   3544 C  C   . ALA   B 1 136 ? 5.000   -35.189 6.399  1.00 42.42  ?  135 ALA   B C   1 
ATOM   3545 O  O   . ALA   B 1 136 ? 4.147   -36.081 6.496  1.00 47.67  ?  135 ALA   B O   1 
ATOM   3546 C  CB  . ALA   B 1 136 ? 7.090   -35.345 7.776  1.00 43.36  ?  135 ALA   B CB  1 
ATOM   3547 N  N   . TYR   B 1 137 ? 4.687   -33.905 6.199  1.00 37.69  ?  136 TYR   B N   1 
ATOM   3548 C  CA  . TYR   B 1 137 ? 3.268   -33.467 6.107  1.00 41.57  ?  136 TYR   B CA  1 
ATOM   3549 C  C   . TYR   B 1 137 ? 2.555   -34.277 5.026  1.00 45.94  ?  136 TYR   B C   1 
ATOM   3550 O  O   . TYR   B 1 137 ? 1.460   -34.814 5.296  1.00 41.51  ?  136 TYR   B O   1 
ATOM   3551 C  CB  . TYR   B 1 137 ? 3.307   -31.974 5.774  1.00 40.14  ?  136 TYR   B CB  1 
ATOM   3552 C  CG  . TYR   B 1 137 ? 2.099   -31.132 6.156  1.00 39.85  ?  136 TYR   B CG  1 
ATOM   3553 C  CD1 . TYR   B 1 137 ? 1.286   -31.472 7.230  1.00 35.11  ?  136 TYR   B CD1 1 
ATOM   3554 C  CD2 . TYR   B 1 137 ? 1.786   -29.981 5.443  1.00 44.37  ?  136 TYR   B CD2 1 
ATOM   3555 C  CE1 . TYR   B 1 137 ? 0.195   -30.693 7.580  1.00 35.26  ?  136 TYR   B CE1 1 
ATOM   3556 C  CE2 . TYR   B 1 137 ? 0.699   -29.195 5.783  1.00 41.00  ?  136 TYR   B CE2 1 
ATOM   3557 C  CZ  . TYR   B 1 137 ? -0.099  -29.552 6.854  1.00 36.60  ?  136 TYR   B CZ  1 
ATOM   3558 O  OH  . TYR   B 1 137 ? -1.167  -28.771 7.182  1.00 45.18  ?  136 TYR   B OH  1 
ATOM   3559 N  N   . TYR   B 1 138 ? 3.146   -34.353 3.828  1.00 38.62  ?  137 TYR   B N   1 
ATOM   3560 C  CA  . TYR   B 1 138 ? 2.550   -35.121 2.737  1.00 39.06  ?  137 TYR   B CA  1 
ATOM   3561 C  C   . TYR   B 1 138 ? 2.361   -36.587 3.125  1.00 47.76  ?  137 TYR   B C   1 
ATOM   3562 O  O   . TYR   B 1 138 ? 1.229   -37.098 3.121  1.00 50.51  ?  137 TYR   B O   1 
ATOM   3563 C  CB  . TYR   B 1 138 ? 3.394   -35.011 1.466  1.00 40.18  ?  137 TYR   B CB  1 
ATOM   3564 C  CG  . TYR   B 1 138 ? 3.395   -33.636 0.791  1.00 41.01  ?  137 TYR   B CG  1 
ATOM   3565 C  CD1 . TYR   B 1 138 ? 2.216   -32.916 0.570  1.00 40.48  ?  137 TYR   B CD1 1 
ATOM   3566 C  CD2 . TYR   B 1 138 ? 4.588   -33.063 0.375  1.00 36.89  ?  137 TYR   B CD2 1 
ATOM   3567 C  CE1 . TYR   B 1 138 ? 2.251   -31.659 -0.034 1.00 41.64  ?  137 TYR   B CE1 1 
ATOM   3568 C  CE2 . TYR   B 1 138 ? 4.627   -31.840 -0.225 1.00 35.67  ?  137 TYR   B CE2 1 
ATOM   3569 C  CZ  . TYR   B 1 138 ? 3.481   -31.132 -0.435 1.00 43.86  ?  137 TYR   B CZ  1 
ATOM   3570 O  OH  . TYR   B 1 138 ? 3.615   -29.891 -1.054 1.00 47.01  ?  137 TYR   B OH  1 
ATOM   3571 N  N   . ARG   B 1 139 ? 3.463   -37.288 3.463  1.00 45.04  ?  138 ARG   B N   1 
ATOM   3572 C  CA  . ARG   B 1 139 ? 3.352   -38.673 3.930  1.00 49.42  ?  138 ARG   B CA  1 
ATOM   3573 C  C   . ARG   B 1 139 ? 2.327   -38.824 5.053  1.00 51.16  ?  138 ARG   B C   1 
ATOM   3574 O  O   . ARG   B 1 139 ? 1.702   -39.883 5.192  1.00 47.91  ?  138 ARG   B O   1 
ATOM   3575 C  CB  . ARG   B 1 139 ? 4.690   -39.208 4.440  1.00 44.12  ?  138 ARG   B CB  1 
ATOM   3576 C  CG  . ARG   B 1 139 ? 5.791   -39.440 3.425  1.00 58.01  ?  138 ARG   B CG  1 
ATOM   3577 C  CD  . ARG   B 1 139 ? 5.390   -39.659 1.925  1.00 70.49  ?  138 ARG   B CD  1 
ATOM   3578 N  NE  . ARG   B 1 139 ? 4.747   -40.932 1.578  1.00 77.57  ?  138 ARG   B NE  1 
ATOM   3579 C  CZ  . ARG   B 1 139 ? 3.558   -41.055 0.994  1.00 72.85  ?  138 ARG   B CZ  1 
ATOM   3580 N  NH1 . ARG   B 1 139 ? 2.849   -39.994 0.637  1.00 72.76  ?  138 ARG   B NH1 1 
ATOM   3581 N  NH2 . ARG   B 1 139 ? 3.084   -42.273 0.735  1.00 74.45  ?  138 ARG   B NH2 1 
ATOM   3582 N  N   . ALA   B 1 140 ? 2.125   -37.780 5.859  1.00 48.19  ?  139 ALA   B N   1 
ATOM   3583 C  CA  . ALA   B 1 140 ? 1.203   -37.918 6.980  1.00 49.57  ?  139 ALA   B CA  1 
ATOM   3584 C  C   . ALA   B 1 140 ? -0.255  -38.014 6.516  1.00 49.95  ?  139 ALA   B C   1 
ATOM   3585 O  O   . ALA   B 1 140 ? -0.971  -38.933 6.938  1.00 48.86  ?  139 ALA   B O   1 
ATOM   3586 C  CB  . ALA   B 1 140 ? 1.403   -36.780 7.975  1.00 47.51  ?  139 ALA   B CB  1 
ATOM   3587 N  N   . ARG   B 1 141 ? -0.737  -37.077 5.661  1.00 49.20  ?  140 ARG   B N   1 
ATOM   3588 C  CA  . ARG   B 1 141 ? -2.116  -37.246 5.176  1.00 51.28  ?  140 ARG   B CA  1 
ATOM   3589 C  C   . ARG   B 1 141 ? -2.261  -38.525 4.379  1.00 49.68  ?  140 ARG   B C   1 
ATOM   3590 O  O   . ARG   B 1 141 ? -3.344  -39.115 4.349  1.00 51.89  ?  140 ARG   B O   1 
ATOM   3591 C  CB  . ARG   B 1 141 ? -2.634  -36.153 4.248  1.00 45.54  ?  140 ARG   B CB  1 
ATOM   3592 C  CG  . ARG   B 1 141 ? -1.992  -34.831 4.164  1.00 55.31  ?  140 ARG   B CG  1 
ATOM   3593 C  CD  . ARG   B 1 141 ? -2.633  -34.181 2.949  1.00 36.67  ?  140 ARG   B CD  1 
ATOM   3594 N  NE  . ARG   B 1 141 ? -3.815  -33.450 3.376  1.00 41.21  ?  140 ARG   B NE  1 
ATOM   3595 C  CZ  . ARG   B 1 141 ? -3.785  -32.231 3.897  1.00 44.92  ?  140 ARG   B CZ  1 
ATOM   3596 N  NH1 . ARG   B 1 141 ? -2.673  -31.500 3.891  1.00 37.50  ?  140 ARG   B NH1 1 
ATOM   3597 N  NH2 . ARG   B 1 141 ? -4.901  -31.727 4.430  1.00 47.55  ?  140 ARG   B NH2 1 
ATOM   3598 N  N   . ALA   B 1 142 ? -1.201  -38.933 3.681  1.00 49.22  ?  141 ALA   B N   1 
ATOM   3599 C  CA  . ALA   B 1 142 ? -1.248  -40.181 2.941  1.00 50.69  ?  141 ALA   B CA  1 
ATOM   3600 C  C   . ALA   B 1 142 ? -1.469  -41.383 3.859  1.00 52.37  ?  141 ALA   B C   1 
ATOM   3601 O  O   . ALA   B 1 142 ? -1.928  -42.428 3.384  1.00 52.51  ?  141 ALA   B O   1 
ATOM   3602 C  CB  . ALA   B 1 142 ? 0.039   -40.333 2.118  1.00 49.36  ?  141 ALA   B CB  1 
ATOM   3603 N  N   . GLY   B 1 143 ? -1.180  -41.253 5.159  1.00 54.88  ?  142 GLY   B N   1 
ATOM   3604 C  CA  . GLY   B 1 143 ? -1.357  -42.332 6.130  1.00 50.16  ?  142 GLY   B CA  1 
ATOM   3605 C  C   . GLY   B 1 143 ? -0.082  -42.834 6.805  1.00 49.16  ?  142 GLY   B C   1 
ATOM   3606 O  O   . GLY   B 1 143 ? -0.180  -43.670 7.709  1.00 54.65  ?  142 GLY   B O   1 
ATOM   3607 N  N   . GLU   B 1 144 ? 1.114   -42.386 6.444  1.00 50.80  ?  143 GLU   B N   1 
ATOM   3608 C  CA  . GLU   B 1 144 ? 2.346   -42.769 7.136  1.00 54.93  ?  143 GLU   B CA  1 
ATOM   3609 C  C   . GLU   B 1 144 ? 2.877   -41.591 7.952  1.00 54.29  ?  143 GLU   B C   1 
ATOM   3610 O  O   . GLU   B 1 144 ? 3.922   -40.999 7.640  1.00 54.68  ?  143 GLU   B O   1 
ATOM   3611 C  CB  . GLU   B 1 144 ? 3.381   -43.234 6.132  1.00 60.61  ?  143 GLU   B CB  1 
ATOM   3612 C  CG  . GLU   B 1 144 ? 2.985   -44.417 5.280  1.00 61.46  ?  143 GLU   B CG  1 
ATOM   3613 C  CD  . GLU   B 1 144 ? 4.106   -44.779 4.313  1.00 89.78  ?  143 GLU   B CD  1 
ATOM   3614 O  OE1 . GLU   B 1 144 ? 4.021   -45.851 3.667  1.00 91.92  ?  143 GLU   B OE1 1 
ATOM   3615 O  OE2 . GLU   B 1 144 ? 5.071   -43.970 4.191  1.00 91.17  -1 143 GLU   B OE2 1 
ATOM   3616 N  N   . ALA   B 1 145 ? 2.166   -41.272 9.036  1.00 47.41  ?  144 ALA   B N   1 
ATOM   3617 C  CA  . ALA   B 1 145 ? 2.458   -40.099 9.855  1.00 49.20  ?  144 ALA   B CA  1 
ATOM   3618 C  C   . ALA   B 1 145 ? 3.601   -40.292 10.884 1.00 46.22  ?  144 ALA   B C   1 
ATOM   3619 O  O   . ALA   B 1 145 ? 3.767   -39.431 11.759 1.00 43.53  ?  144 ALA   B O   1 
ATOM   3620 C  CB  . ALA   B 1 145 ? 1.186   -39.662 10.581 1.00 45.18  ?  144 ALA   B CB  1 
ATOM   3621 N  N   . ALA   B 1 146 ? 4.407   -41.354 10.806 1.00 46.23  ?  145 ALA   B N   1 
ATOM   3622 C  CA  . ALA   B 1 146 ? 5.428   -41.574 11.831 1.00 44.60  ?  145 ALA   B CA  1 
ATOM   3623 C  C   . ALA   B 1 146 ? 6.457   -40.446 11.847 1.00 47.46  ?  145 ALA   B C   1 
ATOM   3624 O  O   . ALA   B 1 146 ? 6.726   -39.855 12.901 1.00 49.21  ?  145 ALA   B O   1 
ATOM   3625 C  CB  . ALA   B 1 146 ? 6.116   -42.929 11.632 1.00 41.63  ?  145 ALA   B CB  1 
ATOM   3626 N  N   . ASN   B 1 147 ? 7.064   -40.147 10.695 1.00 49.22  ?  146 ASN   B N   1 
ATOM   3627 C  CA  . ASN   B 1 147 ? 8.062   -39.080 10.657 1.00 46.91  ?  146 ASN   B CA  1 
ATOM   3628 C  C   . ASN   B 1 147 ? 7.447   -37.752 11.041 1.00 46.67  ?  146 ASN   B C   1 
ATOM   3629 O  O   . ASN   B 1 147 ? 8.034   -36.999 11.827 1.00 53.90  ?  146 ASN   B O   1 
ATOM   3630 C  CB  . ASN   B 1 147 ? 8.719   -38.984 9.279  1.00 50.90  ?  146 ASN   B CB  1 
ATOM   3631 C  CG  . ASN   B 1 147 ? 9.202   -40.334 8.781  1.00 59.11  ?  146 ASN   B CG  1 
ATOM   3632 O  OD1 . ASN   B 1 147 ? 8.432   -41.092 8.178  1.00 62.57  ?  146 ASN   B OD1 1 
ATOM   3633 N  ND2 . ASN   B 1 147 ? 10.464  -40.664 9.065  1.00 57.83  ?  146 ASN   B ND2 1 
ATOM   3634 N  N   . PHE   B 1 148 ? 6.248   -37.458 10.536 1.00 46.38  ?  147 PHE   B N   1 
ATOM   3635 C  CA  . PHE   B 1 148 ? 5.635   -36.178 10.864 1.00 42.74  ?  147 PHE   B CA  1 
ATOM   3636 C  C   . PHE   B 1 148 ? 5.496   -36.010 12.372 1.00 44.85  ?  147 PHE   B C   1 
ATOM   3637 O  O   . PHE   B 1 148 ? 5.809   -34.943 12.915 1.00 41.20  ?  147 PHE   B O   1 
ATOM   3638 C  CB  . PHE   B 1 148 ? 4.277   -36.040 10.175 1.00 38.75  ?  147 PHE   B CB  1 
ATOM   3639 C  CG  . PHE   B 1 148 ? 3.731   -34.642 10.211 1.00 37.11  ?  147 PHE   B CG  1 
ATOM   3640 C  CD1 . PHE   B 1 148 ? 4.500   -33.574 9.766  1.00 34.64  ?  147 PHE   B CD1 1 
ATOM   3641 C  CD2 . PHE   B 1 148 ? 2.466   -34.389 10.722 1.00 37.56  ?  147 PHE   B CD2 1 
ATOM   3642 C  CE1 . PHE   B 1 148 ? 4.015   -32.281 9.812  1.00 32.30  ?  147 PHE   B CE1 1 
ATOM   3643 C  CE2 . PHE   B 1 148 ? 1.954   -33.093 10.764 1.00 36.60  ?  147 PHE   B CE2 1 
ATOM   3644 C  CZ  . PHE   B 1 148 ? 2.733   -32.038 10.310 1.00 37.36  ?  147 PHE   B CZ  1 
ATOM   3645 N  N   . CYS   B 1 149 ? 5.046   -37.064 13.064 1.00 46.61  ?  148 CYS   B N   1 
ATOM   3646 C  CA  . CYS   B 1 149 ? 4.895   -36.997 14.515 1.00 45.43  ?  148 CYS   B CA  1 
ATOM   3647 C  C   . CYS   B 1 149 ? 6.245   -36.879 15.204 1.00 43.25  ?  148 CYS   B C   1 
ATOM   3648 O  O   . CYS   B 1 149 ? 6.436   -36.017 16.068 1.00 46.33  ?  148 CYS   B O   1 
ATOM   3649 C  CB  . CYS   B 1 149 ? 4.145   -38.221 15.023 1.00 51.79  ?  148 CYS   B CB  1 
ATOM   3650 S  SG  . CYS   B 1 149 ? 2.450   -38.347 14.425 1.00 49.79  ?  148 CYS   B SG  1 
ATOM   3651 N  N   . ALA   B 1 150 ? 7.205   -37.726 14.827 1.00 49.60  ?  149 ALA   B N   1 
ATOM   3652 C  CA  . ALA   B 1 150 ? 8.530   -37.636 15.446 1.00 52.05  ?  149 ALA   B CA  1 
ATOM   3653 C  C   . ALA   B 1 150 ? 9.152   -36.256 15.246 1.00 48.20  ?  149 ALA   B C   1 
ATOM   3654 O  O   . ALA   B 1 150 ? 9.852   -35.772 16.138 1.00 48.13  ?  149 ALA   B O   1 
ATOM   3655 C  CB  . ALA   B 1 150 ? 9.459   -38.735 14.912 1.00 48.83  ?  149 ALA   B CB  1 
ATOM   3656 N  N   . LEU   B 1 151 ? 8.890   -35.599 14.104 1.00 48.76  ?  150 LEU   B N   1 
ATOM   3657 C  CA  . LEU   B 1 151 ? 9.383   -34.235 13.897 1.00 44.73  ?  150 LEU   B CA  1 
ATOM   3658 C  C   . LEU   B 1 151 ? 8.674   -33.242 14.812 1.00 45.44  ?  150 LEU   B C   1 
ATOM   3659 O  O   . LEU   B 1 151 ? 9.318   -32.382 15.429 1.00 45.69  ?  150 LEU   B O   1 
ATOM   3660 C  CB  . LEU   B 1 151 ? 9.208   -33.810 12.443 1.00 39.19  ?  150 LEU   B CB  1 
ATOM   3661 C  CG  . LEU   B 1 151 ? 10.267  -34.246 11.432 1.00 46.67  ?  150 LEU   B CG  1 
ATOM   3662 C  CD1 . LEU   B 1 151 ? 9.926   -33.650 10.076 1.00 40.81  ?  150 LEU   B CD1 1 
ATOM   3663 C  CD2 . LEU   B 1 151 ? 11.698  -33.893 11.860 1.00 43.84  ?  150 LEU   B CD2 1 
ATOM   3664 N  N   . ILE   B 1 152 ? 7.340   -33.332 14.897 1.00 46.21  ?  151 ILE   B N   1 
ATOM   3665 C  CA  . ILE   B 1 152 ? 6.581   -32.461 15.797 1.00 45.75  ?  151 ILE   B CA  1 
ATOM   3666 C  C   . ILE   B 1 152 ? 7.147   -32.538 17.213 1.00 50.43  ?  151 ILE   B C   1 
ATOM   3667 O  O   . ILE   B 1 152 ? 7.331   -31.511 17.881 1.00 49.37  ?  151 ILE   B O   1 
ATOM   3668 C  CB  . ILE   B 1 152 ? 5.083   -32.824 15.757 1.00 38.83  ?  151 ILE   B CB  1 
ATOM   3669 C  CG1 . ILE   B 1 152 ? 4.504   -32.514 14.364 1.00 46.88  ?  151 ILE   B CG1 1 
ATOM   3670 C  CG2 . ILE   B 1 152 ? 4.321   -32.067 16.794 1.00 31.25  ?  151 ILE   B CG2 1 
ATOM   3671 C  CD1 . ILE   B 1 152 ? 3.046   -32.905 14.178 1.00 38.58  ?  151 ILE   B CD1 1 
ATOM   3672 N  N   . LEU   B 1 153 ? 7.467   -33.752 17.678 1.00 41.89  ?  152 LEU   B N   1 
ATOM   3673 C  CA  . LEU   B 1 153 ? 8.043   -33.899 19.006 1.00 44.57  ?  152 LEU   B CA  1 
ATOM   3674 C  C   . LEU   B 1 153 ? 9.408   -33.225 19.096 1.00 48.85  ?  152 LEU   B C   1 
ATOM   3675 O  O   . LEU   B 1 153 ? 9.699   -32.521 20.076 1.00 52.65  ?  152 LEU   B O   1 
ATOM   3676 C  CB  . LEU   B 1 153 ? 8.138   -35.379 19.380 1.00 47.41  ?  152 LEU   B CB  1 
ATOM   3677 C  CG  . LEU   B 1 153 ? 6.795   -35.968 19.797 1.00 44.64  ?  152 LEU   B CG  1 
ATOM   3678 C  CD1 . LEU   B 1 153 ? 6.872   -37.467 19.893 1.00 40.73  ?  152 LEU   B CD1 1 
ATOM   3679 C  CD2 . LEU   B 1 153 ? 6.352   -35.347 21.107 1.00 42.00  ?  152 LEU   B CD2 1 
ATOM   3680 N  N   . ALA   B 1 154 ? 10.261  -33.413 18.088 1.00 42.80  ?  153 ALA   B N   1 
ATOM   3681 C  CA  . ALA   B 1 154 ? 11.566  -32.759 18.145 1.00 48.09  ?  153 ALA   B CA  1 
ATOM   3682 C  C   . ALA   B 1 154 ? 11.429  -31.243 18.053 1.00 46.77  ?  153 ALA   B C   1 
ATOM   3683 O  O   . ALA   B 1 154 ? 12.226  -30.513 18.650 1.00 43.94  ?  153 ALA   B O   1 
ATOM   3684 C  CB  . ALA   B 1 154 ? 12.494  -33.295 17.049 1.00 45.76  ?  153 ALA   B CB  1 
ATOM   3685 N  N   . TYR   B 1 155 ? 10.404  -30.745 17.353 1.00 48.50  ?  154 TYR   B N   1 
ATOM   3686 C  CA  . TYR   B 1 155 ? 10.273  -29.297 17.234 1.00 50.01  ?  154 TYR   B CA  1 
ATOM   3687 C  C   . TYR   B 1 155 ? 9.817   -28.680 18.539 1.00 47.39  ?  154 TYR   B C   1 
ATOM   3688 O  O   . TYR   B 1 155 ? 10.128  -27.522 18.814 1.00 55.69  ?  154 TYR   B O   1 
ATOM   3689 C  CB  . TYR   B 1 155 ? 9.320   -28.921 16.097 1.00 41.95  ?  154 TYR   B CB  1 
ATOM   3690 C  CG  . TYR   B 1 155 ? 9.995   -28.894 14.735 1.00 46.01  ?  154 TYR   B CG  1 
ATOM   3691 C  CD1 . TYR   B 1 155 ? 10.889  -27.881 14.412 1.00 45.50  ?  154 TYR   B CD1 1 
ATOM   3692 C  CD2 . TYR   B 1 155 ? 9.752   -29.892 13.774 1.00 46.17  ?  154 TYR   B CD2 1 
ATOM   3693 C  CE1 . TYR   B 1 155 ? 11.524  -27.837 13.178 1.00 44.89  ?  154 TYR   B CE1 1 
ATOM   3694 C  CE2 . TYR   B 1 155 ? 10.386  -29.868 12.525 1.00 40.96  ?  154 TYR   B CE2 1 
ATOM   3695 C  CZ  . TYR   B 1 155 ? 11.272  -28.827 12.235 1.00 47.45  ?  154 TYR   B CZ  1 
ATOM   3696 O  OH  . TYR   B 1 155 ? 11.926  -28.758 11.015 1.00 38.50  ?  154 TYR   B OH  1 
ATOM   3697 N  N   . CYS   B 1 156 ? 9.112   -29.438 19.359 1.00 51.83  ?  155 CYS   B N   1 
ATOM   3698 C  CA  . CYS   B 1 156 ? 8.585   -28.939 20.619 1.00 55.35  ?  155 CYS   B CA  1 
ATOM   3699 C  C   . CYS   B 1 156 ? 9.516   -29.218 21.790 1.00 52.54  ?  155 CYS   B C   1 
ATOM   3700 O  O   . CYS   B 1 156 ? 9.265   -28.728 22.896 1.00 50.55  ?  155 CYS   B O   1 
ATOM   3701 C  CB  . CYS   B 1 156 ? 7.195   -29.549 20.856 1.00 50.83  ?  155 CYS   B CB  1 
ATOM   3702 S  SG  . CYS   B 1 156 ? 5.977   -29.094 19.532 1.00 53.42  ?  155 CYS   B SG  1 
ATOM   3703 N  N   . ASN   B 1 157 ? 10.625  -29.918 21.532 1.00 56.82  ?  156 ASN   B N   1 
ATOM   3704 C  CA  A ASN   B 1 157 ? 11.519  -30.459 22.561 0.52 53.12  ?  156 ASN   B CA  1 
ATOM   3705 C  CA  B ASN   B 1 157 ? 11.511  -30.397 22.589 0.48 53.58  ?  156 ASN   B CA  1 
ATOM   3706 C  C   . ASN   B 1 157 ? 10.724  -31.163 23.649 1.00 54.75  ?  156 ASN   B C   1 
ATOM   3707 O  O   . ASN   B 1 157 ? 11.062  -31.121 24.836 1.00 64.44  ?  156 ASN   B O   1 
ATOM   3708 C  CB  A ASN   B 1 157 ? 12.436  -29.393 23.148 0.52 51.47  ?  156 ASN   B CB  1 
ATOM   3709 C  CB  B ASN   B 1 157 ? 12.305  -29.242 23.205 0.48 51.51  ?  156 ASN   B CB  1 
ATOM   3710 C  CG  A ASN   B 1 157 ? 13.780  -29.960 23.551 0.52 52.90  ?  156 ASN   B CG  1 
ATOM   3711 C  CG  B ASN   B 1 157 ? 12.371  -28.024 22.290 0.48 53.23  ?  156 ASN   B CG  1 
ATOM   3712 O  OD1 A ASN   B 1 157 ? 14.823  -29.435 23.174 0.52 55.02  ?  156 ASN   B OD1 1 
ATOM   3713 O  OD1 B ASN   B 1 157 ? 13.211  -27.963 21.388 0.48 53.58  ?  156 ASN   B OD1 1 
ATOM   3714 N  ND2 A ASN   B 1 157 ? 13.761  -31.046 24.317 0.52 51.87  ?  156 ASN   B ND2 1 
ATOM   3715 N  ND2 B ASN   B 1 157 ? 11.476  -27.055 22.510 0.48 49.21  ?  156 ASN   B ND2 1 
ATOM   3716 N  N   . LYS   B 1 158 ? 9.652   -31.819 23.219 1.00 49.27  ?  157 LYS   B N   1 
ATOM   3717 C  CA  . LYS   B 1 158 ? 8.857   -32.746 24.002 1.00 47.31  ?  157 LYS   B CA  1 
ATOM   3718 C  C   . LYS   B 1 158 ? 9.328   -34.147 23.674 1.00 51.81  ?  157 LYS   B C   1 
ATOM   3719 O  O   . LYS   B 1 158 ? 9.924   -34.401 22.619 1.00 56.92  ?  157 LYS   B O   1 
ATOM   3720 C  CB  . LYS   B 1 158 ? 7.359   -32.637 23.685 1.00 52.06  ?  157 LYS   B CB  1 
ATOM   3721 C  CG  . LYS   B 1 158 ? 6.541   -31.792 24.643 1.00 53.79  ?  157 LYS   B CG  1 
ATOM   3722 C  CD  . LYS   B 1 158 ? 6.981   -30.347 24.546 1.00 60.12  ?  157 LYS   B CD  1 
ATOM   3723 C  CE  . LYS   B 1 158 ? 6.452   -29.499 25.702 1.00 64.52  ?  157 LYS   B CE  1 
ATOM   3724 N  NZ  . LYS   B 1 158 ? 7.164   -28.194 25.705 1.00 57.10  ?  157 LYS   B NZ  1 
ATOM   3725 N  N   . THR   B 1 159 ? 9.058   -35.066 24.585 1.00 50.85  ?  158 THR   B N   1 
ATOM   3726 C  CA  . THR   B 1 159 ? 9.355   -36.459 24.326 1.00 44.81  ?  158 THR   B CA  1 
ATOM   3727 C  C   . THR   B 1 159 ? 8.061   -37.263 24.389 1.00 48.09  ?  158 THR   B C   1 
ATOM   3728 O  O   . THR   B 1 159 ? 7.038   -36.795 24.901 1.00 51.55  ?  158 THR   B O   1 
ATOM   3729 C  CB  . THR   B 1 159 ? 10.433  -36.977 25.300 1.00 44.52  ?  158 THR   B CB  1 
ATOM   3730 O  OG1 . THR   B 1 159 ? 9.902   -38.000 26.140 1.00 43.82  ?  158 THR   B OG1 1 
ATOM   3731 C  CG2 . THR   B 1 159 ? 11.026  -35.847 26.120 1.00 42.94  ?  158 THR   B CG2 1 
ATOM   3732 N  N   . VAL   B 1 160 ? 8.092   -38.447 23.772 1.00 44.41  ?  159 VAL   B N   1 
ATOM   3733 C  CA  . VAL   B 1 160 ? 6.992   -39.398 23.896 1.00 51.28  ?  159 VAL   B CA  1 
ATOM   3734 C  C   . VAL   B 1 160 ? 6.563   -39.569 25.363 1.00 52.75  ?  159 VAL   B C   1 
ATOM   3735 O  O   . VAL   B 1 160 ? 7.378   -39.497 26.287 1.00 58.87  ?  159 VAL   B O   1 
ATOM   3736 C  CB  . VAL   B 1 160 ? 7.422   -40.721 23.237 1.00 50.21  ?  159 VAL   B CB  1 
ATOM   3737 C  CG1 . VAL   B 1 160 ? 6.348   -41.754 23.315 1.00 54.30  ?  159 VAL   B CG1 1 
ATOM   3738 C  CG2 . VAL   B 1 160 ? 7.688   -40.451 21.759 1.00 51.64  ?  159 VAL   B CG2 1 
ATOM   3739 N  N   . GLY   B 1 161 ? 5.265   -39.734 25.584 1.00 48.29  ?  160 GLY   B N   1 
ATOM   3740 C  CA  . GLY   B 1 161 ? 4.795   -39.870 26.956 1.00 58.22  ?  160 GLY   B CA  1 
ATOM   3741 C  C   . GLY   B 1 161 ? 4.960   -38.643 27.833 1.00 62.54  ?  160 GLY   B C   1 
ATOM   3742 O  O   . GLY   B 1 161 ? 5.227   -38.766 29.037 1.00 67.22  ?  160 GLY   B O   1 
ATOM   3743 N  N   . GLU   B 1 162 ? 4.800   -37.460 27.264 1.00 51.41  ?  161 GLU   B N   1 
ATOM   3744 C  CA  . GLU   B 1 162 ? 4.839   -36.207 28.017 1.00 52.04  ?  161 GLU   B CA  1 
ATOM   3745 C  C   . GLU   B 1 162 ? 3.660   -35.421 27.440 1.00 54.05  ?  161 GLU   B C   1 
ATOM   3746 O  O   . GLU   B 1 162 ? 3.797   -34.729 26.432 1.00 66.46  ?  161 GLU   B O   1 
ATOM   3747 C  CB  . GLU   B 1 162 ? 6.213   -35.530 27.873 1.00 50.37  ?  161 GLU   B CB  1 
ATOM   3748 C  CG  . GLU   B 1 162 ? 6.310   -33.996 27.713 1.00 51.09  ?  161 GLU   B CG  1 
ATOM   3749 C  CD  . GLU   B 1 162 ? 7.766   -33.502 27.753 1.00 66.18  ?  161 GLU   B CD  1 
ATOM   3750 O  OE1 . GLU   B 1 162 ? 8.654   -34.208 27.210 1.00 60.56  ?  161 GLU   B OE1 1 
ATOM   3751 O  OE2 . GLU   B 1 162 ? 8.035   -32.406 28.318 1.00 76.80  -1 161 GLU   B OE2 1 
ATOM   3752 N  N   . LEU   B 1 163 ? 2.477   -35.614 28.027 1.00 51.45  ?  162 LEU   B N   1 
ATOM   3753 C  CA  . LEU   B 1 163 ? 1.254   -35.041 27.468 1.00 49.68  ?  162 LEU   B CA  1 
ATOM   3754 C  C   . LEU   B 1 163 ? 1.460   -33.555 27.160 1.00 48.16  ?  162 LEU   B C   1 
ATOM   3755 O  O   . LEU   B 1 163 ? 2.091   -32.831 27.930 1.00 43.77  ?  162 LEU   B O   1 
ATOM   3756 C  CB  . LEU   B 1 163 ? 0.079   -35.245 28.442 1.00 48.19  ?  162 LEU   B CB  1 
ATOM   3757 C  CG  . LEU   B 1 163 ? -1.375  -35.190 27.893 1.00 63.55  ?  162 LEU   B CG  1 
ATOM   3758 C  CD1 . LEU   B 1 163 ? -1.976  -33.794 27.661 1.00 50.23  ?  162 LEU   B CD1 1 
ATOM   3759 C  CD2 . LEU   B 1 163 ? -1.537  -36.014 26.590 1.00 61.66  ?  162 LEU   B CD2 1 
ATOM   3760 N  N   . GLY   B 1 164 ? 0.975   -33.115 25.993 1.00 47.44  ?  163 GLY   B N   1 
ATOM   3761 C  CA  . GLY   B 1 164 ? 1.189   -31.765 25.516 1.00 41.83  ?  163 GLY   B CA  1 
ATOM   3762 C  C   . GLY   B 1 164 ? -0.091  -30.932 25.466 1.00 39.03  ?  163 GLY   B C   1 
ATOM   3763 O  O   . GLY   B 1 164 ? -1.189  -31.421 25.698 1.00 44.88  ?  163 GLY   B O   1 
ATOM   3764 N  N   . ASP   B 1 165 ? 0.077   -29.640 25.194 1.00 37.18  ?  164 ASP   B N   1 
ATOM   3765 C  CA  . ASP   B 1 165 ? -1.048  -28.732 24.981 1.00 44.50  ?  164 ASP   B CA  1 
ATOM   3766 C  C   . ASP   B 1 165 ? -1.166  -28.415 23.483 1.00 49.85  ?  164 ASP   B C   1 
ATOM   3767 O  O   . ASP   B 1 165 ? -0.164  -28.143 22.803 1.00 44.80  ?  164 ASP   B O   1 
ATOM   3768 C  CB  . ASP   B 1 165 ? -0.904  -27.487 25.882 1.00 38.36  ?  164 ASP   B CB  1 
ATOM   3769 C  CG  . ASP   B 1 165 ? -1.682  -26.271 25.389 1.00 50.52  ?  164 ASP   B CG  1 
ATOM   3770 O  OD1 . ASP   B 1 165 ? -2.336  -25.582 26.213 1.00 48.91  ?  164 ASP   B OD1 1 
ATOM   3771 O  OD2 . ASP   B 1 165 ? -1.534  -25.909 24.202 1.00 55.80  -1 164 ASP   B OD2 1 
ATOM   3772 N  N   . VAL   B 1 166 ? -2.389  -28.505 22.955 1.00 45.78  ?  165 VAL   B N   1 
ATOM   3773 C  CA  . VAL   B 1 166 ? -2.555  -28.430 21.507 1.00 51.15  ?  165 VAL   B CA  1 
ATOM   3774 C  C   . VAL   B 1 166 ? -2.231  -27.027 21.003 1.00 49.06  ?  165 VAL   B C   1 
ATOM   3775 O  O   . VAL   B 1 166 ? -1.465  -26.859 20.046 1.00 46.24  ?  165 VAL   B O   1 
ATOM   3776 C  CB  . VAL   B 1 166 ? -3.971  -28.879 21.099 1.00 52.83  ?  165 VAL   B CB  1 
ATOM   3777 C  CG1 . VAL   B 1 166 ? -4.355  -28.281 19.755 1.00 43.85  ?  165 VAL   B CG1 1 
ATOM   3778 C  CG2 . VAL   B 1 166 ? -4.046  -30.413 21.050 1.00 46.94  ?  165 VAL   B CG2 1 
ATOM   3779 N  N   . ARG   B 1 167 ? -2.792  -25.997 21.642 1.00 41.89  ?  166 ARG   B N   1 
ATOM   3780 C  CA  . ARG   B 1 167 ? -2.540  -24.652 21.153 1.00 46.11  ?  166 ARG   B CA  1 
ATOM   3781 C  C   . ARG   B 1 167 ? -1.045  -24.361 21.104 1.00 47.06  ?  166 ARG   B C   1 
ATOM   3782 O  O   . ARG   B 1 167 ? -0.552  -23.728 20.163 1.00 49.17  ?  166 ARG   B O   1 
ATOM   3783 C  CB  . ARG   B 1 167 ? -3.281  -23.638 22.010 1.00 43.40  ?  166 ARG   B CB  1 
ATOM   3784 C  CG  . ARG   B 1 167 ? -2.777  -22.226 21.886 1.00 37.87  ?  166 ARG   B CG  1 
ATOM   3785 C  CD  . ARG   B 1 167 ? -3.486  -21.373 22.951 1.00 56.09  ?  166 ARG   B CD  1 
ATOM   3786 N  NE  . ARG   B 1 167 ? -2.774  -21.365 24.223 1.00 53.58  ?  166 ARG   B NE  1 
ATOM   3787 C  CZ  . ARG   B 1 167 ? -2.063  -20.341 24.669 1.00 47.56  ?  166 ARG   B CZ  1 
ATOM   3788 N  NH1 . ARG   B 1 167 ? -2.008  -19.199 24.010 1.00 50.72  ?  166 ARG   B NH1 1 
ATOM   3789 N  NH2 . ARG   B 1 167 ? -1.394  -20.466 25.807 1.00 46.90  ?  166 ARG   B NH2 1 
ATOM   3790 N  N   . GLU   B 1 168 ? -0.291  -24.855 22.079 1.00 54.01  ?  167 GLU   B N   1 
ATOM   3791 C  CA  . GLU   B 1 168 ? 1.136   -24.573 22.060 1.00 51.35  ?  167 GLU   B CA  1 
ATOM   3792 C  C   . GLU   B 1 168 ? 1.815   -25.334 20.928 1.00 50.28  ?  167 GLU   B C   1 
ATOM   3793 O  O   . GLU   B 1 168 ? 2.569   -24.747 20.142 1.00 54.07  ?  167 GLU   B O   1 
ATOM   3794 C  CB  . GLU   B 1 168 ? 1.755   -24.889 23.419 1.00 39.99  ?  167 GLU   B CB  1 
ATOM   3795 C  CG  . GLU   B 1 168 ? 1.447   -23.792 24.440 1.00 47.28  ?  167 GLU   B CG  1 
ATOM   3796 C  CD  . GLU   B 1 168 ? 2.165   -23.969 25.795 1.00 53.15  ?  167 GLU   B CD  1 
ATOM   3797 O  OE1 . GLU   B 1 168 ? 3.249   -24.634 25.844 1.00 48.45  ?  167 GLU   B OE1 1 
ATOM   3798 O  OE2 . GLU   B 1 168 ? 1.632   -23.429 26.798 1.00 45.10  -1 167 GLU   B OE2 1 
ATOM   3799 N  N   . THR   B 1 169 ? 1.523   -26.632 20.805 1.00 45.71  ?  168 THR   B N   1 
ATOM   3800 C  CA  . THR   B 1 169 ? 2.084   -27.438 19.724 1.00 44.14  ?  168 THR   B CA  1 
ATOM   3801 C  C   . THR   B 1 169 ? 1.879   -26.766 18.373 1.00 51.72  ?  168 THR   B C   1 
ATOM   3802 O  O   . THR   B 1 169 ? 2.775   -26.785 17.517 1.00 49.05  ?  168 THR   B O   1 
ATOM   3803 C  CB  . THR   B 1 169 ? 1.440   -28.828 19.730 1.00 47.77  ?  168 THR   B CB  1 
ATOM   3804 O  OG1 . THR   B 1 169 ? 1.622   -29.443 21.018 1.00 49.23  ?  168 THR   B OG1 1 
ATOM   3805 C  CG2 . THR   B 1 169 ? 2.017   -29.738 18.623 1.00 41.22  ?  168 THR   B CG2 1 
ATOM   3806 N  N   . MET   B 1 170 ? 0.701   -26.160 18.167 1.00 50.62  ?  169 MET   B N   1 
ATOM   3807 C  CA  . MET   B 1 170 ? 0.445   -25.406 16.943 1.00 47.01  ?  169 MET   B CA  1 
ATOM   3808 C  C   . MET   B 1 170 ? 1.477   -24.303 16.767 1.00 46.98  ?  169 MET   B C   1 
ATOM   3809 O  O   . MET   B 1 170 ? 2.126   -24.204 15.722 1.00 45.89  ?  169 MET   B O   1 
ATOM   3810 C  CB  . MET   B 1 170 ? -0.966  -24.835 16.988 1.00 49.44  ?  169 MET   B CB  1 
ATOM   3811 C  CG  . MET   B 1 170 ? -2.087  -25.909 16.867 1.00 58.00  ?  169 MET   B CG  1 
ATOM   3812 S  SD  . MET   B 1 170 ? -2.145  -26.795 15.289 1.00 57.31  ?  169 MET   B SD  1 
ATOM   3813 C  CE  . MET   B 1 170 ? -1.321  -28.291 15.748 1.00 51.98  ?  169 MET   B CE  1 
ATOM   3814 N  N   . SER   B 1 171 ? 1.698   -23.513 17.818 1.00 52.76  ?  170 SER   B N   1 
ATOM   3815 C  CA  . SER   B 1 171 ? 2.616   -22.381 17.744 1.00 46.88  ?  170 SER   B CA  1 
ATOM   3816 C  C   . SER   B 1 171 ? 4.021   -22.801 17.330 1.00 52.45  ?  170 SER   B C   1 
ATOM   3817 O  O   . SER   B 1 171 ? 4.632   -22.183 16.447 1.00 53.88  ?  170 SER   B O   1 
ATOM   3818 C  CB  . SER   B 1 171 ? 2.649   -21.692 19.085 1.00 41.45  ?  170 SER   B CB  1 
ATOM   3819 O  OG  . SER   B 1 171 ? 1.621   -20.738 19.102 1.00 59.36  ?  170 SER   B OG  1 
ATOM   3820 N  N   . TYR   B 1 172 ? 4.571   -23.823 17.988 1.00 50.88  ?  171 TYR   B N   1 
ATOM   3821 C  CA  . TYR   B 1 172 ? 5.861   -24.359 17.565 1.00 50.94  ?  171 TYR   B CA  1 
ATOM   3822 C  C   . TYR   B 1 172 ? 5.871   -24.614 16.054 1.00 48.83  ?  171 TYR   B C   1 
ATOM   3823 O  O   . TYR   B 1 172 ? 6.788   -24.180 15.346 1.00 50.50  ?  171 TYR   B O   1 
ATOM   3824 C  CB  . TYR   B 1 172 ? 6.182   -25.649 18.344 1.00 54.56  ?  171 TYR   B CB  1 
ATOM   3825 C  CG  . TYR   B 1 172 ? 6.825   -25.464 19.716 1.00 60.67  ?  171 TYR   B CG  1 
ATOM   3826 C  CD1 . TYR   B 1 172 ? 7.994   -24.716 19.877 1.00 58.23  ?  171 TYR   B CD1 1 
ATOM   3827 C  CD2 . TYR   B 1 172 ? 6.249   -26.042 20.864 1.00 62.18  ?  171 TYR   B CD2 1 
ATOM   3828 C  CE1 . TYR   B 1 172 ? 8.570   -24.550 21.145 1.00 60.25  ?  171 TYR   B CE1 1 
ATOM   3829 C  CE2 . TYR   B 1 172 ? 6.825   -25.895 22.137 1.00 50.74  ?  171 TYR   B CE2 1 
ATOM   3830 C  CZ  . TYR   B 1 172 ? 7.982   -25.150 22.266 1.00 61.87  ?  171 TYR   B CZ  1 
ATOM   3831 O  OH  . TYR   B 1 172 ? 8.557   -24.998 23.515 1.00 65.43  ?  171 TYR   B OH  1 
ATOM   3832 N  N   . LEU   B 1 173 ? 4.825   -25.275 15.536 1.00 48.41  ?  172 LEU   B N   1 
ATOM   3833 C  CA  . LEU   B 1 173 ? 4.768   -25.602 14.108 1.00 47.73  ?  172 LEU   B CA  1 
ATOM   3834 C  C   . LEU   B 1 173 ? 4.518   -24.358 13.247 1.00 48.67  ?  172 LEU   B C   1 
ATOM   3835 O  O   . LEU   B 1 173 ? 5.254   -24.106 12.284 1.00 45.65  ?  172 LEU   B O   1 
ATOM   3836 C  CB  . LEU   B 1 173 ? 3.696   -26.660 13.848 1.00 41.67  ?  172 LEU   B CB  1 
ATOM   3837 C  CG  . LEU   B 1 173 ? 3.905   -27.990 14.570 1.00 45.98  ?  172 LEU   B CG  1 
ATOM   3838 C  CD1 . LEU   B 1 173 ? 2.797   -28.985 14.258 1.00 43.05  ?  172 LEU   B CD1 1 
ATOM   3839 C  CD2 . LEU   B 1 173 ? 5.280   -28.582 14.294 1.00 38.46  ?  172 LEU   B CD2 1 
ATOM   3840 N  N   . PHE   B 1 174 ? 3.487   -23.561 13.585 1.00 47.81  ?  173 PHE   B N   1 
ATOM   3841 C  CA  . PHE   B 1 174 ? 3.220   -22.302 12.890 1.00 45.53  ?  173 PHE   B CA  1 
ATOM   3842 C  C   . PHE   B 1 174 ? 4.463   -21.439 12.734 1.00 50.97  ?  173 PHE   B C   1 
ATOM   3843 O  O   . PHE   B 1 174 ? 4.517   -20.579 11.846 1.00 58.64  ?  173 PHE   B O   1 
ATOM   3844 C  CB  . PHE   B 1 174 ? 2.160   -21.483 13.623 1.00 37.68  ?  173 PHE   B CB  1 
ATOM   3845 C  CG  . PHE   B 1 174 ? 0.784   -22.018 13.470 1.00 41.41  ?  173 PHE   B CG  1 
ATOM   3846 C  CD1 . PHE   B 1 174 ? 0.553   -23.156 12.713 1.00 40.08  ?  173 PHE   B CD1 1 
ATOM   3847 C  CD2 . PHE   B 1 174 ? -0.297  -21.365 14.048 1.00 40.98  ?  173 PHE   B CD2 1 
ATOM   3848 C  CE1 . PHE   B 1 174 ? -0.738  -23.647 12.547 1.00 44.53  ?  173 PHE   B CE1 1 
ATOM   3849 C  CE2 . PHE   B 1 174 ? -1.587  -21.851 13.895 1.00 40.93  ?  173 PHE   B CE2 1 
ATOM   3850 C  CZ  . PHE   B 1 174 ? -1.810  -22.996 13.151 1.00 45.24  ?  173 PHE   B CZ  1 
ATOM   3851 N  N   . GLN   B 1 175 ? 5.470   -21.639 13.565 1.00 50.84  ?  174 GLN   B N   1 
ATOM   3852 C  CA  . GLN   B 1 175 ? 6.602   -20.740 13.482 1.00 60.07  ?  174 GLN   B CA  1 
ATOM   3853 C  C   . GLN   B 1 175 ? 7.419   -21.008 12.226 1.00 55.00  ?  174 GLN   B C   1 
ATOM   3854 O  O   . GLN   B 1 175 ? 8.020   -20.084 11.676 1.00 62.06  ?  174 GLN   B O   1 
ATOM   3855 C  CB  . GLN   B 1 175 ? 7.439   -20.853 14.764 1.00 65.99  ?  174 GLN   B CB  1 
ATOM   3856 C  CG  . GLN   B 1 175 ? 8.012   -19.515 15.250 1.00 67.47  ?  174 GLN   B CG  1 
ATOM   3857 C  CD  . GLN   B 1 175 ? 9.525   -19.454 15.138 1.00 75.18  ?  174 GLN   B CD  1 
ATOM   3858 O  OE1 . GLN   B 1 175 ? 10.211  -20.477 15.256 1.00 81.00  ?  174 GLN   B OE1 1 
ATOM   3859 N  NE2 . GLN   B 1 175 ? 10.054  -18.259 14.884 1.00 73.98  ?  174 GLN   B NE2 1 
ATOM   3860 N  N   . HIS   B 1 176 ? 7.424   -22.247 11.736 1.00 52.01  ?  175 HIS   B N   1 
ATOM   3861 C  CA  . HIS   B 1 176 ? 8.164   -22.612 10.535 1.00 55.46  ?  175 HIS   B CA  1 
ATOM   3862 C  C   . HIS   B 1 176 ? 7.233   -22.798 9.330  1.00 58.05  ?  175 HIS   B C   1 
ATOM   3863 O  O   . HIS   B 1 176 ? 7.601   -23.438 8.326  1.00 46.57  ?  175 HIS   B O   1 
ATOM   3864 C  CB  . HIS   B 1 176 ? 8.997   -23.867 10.809 1.00 52.92  ?  175 HIS   B CB  1 
ATOM   3865 C  CG  . HIS   B 1 176 ? 10.204  -23.606 11.662 1.00 64.00  ?  175 HIS   B CG  1 
ATOM   3866 N  ND1 . HIS   B 1 176 ? 11.276  -22.846 11.228 1.00 61.74  ?  175 HIS   B ND1 1 
ATOM   3867 C  CD2 . HIS   B 1 176 ? 10.490  -23.969 12.941 1.00 57.81  ?  175 HIS   B CD2 1 
ATOM   3868 C  CE1 . HIS   B 1 176 ? 12.177  -22.771 12.193 1.00 58.77  ?  175 HIS   B CE1 1 
ATOM   3869 N  NE2 . HIS   B 1 176 ? 11.724  -23.443 13.242 1.00 60.81  ?  175 HIS   B NE2 1 
ATOM   3870 N  N   . ALA   B 1 177 ? 6.032   -22.243 9.417  1.00 53.52  ?  176 ALA   B N   1 
ATOM   3871 C  CA  . ALA   B 1 177 ? 5.097   -22.202 8.312  1.00 55.58  ?  176 ALA   B CA  1 
ATOM   3872 C  C   . ALA   B 1 177 ? 5.105   -20.819 7.667  1.00 55.97  ?  176 ALA   B C   1 
ATOM   3873 O  O   . ALA   B 1 177 ? 5.475   -19.818 8.292  1.00 56.56  ?  176 ALA   B O   1 
ATOM   3874 C  CB  . ALA   B 1 177 ? 3.697   -22.576 8.797  1.00 52.58  ?  176 ALA   B CB  1 
ATOM   3875 N  N   . ASN   B 1 178 ? 4.727   -20.784 6.388  1.00 57.44  ?  177 ASN   B N   1 
ATOM   3876 C  CA  . ASN   B 1 178 ? 4.627   -19.539 5.624  1.00 62.86  ?  177 ASN   B CA  1 
ATOM   3877 C  C   . ASN   B 1 178 ? 3.275   -18.901 5.945  1.00 55.77  ?  177 ASN   B C   1 
ATOM   3878 O  O   . ASN   B 1 178 ? 2.254   -19.111 5.283  1.00 49.51  ?  177 ASN   B O   1 
ATOM   3879 C  CB  . ASN   B 1 178 ? 4.818   -19.797 4.127  1.00 59.10  ?  177 ASN   B CB  1 
ATOM   3880 C  CG  . ASN   B 1 178 ? 5.206   -18.522 3.336  1.00 68.90  ?  177 ASN   B CG  1 
ATOM   3881 O  OD1 . ASN   B 1 178 ? 4.960   -17.396 3.783  1.00 74.68  ?  177 ASN   B OD1 1 
ATOM   3882 N  ND2 . ASN   B 1 178 ? 5.809   -18.707 2.158  1.00 61.11  ?  177 ASN   B ND2 1 
ATOM   3883 N  N   . LEU   B 1 179 ? 3.266   -18.132 7.021  1.00 54.57  ?  178 LEU   B N   1 
ATOM   3884 C  CA  . LEU   B 1 179 ? 2.168   -17.228 7.303  1.00 59.21  ?  178 LEU   B CA  1 
ATOM   3885 C  C   . LEU   B 1 179 ? 2.645   -15.786 7.217  1.00 61.09  ?  178 LEU   B C   1 
ATOM   3886 O  O   . LEU   B 1 179 ? 2.076   -14.888 7.837  1.00 64.60  ?  178 LEU   B O   1 
ATOM   3887 C  CB  . LEU   B 1 179 ? 1.540   -17.525 8.661  1.00 60.71  ?  178 LEU   B CB  1 
ATOM   3888 C  CG  . LEU   B 1 179 ? 1.060   -18.950 8.962  1.00 59.80  ?  178 LEU   B CG  1 
ATOM   3889 C  CD1 . LEU   B 1 179 ? 2.215   -19.755 9.475  1.00 55.10  ?  178 LEU   B CD1 1 
ATOM   3890 C  CD2 . LEU   B 1 179 ? -0.054  -18.936 10.010 1.00 59.93  ?  178 LEU   B CD2 1 
ATOM   3891 N  N   . ASP   B 1 180 ? 3.705   -15.560 6.440  1.00 69.94  ?  179 ASP   B N   1 
ATOM   3892 C  CA  . ASP   B 1 180 ? 4.247   -14.221 6.246  1.00 74.33  ?  179 ASP   B CA  1 
ATOM   3893 C  C   . ASP   B 1 180 ? 3.336   -13.329 5.422  1.00 72.32  ?  179 ASP   B C   1 
ATOM   3894 O  O   . ASP   B 1 180 ? 3.572   -12.120 5.357  1.00 81.66  ?  179 ASP   B O   1 
ATOM   3895 C  CB  . ASP   B 1 180 ? 5.653   -14.319 5.635  1.00 73.10  ?  179 ASP   B CB  1 
ATOM   3896 C  CG  . ASP   B 1 180 ? 6.470   -15.481 6.240  1.00 82.90  ?  179 ASP   B CG  1 
ATOM   3897 O  OD1 . ASP   B 1 180 ? 7.192   -16.173 5.473  1.00 79.77  ?  179 ASP   B OD1 1 
ATOM   3898 O  OD2 . ASP   B 1 180 ? 6.369   -15.697 7.492  1.00 73.52  -1 179 ASP   B OD2 1 
ATOM   3899 N  N   . SER   B 1 181 ? 2.276   -13.873 4.848  1.00 71.13  ?  180 SER   B N   1 
ATOM   3900 C  CA  . SER   B 1 181 ? 1.275   -13.047 4.203  1.00 65.34  ?  180 SER   B CA  1 
ATOM   3901 C  C   . SER   B 1 181 ? 0.177   -12.570 5.159  1.00 65.36  ?  180 SER   B C   1 
ATOM   3902 O  O   . SER   B 1 181 ? -0.512  -11.592 4.852  1.00 74.45  ?  180 SER   B O   1 
ATOM   3903 C  CB  . SER   B 1 181 ? 0.665   -13.826 3.030  1.00 67.06  ?  180 SER   B CB  1 
ATOM   3904 O  OG  . SER   B 1 181 ? -0.699  -13.490 2.825  1.00 70.69  ?  180 SER   B OG  1 
ATOM   3905 N  N   . CYS   B 1 182 ? -0.003  -13.202 6.310  1.00 58.94  ?  181 CYS   B N   1 
ATOM   3906 C  CA  . CYS   B 1 182 ? -1.198  -12.932 7.102  1.00 56.12  ?  181 CYS   B CA  1 
ATOM   3907 C  C   . CYS   B 1 182 ? -1.104  -11.590 7.822  1.00 59.00  ?  181 CYS   B C   1 
ATOM   3908 O  O   . CYS   B 1 182 ? -0.027  -11.189 8.269  1.00 69.35  ?  181 CYS   B O   1 
ATOM   3909 C  CB  . CYS   B 1 182 ? -1.418  -14.071 8.101  1.00 59.03  ?  181 CYS   B CB  1 
ATOM   3910 S  SG  . CYS   B 1 182 ? -1.368  -15.778 7.324  1.00 52.23  ?  181 CYS   B SG  1 
ATOM   3911 N  N   . LYS   B 1 183 ? -2.236  -10.869 7.896  1.00 56.07  ?  182 LYS   B N   1 
ATOM   3912 C  CA  . LYS   B 1 183 ? -2.367  -9.677  8.734  1.00 56.39  ?  182 LYS   B CA  1 
ATOM   3913 C  C   . LYS   B 1 183 ? -3.648  -9.728  9.546  1.00 53.74  ?  182 LYS   B C   1 
ATOM   3914 O  O   . LYS   B 1 183 ? -4.616  -10.398 9.194  1.00 50.78  ?  182 LYS   B O   1 
ATOM   3915 C  CB  . LYS   B 1 183 ? -2.436  -8.321  7.996  1.00 57.23  ?  182 LYS   B CB  1 
ATOM   3916 C  CG  . LYS   B 1 183 ? -1.718  -8.145  6.701  1.00 65.89  ?  182 LYS   B CG  1 
ATOM   3917 C  CD  . LYS   B 1 183 ? -1.546  -6.639  6.450  1.00 69.32  ?  182 LYS   B CD  1 
ATOM   3918 C  CE  . LYS   B 1 183 ? -2.843  -5.872  6.706  1.00 63.82  ?  182 LYS   B CE  1 
ATOM   3919 N  NZ  . LYS   B 1 183 ? -3.129  -4.854  5.638  1.00 71.69  ?  182 LYS   B NZ  1 
ATOM   3920 N  N   . ARG   B 1 184 ? -3.655  -8.929  10.606 1.00 57.17  ?  183 ARG   B N   1 
ATOM   3921 C  CA  . ARG   B 1 184 ? -4.808  -8.778  11.470 1.00 49.04  ?  183 ARG   B CA  1 
ATOM   3922 C  C   . ARG   B 1 184 ? -4.741  -7.398  12.090 1.00 53.42  ?  183 ARG   B C   1 
ATOM   3923 O  O   . ARG   B 1 184 ? -3.706  -6.998  12.626 1.00 55.12  ?  183 ARG   B O   1 
ATOM   3924 C  CB  . ARG   B 1 184 ? -4.825  -9.844  12.555 1.00 57.33  ?  183 ARG   B CB  1 
ATOM   3925 C  CG  . ARG   B 1 184 ? -5.608  -9.457  13.794 1.00 51.23  ?  183 ARG   B CG  1 
ATOM   3926 C  CD  . ARG   B 1 184 ? -5.574  -10.616 14.723 1.00 49.73  ?  183 ARG   B CD  1 
ATOM   3927 N  NE  . ARG   B 1 184 ? -6.748  -11.459 14.596 1.00 45.76  ?  183 ARG   B NE  1 
ATOM   3928 C  CZ  . ARG   B 1 184 ? -6.744  -12.775 14.748 1.00 49.48  ?  183 ARG   B CZ  1 
ATOM   3929 N  NH1 . ARG   B 1 184 ? -5.622  -13.450 14.885 1.00 49.79  ?  183 ARG   B NH1 1 
ATOM   3930 N  NH2 . ARG   B 1 184 ? -7.901  -13.430 14.794 1.00 62.41  ?  183 ARG   B NH2 1 
ATOM   3931 N  N   . VAL   B 1 185 ? -5.840  -6.672  12.002 1.00 56.82  ?  184 VAL   B N   1 
ATOM   3932 C  CA  . VAL   B 1 185 ? -5.938  -5.318  12.515 1.00 56.32  ?  184 VAL   B CA  1 
ATOM   3933 C  C   . VAL   B 1 185 ? -7.019  -5.328  13.578 1.00 58.78  ?  184 VAL   B C   1 
ATOM   3934 O  O   . VAL   B 1 185 ? -8.161  -5.727  13.308 1.00 59.65  ?  184 VAL   B O   1 
ATOM   3935 C  CB  . VAL   B 1 185 ? -6.250  -4.300  11.401 1.00 56.00  ?  184 VAL   B CB  1 
ATOM   3936 C  CG1 . VAL   B 1 185 ? -5.937  -2.875  11.870 1.00 57.92  ?  184 VAL   B CG1 1 
ATOM   3937 C  CG2 . VAL   B 1 185 ? -5.441  -4.629  10.139 1.00 47.56  ?  184 VAL   B CG2 1 
ATOM   3938 N  N   . LEU   B 1 186 ? -6.659  -4.915  14.786 1.00 55.08  ?  185 LEU   B N   1 
ATOM   3939 C  CA  . LEU   B 1 186 ? -7.607  -4.825  15.877 1.00 54.89  ?  185 LEU   B CA  1 
ATOM   3940 C  C   . LEU   B 1 186 ? -7.825  -3.368  16.238 1.00 58.62  ?  185 LEU   B C   1 
ATOM   3941 O  O   . LEU   B 1 186 ? -6.956  -2.517  16.028 1.00 59.93  ?  185 LEU   B O   1 
ATOM   3942 C  CB  . LEU   B 1 186 ? -7.128  -5.617  17.107 1.00 54.96  ?  185 LEU   B CB  1 
ATOM   3943 C  CG  . LEU   B 1 186 ? -6.536  -7.007  16.852 1.00 57.21  ?  185 LEU   B CG  1 
ATOM   3944 C  CD1 . LEU   B 1 186 ? -6.127  -7.684  18.135 1.00 55.75  ?  185 LEU   B CD1 1 
ATOM   3945 C  CD2 . LEU   B 1 186 ? -7.558  -7.887  16.123 1.00 55.74  ?  185 LEU   B CD2 1 
ATOM   3946 N  N   . ASN   B 1 187 ? -9.005  -3.091  16.768 1.00 57.72  ?  186 ASN   B N   1 
ATOM   3947 C  CA  . ASN   B 1 187 ? -9.300  -1.813  17.381 1.00 61.50  ?  186 ASN   B CA  1 
ATOM   3948 C  C   . ASN   B 1 187 ? -9.671  -2.073  18.831 1.00 65.90  ?  186 ASN   B C   1 
ATOM   3949 O  O   . ASN   B 1 187 ? -10.432 -3.000  19.118 1.00 65.62  ?  186 ASN   B O   1 
ATOM   3950 C  CB  . ASN   B 1 187 ? -10.430 -1.097  16.642 1.00 65.42  ?  186 ASN   B CB  1 
ATOM   3951 C  CG  . ASN   B 1 187 ? -10.517 0.371   16.998 1.00 69.76  ?  186 ASN   B CG  1 
ATOM   3952 O  OD1 . ASN   B 1 187 ? -9.513  1.090   16.957 1.00 73.17  ?  186 ASN   B OD1 1 
ATOM   3953 N  ND2 . ASN   B 1 187 ? -11.720 0.831   17.343 1.00 71.26  ?  186 ASN   B ND2 1 
ATOM   3954 N  N   . VAL   B 1 188 ? -9.104  -1.281  19.742 1.00 68.84  ?  187 VAL   B N   1 
ATOM   3955 C  CA  . VAL   B 1 188 ? -9.490  -1.286  21.147 1.00 69.34  ?  187 VAL   B CA  1 
ATOM   3956 C  C   . VAL   B 1 188 ? -10.131 0.057   21.455 1.00 69.48  ?  187 VAL   B C   1 
ATOM   3957 O  O   . VAL   B 1 188 ? -9.627  1.106   21.033 1.00 67.40  ?  187 VAL   B O   1 
ATOM   3958 C  CB  . VAL   B 1 188 ? -8.298  -1.540  22.093 1.00 70.92  ?  187 VAL   B CB  1 
ATOM   3959 C  CG1 . VAL   B 1 188 ? -8.799  -2.070  23.448 1.00 65.09  ?  187 VAL   B CG1 1 
ATOM   3960 C  CG2 . VAL   B 1 188 ? -7.291  -2.481  21.466 1.00 64.71  ?  187 VAL   B CG2 1 
ATOM   3961 N  N   . VAL   B 1 189 ? -11.232 0.022   22.205 1.00 71.13  ?  188 VAL   B N   1 
ATOM   3962 C  CA  . VAL   B 1 189 ? -12.031 1.205   22.508 1.00 75.07  ?  188 VAL   B CA  1 
ATOM   3963 C  C   . VAL   B 1 189 ? -12.391 1.156   23.987 1.00 77.43  ?  188 VAL   B C   1 
ATOM   3964 O  O   . VAL   B 1 189 ? -13.118 0.254   24.423 1.00 80.46  ?  188 VAL   B O   1 
ATOM   3965 C  CB  . VAL   B 1 189 ? -13.302 1.283   21.646 1.00 76.04  ?  188 VAL   B CB  1 
ATOM   3966 C  CG1 . VAL   B 1 189 ? -14.402 2.065   22.369 1.00 74.43  ?  188 VAL   B CG1 1 
ATOM   3967 C  CG2 . VAL   B 1 189 ? -12.988 1.888   20.272 1.00 69.73  ?  188 VAL   B CG2 1 
ATOM   3968 N  N   . CYS   B 1 190 ? -11.880 2.105   24.765 1.00 80.76  ?  189 CYS   B N   1 
ATOM   3969 C  CA  . CYS   B 1 190 ? -12.346 2.257   26.133 1.00 89.62  ?  189 CYS   B CA  1 
ATOM   3970 C  C   . CYS   B 1 190 ? -12.862 3.678   26.313 1.00 88.09  ?  189 CYS   B C   1 
ATOM   3971 O  O   . CYS   B 1 190 ? -12.462 4.602   25.593 1.00 79.56  ?  189 CYS   B O   1 
ATOM   3972 C  CB  . CYS   B 1 190 ? -11.258 1.903   27.169 1.00 83.32  ?  189 CYS   B CB  1 
ATOM   3973 S  SG  . CYS   B 1 190 ? -10.362 3.263   27.911 1.00 93.46  ?  189 CYS   B SG  1 
ATOM   3974 N  N   . LYS   B 1 191 ? -13.785 3.825   27.269 1.00 85.63  ?  190 LYS   B N   1 
ATOM   3975 C  CA  . LYS   B 1 191 ? -14.561 5.053   27.386 1.00 83.59  ?  190 LYS   B CA  1 
ATOM   3976 C  C   . LYS   B 1 191 ? -13.701 6.244   27.769 1.00 83.69  ?  190 LYS   B C   1 
ATOM   3977 O  O   . LYS   B 1 191 ? -14.061 7.386   27.473 1.00 90.04  ?  190 LYS   B O   1 
ATOM   3978 C  CB  . LYS   B 1 191 ? -15.664 4.860   28.420 1.00 92.81  ?  190 LYS   B CB  1 
ATOM   3979 C  CG  . LYS   B 1 191 ? -15.953 3.404   28.745 1.00 96.71  ?  190 LYS   B CG  1 
ATOM   3980 C  CD  . LYS   B 1 191 ? -16.377 3.282   30.191 1.00 101.38 ?  190 LYS   B CD  1 
ATOM   3981 C  CE  . LYS   B 1 191 ? -15.219 3.674   31.104 1.00 107.41 ?  190 LYS   B CE  1 
ATOM   3982 N  NZ  . LYS   B 1 191 ? -15.607 3.746   32.537 1.00 110.88 ?  190 LYS   B NZ  1 
ATOM   3983 N  N   . THR   B 1 192 ? -12.576 5.967   28.436 1.00 84.93  ?  191 THR   B N   1 
ATOM   3984 C  CA  . THR   B 1 192 ? -11.697 7.051   28.923 1.00 81.60  ?  191 THR   B CA  1 
ATOM   3985 C  C   . THR   B 1 192 ? -10.563 7.265   27.947 1.00 82.19  ?  191 THR   B C   1 
ATOM   3986 O  O   . THR   B 1 192 ? -10.714 8.132   27.060 1.00 79.43  ?  191 THR   B O   1 
ATOM   3987 C  CB  . THR   B 1 192 ? -11.173 6.684   30.311 1.00 87.88  ?  191 THR   B CB  1 
ATOM   3988 O  OG1 . THR   B 1 192 ? -12.232 5.986   30.960 1.00 82.57  ?  191 THR   B OG1 1 
ATOM   3989 C  CG2 . THR   B 1 192 ? -10.786 7.905   31.126 1.00 86.84  ?  191 THR   B CG2 1 
ATOM   3990 N  N   . CYS   B 1 193 ? -9.467  6.511   28.095 1.00 81.87  ?  192 CYS   B N   1 
ATOM   3991 C  CA  . CYS   B 1 193 ? -8.273  6.687   27.226 1.00 84.32  ?  192 CYS   B CA  1 
ATOM   3992 C  C   . CYS   B 1 193 ? -8.706  7.079   25.805 1.00 81.41  ?  192 CYS   B C   1 
ATOM   3993 O  O   . CYS   B 1 193 ? -8.268  8.150   25.331 1.00 78.69  ?  192 CYS   B O   1 
ATOM   3994 C  CB  . CYS   B 1 193 ? -7.440  5.412   27.173 1.00 90.27  ?  192 CYS   B CB  1 
ATOM   3995 S  SG  . CYS   B 1 193 ? -6.895  4.845   28.804 1.00 83.13  ?  192 CYS   B SG  1 
ATOM   3996 N  N   . GLY   B 1 194 ? -9.519  6.242   25.155 1.00 81.18  ?  193 GLY   B N   1 
ATOM   3997 C  CA  . GLY   B 1 194 ? -10.021 6.578   23.811 1.00 76.33  ?  193 GLY   B CA  1 
ATOM   3998 C  C   . GLY   B 1 194 ? -10.075 5.362   22.912 1.00 78.58  ?  193 GLY   B C   1 
ATOM   3999 O  O   . GLY   B 1 194 ? -10.779 4.395   23.268 1.00 82.37  ?  193 GLY   B O   1 
ATOM   4000 N  N   . GLN   B 1 195 ? -9.349  5.393   21.791 1.00 74.24  ?  194 GLN   B N   1 
ATOM   4001 C  CA  . GLN   B 1 195 ? -9.436  4.293   20.837 1.00 71.64  ?  194 GLN   B CA  1 
ATOM   4002 C  C   . GLN   B 1 195 ? -8.126  4.163   20.060 1.00 68.75  ?  194 GLN   B C   1 
ATOM   4003 O  O   . GLN   B 1 195 ? -7.626  5.149   19.513 1.00 70.07  ?  194 GLN   B O   1 
ATOM   4004 C  CB  . GLN   B 1 195 ? -10.636 4.537   19.903 1.00 68.58  ?  194 GLN   B CB  1 
ATOM   4005 C  CG  . GLN   B 1 195 ? -10.460 4.178   18.433 1.00 72.36  ?  194 GLN   B CG  1 
ATOM   4006 C  CD  . GLN   B 1 195 ? -11.720 4.464   17.626 1.00 79.28  ?  194 GLN   B CD  1 
ATOM   4007 O  OE1 . GLN   B 1 195 ? -12.746 4.876   18.178 1.00 82.60  ?  194 GLN   B OE1 1 
ATOM   4008 N  NE2 . GLN   B 1 195 ? -11.662 4.209   16.324 1.00 76.97  ?  194 GLN   B NE2 1 
ATOM   4009 N  N   . GLN   B 1 196 ? -7.566  2.954   20.007 1.00 66.38  ?  195 GLN   B N   1 
ATOM   4010 C  CA  . GLN   B 1 196 ? -6.276  2.765   19.355 1.00 69.17  ?  195 GLN   B CA  1 
ATOM   4011 C  C   . GLN   B 1 196 ? -6.238  1.441   18.595 1.00 73.45  ?  195 GLN   B C   1 
ATOM   4012 O  O   . GLN   B 1 196 ? -6.825  0.437   19.013 1.00 71.61  ?  195 GLN   B O   1 
ATOM   4013 C  CB  . GLN   B 1 196 ? -5.121  2.825   20.362 1.00 75.44  ?  195 GLN   B CB  1 
ATOM   4014 C  CG  . GLN   B 1 196 ? -3.745  2.945   19.710 1.00 82.29  ?  195 GLN   B CG  1 
ATOM   4015 C  CD  . GLN   B 1 196 ? -2.621  2.424   20.593 1.00 88.17  ?  195 GLN   B CD  1 
ATOM   4016 O  OE1 . GLN   B 1 196 ? -2.448  2.874   21.732 1.00 82.79  ?  195 GLN   B OE1 1 
ATOM   4017 N  NE2 . GLN   B 1 196 ? -1.849  1.467   20.069 1.00 86.91  ?  195 GLN   B NE2 1 
ATOM   4018 N  N   . GLN   B 1 197 ? -5.515  1.457   17.480 1.00 67.66  ?  196 GLN   B N   1 
ATOM   4019 C  CA  . GLN   B 1 197 ? -5.528  0.408   16.477 1.00 65.63  ?  196 GLN   B CA  1 
ATOM   4020 C  C   . GLN   B 1 197 ? -4.195  -0.330  16.498 1.00 67.76  ?  196 GLN   B C   1 
ATOM   4021 O  O   . GLN   B 1 197 ? -3.148  0.256   16.782 1.00 72.45  ?  196 GLN   B O   1 
ATOM   4022 C  CB  . GLN   B 1 197 ? -5.795  1.013   15.083 1.00 62.85  ?  196 GLN   B CB  1 
ATOM   4023 C  CG  . GLN   B 1 197 ? -5.876  0.025   13.927 1.00 63.71  ?  196 GLN   B CG  1 
ATOM   4024 C  CD  . GLN   B 1 197 ? -6.712  0.523   12.754 1.00 71.40  ?  196 GLN   B CD  1 
ATOM   4025 O  OE1 . GLN   B 1 197 ? -7.920  0.779   12.886 1.00 71.65  ?  196 GLN   B OE1 1 
ATOM   4026 N  NE2 . GLN   B 1 197 ? -6.072  0.653   11.591 1.00 62.58  ?  196 GLN   B NE2 1 
ATOM   4027 N  N   . THR   B 1 198 ? -4.239  -1.622  16.184 1.00 65.55  ?  197 THR   B N   1 
ATOM   4028 C  CA  . THR   B 1 198 ? -3.058  -2.472  16.182 1.00 60.59  ?  197 THR   B CA  1 
ATOM   4029 C  C   . THR   B 1 198 ? -3.015  -3.289  14.900 1.00 57.90  ?  197 THR   B C   1 
ATOM   4030 O  O   . THR   B 1 198 ? -4.053  -3.637  14.334 1.00 60.10  ?  197 THR   B O   1 
ATOM   4031 C  CB  . THR   B 1 198 ? -3.075  -3.386  17.400 1.00 62.28  ?  197 THR   B CB  1 
ATOM   4032 O  OG1 . THR   B 1 198 ? -3.345  -2.591  18.565 1.00 69.95  ?  197 THR   B OG1 1 
ATOM   4033 C  CG2 . THR   B 1 198 ? -1.759  -4.124  17.558 1.00 58.11  ?  197 THR   B CG2 1 
ATOM   4034 N  N   . THR   B 1 199 ? -1.805  -3.590  14.440 1.00 53.42  ?  198 THR   B N   1 
ATOM   4035 C  CA  . THR   B 1 199 ? -1.602  -4.402  13.243 1.00 59.21  ?  198 THR   B CA  1 
ATOM   4036 C  C   . THR   B 1 199 ? -0.534  -5.445  13.539 1.00 60.47  ?  198 THR   B C   1 
ATOM   4037 O  O   . THR   B 1 199 ? 0.646   -5.111  13.696 1.00 62.61  ?  198 THR   B O   1 
ATOM   4038 C  CB  . THR   B 1 199 ? -1.197  -3.548  12.042 1.00 51.82  ?  198 THR   B CB  1 
ATOM   4039 O  OG1 . THR   B 1 199 ? -2.114  -2.460  11.912 1.00 60.86  ?  198 THR   B OG1 1 
ATOM   4040 C  CG2 . THR   B 1 199 ? -1.195  -4.373  10.784 1.00 46.22  ?  198 THR   B CG2 1 
ATOM   4041 N  N   . LEU   B 1 200 ? -0.937  -6.707  13.587 1.00 56.64  ?  199 LEU   B N   1 
ATOM   4042 C  CA  . LEU   B 1 200 ? -0.025  -7.796  13.884 1.00 62.08  ?  199 LEU   B CA  1 
ATOM   4043 C  C   . LEU   B 1 200 ? -0.004  -8.767  12.710 1.00 59.05  ?  199 LEU   B C   1 
ATOM   4044 O  O   . LEU   B 1 200 ? -1.054  -9.107  12.156 1.00 61.27  ?  199 LEU   B O   1 
ATOM   4045 C  CB  . LEU   B 1 200 ? -0.408  -8.446  15.226 1.00 57.16  ?  199 LEU   B CB  1 
ATOM   4046 C  CG  . LEU   B 1 200 ? -1.861  -8.849  15.422 1.00 58.39  ?  199 LEU   B CG  1 
ATOM   4047 C  CD1 . LEU   B 1 200 ? -1.947  -10.067 16.274 1.00 67.39  ?  199 LEU   B CD1 1 
ATOM   4048 C  CD2 . LEU   B 1 200 ? -2.643  -7.743  16.081 1.00 62.19  ?  199 LEU   B CD2 1 
ATOM   4049 N  N   . LYS   B 1 201 ? 1.199   -9.144  12.286 1.00 57.86  ?  200 LYS   B N   1 
ATOM   4050 C  CA  . LYS   B 1 201 ? 1.407   -10.029 11.150 1.00 59.63  ?  200 LYS   B CA  1 
ATOM   4051 C  C   . LYS   B 1 201 ? 1.898   -11.386 11.646 1.00 57.91  ?  200 LYS   B C   1 
ATOM   4052 O  O   . LYS   B 1 201 ? 2.234   -11.552 12.822 1.00 64.39  ?  200 LYS   B O   1 
ATOM   4053 C  CB  . LYS   B 1 201 ? 2.403   -9.406  10.156 1.00 55.53  ?  200 LYS   B CB  1 
ATOM   4054 C  CG  . LYS   B 1 201 ? 1.909   -8.092  9.557  1.00 68.37  ?  200 LYS   B CG  1 
ATOM   4055 C  CD  . LYS   B 1 201 ? 2.374   -7.857  8.106  1.00 75.05  ?  200 LYS   B CD  1 
ATOM   4056 C  CE  . LYS   B 1 201 ? 3.239   -6.589  7.972  1.00 71.59  ?  200 LYS   B CE  1 
ATOM   4057 N  NZ  . LYS   B 1 201 ? 2.886   -5.768  6.764  1.00 67.40  ?  200 LYS   B NZ  1 
ATOM   4058 N  N   . GLY   B 1 202 ? 1.921   -12.370 10.740 1.00 54.34  ?  201 GLY   B N   1 
ATOM   4059 C  CA  . GLY   B 1 202 ? 2.470   -13.688 11.042 1.00 49.41  ?  201 GLY   B CA  1 
ATOM   4060 C  C   . GLY   B 1 202 ? 1.580   -14.522 11.950 1.00 54.80  ?  201 GLY   B C   1 
ATOM   4061 O  O   . GLY   B 1 202 ? 0.349   -14.434 11.915 1.00 60.98  ?  201 GLY   B O   1 
ATOM   4062 N  N   . VAL   B 1 203 ? 2.220   -15.339 12.796 1.00 53.00  ?  202 VAL   B N   1 
ATOM   4063 C  CA  . VAL   B 1 203 ? 1.475   -16.238 13.674 1.00 45.77  ?  202 VAL   B CA  1 
ATOM   4064 C  C   . VAL   B 1 203 ? 0.569   -15.470 14.626 1.00 49.75  ?  202 VAL   B C   1 
ATOM   4065 O  O   . VAL   B 1 203 ? -0.499  -15.963 15.018 1.00 50.28  ?  202 VAL   B O   1 
ATOM   4066 C  CB  . VAL   B 1 203 ? 2.436   -17.155 14.449 1.00 44.48  ?  202 VAL   B CB  1 
ATOM   4067 C  CG1 . VAL   B 1 203 ? 1.645   -18.041 15.411 1.00 47.64  ?  202 VAL   B CG1 1 
ATOM   4068 C  CG2 . VAL   B 1 203 ? 3.231   -18.023 13.484 1.00 45.86  ?  202 VAL   B CG2 1 
ATOM   4069 N  N   . GLU   B 1 204 ? 0.975   -14.263 15.029 1.00 51.57  ?  203 GLU   B N   1 
ATOM   4070 C  CA  . GLU   B 1 204 ? 0.084   -13.434 15.831 1.00 49.79  ?  203 GLU   B CA  1 
ATOM   4071 C  C   . GLU   B 1 204 ? -1.202  -13.110 15.079 1.00 51.89  ?  203 GLU   B C   1 
ATOM   4072 O  O   . GLU   B 1 204 ? -2.252  -12.898 15.699 1.00 50.86  ?  203 GLU   B O   1 
ATOM   4073 C  CB  . GLU   B 1 204 ? 0.786   -12.140 16.226 1.00 58.43  ?  203 GLU   B CB  1 
ATOM   4074 C  CG  . GLU   B 1 204 ? 1.942   -12.252 17.191 1.00 61.83  ?  203 GLU   B CG  1 
ATOM   4075 C  CD  . GLU   B 1 204 ? 2.380   -10.878 17.664 1.00 79.56  ?  203 GLU   B CD  1 
ATOM   4076 O  OE1 . GLU   B 1 204 ? 2.035   -10.509 18.821 1.00 78.19  ?  203 GLU   B OE1 1 
ATOM   4077 O  OE2 . GLU   B 1 204 ? 3.039   -10.161 16.861 1.00 78.52  -1 203 GLU   B OE2 1 
ATOM   4078 N  N   . ALA   B 1 205 ? -1.144  -13.066 13.745 1.00 50.52  ?  204 ALA   B N   1 
ATOM   4079 C  CA  . ALA   B 1 205 ? -2.329  -12.712 12.983 1.00 47.67  ?  204 ALA   B CA  1 
ATOM   4080 C  C   . ALA   B 1 205 ? -3.381  -13.818 13.021 1.00 50.27  ?  204 ALA   B C   1 
ATOM   4081 O  O   . ALA   B 1 205 ? -4.579  -13.528 12.907 1.00 52.83  ?  204 ALA   B O   1 
ATOM   4082 C  CB  . ALA   B 1 205 ? -1.941  -12.369 11.549 1.00 47.95  ?  204 ALA   B CB  1 
ATOM   4083 N  N   . VAL   B 1 206 ? -2.988  -15.076 13.219 1.00 43.17  ?  205 VAL   B N   1 
ATOM   4084 C  CA  . VAL   B 1 206 ? -3.947  -16.174 13.133 1.00 43.80  ?  205 VAL   B CA  1 
ATOM   4085 C  C   . VAL   B 1 206 ? -4.346  -16.751 14.492 1.00 50.94  ?  205 VAL   B C   1 
ATOM   4086 O  O   . VAL   B 1 206 ? -5.356  -17.475 14.560 1.00 49.84  ?  205 VAL   B O   1 
ATOM   4087 C  CB  . VAL   B 1 206 ? -3.440  -17.302 12.205 1.00 49.02  ?  205 VAL   B CB  1 
ATOM   4088 C  CG1 . VAL   B 1 206 ? -2.819  -16.718 10.937 1.00 50.08  ?  205 VAL   B CG1 1 
ATOM   4089 C  CG2 . VAL   B 1 206 ? -2.465  -18.218 12.893 1.00 47.47  ?  205 VAL   B CG2 1 
ATOM   4090 N  N   . MET   B 1 207 ? -3.622  -16.450 15.574 1.00 47.82  ?  206 MET   B N   1 
ATOM   4091 C  CA  . MET   B 1 207 ? -3.873  -17.078 16.868 1.00 44.75  ?  206 MET   B CA  1 
ATOM   4092 C  C   . MET   B 1 207 ? -4.377  -16.055 17.873 1.00 40.90  ?  206 MET   B C   1 
ATOM   4093 O  O   . MET   B 1 207 ? -3.819  -14.962 17.979 1.00 46.90  ?  206 MET   B O   1 
ATOM   4094 C  CB  . MET   B 1 207 ? -2.608  -17.736 17.406 1.00 42.27  ?  206 MET   B CB  1 
ATOM   4095 C  CG  . MET   B 1 207 ? -2.299  -19.049 16.768 1.00 44.42  ?  206 MET   B CG  1 
ATOM   4096 S  SD  . MET   B 1 207 ? -0.759  -19.721 17.422 1.00 57.50  ?  206 MET   B SD  1 
ATOM   4097 C  CE  . MET   B 1 207 ? -1.365  -20.857 18.663 1.00 47.21  ?  206 MET   B CE  1 
ATOM   4098 N  N   . TYR   B 1 208 ? -5.424  -16.408 18.609 1.00 36.60  ?  207 TYR   B N   1 
ATOM   4099 C  CA  . TYR   B 1 208 ? -5.918  -15.557 19.681 1.00 41.07  ?  207 TYR   B CA  1 
ATOM   4100 C  C   . TYR   B 1 208 ? -6.306  -16.422 20.883 1.00 49.37  ?  207 TYR   B C   1 
ATOM   4101 O  O   . TYR   B 1 208 ? -6.652  -17.603 20.740 1.00 47.25  ?  207 TYR   B O   1 
ATOM   4102 C  CB  . TYR   B 1 208 ? -7.089  -14.696 19.208 1.00 39.82  ?  207 TYR   B CB  1 
ATOM   4103 C  CG  . TYR   B 1 208 ? -7.683  -13.841 20.305 1.00 52.55  ?  207 TYR   B CG  1 
ATOM   4104 C  CD1 . TYR   B 1 208 ? -8.772  -14.298 21.062 1.00 49.10  ?  207 TYR   B CD1 1 
ATOM   4105 C  CD2 . TYR   B 1 208 ? -7.163  -12.564 20.587 1.00 50.62  ?  207 TYR   B CD2 1 
ATOM   4106 C  CE1 . TYR   B 1 208 ? -9.320  -13.513 22.070 1.00 54.18  ?  207 TYR   B CE1 1 
ATOM   4107 C  CE2 . TYR   B 1 208 ? -7.698  -11.771 21.598 1.00 45.80  ?  207 TYR   B CE2 1 
ATOM   4108 C  CZ  . TYR   B 1 208 ? -8.775  -12.248 22.339 1.00 60.34  ?  207 TYR   B CZ  1 
ATOM   4109 O  OH  . TYR   B 1 208 ? -9.326  -11.472 23.347 1.00 66.02  ?  207 TYR   B OH  1 
ATOM   4110 N  N   . MET   B 1 209 ? -6.219  -15.825 22.078 1.00 50.10  ?  208 MET   B N   1 
ATOM   4111 C  CA  . MET   B 1 209 ? -6.417  -16.536 23.342 1.00 50.73  ?  208 MET   B CA  1 
ATOM   4112 C  C   . MET   B 1 209 ? -7.287  -15.697 24.262 1.00 46.98  ?  208 MET   B C   1 
ATOM   4113 O  O   . MET   B 1 209 ? -6.893  -14.595 24.654 1.00 44.96  ?  208 MET   B O   1 
ATOM   4114 C  CB  . MET   B 1 209 ? -5.074  -16.851 24.009 1.00 44.28  ?  208 MET   B CB  1 
ATOM   4115 C  CG  . MET   B 1 209 ? -5.176  -17.502 25.376 1.00 48.15  ?  208 MET   B CG  1 
ATOM   4116 S  SD  . MET   B 1 209 ? -5.681  -19.220 25.235 1.00 60.48  ?  208 MET   B SD  1 
ATOM   4117 C  CE  . MET   B 1 209 ? -5.659  -19.779 26.926 1.00 53.10  ?  208 MET   B CE  1 
ATOM   4118 N  N   . GLY   B 1 210 ? -8.462  -16.212 24.611 1.00 48.88  ?  209 GLY   B N   1 
ATOM   4119 C  CA  . GLY   B 1 210 ? -9.435  -15.376 25.288 1.00 48.21  ?  209 GLY   B CA  1 
ATOM   4120 C  C   . GLY   B 1 210 ? -10.892 -15.702 24.990 1.00 62.12  ?  209 GLY   B C   1 
ATOM   4121 O  O   . GLY   B 1 210 ? -11.709 -15.693 25.923 1.00 61.39  ?  209 GLY   B O   1 
ATOM   4122 N  N   . THR   B 1 211 ? -11.256 -15.961 23.719 1.00 59.07  ?  210 THR   B N   1 
ATOM   4123 C  CA  . THR   B 1 211 ? -12.577 -16.515 23.414 1.00 63.92  ?  210 THR   B CA  1 
ATOM   4124 C  C   . THR   B 1 211 ? -12.506 -17.542 22.289 1.00 58.73  ?  210 THR   B C   1 
ATOM   4125 O  O   . THR   B 1 211 ? -11.619 -17.514 21.425 1.00 51.28  ?  210 THR   B O   1 
ATOM   4126 C  CB  . THR   B 1 211 ? -13.637 -15.455 23.019 1.00 66.66  ?  210 THR   B CB  1 
ATOM   4127 O  OG1 . THR   B 1 211 ? -13.097 -14.542 22.060 1.00 62.66  ?  210 THR   B OG1 1 
ATOM   4128 C  CG2 . THR   B 1 211 ? -14.160 -14.691 24.267 1.00 66.42  ?  210 THR   B CG2 1 
ATOM   4129 N  N   . LEU   B 1 212 ? -13.472 -18.457 22.317 1.00 57.41  ?  211 LEU   B N   1 
ATOM   4130 C  CA  . LEU   B 1 212 ? -13.573 -19.444 21.255 1.00 58.41  ?  211 LEU   B CA  1 
ATOM   4131 C  C   . LEU   B 1 212 ? -14.333 -18.910 20.049 1.00 56.71  ?  211 LEU   B C   1 
ATOM   4132 O  O   . LEU   B 1 212 ? -14.001 -19.277 18.919 1.00 58.26  ?  211 LEU   B O   1 
ATOM   4133 C  CB  . LEU   B 1 212 ? -14.257 -20.712 21.767 1.00 59.58  ?  211 LEU   B CB  1 
ATOM   4134 C  CG  . LEU   B 1 212 ? -13.614 -21.517 22.890 1.00 51.05  ?  211 LEU   B CG  1 
ATOM   4135 C  CD1 . LEU   B 1 212 ? -14.512 -22.680 23.192 1.00 42.09  ?  211 LEU   B CD1 1 
ATOM   4136 C  CD2 . LEU   B 1 212 ? -12.233 -21.991 22.474 1.00 50.94  ?  211 LEU   B CD2 1 
ATOM   4137 N  N   . SER   B 1 213 ? -15.331 -18.041 20.272 1.00 57.78  ?  212 SER   B N   1 
ATOM   4138 C  CA  . SER   B 1 213 ? -16.210 -17.539 19.212 1.00 57.16  ?  212 SER   B CA  1 
ATOM   4139 C  C   . SER   B 1 213 ? -15.498 -16.512 18.321 1.00 55.92  ?  212 SER   B C   1 
ATOM   4140 O  O   . SER   B 1 213 ? -15.140 -15.420 18.775 1.00 57.90  ?  212 SER   B O   1 
ATOM   4141 C  CB  . SER   B 1 213 ? -17.467 -16.922 19.837 1.00 58.87  ?  212 SER   B CB  1 
ATOM   4142 O  OG  . SER   B 1 213 ? -18.072 -15.937 18.999 1.00 54.55  ?  212 SER   B OG  1 
ATOM   4143 N  N   . TYR   B 1 214 ? -15.310 -16.862 17.043 1.00 59.53  ?  213 TYR   B N   1 
ATOM   4144 C  CA  . TYR   B 1 214 ? -14.821 -15.911 16.044 1.00 52.90  ?  213 TYR   B CA  1 
ATOM   4145 C  C   . TYR   B 1 214 ? -15.834 -14.802 15.797 1.00 55.54  ?  213 TYR   B C   1 
ATOM   4146 O  O   . TYR   B 1 214 ? -15.446 -13.666 15.509 1.00 54.80  ?  213 TYR   B O   1 
ATOM   4147 C  CB  . TYR   B 1 214 ? -14.516 -16.659 14.749 1.00 47.31  ?  213 TYR   B CB  1 
ATOM   4148 C  CG  . TYR   B 1 214 ? -13.731 -15.918 13.690 1.00 54.93  ?  213 TYR   B CG  1 
ATOM   4149 C  CD1 . TYR   B 1 214 ? -12.733 -15.004 14.019 1.00 56.76  ?  213 TYR   B CD1 1 
ATOM   4150 C  CD2 . TYR   B 1 214 ? -13.961 -16.178 12.346 1.00 52.04  ?  213 TYR   B CD2 1 
ATOM   4151 C  CE1 . TYR   B 1 214 ? -12.008 -14.354 13.020 1.00 60.73  ?  213 TYR   B CE1 1 
ATOM   4152 C  CE2 . TYR   B 1 214 ? -13.259 -15.535 11.354 1.00 53.18  ?  213 TYR   B CE2 1 
ATOM   4153 C  CZ  . TYR   B 1 214 ? -12.286 -14.628 11.683 1.00 58.59  ?  213 TYR   B CZ  1 
ATOM   4154 O  OH  . TYR   B 1 214 ? -11.599 -14.009 10.660 1.00 49.88  ?  213 TYR   B OH  1 
ATOM   4155 N  N   . GLU   B 1 215 ? -17.132 -15.110 15.917 1.00 56.59  ?  214 GLU   B N   1 
ATOM   4156 C  CA  . GLU   B 1 215 ? -18.154 -14.080 15.765 1.00 56.50  ?  214 GLU   B CA  1 
ATOM   4157 C  C   . GLU   B 1 215 ? -18.063 -13.050 16.887 1.00 60.80  ?  214 GLU   B C   1 
ATOM   4158 O  O   . GLU   B 1 215 ? -18.102 -11.842 16.630 1.00 61.96  ?  214 GLU   B O   1 
ATOM   4159 C  CB  . GLU   B 1 215 ? -19.546 -14.716 15.708 1.00 63.46  ?  214 GLU   B CB  1 
ATOM   4160 C  CG  . GLU   B 1 215 ? -20.060 -15.005 14.277 1.00 79.69  ?  214 GLU   B CG  1 
ATOM   4161 C  CD  . GLU   B 1 215 ? -20.863 -13.850 13.672 1.00 96.60  ?  214 GLU   B CD  1 
ATOM   4162 O  OE1 . GLU   B 1 215 ? -20.356 -12.698 13.713 1.00 96.94  ?  214 GLU   B OE1 1 
ATOM   4163 O  OE2 . GLU   B 1 215 ? -21.999 -14.088 13.172 1.00 92.47  -1 214 GLU   B OE2 1 
ATOM   4164 N  N   . GLN   B 1 216 ? -17.911 -13.501 18.137 1.00 63.78  ?  215 GLN   B N   1 
ATOM   4165 C  CA  . GLN   B 1 216 ? -17.757 -12.553 19.239 1.00 62.80  ?  215 GLN   B CA  1 
ATOM   4166 C  C   . GLN   B 1 216 ? -16.512 -11.691 19.065 1.00 61.85  ?  215 GLN   B C   1 
ATOM   4167 O  O   . GLN   B 1 216 ? -16.509 -10.516 19.453 1.00 60.73  ?  215 GLN   B O   1 
ATOM   4168 C  CB  . GLN   B 1 216 ? -17.694 -13.292 20.574 1.00 60.31  ?  215 GLN   B CB  1 
ATOM   4169 C  CG  . GLN   B 1 216 ? -18.997 -13.296 21.372 1.00 68.29  ?  215 GLN   B CG  1 
ATOM   4170 C  CD  . GLN   B 1 216 ? -19.418 -11.935 21.885 1.00 72.00  ?  215 GLN   B CD  1 
ATOM   4171 O  OE1 . GLN   B 1 216 ? -18.979 -10.890 21.389 1.00 72.62  ?  215 GLN   B OE1 1 
ATOM   4172 N  NE2 . GLN   B 1 216 ? -20.307 -11.941 22.874 1.00 77.39  ?  215 GLN   B NE2 1 
ATOM   4173 N  N   . PHE   B 1 217 ? -15.446 -12.261 18.491 1.00 61.11  ?  216 PHE   B N   1 
ATOM   4174 C  CA  . PHE   B 1 217 ? -14.237 -11.490 18.214 1.00 62.65  ?  216 PHE   B CA  1 
ATOM   4175 C  C   . PHE   B 1 217 ? -14.526 -10.358 17.229 1.00 66.43  ?  216 PHE   B C   1 
ATOM   4176 O  O   . PHE   B 1 217 ? -14.008 -9.241  17.376 1.00 61.81  ?  216 PHE   B O   1 
ATOM   4177 C  CB  . PHE   B 1 217 ? -13.151 -12.428 17.686 1.00 51.71  ?  216 PHE   B CB  1 
ATOM   4178 C  CG  . PHE   B 1 217 ? -11.776 -11.844 17.697 1.00 51.10  ?  216 PHE   B CG  1 
ATOM   4179 C  CD1 . PHE   B 1 217 ? -11.327 -11.113 18.781 1.00 58.74  ?  216 PHE   B CD1 1 
ATOM   4180 C  CD2 . PHE   B 1 217 ? -10.902 -12.073 16.637 1.00 59.01  ?  216 PHE   B CD2 1 
ATOM   4181 C  CE1 . PHE   B 1 217 ? -10.031 -10.587 18.795 1.00 61.54  ?  216 PHE   B CE1 1 
ATOM   4182 C  CE2 . PHE   B 1 217 ? -9.606  -11.557 16.638 1.00 55.10  ?  216 PHE   B CE2 1 
ATOM   4183 C  CZ  . PHE   B 1 217 ? -9.171  -10.811 17.718 1.00 60.14  ?  216 PHE   B CZ  1 
ATOM   4184 N  N   . LYS   B 1 218 ? -15.374 -10.624 16.227 1.00 65.16  ?  217 LYS   B N   1 
ATOM   4185 C  CA  . LYS   B 1 218 ? -15.781 -9.577  15.295 1.00 62.93  ?  217 LYS   B CA  1 
ATOM   4186 C  C   . LYS   B 1 218 ? -16.680 -8.540  15.981 1.00 58.98  ?  217 LYS   B C   1 
ATOM   4187 O  O   . LYS   B 1 218 ? -16.511 -7.333  15.770 1.00 61.79  ?  217 LYS   B O   1 
ATOM   4188 C  CB  . LYS   B 1 218 ? -16.470 -10.206 14.072 1.00 56.29  ?  217 LYS   B CB  1 
ATOM   4189 C  CG  . LYS   B 1 218 ? -15.639 -11.270 13.360 1.00 51.43  ?  217 LYS   B CG  1 
ATOM   4190 C  CD  . LYS   B 1 218 ? -16.485 -12.200 12.494 1.00 53.85  ?  217 LYS   B CD  1 
ATOM   4191 C  CE  . LYS   B 1 218 ? -15.660 -12.805 11.345 1.00 59.45  ?  217 LYS   B CE  1 
ATOM   4192 N  NZ  . LYS   B 1 218 ? -16.470 -13.436 10.238 1.00 54.00  ?  217 LYS   B NZ  1 
ATOM   4193 N  N   . LYS   B 1 219 ? -17.625 -8.977  16.824 1.00 53.60  ?  218 LYS   B N   1 
ATOM   4194 C  CA  . LYS   B 1 219 ? -18.453 -7.999  17.530 1.00 59.15  ?  218 LYS   B CA  1 
ATOM   4195 C  C   . LYS   B 1 219 ? -17.630 -7.250  18.576 1.00 71.19  ?  218 LYS   B C   1 
ATOM   4196 O  O   . LYS   B 1 219 ? -17.743 -6.026  18.688 1.00 73.23  ?  218 LYS   B O   1 
ATOM   4197 C  CB  . LYS   B 1 219 ? -19.698 -8.678  18.145 1.00 64.46  ?  218 LYS   B CB  1 
ATOM   4198 C  CG  . LYS   B 1 219 ? -20.572 -7.822  19.142 1.00 82.76  ?  218 LYS   B CG  1 
ATOM   4199 C  CD  . LYS   B 1 219 ? -19.897 -7.461  20.519 1.00 86.75  ?  218 LYS   B CD  1 
ATOM   4200 C  CE  . LYS   B 1 219 ? -20.568 -6.277  21.250 1.00 89.77  ?  218 LYS   B CE  1 
ATOM   4201 N  NZ  . LYS   B 1 219 ? -19.732 -5.727  22.384 1.00 76.13  ?  218 LYS   B NZ  1 
ATOM   4202 N  N   . GLY   B 1 220 ? -16.813 -7.966  19.363 1.00 68.76  ?  219 GLY   B N   1 
ATOM   4203 C  CA  . GLY   B 1 220 ? -15.989 -7.354  20.387 1.00 65.87  ?  219 GLY   B CA  1 
ATOM   4204 C  C   . GLY   B 1 220 ? -15.989 -8.088  21.720 1.00 73.72  ?  219 GLY   B C   1 
ATOM   4205 O  O   . GLY   B 1 220 ? -17.053 -8.442  22.239 1.00 76.20  ?  219 GLY   B O   1 
ATOM   4206 N  N   . VAL   B 1 221 ? -14.807 -8.322  22.290 1.00 68.90  ?  220 VAL   B N   1 
ATOM   4207 C  CA  . VAL   B 1 221 ? -14.679 -8.914  23.617 1.00 66.58  ?  220 VAL   B CA  1 
ATOM   4208 C  C   . VAL   B 1 221 ? -14.173 -7.870  24.614 1.00 68.80  ?  220 VAL   B C   1 
ATOM   4209 O  O   . VAL   B 1 221 ? -13.576 -6.845  24.254 1.00 65.90  ?  220 VAL   B O   1 
ATOM   4210 C  CB  . VAL   B 1 221 ? -13.765 -10.163 23.629 1.00 60.99  ?  220 VAL   B CB  1 
ATOM   4211 C  CG1 . VAL   B 1 221 ? -14.243 -11.187 22.619 1.00 62.46  ?  220 VAL   B CG1 1 
ATOM   4212 C  CG2 . VAL   B 1 221 ? -12.298 -9.780  23.367 1.00 56.71  ?  220 VAL   B CG2 1 
ATOM   4213 N  N   . GLN   B 1 222 ? -14.423 -8.148  25.895 1.00 65.35  ?  221 GLN   B N   1 
ATOM   4214 C  CA  . GLN   B 1 222 ? -14.003 -7.270  26.977 1.00 72.33  ?  221 GLN   B CA  1 
ATOM   4215 C  C   . GLN   B 1 222 ? -12.617 -7.680  27.476 1.00 69.44  ?  221 GLN   B C   1 
ATOM   4216 O  O   . GLN   B 1 222 ? -12.380 -8.847  27.799 1.00 66.58  ?  221 GLN   B O   1 
ATOM   4217 C  CB  . GLN   B 1 222 ? -15.023 -7.298  28.117 1.00 71.90  ?  221 GLN   B CB  1 
ATOM   4218 C  CG  . GLN   B 1 222 ? -16.367 -6.674  27.771 1.00 64.89  ?  221 GLN   B CG  1 
ATOM   4219 C  CD  . GLN   B 1 222 ? -16.369 -5.166  27.942 1.00 80.97  ?  221 GLN   B CD  1 
ATOM   4220 O  OE1 . GLN   B 1 222 ? -16.018 -4.427  27.014 1.00 77.77  ?  221 GLN   B OE1 1 
ATOM   4221 N  NE2 . GLN   B 1 222 ? -16.764 -4.696  29.132 1.00 85.02  ?  221 GLN   B NE2 1 
ATOM   4222 N  N   . ILE   B 1 223 ? -11.700 -6.722  27.502 1.00 70.68  ?  222 ILE   B N   1 
ATOM   4223 C  CA  . ILE   B 1 223 ? -10.357 -6.923  28.035 1.00 73.08  ?  222 ILE   B CA  1 
ATOM   4224 C  C   . ILE   B 1 223 ? -10.139 -5.792  29.035 1.00 80.20  ?  222 ILE   B C   1 
ATOM   4225 O  O   . ILE   B 1 223 ? -10.950 -4.856  29.078 1.00 84.87  ?  222 ILE   B O   1 
ATOM   4226 C  CB  . ILE   B 1 223 ? -9.295  -6.910  26.923 1.00 74.68  ?  222 ILE   B CB  1 
ATOM   4227 C  CG1 . ILE   B 1 223 ? -9.421  -5.631  26.101 1.00 72.72  ?  222 ILE   B CG1 1 
ATOM   4228 C  CG2 . ILE   B 1 223 ? -9.429  -8.135  26.018 1.00 61.10  ?  222 ILE   B CG2 1 
ATOM   4229 C  CD1 . ILE   B 1 223 ? -8.253  -5.405  25.197 1.00 69.83  ?  222 ILE   B CD1 1 
ATOM   4230 N  N   . PRO   B 1 224 ? -9.084  -5.808  29.852 1.00 86.76  ?  223 PRO   B N   1 
ATOM   4231 C  CA  . PRO   B 1 224 ? -8.924  -4.723  30.831 1.00 86.18  ?  223 PRO   B CA  1 
ATOM   4232 C  C   . PRO   B 1 224 ? -7.987  -3.627  30.349 1.00 85.82  ?  223 PRO   B C   1 
ATOM   4233 O  O   . PRO   B 1 224 ? -6.889  -3.916  29.863 1.00 80.44  ?  223 PRO   B O   1 
ATOM   4234 C  CB  . PRO   B 1 224 ? -8.357  -5.437  32.065 1.00 77.86  ?  223 PRO   B CB  1 
ATOM   4235 C  CG  . PRO   B 1 224 ? -7.742  -6.719  31.532 1.00 80.20  ?  223 PRO   B CG  1 
ATOM   4236 C  CD  . PRO   B 1 224 ? -8.124  -6.899  30.092 1.00 84.54  ?  223 PRO   B CD  1 
ATOM   4237 N  N   . CYS   B 1 225 ? -8.419  -2.374  30.474 1.00 87.02  ?  224 CYS   B N   1 
ATOM   4238 C  CA  . CYS   B 1 225 ? -7.611  -1.221  30.114 1.00 88.02  ?  224 CYS   B CA  1 
ATOM   4239 C  C   . CYS   B 1 225 ? -6.750  -0.775  31.293 1.00 95.88  ?  224 CYS   B C   1 
ATOM   4240 O  O   . CYS   B 1 225 ? -6.962  -1.169  32.444 1.00 92.71  ?  224 CYS   B O   1 
ATOM   4241 C  CB  . CYS   B 1 225 ? -8.504  -0.067  29.652 1.00 94.68  ?  224 CYS   B CB  1 
ATOM   4242 S  SG  . CYS   B 1 225 ? -7.598  1.333   28.908 1.00 94.64  ?  224 CYS   B SG  1 
ATOM   4243 N  N   . THR   B 1 226 ? -5.775  0.087   30.991 1.00 97.42  ?  225 THR   B N   1 
ATOM   4244 C  CA  . THR   B 1 226 ? -4.955  0.672   32.045 1.00 93.45  ?  225 THR   B CA  1 
ATOM   4245 C  C   . THR   B 1 226 ? -5.771  1.571   32.972 1.00 94.73  ?  225 THR   B C   1 
ATOM   4246 O  O   . THR   B 1 226 ? -5.468  1.657   34.167 1.00 94.71  ?  225 THR   B O   1 
ATOM   4247 C  CB  . THR   B 1 226 ? -3.800  1.455   31.428 1.00 95.11  ?  225 THR   B CB  1 
ATOM   4248 O  OG1 . THR   B 1 226 ? -3.340  0.775   30.256 1.00 90.74  ?  225 THR   B OG1 1 
ATOM   4249 C  CG2 . THR   B 1 226 ? -2.656  1.579   32.416 1.00 95.05  ?  225 THR   B CG2 1 
ATOM   4250 N  N   . CYS   B 1 227 ? -6.824  2.218   32.460 1.00 97.53  ?  226 CYS   B N   1 
ATOM   4251 C  CA  . CYS   B 1 227 ? -7.627  3.139   33.267 1.00 101.10 ?  226 CYS   B CA  1 
ATOM   4252 C  C   . CYS   B 1 227 ? -8.386  2.412   34.374 1.00 102.01 ?  226 CYS   B C   1 
ATOM   4253 O  O   . CYS   B 1 227 ? -9.213  3.021   35.067 1.00 99.88  ?  226 CYS   B O   1 
ATOM   4254 C  CB  . CYS   B 1 227 ? -8.635  3.894   32.397 1.00 100.61 ?  226 CYS   B CB  1 
ATOM   4255 S  SG  . CYS   B 1 227 ? -9.612  2.838   31.308 1.00 97.78  ?  226 CYS   B SG  1 
ATOM   4256 N  N   . GLY   B 1 228 ? -8.121  1.116   34.545 1.00 98.41  ?  227 GLY   B N   1 
ATOM   4257 C  CA  . GLY   B 1 228 ? -8.845  0.306   35.509 1.00 101.75 ?  227 GLY   B CA  1 
ATOM   4258 C  C   . GLY   B 1 228 ? -10.229 -0.109  35.073 1.00 103.88 ?  227 GLY   B C   1 
ATOM   4259 O  O   . GLY   B 1 228 ? -10.906 -0.825  35.820 1.00 101.54 ?  227 GLY   B O   1 
ATOM   4260 N  N   . LYS   B 1 229 ? -10.666 0.318   33.890 1.00 102.18 ?  228 LYS   B N   1 
ATOM   4261 C  CA  . LYS   B 1 229 ? -11.979 0.000   33.357 1.00 106.81 ?  228 LYS   B CA  1 
ATOM   4262 C  C   . LYS   B 1 229 ? -11.852 -0.990  32.203 1.00 98.92  ?  228 LYS   B C   1 
ATOM   4263 O  O   . LYS   B 1 229 ? -10.751 -1.362  31.785 1.00 87.29  ?  228 LYS   B O   1 
ATOM   4264 C  CB  . LYS   B 1 229 ? -12.703 1.281   32.915 1.00 108.58 ?  228 LYS   B CB  1 
ATOM   4265 C  CG  . LYS   B 1 229 ? -13.028 2.237   34.073 1.00 119.57 ?  228 LYS   B CG  1 
ATOM   4266 C  CD  . LYS   B 1 229 ? -14.348 1.892   34.791 1.00 153.03 ?  228 LYS   B CD  1 
ATOM   4267 C  CE  . LYS   B 1 229 ? -14.219 0.762   35.819 1.00 120.30 ?  228 LYS   B CE  1 
ATOM   4268 N  NZ  . LYS   B 1 229 ? -14.640 -0.550  35.239 1.00 109.19 ?  228 LYS   B NZ  1 
ATOM   4269 N  N   . GLN   B 1 230 ? -13.007 -1.421  31.698 1.00 96.54  ?  229 GLN   B N   1 
ATOM   4270 C  CA  . GLN   B 1 230 ? -13.084 -2.476  30.696 1.00 87.39  ?  229 GLN   B CA  1 
ATOM   4271 C  C   . GLN   B 1 230 ? -13.140 -1.889  29.296 1.00 82.35  ?  229 GLN   B C   1 
ATOM   4272 O  O   . GLN   B 1 230 ? -13.975 -1.026  29.013 1.00 85.66  ?  229 GLN   B O   1 
ATOM   4273 C  CB  . GLN   B 1 230 ? -14.312 -3.351  30.939 1.00 88.27  ?  229 GLN   B CB  1 
ATOM   4274 C  CG  . GLN   B 1 230 ? -14.199 -4.161  32.193 1.00 89.51  ?  229 GLN   B CG  1 
ATOM   4275 C  CD  . GLN   B 1 230 ? -13.494 -5.460  31.932 1.00 88.44  ?  229 GLN   B CD  1 
ATOM   4276 O  OE1 . GLN   B 1 230 ? -14.117 -6.439  31.510 1.00 87.46  ?  229 GLN   B OE1 1 
ATOM   4277 N  NE2 . GLN   B 1 230 ? -12.175 -5.473  32.136 1.00 85.04  ?  229 GLN   B NE2 1 
ATOM   4278 N  N   . ALA   B 1 231 ? -12.259 -2.368  28.421 1.00 82.16  ?  230 ALA   B N   1 
ATOM   4279 C  CA  . ALA   B 1 231 ? -12.239 -1.958  27.024 1.00 85.62  ?  230 ALA   B CA  1 
ATOM   4280 C  C   . ALA   B 1 231 ? -12.831 -3.038  26.113 1.00 78.76  ?  230 ALA   B C   1 
ATOM   4281 O  O   . ALA   B 1 231 ? -12.923 -4.217  26.470 1.00 75.06  ?  230 ALA   B O   1 
ATOM   4282 C  CB  . ALA   B 1 231 ? -10.813 -1.626  26.581 1.00 81.27  ?  230 ALA   B CB  1 
ATOM   4283 N  N   . THR   B 1 232 ? -13.240 -2.614  24.923 1.00 70.99  ?  231 THR   B N   1 
ATOM   4284 C  CA  . THR   B 1 232 ? -13.807 -3.505  23.918 1.00 73.30  ?  231 THR   B CA  1 
ATOM   4285 C  C   . THR   B 1 232 ? -12.792 -3.683  22.791 1.00 72.24  ?  231 THR   B C   1 
ATOM   4286 O  O   . THR   B 1 232 ? -12.353 -2.700  22.183 1.00 73.80  ?  231 THR   B O   1 
ATOM   4287 C  CB  . THR   B 1 232 ? -15.130 -2.955  23.377 1.00 66.53  ?  231 THR   B CB  1 
ATOM   4288 O  OG1 . THR   B 1 232 ? -15.899 -2.417  24.455 1.00 74.17  ?  231 THR   B OG1 1 
ATOM   4289 C  CG2 . THR   B 1 232 ? -15.936 -4.060  22.739 1.00 72.20  ?  231 THR   B CG2 1 
ATOM   4290 N  N   . LYS   B 1 233 ? -12.418 -4.928  22.513 1.00 61.46  ?  232 LYS   B N   1 
ATOM   4291 C  CA  . LYS   B 1 233 ? -11.502 -5.236  21.427 1.00 65.35  ?  232 LYS   B CA  1 
ATOM   4292 C  C   . LYS   B 1 233 ? -12.264 -5.941  20.301 1.00 65.20  ?  232 LYS   B C   1 
ATOM   4293 O  O   . LYS   B 1 233 ? -13.018 -6.881  20.566 1.00 65.51  ?  232 LYS   B O   1 
ATOM   4294 C  CB  . LYS   B 1 233 ? -10.347 -6.089  21.957 1.00 62.21  ?  232 LYS   B CB  1 
ATOM   4295 C  CG  . LYS   B 1 233 ? -9.156  -6.199  21.019 1.00 66.22  ?  232 LYS   B CG  1 
ATOM   4296 C  CD  . LYS   B 1 233 ? -8.359  -7.462  21.289 1.00 57.22  ?  232 LYS   B CD  1 
ATOM   4297 C  CE  . LYS   B 1 233 ? -6.922  -7.133  21.608 1.00 53.87  ?  232 LYS   B CE  1 
ATOM   4298 N  NZ  . LYS   B 1 233 ? -6.348  -8.151  22.516 1.00 69.07  ?  232 LYS   B NZ  1 
ATOM   4299 N  N   . TYR   B 1 234 ? -12.082 -5.480  19.054 1.00 60.88  ?  233 TYR   B N   1 
ATOM   4300 C  CA  . TYR   B 1 234 ? -12.783 -6.060  17.902 1.00 64.23  ?  233 TYR   B CA  1 
ATOM   4301 C  C   . TYR   B 1 234 ? -11.893 -6.109  16.657 1.00 62.12  ?  233 TYR   B C   1 
ATOM   4302 O  O   . TYR   B 1 234 ? -10.932 -5.345  16.498 1.00 59.66  ?  233 TYR   B O   1 
ATOM   4303 C  CB  . TYR   B 1 234 ? -14.102 -5.313  17.569 1.00 65.49  ?  233 TYR   B CB  1 
ATOM   4304 C  CG  . TYR   B 1 234 ? -13.986 -3.933  16.909 1.00 65.14  ?  233 TYR   B CG  1 
ATOM   4305 C  CD1 . TYR   B 1 234 ? -14.253 -2.772  17.641 1.00 61.63  ?  233 TYR   B CD1 1 
ATOM   4306 C  CD2 . TYR   B 1 234 ? -13.657 -3.794  15.559 1.00 57.51  ?  233 TYR   B CD2 1 
ATOM   4307 C  CE1 . TYR   B 1 234 ? -14.178 -1.511  17.065 1.00 61.65  ?  233 TYR   B CE1 1 
ATOM   4308 C  CE2 . TYR   B 1 234 ? -13.571 -2.522  14.971 1.00 67.33  ?  233 TYR   B CE2 1 
ATOM   4309 C  CZ  . TYR   B 1 234 ? -13.835 -1.384  15.738 1.00 66.36  ?  233 TYR   B CZ  1 
ATOM   4310 O  OH  . TYR   B 1 234 ? -13.759 -0.119  15.191 1.00 62.58  ?  233 TYR   B OH  1 
ATOM   4311 N  N   . LEU   B 1 235 ? -12.270 -7.006  15.750 1.00 59.08  ?  234 LEU   B N   1 
ATOM   4312 C  CA  . LEU   B 1 235 ? -11.494 -7.317  14.558 1.00 54.65  ?  234 LEU   B CA  1 
ATOM   4313 C  C   . LEU   B 1 235 ? -11.866 -6.348  13.429 1.00 65.77  ?  234 LEU   B C   1 
ATOM   4314 O  O   . LEU   B 1 235 ? -13.036 -6.270  13.017 1.00 67.63  ?  234 LEU   B O   1 
ATOM   4315 C  CB  . LEU   B 1 235 ? -11.754 -8.772  14.164 1.00 51.38  ?  234 LEU   B CB  1 
ATOM   4316 C  CG  . LEU   B 1 235 ? -10.997 -9.419  13.000 1.00 61.32  ?  234 LEU   B CG  1 
ATOM   4317 C  CD1 . LEU   B 1 235 ? -9.499  -9.185  13.123 1.00 56.76  ?  234 LEU   B CD1 1 
ATOM   4318 C  CD2 . LEU   B 1 235 ? -11.300 -10.920 12.902 1.00 56.38  ?  234 LEU   B CD2 1 
ATOM   4319 N  N   . VAL   B 1 236 ? -10.881 -5.604  12.934 1.00 59.13  ?  235 VAL   B N   1 
ATOM   4320 C  CA  . VAL   B 1 236 ? -11.119 -4.673  11.831 1.00 59.81  ?  235 VAL   B CA  1 
ATOM   4321 C  C   . VAL   B 1 236 ? -10.886 -5.341  10.485 1.00 59.26  ?  235 VAL   B C   1 
ATOM   4322 O  O   . VAL   B 1 236 ? -11.706 -5.228  9.570  1.00 56.49  ?  235 VAL   B O   1 
ATOM   4323 C  CB  . VAL   B 1 236 ? -10.229 -3.422  11.985 1.00 56.60  ?  235 VAL   B CB  1 
ATOM   4324 C  CG1 . VAL   B 1 236 ? -10.190 -2.643  10.675 1.00 44.82  ?  235 VAL   B CG1 1 
ATOM   4325 C  CG2 . VAL   B 1 236 ? -10.719 -2.560  13.139 1.00 55.44  ?  235 VAL   B CG2 1 
ATOM   4326 N  N   . GLN   B 1 237 ? -9.761  -6.045  10.350 1.00 59.02  ?  236 GLN   B N   1 
ATOM   4327 C  CA  . GLN   B 1 237 ? -9.363  -6.670  9.096  1.00 58.45  ?  236 GLN   B CA  1 
ATOM   4328 C  C   . GLN   B 1 237 ? -8.707  -8.009  9.411  1.00 55.36  ?  236 GLN   B C   1 
ATOM   4329 O  O   . GLN   B 1 237 ? -7.794  -8.085  10.238 1.00 56.95  ?  236 GLN   B O   1 
ATOM   4330 C  CB  . GLN   B 1 237 ? -8.408  -5.749  8.297  1.00 57.61  ?  236 GLN   B CB  1 
ATOM   4331 C  CG  . GLN   B 1 237 ? -8.252  -6.064  6.798  1.00 53.03  ?  236 GLN   B CG  1 
ATOM   4332 C  CD  . GLN   B 1 237 ? -7.150  -5.234  6.114  1.00 61.70  ?  236 GLN   B CD  1 
ATOM   4333 O  OE1 . GLN   B 1 237 ? -6.689  -4.213  6.644  1.00 58.86  ?  236 GLN   B OE1 1 
ATOM   4334 N  NE2 . GLN   B 1 237 ? -6.710  -5.691  4.937  1.00 54.32  ?  236 GLN   B NE2 1 
ATOM   4335 N  N   . GLN   B 1 238 ? -9.193  -9.066  8.781  1.00 58.18  ?  237 GLN   B N   1 
ATOM   4336 C  CA  . GLN   B 1 238 ? -8.524  -10.353 8.821  1.00 53.30  ?  237 GLN   B CA  1 
ATOM   4337 C  C   . GLN   B 1 238 ? -8.089  -10.739 7.413  1.00 54.89  ?  237 GLN   B C   1 
ATOM   4338 O  O   . GLN   B 1 238 ? -8.754  -10.418 6.423  1.00 55.45  ?  237 GLN   B O   1 
ATOM   4339 C  CB  . GLN   B 1 238 ? -9.405  -11.447 9.410  1.00 54.03  ?  237 GLN   B CB  1 
ATOM   4340 C  CG  . GLN   B 1 238 ? -8.642  -12.750 9.593  1.00 58.08  ?  237 GLN   B CG  1 
ATOM   4341 C  CD  . GLN   B 1 238 ? -7.539  -12.647 10.637 1.00 52.83  ?  237 GLN   B CD  1 
ATOM   4342 O  OE1 . GLN   B 1 238 ? -7.654  -11.894 11.599 1.00 55.97  ?  237 GLN   B OE1 1 
ATOM   4343 N  NE2 . GLN   B 1 238 ? -6.441  -13.359 10.415 1.00 49.57  ?  237 GLN   B NE2 1 
ATOM   4344 N  N   . GLU   B 1 239 ? -6.953  -11.437 7.339  1.00 55.96  ?  238 GLU   B N   1 
ATOM   4345 C  CA  . GLU   B 1 239 ? -6.293  -11.790 6.100  1.00 53.84  ?  238 GLU   B CA  1 
ATOM   4346 C  C   . GLU   B 1 239 ? -5.476  -13.062 6.361  1.00 51.15  ?  238 GLU   B C   1 
ATOM   4347 O  O   . GLU   B 1 239 ? -4.284  -13.004 6.653  1.00 51.64  ?  238 GLU   B O   1 
ATOM   4348 C  CB  . GLU   B 1 239 ? -5.419  -10.637 5.608  1.00 51.90  ?  238 GLU   B CB  1 
ATOM   4349 C  CG  . GLU   B 1 239 ? -5.242  -10.667 4.123  1.00 67.38  ?  238 GLU   B CG  1 
ATOM   4350 C  CD  . GLU   B 1 239 ? -6.322  -9.868  3.390  1.00 74.43  ?  238 GLU   B CD  1 
ATOM   4351 O  OE1 . GLU   B 1 239 ? -6.392  -9.975  2.137  1.00 81.58  ?  238 GLU   B OE1 1 
ATOM   4352 O  OE2 . GLU   B 1 239 ? -7.080  -9.124  4.064  1.00 67.63  -1 238 GLU   B OE2 1 
ATOM   4353 N  N   . SER   B 1 240 ? -6.135  -14.223 6.265  1.00 54.38  ?  239 SER   B N   1 
ATOM   4354 C  CA  . SER   B 1 240 ? -5.475  -15.507 6.503  1.00 54.82  ?  239 SER   B CA  1 
ATOM   4355 C  C   . SER   B 1 240 ? -6.343  -16.640 5.945  1.00 54.41  ?  239 SER   B C   1 
ATOM   4356 O  O   . SER   B 1 240 ? -7.572  -16.508 5.851  1.00 55.14  ?  239 SER   B O   1 
ATOM   4357 C  CB  . SER   B 1 240 ? -5.204  -15.730 8.004  1.00 54.16  ?  239 SER   B CB  1 
ATOM   4358 O  OG  . SER   B 1 240 ? -6.371  -15.486 8.775  1.00 55.65  ?  239 SER   B OG  1 
ATOM   4359 N  N   . PRO   B 1 241 ? -5.736  -17.782 5.605  1.00 45.99  ?  240 PRO   B N   1 
ATOM   4360 C  CA  . PRO   B 1 241 ? -6.535  -18.951 5.216  1.00 42.25  ?  240 PRO   B CA  1 
ATOM   4361 C  C   . PRO   B 1 241 ? -7.294  -19.596 6.356  1.00 51.20  ?  240 PRO   B C   1 
ATOM   4362 O  O   . PRO   B 1 241 ? -8.042  -20.549 6.092  1.00 53.47  ?  240 PRO   B O   1 
ATOM   4363 C  CB  . PRO   B 1 241 ? -5.500  -19.933 4.661  1.00 50.35  ?  240 PRO   B CB  1 
ATOM   4364 C  CG  . PRO   B 1 241 ? -4.160  -19.384 4.996  1.00 47.51  ?  240 PRO   B CG  1 
ATOM   4365 C  CD  . PRO   B 1 241 ? -4.288  -18.048 5.618  1.00 47.51  ?  240 PRO   B CD  1 
ATOM   4366 N  N   . PHE   B 1 242 ? -7.102  -19.158 7.605  1.00 54.09  ?  241 PHE   B N   1 
ATOM   4367 C  CA  . PHE   B 1 242 ? -7.795  -19.717 8.768  1.00 53.56  ?  241 PHE   B CA  1 
ATOM   4368 C  C   . PHE   B 1 242 ? -7.499  -18.840 9.974  1.00 55.53  ?  241 PHE   B C   1 
ATOM   4369 O  O   . PHE   B 1 242 ? -6.609  -17.986 9.938  1.00 52.69  ?  241 PHE   B O   1 
ATOM   4370 C  CB  . PHE   B 1 242 ? -7.384  -21.165 9.075  1.00 48.67  ?  241 PHE   B CB  1 
ATOM   4371 C  CG  . PHE   B 1 242 ? -5.937  -21.325 9.469  1.00 49.87  ?  241 PHE   B CG  1 
ATOM   4372 C  CD1 . PHE   B 1 242 ? -4.935  -21.422 8.498  1.00 50.42  ?  241 PHE   B CD1 1 
ATOM   4373 C  CD2 . PHE   B 1 242 ? -5.569  -21.379 10.811 1.00 49.48  ?  241 PHE   B CD2 1 
ATOM   4374 C  CE1 . PHE   B 1 242 ? -3.591  -21.575 8.862  1.00 44.00  ?  241 PHE   B CE1 1 
ATOM   4375 C  CE2 . PHE   B 1 242 ? -4.225  -21.530 11.176 1.00 45.75  ?  241 PHE   B CE2 1 
ATOM   4376 C  CZ  . PHE   B 1 242 ? -3.240  -21.626 10.198 1.00 41.97  ?  241 PHE   B CZ  1 
ATOM   4377 N  N   . VAL   B 1 243 ? -8.252  -19.070 11.050 1.00 48.58  ?  242 VAL   B N   1 
ATOM   4378 C  CA  . VAL   B 1 243 ? -7.950  -18.480 12.345 1.00 46.27  ?  242 VAL   B CA  1 
ATOM   4379 C  C   . VAL   B 1 243 ? -8.108  -19.551 13.420 1.00 52.07  ?  242 VAL   B C   1 
ATOM   4380 O  O   . VAL   B 1 243 ? -9.033  -20.372 13.368 1.00 56.14  ?  242 VAL   B O   1 
ATOM   4381 C  CB  . VAL   B 1 243 ? -8.829  -17.240 12.648 1.00 51.56  ?  242 VAL   B CB  1 
ATOM   4382 C  CG1 . VAL   B 1 243 ? -8.490  -16.088 11.694 1.00 51.07  ?  242 VAL   B CG1 1 
ATOM   4383 C  CG2 . VAL   B 1 243 ? -10.331 -17.569 12.628 1.00 48.90  ?  242 VAL   B CG2 1 
ATOM   4384 N  N   . MET   B 1 244 ? -7.198  -19.553 14.390 1.00 46.84  ?  243 MET   B N   1 
ATOM   4385 C  CA  . MET   B 1 244 ? -7.344  -20.378 15.576 1.00 46.90  ?  243 MET   B CA  1 
ATOM   4386 C  C   . MET   B 1 244 ? -7.795  -19.518 16.742 1.00 42.20  ?  243 MET   B C   1 
ATOM   4387 O  O   . MET   B 1 244 ? -7.239  -18.439 16.967 1.00 46.11  ?  243 MET   B O   1 
ATOM   4388 C  CB  . MET   B 1 244 ? -6.036  -21.089 15.885 1.00 49.24  ?  243 MET   B CB  1 
ATOM   4389 C  CG  . MET   B 1 244 ? -6.214  -22.318 16.728 1.00 51.54  ?  243 MET   B CG  1 
ATOM   4390 S  SD  . MET   B 1 244 ? -4.878  -22.580 17.877 1.00 56.64  ?  243 MET   B SD  1 
ATOM   4391 C  CE  . MET   B 1 244 ? -3.555  -22.577 16.705 1.00 50.54  ?  243 MET   B CE  1 
ATOM   4392 N  N   . MET   B 1 245 ? -8.826  -19.973 17.453 1.00 38.94  ?  244 MET   B N   1 
ATOM   4393 C  CA  . MET   B 1 245 ? -9.366  -19.236 18.588 1.00 43.72  ?  244 MET   B CA  1 
ATOM   4394 C  C   . MET   B 1 245 ? -9.328  -20.134 19.814 1.00 50.70  ?  244 MET   B C   1 
ATOM   4395 O  O   . MET   B 1 245 ? -9.928  -21.210 19.820 1.00 56.06  ?  244 MET   B O   1 
ATOM   4396 C  CB  . MET   B 1 245 ? -10.780 -18.753 18.300 1.00 44.31  ?  244 MET   B CB  1 
ATOM   4397 C  CG  . MET   B 1 245 ? -10.818 -17.946 17.032 1.00 45.91  ?  244 MET   B CG  1 
ATOM   4398 S  SD  . MET   B 1 245 ? -10.378 -16.210 17.193 1.00 52.00  ?  244 MET   B SD  1 
ATOM   4399 C  CE  . MET   B 1 245 ? -11.260 -15.697 18.688 1.00 49.34  ?  244 MET   B CE  1 
ATOM   4400 N  N   . SER   B 1 246 ? -8.595  -19.721 20.832 1.00 47.69  ?  245 SER   B N   1 
ATOM   4401 C  CA  . SER   B 1 246 ? -8.402  -20.554 21.999 1.00 45.43  ?  245 SER   B CA  1 
ATOM   4402 C  C   . SER   B 1 246 ? -8.859  -19.793 23.223 1.00 50.32  ?  245 SER   B C   1 
ATOM   4403 O  O   . SER   B 1 246 ? -8.781  -18.557 23.277 1.00 50.68  ?  245 SER   B O   1 
ATOM   4404 C  CB  . SER   B 1 246 ? -6.940  -20.972 22.155 1.00 51.52  ?  245 SER   B CB  1 
ATOM   4405 O  OG  . SER   B 1 246 ? -6.524  -21.802 21.072 1.00 54.34  ?  245 SER   B OG  1 
ATOM   4406 N  N   . ALA   B 1 247 ? -9.377  -20.540 24.188 1.00 49.60  ?  246 ALA   B N   1 
ATOM   4407 C  CA  . ALA   B 1 247 ? -9.711  -20.003 25.499 1.00 55.21  ?  246 ALA   B CA  1 
ATOM   4408 C  C   . ALA   B 1 247 ? -9.559  -21.129 26.510 1.00 59.36  ?  246 ALA   B C   1 
ATOM   4409 O  O   . ALA   B 1 247 ? -9.569  -22.307 26.136 1.00 60.62  ?  246 ALA   B O   1 
ATOM   4410 C  CB  . ALA   B 1 247 ? -11.134 -19.424 25.535 1.00 48.42  ?  246 ALA   B CB  1 
ATOM   4411 N  N   . PRO   B 1 248 ? -9.374  -20.812 27.784 1.00 61.92  ?  247 PRO   B N   1 
ATOM   4412 C  CA  . PRO   B 1 248 ? -9.344  -21.863 28.790 1.00 59.21  ?  247 PRO   B CA  1 
ATOM   4413 C  C   . PRO   B 1 248 ? -10.534 -22.781 28.608 1.00 56.48  ?  247 PRO   B C   1 
ATOM   4414 O  O   . PRO   B 1 248 ? -11.590 -22.335 28.130 1.00 62.37  ?  247 PRO   B O   1 
ATOM   4415 C  CB  . PRO   B 1 248 ? -9.416  -21.091 30.110 1.00 53.29  ?  247 PRO   B CB  1 
ATOM   4416 C  CG  . PRO   B 1 248 ? -8.751  -19.766 29.783 1.00 52.09  ?  247 PRO   B CG  1 
ATOM   4417 C  CD  . PRO   B 1 248 ? -8.835  -19.548 28.294 1.00 58.99  ?  247 PRO   B CD  1 
ATOM   4418 N  N   . PRO   B 1 249 ? -10.379 -24.073 28.894 1.00 57.03  ?  248 PRO   B N   1 
ATOM   4419 C  CA  . PRO   B 1 249 ? -11.510 -25.008 28.777 1.00 54.93  ?  248 PRO   B CA  1 
ATOM   4420 C  C   . PRO   B 1 249 ? -12.772 -24.511 29.472 1.00 57.23  ?  248 PRO   B C   1 
ATOM   4421 O  O   . PRO   B 1 249 ? -12.749 -24.066 30.629 1.00 50.83  ?  248 PRO   B O   1 
ATOM   4422 C  CB  . PRO   B 1 249 ? -10.970 -26.285 29.424 1.00 51.87  ?  248 PRO   B CB  1 
ATOM   4423 C  CG  . PRO   B 1 249 ? -9.487  -26.229 29.138 1.00 48.22  ?  248 PRO   B CG  1 
ATOM   4424 C  CD  . PRO   B 1 249 ? -9.116  -24.768 29.212 1.00 54.46  ?  248 PRO   B CD  1 
ATOM   4425 N  N   . ALA   B 1 250 ? -13.879 -24.573 28.735 1.00 58.49  ?  249 ALA   B N   1 
ATOM   4426 C  CA  . ALA   B 1 250 ? -15.199 -24.247 29.255 1.00 57.90  ?  249 ALA   B CA  1 
ATOM   4427 C  C   . ALA   B 1 250 ? -16.232 -24.993 28.418 1.00 60.98  ?  249 ALA   B C   1 
ATOM   4428 O  O   . ALA   B 1 250 ? -15.919 -25.540 27.355 1.00 62.85  ?  249 ALA   B O   1 
ATOM   4429 C  CB  . ALA   B 1 250 ? -15.446 -22.740 29.240 1.00 49.06  ?  249 ALA   B CB  1 
ATOM   4430 N  N   . GLN   B 1 251 ? -17.463 -25.036 28.928 1.00 61.53  ?  250 GLN   B N   1 
ATOM   4431 C  CA  . GLN   B 1 251 ? -18.561 -25.645 28.187 1.00 59.47  ?  250 GLN   B CA  1 
ATOM   4432 C  C   . GLN   B 1 251 ? -18.948 -24.741 27.025 1.00 65.05  ?  250 GLN   B C   1 
ATOM   4433 O  O   . GLN   B 1 251 ? -19.166 -23.538 27.210 1.00 60.71  ?  250 GLN   B O   1 
ATOM   4434 C  CB  . GLN   B 1 251 ? -19.766 -25.888 29.098 1.00 59.82  ?  250 GLN   B CB  1 
ATOM   4435 C  CG  . GLN   B 1 251 ? -19.563 -26.999 30.107 1.00 50.60  ?  250 GLN   B CG  1 
ATOM   4436 C  CD  . GLN   B 1 251 ? -19.605 -28.365 29.450 1.00 62.59  ?  250 GLN   B CD  1 
ATOM   4437 O  OE1 . GLN   B 1 251 ? -20.544 -28.688 28.719 1.00 67.52  ?  250 GLN   B OE1 1 
ATOM   4438 N  NE2 . GLN   B 1 251 ? -18.567 -29.159 29.672 1.00 63.53  ?  250 GLN   B NE2 1 
ATOM   4439 N  N   . TYR   B 1 252 ? -19.014 -25.320 25.825 1.00 63.77  ?  251 TYR   B N   1 
ATOM   4440 C  CA  . TYR   B 1 252 ? -19.297 -24.591 24.597 1.00 56.30  ?  251 TYR   B CA  1 
ATOM   4441 C  C   . TYR   B 1 252 ? -20.262 -25.420 23.772 1.00 59.31  ?  251 TYR   B C   1 
ATOM   4442 O  O   . TYR   B 1 252 ? -20.207 -26.654 23.787 1.00 60.42  ?  251 TYR   B O   1 
ATOM   4443 C  CB  . TYR   B 1 252 ? -18.013 -24.334 23.790 1.00 56.28  ?  251 TYR   B CB  1 
ATOM   4444 C  CG  . TYR   B 1 252 ? -18.043 -23.253 22.706 1.00 57.16  ?  251 TYR   B CG  1 
ATOM   4445 C  CD1 . TYR   B 1 252 ? -17.820 -23.582 21.367 1.00 54.17  ?  251 TYR   B CD1 1 
ATOM   4446 C  CD2 . TYR   B 1 252 ? -18.223 -21.906 23.024 1.00 47.03  ?  251 TYR   B CD2 1 
ATOM   4447 C  CE1 . TYR   B 1 252 ? -17.805 -22.607 20.373 1.00 58.38  ?  251 TYR   B CE1 1 
ATOM   4448 C  CE2 . TYR   B 1 252 ? -18.209 -20.923 22.042 1.00 48.88  ?  251 TYR   B CE2 1 
ATOM   4449 C  CZ  . TYR   B 1 252 ? -18.001 -21.270 20.709 1.00 60.70  ?  251 TYR   B CZ  1 
ATOM   4450 O  OH  . TYR   B 1 252 ? -17.985 -20.285 19.713 1.00 52.43  ?  251 TYR   B OH  1 
ATOM   4451 N  N   . GLU   B 1 253 ? -21.146 -24.740 23.052 1.00 57.56  ?  252 GLU   B N   1 
ATOM   4452 C  CA  . GLU   B 1 253 ? -21.989 -25.391 22.062 1.00 61.02  ?  252 GLU   B CA  1 
ATOM   4453 C  C   . GLU   B 1 253 ? -21.365 -25.190 20.680 1.00 66.97  ?  252 GLU   B C   1 
ATOM   4454 O  O   . GLU   B 1 253 ? -21.067 -24.055 20.281 1.00 61.83  ?  252 GLU   B O   1 
ATOM   4455 C  CB  . GLU   B 1 253 ? -23.415 -24.849 22.124 1.00 63.64  ?  252 GLU   B CB  1 
ATOM   4456 C  CG  . GLU   B 1 253 ? -24.390 -25.581 21.215 1.00 80.46  ?  252 GLU   B CG  1 
ATOM   4457 C  CD  . GLU   B 1 253 ? -25.817 -25.550 21.736 1.00 87.04  ?  252 GLU   B CD  1 
ATOM   4458 O  OE1 . GLU   B 1 253 ? -26.712 -26.122 21.069 1.00 88.80  ?  252 GLU   B OE1 1 
ATOM   4459 O  OE2 . GLU   B 1 253 ? -26.036 -24.964 22.820 1.00 84.16  -1 252 GLU   B OE2 1 
ATOM   4460 N  N   . LEU   B 1 254 ? -21.123 -26.297 19.980 1.00 69.33  ?  253 LEU   B N   1 
ATOM   4461 C  CA  . LEU   B 1 254 ? -20.640 -26.299 18.606 1.00 70.46  ?  253 LEU   B CA  1 
ATOM   4462 C  C   . LEU   B 1 254 ? -21.782 -26.715 17.689 1.00 72.16  ?  253 LEU   B C   1 
ATOM   4463 O  O   . LEU   B 1 254 ? -22.600 -27.564 18.060 1.00 77.03  ?  253 LEU   B O   1 
ATOM   4464 C  CB  . LEU   B 1 254 ? -19.452 -27.256 18.442 1.00 69.30  ?  253 LEU   B CB  1 
ATOM   4465 C  CG  . LEU   B 1 254 ? -18.093 -26.931 19.074 1.00 59.94  ?  253 LEU   B CG  1 
ATOM   4466 C  CD1 . LEU   B 1 254 ? -17.133 -28.116 18.902 1.00 59.68  ?  253 LEU   B CD1 1 
ATOM   4467 C  CD2 . LEU   B 1 254 ? -17.492 -25.676 18.472 1.00 46.76  ?  253 LEU   B CD2 1 
ATOM   4468 N  N   . LYS   B 1 255 ? -21.841 -26.116 16.496 1.00 68.85  ?  254 LYS   B N   1 
ATOM   4469 C  CA  . LYS   B 1 255 ? -22.985 -26.257 15.597 1.00 75.40  ?  254 LYS   B CA  1 
ATOM   4470 C  C   . LYS   B 1 255 ? -22.554 -26.700 14.204 1.00 72.10  ?  254 LYS   B C   1 
ATOM   4471 O  O   . LYS   B 1 255 ? -21.539 -26.238 13.680 1.00 65.52  ?  254 LYS   B O   1 
ATOM   4472 C  CB  . LYS   B 1 255 ? -23.770 -24.946 15.464 1.00 68.59  ?  254 LYS   B CB  1 
ATOM   4473 C  CG  . LYS   B 1 255 ? -25.030 -24.864 16.289 1.00 64.89  ?  254 LYS   B CG  1 
ATOM   4474 C  CD  . LYS   B 1 255 ? -25.132 -23.515 16.957 1.00 72.68  ?  254 LYS   B CD  1 
ATOM   4475 C  CE  . LYS   B 1 255 ? -26.389 -23.423 17.793 1.00 80.44  ?  254 LYS   B CE  1 
ATOM   4476 N  NZ  . LYS   B 1 255 ? -26.603 -24.672 18.563 1.00 85.76  ?  254 LYS   B NZ  1 
ATOM   4477 N  N   . HIS   B 1 256 ? -23.342 -27.577 13.588 1.00 76.55  ?  255 HIS   B N   1 
ATOM   4478 C  CA  . HIS   B 1 256 ? -22.993 -28.039 12.251 1.00 71.12  ?  255 HIS   B CA  1 
ATOM   4479 C  C   . HIS   B 1 256 ? -22.825 -26.856 11.305 1.00 69.59  ?  255 HIS   B C   1 
ATOM   4480 O  O   . HIS   B 1 256 ? -23.757 -26.069 11.113 1.00 67.91  ?  255 HIS   B O   1 
ATOM   4481 C  CB  . HIS   B 1 256 ? -24.060 -28.986 11.708 1.00 75.07  ?  255 HIS   B CB  1 
ATOM   4482 C  CG  . HIS   B 1 256 ? -23.802 -29.390 10.297 1.00 73.99  ?  255 HIS   B CG  1 
ATOM   4483 N  ND1 . HIS   B 1 256 ? -24.424 -28.783 9.228  1.00 80.96  ?  255 HIS   B ND1 1 
ATOM   4484 C  CD2 . HIS   B 1 256 ? -22.937 -30.290 9.773  1.00 74.43  ?  255 HIS   B CD2 1 
ATOM   4485 C  CE1 . HIS   B 1 256 ? -23.968 -29.305 8.104  1.00 83.97  ?  255 HIS   B CE1 1 
ATOM   4486 N  NE2 . HIS   B 1 256 ? -23.066 -30.224 8.407  1.00 84.35  ?  255 HIS   B NE2 1 
ATOM   4487 N  N   . GLY   B 1 257 ? -21.626 -26.718 10.734 1.00 62.78  ?  256 GLY   B N   1 
ATOM   4488 C  CA  . GLY   B 1 257 ? -21.376 -25.764 9.681  1.00 55.10  ?  256 GLY   B CA  1 
ATOM   4489 C  C   . GLY   B 1 257 ? -20.842 -24.409 10.108 1.00 62.33  ?  256 GLY   B C   1 
ATOM   4490 O  O   . GLY   B 1 257 ? -20.468 -23.614 9.233  1.00 61.32  ?  256 GLY   B O   1 
ATOM   4491 N  N   . THR   B 1 258 ? -20.796 -24.109 11.413 1.00 64.28  ?  257 THR   B N   1 
ATOM   4492 C  CA  . THR   B 1 258 ? -20.331 -22.808 11.883 1.00 61.00  ?  257 THR   B CA  1 
ATOM   4493 C  C   . THR   B 1 258 ? -18.806 -22.730 12.028 1.00 60.13  ?  257 THR   B C   1 
ATOM   4494 O  O   . THR   B 1 258 ? -18.274 -21.620 12.195 1.00 54.77  ?  257 THR   B O   1 
ATOM   4495 C  CB  . THR   B 1 258 ? -20.982 -22.453 13.238 1.00 63.76  ?  257 THR   B CB  1 
ATOM   4496 O  OG1 . THR   B 1 258 ? -20.322 -21.316 13.813 1.00 72.82  ?  257 THR   B OG1 1 
ATOM   4497 C  CG2 . THR   B 1 258 ? -20.806 -23.566 14.229 1.00 55.74  ?  257 THR   B CG2 1 
ATOM   4498 N  N   . PHE   B 1 259 ? -18.099 -23.867 11.969 1.00 56.88  ?  258 PHE   B N   1 
ATOM   4499 C  CA  . PHE   B 1 259 ? -16.676 -23.954 12.298 1.00 53.24  ?  258 PHE   B CA  1 
ATOM   4500 C  C   . PHE   B 1 259 ? -16.074 -25.115 11.518 1.00 45.84  ?  258 PHE   B C   1 
ATOM   4501 O  O   . PHE   B 1 259 ? -16.786 -25.865 10.856 1.00 51.30  ?  258 PHE   B O   1 
ATOM   4502 C  CB  . PHE   B 1 259 ? -16.457 -24.145 13.805 1.00 52.69  ?  258 PHE   B CB  1 
ATOM   4503 C  CG  . PHE   B 1 259 ? -16.787 -25.541 14.290 1.00 57.76  ?  258 PHE   B CG  1 
ATOM   4504 C  CD1 . PHE   B 1 259 ? -15.772 -26.455 14.579 1.00 55.21  ?  258 PHE   B CD1 1 
ATOM   4505 C  CD2 . PHE   B 1 259 ? -18.105 -25.949 14.436 1.00 53.61  ?  258 PHE   B CD2 1 
ATOM   4506 C  CE1 . PHE   B 1 259 ? -16.073 -27.743 15.009 1.00 53.55  ?  258 PHE   B CE1 1 
ATOM   4507 C  CE2 . PHE   B 1 259 ? -18.406 -27.239 14.866 1.00 55.26  ?  258 PHE   B CE2 1 
ATOM   4508 C  CZ  . PHE   B 1 259 ? -17.392 -28.131 15.148 1.00 56.67  ?  258 PHE   B CZ  1 
ATOM   4509 N  N   . THR   B 1 260 ? -14.757 -25.281 11.620 1.00 46.53  ?  259 THR   B N   1 
ATOM   4510 C  CA  . THR   B 1 260 ? -14.030 -26.291 10.854 1.00 44.71  ?  259 THR   B CA  1 
ATOM   4511 C  C   . THR   B 1 260 ? -13.673 -27.516 11.684 1.00 48.13  ?  259 THR   B C   1 
ATOM   4512 O  O   . THR   B 1 260 ? -13.882 -28.651 11.246 1.00 48.91  ?  259 THR   B O   1 
ATOM   4513 C  CB  . THR   B 1 260 ? -12.746 -25.702 10.272 1.00 41.79  ?  259 THR   B CB  1 
ATOM   4514 O  OG1 . THR   B 1 260 ? -13.067 -24.623 9.391  1.00 50.72  ?  259 THR   B OG1 1 
ATOM   4515 C  CG2 . THR   B 1 260 ? -11.952 -26.781 9.519  1.00 38.17  ?  259 THR   B CG2 1 
ATOM   4516 N  N   . CYS   B 1 261 ? -13.092 -27.302 12.861 1.00 48.25  ?  260 CYS   B N   1 
ATOM   4517 C  CA  . CYS   B 1 261 ? -12.805 -28.361 13.813 1.00 50.01  ?  260 CYS   B CA  1 
ATOM   4518 C  C   . CYS   B 1 261 ? -12.436 -27.701 15.125 1.00 48.59  ?  260 CYS   B C   1 
ATOM   4519 O  O   . CYS   B 1 261 ? -12.201 -26.491 15.178 1.00 48.77  ?  260 CYS   B O   1 
ATOM   4520 C  CB  . CYS   B 1 261 ? -11.700 -29.311 13.326 1.00 48.54  ?  260 CYS   B CB  1 
ATOM   4521 S  SG  . CYS   B 1 261 ? -10.153 -28.511 12.915 1.00 44.31  ?  260 CYS   B SG  1 
ATOM   4522 N  N   . ALA   B 1 262 ? -12.420 -28.507 16.189 1.00 50.80  ?  261 ALA   B N   1 
ATOM   4523 C  CA  . ALA   B 1 262 ? -12.209 -28.018 17.546 1.00 49.83  ?  261 ALA   B CA  1 
ATOM   4524 C  C   . ALA   B 1 262 ? -11.410 -29.036 18.351 1.00 53.36  ?  261 ALA   B C   1 
ATOM   4525 O  O   . ALA   B 1 262 ? -11.243 -30.196 17.949 1.00 52.36  ?  261 ALA   B O   1 
ATOM   4526 C  CB  . ALA   B 1 262 ? -13.540 -27.716 18.243 1.00 50.80  ?  261 ALA   B CB  1 
ATOM   4527 N  N   . SER   B 1 263 ? -10.901 -28.584 19.502 1.00 53.89  ?  262 SER   B N   1 
ATOM   4528 C  CA  . SER   B 1 263 ? -10.277 -29.459 20.494 1.00 54.09  ?  262 SER   B CA  1 
ATOM   4529 C  C   . SER   B 1 263 ? -11.188 -29.581 21.714 1.00 52.82  ?  262 SER   B C   1 
ATOM   4530 O  O   . SER   B 1 263 ? -11.550 -28.567 22.325 1.00 50.34  ?  262 SER   B O   1 
ATOM   4531 C  CB  . SER   B 1 263 ? -8.910  -28.931 20.905 1.00 49.43  ?  262 SER   B CB  1 
ATOM   4532 O  OG  . SER   B 1 263 ? -8.157  -28.591 19.765 1.00 53.91  ?  262 SER   B OG  1 
ATOM   4533 N  N   . GLU   B 1 264 ? -11.589 -30.819 22.032 1.00 52.03  ?  263 GLU   B N   1 
ATOM   4534 C  CA  . GLU   B 1 264 ? -12.301 -31.135 23.261 1.00 54.82  ?  263 GLU   B CA  1 
ATOM   4535 C  C   . GLU   B 1 264 ? -11.300 -31.566 24.324 1.00 55.74  ?  263 GLU   B C   1 
ATOM   4536 O  O   . GLU   B 1 264 ? -10.399 -32.368 24.055 1.00 54.54  ?  263 GLU   B O   1 
ATOM   4537 C  CB  . GLU   B 1 264 ? -13.326 -32.255 23.044 1.00 56.98  ?  263 GLU   B CB  1 
ATOM   4538 C  CG  . GLU   B 1 264 ? -14.089 -32.614 24.347 1.00 58.59  ?  263 GLU   B CG  1 
ATOM   4539 C  CD  . GLU   B 1 264 ? -14.657 -34.027 24.362 1.00 62.50  ?  263 GLU   B CD  1 
ATOM   4540 O  OE1 . GLU   B 1 264 ? -14.147 -34.886 25.126 1.00 67.26  ?  263 GLU   B OE1 1 
ATOM   4541 O  OE2 . GLU   B 1 264 ? -15.637 -34.273 23.625 1.00 66.17  -1 263 GLU   B OE2 1 
ATOM   4542 N  N   . TYR   B 1 265 ? -11.463 -31.057 25.540 1.00 45.97  ?  264 TYR   B N   1 
ATOM   4543 C  CA  . TYR   B 1 265 ? -10.479 -31.347 26.568 1.00 47.99  ?  264 TYR   B CA  1 
ATOM   4544 C  C   . TYR   B 1 265 ? -11.178 -31.550 27.903 1.00 56.41  ?  264 TYR   B C   1 
ATOM   4545 O  O   . TYR   B 1 265 ? -11.805 -30.618 28.428 1.00 53.74  ?  264 TYR   B O   1 
ATOM   4546 C  CB  . TYR   B 1 265 ? -9.458  -30.215 26.642 1.00 49.44  ?  264 TYR   B CB  1 
ATOM   4547 C  CG  . TYR   B 1 265 ? -8.382  -30.410 27.675 1.00 51.47  ?  264 TYR   B CG  1 
ATOM   4548 C  CD1 . TYR   B 1 265 ? -7.149  -30.950 27.327 1.00 51.24  ?  264 TYR   B CD1 1 
ATOM   4549 C  CD2 . TYR   B 1 265 ? -8.591  -30.041 29.004 1.00 52.67  ?  264 TYR   B CD2 1 
ATOM   4550 C  CE1 . TYR   B 1 265 ? -6.159  -31.135 28.289 1.00 55.61  ?  264 TYR   B CE1 1 
ATOM   4551 C  CE2 . TYR   B 1 265 ? -7.608  -30.219 29.968 1.00 49.06  ?  264 TYR   B CE2 1 
ATOM   4552 C  CZ  . TYR   B 1 265 ? -6.400  -30.758 29.610 1.00 49.82  ?  264 TYR   B CZ  1 
ATOM   4553 O  OH  . TYR   B 1 265 ? -5.426  -30.924 30.565 1.00 49.74  ?  264 TYR   B OH  1 
ATOM   4554 N  N   . THR   B 1 266 ? -11.069 -32.763 28.458 1.00 53.74  ?  265 THR   B N   1 
ATOM   4555 C  CA  . THR   B 1 266 ? -11.588 -33.041 29.793 1.00 59.04  ?  265 THR   B CA  1 
ATOM   4556 C  C   . THR   B 1 266 ? -10.427 -33.410 30.717 1.00 57.01  ?  265 THR   B C   1 
ATOM   4557 O  O   . THR   B 1 266 ? -9.493  -34.120 30.315 1.00 51.66  ?  265 THR   B O   1 
ATOM   4558 C  CB  . THR   B 1 266 ? -12.672 -34.149 29.772 1.00 48.48  ?  265 THR   B CB  1 
ATOM   4559 O  OG1 . THR   B 1 266 ? -12.057 -35.440 29.833 1.00 54.31  ?  265 THR   B OG1 1 
ATOM   4560 C  CG2 . THR   B 1 266 ? -13.494 -34.071 28.470 1.00 54.74  ?  265 THR   B CG2 1 
ATOM   4561 N  N   . GLY   B 1 267 ? -10.482 -32.905 31.948 1.00 50.84  ?  266 GLY   B N   1 
ATOM   4562 C  CA  . GLY   B 1 267 ? -9.461  -33.135 32.946 1.00 52.17  ?  266 GLY   B CA  1 
ATOM   4563 C  C   . GLY   B 1 267 ? -9.018  -31.844 33.594 1.00 51.69  ?  266 GLY   B C   1 
ATOM   4564 O  O   . GLY   B 1 267 ? -9.505  -30.757 33.291 1.00 56.25  ?  266 GLY   B O   1 
ATOM   4565 N  N   . ASN   B 1 268 ? -8.080  -31.974 34.515 1.00 54.60  ?  267 ASN   B N   1 
ATOM   4566 C  CA  . ASN   B 1 268 ? -7.503  -30.764 35.075 1.00 57.52  ?  267 ASN   B CA  1 
ATOM   4567 C  C   . ASN   B 1 268 ? -6.339  -30.292 34.205 1.00 56.08  ?  267 ASN   B C   1 
ATOM   4568 O  O   . ASN   B 1 268 ? -5.853  -31.005 33.318 1.00 53.45  ?  267 ASN   B O   1 
ATOM   4569 C  CB  . ASN   B 1 268 ? -7.066  -30.988 36.526 1.00 56.24  ?  267 ASN   B CB  1 
ATOM   4570 C  CG  . ASN   B 1 268 ? -8.244  -30.912 37.515 1.00 64.62  ?  267 ASN   B CG  1 
ATOM   4571 O  OD1 . ASN   B 1 268 ? -9.283  -30.296 37.227 1.00 61.51  ?  267 ASN   B OD1 1 
ATOM   4572 N  ND2 . ASN   B 1 268 ? -8.074  -31.526 38.692 1.00 65.89  ?  267 ASN   B ND2 1 
ATOM   4573 N  N   . TYR   B 1 269 ? -5.921  -29.052 34.442 1.00 48.15  ?  268 TYR   B N   1 
ATOM   4574 C  CA  . TYR   B 1 269 ? -4.798  -28.490 33.712 1.00 41.45  ?  268 TYR   B CA  1 
ATOM   4575 C  C   . TYR   B 1 269 ? -3.617  -29.445 33.793 1.00 45.88  ?  268 TYR   B C   1 
ATOM   4576 O  O   . TYR   B 1 269 ? -3.292  -29.962 34.858 1.00 55.85  ?  268 TYR   B O   1 
ATOM   4577 C  CB  . TYR   B 1 269 ? -4.474  -27.125 34.312 1.00 44.62  ?  268 TYR   B CB  1 
ATOM   4578 C  CG  . TYR   B 1 269 ? -3.239  -26.394 33.827 1.00 51.10  ?  268 TYR   B CG  1 
ATOM   4579 C  CD1 . TYR   B 1 269 ? -3.205  -25.757 32.561 1.00 50.48  ?  268 TYR   B CD1 1 
ATOM   4580 C  CD2 . TYR   B 1 269 ? -2.118  -26.284 34.654 1.00 38.49  ?  268 TYR   B CD2 1 
ATOM   4581 C  CE1 . TYR   B 1 269 ? -2.058  -25.050 32.133 1.00 44.52  ?  268 TYR   B CE1 1 
ATOM   4582 C  CE2 . TYR   B 1 269 ? -0.983  -25.604 34.236 1.00 46.85  ?  268 TYR   B CE2 1 
ATOM   4583 C  CZ  . TYR   B 1 269 ? -0.954  -24.981 32.985 1.00 49.24  ?  268 TYR   B CZ  1 
ATOM   4584 O  OH  . TYR   B 1 269 ? 0.179   -24.300 32.609 1.00 44.92  ?  268 TYR   B OH  1 
ATOM   4585 N  N   . GLN   B 1 270 ? -3.048  -29.764 32.647 1.00 48.29  ?  269 GLN   B N   1 
ATOM   4586 C  CA  . GLN   B 1 270 ? -1.844  -30.562 32.431 1.00 47.62  ?  269 GLN   B CA  1 
ATOM   4587 C  C   . GLN   B 1 270 ? -2.018  -32.087 32.649 1.00 52.96  ?  269 GLN   B C   1 
ATOM   4588 O  O   . GLN   B 1 270 ? -1.092  -32.832 32.318 1.00 59.20  ?  269 GLN   B O   1 
ATOM   4589 C  CB  . GLN   B 1 270 ? -0.640  -30.052 33.249 1.00 42.26  ?  269 GLN   B CB  1 
ATOM   4590 C  CG  . GLN   B 1 270 ? -0.114  -28.721 32.721 1.00 44.02  ?  269 GLN   B CG  1 
ATOM   4591 C  CD  . GLN   B 1 270 ? 1.227   -28.245 33.320 1.00 51.69  ?  269 GLN   B CD  1 
ATOM   4592 O  OE1 . GLN   B 1 270 ? 1.524   -28.455 34.519 1.00 51.34  ?  269 GLN   B OE1 1 
ATOM   4593 N  NE2 . GLN   B 1 270 ? 2.055   -27.609 32.469 1.00 42.25  ?  269 GLN   B NE2 1 
ATOM   4594 N  N   . CYS   B 1 271 ? -3.165  -32.594 33.126 1.00 53.77  ?  270 CYS   B N   1 
ATOM   4595 C  CA  . CYS   B 1 271 ? -3.339  -34.049 33.216 1.00 55.48  ?  270 CYS   B CA  1 
ATOM   4596 C  C   . CYS   B 1 271 ? -4.563  -34.564 32.456 1.00 55.89  ?  270 CYS   B C   1 
ATOM   4597 O  O   . CYS   B 1 271 ? -4.946  -35.728 32.620 1.00 53.98  ?  270 CYS   B O   1 
ATOM   4598 C  CB  . CYS   B 1 271 ? -3.410  -34.514 34.671 1.00 50.40  ?  270 CYS   B CB  1 
ATOM   4599 S  SG  . CYS   B 1 271 ? -4.828  -33.893 35.578 1.00 63.61  ?  270 CYS   B SG  1 
ATOM   4600 N  N   . GLY   B 1 272 ? -5.169  -33.744 31.605 1.00 54.26  ?  271 GLY   B N   1 
ATOM   4601 C  CA  . GLY   B 1 272 ? -6.393  -34.111 30.922 1.00 56.91  ?  271 GLY   B CA  1 
ATOM   4602 C  C   . GLY   B 1 272 ? -6.187  -34.958 29.673 1.00 52.82  ?  271 GLY   B C   1 
ATOM   4603 O  O   . GLY   B 1 272 ? -5.100  -35.464 29.382 1.00 53.76  ?  271 GLY   B O   1 
ATOM   4604 N  N   . HIS   B 1 273 ? -7.298  -35.072 28.935 1.00 51.35  ?  272 HIS   B N   1 
ATOM   4605 C  CA  . HIS   B 1 273 ? -7.296  -35.834 27.665 1.00 51.80  ?  272 HIS   B CA  1 
ATOM   4606 C  C   . HIS   B 1 273 ? -7.994  -35.002 26.591 1.00 52.04  ?  272 HIS   B C   1 
ATOM   4607 O  O   . HIS   B 1 273 ? -8.970  -34.300 26.900 1.00 46.98  ?  272 HIS   B O   1 
ATOM   4608 C  CB  . HIS   B 1 273 ? -7.985  -37.188 27.848 1.00 50.61  ?  272 HIS   B CB  1 
ATOM   4609 C  CG  . HIS   B 1 273 ? -8.046  -38.051 26.634 1.00 63.76  ?  272 HIS   B CG  1 
ATOM   4610 N  ND1 . HIS   B 1 273 ? -6.970  -38.779 26.178 1.00 59.54  ?  272 HIS   B ND1 1 
ATOM   4611 C  CD2 . HIS   B 1 273 ? -9.057  -38.322 25.800 1.00 65.74  ?  272 HIS   B CD2 1 
ATOM   4612 C  CE1 . HIS   B 1 273 ? -7.330  -39.455 25.097 1.00 59.39  ?  272 HIS   B CE1 1 
ATOM   4613 N  NE2 . HIS   B 1 273 ? -8.591  -39.188 24.848 1.00 65.78  ?  272 HIS   B NE2 1 
ATOM   4614 N  N   . TYR   B 1 274 ? -7.503  -35.088 25.363 1.00 54.33  ?  273 TYR   B N   1 
ATOM   4615 C  CA  . TYR   B 1 274 ? -8.037  -34.369 24.209 1.00 50.32  ?  273 TYR   B CA  1 
ATOM   4616 C  C   . TYR   B 1 274 ? -8.891  -35.287 23.353 1.00 49.56  ?  273 TYR   B C   1 
ATOM   4617 O  O   . TYR   B 1 274 ? -8.559  -36.462 23.161 1.00 52.11  ?  273 TYR   B O   1 
ATOM   4618 C  CB  . TYR   B 1 274 ? -6.922  -33.809 23.318 1.00 45.85  ?  273 TYR   B CB  1 
ATOM   4619 C  CG  . TYR   B 1 274 ? -6.356  -32.477 23.731 1.00 47.36  ?  273 TYR   B CG  1 
ATOM   4620 C  CD1 . TYR   B 1 274 ? -6.991  -31.292 23.392 1.00 45.57  ?  273 TYR   B CD1 1 
ATOM   4621 C  CD2 . TYR   B 1 274 ? -5.168  -32.404 24.458 1.00 49.69  ?  273 TYR   B CD2 1 
ATOM   4622 C  CE1 . TYR   B 1 274 ? -6.457  -30.062 23.767 1.00 50.16  ?  273 TYR   B CE1 1 
ATOM   4623 C  CE2 . TYR   B 1 274 ? -4.637  -31.190 24.845 1.00 46.66  ?  273 TYR   B CE2 1 
ATOM   4624 C  CZ  . TYR   B 1 274 ? -5.277  -30.017 24.494 1.00 52.47  ?  273 TYR   B CZ  1 
ATOM   4625 O  OH  . TYR   B 1 274 ? -4.723  -28.798 24.866 1.00 52.37  ?  273 TYR   B OH  1 
ATOM   4626 N  N   . LYS   B 1 275 ? -9.969  -34.730 22.813 1.00 52.83  ?  274 LYS   B N   1 
ATOM   4627 C  CA  . LYS   B 1 275 ? -10.699 -35.318 21.696 1.00 57.61  ?  274 LYS   B CA  1 
ATOM   4628 C  C   . LYS   B 1 275 ? -10.855 -34.247 20.614 1.00 54.45  ?  274 LYS   B C   1 
ATOM   4629 O  O   . LYS   B 1 275 ? -10.727 -33.049 20.886 1.00 52.29  ?  274 LYS   B O   1 
ATOM   4630 C  CB  . LYS   B 1 275 ? -12.081 -35.867 22.137 1.00 55.73  ?  274 LYS   B CB  1 
ATOM   4631 C  CG  . LYS   B 1 275 ? -12.096 -37.261 22.801 1.00 50.32  ?  274 LYS   B CG  1 
ATOM   4632 C  CD  . LYS   B 1 275 ? -13.524 -37.599 23.240 1.00 57.10  ?  274 LYS   B CD  1 
ATOM   4633 C  CE  . LYS   B 1 275 ? -13.598 -38.487 24.460 1.00 56.64  ?  274 LYS   B CE  1 
ATOM   4634 N  NZ  . LYS   B 1 275 ? -14.255 -39.781 24.131 1.00 64.89  ?  274 LYS   B NZ  1 
ATOM   4635 N  N   . HIS   B 1 276 ? -11.156 -34.682 19.384 1.00 52.45  ?  275 HIS   B N   1 
ATOM   4636 C  CA  . HIS   B 1 276 ? -11.213 -33.806 18.210 1.00 55.08  ?  275 HIS   B CA  1 
ATOM   4637 C  C   . HIS   B 1 276 ? -12.622 -33.804 17.607 1.00 55.86  ?  275 HIS   B C   1 
ATOM   4638 O  O   . HIS   B 1 276 ? -13.178 -34.863 17.301 1.00 54.48  ?  275 HIS   B O   1 
ATOM   4639 C  CB  . HIS   B 1 276 ? -10.163 -34.264 17.195 1.00 52.73  ?  275 HIS   B CB  1 
ATOM   4640 C  CG  . HIS   B 1 276 ? -10.084 -33.437 15.950 1.00 58.18  ?  275 HIS   B CG  1 
ATOM   4641 N  ND1 . HIS   B 1 276 ? -9.542  -32.168 15.930 1.00 57.33  ?  275 HIS   B ND1 1 
ATOM   4642 C  CD2 . HIS   B 1 276 ? -10.397 -33.735 14.664 1.00 51.21  ?  275 HIS   B CD2 1 
ATOM   4643 C  CE1 . HIS   B 1 276 ? -9.556  -31.708 14.689 1.00 57.53  ?  275 HIS   B CE1 1 
ATOM   4644 N  NE2 . HIS   B 1 276 ? -10.069 -32.640 13.902 1.00 54.24  ?  275 HIS   B NE2 1 
ATOM   4645 N  N   . ILE   B 1 277 ? -13.206 -32.618 17.460 1.00 57.19  ?  276 ILE   B N   1 
ATOM   4646 C  CA  . ILE   B 1 277 ? -14.519 -32.432 16.847 1.00 53.83  ?  276 ILE   B CA  1 
ATOM   4647 C  C   . ILE   B 1 277 ? -14.313 -31.817 15.472 1.00 52.94  ?  276 ILE   B C   1 
ATOM   4648 O  O   . ILE   B 1 277 ? -13.712 -30.746 15.351 1.00 48.35  ?  276 ILE   B O   1 
ATOM   4649 C  CB  . ILE   B 1 277 ? -15.427 -31.514 17.686 1.00 52.53  ?  276 ILE   B CB  1 
ATOM   4650 C  CG1 . ILE   B 1 277 ? -15.241 -31.744 19.188 1.00 55.88  ?  276 ILE   B CG1 1 
ATOM   4651 C  CG2 . ILE   B 1 277 ? -16.870 -31.659 17.248 1.00 51.73  ?  276 ILE   B CG2 1 
ATOM   4652 C  CD1 . ILE   B 1 277 ? -15.803 -33.057 19.690 1.00 58.50  ?  276 ILE   B CD1 1 
ATOM   4653 N  N   . THR   B 1 278 ? -14.834 -32.464 14.444 1.00 56.51  ?  277 THR   B N   1 
ATOM   4654 C  CA  . THR   B 1 278 ? -14.809 -31.899 13.104 1.00 57.50  ?  277 THR   B CA  1 
ATOM   4655 C  C   . THR   B 1 278 ? -16.240 -31.752 12.601 1.00 56.62  ?  277 THR   B C   1 
ATOM   4656 O  O   . THR   B 1 278 ? -17.067 -32.644 12.785 1.00 60.71  ?  277 THR   B O   1 
ATOM   4657 C  CB  . THR   B 1 278 ? -13.966 -32.773 12.153 1.00 58.93  ?  277 THR   B CB  1 
ATOM   4658 O  OG1 . THR   B 1 278 ? -13.995 -32.229 10.828 1.00 50.36  ?  277 THR   B OG1 1 
ATOM   4659 C  CG2 . THR   B 1 278 ? -14.457 -34.230 12.142 1.00 56.36  ?  277 THR   B CG2 1 
ATOM   4660 N  N   . SER   B 1 279 ? -16.550 -30.614 12.005 1.00 57.87  ?  278 SER   B N   1 
ATOM   4661 C  CA  . SER   B 1 279 ? -17.837 -30.439 11.341 1.00 67.33  ?  278 SER   B CA  1 
ATOM   4662 C  C   . SER   B 1 279 ? -17.708 -30.885 9.886  1.00 65.90  ?  278 SER   B C   1 
ATOM   4663 O  O   . SER   B 1 279 ? -16.832 -30.398 9.161  1.00 60.71  ?  278 SER   B O   1 
ATOM   4664 C  CB  . SER   B 1 279 ? -18.305 -28.986 11.425 1.00 62.71  ?  278 SER   B CB  1 
ATOM   4665 O  OG  . SER   B 1 279 ? -19.307 -28.731 10.464 1.00 64.95  ?  278 SER   B OG  1 
ATOM   4666 N  N   . LYS   B 1 280 ? -18.561 -31.833 9.478  1.00 69.75  ?  279 LYS   B N   1 
ATOM   4667 C  CA  . LYS   B 1 280 ? -18.655 -32.289 8.092  1.00 75.54  ?  279 LYS   B CA  1 
ATOM   4668 C  C   . LYS   B 1 280 ? -20.111 -32.205 7.640  1.00 79.23  ?  279 LYS   B C   1 
ATOM   4669 O  O   . LYS   B 1 280 ? -20.686 -31.111 7.594  1.00 77.95  ?  279 LYS   B O   1 
ATOM   4670 C  CB  . LYS   B 1 280 ? -18.137 -33.726 7.945  1.00 68.61  ?  279 LYS   B CB  1 
ATOM   4671 C  CG  . LYS   B 1 280 ? -16.737 -33.934 8.449  1.00 59.45  ?  279 LYS   B CG  1 
ATOM   4672 C  CD  . LYS   B 1 280 ? -15.688 -33.773 7.385  1.00 49.71  ?  279 LYS   B CD  1 
ATOM   4673 C  CE  . LYS   B 1 280 ? -14.400 -34.427 7.865  1.00 57.47  ?  279 LYS   B CE  1 
ATOM   4674 N  NZ  . LYS   B 1 280 ? -13.996 -35.689 7.149  1.00 60.68  ?  279 LYS   B NZ  1 
ATOM   4675 N  N   . GLU   B 1 281 ? -20.716 -33.360 7.328  1.00 82.04  ?  280 GLU   B N   1 
ATOM   4676 C  CA  . GLU   B 1 281 ? -22.156 -33.437 7.079  1.00 81.68  ?  280 GLU   B CA  1 
ATOM   4677 C  C   . GLU   B 1 281 ? -22.950 -33.377 8.389  1.00 82.08  ?  280 GLU   B C   1 
ATOM   4678 O  O   . GLU   B 1 281 ? -24.022 -32.761 8.448  1.00 83.37  ?  280 GLU   B O   1 
ATOM   4679 C  CB  . GLU   B 1 281 ? -22.481 -34.714 6.285  1.00 78.89  ?  280 GLU   B CB  1 
ATOM   4680 C  CG  . GLU   B 1 281 ? -22.985 -35.907 7.110  1.00 81.38  ?  280 GLU   B CG  1 
ATOM   4681 C  CD  . GLU   B 1 281 ? -21.878 -36.850 7.582  1.00 84.01  ?  280 GLU   B CD  1 
ATOM   4682 O  OE1 . GLU   B 1 281 ? -22.219 -37.867 8.241  1.00 81.75  ?  280 GLU   B OE1 1 
ATOM   4683 O  OE2 . GLU   B 1 281 ? -20.682 -36.593 7.285  1.00 78.41  -1 280 GLU   B OE2 1 
ATOM   4684 N  N   . THR   B 1 282 ? -22.438 -34.017 9.439  1.00 81.07  ?  281 THR   B N   1 
ATOM   4685 C  CA  . THR   B 1 282 ? -22.830 -33.815 10.830 1.00 81.19  ?  281 THR   B CA  1 
ATOM   4686 C  C   . THR   B 1 282 ? -21.544 -33.550 11.616 1.00 75.80  ?  281 THR   B C   1 
ATOM   4687 O  O   . THR   B 1 282 ? -20.437 -33.603 11.063 1.00 73.33  ?  281 THR   B O   1 
ATOM   4688 C  CB  . THR   B 1 282 ? -23.614 -35.032 11.366 1.00 76.87  ?  281 THR   B CB  1 
ATOM   4689 O  OG1 . THR   B 1 282 ? -23.981 -34.842 12.741 1.00 74.27  ?  281 THR   B OG1 1 
ATOM   4690 C  CG2 . THR   B 1 282 ? -22.802 -36.313 11.229 1.00 69.82  ?  281 THR   B CG2 1 
ATOM   4691 N  N   . LEU   B 1 283 ? -21.672 -33.236 12.900 1.00 71.07  ?  282 LEU   B N   1 
ATOM   4692 C  CA  . LEU   B 1 283 ? -20.480 -33.187 13.730 1.00 68.56  ?  282 LEU   B CA  1 
ATOM   4693 C  C   . LEU   B 1 283 ? -19.901 -34.594 13.890 1.00 65.20  ?  282 LEU   B C   1 
ATOM   4694 O  O   . LEU   B 1 283 ? -20.585 -35.602 13.713 1.00 69.55  ?  282 LEU   B O   1 
ATOM   4695 C  CB  . LEU   B 1 283 ? -20.798 -32.570 15.095 1.00 70.10  ?  282 LEU   B CB  1 
ATOM   4696 C  CG  . LEU   B 1 283 ? -21.501 -31.214 15.053 1.00 65.65  ?  282 LEU   B CG  1 
ATOM   4697 C  CD1 . LEU   B 1 283 ? -21.757 -30.693 16.435 1.00 69.66  ?  282 LEU   B CD1 1 
ATOM   4698 C  CD2 . LEU   B 1 283 ? -20.665 -30.237 14.270 1.00 66.96  ?  282 LEU   B CD2 1 
ATOM   4699 N  N   . TYR   B 1 284 ? -18.612 -34.655 14.202 1.00 60.99  ?  283 TYR   B N   1 
ATOM   4700 C  CA  . TYR   B 1 284 ? -17.939 -35.921 14.453 1.00 61.41  ?  283 TYR   B CA  1 
ATOM   4701 C  C   . TYR   B 1 284 ? -16.923 -35.720 15.564 1.00 65.05  ?  283 TYR   B C   1 
ATOM   4702 O  O   . TYR   B 1 284 ? -16.289 -34.663 15.656 1.00 62.39  ?  283 TYR   B O   1 
ATOM   4703 C  CB  . TYR   B 1 284 ? -17.234 -36.461 13.210 1.00 68.55  ?  283 TYR   B CB  1 
ATOM   4704 C  CG  . TYR   B 1 284 ? -18.120 -37.246 12.257 1.00 79.29  ?  283 TYR   B CG  1 
ATOM   4705 C  CD1 . TYR   B 1 284 ? -18.275 -38.624 12.398 1.00 79.10  ?  283 TYR   B CD1 1 
ATOM   4706 C  CD2 . TYR   B 1 284 ? -18.750 -36.623 11.179 1.00 71.95  ?  283 TYR   B CD2 1 
ATOM   4707 C  CE1 . TYR   B 1 284 ? -19.062 -39.351 11.524 1.00 76.05  ?  283 TYR   B CE1 1 
ATOM   4708 C  CE2 . TYR   B 1 284 ? -19.531 -37.344 10.301 1.00 74.41  ?  283 TYR   B CE2 1 
ATOM   4709 C  CZ  . TYR   B 1 284 ? -19.687 -38.707 10.476 1.00 81.19  ?  283 TYR   B CZ  1 
ATOM   4710 O  OH  . TYR   B 1 284 ? -20.474 -39.429 9.595  1.00 87.82  ?  283 TYR   B OH  1 
ATOM   4711 N  N   . CYS   B 1 285 ? -16.792 -36.732 16.417 1.00 66.90  ?  284 CYS   B N   1 
ATOM   4712 C  CA  . CYS   B 1 285 ? -15.888 -36.718 17.561 1.00 61.97  ?  284 CYS   B CA  1 
ATOM   4713 C  C   . CYS   B 1 285 ? -14.902 -37.854 17.318 1.00 63.21  ?  284 CYS   B C   1 
ATOM   4714 O  O   . CYS   B 1 285 ? -15.234 -39.023 17.540 1.00 68.14  ?  284 CYS   B O   1 
ATOM   4715 C  CB  . CYS   B 1 285 ? -16.663 -36.877 18.870 1.00 63.23  ?  284 CYS   B CB  1 
ATOM   4716 S  SG  . CYS   B 1 285 ? -15.682 -37.193 20.381 1.00 74.52  ?  284 CYS   B SG  1 
ATOM   4717 N  N   . ILE   B 1 286 ? -13.710 -37.516 16.826 1.00 56.84  ?  285 ILE   B N   1 
ATOM   4718 C  CA  . ILE   B 1 286 ? -12.648 -38.492 16.597 1.00 56.99  ?  285 ILE   B CA  1 
ATOM   4719 C  C   . ILE   B 1 286 ? -11.807 -38.605 17.867 1.00 58.54  ?  285 ILE   B C   1 
ATOM   4720 O  O   . ILE   B 1 286 ? -11.255 -37.606 18.337 1.00 57.92  ?  285 ILE   B O   1 
ATOM   4721 C  CB  . ILE   B 1 286 ? -11.786 -38.085 15.397 1.00 53.32  ?  285 ILE   B CB  1 
ATOM   4722 C  CG1 . ILE   B 1 286 ? -12.670 -38.017 14.150 1.00 60.95  ?  285 ILE   B CG1 1 
ATOM   4723 C  CG2 . ILE   B 1 286 ? -10.646 -39.075 15.203 1.00 45.14  ?  285 ILE   B CG2 1 
ATOM   4724 C  CD1 . ILE   B 1 286 ? -11.989 -37.469 12.909 1.00 60.90  ?  285 ILE   B CD1 1 
ATOM   4725 N  N   . ASP   B 1 287 ? -11.712 -39.816 18.433 1.00 57.02  ?  286 ASP   B N   1 
ATOM   4726 C  CA  . ASP   B 1 287 ? -11.059 -40.042 19.729 1.00 52.06  ?  286 ASP   B CA  1 
ATOM   4727 C  C   . ASP   B 1 287 ? -9.996  -41.132 19.586 1.00 59.25  ?  286 ASP   B C   1 
ATOM   4728 O  O   . ASP   B 1 287 ? -10.037 -42.167 20.247 1.00 57.06  ?  286 ASP   B O   1 
ATOM   4729 C  CB  . ASP   B 1 287 ? -12.055 -40.428 20.820 1.00 54.83  ?  286 ASP   B CB  1 
ATOM   4730 C  CG  . ASP   B 1 287 ? -11.384 -40.646 22.194 1.00 71.24  ?  286 ASP   B CG  1 
ATOM   4731 O  OD1 . ASP   B 1 287 ? -11.864 -41.495 22.988 1.00 74.35  ?  286 ASP   B OD1 1 
ATOM   4732 O  OD2 . ASP   B 1 287 ? -10.371 -39.965 22.486 1.00 72.69  -1 286 ASP   B OD2 1 
ATOM   4733 N  N   . GLY   B 1 288 ? -9.014  -40.881 18.723 1.00 58.22  ?  287 GLY   B N   1 
ATOM   4734 C  CA  . GLY   B 1 288 ? -7.980  -41.866 18.408 1.00 45.15  ?  287 GLY   B CA  1 
ATOM   4735 C  C   . GLY   B 1 288 ? -8.367  -42.691 17.183 1.00 58.11  ?  287 GLY   B C   1 
ATOM   4736 O  O   . GLY   B 1 288 ? -8.412  -42.160 16.079 1.00 67.47  ?  287 GLY   B O   1 
ATOM   4737 N  N   . ALA   B 1 289 ? -8.653  -43.972 17.395 1.00 60.36  ?  288 ALA   B N   1 
ATOM   4738 C  CA  . ALA   B 1 289 ? -9.280  -44.764 16.353 1.00 53.79  ?  288 ALA   B CA  1 
ATOM   4739 C  C   . ALA   B 1 289 ? -10.796 -44.792 16.483 1.00 61.59  ?  288 ALA   B C   1 
ATOM   4740 O  O   . ALA   B 1 289 ? -11.473 -45.285 15.572 1.00 65.63  ?  288 ALA   B O   1 
ATOM   4741 C  CB  . ALA   B 1 289 ? -8.730  -46.190 16.352 1.00 51.41  ?  288 ALA   B CB  1 
ATOM   4742 N  N   . LEU   B 1 290 ? -11.339 -44.232 17.561 1.00 58.83  ?  289 LEU   B N   1 
ATOM   4743 C  CA  . LEU   B 1 290 ? -12.774 -44.236 17.803 1.00 60.78  ?  289 LEU   B CA  1 
ATOM   4744 C  C   . LEU   B 1 290 ? -13.448 -43.031 17.154 1.00 66.86  ?  289 LEU   B C   1 
ATOM   4745 O  O   . LEU   B 1 290 ? -12.837 -41.972 16.973 1.00 65.12  ?  289 LEU   B O   1 
ATOM   4746 C  CB  . LEU   B 1 290 ? -13.085 -44.252 19.304 1.00 67.38  ?  289 LEU   B CB  1 
ATOM   4747 C  CG  . LEU   B 1 290 ? -12.743 -45.481 20.172 1.00 66.50  ?  289 LEU   B CG  1 
ATOM   4748 C  CD1 . LEU   B 1 290 ? -13.558 -46.685 19.708 1.00 69.80  ?  289 LEU   B CD1 1 
ATOM   4749 C  CD2 . LEU   B 1 290 ? -11.266 -45.819 20.235 1.00 62.89  ?  289 LEU   B CD2 1 
ATOM   4750 N  N   . LEU   B 1 291 ? -14.737 -43.203 16.831 1.00 70.78  ?  290 LEU   B N   1 
ATOM   4751 C  CA  . LEU   B 1 291 ? -15.506 -42.252 16.037 1.00 61.60  ?  290 LEU   B CA  1 
ATOM   4752 C  C   . LEU   B 1 291 ? -16.972 -42.295 16.453 1.00 65.50  ?  290 LEU   B C   1 
ATOM   4753 O  O   . LEU   B 1 291 ? -17.562 -43.377 16.512 1.00 70.72  ?  290 LEU   B O   1 
ATOM   4754 C  CB  . LEU   B 1 291 ? -15.369 -42.582 14.550 1.00 58.89  ?  290 LEU   B CB  1 
ATOM   4755 C  CG  . LEU   B 1 291 ? -16.062 -41.606 13.615 1.00 64.19  ?  290 LEU   B CG  1 
ATOM   4756 C  CD1 . LEU   B 1 291 ? -15.755 -40.196 14.089 1.00 69.86  ?  290 LEU   B CD1 1 
ATOM   4757 C  CD2 . LEU   B 1 291 ? -15.587 -41.808 12.190 1.00 66.31  ?  290 LEU   B CD2 1 
ATOM   4758 N  N   . THR   B 1 292 ? -17.567 -41.132 16.734 1.00 63.14  ?  291 THR   B N   1 
ATOM   4759 C  CA  . THR   B 1 292 ? -18.976 -41.065 17.117 1.00 61.78  ?  291 THR   B CA  1 
ATOM   4760 C  C   . THR   B 1 292 ? -19.581 -39.802 16.525 1.00 63.33  ?  291 THR   B C   1 
ATOM   4761 O  O   . THR   B 1 292 ? -19.086 -38.702 16.785 1.00 60.61  ?  291 THR   B O   1 
ATOM   4762 C  CB  . THR   B 1 292 ? -19.175 -41.079 18.648 1.00 64.44  ?  291 THR   B CB  1 
ATOM   4763 O  OG1 . THR   B 1 292 ? -18.335 -40.106 19.283 1.00 66.49  ?  291 THR   B OG1 1 
ATOM   4764 C  CG2 . THR   B 1 292 ? -18.860 -42.447 19.223 1.00 60.74  ?  291 THR   B CG2 1 
ATOM   4765 N  N   . LYS   B 1 293 ? -20.654 -39.960 15.744 1.00 69.11  ?  292 LYS   B N   1 
ATOM   4766 C  CA  . LYS   B 1 293 ? -21.364 -38.836 15.151 1.00 67.60  ?  292 LYS   B CA  1 
ATOM   4767 C  C   . LYS   B 1 293 ? -22.411 -38.306 16.125 1.00 67.97  ?  292 LYS   B C   1 
ATOM   4768 O  O   . LYS   B 1 293 ? -22.730 -38.925 17.142 1.00 73.53  ?  292 LYS   B O   1 
ATOM   4769 C  CB  . LYS   B 1 293 ? -22.017 -39.226 13.817 1.00 73.89  ?  292 LYS   B CB  1 
ATOM   4770 C  CG  . LYS   B 1 293 ? -22.710 -40.600 13.786 1.00 77.29  ?  292 LYS   B CG  1 
ATOM   4771 C  CD  . LYS   B 1 293 ? -22.890 -41.137 12.350 1.00 76.49  ?  292 LYS   B CD  1 
ATOM   4772 C  CE  . LYS   B 1 293 ? -23.185 -40.040 11.319 1.00 74.78  ?  292 LYS   B CE  1 
ATOM   4773 N  NZ  . LYS   B 1 293 ? -23.827 -40.557 10.054 1.00 75.13  ?  292 LYS   B NZ  1 
ATOM   4774 N  N   . SER   B 1 294 ? -22.943 -37.133 15.802 1.00 71.05  ?  293 SER   B N   1 
ATOM   4775 C  CA  . SER   B 1 294 ? -23.891 -36.450 16.674 1.00 76.50  ?  293 SER   B CA  1 
ATOM   4776 C  C   . SER   B 1 294 ? -24.387 -35.190 15.981 1.00 84.39  ?  293 SER   B C   1 
ATOM   4777 O  O   . SER   B 1 294 ? -23.582 -34.427 15.438 1.00 87.50  ?  293 SER   B O   1 
ATOM   4778 C  CB  . SER   B 1 294 ? -23.243 -36.107 18.017 1.00 75.38  ?  293 SER   B CB  1 
ATOM   4779 O  OG  . SER   B 1 294 ? -22.628 -34.835 17.976 1.00 76.87  ?  293 SER   B OG  1 
ATOM   4780 N  N   . SER   B 1 295 ? -25.699 -34.960 15.966 1.00 86.02  ?  294 SER   B N   1 
ATOM   4781 C  CA  . SER   B 1 295 ? -26.188 -33.741 15.331 1.00 85.26  ?  294 SER   B CA  1 
ATOM   4782 C  C   . SER   B 1 295 ? -25.649 -32.510 16.047 1.00 91.87  ?  294 SER   B C   1 
ATOM   4783 O  O   . SER   B 1 295 ? -25.176 -31.565 15.400 1.00 93.78  ?  294 SER   B O   1 
ATOM   4784 C  CB  . SER   B 1 295 ? -27.714 -33.719 15.305 1.00 86.78  ?  294 SER   B CB  1 
ATOM   4785 O  OG  . SER   B 1 295 ? -28.230 -33.267 16.547 1.00 95.37  ?  294 SER   B OG  1 
ATOM   4786 N  N   . GLU   B 1 296 ? -25.675 -32.518 17.386 1.00 94.46  ?  295 GLU   B N   1 
ATOM   4787 C  CA  . GLU   B 1 296 ? -25.316 -31.353 18.185 1.00 95.60  ?  295 GLU   B CA  1 
ATOM   4788 C  C   . GLU   B 1 296 ? -24.327 -31.720 19.290 1.00 90.66  ?  295 GLU   B C   1 
ATOM   4789 O  O   . GLU   B 1 296 ? -24.286 -32.867 19.755 1.00 87.67  ?  295 GLU   B O   1 
ATOM   4790 C  CB  . GLU   B 1 296 ? -26.569 -30.695 18.772 1.00 94.18  ?  295 GLU   B CB  1 
ATOM   4791 C  CG  . GLU   B 1 296 ? -27.121 -29.610 17.856 1.00 98.30  ?  295 GLU   B CG  1 
ATOM   4792 C  CD  . GLU   B 1 296 ? -26.017 -28.647 17.399 1.00 109.28 ?  295 GLU   B CD  1 
ATOM   4793 O  OE1 . GLU   B 1 296 ? -25.438 -27.945 18.278 1.00 103.32 ?  295 GLU   B OE1 1 
ATOM   4794 O  OE2 . GLU   B 1 296 ? -25.728 -28.599 16.169 1.00 111.51 -1 295 GLU   B OE2 1 
ATOM   4795 N  N   . TYR   B 1 297 ? -23.519 -30.731 19.700 1.00 82.67  ?  296 TYR   B N   1 
ATOM   4796 C  CA  . TYR   B 1 297 ? -22.409 -30.982 20.616 1.00 73.62  ?  296 TYR   B CA  1 
ATOM   4797 C  C   . TYR   B 1 297 ? -22.299 -29.896 21.677 1.00 68.56  ?  296 TYR   B C   1 
ATOM   4798 O  O   . TYR   B 1 297 ? -22.176 -28.710 21.364 1.00 70.07  ?  296 TYR   B O   1 
ATOM   4799 C  CB  . TYR   B 1 297 ? -21.071 -31.096 19.866 1.00 75.29  ?  296 TYR   B CB  1 
ATOM   4800 C  CG  . TYR   B 1 297 ? -19.914 -31.435 20.780 1.00 69.64  ?  296 TYR   B CG  1 
ATOM   4801 C  CD1 . TYR   B 1 297 ? -19.318 -30.456 21.575 1.00 64.59  ?  296 TYR   B CD1 1 
ATOM   4802 C  CD2 . TYR   B 1 297 ? -19.446 -32.742 20.876 1.00 64.96  ?  296 TYR   B CD2 1 
ATOM   4803 C  CE1 . TYR   B 1 297 ? -18.294 -30.763 22.424 1.00 68.82  ?  296 TYR   B CE1 1 
ATOM   4804 C  CE2 . TYR   B 1 297 ? -18.423 -33.065 21.728 1.00 66.34  ?  296 TYR   B CE2 1 
ATOM   4805 C  CZ  . TYR   B 1 297 ? -17.842 -32.065 22.500 1.00 73.67  ?  296 TYR   B CZ  1 
ATOM   4806 O  OH  . TYR   B 1 297 ? -16.809 -32.353 23.370 1.00 69.67  ?  296 TYR   B OH  1 
ATOM   4807 N  N   . LYS   B 1 298 ? -22.292 -30.319 22.932 1.00 68.16  ?  297 LYS   B N   1 
ATOM   4808 C  CA  . LYS   B 1 298 ? -21.976 -29.445 24.050 1.00 68.53  ?  297 LYS   B CA  1 
ATOM   4809 C  C   . LYS   B 1 298 ? -20.909 -30.151 24.879 1.00 60.52  ?  297 LYS   B C   1 
ATOM   4810 O  O   . LYS   B 1 298 ? -21.003 -31.358 25.110 1.00 64.17  ?  297 LYS   B O   1 
ATOM   4811 C  CB  . LYS   B 1 298 ? -23.239 -29.122 24.862 1.00 59.44  ?  297 LYS   B CB  1 
ATOM   4812 C  CG  . LYS   B 1 298 ? -22.991 -28.432 26.172 1.00 67.25  ?  297 LYS   B CG  1 
ATOM   4813 C  CD  . LYS   B 1 298 ? -23.347 -26.951 26.134 1.00 69.42  ?  297 LYS   B CD  1 
ATOM   4814 C  CE  . LYS   B 1 298 ? -23.207 -26.341 27.550 1.00 74.11  ?  297 LYS   B CE  1 
ATOM   4815 N  NZ  . LYS   B 1 298 ? -23.617 -24.900 27.636 1.00 78.03  ?  297 LYS   B NZ  1 
ATOM   4816 N  N   . GLY   B 1 299 ? -19.865 -29.428 25.262 1.00 58.29  ?  298 GLY   B N   1 
ATOM   4817 C  CA  . GLY   B 1 299 ? -18.732 -30.051 25.901 1.00 64.24  ?  298 GLY   B CA  1 
ATOM   4818 C  C   . GLY   B 1 299 ? -17.629 -29.066 26.229 1.00 70.05  ?  298 GLY   B C   1 
ATOM   4819 O  O   . GLY   B 1 299 ? -17.749 -27.858 25.976 1.00 69.66  ?  298 GLY   B O   1 
ATOM   4820 N  N   . PRO   B 1 300 ? -16.523 -29.565 26.823 1.00 64.15  ?  299 PRO   B N   1 
ATOM   4821 C  CA  . PRO   B 1 300 ? -15.409 -28.670 27.165 1.00 55.54  ?  299 PRO   B CA  1 
ATOM   4822 C  C   . PRO   B 1 300 ? -14.476 -28.447 25.985 1.00 57.23  ?  299 PRO   B C   1 
ATOM   4823 O  O   . PRO   B 1 300 ? -13.762 -29.363 25.537 1.00 51.92  ?  299 PRO   B O   1 
ATOM   4824 C  CB  . PRO   B 1 300 ? -14.716 -29.401 28.323 1.00 58.66  ?  299 PRO   B CB  1 
ATOM   4825 C  CG  . PRO   B 1 300 ? -15.035 -30.842 28.127 1.00 55.43  ?  299 PRO   B CG  1 
ATOM   4826 C  CD  . PRO   B 1 300 ? -16.280 -30.952 27.259 1.00 59.17  ?  299 PRO   B CD  1 
ATOM   4827 N  N   . ILE   B 1 301 ? -14.476 -27.216 25.477 1.00 55.84  ?  300 ILE   B N   1 
ATOM   4828 C  CA  . ILE   B 1 301 ? -13.747 -26.868 24.266 1.00 52.27  ?  300 ILE   B CA  1 
ATOM   4829 C  C   . ILE   B 1 301 ? -12.675 -25.851 24.628 1.00 51.53  ?  300 ILE   B C   1 
ATOM   4830 O  O   . ILE   B 1 301 ? -12.915 -24.954 25.445 1.00 57.59  ?  300 ILE   B O   1 
ATOM   4831 C  CB  . ILE   B 1 301 ? -14.701 -26.333 23.177 1.00 51.24  ?  300 ILE   B CB  1 
ATOM   4832 C  CG1 . ILE   B 1 301 ? -15.615 -27.471 22.746 1.00 53.20  ?  300 ILE   B CG1 1 
ATOM   4833 C  CG2 . ILE   B 1 301 ? -13.927 -25.857 21.963 1.00 56.02  ?  300 ILE   B CG2 1 
ATOM   4834 C  CD1 . ILE   B 1 301 ? -14.889 -28.577 22.006 1.00 52.62  ?  300 ILE   B CD1 1 
ATOM   4835 N  N   . THR   B 1 302 ? -11.483 -26.014 24.046 1.00 47.55  ?  301 THR   B N   1 
ATOM   4836 C  CA  . THR   B 1 302 ? -10.344 -25.137 24.299 1.00 52.81  ?  301 THR   B CA  1 
ATOM   4837 C  C   . THR   B 1 302 ? -9.733  -24.501 23.041 1.00 54.88  ?  301 THR   B C   1 
ATOM   4838 O  O   . THR   B 1 302 ? -9.165  -23.407 23.146 1.00 55.24  ?  301 THR   B O   1 
ATOM   4839 C  CB  . THR   B 1 302 ? -9.251  -25.891 25.122 1.00 48.48  ?  301 THR   B CB  1 
ATOM   4840 O  OG1 . THR   B 1 302 ? -8.249  -24.975 25.577 1.00 48.37  ?  301 THR   B OG1 1 
ATOM   4841 C  CG2 . THR   B 1 302 ? -8.576  -27.031 24.360 1.00 49.03  ?  301 THR   B CG2 1 
ATOM   4842 N  N   . ASP   B 1 303 ? -9.820  -25.135 21.865 1.00 48.96  ?  302 ASP   B N   1 
ATOM   4843 C  CA  . ASP   B 1 303 ? -9.513  -24.458 20.606 1.00 55.84  ?  302 ASP   B CA  1 
ATOM   4844 C  C   . ASP   B 1 303 ? -10.618 -24.692 19.579 1.00 55.61  ?  302 ASP   B C   1 
ATOM   4845 O  O   . ASP   B 1 303 ? -11.163 -25.798 19.471 1.00 53.13  ?  302 ASP   B O   1 
ATOM   4846 C  CB  . ASP   B 1 303 ? -8.197  -24.919 19.942 1.00 59.05  ?  302 ASP   B CB  1 
ATOM   4847 C  CG  . ASP   B 1 303 ? -7.098  -25.244 20.922 1.00 60.99  ?  302 ASP   B CG  1 
ATOM   4848 O  OD1 . ASP   B 1 303 ? -6.477  -24.295 21.482 1.00 65.37  -1 302 ASP   B OD1 1 
ATOM   4849 O  OD2 . ASP   B 1 303 ? -6.784  -26.457 21.038 1.00 57.53  ?  302 ASP   B OD2 1 
ATOM   4850 N  N   . VAL   B 1 304 ? -10.907 -23.655 18.798 1.00 52.82  ?  303 VAL   B N   1 
ATOM   4851 C  CA  . VAL   B 1 304 ? -11.768 -23.756 17.627 1.00 55.49  ?  303 VAL   B CA  1 
ATOM   4852 C  C   . VAL   B 1 304 ? -11.045 -23.162 16.423 1.00 49.28  ?  303 VAL   B C   1 
ATOM   4853 O  O   . VAL   B 1 304 ? -10.390 -22.117 16.528 1.00 47.02  ?  303 VAL   B O   1 
ATOM   4854 C  CB  . VAL   B 1 304 ? -13.124 -23.058 17.846 1.00 54.87  ?  303 VAL   B CB  1 
ATOM   4855 C  CG1 . VAL   B 1 304 ? -13.969 -23.195 16.587 1.00 47.72  ?  303 VAL   B CG1 1 
ATOM   4856 C  CG2 . VAL   B 1 304 ? -13.842 -23.639 19.091 1.00 46.34  ?  303 VAL   B CG2 1 
ATOM   4857 N  N   . PHE   B 1 305 ? -11.152 -23.839 15.286 1.00 46.14  ?  304 PHE   B N   1 
ATOM   4858 C  CA  . PHE   B 1 305 ? -10.579 -23.382 14.032 1.00 49.25  ?  304 PHE   B CA  1 
ATOM   4859 C  C   . PHE   B 1 305 ? -11.685 -23.010 13.057 1.00 50.98  ?  304 PHE   B C   1 
ATOM   4860 O  O   . PHE   B 1 305 ? -12.741 -23.645 13.014 1.00 53.65  ?  304 PHE   B O   1 
ATOM   4861 C  CB  . PHE   B 1 305 ? -9.702  -24.457 13.411 1.00 49.30  ?  304 PHE   B CB  1 
ATOM   4862 C  CG  . PHE   B 1 305 ? -8.511  -24.807 14.238 1.00 50.07  ?  304 PHE   B CG  1 
ATOM   4863 C  CD1 . PHE   B 1 305 ? -8.633  -25.656 15.327 1.00 50.60  ?  304 PHE   B CD1 1 
ATOM   4864 C  CD2 . PHE   B 1 305 ? -7.258  -24.318 13.912 1.00 49.51  ?  304 PHE   B CD2 1 
ATOM   4865 C  CE1 . PHE   B 1 305 ? -7.525  -25.996 16.084 1.00 51.24  ?  304 PHE   B CE1 1 
ATOM   4866 C  CE2 . PHE   B 1 305 ? -6.142  -24.672 14.662 1.00 51.24  ?  304 PHE   B CE2 1 
ATOM   4867 C  CZ  . PHE   B 1 305 ? -6.280  -25.495 15.754 1.00 48.70  ?  304 PHE   B CZ  1 
ATOM   4868 N  N   . TYR   B 1 306 ? -11.426 -21.974 12.269 1.00 51.73  ?  305 TYR   B N   1 
ATOM   4869 C  CA  . TYR   B 1 306 ? -12.405 -21.382 11.368 1.00 48.45  ?  305 TYR   B CA  1 
ATOM   4870 C  C   . TYR   B 1 306 ? -11.745 -21.122 10.022 1.00 53.78  ?  305 TYR   B C   1 
ATOM   4871 O  O   . TYR   B 1 306 ? -10.640 -20.570 9.974  1.00 54.38  ?  305 TYR   B O   1 
ATOM   4872 C  CB  . TYR   B 1 306 ? -12.911 -20.064 11.930 1.00 43.63  ?  305 TYR   B CB  1 
ATOM   4873 C  CG  . TYR   B 1 306 ? -13.664 -20.143 13.222 1.00 49.14  ?  305 TYR   B CG  1 
ATOM   4874 C  CD1 . TYR   B 1 306 ? -14.997 -20.527 13.246 1.00 45.63  ?  305 TYR   B CD1 1 
ATOM   4875 C  CD2 . TYR   B 1 306 ? -13.050 -19.795 14.428 1.00 50.08  ?  305 TYR   B CD2 1 
ATOM   4876 C  CE1 . TYR   B 1 306 ? -15.710 -20.559 14.426 1.00 48.61  ?  305 TYR   B CE1 1 
ATOM   4877 C  CE2 . TYR   B 1 306 ? -13.751 -19.834 15.629 1.00 46.96  ?  305 TYR   B CE2 1 
ATOM   4878 C  CZ  . TYR   B 1 306 ? -15.081 -20.214 15.623 1.00 52.67  ?  305 TYR   B CZ  1 
ATOM   4879 O  OH  . TYR   B 1 306 ? -15.779 -20.269 16.816 1.00 51.13  ?  305 TYR   B OH  1 
ATOM   4880 N  N   . LYS   B 1 307 ? -12.408 -21.502 8.934  1.00 53.58  ?  306 LYS   B N   1 
ATOM   4881 C  CA  . LYS   B 1 307 ? -11.863 -21.177 7.623  1.00 60.30  ?  306 LYS   B CA  1 
ATOM   4882 C  C   . LYS   B 1 307 ? -12.010 -19.679 7.363  1.00 57.13  ?  306 LYS   B C   1 
ATOM   4883 O  O   . LYS   B 1 307 ? -12.972 -19.043 7.815  1.00 54.33  ?  306 LYS   B O   1 
ATOM   4884 C  CB  . LYS   B 1 307 ? -12.548 -21.997 6.529  1.00 62.82  ?  306 LYS   B CB  1 
ATOM   4885 C  CG  . LYS   B 1 307 ? -12.652 -21.305 5.178  1.00 61.71  ?  306 LYS   B CG  1 
ATOM   4886 C  CD  . LYS   B 1 307 ? -13.169 -22.270 4.115  1.00 73.52  ?  306 LYS   B CD  1 
ATOM   4887 C  CE  . LYS   B 1 307 ? -14.686 -22.431 4.185  1.00 72.56  ?  306 LYS   B CE  1 
ATOM   4888 N  NZ  . LYS   B 1 307 ? -15.287 -22.510 2.816  1.00 81.78  ?  306 LYS   B NZ  1 
ATOM   4889 N  N   . GLU   B 1 308 ? -11.023 -19.109 6.673  1.00 51.12  ?  307 GLU   B N   1 
ATOM   4890 C  CA  . GLU   B 1 308 ? -10.952 -17.667 6.482  1.00 55.32  ?  307 GLU   B CA  1 
ATOM   4891 C  C   . GLU   B 1 308 ? -10.362 -17.365 5.114  1.00 57.46  ?  307 GLU   B C   1 
ATOM   4892 O  O   . GLU   B 1 308 ? -9.654  -18.180 4.516  1.00 58.03  ?  307 GLU   B O   1 
ATOM   4893 C  CB  . GLU   B 1 308 ? -10.117 -16.975 7.578  1.00 50.80  ?  307 GLU   B CB  1 
ATOM   4894 C  CG  . GLU   B 1 308 ? -10.071 -15.406 7.537  1.00 56.59  ?  307 GLU   B CG  1 
ATOM   4895 C  CD  . GLU   B 1 308 ? -11.450 -14.697 7.330  1.00 60.69  ?  307 GLU   B CD  1 
ATOM   4896 O  OE1 . GLU   B 1 308 ? -11.992 -14.707 6.192  1.00 61.71  ?  307 GLU   B OE1 1 
ATOM   4897 O  OE2 . GLU   B 1 308 ? -11.986 -14.120 8.307  1.00 53.90  -1 307 GLU   B OE2 1 
ATOM   4898 N  N   . ASN   B 1 309 ? -10.666 -16.166 4.635  1.00 56.51  ?  308 ASN   B N   1 
ATOM   4899 C  CA  . ASN   B 1 309 ? -10.168 -15.649 3.374  1.00 54.49  ?  308 ASN   B CA  1 
ATOM   4900 C  C   . ASN   B 1 309 ? -9.628  -14.255 3.619  1.00 53.86  ?  308 ASN   B C   1 
ATOM   4901 O  O   . ASN   B 1 309 ? -8.423  -14.000 3.540  1.00 53.35  ?  308 ASN   B O   1 
ATOM   4902 C  CB  . ASN   B 1 309 ? -11.306 -15.596 2.364  1.00 60.02  ?  308 ASN   B CB  1 
ATOM   4903 C  CG  . ASN   B 1 309 ? -10.872 -15.971 1.002  1.00 73.98  ?  308 ASN   B CG  1 
ATOM   4904 O  OD1 . ASN   B 1 309 ? -9.679  -15.922 0.682  1.00 72.36  ?  308 ASN   B OD1 1 
ATOM   4905 N  ND2 . ASN   B 1 309 ? -11.828 -16.394 0.180  1.00 81.05  ?  308 ASN   B ND2 1 
ATOM   4906 N  N   . SER   B 1 310 ? -10.550 -13.390 4.019  1.00 51.01  ?  309 SER   B N   1 
ATOM   4907 C  CA  . SER   B 1 310 ? -10.443 -11.947 3.971  1.00 53.07  ?  309 SER   B CA  1 
ATOM   4908 C  C   . SER   B 1 310 ? -11.708 -11.384 4.618  1.00 55.29  ?  309 SER   B C   1 
ATOM   4909 O  O   . SER   B 1 310 ? -12.823 -11.815 4.299  1.00 58.72  ?  309 SER   B O   1 
ATOM   4910 C  CB  . SER   B 1 310 ? -10.268 -11.488 2.521  1.00 56.78  ?  309 SER   B CB  1 
ATOM   4911 O  OG  . SER   B 1 310 ? -10.536 -10.113 2.386  1.00 64.21  ?  309 SER   B OG  1 
ATOM   4912 N  N   . TYR   B 1 311 ? -11.552 -10.465 5.564  1.00 51.52  ?  310 TYR   B N   1 
ATOM   4913 C  CA  . TYR   B 1 311 ? -12.679 -9.953  6.319  1.00 53.43  ?  310 TYR   B CA  1 
ATOM   4914 C  C   . TYR   B 1 311 ? -12.456 -8.478  6.603  1.00 60.27  ?  310 TYR   B C   1 
ATOM   4915 O  O   . TYR   B 1 311 ? -11.321 -8.052  6.840  1.00 61.39  ?  310 TYR   B O   1 
ATOM   4916 C  CB  . TYR   B 1 311 ? -12.856 -10.719 7.637  1.00 56.77  ?  310 TYR   B CB  1 
ATOM   4917 C  CG  . TYR   B 1 311 ? -13.822 -10.057 8.610  1.00 58.20  ?  310 TYR   B CG  1 
ATOM   4918 C  CD1 . TYR   B 1 311 ? -13.375 -9.131  9.555  1.00 61.13  ?  310 TYR   B CD1 1 
ATOM   4919 C  CD2 . TYR   B 1 311 ? -15.171 -10.367 8.595  1.00 49.72  ?  310 TYR   B CD2 1 
ATOM   4920 C  CE1 . TYR   B 1 311 ? -14.258 -8.525  10.436 1.00 62.11  ?  310 TYR   B CE1 1 
ATOM   4921 C  CE2 . TYR   B 1 311 ? -16.048 -9.772  9.481  1.00 54.28  ?  310 TYR   B CE2 1 
ATOM   4922 C  CZ  . TYR   B 1 311 ? -15.594 -8.858  10.391 1.00 53.47  ?  310 TYR   B CZ  1 
ATOM   4923 O  OH  . TYR   B 1 311 ? -16.477 -8.274  11.260 1.00 55.09  ?  310 TYR   B OH  1 
ATOM   4924 N  N   . THR   B 1 312 ? -13.539 -7.703  6.582  1.00 59.26  ?  311 THR   B N   1 
ATOM   4925 C  CA  . THR   B 1 312 ? -13.505 -6.317  7.028  1.00 61.34  ?  311 THR   B CA  1 
ATOM   4926 C  C   . THR   B 1 312 ? -14.728 -6.054  7.891  1.00 63.24  ?  311 THR   B C   1 
ATOM   4927 O  O   . THR   B 1 312 ? -15.820 -6.541  7.591  1.00 70.55  ?  311 THR   B O   1 
ATOM   4928 C  CB  . THR   B 1 312 ? -13.453 -5.322  5.850  1.00 57.08  ?  311 THR   B CB  1 
ATOM   4929 O  OG1 . THR   B 1 312 ? -12.650 -5.856  4.788  1.00 56.34  ?  311 THR   B OG1 1 
ATOM   4930 C  CG2 . THR   B 1 312 ? -12.861 -4.008  6.296  1.00 59.49  ?  311 THR   B CG2 1 
ATOM   4931 N  N   . THR   B 1 313 ? -14.541 -5.312  8.976  1.00 60.14  ?  312 THR   B N   1 
ATOM   4932 C  CA  . THR   B 1 313 ? -15.664 -4.987  9.838  1.00 62.32  ?  312 THR   B CA  1 
ATOM   4933 C  C   . THR   B 1 313 ? -16.621 -4.044  9.112  1.00 63.55  ?  312 THR   B C   1 
ATOM   4934 O  O   . THR   B 1 313 ? -16.208 -3.182  8.328  1.00 58.35  ?  312 THR   B O   1 
ATOM   4935 C  CB  . THR   B 1 313 ? -15.165 -4.373  11.166 1.00 62.33  ?  312 THR   B CB  1 
ATOM   4936 O  OG1 . THR   B 1 313 ? -16.253 -4.176  12.080 1.00 58.43  ?  312 THR   B OG1 1 
ATOM   4937 C  CG2 . THR   B 1 313 ? -14.468 -3.047  10.950 1.00 58.00  ?  312 THR   B CG2 1 
ATOM   4938 N  N   . THR   B 1 314 ? -17.915 -4.264  9.330  1.00 66.49  ?  313 THR   B N   1 
ATOM   4939 C  CA  . THR   B 1 314 ? -18.930 -3.270  9.012  1.00 67.76  ?  313 THR   B CA  1 
ATOM   4940 C  C   . THR   B 1 314 ? -18.997 -2.164  10.055 1.00 73.63  ?  313 THR   B C   1 
ATOM   4941 O  O   . THR   B 1 314 ? -19.623 -1.130  9.798  1.00 78.21  ?  313 THR   B O   1 
ATOM   4942 C  CB  . THR   B 1 314 ? -20.310 -3.932  8.907  1.00 69.33  ?  313 THR   B CB  1 
ATOM   4943 O  OG1 . THR   B 1 314 ? -20.898 -4.056  10.218 1.00 65.79  ?  313 THR   B OG1 1 
ATOM   4944 C  CG2 . THR   B 1 314 ? -20.195 -5.316  8.253  1.00 66.05  ?  313 THR   B CG2 1 
ATOM   4945 N  N   . ILE   B 1 315 ? -18.393 -2.371  11.228 1.00 71.76  ?  314 ILE   B N   1 
ATOM   4946 C  CA  . ILE   B 1 315 ? -18.450 -1.382  12.298 1.00 74.53  ?  314 ILE   B CA  1 
ATOM   4947 C  C   . ILE   B 1 315 ? -17.563 -0.203  11.914 1.00 79.66  ?  314 ILE   B C   1 
ATOM   4948 O  O   . ILE   B 1 315 ? -16.354 -0.353  11.688 1.00 78.98  ?  314 ILE   B O   1 
ATOM   4949 C  CB  . ILE   B 1 315 ? -18.050 -1.995  13.652 1.00 70.40  ?  314 ILE   B CB  1 
ATOM   4950 C  CG1 . ILE   B 1 315 ? -19.286 -2.574  14.356 1.00 78.98  ?  314 ILE   B CG1 1 
ATOM   4951 C  CG2 . ILE   B 1 315 ? -17.413 -0.961  14.562 1.00 60.57  ?  314 ILE   B CG2 1 
ATOM   4952 C  CD1 . ILE   B 1 315 ? -20.342 -1.516  14.807 1.00 77.99  ?  314 ILE   B CD1 1 
ATOM   4953 N  N   . LYS   B 1 316 ? -18.176 0.970   11.796 1.00 88.06  ?  315 LYS   B N   1 
ATOM   4954 C  CA  . LYS   B 1 316 ? -17.492 2.189   11.381 1.00 87.22  ?  315 LYS   B CA  1 
ATOM   4955 C  C   . LYS   B 1 316 ? -17.258 3.064   12.609 1.00 83.70  ?  315 LYS   B C   1 
ATOM   4956 O  O   . LYS   B 1 316 ? -17.882 2.851   13.655 1.00 83.02  ?  315 LYS   B O   1 
ATOM   4957 C  CB  . LYS   B 1 316 ? -18.317 2.926   10.312 1.00 82.60  ?  315 LYS   B CB  1 
ATOM   4958 C  CG  . LYS   B 1 316 ? -19.627 3.563   10.830 1.00 85.50  ?  315 LYS   B CG  1 
ATOM   4959 C  CD  . LYS   B 1 316 ? -20.741 2.528   10.992 1.00 86.17  ?  315 LYS   B CD  1 
ATOM   4960 C  CE  . LYS   B 1 316 ? -22.141 3.119   10.818 1.00 78.74  ?  315 LYS   B CE  1 
ATOM   4961 N  NZ  . LYS   B 1 316 ? -23.148 2.026   10.592 1.00 65.12  ?  315 LYS   B NZ  1 
HETATM 4962 ZN ZN  . ZN    C 2 .   ? 44.524  -50.354 28.135 1.00 91.06  ?  401 ZN    A ZN  1 
HETATM 4963 ZN ZN  . ZN    D 2 .   ? 3.420   -44.614 34.463 1.00 60.83  ?  402 ZN    A ZN  1 
HETATM 4964 ZN ZN  . ZN    E 2 .   ? -3.760  -34.394 37.949 1.00 59.26  ?  403 ZN    A ZN  1 
HETATM 4965 ZN ZN  . ZN    F 2 .   ? 21.540  -28.571 48.213 1.00 55.40  ?  404 ZN    A ZN  1 
HETATM 4966 C  C16 . A1L2A G 3 .   ? 17.476  -48.573 27.812 1.00 39.46  ?  405 A1L2A A C16 1 
HETATM 4967 C  C17 . A1L2A G 3 .   ? 13.095  -43.548 30.968 1.00 38.59  ?  405 A1L2A A C17 1 
HETATM 4968 C  C22 . A1L2A G 3 .   ? 15.767  -37.812 30.583 1.00 32.04  ?  405 A1L2A A C22 1 
HETATM 4969 C  C21 . A1L2A G 3 .   ? 14.712  -38.806 31.005 1.00 30.94  ?  405 A1L2A A C21 1 
HETATM 4970 N  N23 . A1L2A G 3 .   ? 17.130  -38.379 30.571 1.00 38.03  ?  405 A1L2A A N23 1 
HETATM 4971 C  C26 . A1L2A G 3 .   ? 16.084  -40.601 29.966 1.00 36.36  ?  405 A1L2A A C26 1 
HETATM 4972 C  C19 . A1L2A G 3 .   ? 13.625  -41.135 30.663 1.00 36.09  ?  405 A1L2A A C19 1 
HETATM 4973 C  C18 . A1L2A G 3 .   ? 13.982  -42.505 30.616 1.00 35.54  ?  405 A1L2A A C18 1 
HETATM 4974 C  C13 . A1L2A G 3 .   ? 15.157  -48.409 29.405 1.00 49.21  ?  405 A1L2A A C13 1 
HETATM 4975 C  C11 . A1L2A G 3 .   ? 17.517  -47.751 28.962 1.00 41.96  ?  405 A1L2A A C11 1 
HETATM 4976 C  C12 . A1L2A G 3 .   ? 16.371  -47.665 29.771 1.00 48.39  ?  405 A1L2A A C12 1 
HETATM 4977 C  C14 . A1L2A G 3 .   ? 15.110  -49.215 28.268 1.00 44.23  ?  405 A1L2A A C14 1 
HETATM 4978 C  C02 . A1L2A G 3 .   ? 13.597  -45.010 30.930 1.00 46.22  ?  405 A1L2A A C02 1 
HETATM 4979 C  C04 . A1L2A G 3 .   ? 15.238  -46.628 32.050 1.00 48.59  ?  405 A1L2A A C04 1 
HETATM 4980 C  C05 . A1L2A G 3 .   ? 14.978  -47.141 33.533 1.00 45.98  ?  405 A1L2A A C05 1 
HETATM 4981 C  C06 . A1L2A G 3 .   ? 14.332  -47.880 32.379 1.00 44.23  ?  405 A1L2A A C06 1 
HETATM 4982 C  C07 . A1L2A G 3 .   ? 16.414  -46.859 30.994 1.00 44.99  ?  405 A1L2A A C07 1 
HETATM 4983 C  C08 . A1L2A G 3 .   ? 17.644  -46.158 31.253 1.00 41.96  ?  405 A1L2A A C08 1 
HETATM 4984 C  C09 . A1L2A G 3 .   ? 18.813  -46.256 30.385 1.00 39.88  ?  405 A1L2A A C09 1 
HETATM 4985 C  C15 . A1L2A G 3 .   ? 16.291  -49.270 27.478 1.00 50.86  ?  405 A1L2A A C15 1 
HETATM 4986 C  C24 . A1L2A G 3 .   ? 18.045  -37.394 30.142 1.00 34.25  ?  405 A1L2A A C24 1 
HETATM 4987 C  C25 . A1L2A G 3 .   ? 17.204  -39.581 29.709 1.00 27.29  ?  405 A1L2A A C25 1 
HETATM 4988 C  C27 . A1L2A G 3 .   ? 12.324  -40.836 31.123 1.00 37.58  ?  405 A1L2A A C27 1 
HETATM 4989 C  C28 . A1L2A G 3 .   ? 11.411  -41.883 31.507 1.00 39.50  ?  405 A1L2A A C28 1 
HETATM 4990 C  C29 . A1L2A G 3 .   ? 11.812  -43.255 31.449 1.00 41.78  ?  405 A1L2A A C29 1 
HETATM 4991 C  C30 . A1L2A G 3 .   ? 10.871  -44.385 31.870 1.00 43.01  ?  405 A1L2A A C30 1 
HETATM 4992 N  N03 . A1L2A G 3 .   ? 14.566  -45.406 31.852 1.00 47.94  ?  405 A1L2A A N03 1 
HETATM 4993 N  N10 . A1L2A G 3 .   ? 18.758  -47.049 29.250 1.00 49.24  ?  405 A1L2A A N10 1 
HETATM 4994 N  N20 . A1L2A G 3 .   ? 14.642  -40.098 30.235 1.00 39.23  ?  405 A1L2A A N20 1 
HETATM 4995 O  O01 . A1L2A G 3 .   ? 13.161  -45.845 30.085 1.00 45.74  ?  405 A1L2A A O01 1 
HETATM 4996 ZN ZN  . ZN    H 2 .   ? -8.459  3.299   29.593 1.00 95.70  ?  401 ZN    B ZN  1 
HETATM 4997 ZN ZN  . ZN    I 2 .   ? -4.518  -38.232 26.449 1.00 61.51  ?  402 ZN    B ZN  1 
HETATM 4998 ZN ZN  . ZN    J 2 .   ? 6.525   -46.062 23.073 1.00 61.75  ?  403 ZN    B ZN  1 
HETATM 4999 ZN ZN  . ZN    K 2 .   ? 12.096  -21.362 9.932  1.00 55.31  ?  404 ZN    B ZN  1 
HETATM 5000 C  C16 . A1L2A L 3 .   ? -5.694  -22.444 31.462 1.00 49.26  ?  405 A1L2A B C16 1 
HETATM 5001 C  C17 . A1L2A L 3 .   ? -1.725  -28.377 29.247 1.00 35.78  ?  405 A1L2A B C17 1 
HETATM 5002 C  C22 . A1L2A L 3 .   ? 3.984   -25.656 28.575 1.00 36.62  ?  405 A1L2A B C22 1 
HETATM 5003 C  C21 . A1L2A L 3 .   ? 3.145   -26.869 29.010 1.00 36.63  ?  405 A1L2A B C21 1 
HETATM 5004 N  N23 . A1L2A L 3 .   ? 3.806   -24.445 29.416 1.00 35.61  ?  405 A1L2A B N23 1 
HETATM 5005 C  C26 . A1L2A L 3 .   ? 1.406   -25.289 29.937 1.00 35.04  ?  405 A1L2A B C26 1 
HETATM 5006 C  C19 . A1L2A L 3 .   ? 0.667   -27.740 29.114 1.00 35.73  ?  405 A1L2A B C19 1 
HETATM 5007 C  C18 . A1L2A L 3 .   ? -0.705  -27.420 29.283 1.00 36.71  ?  405 A1L2A B C18 1 
HETATM 5008 C  C13 . A1L2A L 3 .   ? -4.609  -23.528 29.020 1.00 44.13  ?  405 A1L2A B C13 1 
HETATM 5009 C  C11 . A1L2A L 3 .   ? -5.920  -23.840 31.122 1.00 51.68  ?  405 A1L2A B C11 1 
HETATM 5010 C  C12 . A1L2A L 3 .   ? -5.396  -24.373 29.926 1.00 55.68  ?  405 A1L2A B C12 1 
HETATM 5011 C  C14 . A1L2A L 3 .   ? -4.382  -22.183 29.349 1.00 48.40  ?  405 A1L2A B C14 1 
HETATM 5012 C  C02 . A1L2A L 3 .   ? -3.193  -27.929 29.343 1.00 44.27  ?  405 A1L2A B C02 1 
HETATM 5013 C  C04 . A1L2A L 3 .   ? -5.124  -26.494 28.326 1.00 51.30  ?  405 A1L2A B C04 1 
HETATM 5014 C  C05 . A1L2A L 3 .   ? -5.601  -26.501 26.814 1.00 51.93  ?  405 A1L2A B C05 1 
HETATM 5015 C  C06 . A1L2A L 3 .   ? -6.208  -27.488 27.807 1.00 49.12  ?  405 A1L2A B C06 1 
HETATM 5016 C  C07 . A1L2A L 3 .   ? -5.631  -25.779 29.591 1.00 51.08  ?  405 A1L2A B C07 1 
HETATM 5017 C  C08 . A1L2A L 3 .   ? -6.378  -26.540 30.515 1.00 49.03  ?  405 A1L2A B C08 1 
HETATM 5018 C  C09 . A1L2A L 3 .   ? -6.894  -25.930 31.737 1.00 49.13  ?  405 A1L2A B C09 1 
HETATM 5019 C  C15 . A1L2A L 3 .   ? -4.929  -21.642 30.583 1.00 53.88  ?  405 A1L2A B C15 1 
HETATM 5020 C  C24 . A1L2A L 3 .   ? 4.573   -23.405 28.874 1.00 30.54  ?  405 A1L2A B C24 1 
HETATM 5021 C  C25 . A1L2A L 3 .   ? 2.357   -24.082 29.557 1.00 29.76  ?  405 A1L2A B C25 1 
HETATM 5022 C  C27 . A1L2A L 3 .   ? 0.998   -29.107 28.873 1.00 30.99  ?  405 A1L2A B C27 1 
HETATM 5023 C  C28 . A1L2A L 3 .   ? -0.045  -30.108 28.827 1.00 34.31  ?  405 A1L2A B C28 1 
HETATM 5024 C  C29 . A1L2A L 3 .   ? -1.418  -29.734 29.006 1.00 36.33  ?  405 A1L2A B C29 1 
HETATM 5025 C  C30 . A1L2A L 3 .   ? -2.539  -30.763 28.934 1.00 40.40  ?  405 A1L2A B C30 1 
HETATM 5026 N  N03 . A1L2A L 3 .   ? -3.758  -27.021 28.409 1.00 48.34  ?  405 A1L2A B N03 1 
HETATM 5027 N  N10 . A1L2A L 3 .   ? -6.668  -24.618 32.028 1.00 49.95  ?  405 A1L2A B N10 1 
HETATM 5028 N  N20 . A1L2A L 3 .   ? 1.667   -26.619 29.176 1.00 38.46  ?  405 A1L2A B N20 1 
HETATM 5029 O  O01 . A1L2A L 3 .   ? -3.944  -28.390 30.218 1.00 48.90  ?  405 A1L2A B O01 1 
HETATM 5030 O  O   . HOH   M 4 .   ? 29.419  -55.829 53.941 1.00 57.03  ?  501 HOH   A O   1 
HETATM 5031 O  O   . HOH   M 4 .   ? 5.066   -35.001 52.334 1.00 40.93  ?  502 HOH   A O   1 
HETATM 5032 O  O   . HOH   M 4 .   ? 13.277  -51.937 28.174 1.00 39.10  ?  503 HOH   A O   1 
HETATM 5033 O  O   . HOH   M 4 .   ? 20.518  -14.093 46.870 1.00 41.81  ?  504 HOH   A O   1 
HETATM 5034 O  O   . HOH   N 4 .   ? -3.167  -40.017 25.866 1.00 39.43  ?  501 HOH   B O   1 
HETATM 5035 O  O   . HOH   N 4 .   ? -7.633  -23.300 5.771  1.00 46.91  ?  502 HOH   B O   1 
HETATM 5036 O  O   . HOH   N 4 .   ? -5.067  -26.446 23.118 1.00 48.08  ?  503 HOH   B O   1 
HETATM 5037 O  O   . HOH   N 4 .   ? -5.564  -32.666 38.792 1.00 50.04  ?  504 HOH   B O   1 
HETATM 5038 O  O   . HOH   N 4 .   ? -12.043 -29.205 30.820 1.00 53.80  ?  505 HOH   B O   1 
HETATM 5039 O  O   . HOH   N 4 .   ? 26.860  -22.288 11.353 1.00 38.03  ?  506 HOH   B O   1 
HETATM 5040 O  O   . HOH   N 4 .   ? 4.041   -36.553 24.110 1.00 46.38  ?  507 HOH   B O   1 
HETATM 5041 O  O   . HOH   N 4 .   ? 6.411   -17.551 10.220 1.00 54.24  ?  508 HOH   B O   1 
# 
