data_8WS1
# 
_entry.id   8WS1 
# 
_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   8WS1         pdb_00008ws1 10.2210/pdb8ws1/pdb 
WWPDB D_1300040147 ?            ?                   
# 
_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       2025-04-16 
_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                        8WS1 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-16 
_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           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              dbearss@haliatherapeutics.com 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Bearss 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4458-826X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Bijpuria, S.'  1 0000-0002-9619-7826 
'Kanavalli, M.' 2 0000-0002-8760-4258 
'Subbiah, R.'   3 0000-0002-1899-5400 
'Mollard, A.'   4 0000-0002-3289-4227 
'Bearss, D.'    5 0000-0002-4458-826X 
# 
_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 human NEK7 D161N mutant' 
_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 'Bijpuria, S.'  1 0000-0002-9619-7826 
primary 'Kanavalli, M.' 2 0000-0002-8760-4258 
primary 'Subbiah, R.'   3 0000-0002-1899-5400 
primary 'Mollard, A.'   4 0000-0002-3289-4227 
primary 'Bearss, D.'    5 0000-0002-4458-826X 
# 
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 'Serine/threonine-protein kinase Nek7' 35669.125 2   2.7.11.34 D161N ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                         62.068    5   ?         ?     ? ? 
3 water       nat water                                  18.015    176 ?         ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Never in mitosis A-related kinase 7,NimA-related protein kinase 7' 
# 
_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       
;MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCI
KEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHR
NIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK
MNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASSLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCI
KEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHR
NIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK
MNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASSLEHHHHHH
;
_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 1,2-ETHANEDIOL EDO 
3 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASP n 
1 3   GLU n 
1 4   GLN n 
1 5   SER n 
1 6   GLN n 
1 7   GLY n 
1 8   MET n 
1 9   GLN n 
1 10  GLY n 
1 11  PRO n 
1 12  PRO n 
1 13  VAL n 
1 14  PRO n 
1 15  GLN n 
1 16  PHE n 
1 17  GLN n 
1 18  PRO n 
1 19  GLN n 
1 20  LYS n 
1 21  ALA n 
1 22  LEU n 
1 23  ARG n 
1 24  PRO n 
1 25  ASP n 
1 26  MET n 
1 27  GLY n 
1 28  TYR n 
1 29  ASN n 
1 30  THR n 
1 31  LEU n 
1 32  ALA n 
1 33  ASN n 
1 34  PHE n 
1 35  ARG n 
1 36  ILE n 
1 37  GLU n 
1 38  LYS n 
1 39  LYS n 
1 40  ILE n 
1 41  GLY n 
1 42  ARG n 
1 43  GLY n 
1 44  GLN n 
1 45  PHE n 
1 46  SER n 
1 47  GLU n 
1 48  VAL n 
1 49  TYR n 
1 50  ARG n 
1 51  ALA n 
1 52  ALA n 
1 53  CYS n 
1 54  LEU n 
1 55  LEU n 
1 56  ASP n 
1 57  GLY n 
1 58  VAL n 
1 59  PRO n 
1 60  VAL n 
1 61  ALA n 
1 62  LEU n 
1 63  LYS n 
1 64  LYS n 
1 65  VAL n 
1 66  GLN n 
1 67  ILE n 
1 68  PHE n 
1 69  ASP n 
1 70  LEU n 
1 71  MET n 
1 72  ASP n 
1 73  ALA n 
1 74  LYS n 
1 75  ALA n 
1 76  ARG n 
1 77  ALA n 
1 78  ASP n 
1 79  CYS n 
1 80  ILE n 
1 81  LYS n 
1 82  GLU n 
1 83  ILE n 
1 84  ASP n 
1 85  LEU n 
1 86  LEU n 
1 87  LYS n 
1 88  GLN n 
1 89  LEU n 
1 90  ASN n 
1 91  HIS n 
1 92  PRO n 
1 93  ASN n 
1 94  VAL n 
1 95  ILE n 
1 96  LYS n 
1 97  TYR n 
1 98  TYR n 
1 99  ALA n 
1 100 SER n 
1 101 PHE n 
1 102 ILE n 
1 103 GLU n 
1 104 ASP n 
1 105 ASN n 
1 106 GLU n 
1 107 LEU n 
1 108 ASN n 
1 109 ILE n 
1 110 VAL n 
1 111 LEU n 
1 112 GLU n 
1 113 LEU n 
1 114 ALA n 
1 115 ASP n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 LEU n 
1 120 SER n 
1 121 ARG n 
1 122 MET n 
1 123 ILE n 
1 124 LYS n 
1 125 HIS n 
1 126 PHE n 
1 127 LYS n 
1 128 LYS n 
1 129 GLN n 
1 130 LYS n 
1 131 ARG n 
1 132 LEU n 
1 133 ILE n 
1 134 PRO n 
1 135 GLU n 
1 136 ARG n 
1 137 THR n 
1 138 VAL n 
1 139 TRP n 
1 140 LYS n 
1 141 TYR n 
1 142 PHE n 
1 143 VAL n 
1 144 GLN n 
1 145 LEU n 
1 146 CYS n 
1 147 SER n 
1 148 ALA n 
1 149 LEU n 
1 150 GLU n 
1 151 HIS n 
1 152 MET n 
1 153 HIS n 
1 154 SER n 
1 155 ARG n 
1 156 ARG n 
1 157 VAL n 
1 158 MET n 
1 159 HIS n 
1 160 ARG n 
1 161 ASN n 
1 162 ILE n 
1 163 LYS n 
1 164 PRO n 
1 165 ALA n 
1 166 ASN n 
1 167 VAL n 
1 168 PHE n 
1 169 ILE n 
1 170 THR n 
1 171 ALA n 
1 172 THR n 
1 173 GLY n 
1 174 VAL n 
1 175 VAL n 
1 176 LYS n 
1 177 LEU n 
1 178 GLY n 
1 179 ASP n 
1 180 LEU n 
1 181 GLY n 
1 182 LEU n 
1 183 GLY n 
1 184 ARG n 
1 185 PHE n 
1 186 PHE n 
1 187 SER n 
1 188 SER n 
1 189 LYS n 
1 190 THR n 
1 191 THR n 
1 192 ALA n 
1 193 ALA n 
1 194 HIS n 
1 195 SER n 
1 196 LEU n 
1 197 VAL n 
1 198 GLY n 
1 199 THR n 
1 200 PRO n 
1 201 TYR n 
1 202 TYR n 
1 203 MET n 
1 204 SER n 
1 205 PRO n 
1 206 GLU n 
1 207 ARG n 
1 208 ILE n 
1 209 HIS n 
1 210 GLU n 
1 211 ASN n 
1 212 GLY n 
1 213 TYR n 
1 214 ASN n 
1 215 PHE n 
1 216 LYS n 
1 217 SER n 
1 218 ASP n 
1 219 ILE n 
1 220 TRP n 
1 221 SER n 
1 222 LEU n 
1 223 GLY n 
1 224 CYS n 
1 225 LEU n 
1 226 LEU n 
1 227 TYR n 
1 228 GLU n 
1 229 MET n 
1 230 ALA n 
1 231 ALA n 
1 232 LEU n 
1 233 GLN n 
1 234 SER n 
1 235 PRO n 
1 236 PHE n 
1 237 TYR n 
1 238 GLY n 
1 239 ASP n 
1 240 LYS n 
1 241 MET n 
1 242 ASN n 
1 243 LEU n 
1 244 TYR n 
1 245 SER n 
1 246 LEU n 
1 247 CYS n 
1 248 LYS n 
1 249 LYS n 
1 250 ILE n 
1 251 GLU n 
1 252 GLN n 
1 253 CYS n 
1 254 ASP n 
1 255 TYR n 
1 256 PRO n 
1 257 PRO n 
1 258 LEU n 
1 259 PRO n 
1 260 SER n 
1 261 ASP n 
1 262 HIS n 
1 263 TYR n 
1 264 SER n 
1 265 GLU n 
1 266 GLU n 
1 267 LEU n 
1 268 ARG n 
1 269 GLN n 
1 270 LEU n 
1 271 VAL n 
1 272 ASN n 
1 273 MET n 
1 274 CYS n 
1 275 ILE n 
1 276 ASN n 
1 277 PRO n 
1 278 ASP n 
1 279 PRO n 
1 280 GLU n 
1 281 LYS n 
1 282 ARG n 
1 283 PRO n 
1 284 ASP n 
1 285 VAL n 
1 286 THR n 
1 287 TYR n 
1 288 VAL n 
1 289 TYR n 
1 290 ASP n 
1 291 VAL n 
1 292 ALA n 
1 293 LYS n 
1 294 ARG n 
1 295 MET n 
1 296 HIS n 
1 297 ALA n 
1 298 CYS n 
1 299 THR n 
1 300 ALA n 
1 301 SER n 
1 302 SER n 
1 303 LEU n 
1 304 GLU n 
1 305 HIS n 
1 306 HIS n 
1 307 HIS n 
1 308 HIS n 
1 309 HIS n 
1 310 HIS 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                   310 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NEK7 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASP 2   2   ?   ?   ?   A . n 
A 1 3   GLU 3   3   ?   ?   ?   A . n 
A 1 4   GLN 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   GLN 6   6   ?   ?   ?   A . n 
A 1 7   GLY 7   7   ?   ?   ?   A . n 
A 1 8   MET 8   8   ?   ?   ?   A . n 
A 1 9   GLN 9   9   ?   ?   ?   A . n 
A 1 10  GLY 10  10  ?   ?   ?   A . n 
A 1 11  PRO 11  11  ?   ?   ?   A . n 
A 1 12  PRO 12  12  ?   ?   ?   A . n 
A 1 13  VAL 13  13  ?   ?   ?   A . n 
A 1 14  PRO 14  14  ?   ?   ?   A . n 
A 1 15  GLN 15  15  ?   ?   ?   A . n 
A 1 16  PHE 16  16  ?   ?   ?   A . n 
A 1 17  GLN 17  17  ?   ?   ?   A . n 
A 1 18  PRO 18  18  ?   ?   ?   A . n 
A 1 19  GLN 19  19  ?   ?   ?   A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  PRO 24  24  24  PRO PRO A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  MET 26  26  26  MET MET A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  ASN 29  29  29  ASN ASN A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  ASN 33  33  33  ASN ASN A . n 
A 1 34  PHE 34  34  34  PHE PHE A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  ARG 50  50  50  ARG ARG A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  CYS 53  53  53  CYS CYS A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  VAL 60  60  60  VAL VAL A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  LEU 62  62  62  LEU LEU A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  LYS 64  64  64  LYS LYS A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  GLN 66  66  66  GLN GLN A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  PHE 68  68  68  PHE PHE A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  MET 71  71  71  MET MET A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  ALA 73  73  73  ALA ALA A . n 
A 1 74  LYS 74  74  74  LYS LYS A . n 
A 1 75  ALA 75  75  75  ALA ALA A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  CYS 79  79  79  CYS CYS A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  LYS 81  81  81  LYS LYS A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  LYS 96  96  96  LYS LYS A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  ALA 99  99  99  ALA ALA A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 PHE 101 101 101 PHE PHE A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 GLU 112 112 112 GLU GLU A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 HIS 125 125 125 HIS HIS A . n 
A 1 126 PHE 126 126 126 PHE PHE A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLN 129 129 129 GLN GLN A . n 
A 1 130 LYS 130 130 130 LYS LYS A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 LEU 132 132 132 LEU LEU A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 TRP 139 139 139 TRP TRP A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 TYR 141 141 141 TYR TYR A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 HIS 153 153 153 HIS HIS A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 ARG 160 160 160 ARG ARG A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 ILE 162 162 162 ILE ILE A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ALA 165 165 165 ALA ALA A . n 
A 1 166 ASN 166 166 166 ASN ASN A . n 
A 1 167 VAL 167 167 167 VAL VAL A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 PHE 186 186 186 PHE PHE A . n 
A 1 187 SER 187 187 ?   ?   ?   A . n 
A 1 188 SER 188 188 ?   ?   ?   A . n 
A 1 189 LYS 189 189 ?   ?   ?   A . n 
A 1 190 THR 190 190 ?   ?   ?   A . n 
A 1 191 THR 191 191 ?   ?   ?   A . n 
A 1 192 ALA 192 192 ?   ?   ?   A . n 
A 1 193 ALA 193 193 ?   ?   ?   A . n 
A 1 194 HIS 194 194 ?   ?   ?   A . n 
A 1 195 SER 195 195 ?   ?   ?   A . n 
A 1 196 LEU 196 196 ?   ?   ?   A . n 
A 1 197 VAL 197 197 ?   ?   ?   A . n 
A 1 198 GLY 198 198 ?   ?   ?   A . n 
A 1 199 THR 199 199 ?   ?   ?   A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ARG 207 207 207 ARG ARG A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 HIS 209 209 209 HIS HIS A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 TYR 213 213 213 TYR TYR A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 PHE 215 215 215 PHE PHE A . n 
A 1 216 LYS 216 216 216 LYS LYS A . n 
A 1 217 SER 217 217 217 SER SER A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 TRP 220 220 220 TRP TRP A . n 
A 1 221 SER 221 221 221 SER SER A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 CYS 224 224 224 CYS CYS A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 MET 229 229 229 MET MET A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 SER 234 234 234 SER SER A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 PHE 236 236 236 PHE PHE A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 GLY 238 238 238 GLY GLY A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 MET 241 241 241 MET MET A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 TYR 244 244 244 TYR TYR A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 LEU 246 246 246 LEU LEU A . n 
A 1 247 CYS 247 247 247 CYS CYS A . n 
A 1 248 LYS 248 248 248 LYS LYS A . n 
A 1 249 LYS 249 249 249 LYS LYS A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 GLU 251 251 251 GLU GLU A . n 
A 1 252 GLN 252 252 252 GLN GLN A . n 
A 1 253 CYS 253 253 253 CYS CYS A . n 
A 1 254 ASP 254 254 254 ASP ASP A . n 
A 1 255 TYR 255 255 255 TYR TYR A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 PRO 257 257 257 PRO PRO A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 HIS 262 262 262 HIS HIS A . n 
A 1 263 TYR 263 263 263 TYR TYR A . n 
A 1 264 SER 264 264 264 SER SER A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 GLU 266 266 266 GLU GLU A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 ARG 268 268 268 ARG ARG A . n 
A 1 269 GLN 269 269 269 GLN GLN A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 MET 273 273 273 MET MET A . n 
A 1 274 CYS 274 274 274 CYS CYS A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 ASN 276 276 276 ASN ASN A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 LYS 281 281 281 LYS LYS A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 ASP 284 284 284 ASP ASP A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 VAL 288 288 288 VAL VAL A . n 
A 1 289 TYR 289 289 289 TYR TYR A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 VAL 291 291 291 VAL VAL A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 LYS 293 293 293 LYS LYS A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 MET 295 295 295 MET MET A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 CYS 298 298 298 CYS CYS A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 SER 301 301 ?   ?   ?   A . n 
A 1 302 SER 302 302 ?   ?   ?   A . n 
A 1 303 LEU 303 303 ?   ?   ?   A . n 
A 1 304 GLU 304 304 ?   ?   ?   A . n 
A 1 305 HIS 305 305 ?   ?   ?   A . n 
A 1 306 HIS 306 306 ?   ?   ?   A . n 
A 1 307 HIS 307 307 ?   ?   ?   A . n 
A 1 308 HIS 308 308 ?   ?   ?   A . n 
A 1 309 HIS 309 309 ?   ?   ?   A . n 
A 1 310 HIS 310 310 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASP 2   2   ?   ?   ?   B . n 
B 1 3   GLU 3   3   ?   ?   ?   B . n 
B 1 4   GLN 4   4   ?   ?   ?   B . n 
B 1 5   SER 5   5   ?   ?   ?   B . n 
B 1 6   GLN 6   6   ?   ?   ?   B . n 
B 1 7   GLY 7   7   ?   ?   ?   B . n 
B 1 8   MET 8   8   ?   ?   ?   B . n 
B 1 9   GLN 9   9   ?   ?   ?   B . n 
B 1 10  GLY 10  10  ?   ?   ?   B . n 
B 1 11  PRO 11  11  ?   ?   ?   B . n 
B 1 12  PRO 12  12  ?   ?   ?   B . n 
B 1 13  VAL 13  13  ?   ?   ?   B . n 
B 1 14  PRO 14  14  ?   ?   ?   B . n 
B 1 15  GLN 15  15  ?   ?   ?   B . n 
B 1 16  PHE 16  16  ?   ?   ?   B . n 
B 1 17  GLN 17  17  ?   ?   ?   B . n 
B 1 18  PRO 18  18  ?   ?   ?   B . n 
B 1 19  GLN 19  19  ?   ?   ?   B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  PRO 24  24  24  PRO PRO B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  MET 26  26  26  MET MET B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  TYR 28  28  28  TYR TYR B . n 
B 1 29  ASN 29  29  29  ASN ASN B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  ASN 33  33  33  ASN ASN B . n 
B 1 34  PHE 34  34  34  PHE PHE B . n 
B 1 35  ARG 35  35  35  ARG ARG B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  GLU 37  37  37  GLU GLU B . n 
B 1 38  LYS 38  38  38  LYS LYS B . n 
B 1 39  LYS 39  39  39  LYS LYS B . n 
B 1 40  ILE 40  40  40  ILE ILE B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ARG 42  42  42  ARG ARG B . n 
B 1 43  GLY 43  43  43  GLY GLY B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  TYR 49  49  49  TYR TYR B . n 
B 1 50  ARG 50  50  50  ARG ARG B . n 
B 1 51  ALA 51  51  51  ALA ALA B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  CYS 53  53  53  CYS CYS B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  GLY 57  57  57  GLY GLY B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  PRO 59  59  59  PRO PRO B . n 
B 1 60  VAL 60  60  60  VAL VAL B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  LEU 62  62  62  LEU LEU B . n 
B 1 63  LYS 63  63  63  LYS LYS B . n 
B 1 64  LYS 64  64  64  LYS LYS B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  GLN 66  66  66  GLN GLN B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  PHE 68  68  68  PHE PHE B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  MET 71  71  71  MET MET B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  ALA 73  73  73  ALA ALA B . n 
B 1 74  LYS 74  74  74  LYS LYS B . n 
B 1 75  ALA 75  75  75  ALA ALA B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  ALA 77  77  77  ALA ALA B . n 
B 1 78  ASP 78  78  78  ASP ASP B . n 
B 1 79  CYS 79  79  79  CYS CYS B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  LYS 81  81  81  LYS LYS B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  ASP 84  84  84  ASP ASP B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  GLN 88  88  88  GLN GLN B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  PRO 92  92  92  PRO PRO B . n 
B 1 93  ASN 93  93  93  ASN ASN B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ILE 95  95  95  ILE ILE B . n 
B 1 96  LYS 96  96  96  LYS LYS B . n 
B 1 97  TYR 97  97  97  TYR TYR B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  ALA 99  99  99  ALA ALA B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 PHE 101 101 101 PHE PHE B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 GLU 103 103 103 GLU GLU B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 ASN 105 105 105 ASN ASN B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 LEU 107 107 107 LEU LEU B . n 
B 1 108 ASN 108 108 108 ASN ASN B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 GLU 112 112 112 GLU GLU B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 ASP 118 118 118 ASP ASP B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 SER 120 120 120 SER SER B . n 
B 1 121 ARG 121 121 121 ARG ARG B . n 
B 1 122 MET 122 122 122 MET MET B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 LYS 124 124 124 LYS LYS B . n 
B 1 125 HIS 125 125 125 HIS HIS B . n 
B 1 126 PHE 126 126 126 PHE PHE B . n 
B 1 127 LYS 127 127 127 LYS LYS B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLN 129 129 129 GLN GLN B . n 
B 1 130 LYS 130 130 130 LYS LYS B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 LEU 132 132 132 LEU LEU B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 GLU 135 135 135 GLU GLU B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 TRP 139 139 139 TRP TRP B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 TYR 141 141 141 TYR TYR B . n 
B 1 142 PHE 142 142 142 PHE PHE B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 GLN 144 144 144 GLN GLN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 ALA 148 148 148 ALA ALA B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 HIS 151 151 151 HIS HIS B . n 
B 1 152 MET 152 152 152 MET MET B . n 
B 1 153 HIS 153 153 153 HIS HIS B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 MET 158 158 158 MET MET B . n 
B 1 159 HIS 159 159 159 HIS HIS B . n 
B 1 160 ARG 160 160 160 ARG ARG B . n 
B 1 161 ASN 161 161 161 ASN ASN B . n 
B 1 162 ILE 162 162 162 ILE ILE B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 PRO 164 164 164 PRO PRO B . n 
B 1 165 ALA 165 165 165 ALA ALA B . n 
B 1 166 ASN 166 166 166 ASN ASN B . n 
B 1 167 VAL 167 167 167 VAL VAL B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 ALA 171 171 171 ALA ALA B . n 
B 1 172 THR 172 172 172 THR THR B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLY 178 178 178 GLY GLY B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 PHE 186 186 186 PHE PHE B . n 
B 1 187 SER 187 187 187 SER SER B . n 
B 1 188 SER 188 188 ?   ?   ?   B . n 
B 1 189 LYS 189 189 ?   ?   ?   B . n 
B 1 190 THR 190 190 ?   ?   ?   B . n 
B 1 191 THR 191 191 ?   ?   ?   B . n 
B 1 192 ALA 192 192 ?   ?   ?   B . n 
B 1 193 ALA 193 193 ?   ?   ?   B . n 
B 1 194 HIS 194 194 ?   ?   ?   B . n 
B 1 195 SER 195 195 ?   ?   ?   B . n 
B 1 196 LEU 196 196 ?   ?   ?   B . n 
B 1 197 VAL 197 197 ?   ?   ?   B . n 
B 1 198 GLY 198 198 ?   ?   ?   B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 TYR 202 202 202 TYR TYR B . n 
B 1 203 MET 203 203 203 MET MET B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 PRO 205 205 205 PRO PRO B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 ARG 207 207 207 ARG ARG B . n 
B 1 208 ILE 208 208 208 ILE ILE B . n 
B 1 209 HIS 209 209 209 HIS HIS B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 TYR 213 213 213 TYR TYR B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 PHE 215 215 215 PHE PHE B . n 
B 1 216 LYS 216 216 216 LYS LYS B . n 
B 1 217 SER 217 217 217 SER SER B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 TRP 220 220 220 TRP TRP B . n 
B 1 221 SER 221 221 221 SER SER B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 CYS 224 224 224 CYS CYS B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 LEU 226 226 226 LEU LEU B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 MET 229 229 229 MET MET B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ALA 231 231 231 ALA ALA B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 SER 234 234 234 SER SER B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 PHE 236 236 236 PHE PHE B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 GLY 238 238 238 GLY GLY B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 MET 241 241 241 MET MET B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 TYR 244 244 244 TYR TYR B . n 
B 1 245 SER 245 245 245 SER SER B . n 
B 1 246 LEU 246 246 246 LEU LEU B . n 
B 1 247 CYS 247 247 247 CYS CYS B . n 
B 1 248 LYS 248 248 248 LYS LYS B . n 
B 1 249 LYS 249 249 249 LYS LYS B . n 
B 1 250 ILE 250 250 250 ILE ILE B . n 
B 1 251 GLU 251 251 251 GLU GLU B . n 
B 1 252 GLN 252 252 252 GLN GLN B . n 
B 1 253 CYS 253 253 253 CYS CYS B . n 
B 1 254 ASP 254 254 254 ASP ASP B . n 
B 1 255 TYR 255 255 255 TYR TYR B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 PRO 257 257 257 PRO PRO B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 PRO 259 259 259 PRO PRO B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 HIS 262 262 262 HIS HIS B . n 
B 1 263 TYR 263 263 263 TYR TYR B . n 
B 1 264 SER 264 264 264 SER SER B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 GLU 266 266 266 GLU GLU B . n 
B 1 267 LEU 267 267 267 LEU LEU B . n 
B 1 268 ARG 268 268 268 ARG ARG B . n 
B 1 269 GLN 269 269 269 GLN GLN B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 ASN 272 272 272 ASN ASN B . n 
B 1 273 MET 273 273 273 MET MET B . n 
B 1 274 CYS 274 274 274 CYS CYS B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 ASN 276 276 276 ASN ASN B . n 
B 1 277 PRO 277 277 277 PRO PRO B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 PRO 279 279 279 PRO PRO B . n 
B 1 280 GLU 280 280 280 GLU GLU B . n 
B 1 281 LYS 281 281 281 LYS LYS B . n 
B 1 282 ARG 282 282 282 ARG ARG B . n 
B 1 283 PRO 283 283 283 PRO PRO B . n 
B 1 284 ASP 284 284 284 ASP ASP B . n 
B 1 285 VAL 285 285 285 VAL VAL B . n 
B 1 286 THR 286 286 286 THR THR B . n 
B 1 287 TYR 287 287 287 TYR TYR B . n 
B 1 288 VAL 288 288 288 VAL VAL B . n 
B 1 289 TYR 289 289 289 TYR TYR B . n 
B 1 290 ASP 290 290 290 ASP ASP B . n 
B 1 291 VAL 291 291 291 VAL VAL B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 LYS 293 293 293 LYS LYS B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 MET 295 295 295 MET MET B . n 
B 1 296 HIS 296 296 296 HIS HIS B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 CYS 298 298 298 CYS CYS B . n 
B 1 299 THR 299 299 299 THR THR B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 SER 301 301 ?   ?   ?   B . n 
B 1 302 SER 302 302 ?   ?   ?   B . n 
B 1 303 LEU 303 303 ?   ?   ?   B . n 
B 1 304 GLU 304 304 ?   ?   ?   B . n 
B 1 305 HIS 305 305 ?   ?   ?   B . n 
B 1 306 HIS 306 306 ?   ?   ?   B . n 
B 1 307 HIS 307 307 ?   ?   ?   B . n 
B 1 308 HIS 308 308 ?   ?   ?   B . n 
B 1 309 HIS 309 309 ?   ?   ?   B . n 
B 1 310 HIS 310 310 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 EDO 1  401 401 EDO EDO A . 
D 2 EDO 1  401 402 EDO EDO B . 
E 2 EDO 1  402 403 EDO EDO B . 
F 2 EDO 1  403 404 EDO EDO B . 
G 2 EDO 1  404 405 EDO EDO B . 
H 3 HOH 1  501 8   HOH HOH A . 
H 3 HOH 2  502 14  HOH HOH A . 
H 3 HOH 3  503 32  HOH HOH A . 
H 3 HOH 4  504 35  HOH HOH A . 
H 3 HOH 5  505 38  HOH HOH A . 
H 3 HOH 6  506 65  HOH HOH A . 
H 3 HOH 7  507 33  HOH HOH A . 
H 3 HOH 8  508 169 HOH HOH A . 
H 3 HOH 9  509 22  HOH HOH A . 
H 3 HOH 10 510 46  HOH HOH A . 
H 3 HOH 11 511 61  HOH HOH A . 
H 3 HOH 12 512 138 HOH HOH A . 
H 3 HOH 13 513 50  HOH HOH A . 
H 3 HOH 14 514 34  HOH HOH A . 
H 3 HOH 15 515 59  HOH HOH A . 
H 3 HOH 16 516 16  HOH HOH A . 
H 3 HOH 17 517 18  HOH HOH A . 
H 3 HOH 18 518 60  HOH HOH A . 
H 3 HOH 19 519 54  HOH HOH A . 
H 3 HOH 20 520 123 HOH HOH A . 
H 3 HOH 21 521 4   HOH HOH A . 
H 3 HOH 22 522 132 HOH HOH A . 
H 3 HOH 23 523 125 HOH HOH A . 
H 3 HOH 24 524 30  HOH HOH A . 
H 3 HOH 25 525 153 HOH HOH A . 
H 3 HOH 26 526 58  HOH HOH A . 
H 3 HOH 27 527 45  HOH HOH A . 
H 3 HOH 28 528 139 HOH HOH A . 
H 3 HOH 29 529 40  HOH HOH A . 
H 3 HOH 30 530 12  HOH HOH A . 
H 3 HOH 31 531 157 HOH HOH A . 
H 3 HOH 32 532 6   HOH HOH A . 
H 3 HOH 33 533 136 HOH HOH A . 
H 3 HOH 34 534 117 HOH HOH A . 
H 3 HOH 35 535 166 HOH HOH A . 
H 3 HOH 36 536 23  HOH HOH A . 
H 3 HOH 37 537 44  HOH HOH A . 
H 3 HOH 38 538 177 HOH HOH A . 
H 3 HOH 39 539 135 HOH HOH A . 
H 3 HOH 40 540 31  HOH HOH A . 
H 3 HOH 41 541 187 HOH HOH A . 
H 3 HOH 42 542 163 HOH HOH A . 
H 3 HOH 43 543 95  HOH HOH A . 
H 3 HOH 44 544 178 HOH HOH A . 
H 3 HOH 45 545 124 HOH HOH A . 
H 3 HOH 46 546 57  HOH HOH A . 
H 3 HOH 47 547 48  HOH HOH A . 
H 3 HOH 48 548 51  HOH HOH A . 
H 3 HOH 49 549 39  HOH HOH A . 
H 3 HOH 50 550 5   HOH HOH A . 
H 3 HOH 51 551 142 HOH HOH A . 
H 3 HOH 52 552 165 HOH HOH A . 
H 3 HOH 53 553 185 HOH HOH A . 
H 3 HOH 54 554 70  HOH HOH A . 
H 3 HOH 55 555 41  HOH HOH A . 
H 3 HOH 56 556 174 HOH HOH A . 
H 3 HOH 57 557 53  HOH HOH A . 
H 3 HOH 58 558 186 HOH HOH A . 
H 3 HOH 59 559 167 HOH HOH A . 
H 3 HOH 60 560 128 HOH HOH A . 
H 3 HOH 61 561 64  HOH HOH A . 
H 3 HOH 62 562 97  HOH HOH A . 
H 3 HOH 63 563 143 HOH HOH A . 
H 3 HOH 64 564 162 HOH HOH A . 
H 3 HOH 65 565 72  HOH HOH A . 
H 3 HOH 66 566 146 HOH HOH A . 
H 3 HOH 67 567 130 HOH HOH A . 
H 3 HOH 68 568 56  HOH HOH A . 
H 3 HOH 69 569 116 HOH HOH A . 
H 3 HOH 70 570 94  HOH HOH A . 
H 3 HOH 71 571 66  HOH HOH A . 
H 3 HOH 72 572 137 HOH HOH A . 
H 3 HOH 73 573 129 HOH HOH A . 
H 3 HOH 74 574 17  HOH HOH A . 
H 3 HOH 75 575 63  HOH HOH A . 
H 3 HOH 76 576 141 HOH HOH A . 
H 3 HOH 77 577 52  HOH HOH A . 
H 3 HOH 78 578 29  HOH HOH A . 
H 3 HOH 79 579 37  HOH HOH A . 
H 3 HOH 80 580 47  HOH HOH A . 
H 3 HOH 81 581 62  HOH HOH A . 
H 3 HOH 82 582 24  HOH HOH A . 
H 3 HOH 83 583 159 HOH HOH A . 
H 3 HOH 84 584 42  HOH HOH A . 
H 3 HOH 85 585 133 HOH HOH A . 
H 3 HOH 86 586 43  HOH HOH A . 
H 3 HOH 87 587 173 HOH HOH A . 
I 3 HOH 1  501 109 HOH HOH B . 
I 3 HOH 2  502 98  HOH HOH B . 
I 3 HOH 3  503 120 HOH HOH B . 
I 3 HOH 4  504 75  HOH HOH B . 
I 3 HOH 5  505 172 HOH HOH B . 
I 3 HOH 6  506 79  HOH HOH B . 
I 3 HOH 7  507 83  HOH HOH B . 
I 3 HOH 8  508 134 HOH HOH B . 
I 3 HOH 9  509 27  HOH HOH B . 
I 3 HOH 10 510 170 HOH HOH B . 
I 3 HOH 11 511 107 HOH HOH B . 
I 3 HOH 12 512 168 HOH HOH B . 
I 3 HOH 13 513 108 HOH HOH B . 
I 3 HOH 14 514 156 HOH HOH B . 
I 3 HOH 15 515 158 HOH HOH B . 
I 3 HOH 16 516 3   HOH HOH B . 
I 3 HOH 17 517 121 HOH HOH B . 
I 3 HOH 18 518 28  HOH HOH B . 
I 3 HOH 19 519 102 HOH HOH B . 
I 3 HOH 20 520 67  HOH HOH B . 
I 3 HOH 21 521 101 HOH HOH B . 
I 3 HOH 22 522 100 HOH HOH B . 
I 3 HOH 23 523 9   HOH HOH B . 
I 3 HOH 24 524 182 HOH HOH B . 
I 3 HOH 25 525 49  HOH HOH B . 
I 3 HOH 26 526 69  HOH HOH B . 
I 3 HOH 27 527 81  HOH HOH B . 
I 3 HOH 28 528 155 HOH HOH B . 
I 3 HOH 29 529 11  HOH HOH B . 
I 3 HOH 30 530 68  HOH HOH B . 
I 3 HOH 31 531 183 HOH HOH B . 
I 3 HOH 32 532 1   HOH HOH B . 
I 3 HOH 33 533 171 HOH HOH B . 
I 3 HOH 34 534 106 HOH HOH B . 
I 3 HOH 35 535 25  HOH HOH B . 
I 3 HOH 36 536 90  HOH HOH B . 
I 3 HOH 37 537 160 HOH HOH B . 
I 3 HOH 38 538 21  HOH HOH B . 
I 3 HOH 39 539 26  HOH HOH B . 
I 3 HOH 40 540 7   HOH HOH B . 
I 3 HOH 41 541 89  HOH HOH B . 
I 3 HOH 42 542 175 HOH HOH B . 
I 3 HOH 43 543 73  HOH HOH B . 
I 3 HOH 44 544 77  HOH HOH B . 
I 3 HOH 45 545 164 HOH HOH B . 
I 3 HOH 46 546 154 HOH HOH B . 
I 3 HOH 47 547 93  HOH HOH B . 
I 3 HOH 48 548 76  HOH HOH B . 
I 3 HOH 49 549 10  HOH HOH B . 
I 3 HOH 50 550 99  HOH HOH B . 
I 3 HOH 51 551 80  HOH HOH B . 
I 3 HOH 52 552 19  HOH HOH B . 
I 3 HOH 53 553 86  HOH HOH B . 
I 3 HOH 54 554 161 HOH HOH B . 
I 3 HOH 55 555 84  HOH HOH B . 
I 3 HOH 56 556 140 HOH HOH B . 
I 3 HOH 57 557 104 HOH HOH B . 
I 3 HOH 58 558 189 HOH HOH B . 
I 3 HOH 59 559 148 HOH HOH B . 
I 3 HOH 60 560 147 HOH HOH B . 
I 3 HOH 61 561 20  HOH HOH B . 
I 3 HOH 62 562 88  HOH HOH B . 
I 3 HOH 63 563 144 HOH HOH B . 
I 3 HOH 64 564 13  HOH HOH B . 
I 3 HOH 65 565 180 HOH HOH B . 
I 3 HOH 66 566 91  HOH HOH B . 
I 3 HOH 67 567 15  HOH HOH B . 
I 3 HOH 68 568 74  HOH HOH B . 
I 3 HOH 69 569 115 HOH HOH B . 
I 3 HOH 70 570 111 HOH HOH B . 
I 3 HOH 71 571 184 HOH HOH B . 
I 3 HOH 72 572 149 HOH HOH B . 
I 3 HOH 73 573 85  HOH HOH B . 
I 3 HOH 74 574 82  HOH HOH B . 
I 3 HOH 75 575 112 HOH HOH B . 
I 3 HOH 76 576 110 HOH HOH B . 
I 3 HOH 77 577 151 HOH HOH B . 
I 3 HOH 78 578 179 HOH HOH B . 
I 3 HOH 79 579 190 HOH HOH B . 
I 3 HOH 80 580 126 HOH HOH B . 
I 3 HOH 81 581 181 HOH HOH B . 
I 3 HOH 82 582 105 HOH HOH B . 
I 3 HOH 83 583 92  HOH HOH B . 
I 3 HOH 84 584 71  HOH HOH B . 
I 3 HOH 85 585 176 HOH HOH B . 
I 3 HOH 86 586 87  HOH HOH B . 
I 3 HOH 87 587 152 HOH HOH B . 
I 3 HOH 88 588 103 HOH HOH B . 
I 3 HOH 89 589 150 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 20  ? CG  ? A LYS 20  CG  
2  1 Y 1 A LYS 20  ? CD  ? A LYS 20  CD  
3  1 Y 1 A LYS 20  ? CE  ? A LYS 20  CE  
4  1 Y 1 A LYS 20  ? NZ  ? A LYS 20  NZ  
5  1 Y 1 A PHE 186 ? CG  ? A PHE 186 CG  
6  1 Y 1 A PHE 186 ? CD1 ? A PHE 186 CD1 
7  1 Y 1 A PHE 186 ? CD2 ? A PHE 186 CD2 
8  1 Y 1 A PHE 186 ? CE1 ? A PHE 186 CE1 
9  1 Y 1 A PHE 186 ? CE2 ? A PHE 186 CE2 
10 1 Y 1 A PHE 186 ? CZ  ? A PHE 186 CZ  
11 1 Y 1 A LYS 240 ? CG  ? A LYS 240 CG  
12 1 Y 1 A LYS 240 ? CD  ? A LYS 240 CD  
13 1 Y 1 A LYS 240 ? CE  ? A LYS 240 CE  
14 1 Y 1 A LYS 240 ? NZ  ? A LYS 240 NZ  
15 1 Y 1 B LYS 20  ? CG  ? B LYS 20  CG  
16 1 Y 1 B LYS 20  ? CD  ? B LYS 20  CD  
17 1 Y 1 B LYS 20  ? CE  ? B LYS 20  CE  
18 1 Y 1 B LYS 20  ? NZ  ? B LYS 20  NZ  
19 1 Y 1 B THR 199 ? OG1 ? B THR 199 OG1 
20 1 Y 1 B THR 199 ? CG2 ? B THR 199 CG2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0267 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WS1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     87.894 
_cell.length_a_esd                 ? 
_cell.length_b                     87.894 
_cell.length_b_esd                 ? 
_cell.length_c                     155.319 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8WS1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WS1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.74 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Tris pH 8.4, PEG 8000 15%' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-12 
_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   0.95373 
_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                        'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.95373 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MX2 
_diffrn_source.pdbx_synchrotron_site       'Australian Synchrotron' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WS1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               43.99 
_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                                     27883 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4 
_reflns_shell.d_res_low                                     2.53 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4011 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.794 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.65 
_refine.aniso_B[1][2]                            0.32 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.65 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.11 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               56.821 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8WS1 
_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                            2.40 
_refine.ls_d_res_low                             43.99 
_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                     26478 
_refine.ls_number_reflns_R_free                  1365 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.96 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18234 
_refine.ls_R_factor_R_free                       0.23837 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17929 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5DE2 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.325 
_refine.pdbx_overall_ESU_R_Free                  0.241 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             9.031 
_refine.overall_SU_ML                            0.200 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        43.99 
_refine_hist.number_atoms_solvent             176 
_refine_hist.number_atoms_total               4543 
_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        4347 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_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' ? 0.007  0.013  4478 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.015  4305 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.529  1.648  6037 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.244  1.583  9919 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.218  5.000  540  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 33.008 21.811 243  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.957 15.000 808  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 21.299 15.000 32   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.200  561  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  4989 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1039 ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 4.511  5.660  2154 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 4.512  5.659  2153 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 6.651  8.474  2687 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 6.650  8.476  2688 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.262  6.277  2324 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.261  6.278  2325 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 8.098  9.146  3348 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 10.853 64.664 4879 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 10.849 64.645 4871 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.400 
_refine_ls_shell.d_res_low                        2.462 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             99 
_refine_ls_shell.number_reflns_R_work             1923 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.262 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.308 
# 
_struct.entry_id                     8WS1 
_struct.title                        'Crystal structure of human NEK7 D161N mutant' 
_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        8WS1 
_struct_keywords.text            'Kinase, Complex, autoinhibitory, human, inflammasomes, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
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 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NEK7_HUMAN 
_struct_ref.pdbx_db_accession          Q8TDX7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCI
KEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHR
DIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK
MNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS
;
_struct_ref.pdbx_align_begin           1 
# 
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 8WS1 A 1 ? 302 ? Q8TDX7 1 ? 302 ? 1 302 
2 1 8WS1 B 1 ? 302 ? Q8TDX7 1 ? 302 ? 1 302 
# 
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 8WS1 ASN A 161 ? UNP Q8TDX7 ASP 161 'engineered mutation' 161 1  
1 8WS1 LEU A 303 ? UNP Q8TDX7 ?   ?   'expression tag'      303 2  
1 8WS1 GLU A 304 ? UNP Q8TDX7 ?   ?   'expression tag'      304 3  
1 8WS1 HIS A 305 ? UNP Q8TDX7 ?   ?   'expression tag'      305 4  
1 8WS1 HIS A 306 ? UNP Q8TDX7 ?   ?   'expression tag'      306 5  
1 8WS1 HIS A 307 ? UNP Q8TDX7 ?   ?   'expression tag'      307 6  
1 8WS1 HIS A 308 ? UNP Q8TDX7 ?   ?   'expression tag'      308 7  
1 8WS1 HIS A 309 ? UNP Q8TDX7 ?   ?   'expression tag'      309 8  
1 8WS1 HIS A 310 ? UNP Q8TDX7 ?   ?   'expression tag'      310 9  
2 8WS1 ASN B 161 ? UNP Q8TDX7 ASP 161 'engineered mutation' 161 10 
2 8WS1 LEU B 303 ? UNP Q8TDX7 ?   ?   'expression tag'      303 11 
2 8WS1 GLU B 304 ? UNP Q8TDX7 ?   ?   'expression tag'      304 12 
2 8WS1 HIS B 305 ? UNP Q8TDX7 ?   ?   'expression tag'      305 13 
2 8WS1 HIS B 306 ? UNP Q8TDX7 ?   ?   'expression tag'      306 14 
2 8WS1 HIS B 307 ? UNP Q8TDX7 ?   ?   'expression tag'      307 15 
2 8WS1 HIS B 308 ? UNP Q8TDX7 ?   ?   'expression tag'      308 16 
2 8WS1 HIS B 309 ? UNP Q8TDX7 ?   ?   'expression tag'      309 17 
2 8WS1 HIS B 310 ? UNP Q8TDX7 ?   ?   'expression tag'      310 18 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ARG A 23  ? GLY A 27  ? ARG A 23  GLY A 27  5 ? 5  
HELX_P HELX_P2  AA2 THR A 30  ? ALA A 32  ? THR A 30  ALA A 32  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 72  ? LYS A 87  ? ASP A 72  LYS A 87  1 ? 16 
HELX_P HELX_P4  AA4 LEU A 119 ? GLN A 129 ? LEU A 119 GLN A 129 1 ? 11 
HELX_P HELX_P5  AA5 PRO A 134 ? ARG A 155 ? PRO A 134 ARG A 155 1 ? 22 
HELX_P HELX_P6  AA6 LYS A 163 ? ALA A 165 ? LYS A 163 ALA A 165 5 ? 3  
HELX_P HELX_P7  AA7 SER A 204 ? HIS A 209 ? SER A 204 HIS A 209 1 ? 6  
HELX_P HELX_P8  AA8 ASN A 214 ? LEU A 232 ? ASN A 214 LEU A 232 1 ? 19 
HELX_P HELX_P9  AA9 ASN A 242 ? GLN A 252 ? ASN A 242 GLN A 252 1 ? 11 
HELX_P HELX_P10 AB1 SER A 264 ? ILE A 275 ? SER A 264 ILE A 275 1 ? 12 
HELX_P HELX_P11 AB2 ASP A 278 ? ARG A 282 ? ASP A 278 ARG A 282 5 ? 5  
HELX_P HELX_P12 AB3 ASP A 284 ? ALA A 300 ? ASP A 284 ALA A 300 1 ? 17 
HELX_P HELX_P13 AB4 MET B 26  ? ALA B 32  ? MET B 26  ALA B 32  5 ? 7  
HELX_P HELX_P14 AB5 ASP B 72  ? LYS B 87  ? ASP B 72  LYS B 87  1 ? 16 
HELX_P HELX_P15 AB6 LEU B 119 ? GLN B 129 ? LEU B 119 GLN B 129 1 ? 11 
HELX_P HELX_P16 AB7 PRO B 134 ? ARG B 155 ? PRO B 134 ARG B 155 1 ? 22 
HELX_P HELX_P17 AB8 LYS B 163 ? ALA B 165 ? LYS B 163 ALA B 165 5 ? 3  
HELX_P HELX_P18 AB9 SER B 204 ? ASN B 211 ? SER B 204 ASN B 211 1 ? 8  
HELX_P HELX_P19 AC1 ASN B 214 ? LEU B 232 ? ASN B 214 LEU B 232 1 ? 19 
HELX_P HELX_P20 AC2 ASN B 242 ? GLN B 252 ? ASN B 242 GLN B 252 1 ? 11 
HELX_P HELX_P21 AC3 SER B 264 ? ILE B 275 ? SER B 264 ILE B 275 1 ? 12 
HELX_P HELX_P22 AC4 ASP B 278 ? ARG B 282 ? ASP B 278 ARG B 282 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 284 ? ALA B 300 ? ASP B 284 ALA B 300 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 5 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 34  ? GLY A 43  ? PHE A 34  GLY A 43  
AA1 2 SER A 46  ? CYS A 53  ? SER A 46  CYS A 53  
AA1 3 PRO A 59  ? VAL A 65  ? PRO A 59  VAL A 65  
AA1 4 GLU A 106 ? GLU A 112 ? GLU A 106 GLU A 112 
AA1 5 TYR A 97  ? GLU A 103 ? TYR A 97  GLU A 103 
AA2 1 GLY A 117 ? ASP A 118 ? GLY A 117 ASP A 118 
AA2 2 VAL A 167 ? ILE A 169 ? VAL A 167 ILE A 169 
AA2 3 VAL A 175 ? LEU A 177 ? VAL A 175 LEU A 177 
AA3 1 PHE B 34  ? ARG B 42  ? PHE B 34  ARG B 42  
AA3 2 SER B 46  ? CYS B 53  ? SER B 46  CYS B 53  
AA3 3 PRO B 59  ? VAL B 65  ? PRO B 59  VAL B 65  
AA3 4 GLU B 106 ? GLU B 112 ? GLU B 106 GLU B 112 
AA3 5 TYR B 97  ? GLU B 103 ? TYR B 97  GLU B 103 
AA4 1 GLY B 117 ? ASP B 118 ? GLY B 117 ASP B 118 
AA4 2 VAL B 167 ? ILE B 169 ? VAL B 167 ILE B 169 
AA4 3 VAL B 175 ? LEU B 177 ? VAL B 175 LEU B 177 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 43  ? N GLY A 43  O SER A 46  ? O SER A 46  
AA1 2 3 N ALA A 51  ? N ALA A 51  O VAL A 60  ? O VAL A 60  
AA1 3 4 N ALA A 61  ? N ALA A 61  O LEU A 111 ? O LEU A 111 
AA1 4 5 O ASN A 108 ? O ASN A 108 N PHE A 101 ? N PHE A 101 
AA2 1 2 N GLY A 117 ? N GLY A 117 O ILE A 169 ? O ILE A 169 
AA2 2 3 N PHE A 168 ? N PHE A 168 O LYS A 176 ? O LYS A 176 
AA3 1 2 N GLU B 37  ? N GLU B 37  O ARG B 50  ? O ARG B 50  
AA3 2 3 N TYR B 49  ? N TYR B 49  O LEU B 62  ? O LEU B 62  
AA3 3 4 N LYS B 63  ? N LYS B 63  O ILE B 109 ? O ILE B 109 
AA3 4 5 O ASN B 108 ? O ASN B 108 N PHE B 101 ? N PHE B 101 
AA4 1 2 N GLY B 117 ? N GLY B 117 O ILE B 169 ? O ILE B 169 
AA4 2 3 N PHE B 168 ? N PHE B 168 O LYS B 176 ? O LYS B 176 
# 
_pdbx_entry_details.entry_id                   8WS1 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              50 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                97.56 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -14.24 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                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 ARG A 23  ? ? -163.82 75.45   
2  1 ASN A 33  ? ? -85.31  30.06   
3  1 LYS A 38  ? ? 178.35  160.89  
4  1 ALA A 116 ? ? -74.04  -126.46 
5  1 ARG A 160 ? ? 81.38   -4.82   
6  1 ASN A 161 ? ? -154.03 59.32   
7  1 ASP A 179 ? ? -158.98 87.80   
8  1 LEU A 182 ? ? 21.08   64.39   
9  1 GLU A 210 ? ? 64.09   -32.16  
10 1 ASN A 211 ? ? 6.51    -20.87  
11 1 ASP A 239 ? ? -66.63  -74.66  
12 1 CYS A 253 ? ? 39.05   62.00   
13 1 GLU B 37  ? ? -95.48  -78.42  
14 1 ASP B 56  ? ? -142.84 -6.57   
15 1 GLU B 135 ? ? -39.60  -33.61  
16 1 ARG B 160 ? ? 80.92   -17.68  
17 1 TYR B 237 ? ? -68.37  -84.02  
18 1 ASP B 239 ? ? -129.37 -82.66  
19 1 LYS B 240 ? ? -43.71  -77.26  
20 1 MET B 241 ? ? 66.12   77.75   
21 1 CYS B 253 ? ? 37.00   54.98   
22 1 SER B 264 ? ? -47.66  157.16  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   MET 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    241 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    242 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            142.60 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A ASP 2   ? A ASP 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A GLN 4   ? A GLN 4   
5  1 Y 1 A SER 5   ? A SER 5   
6  1 Y 1 A GLN 6   ? A GLN 6   
7  1 Y 1 A GLY 7   ? A GLY 7   
8  1 Y 1 A MET 8   ? A MET 8   
9  1 Y 1 A GLN 9   ? A GLN 9   
10 1 Y 1 A GLY 10  ? A GLY 10  
11 1 Y 1 A PRO 11  ? A PRO 11  
12 1 Y 1 A PRO 12  ? A PRO 12  
13 1 Y 1 A VAL 13  ? A VAL 13  
14 1 Y 1 A PRO 14  ? A PRO 14  
15 1 Y 1 A GLN 15  ? A GLN 15  
16 1 Y 1 A PHE 16  ? A PHE 16  
17 1 Y 1 A GLN 17  ? A GLN 17  
18 1 Y 1 A PRO 18  ? A PRO 18  
19 1 Y 1 A GLN 19  ? A GLN 19  
20 1 Y 1 A SER 187 ? A SER 187 
21 1 Y 1 A SER 188 ? A SER 188 
22 1 Y 1 A LYS 189 ? A LYS 189 
23 1 Y 1 A THR 190 ? A THR 190 
24 1 Y 1 A THR 191 ? A THR 191 
25 1 Y 1 A ALA 192 ? A ALA 192 
26 1 Y 1 A ALA 193 ? A ALA 193 
27 1 Y 1 A HIS 194 ? A HIS 194 
28 1 Y 1 A SER 195 ? A SER 195 
29 1 Y 1 A LEU 196 ? A LEU 196 
30 1 Y 1 A VAL 197 ? A VAL 197 
31 1 Y 1 A GLY 198 ? A GLY 198 
32 1 Y 1 A THR 199 ? A THR 199 
33 1 Y 1 A SER 301 ? A SER 301 
34 1 Y 1 A SER 302 ? A SER 302 
35 1 Y 1 A LEU 303 ? A LEU 303 
36 1 Y 1 A GLU 304 ? A GLU 304 
37 1 Y 1 A HIS 305 ? A HIS 305 
38 1 Y 1 A HIS 306 ? A HIS 306 
39 1 Y 1 A HIS 307 ? A HIS 307 
40 1 Y 1 A HIS 308 ? A HIS 308 
41 1 Y 1 A HIS 309 ? A HIS 309 
42 1 Y 1 A HIS 310 ? A HIS 310 
43 1 Y 1 B MET 1   ? B MET 1   
44 1 Y 1 B ASP 2   ? B ASP 2   
45 1 Y 1 B GLU 3   ? B GLU 3   
46 1 Y 1 B GLN 4   ? B GLN 4   
47 1 Y 1 B SER 5   ? B SER 5   
48 1 Y 1 B GLN 6   ? B GLN 6   
49 1 Y 1 B GLY 7   ? B GLY 7   
50 1 Y 1 B MET 8   ? B MET 8   
51 1 Y 1 B GLN 9   ? B GLN 9   
52 1 Y 1 B GLY 10  ? B GLY 10  
53 1 Y 1 B PRO 11  ? B PRO 11  
54 1 Y 1 B PRO 12  ? B PRO 12  
55 1 Y 1 B VAL 13  ? B VAL 13  
56 1 Y 1 B PRO 14  ? B PRO 14  
57 1 Y 1 B GLN 15  ? B GLN 15  
58 1 Y 1 B PHE 16  ? B PHE 16  
59 1 Y 1 B GLN 17  ? B GLN 17  
60 1 Y 1 B PRO 18  ? B PRO 18  
61 1 Y 1 B GLN 19  ? B GLN 19  
62 1 Y 1 B SER 188 ? B SER 188 
63 1 Y 1 B LYS 189 ? B LYS 189 
64 1 Y 1 B THR 190 ? B THR 190 
65 1 Y 1 B THR 191 ? B THR 191 
66 1 Y 1 B ALA 192 ? B ALA 192 
67 1 Y 1 B ALA 193 ? B ALA 193 
68 1 Y 1 B HIS 194 ? B HIS 194 
69 1 Y 1 B SER 195 ? B SER 195 
70 1 Y 1 B LEU 196 ? B LEU 196 
71 1 Y 1 B VAL 197 ? B VAL 197 
72 1 Y 1 B GLY 198 ? B GLY 198 
73 1 Y 1 B SER 301 ? B SER 301 
74 1 Y 1 B SER 302 ? B SER 302 
75 1 Y 1 B LEU 303 ? B LEU 303 
76 1 Y 1 B GLU 304 ? B GLU 304 
77 1 Y 1 B HIS 305 ? B HIS 305 
78 1 Y 1 B HIS 306 ? B HIS 306 
79 1 Y 1 B HIS 307 ? B HIS 307 
80 1 Y 1 B HIS 308 ? B HIS 308 
81 1 Y 1 B HIS 309 ? B HIS 309 
82 1 Y 1 B HIS 310 ? B HIS 310 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
THR N    N N N 314 
THR CA   C N S 315 
THR C    C N N 316 
THR O    O N N 317 
THR CB   C N R 318 
THR OG1  O N N 319 
THR CG2  C N N 320 
THR OXT  O N N 321 
THR H    H N N 322 
THR H2   H N N 323 
THR HA   H N N 324 
THR HB   H N N 325 
THR HG1  H N N 326 
THR HG21 H N N 327 
THR HG22 H N N 328 
THR HG23 H N N 329 
THR HXT  H N N 330 
TRP N    N N N 331 
TRP CA   C N S 332 
TRP C    C N N 333 
TRP O    O N N 334 
TRP CB   C N N 335 
TRP CG   C Y N 336 
TRP CD1  C Y N 337 
TRP CD2  C Y N 338 
TRP NE1  N Y N 339 
TRP CE2  C Y N 340 
TRP CE3  C Y N 341 
TRP CZ2  C Y N 342 
TRP CZ3  C Y N 343 
TRP CH2  C Y N 344 
TRP OXT  O N N 345 
TRP H    H N N 346 
TRP H2   H N N 347 
TRP HA   H N N 348 
TRP HB2  H N N 349 
TRP HB3  H N N 350 
TRP HD1  H N N 351 
TRP HE1  H N N 352 
TRP HE3  H N N 353 
TRP HZ2  H N N 354 
TRP HZ3  H N N 355 
TRP HH2  H N N 356 
TRP HXT  H N N 357 
TYR N    N N N 358 
TYR CA   C N S 359 
TYR C    C N N 360 
TYR O    O N N 361 
TYR CB   C N N 362 
TYR CG   C Y N 363 
TYR CD1  C Y N 364 
TYR CD2  C Y N 365 
TYR CE1  C Y N 366 
TYR CE2  C Y N 367 
TYR CZ   C Y N 368 
TYR OH   O N N 369 
TYR OXT  O N N 370 
TYR H    H N N 371 
TYR H2   H N N 372 
TYR HA   H N N 373 
TYR HB2  H N N 374 
TYR HB3  H N N 375 
TYR HD1  H N N 376 
TYR HD2  H N N 377 
TYR HE1  H N N 378 
TYR HE2  H N N 379 
TYR HH   H N N 380 
TYR HXT  H N N 381 
VAL N    N N N 382 
VAL CA   C N S 383 
VAL C    C N N 384 
VAL O    O N N 385 
VAL CB   C N N 386 
VAL CG1  C N N 387 
VAL CG2  C N N 388 
VAL OXT  O N N 389 
VAL H    H N N 390 
VAL H2   H N N 391 
VAL HA   H N N 392 
VAL HB   H N N 393 
VAL HG11 H N N 394 
VAL HG12 H N N 395 
VAL HG13 H N N 396 
VAL HG21 H N N 397 
VAL HG22 H N N 398 
VAL HG23 H N N 399 
VAL HXT  H N N 400 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5de2 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8WS1 
_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]   0.011377 
_atom_sites.fract_transf_matrix[1][2]   0.006569 
_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]   0.013137 
_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]   0.006438 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 20  ? 55.416 15.981  -29.514 1.00 128.08 ? 20  LYS A N   1 
ATOM   2    C CA  . LYS A 1 20  ? 54.190 15.523  -28.796 1.00 122.49 ? 20  LYS A CA  1 
ATOM   3    C C   . LYS A 1 20  ? 54.302 14.020  -28.513 1.00 113.59 ? 20  LYS A C   1 
ATOM   4    O O   . LYS A 1 20  ? 53.864 13.228  -29.375 1.00 105.79 ? 20  LYS A O   1 
ATOM   5    C CB  . LYS A 1 20  ? 52.932 15.842  -29.615 1.00 121.71 ? 20  LYS A CB  1 
ATOM   6    N N   . ALA A 1 21  ? 54.881 13.662  -27.358 1.00 100.83 ? 21  ALA A N   1 
ATOM   7    C CA  . ALA A 1 21  ? 54.875 12.300  -26.773 1.00 96.17  ? 21  ALA A CA  1 
ATOM   8    C C   . ALA A 1 21  ? 54.440 12.359  -25.297 1.00 97.22  ? 21  ALA A C   1 
ATOM   9    O O   . ALA A 1 21  ? 54.581 13.429  -24.664 1.00 88.44  ? 21  ALA A O   1 
ATOM   10   C CB  . ALA A 1 21  ? 56.237 11.677  -26.935 1.00 99.03  ? 21  ALA A CB  1 
ATOM   11   N N   . LEU A 1 22  ? 53.977 11.223  -24.761 1.00 90.56  ? 22  LEU A N   1 
ATOM   12   C CA  . LEU A 1 22  ? 53.187 11.090  -23.500 1.00 96.38  ? 22  LEU A CA  1 
ATOM   13   C C   . LEU A 1 22  ? 53.885 11.737  -22.286 1.00 87.74  ? 22  LEU A C   1 
ATOM   14   O O   . LEU A 1 22  ? 55.101 11.940  -22.346 1.00 78.32  ? 22  LEU A O   1 
ATOM   15   C CB  . LEU A 1 22  ? 52.942 9.596   -23.264 1.00 99.60  ? 22  LEU A CB  1 
ATOM   16   C CG  . LEU A 1 22  ? 51.902 9.259   -22.201 1.00 104.30 ? 22  LEU A CG  1 
ATOM   17   C CD1 . LEU A 1 22  ? 50.509 9.656   -22.670 1.00 102.23 ? 22  LEU A CD1 1 
ATOM   18   C CD2 . LEU A 1 22  ? 51.949 7.783   -21.839 1.00 111.60 ? 22  LEU A CD2 1 
ATOM   19   N N   . ARG A 1 23  ? 53.115 12.043  -21.229 1.00 87.50  ? 23  ARG A N   1 
ATOM   20   C CA  . ARG A 1 23  ? 53.569 12.636  -19.938 1.00 94.52  ? 23  ARG A CA  1 
ATOM   21   C C   . ARG A 1 23  ? 52.491 12.465  -18.862 1.00 90.78  ? 23  ARG A C   1 
ATOM   22   O O   . ARG A 1 23  ? 51.821 13.436  -18.513 1.00 85.80  ? 23  ARG A O   1 
ATOM   23   C CB  . ARG A 1 23  ? 53.857 14.131  -20.116 1.00 95.66  ? 23  ARG A CB  1 
ATOM   24   C CG  . ARG A 1 23  ? 55.222 14.447  -20.705 1.00 105.40 ? 23  ARG A CG  1 
ATOM   25   C CD  . ARG A 1 23  ? 55.407 15.935  -20.893 1.00 110.03 ? 23  ARG A CD  1 
ATOM   26   N NE  . ARG A 1 23  ? 54.705 16.451  -22.055 1.00 114.62 ? 23  ARG A NE  1 
ATOM   27   C CZ  . ARG A 1 23  ? 54.540 17.745  -22.321 1.00 121.89 ? 23  ARG A CZ  1 
ATOM   28   N NH1 . ARG A 1 23  ? 55.021 18.662  -21.498 1.00 119.53 ? 23  ARG A NH1 1 
ATOM   29   N NH2 . ARG A 1 23  ? 53.889 18.120  -23.409 1.00 119.09 ? 23  ARG A NH2 1 
ATOM   30   N N   . PRO A 1 24  ? 52.297 11.252  -18.283 1.00 95.18  ? 24  PRO A N   1 
ATOM   31   C CA  . PRO A 1 24  ? 51.240 11.011  -17.288 1.00 96.38  ? 24  PRO A CA  1 
ATOM   32   C C   . PRO A 1 24  ? 51.185 11.982  -16.096 1.00 100.48 ? 24  PRO A C   1 
ATOM   33   O O   . PRO A 1 24  ? 50.115 12.186  -15.542 1.00 103.31 ? 24  PRO A O   1 
ATOM   34   C CB  . PRO A 1 24  ? 51.576 9.613   -16.737 1.00 97.34  ? 24  PRO A CB  1 
ATOM   35   C CG  . PRO A 1 24  ? 52.296 8.928   -17.881 1.00 96.34  ? 24  PRO A CG  1 
ATOM   36   C CD  . PRO A 1 24  ? 53.077 10.034  -18.566 1.00 92.93  ? 24  PRO A CD  1 
ATOM   37   N N   . ASP A 1 25  ? 52.343 12.520  -15.713 1.00 100.84 ? 25  ASP A N   1 
ATOM   38   C CA  . ASP A 1 25  ? 52.515 13.455  -14.570 1.00 101.11 ? 25  ASP A CA  1 
ATOM   39   C C   . ASP A 1 25  ? 51.743 14.753  -14.840 1.00 94.72  ? 25  ASP A C   1 
ATOM   40   O O   . ASP A 1 25  ? 51.278 15.364  -13.865 1.00 94.13  ? 25  ASP A O   1 
ATOM   41   C CB  . ASP A 1 25  ? 54.002 13.722  -14.311 1.00 108.57 ? 25  ASP A CB  1 
ATOM   42   C CG  . ASP A 1 25  ? 54.787 14.103  -15.558 1.00 113.93 ? 25  ASP A CG  1 
ATOM   43   O OD1 . ASP A 1 25  ? 54.679 13.371  -16.567 1.00 118.13 ? 25  ASP A OD1 1 
ATOM   44   O OD2 . ASP A 1 25  ? 55.491 15.133  -15.518 1.00 113.20 ? 25  ASP A OD2 1 
ATOM   45   N N   . MET A 1 26  ? 51.616 15.147  -16.113 1.00 95.79  ? 26  MET A N   1 
ATOM   46   C CA  . MET A 1 26  ? 51.024 16.441  -16.562 1.00 92.33  ? 26  MET A CA  1 
ATOM   47   C C   . MET A 1 26  ? 49.485 16.350  -16.609 1.00 85.79  ? 26  MET A C   1 
ATOM   48   O O   . MET A 1 26  ? 48.830 17.407  -16.633 1.00 83.39  ? 26  MET A O   1 
ATOM   49   C CB  . MET A 1 26  ? 51.582 16.819  -17.940 1.00 93.33  ? 26  MET A CB  1 
ATOM   50   C CG  . MET A 1 26  ? 51.543 18.311  -18.224 1.00 104.38 ? 26  MET A CG  1 
ATOM   51   S SD  . MET A 1 26  ? 52.841 19.266  -17.406 1.00 100.73 ? 26  MET A SD  1 
ATOM   52   C CE  . MET A 1 26  ? 53.938 19.606  -18.783 1.00 90.34  ? 26  MET A CE  1 
ATOM   53   N N   . GLY A 1 27  ? 48.926 15.134  -16.606 1.00 81.24  ? 27  GLY A N   1 
ATOM   54   C CA  . GLY A 1 27  ? 47.480 14.874  -16.447 1.00 73.91  ? 27  GLY A CA  1 
ATOM   55   C C   . GLY A 1 27  ? 46.693 15.281  -17.684 1.00 70.54  ? 27  GLY A C   1 
ATOM   56   O O   . GLY A 1 27  ? 47.209 15.102  -18.799 1.00 60.25  ? 27  GLY A O   1 
ATOM   57   N N   . TYR A 1 28  ? 45.494 15.832  -17.488 1.00 62.12  ? 28  TYR A N   1 
ATOM   58   C CA  . TYR A 1 28  ? 44.621 16.388  -18.554 1.00 65.52  ? 28  TYR A CA  1 
ATOM   59   C C   . TYR A 1 28  ? 45.100 17.785  -19.011 1.00 69.02  ? 28  TYR A C   1 
ATOM   60   O O   . TYR A 1 28  ? 44.318 18.454  -19.727 1.00 71.56  ? 28  TYR A O   1 
ATOM   61   C CB  . TYR A 1 28  ? 43.178 16.469  -18.044 1.00 64.70  ? 28  TYR A CB  1 
ATOM   62   C CG  . TYR A 1 28  ? 42.334 15.237  -18.250 1.00 64.25  ? 28  TYR A CG  1 
ATOM   63   C CD1 . TYR A 1 28  ? 42.785 13.973  -17.907 1.00 74.06  ? 28  TYR A CD1 1 
ATOM   64   C CD2 . TYR A 1 28  ? 41.055 15.347  -18.757 1.00 65.23  ? 28  TYR A CD2 1 
ATOM   65   C CE1 . TYR A 1 28  ? 41.992 12.848  -18.085 1.00 73.76  ? 28  TYR A CE1 1 
ATOM   66   C CE2 . TYR A 1 28  ? 40.250 14.238  -18.949 1.00 70.97  ? 28  TYR A CE2 1 
ATOM   67   C CZ  . TYR A 1 28  ? 40.717 12.979  -18.614 1.00 78.17  ? 28  TYR A CZ  1 
ATOM   68   O OH  . TYR A 1 28  ? 39.894 11.898  -18.793 1.00 74.58  ? 28  TYR A OH  1 
ATOM   69   N N   . ASN A 1 29  ? 46.328 18.216  -18.674 1.00 63.65  ? 29  ASN A N   1 
ATOM   70   C CA  . ASN A 1 29  ? 46.769 19.634  -18.815 1.00 65.12  ? 29  ASN A CA  1 
ATOM   71   C C   . ASN A 1 29  ? 47.883 19.808  -19.858 1.00 62.90  ? 29  ASN A C   1 
ATOM   72   O O   . ASN A 1 29  ? 48.680 20.735  -19.698 1.00 75.01  ? 29  ASN A O   1 
ATOM   73   C CB  . ASN A 1 29  ? 47.227 20.202  -17.471 1.00 70.61  ? 29  ASN A CB  1 
ATOM   74   C CG  . ASN A 1 29  ? 46.077 20.386  -16.508 1.00 72.68  ? 29  ASN A CG  1 
ATOM   75   O OD1 . ASN A 1 29  ? 45.245 21.275  -16.692 1.00 76.92  ? 29  ASN A OD1 1 
ATOM   76   N ND2 . ASN A 1 29  ? 46.030 19.562  -15.477 1.00 74.64  ? 29  ASN A ND2 1 
ATOM   77   N N   . THR A 1 30  ? 47.930 18.989  -20.905 1.00 61.33  ? 30  THR A N   1 
ATOM   78   C CA  . THR A 1 30  ? 48.828 19.192  -22.077 1.00 62.35  ? 30  THR A CA  1 
ATOM   79   C C   . THR A 1 30  ? 48.291 18.376  -23.251 1.00 57.55  ? 30  THR A C   1 
ATOM   80   O O   . THR A 1 30  ? 47.797 17.275  -22.994 1.00 63.14  ? 30  THR A O   1 
ATOM   81   C CB  . THR A 1 30  ? 50.284 18.800  -21.787 1.00 65.01  ? 30  THR A CB  1 
ATOM   82   O OG1 . THR A 1 30  ? 51.031 18.851  -23.011 1.00 63.42  ? 30  THR A OG1 1 
ATOM   83   C CG2 . THR A 1 30  ? 50.402 17.410  -21.207 1.00 67.36  ? 30  THR A CG2 1 
ATOM   84   N N   . LEU A 1 31  ? 48.411 18.902  -24.473 1.00 57.65  ? 31  LEU A N   1 
ATOM   85   C CA  . LEU A 1 31  ? 47.911 18.292  -25.736 1.00 61.18  ? 31  LEU A CA  1 
ATOM   86   C C   . LEU A 1 31  ? 48.553 16.912  -25.954 1.00 65.43  ? 31  LEU A C   1 
ATOM   87   O O   . LEU A 1 31  ? 47.910 16.051  -26.606 1.00 68.53  ? 31  LEU A O   1 
ATOM   88   C CB  . LEU A 1 31  ? 48.208 19.231  -26.913 1.00 58.65  ? 31  LEU A CB  1 
ATOM   89   C CG  . LEU A 1 31  ? 47.426 20.551  -26.930 1.00 61.99  ? 31  LEU A CG  1 
ATOM   90   C CD1 . LEU A 1 31  ? 47.881 21.458  -28.071 1.00 62.74  ? 31  LEU A CD1 1 
ATOM   91   C CD2 . LEU A 1 31  ? 45.925 20.301  -27.039 1.00 61.73  ? 31  LEU A CD2 1 
ATOM   92   N N   . ALA A 1 32  ? 49.758 16.707  -25.421 1.00 64.06  ? 32  ALA A N   1 
ATOM   93   C CA  . ALA A 1 32  ? 50.550 15.464  -25.560 1.00 73.73  ? 32  ALA A CA  1 
ATOM   94   C C   . ALA A 1 32  ? 49.701 14.237  -25.196 1.00 71.46  ? 32  ALA A C   1 
ATOM   95   O O   . ALA A 1 32  ? 49.751 13.256  -25.952 1.00 76.62  ? 32  ALA A O   1 
ATOM   96   C CB  . ALA A 1 32  ? 51.782 15.546  -24.694 1.00 78.18  ? 32  ALA A CB  1 
ATOM   97   N N   . ASN A 1 33  ? 48.936 14.306  -24.104 1.00 60.98  ? 33  ASN A N   1 
ATOM   98   C CA  . ASN A 1 33  ? 48.166 13.164  -23.550 1.00 61.92  ? 33  ASN A CA  1 
ATOM   99   C C   . ASN A 1 33  ? 46.806 13.040  -24.239 1.00 57.26  ? 33  ASN A C   1 
ATOM   100  O O   . ASN A 1 33  ? 45.891 12.510  -23.599 1.00 65.27  ? 33  ASN A O   1 
ATOM   101  C CB  . ASN A 1 33  ? 48.037 13.284  -22.031 1.00 63.83  ? 33  ASN A CB  1 
ATOM   102  C CG  . ASN A 1 33  ? 49.406 13.418  -21.415 1.00 61.55  ? 33  ASN A CG  1 
ATOM   103  O OD1 . ASN A 1 33  ? 50.387 13.119  -22.084 1.00 70.90  ? 33  ASN A OD1 1 
ATOM   104  N ND2 . ASN A 1 33  ? 49.487 13.914  -20.195 1.00 62.86  ? 33  ASN A ND2 1 
ATOM   105  N N   . PHE A 1 34  ? 46.692 13.436  -25.509 1.00 61.57  ? 34  PHE A N   1 
ATOM   106  C CA  . PHE A 1 34  ? 45.410 13.433  -26.267 1.00 67.62  ? 34  PHE A CA  1 
ATOM   107  C C   . PHE A 1 34  ? 45.666 13.143  -27.753 1.00 60.05  ? 34  PHE A C   1 
ATOM   108  O O   . PHE A 1 34  ? 46.614 13.705  -28.305 1.00 63.33  ? 34  PHE A O   1 
ATOM   109  C CB  . PHE A 1 34  ? 44.672 14.772  -26.091 1.00 64.69  ? 34  PHE A CB  1 
ATOM   110  C CG  . PHE A 1 34  ? 44.186 15.049  -24.693 1.00 57.75  ? 34  PHE A CG  1 
ATOM   111  C CD1 . PHE A 1 34  ? 43.081 14.392  -24.187 1.00 61.99  ? 34  PHE A CD1 1 
ATOM   112  C CD2 . PHE A 1 34  ? 44.839 15.954  -23.880 1.00 54.58  ? 34  PHE A CD2 1 
ATOM   113  C CE1 . PHE A 1 34  ? 42.645 14.627  -22.895 1.00 56.95  ? 34  PHE A CE1 1 
ATOM   114  C CE2 . PHE A 1 34  ? 44.408 16.183  -22.587 1.00 55.57  ? 34  PHE A CE2 1 
ATOM   115  C CZ  . PHE A 1 34  ? 43.309 15.525  -22.099 1.00 59.55  ? 34  PHE A CZ  1 
ATOM   116  N N   . ARG A 1 35  ? 44.814 12.320  -28.370 1.00 70.30  ? 35  ARG A N   1 
ATOM   117  C CA  . ARG A 1 35  ? 44.767 12.069  -29.839 1.00 77.34  ? 35  ARG A CA  1 
ATOM   118  C C   . ARG A 1 35  ? 43.487 12.700  -30.377 1.00 67.91  ? 35  ARG A C   1 
ATOM   119  O O   . ARG A 1 35  ? 42.419 12.198  -30.014 1.00 71.04  ? 35  ARG A O   1 
ATOM   120  C CB  . ARG A 1 35  ? 44.759 10.566  -30.164 1.00 92.29  ? 35  ARG A CB  1 
ATOM   121  C CG  . ARG A 1 35  ? 46.014 10.047  -30.857 1.00 105.67 ? 35  ARG A CG  1 
ATOM   122  C CD  . ARG A 1 35  ? 46.029 8.532   -31.046 1.00 111.27 ? 35  ARG A CD  1 
ATOM   123  N NE  . ARG A 1 35  ? 47.353 7.957   -30.781 1.00 116.62 ? 35  ARG A NE  1 
ATOM   124  C CZ  . ARG A 1 35  ? 47.599 6.786   -30.177 1.00 117.71 ? 35  ARG A CZ  1 
ATOM   125  N NH1 . ARG A 1 35  ? 46.612 6.012   -29.747 1.00 113.71 ? 35  ARG A NH1 1 
ATOM   126  N NH2 . ARG A 1 35  ? 48.851 6.396   -29.995 1.00 110.28 ? 35  ARG A NH2 1 
ATOM   127  N N   . ILE A 1 36  ? 43.606 13.744  -31.197 1.00 64.00  ? 36  ILE A N   1 
ATOM   128  C CA  . ILE A 1 36  ? 42.466 14.410  -31.893 1.00 71.29  ? 36  ILE A CA  1 
ATOM   129  C C   . ILE A 1 36  ? 41.943 13.442  -32.960 1.00 71.92  ? 36  ILE A C   1 
ATOM   130  O O   . ILE A 1 36  ? 42.750 13.058  -33.815 1.00 82.02  ? 36  ILE A O   1 
ATOM   131  C CB  . ILE A 1 36  ? 42.915 15.760  -32.499 1.00 78.43  ? 36  ILE A CB  1 
ATOM   132  C CG1 . ILE A 1 36  ? 43.484 16.712  -31.440 1.00 83.82  ? 36  ILE A CG1 1 
ATOM   133  C CG2 . ILE A 1 36  ? 41.782 16.418  -33.274 1.00 77.09  ? 36  ILE A CG2 1 
ATOM   134  C CD1 . ILE A 1 36  ? 44.517 17.684  -31.971 1.00 91.41  ? 36  ILE A CD1 1 
ATOM   135  N N   . GLU A 1 37  ? 40.659 13.063  -32.914 1.00 71.89  ? 37  GLU A N   1 
ATOM   136  C CA  . GLU A 1 37  ? 40.056 12.052  -33.834 1.00 70.01  ? 37  GLU A CA  1 
ATOM   137  C C   . GLU A 1 37  ? 39.213 12.710  -34.937 1.00 70.45  ? 37  GLU A C   1 
ATOM   138  O O   . GLU A 1 37  ? 39.059 12.054  -35.965 1.00 77.34  ? 37  GLU A O   1 
ATOM   139  C CB  . GLU A 1 37  ? 39.168 11.045  -33.100 1.00 70.83  ? 37  GLU A CB  1 
ATOM   140  C CG  . GLU A 1 37  ? 39.925 9.905   -32.435 1.00 78.92  ? 37  GLU A CG  1 
ATOM   141  C CD  . GLU A 1 37  ? 39.104 9.176   -31.379 1.00 86.13  ? 37  GLU A CD  1 
ATOM   142  O OE1 . GLU A 1 37  ? 37.856 9.316   -31.396 1.00 84.74  ? 37  GLU A OE1 1 
ATOM   143  O OE2 . GLU A 1 37  ? 39.705 8.486   -30.528 1.00 88.56  ? 37  GLU A OE2 1 
ATOM   144  N N   . LYS A 1 38  ? 38.631 13.895  -34.729 1.00 66.29  ? 38  LYS A N   1 
ATOM   145  C CA  . LYS A 1 38  ? 37.842 14.627  -35.769 1.00 70.52  ? 38  LYS A CA  1 
ATOM   146  C C   . LYS A 1 38  ? 37.288 15.924  -35.180 1.00 68.58  ? 38  LYS A C   1 
ATOM   147  O O   . LYS A 1 38  ? 37.178 16.011  -33.946 1.00 75.66  ? 38  LYS A O   1 
ATOM   148  C CB  . LYS A 1 38  ? 36.649 13.831  -36.328 1.00 70.74  ? 38  LYS A CB  1 
ATOM   149  C CG  . LYS A 1 38  ? 35.618 13.371  -35.307 1.00 76.55  ? 38  LYS A CG  1 
ATOM   150  C CD  . LYS A 1 38  ? 34.233 13.066  -35.856 1.00 75.04  ? 38  LYS A CD  1 
ATOM   151  C CE  . LYS A 1 38  ? 33.308 12.598  -34.749 1.00 82.64  ? 38  LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 38  ? 31.899 12.518  -35.186 1.00 82.30  ? 38  LYS A NZ  1 
ATOM   153  N N   . LYS A 1 39  ? 36.910 16.861  -36.045 1.00 59.56  ? 39  LYS A N   1 
ATOM   154  C CA  . LYS A 1 39  ? 36.239 18.130  -35.668 1.00 62.75  ? 39  LYS A CA  1 
ATOM   155  C C   . LYS A 1 39  ? 34.740 17.860  -35.511 1.00 59.81  ? 39  LYS A C   1 
ATOM   156  O O   . LYS A 1 39  ? 34.208 17.083  -36.309 1.00 63.65  ? 39  LYS A O   1 
ATOM   157  C CB  . LYS A 1 39  ? 36.512 19.198  -36.729 1.00 66.53  ? 39  LYS A CB  1 
ATOM   158  C CG  . LYS A 1 39  ? 35.788 20.521  -36.522 1.00 73.77  ? 39  LYS A CG  1 
ATOM   159  C CD  . LYS A 1 39  ? 36.222 21.632  -37.469 1.00 82.13  ? 39  LYS A CD  1 
ATOM   160  C CE  . LYS A 1 39  ? 37.723 21.840  -37.535 1.00 78.87  ? 39  LYS A CE  1 
ATOM   161  N NZ  . LYS A 1 39  ? 38.040 23.161  -38.119 1.00 75.87  ? 39  LYS A NZ  1 
ATOM   162  N N   . ILE A 1 40  ? 34.098 18.462  -34.506 1.00 59.45  ? 40  ILE A N   1 
ATOM   163  C CA  . ILE A 1 40  ? 32.651 18.257  -34.192 1.00 58.55  ? 40  ILE A CA  1 
ATOM   164  C C   . ILE A 1 40  ? 31.957 19.606  -33.989 1.00 56.62  ? 40  ILE A C   1 
ATOM   165  O O   . ILE A 1 40  ? 30.745 19.608  -33.720 1.00 56.36  ? 40  ILE A O   1 
ATOM   166  C CB  . ILE A 1 40  ? 32.458 17.319  -32.977 1.00 62.50  ? 40  ILE A CB  1 
ATOM   167  C CG1 . ILE A 1 40  ? 33.079 17.863  -31.688 1.00 64.64  ? 40  ILE A CG1 1 
ATOM   168  C CG2 . ILE A 1 40  ? 32.988 15.929  -33.286 1.00 66.77  ? 40  ILE A CG2 1 
ATOM   169  C CD1 . ILE A 1 40  ? 32.837 16.972  -30.481 1.00 64.09  ? 40  ILE A CD1 1 
ATOM   170  N N   . GLY A 1 41  ? 32.674 20.717  -34.151 1.00 61.92  ? 41  GLY A N   1 
ATOM   171  C CA  . GLY A 1 41  ? 32.138 22.054  -33.839 1.00 59.79  ? 41  GLY A CA  1 
ATOM   172  C C   . GLY A 1 41  ? 33.064 23.144  -34.330 1.00 58.69  ? 41  GLY A C   1 
ATOM   173  O O   . GLY A 1 41  ? 34.283 22.896  -34.419 1.00 53.94  ? 41  GLY A O   1 
ATOM   174  N N   . ARG A 1 42  ? 32.496 24.318  -34.597 1.00 56.81  ? 42  ARG A N   1 
ATOM   175  C CA  . ARG A 1 42  ? 33.212 25.504  -35.122 1.00 59.10  ? 42  ARG A CA  1 
ATOM   176  C C   . ARG A 1 42  ? 32.396 26.720  -34.702 1.00 58.04  ? 42  ARG A C   1 
ATOM   177  O O   . ARG A 1 42  ? 31.205 26.741  -35.011 1.00 65.60  ? 42  ARG A O   1 
ATOM   178  C CB  . ARG A 1 42  ? 33.316 25.355  -36.641 1.00 63.39  ? 42  ARG A CB  1 
ATOM   179  C CG  . ARG A 1 42  ? 34.162 26.391  -37.362 1.00 68.18  ? 42  ARG A CG  1 
ATOM   180  C CD  . ARG A 1 42  ? 33.972 26.225  -38.863 1.00 68.83  ? 42  ARG A CD  1 
ATOM   181  N NE  . ARG A 1 42  ? 34.156 27.469  -39.587 1.00 65.65  ? 42  ARG A NE  1 
ATOM   182  C CZ  . ARG A 1 42  ? 35.340 28.011  -39.828 1.00 75.12  ? 42  ARG A CZ  1 
ATOM   183  N NH1 . ARG A 1 42  ? 36.444 27.429  -39.388 1.00 78.49  ? 42  ARG A NH1 1 
ATOM   184  N NH2 . ARG A 1 42  ? 35.421 29.135  -40.515 1.00 75.17  ? 42  ARG A NH2 1 
ATOM   185  N N   . GLY A 1 43  ? 32.990 27.642  -33.957 1.00 54.08  ? 43  GLY A N   1 
ATOM   186  C CA  . GLY A 1 43  ? 32.348 28.906  -33.562 1.00 54.76  ? 43  GLY A CA  1 
ATOM   187  C C   . GLY A 1 43  ? 33.188 30.091  -33.998 1.00 55.76  ? 43  GLY A C   1 
ATOM   188  O O   . GLY A 1 43  ? 34.271 29.876  -34.585 1.00 60.37  ? 43  GLY A O   1 
ATOM   189  N N   . GLN A 1 44  ? 32.727 31.300  -33.698 1.00 58.14  ? 44  GLN A N   1 
ATOM   190  C CA  A GLN A 1 44  ? 33.387 32.582  -34.067 0.50 61.84  ? 44  GLN A CA  1 
ATOM   191  C CA  B GLN A 1 44  ? 33.413 32.541  -34.146 0.50 60.43  ? 44  GLN A CA  1 
ATOM   192  C C   . GLN A 1 44  ? 34.870 32.536  -33.660 1.00 60.80  ? 44  GLN A C   1 
ATOM   193  O O   . GLN A 1 44  ? 35.714 33.039  -34.422 1.00 58.32  ? 44  GLN A O   1 
ATOM   194  C CB  A GLN A 1 44  ? 32.624 33.737  -33.406 0.50 64.69  ? 44  GLN A CB  1 
ATOM   195  C CB  B GLN A 1 44  ? 32.671 33.804  -33.704 0.50 60.91  ? 44  GLN A CB  1 
ATOM   196  C CG  A GLN A 1 44  ? 32.597 35.024  -34.221 0.50 70.79  ? 44  GLN A CG  1 
ATOM   197  C CG  B GLN A 1 44  ? 33.241 35.083  -34.319 0.50 64.60  ? 44  GLN A CG  1 
ATOM   198  C CD  A GLN A 1 44  ? 31.403 35.883  -33.877 0.50 70.74  ? 44  GLN A CD  1 
ATOM   199  C CD  B GLN A 1 44  ? 33.513 34.985  -35.806 0.50 62.94  ? 44  GLN A CD  1 
ATOM   200  O OE1 A GLN A 1 44  ? 30.423 35.415  -33.301 0.50 77.72  ? 44  GLN A OE1 1 
ATOM   201  O OE1 B GLN A 1 44  ? 32.604 34.945  -36.635 0.50 62.82  ? 44  GLN A OE1 1 
ATOM   202  N NE2 A GLN A 1 44  ? 31.474 37.154  -34.233 0.50 67.48  ? 44  GLN A NE2 1 
ATOM   203  N NE2 B GLN A 1 44  ? 34.787 34.975  -36.163 0.50 56.65  ? 44  GLN A NE2 1 
ATOM   204  N N   . PHE A 1 45  ? 35.178 31.958  -32.491 1.00 56.68  ? 45  PHE A N   1 
ATOM   205  C CA  . PHE A 1 45  ? 36.540 32.090  -31.897 1.00 57.63  ? 45  PHE A CA  1 
ATOM   206  C C   . PHE A 1 45  ? 37.164 30.749  -31.495 1.00 52.79  ? 45  PHE A C   1 
ATOM   207  O O   . PHE A 1 45  ? 38.170 30.790  -30.751 1.00 57.41  ? 45  PHE A O   1 
ATOM   208  C CB  . PHE A 1 45  ? 36.496 32.984  -30.653 1.00 58.98  ? 45  PHE A CB  1 
ATOM   209  C CG  . PHE A 1 45  ? 35.942 34.360  -30.881 1.00 56.50  ? 45  PHE A CG  1 
ATOM   210  C CD1 . PHE A 1 45  ? 36.744 35.367  -31.395 1.00 60.41  ? 45  PHE A CD1 1 
ATOM   211  C CD2 . PHE A 1 45  ? 34.622 34.650  -30.578 1.00 63.69  ? 45  PHE A CD2 1 
ATOM   212  C CE1 . PHE A 1 45  ? 36.237 36.638  -31.605 1.00 58.88  ? 45  PHE A CE1 1 
ATOM   213  C CE2 . PHE A 1 45  ? 34.111 35.920  -30.802 1.00 64.44  ? 45  PHE A CE2 1 
ATOM   214  C CZ  . PHE A 1 45  ? 34.919 36.910  -31.318 1.00 63.28  ? 45  PHE A CZ  1 
ATOM   215  N N   . SER A 1 46  ? 36.618 29.625  -31.955 1.00 53.73  ? 46  SER A N   1 
ATOM   216  C CA  . SER A 1 46  ? 36.939 28.277  -31.419 1.00 57.65  ? 46  SER A CA  1 
ATOM   217  C C   . SER A 1 46  ? 36.551 27.167  -32.401 1.00 55.93  ? 46  SER A C   1 
ATOM   218  O O   . SER A 1 46  ? 35.567 27.341  -33.124 1.00 54.91  ? 46  SER A O   1 
ATOM   219  C CB  . SER A 1 46  ? 36.264 28.060  -30.086 1.00 57.59  ? 46  SER A CB  1 
ATOM   220  O OG  . SER A 1 46  ? 34.862 28.293  -30.175 1.00 57.56  ? 46  SER A OG  1 
ATOM   221  N N   . GLU A 1 47  ? 37.318 26.075  -32.377 1.00 55.04  ? 47  GLU A N   1 
ATOM   222  C CA  . GLU A 1 47  ? 37.035 24.769  -33.018 1.00 62.85  ? 47  GLU A CA  1 
ATOM   223  C C   . GLU A 1 47  ? 36.849 23.756  -31.884 1.00 65.75  ? 47  GLU A C   1 
ATOM   224  O O   . GLU A 1 47  ? 37.567 23.895  -30.892 1.00 66.20  ? 47  GLU A O   1 
ATOM   225  C CB  . GLU A 1 47  ? 38.216 24.320  -33.886 1.00 67.82  ? 47  GLU A CB  1 
ATOM   226  C CG  . GLU A 1 47  ? 38.963 25.450  -34.582 1.00 76.91  ? 47  GLU A CG  1 
ATOM   227  C CD  . GLU A 1 47  ? 38.815 25.517  -36.098 1.00 79.68  ? 47  GLU A CD  1 
ATOM   228  O OE1 . GLU A 1 47  ? 37.699 25.288  -36.608 1.00 75.45  ? 47  GLU A OE1 1 
ATOM   229  O OE2 . GLU A 1 47  ? 39.820 25.826  -36.773 1.00 94.58  ? 47  GLU A OE2 1 
ATOM   230  N N   . VAL A 1 48  ? 35.950 22.778  -32.019 1.00 63.38  ? 48  VAL A N   1 
ATOM   231  C CA  . VAL A 1 48  ? 35.808 21.662  -31.039 1.00 58.87  ? 48  VAL A CA  1 
ATOM   232  C C   . VAL A 1 48  ? 36.205 20.371  -31.727 1.00 50.34  ? 48  VAL A C   1 
ATOM   233  O O   . VAL A 1 48  ? 35.755 20.162  -32.836 1.00 52.70  ? 48  VAL A O   1 
ATOM   234  C CB  . VAL A 1 48  ? 34.378 21.506  -30.491 1.00 62.07  ? 48  VAL A CB  1 
ATOM   235  C CG1 . VAL A 1 48  ? 34.377 20.725  -29.180 1.00 57.46  ? 48  VAL A CG1 1 
ATOM   236  C CG2 . VAL A 1 48  ? 33.687 22.841  -30.330 1.00 65.41  ? 48  VAL A CG2 1 
ATOM   237  N N   . TYR A 1 49  ? 36.909 19.500  -31.023 1.00 49.84  ? 49  TYR A N   1 
ATOM   238  C CA  . TYR A 1 49  ? 37.360 18.181  -31.527 1.00 51.95  ? 49  TYR A CA  1 
ATOM   239  C C   . TYR A 1 49  ? 36.799 17.073  -30.624 1.00 52.21  ? 49  TYR A C   1 
ATOM   240  O O   . TYR A 1 49  ? 36.661 17.289  -29.416 1.00 48.80  ? 49  TYR A O   1 
ATOM   241  C CB  . TYR A 1 49  ? 38.892 18.157  -31.608 1.00 54.78  ? 49  TYR A CB  1 
ATOM   242  C CG  . TYR A 1 49  ? 39.461 19.239  -32.491 1.00 58.33  ? 49  TYR A CG  1 
ATOM   243  C CD1 . TYR A 1 49  ? 39.593 19.060  -33.860 1.00 64.50  ? 49  TYR A CD1 1 
ATOM   244  C CD2 . TYR A 1 49  ? 39.807 20.471  -31.968 1.00 58.94  ? 49  TYR A CD2 1 
ATOM   245  C CE1 . TYR A 1 49  ? 40.082 20.065  -34.679 1.00 65.50  ? 49  TYR A CE1 1 
ATOM   246  C CE2 . TYR A 1 49  ? 40.299 21.484  -32.770 1.00 60.59  ? 49  TYR A CE2 1 
ATOM   247  C CZ  . TYR A 1 49  ? 40.429 21.286  -34.132 1.00 64.04  ? 49  TYR A CZ  1 
ATOM   248  O OH  . TYR A 1 49  ? 40.915 22.291  -34.913 1.00 68.12  ? 49  TYR A OH  1 
ATOM   249  N N   . ARG A 1 50  ? 36.466 15.921  -31.206 1.00 51.71  ? 50  ARG A N   1 
ATOM   250  C CA  . ARG A 1 50  ? 36.404 14.634  -30.474 1.00 52.03  ? 50  ARG A CA  1 
ATOM   251  C C   . ARG A 1 50  ? 37.854 14.222  -30.274 1.00 47.98  ? 50  ARG A C   1 
ATOM   252  O O   . ARG A 1 50  ? 38.633 14.419  -31.199 1.00 55.90  ? 50  ARG A O   1 
ATOM   253  C CB  . ARG A 1 50  ? 35.602 13.585  -31.252 1.00 66.14  ? 50  ARG A CB  1 
ATOM   254  C CG  . ARG A 1 50  ? 35.393 12.295  -30.480 1.00 70.54  ? 50  ARG A CG  1 
ATOM   255  C CD  . ARG A 1 50  ? 35.062 11.017  -31.237 1.00 79.92  ? 50  ARG A CD  1 
ATOM   256  N NE  . ARG A 1 50  ? 35.048 10.113  -30.091 1.00 91.39  ? 50  ARG A NE  1 
ATOM   257  C CZ  . ARG A 1 50  ? 34.093 9.253   -29.749 1.00 94.13  ? 50  ARG A CZ  1 
ATOM   258  N NH1 . ARG A 1 50  ? 33.043 9.033   -30.526 1.00 105.27 ? 50  ARG A NH1 1 
ATOM   259  N NH2 . ARG A 1 50  ? 34.219 8.575   -28.619 1.00 94.89  ? 50  ARG A NH2 1 
ATOM   260  N N   . ALA A 1 51  ? 38.237 13.762  -29.092 1.00 46.33  ? 51  ALA A N   1 
ATOM   261  C CA  . ALA A 1 51  ? 39.620 13.321  -28.826 1.00 46.20  ? 51  ALA A CA  1 
ATOM   262  C C   . ALA A 1 51  ? 39.593 12.161  -27.841 1.00 53.65  ? 51  ALA A C   1 
ATOM   263  O O   . ALA A 1 51  ? 38.493 11.876  -27.322 1.00 54.26  ? 51  ALA A O   1 
ATOM   264  C CB  . ALA A 1 51  ? 40.424 14.468  -28.294 1.00 47.37  ? 51  ALA A CB  1 
ATOM   265  N N   . ALA A 1 52  ? 40.755 11.551  -27.582 1.00 60.35  ? 52  ALA A N   1 
ATOM   266  C CA  . ALA A 1 52  ? 40.923 10.427  -26.624 1.00 63.10  ? 52  ALA A CA  1 
ATOM   267  C C   . ALA A 1 52  ? 42.087 10.716  -25.677 1.00 60.34  ? 52  ALA A C   1 
ATOM   268  O O   . ALA A 1 52  ? 43.211 10.957  -26.159 1.00 59.39  ? 52  ALA A O   1 
ATOM   269  C CB  . ALA A 1 52  ? 41.138 9.123   -27.361 1.00 65.38  ? 52  ALA A CB  1 
ATOM   270  N N   . CYS A 1 53  ? 41.817 10.697  -24.373 1.00 67.75  ? 53  CYS A N   1 
ATOM   271  C CA  . CYS A 1 53  ? 42.849 10.730  -23.312 1.00 71.44  ? 53  CYS A CA  1 
ATOM   272  C C   . CYS A 1 53  ? 43.642 9.435   -23.441 1.00 72.46  ? 53  CYS A C   1 
ATOM   273  O O   . CYS A 1 53  ? 43.010 8.371   -23.454 1.00 80.61  ? 53  CYS A O   1 
ATOM   274  C CB  . CYS A 1 53  ? 42.230 10.855  -21.924 1.00 78.74  ? 53  CYS A CB  1 
ATOM   275  S SG  . CYS A 1 53  ? 43.424 11.312  -20.637 1.00 85.12  ? 53  CYS A SG  1 
ATOM   276  N N   . LEU A 1 54  ? 44.958 9.536   -23.596 1.00 76.69  ? 54  LEU A N   1 
ATOM   277  C CA  . LEU A 1 54  ? 45.866 8.366   -23.716 1.00 79.95  ? 54  LEU A CA  1 
ATOM   278  C C   . LEU A 1 54  ? 46.202 7.812   -22.322 1.00 75.93  ? 54  LEU A C   1 
ATOM   279  O O   . LEU A 1 54  ? 46.797 6.727   -22.263 1.00 80.71  ? 54  LEU A O   1 
ATOM   280  C CB  . LEU A 1 54  ? 47.111 8.796   -24.499 1.00 73.71  ? 54  LEU A CB  1 
ATOM   281  C CG  . LEU A 1 54  ? 46.828 9.285   -25.918 1.00 77.59  ? 54  LEU A CG  1 
ATOM   282  C CD1 . LEU A 1 54  ? 48.087 9.849   -26.566 1.00 76.54  ? 54  LEU A CD1 1 
ATOM   283  C CD2 . LEU A 1 54  ? 46.234 8.169   -26.766 1.00 77.31  ? 54  LEU A CD2 1 
ATOM   284  N N   . LEU A 1 55  ? 45.788 8.488   -21.245 1.00 78.37  ? 55  LEU A N   1 
ATOM   285  C CA  . LEU A 1 55  ? 46.050 8.056   -19.842 1.00 85.76  ? 55  LEU A CA  1 
ATOM   286  C C   . LEU A 1 55  ? 44.967 7.087   -19.339 1.00 84.97  ? 55  LEU A C   1 
ATOM   287  O O   . LEU A 1 55  ? 45.276 6.321   -18.411 1.00 86.58  ? 55  LEU A O   1 
ATOM   288  C CB  . LEU A 1 55  ? 46.126 9.278   -18.919 1.00 82.88  ? 55  LEU A CB  1 
ATOM   289  C CG  . LEU A 1 55  ? 47.107 10.377  -19.326 1.00 86.71  ? 55  LEU A CG  1 
ATOM   290  C CD1 . LEU A 1 55  ? 47.522 11.195  -18.113 1.00 89.16  ? 55  LEU A CD1 1 
ATOM   291  C CD2 . LEU A 1 55  ? 48.337 9.814   -20.022 1.00 81.82  ? 55  LEU A CD2 1 
ATOM   292  N N   . ASP A 1 56  ? 43.743 7.134   -19.874 1.00 82.59  ? 56  ASP A N   1 
ATOM   293  C CA  . ASP A 1 56  ? 42.617 6.309   -19.352 1.00 84.39  ? 56  ASP A CA  1 
ATOM   294  C C   . ASP A 1 56  ? 41.726 5.777   -20.482 1.00 76.58  ? 56  ASP A C   1 
ATOM   295  O O   . ASP A 1 56  ? 40.730 5.100   -20.148 1.00 86.99  ? 56  ASP A O   1 
ATOM   296  C CB  . ASP A 1 56  ? 41.799 7.094   -18.315 1.00 91.73  ? 56  ASP A CB  1 
ATOM   297  C CG  . ASP A 1 56  ? 41.385 8.496   -18.744 1.00 88.81  ? 56  ASP A CG  1 
ATOM   298  O OD1 . ASP A 1 56  ? 41.368 8.759   -19.957 1.00 85.59  ? 56  ASP A OD1 1 
ATOM   299  O OD2 . ASP A 1 56  ? 41.069 9.311   -17.855 1.00 87.80  ? 56  ASP A OD2 1 
ATOM   300  N N   . GLY A 1 57  ? 42.057 6.059   -21.747 1.00 69.61  ? 57  GLY A N   1 
ATOM   301  C CA  . GLY A 1 57  ? 41.248 5.695   -22.928 1.00 65.64  ? 57  GLY A CA  1 
ATOM   302  C C   . GLY A 1 57  ? 39.874 6.358   -22.938 1.00 69.67  ? 57  GLY A C   1 
ATOM   303  O O   . GLY A 1 57  ? 39.069 6.020   -23.819 1.00 73.21  ? 57  GLY A O   1 
ATOM   304  N N   . VAL A 1 58  ? 39.603 7.281   -22.012 1.00 71.57  ? 58  VAL A N   1 
ATOM   305  C CA  . VAL A 1 58  ? 38.313 8.026   -21.933 1.00 69.98  ? 58  VAL A CA  1 
ATOM   306  C C   . VAL A 1 58  ? 38.245 8.956   -23.138 1.00 70.35  ? 58  VAL A C   1 
ATOM   307  O O   . VAL A 1 58  ? 39.226 9.605   -23.485 1.00 71.27  ? 58  VAL A O   1 
ATOM   308  C CB  . VAL A 1 58  ? 38.182 8.793   -20.601 1.00 77.12  ? 58  VAL A CB  1 
ATOM   309  C CG1 . VAL A 1 58  ? 36.945 9.688   -20.556 1.00 77.46  ? 58  VAL A CG1 1 
ATOM   310  C CG2 . VAL A 1 58  ? 38.186 7.838   -19.417 1.00 78.63  ? 58  VAL A CG2 1 
ATOM   311  N N   . PRO A 1 59  ? 37.102 9.006   -23.850 1.00 74.45  ? 59  PRO A N   1 
ATOM   312  C CA  . PRO A 1 59  ? 36.929 9.952   -24.950 1.00 69.08  ? 59  PRO A CA  1 
ATOM   313  C C   . PRO A 1 59  ? 36.468 11.326  -24.443 1.00 65.97  ? 59  PRO A C   1 
ATOM   314  O O   . PRO A 1 59  ? 35.589 11.378  -23.611 1.00 58.85  ? 59  PRO A O   1 
ATOM   315  C CB  . PRO A 1 59  ? 35.826 9.288   -25.772 1.00 74.03  ? 59  PRO A CB  1 
ATOM   316  C CG  . PRO A 1 59  ? 34.955 8.623   -24.712 1.00 77.60  ? 59  PRO A CG  1 
ATOM   317  C CD  . PRO A 1 59  ? 35.928 8.138   -23.655 1.00 71.92  ? 59  PRO A CD  1 
ATOM   318  N N   . VAL A 1 60  ? 37.051 12.402  -24.976 1.00 60.00  ? 60  VAL A N   1 
ATOM   319  C CA  . VAL A 1 60  ? 36.792 13.791  -24.513 1.00 52.96  ? 60  VAL A CA  1 
ATOM   320  C C   . VAL A 1 60  ? 36.472 14.658  -25.728 1.00 53.40  ? 60  VAL A C   1 
ATOM   321  O O   . VAL A 1 60  ? 36.625 14.195  -26.855 1.00 50.89  ? 60  VAL A O   1 
ATOM   322  C CB  . VAL A 1 60  ? 37.985 14.345  -23.720 1.00 54.70  ? 60  VAL A CB  1 
ATOM   323  C CG1 . VAL A 1 60  ? 38.174 13.594  -22.413 1.00 58.16  ? 60  VAL A CG1 1 
ATOM   324  C CG2 . VAL A 1 60  ? 39.272 14.328  -24.535 1.00 57.35  ? 60  VAL A CG2 1 
ATOM   325  N N   . ALA A 1 61  ? 35.960 15.850  -25.466 1.00 51.78  ? 61  ALA A N   1 
ATOM   326  C CA  . ALA A 1 61  ? 35.942 16.971  -26.416 1.00 55.53  ? 61  ALA A CA  1 
ATOM   327  C C   . ALA A 1 61  ? 37.115 17.888  -26.053 1.00 54.86  ? 61  ALA A C   1 
ATOM   328  O O   . ALA A 1 61  ? 37.459 18.011  -24.861 1.00 55.20  ? 61  ALA A O   1 
ATOM   329  C CB  . ALA A 1 61  ? 34.601 17.677  -26.391 1.00 51.38  ? 61  ALA A CB  1 
ATOM   330  N N   . LEU A 1 62  ? 37.724 18.487  -27.066 1.00 53.04  ? 62  LEU A N   1 
ATOM   331  C CA  . LEU A 1 62  ? 38.874 19.396  -26.922 1.00 52.62  ? 62  LEU A CA  1 
ATOM   332  C C   . LEU A 1 62  ? 38.496 20.653  -27.680 1.00 52.62  ? 62  LEU A C   1 
ATOM   333  O O   . LEU A 1 62  ? 38.292 20.536  -28.885 1.00 53.48  ? 62  LEU A O   1 
ATOM   334  C CB  . LEU A 1 62  ? 40.100 18.695  -27.502 1.00 63.47  ? 62  LEU A CB  1 
ATOM   335  C CG  . LEU A 1 62  ? 41.410 19.466  -27.426 1.00 72.77  ? 62  LEU A CG  1 
ATOM   336  C CD1 . LEU A 1 62  ? 41.776 19.769  -25.989 1.00 75.46  ? 62  LEU A CD1 1 
ATOM   337  C CD2 . LEU A 1 62  ? 42.515 18.666  -28.086 1.00 80.32  ? 62  LEU A CD2 1 
ATOM   338  N N   . LYS A 1 63  ? 38.264 21.762  -26.975 1.00 50.48  ? 63  LYS A N   1 
ATOM   339  C CA  . LYS A 1 63  ? 37.995 23.076  -27.605 1.00 50.15  ? 63  LYS A CA  1 
ATOM   340  C C   . LYS A 1 63  ? 39.313 23.848  -27.658 1.00 45.62  ? 63  LYS A C   1 
ATOM   341  O O   . LYS A 1 63  ? 39.987 23.944  -26.624 1.00 45.36  ? 63  LYS A O   1 
ATOM   342  C CB  . LYS A 1 63  ? 36.917 23.858  -26.853 1.00 57.39  ? 63  LYS A CB  1 
ATOM   343  C CG  . LYS A 1 63  ? 35.494 23.356  -27.054 1.00 64.05  ? 63  LYS A CG  1 
ATOM   344  C CD  . LYS A 1 63  ? 34.431 24.091  -26.225 1.00 65.76  ? 63  LYS A CD  1 
ATOM   345  C CE  . LYS A 1 63  ? 33.025 23.537  -26.410 0.50 59.42  ? 63  LYS A CE  1 
ATOM   346  N NZ  . LYS A 1 63  ? 32.082 24.022  -25.367 0.50 56.56  ? 63  LYS A NZ  1 
ATOM   347  N N   . LYS A 1 64  ? 39.665 24.349  -28.840 1.00 47.58  ? 64  LYS A N   1 
ATOM   348  C CA  . LYS A 1 64  ? 40.816 25.260  -29.068 1.00 46.61  ? 64  LYS A CA  1 
ATOM   349  C C   . LYS A 1 64  ? 40.249 26.662  -29.307 1.00 43.90  ? 64  LYS A C   1 
ATOM   350  O O   . LYS A 1 64  ? 39.417 26.782  -30.197 1.00 46.47  ? 64  LYS A O   1 
ATOM   351  C CB  . LYS A 1 64  ? 41.644 24.694  -30.220 1.00 51.64  ? 64  LYS A CB  1 
ATOM   352  C CG  . LYS A 1 64  ? 42.267 23.337  -29.920 1.00 54.09  ? 64  LYS A CG  1 
ATOM   353  C CD  . LYS A 1 64  ? 43.256 22.833  -30.963 1.00 58.39  ? 64  LYS A CD  1 
ATOM   354  C CE  . LYS A 1 64  ? 44.308 21.923  -30.352 1.00 59.02  ? 64  LYS A CE  1 
ATOM   355  N NZ  . LYS A 1 64  ? 44.945 21.047  -31.364 1.00 65.73  ? 64  LYS A NZ  1 
ATOM   356  N N   . VAL A 1 65  ? 40.589 27.650  -28.468 1.00 45.55  ? 65  VAL A N   1 
ATOM   357  C CA  . VAL A 1 65  ? 40.060 29.047  -28.550 1.00 45.90  ? 65  VAL A CA  1 
ATOM   358  C C   . VAL A 1 65  ? 41.219 29.970  -28.941 1.00 51.84  ? 65  VAL A C   1 
ATOM   359  O O   . VAL A 1 65  ? 42.316 29.853  -28.320 1.00 48.43  ? 65  VAL A O   1 
ATOM   360  C CB  . VAL A 1 65  ? 39.384 29.493  -27.235 1.00 47.74  ? 65  VAL A CB  1 
ATOM   361  C CG1 . VAL A 1 65  ? 38.638 30.817  -27.383 1.00 45.58  ? 65  VAL A CG1 1 
ATOM   362  C CG2 . VAL A 1 65  ? 38.439 28.432  -26.679 1.00 48.64  ? 65  VAL A CG2 1 
ATOM   363  N N   . GLN A 1 66  ? 40.986 30.837  -29.937 1.00 54.91  ? 66  GLN A N   1 
ATOM   364  C CA  . GLN A 1 66  ? 42.027 31.680  -30.584 1.00 57.86  ? 66  GLN A CA  1 
ATOM   365  C C   . GLN A 1 66  ? 42.064 33.026  -29.860 1.00 56.35  ? 66  GLN A C   1 
ATOM   366  O O   . GLN A 1 66  ? 41.683 34.045  -30.433 1.00 57.94  ? 66  GLN A O   1 
ATOM   367  C CB  . GLN A 1 66  ? 41.739 31.792  -32.080 1.00 66.20  ? 66  GLN A CB  1 
ATOM   368  C CG  . GLN A 1 66  ? 42.157 30.557  -32.876 1.00 74.23  ? 66  GLN A CG  1 
ATOM   369  C CD  . GLN A 1 66  ? 41.029 29.580  -33.099 1.00 89.99  ? 66  GLN A CD  1 
ATOM   370  O OE1 . GLN A 1 66  ? 40.013 29.908  -33.708 1.00 100.73 ? 66  GLN A OE1 1 
ATOM   371  N NE2 . GLN A 1 66  ? 41.206 28.354  -32.627 1.00 96.35  ? 66  GLN A NE2 1 
ATOM   372  N N   . ILE A 1 67  ? 42.489 33.002  -28.604 1.00 58.98  ? 67  ILE A N   1 
ATOM   373  C CA  . ILE A 1 67  ? 42.468 34.176  -27.686 1.00 56.29  ? 67  ILE A CA  1 
ATOM   374  C C   . ILE A 1 67  ? 43.566 35.177  -28.065 1.00 51.96  ? 67  ILE A C   1 
ATOM   375  O O   . ILE A 1 67  ? 43.511 36.303  -27.568 1.00 55.69  ? 67  ILE A O   1 
ATOM   376  C CB  . ILE A 1 67  ? 42.582 33.725  -26.216 1.00 51.42  ? 67  ILE A CB  1 
ATOM   377  C CG1 . ILE A 1 67  ? 43.844 32.908  -25.940 1.00 49.61  ? 67  ILE A CG1 1 
ATOM   378  C CG2 . ILE A 1 67  ? 41.325 32.974  -25.810 1.00 57.96  ? 67  ILE A CG2 1 
ATOM   379  C CD1 . ILE A 1 67  ? 44.309 33.008  -24.507 1.00 53.88  ? 67  ILE A CD1 1 
ATOM   380  N N   . PHE A 1 68  ? 44.537 34.792  -28.889 1.00 54.35  ? 68  PHE A N   1 
ATOM   381  C CA  . PHE A 1 68  ? 45.646 35.690  -29.310 1.00 55.64  ? 68  PHE A CA  1 
ATOM   382  C C   . PHE A 1 68  ? 45.524 36.144  -30.780 1.00 57.67  ? 68  PHE A C   1 
ATOM   383  O O   . PHE A 1 68  ? 46.256 37.076  -31.127 1.00 73.32  ? 68  PHE A O   1 
ATOM   384  C CB  . PHE A 1 68  ? 46.989 35.015  -29.064 1.00 49.71  ? 68  PHE A CB  1 
ATOM   385  C CG  . PHE A 1 68  ? 47.227 34.671  -27.624 1.00 49.65  ? 68  PHE A CG  1 
ATOM   386  C CD1 . PHE A 1 68  ? 47.256 35.662  -26.657 1.00 49.78  ? 68  PHE A CD1 1 
ATOM   387  C CD2 . PHE A 1 68  ? 47.453 33.363  -27.240 1.00 48.66  ? 68  PHE A CD2 1 
ATOM   388  C CE1 . PHE A 1 68  ? 47.476 35.349  -25.331 1.00 46.74  ? 68  PHE A CE1 1 
ATOM   389  C CE2 . PHE A 1 68  ? 47.652 33.050  -25.909 1.00 49.12  ? 68  PHE A CE2 1 
ATOM   390  C CZ  . PHE A 1 68  ? 47.664 34.041  -24.957 1.00 49.94  ? 68  PHE A CZ  1 
ATOM   391  N N   . ASP A 1 69  ? 44.648 35.572  -31.613 1.00 55.05  ? 69  ASP A N   1 
ATOM   392  C CA  . ASP A 1 69  ? 44.595 35.939  -33.056 1.00 60.93  ? 69  ASP A CA  1 
ATOM   393  C C   . ASP A 1 69  ? 43.250 36.599  -33.405 1.00 61.97  ? 69  ASP A C   1 
ATOM   394  O O   . ASP A 1 69  ? 43.298 37.713  -33.944 1.00 64.93  ? 69  ASP A O   1 
ATOM   395  C CB  . ASP A 1 69  ? 45.066 34.777  -33.925 1.00 66.57  ? 69  ASP A CB  1 
ATOM   396  C CG  . ASP A 1 69  ? 46.517 34.387  -33.619 1.00 81.74  ? 69  ASP A CG  1 
ATOM   397  O OD1 . ASP A 1 69  ? 47.195 35.120  -32.845 1.00 72.61  ? 69  ASP A OD1 1 
ATOM   398  O OD2 . ASP A 1 69  ? 46.974 33.343  -34.138 1.00 93.99  ? 69  ASP A OD2 1 
ATOM   399  N N   . LEU A 1 70  ? 42.104 36.053  -33.007 1.00 59.76  ? 70  LEU A N   1 
ATOM   400  C CA  . LEU A 1 70  ? 40.787 36.655  -33.361 1.00 71.42  ? 70  LEU A CA  1 
ATOM   401  C C   . LEU A 1 70  ? 40.265 37.635  -32.283 1.00 75.55  ? 70  LEU A C   1 
ATOM   402  O O   . LEU A 1 70  ? 39.110 38.098  -32.437 1.00 73.87  ? 70  LEU A O   1 
ATOM   403  C CB  . LEU A 1 70  ? 39.807 35.502  -33.611 1.00 80.09  ? 70  LEU A CB  1 
ATOM   404  C CG  . LEU A 1 70  ? 40.203 34.542  -34.737 1.00 84.33  ? 70  LEU A CG  1 
ATOM   405  C CD1 . LEU A 1 70  ? 39.411 33.247  -34.658 1.00 85.73  ? 70  LEU A CD1 1 
ATOM   406  C CD2 . LEU A 1 70  ? 40.016 35.190  -36.103 1.00 84.87  ? 70  LEU A CD2 1 
ATOM   407  N N   . MET A 1 71  ? 41.062 38.007  -31.271 1.00 70.70  ? 71  MET A N   1 
ATOM   408  C CA  . MET A 1 71  ? 40.567 38.719  -30.057 1.00 70.62  ? 71  MET A CA  1 
ATOM   409  C C   . MET A 1 71  ? 41.484 39.878  -29.648 1.00 63.16  ? 71  MET A C   1 
ATOM   410  O O   . MET A 1 71  ? 42.708 39.726  -29.714 1.00 56.54  ? 71  MET A O   1 
ATOM   411  C CB  . MET A 1 71  ? 40.472 37.751  -28.871 1.00 77.08  ? 71  MET A CB  1 
ATOM   412  C CG  . MET A 1 71  ? 39.113 37.096  -28.731 1.00 74.05  ? 71  MET A CG  1 
ATOM   413  S SD  . MET A 1 71  ? 39.128 35.856  -27.429 1.00 66.93  ? 71  MET A SD  1 
ATOM   414  C CE  . MET A 1 71  ? 37.458 35.220  -27.547 1.00 78.10  ? 71  MET A CE  1 
ATOM   415  N N   . ASP A 1 72  ? 40.886 40.966  -29.162 1.00 60.52  ? 72  ASP A N   1 
ATOM   416  C CA  . ASP A 1 72  ? 41.587 42.095  -28.492 1.00 64.43  ? 72  ASP A CA  1 
ATOM   417  C C   . ASP A 1 72  ? 41.747 41.745  -27.005 1.00 61.03  ? 72  ASP A C   1 
ATOM   418  O O   . ASP A 1 72  ? 41.116 40.778  -26.564 1.00 63.49  ? 72  ASP A O   1 
ATOM   419  C CB  . ASP A 1 72  ? 40.833 43.415  -28.691 1.00 70.96  ? 72  ASP A CB  1 
ATOM   420  C CG  . ASP A 1 72  ? 39.337 43.315  -28.434 1.00 84.86  ? 72  ASP A CG  1 
ATOM   421  O OD1 . ASP A 1 72  ? 38.630 42.778  -29.314 1.00 94.28  ? 72  ASP A OD1 1 
ATOM   422  O OD2 . ASP A 1 72  ? 38.891 43.747  -27.349 1.00 88.75  ? 72  ASP A OD2 1 
ATOM   423  N N   . ALA A 1 73  ? 42.548 42.514  -26.268 1.00 56.22  ? 73  ALA A N   1 
ATOM   424  C CA  . ALA A 1 73  ? 42.976 42.222  -24.883 1.00 59.58  ? 73  ALA A CA  1 
ATOM   425  C C   . ALA A 1 73  ? 41.755 42.037  -23.972 1.00 58.67  ? 73  ALA A C   1 
ATOM   426  O O   . ALA A 1 73  ? 41.756 41.108  -23.147 1.00 57.92  ? 73  ALA A O   1 
ATOM   427  C CB  . ALA A 1 73  ? 43.872 43.331  -24.391 1.00 63.73  ? 73  ALA A CB  1 
ATOM   428  N N   . LYS A 1 74  ? 40.763 42.911  -24.109 1.00 56.55  ? 74  LYS A N   1 
ATOM   429  C CA  . LYS A 1 74  ? 39.515 42.941  -23.306 1.00 59.50  ? 74  LYS A CA  1 
ATOM   430  C C   . LYS A 1 74  ? 38.801 41.587  -23.410 1.00 51.93  ? 74  LYS A C   1 
ATOM   431  O O   . LYS A 1 74  ? 38.534 40.969  -22.367 1.00 55.88  ? 74  LYS A O   1 
ATOM   432  C CB  . LYS A 1 74  ? 38.628 44.086  -23.808 1.00 62.02  ? 74  LYS A CB  1 
ATOM   433  C CG  . LYS A 1 74  ? 37.289 44.234  -23.109 1.00 67.10  ? 74  LYS A CG  1 
ATOM   434  C CD  . LYS A 1 74  ? 37.416 44.433  -21.622 1.00 78.49  ? 74  LYS A CD  1 
ATOM   435  C CE  . LYS A 1 74  ? 36.150 45.009  -21.020 1.00 86.39  ? 74  LYS A CE  1 
ATOM   436  N NZ  . LYS A 1 74  ? 34.971 44.153  -21.297 1.00 88.74  ? 74  LYS A NZ  1 
ATOM   437  N N   . ALA A 1 75  ? 38.498 41.176  -24.634 1.00 48.60  ? 75  ALA A N   1 
ATOM   438  C CA  . ALA A 1 75  ? 37.810 39.919  -24.992 1.00 50.62  ? 75  ALA A CA  1 
ATOM   439  C C   . ALA A 1 75  ? 38.632 38.707  -24.529 1.00 48.85  ? 75  ALA A C   1 
ATOM   440  O O   . ALA A 1 75  ? 38.027 37.734  -24.073 1.00 51.54  ? 75  ALA A O   1 
ATOM   441  C CB  . ALA A 1 75  ? 37.571 39.902  -26.484 1.00 52.57  ? 75  ALA A CB  1 
ATOM   442  N N   . ARG A 1 76  ? 39.958 38.763  -24.631 1.00 46.53  ? 76  ARG A N   1 
ATOM   443  C CA  . ARG A 1 76  ? 40.849 37.677  -24.152 1.00 49.61  ? 76  ARG A CA  1 
ATOM   444  C C   . ARG A 1 76  ? 40.656 37.556  -22.636 1.00 51.34  ? 76  ARG A C   1 
ATOM   445  O O   . ARG A 1 76  ? 40.388 36.439  -22.163 1.00 55.63  ? 76  ARG A O   1 
ATOM   446  C CB  . ARG A 1 76  ? 42.307 37.937  -24.542 1.00 45.66  ? 76  ARG A CB  1 
ATOM   447  C CG  . ARG A 1 76  ? 43.313 36.942  -23.970 1.00 50.77  ? 76  ARG A CG  1 
ATOM   448  C CD  . ARG A 1 76  ? 44.755 37.402  -24.094 1.00 53.17  ? 76  ARG A CD  1 
ATOM   449  N NE  . ARG A 1 76  ? 44.865 37.894  -25.453 1.00 66.86  ? 76  ARG A NE  1 
ATOM   450  C CZ  . ARG A 1 76  ? 45.285 39.091  -25.835 1.00 60.33  ? 76  ARG A CZ  1 
ATOM   451  N NH1 . ARG A 1 76  ? 45.782 39.966  -24.976 1.00 51.36  ? 76  ARG A NH1 1 
ATOM   452  N NH2 . ARG A 1 76  ? 45.233 39.372  -27.121 1.00 67.27  ? 76  ARG A NH2 1 
ATOM   453  N N   . ALA A 1 77  ? 40.784 38.663  -21.907 1.00 56.30  ? 77  ALA A N   1 
ATOM   454  C CA  . ALA A 1 77  ? 40.700 38.681  -20.432 1.00 53.42  ? 77  ALA A CA  1 
ATOM   455  C C   . ALA A 1 77  ? 39.290 38.238  -20.033 1.00 49.73  ? 77  ALA A C   1 
ATOM   456  O O   . ALA A 1 77  ? 39.205 37.418  -19.121 1.00 56.17  ? 77  ALA A O   1 
ATOM   457  C CB  . ALA A 1 77  ? 41.082 40.024  -19.862 1.00 50.70  ? 77  ALA A CB  1 
ATOM   458  N N   . ASP A 1 78  ? 38.237 38.699  -20.712 1.00 45.52  ? 78  ASP A N   1 
ATOM   459  C CA  . ASP A 1 78  ? 36.838 38.287  -20.380 1.00 49.86  ? 78  ASP A CA  1 
ATOM   460  C C   . ASP A 1 78  ? 36.659 36.774  -20.602 1.00 51.80  ? 78  ASP A C   1 
ATOM   461  O O   . ASP A 1 78  ? 36.124 36.106  -19.708 1.00 54.07  ? 78  ASP A O   1 
ATOM   462  C CB  . ASP A 1 78  ? 35.785 39.106  -21.136 1.00 50.46  ? 78  ASP A CB  1 
ATOM   463  C CG  . ASP A 1 78  ? 35.684 40.542  -20.640 1.00 57.94  ? 78  ASP A CG  1 
ATOM   464  O OD1 . ASP A 1 78  ? 36.269 40.827  -19.574 1.00 64.21  ? 78  ASP A OD1 1 
ATOM   465  O OD2 . ASP A 1 78  ? 35.043 41.371  -21.333 1.00 60.09  ? 78  ASP A OD2 1 
ATOM   466  N N   . CYS A 1 79  ? 37.133 36.248  -21.732 1.00 54.48  ? 79  CYS A N   1 
ATOM   467  C CA  . CYS A 1 79  ? 37.006 34.827  -22.151 1.00 48.78  ? 79  CYS A CA  1 
ATOM   468  C C   . CYS A 1 79  ? 37.731 33.926  -21.143 1.00 46.17  ? 79  CYS A C   1 
ATOM   469  O O   . CYS A 1 79  ? 37.127 32.971  -20.670 1.00 51.48  ? 79  CYS A O   1 
ATOM   470  C CB  . CYS A 1 79  ? 37.492 34.667  -23.589 1.00 53.98  ? 79  CYS A CB  1 
ATOM   471  S SG  . CYS A 1 79  ? 37.695 32.956  -24.136 1.00 59.27  ? 79  CYS A SG  1 
ATOM   472  N N   . ILE A 1 80  ? 38.944 34.258  -20.737 1.00 47.28  ? 80  ILE A N   1 
ATOM   473  C CA  . ILE A 1 80  ? 39.670 33.528  -19.656 1.00 47.65  ? 80  ILE A CA  1 
ATOM   474  C C   . ILE A 1 80  ? 38.880 33.516  -18.322 1.00 52.46  ? 80  ILE A C   1 
ATOM   475  O O   . ILE A 1 80  ? 38.725 32.415  -17.760 1.00 52.41  ? 80  ILE A O   1 
ATOM   476  C CB  . ILE A 1 80  ? 41.092 34.103  -19.507 1.00 46.23  ? 80  ILE A CB  1 
ATOM   477  C CG1 . ILE A 1 80  ? 41.967 33.621  -20.672 1.00 49.13  ? 80  ILE A CG1 1 
ATOM   478  C CG2 . ILE A 1 80  ? 41.681 33.758  -18.140 1.00 45.23  ? 80  ILE A CG2 1 
ATOM   479  C CD1 . ILE A 1 80  ? 43.414 34.104  -20.673 1.00 50.45  ? 80  ILE A CD1 1 
ATOM   480  N N   . LYS A 1 81  ? 38.439 34.664  -17.790 1.00 55.71  ? 81  LYS A N   1 
ATOM   481  C CA  . LYS A 1 81  ? 37.619 34.762  -16.543 1.00 57.41  ? 81  LYS A CA  1 
ATOM   482  C C   . LYS A 1 81  ? 36.417 33.816  -16.659 1.00 52.54  ? 81  LYS A C   1 
ATOM   483  O O   . LYS A 1 81  ? 36.132 33.068  -15.710 1.00 51.05  ? 81  LYS A O   1 
ATOM   484  C CB  . LYS A 1 81  ? 37.081 36.180  -16.287 1.00 64.08  ? 81  LYS A CB  1 
ATOM   485  C CG  . LYS A 1 81  ? 38.090 37.220  -15.802 1.00 72.31  ? 81  LYS A CG  1 
ATOM   486  C CD  . LYS A 1 81  ? 37.468 38.582  -15.470 1.00 84.23  ? 81  LYS A CD  1 
ATOM   487  C CE  . LYS A 1 81  ? 37.793 39.698  -16.454 1.00 88.90  ? 81  LYS A CE  1 
ATOM   488  N NZ  . LYS A 1 81  ? 39.040 40.417  -16.090 1.00 91.07  ? 81  LYS A NZ  1 
ATOM   489  N N   . GLU A 1 82  ? 35.732 33.850  -17.795 1.00 51.56  ? 82  GLU A N   1 
ATOM   490  C CA  . GLU A 1 82  ? 34.539 33.006  -18.016 1.00 56.81  ? 82  GLU A CA  1 
ATOM   491  C C   . GLU A 1 82  ? 34.926 31.529  -17.986 1.00 50.39  ? 82  GLU A C   1 
ATOM   492  O O   . GLU A 1 82  ? 34.184 30.756  -17.396 1.00 48.10  ? 82  GLU A O   1 
ATOM   493  C CB  . GLU A 1 82  ? 33.823 33.410  -19.295 1.00 55.08  ? 82  GLU A CB  1 
ATOM   494  C CG  . GLU A 1 82  ? 33.163 34.755  -19.114 1.00 68.22  ? 82  GLU A CG  1 
ATOM   495  C CD  . GLU A 1 82  ? 31.956 35.036  -19.978 1.00 77.69  ? 82  GLU A CD  1 
ATOM   496  O OE1 . GLU A 1 82  ? 31.599 34.161  -20.810 1.00 72.85  ? 82  GLU A OE1 1 
ATOM   497  O OE2 . GLU A 1 82  ? 31.387 36.143  -19.810 1.00 78.07  ? 82  GLU A OE2 1 
ATOM   498  N N   . ILE A 1 83  ? 36.018 31.139  -18.620 1.00 49.63  ? 83  ILE A N   1 
ATOM   499  C CA  . ILE A 1 83  ? 36.383 29.697  -18.694 1.00 54.45  ? 83  ILE A CA  1 
ATOM   500  C C   . ILE A 1 83  ? 36.698 29.236  -17.264 1.00 54.14  ? 83  ILE A C   1 
ATOM   501  O O   . ILE A 1 83  ? 36.300 28.124  -16.912 1.00 50.03  ? 83  ILE A O   1 
ATOM   502  C CB  . ILE A 1 83  ? 37.546 29.456  -19.671 1.00 52.51  ? 83  ILE A CB  1 
ATOM   503  C CG1 . ILE A 1 83  ? 37.174 29.831  -21.111 1.00 56.96  ? 83  ILE A CG1 1 
ATOM   504  C CG2 . ILE A 1 83  ? 38.043 28.024  -19.565 1.00 53.88  ? 83  ILE A CG2 1 
ATOM   505  C CD1 . ILE A 1 83  ? 36.044 29.033  -21.711 1.00 59.82  ? 83  ILE A CD1 1 
ATOM   506  N N   . ASP A 1 84  ? 37.340 30.090  -16.465 1.00 56.90  ? 84  ASP A N   1 
ATOM   507  C CA  . ASP A 1 84  ? 37.713 29.790  -15.058 1.00 59.20  ? 84  ASP A CA  1 
ATOM   508  C C   . ASP A 1 84  ? 36.442 29.567  -14.227 1.00 53.52  ? 84  ASP A C   1 
ATOM   509  O O   . ASP A 1 84  ? 36.465 28.676  -13.382 1.00 54.34  ? 84  ASP A O   1 
ATOM   510  C CB  . ASP A 1 84  ? 38.617 30.873  -14.459 1.00 63.12  ? 84  ASP A CB  1 
ATOM   511  C CG  . ASP A 1 84  ? 40.071 30.801  -14.908 1.00 69.55  ? 84  ASP A CG  1 
ATOM   512  O OD1 . ASP A 1 84  ? 40.501 29.718  -15.373 1.00 74.39  ? 84  ASP A OD1 1 
ATOM   513  O OD2 . ASP A 1 84  ? 40.768 31.835  -14.790 1.00 70.92  ? 84  ASP A OD2 1 
ATOM   514  N N   . LEU A 1 85  ? 35.382 30.345  -14.448 1.00 53.13  ? 85  LEU A N   1 
ATOM   515  C CA  . LEU A 1 85  ? 34.065 30.120  -13.791 1.00 50.07  ? 85  LEU A CA  1 
ATOM   516  C C   . LEU A 1 85  ? 33.415 28.839  -14.350 1.00 47.07  ? 85  LEU A C   1 
ATOM   517  O O   . LEU A 1 85  ? 32.878 28.054  -13.555 1.00 44.88  ? 85  LEU A O   1 
ATOM   518  C CB  . LEU A 1 85  ? 33.185 31.365  -13.959 1.00 51.96  ? 85  LEU A CB  1 
ATOM   519  C CG  . LEU A 1 85  ? 33.648 32.598  -13.176 1.00 56.78  ? 85  LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 85  ? 32.622 33.719  -13.264 1.00 61.67  ? 85  LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 85  ? 33.939 32.267  -11.716 1.00 51.61  ? 85  LEU A CD2 1 
ATOM   522  N N   . LEU A 1 86  ? 33.495 28.583  -15.657 1.00 45.36  ? 86  LEU A N   1 
ATOM   523  C CA  . LEU A 1 86  ? 32.800 27.426  -16.280 1.00 46.29  ? 86  LEU A CA  1 
ATOM   524  C C   . LEU A 1 86  ? 33.393 26.121  -15.749 1.00 46.98  ? 86  LEU A C   1 
ATOM   525  O O   . LEU A 1 86  ? 32.613 25.196  -15.490 1.00 51.10  ? 86  LEU A O   1 
ATOM   526  C CB  . LEU A 1 86  ? 32.895 27.473  -17.807 1.00 47.26  ? 86  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 86  ? 31.943 28.441  -18.498 1.00 48.10  ? 86  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 86  ? 32.304 28.559  -19.960 1.00 48.31  ? 86  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 86  ? 30.489 28.017  -18.355 1.00 50.39  ? 86  LEU A CD2 1 
ATOM   530  N N   . LYS A 1 87  ? 34.709 26.043  -15.586 1.00 49.36  ? 87  LYS A N   1 
ATOM   531  C CA  . LYS A 1 87  ? 35.367 24.805  -15.104 1.00 54.04  ? 87  LYS A CA  1 
ATOM   532  C C   . LYS A 1 87  ? 35.007 24.552  -13.636 1.00 51.18  ? 87  LYS A C   1 
ATOM   533  O O   . LYS A 1 87  ? 35.186 23.408  -13.200 1.00 57.97  ? 87  LYS A O   1 
ATOM   534  C CB  . LYS A 1 87  ? 36.876 24.838  -15.360 1.00 61.73  ? 87  LYS A CB  1 
ATOM   535  C CG  . LYS A 1 87  ? 37.663 25.829  -14.528 1.00 69.88  ? 87  LYS A CG  1 
ATOM   536  C CD  . LYS A 1 87  ? 38.990 26.205  -15.170 1.00 79.77  ? 87  LYS A CD  1 
ATOM   537  C CE  . LYS A 1 87  ? 39.917 25.035  -15.421 1.00 74.78  ? 87  LYS A CE  1 
ATOM   538  N NZ  . LYS A 1 87  ? 41.309 25.512  -15.589 1.00 73.36  ? 87  LYS A NZ  1 
ATOM   539  N N   . GLN A 1 88  ? 34.453 25.528  -12.911 1.00 46.04  ? 88  GLN A N   1 
ATOM   540  C CA  . GLN A 1 88  ? 33.940 25.263  -11.539 1.00 48.41  ? 88  GLN A CA  1 
ATOM   541  C C   . GLN A 1 88  ? 32.559 24.568  -11.562 1.00 49.40  ? 88  GLN A C   1 
ATOM   542  O O   . GLN A 1 88  ? 32.208 23.948  -10.544 1.00 50.67  ? 88  GLN A O   1 
ATOM   543  C CB  . GLN A 1 88  ? 33.909 26.558  -10.737 1.00 46.23  ? 88  GLN A CB  1 
ATOM   544  C CG  . GLN A 1 88  ? 35.289 27.171  -10.587 1.00 46.27  ? 88  GLN A CG  1 
ATOM   545  C CD  . GLN A 1 88  ? 35.256 28.328  -9.627  1.00 46.82  ? 88  GLN A CD  1 
ATOM   546  O OE1 . GLN A 1 88  ? 34.271 28.544  -8.909  1.00 45.53  ? 88  GLN A OE1 1 
ATOM   547  N NE2 . GLN A 1 88  ? 36.353 29.066  -9.599  1.00 49.06  ? 88  GLN A NE2 1 
ATOM   548  N N   . LEU A 1 89  ? 31.794 24.636  -12.657 1.00 44.13  ? 89  LEU A N   1 
ATOM   549  C CA  . LEU A 1 89  ? 30.424 24.076  -12.678 1.00 44.84  ? 89  LEU A CA  1 
ATOM   550  C C   . LEU A 1 89  ? 30.559 22.581  -12.434 1.00 45.45  ? 89  LEU A C   1 
ATOM   551  O O   . LEU A 1 89  ? 31.539 22.011  -12.919 1.00 53.26  ? 89  LEU A O   1 
ATOM   552  C CB  . LEU A 1 89  ? 29.715 24.377  -14.001 1.00 43.25  ? 89  LEU A CB  1 
ATOM   553  C CG  . LEU A 1 89  ? 29.456 25.857  -14.289 1.00 47.55  ? 89  LEU A CG  1 
ATOM   554  C CD1 . LEU A 1 89  ? 28.789 26.043  -15.645 1.00 45.53  ? 89  LEU A CD1 1 
ATOM   555  C CD2 . LEU A 1 89  ? 28.619 26.499  -13.194 1.00 45.13  ? 89  LEU A CD2 1 
ATOM   556  N N   . ASN A 1 90  ? 29.636 21.987  -11.679 1.00 42.04  ? 90  ASN A N   1 
ATOM   557  C CA  . ASN A 1 90  ? 29.654 20.527  -11.404 1.00 41.53  ? 90  ASN A CA  1 
ATOM   558  C C   . ASN A 1 90  ? 28.224 20.093  -11.137 1.00 39.89  ? 90  ASN A C   1 
ATOM   559  O O   . ASN A 1 90  ? 27.730 20.330  -10.024 1.00 43.13  ? 90  ASN A O   1 
ATOM   560  C CB  . ASN A 1 90  ? 30.593 20.164  -10.252 1.00 46.06  ? 90  ASN A CB  1 
ATOM   561  C CG  . ASN A 1 90  ? 30.932 18.687  -10.215 1.00 49.51  ? 90  ASN A CG  1 
ATOM   562  O OD1 . ASN A 1 90  ? 30.169 17.841  -10.682 1.00 49.54  ? 90  ASN A OD1 1 
ATOM   563  N ND2 . ASN A 1 90  ? 32.079 18.364  -9.646  1.00 55.36  ? 90  ASN A ND2 1 
ATOM   564  N N   . HIS A 1 91  ? 27.591 19.529  -12.161 1.00 37.07  ? 91  HIS A N   1 
ATOM   565  C CA  . HIS A 1 91  ? 26.179 19.108  -12.133 1.00 37.42  ? 91  HIS A CA  1 
ATOM   566  C C   . HIS A 1 91  ? 26.037 17.994  -13.140 1.00 36.31  ? 91  HIS A C   1 
ATOM   567  O O   . HIS A 1 91  ? 26.549 18.144  -14.233 1.00 35.08  ? 91  HIS A O   1 
ATOM   568  C CB  . HIS A 1 91  ? 25.270 20.278  -12.511 1.00 39.05  ? 91  HIS A CB  1 
ATOM   569  C CG  . HIS A 1 91  ? 23.828 20.039  -12.246 1.00 34.29  ? 91  HIS A CG  1 
ATOM   570  N ND1 . HIS A 1 91  ? 23.033 19.336  -13.105 1.00 39.36  ? 91  HIS A ND1 1 
ATOM   571  C CD2 . HIS A 1 91  ? 23.042 20.419  -11.222 1.00 38.99  ? 91  HIS A CD2 1 
ATOM   572  C CE1 . HIS A 1 91  ? 21.800 19.288  -12.629 1.00 41.03  ? 91  HIS A CE1 1 
ATOM   573  N NE2 . HIS A 1 91  ? 21.779 19.955  -11.464 1.00 38.81  ? 91  HIS A NE2 1 
ATOM   574  N N   . PRO A 1 92  ? 25.314 16.900  -12.830 1.00 37.60  ? 92  PRO A N   1 
ATOM   575  C CA  . PRO A 1 92  ? 25.154 15.791  -13.778 1.00 38.91  ? 92  PRO A CA  1 
ATOM   576  C C   . PRO A 1 92  ? 24.580 16.177  -15.153 1.00 37.89  ? 92  PRO A C   1 
ATOM   577  O O   . PRO A 1 92  ? 24.763 15.413  -16.077 1.00 42.12  ? 92  PRO A O   1 
ATOM   578  C CB  . PRO A 1 92  ? 24.165 14.811  -13.116 1.00 38.97  ? 92  PRO A CB  1 
ATOM   579  C CG  . PRO A 1 92  ? 24.044 15.288  -11.663 1.00 43.18  ? 92  PRO A CG  1 
ATOM   580  C CD  . PRO A 1 92  ? 24.574 16.707  -11.577 1.00 38.00  ? 92  PRO A CD  1 
ATOM   581  N N   . ASN A 1 93  ? 23.881 17.313  -15.265 1.00 40.29  ? 93  ASN A N   1 
ATOM   582  C CA  . ASN A 1 93  ? 23.169 17.714  -16.511 1.00 40.13  ? 93  ASN A CA  1 
ATOM   583  C C   . ASN A 1 93  ? 23.929 18.834  -17.229 1.00 39.26  ? 93  ASN A C   1 
ATOM   584  O O   . ASN A 1 93  ? 23.422 19.342  -18.241 1.00 37.87  ? 93  ASN A O   1 
ATOM   585  C CB  . ASN A 1 93  ? 21.727 18.119  -16.206 1.00 43.55  ? 93  ASN A CB  1 
ATOM   586  C CG  . ASN A 1 93  ? 20.920 16.981  -15.609 1.00 42.40  ? 93  ASN A CG  1 
ATOM   587  O OD1 . ASN A 1 93  ? 20.296 17.133  -14.567 1.00 38.41  ? 93  ASN A OD1 1 
ATOM   588  N ND2 . ASN A 1 93  ? 20.927 15.840  -16.266 1.00 40.78  ? 93  ASN A ND2 1 
ATOM   589  N N   . VAL A 1 94  ? 25.091 19.232  -16.725 1.00 38.77  ? 94  VAL A N   1 
ATOM   590  C CA  . VAL A 1 94  ? 25.930 20.290  -17.359 1.00 39.12  ? 94  VAL A CA  1 
ATOM   591  C C   . VAL A 1 94  ? 27.223 19.638  -17.836 1.00 38.84  ? 94  VAL A C   1 
ATOM   592  O O   . VAL A 1 94  ? 27.863 18.930  -17.004 1.00 37.02  ? 94  VAL A O   1 
ATOM   593  C CB  . VAL A 1 94  ? 26.241 21.429  -16.385 1.00 39.44  ? 94  VAL A CB  1 
ATOM   594  C CG1 . VAL A 1 94  ? 27.244 22.390  -16.991 1.00 40.66  ? 94  VAL A CG1 1 
ATOM   595  C CG2 . VAL A 1 94  ? 24.982 22.148  -15.940 1.00 42.03  ? 94  VAL A CG2 1 
ATOM   596  N N   . ILE A 1 95  ? 27.591 19.859  -19.104 1.00 36.83  ? 95  ILE A N   1 
ATOM   597  C CA  . ILE A 1 95  ? 28.840 19.290  -19.671 1.00 38.66  ? 95  ILE A CA  1 
ATOM   598  C C   . ILE A 1 95  ? 29.947 19.740  -18.731 1.00 40.97  ? 95  ILE A C   1 
ATOM   599  O O   . ILE A 1 95  ? 29.990 20.925  -18.419 1.00 44.67  ? 95  ILE A O   1 
ATOM   600  C CB  . ILE A 1 95  ? 29.068 19.719  -21.131 1.00 41.54  ? 95  ILE A CB  1 
ATOM   601  C CG1 . ILE A 1 95  ? 28.229 18.882  -22.106 1.00 45.69  ? 95  ILE A CG1 1 
ATOM   602  C CG2 . ILE A 1 95  ? 30.542 19.666  -21.479 1.00 43.85  ? 95  ILE A CG2 1 
ATOM   603  C CD1 . ILE A 1 95  ? 28.475 17.370  -22.061 1.00 46.09  ? 95  ILE A CD1 1 
ATOM   604  N N   . LYS A 1 96  ? 30.737 18.809  -18.207 1.00 43.43  ? 96  LYS A N   1 
ATOM   605  C CA  . LYS A 1 96  ? 31.825 19.169  -17.274 1.00 45.27  ? 96  LYS A CA  1 
ATOM   606  C C   . LYS A 1 96  ? 33.029 19.668  -18.067 1.00 42.81  ? 96  LYS A C   1 
ATOM   607  O O   . LYS A 1 96  ? 33.382 19.027  -19.051 1.00 48.13  ? 96  LYS A O   1 
ATOM   608  C CB  . LYS A 1 96  ? 32.227 17.981  -16.399 1.00 49.33  ? 96  LYS A CB  1 
ATOM   609  C CG  . LYS A 1 96  ? 33.167 18.343  -15.254 1.00 48.94  ? 96  LYS A CG  1 
ATOM   610  C CD  . LYS A 1 96  ? 32.476 18.868  -14.025 1.00 50.80  ? 96  LYS A CD  1 
ATOM   611  C CE  . LYS A 1 96  ? 33.442 19.182  -12.895 1.00 56.13  ? 96  LYS A CE  1 
ATOM   612  N NZ  . LYS A 1 96  ? 34.215 20.434  -13.131 1.00 56.83  ? 96  LYS A NZ  1 
ATOM   613  N N   . TYR A 1 97  ? 33.654 20.744  -17.595 1.00 43.53  ? 97  TYR A N   1 
ATOM   614  C CA  . TYR A 1 97  ? 34.971 21.251  -18.051 1.00 44.34  ? 97  TYR A CA  1 
ATOM   615  C C   . TYR A 1 97  ? 36.044 20.636  -17.155 1.00 44.16  ? 97  TYR A C   1 
ATOM   616  O O   . TYR A 1 97  ? 36.096 21.031  -15.987 1.00 55.35  ? 97  TYR A O   1 
ATOM   617  C CB  . TYR A 1 97  ? 35.011 22.776  -17.963 1.00 44.28  ? 97  TYR A CB  1 
ATOM   618  C CG  . TYR A 1 97  ? 34.269 23.502  -19.057 1.00 52.23  ? 97  TYR A CG  1 
ATOM   619  C CD1 . TYR A 1 97  ? 32.975 23.155  -19.408 1.00 59.98  ? 97  TYR A CD1 1 
ATOM   620  C CD2 . TYR A 1 97  ? 34.844 24.577  -19.716 1.00 57.10  ? 97  TYR A CD2 1 
ATOM   621  C CE1 . TYR A 1 97  ? 32.283 23.831  -20.403 1.00 66.25  ? 97  TYR A CE1 1 
ATOM   622  C CE2 . TYR A 1 97  ? 34.174 25.255  -20.724 1.00 60.71  ? 97  TYR A CE2 1 
ATOM   623  C CZ  . TYR A 1 97  ? 32.887 24.882  -21.068 1.00 63.41  ? 97  TYR A CZ  1 
ATOM   624  O OH  . TYR A 1 97  ? 32.218 25.541  -22.056 1.00 64.94  ? 97  TYR A OH  1 
ATOM   625  N N   . TYR A 1 98  ? 36.877 19.744  -17.692 1.00 40.32  ? 98  TYR A N   1 
ATOM   626  C CA  . TYR A 1 98  ? 37.927 19.002  -16.948 1.00 42.61  ? 98  TYR A CA  1 
ATOM   627  C C   . TYR A 1 98  ? 39.185 19.856  -16.746 1.00 48.08  ? 98  TYR A C   1 
ATOM   628  O O   . TYR A 1 98  ? 39.875 19.668  -15.729 1.00 50.00  ? 98  TYR A O   1 
ATOM   629  C CB  . TYR A 1 98  ? 38.323 17.713  -17.675 1.00 42.33  ? 98  TYR A CB  1 
ATOM   630  C CG  . TYR A 1 98  ? 37.212 16.714  -17.897 1.00 44.64  ? 98  TYR A CG  1 
ATOM   631  C CD1 . TYR A 1 98  ? 36.251 16.448  -16.932 1.00 44.76  ? 98  TYR A CD1 1 
ATOM   632  C CD2 . TYR A 1 98  ? 37.125 16.007  -19.086 1.00 48.72  ? 98  TYR A CD2 1 
ATOM   633  C CE1 . TYR A 1 98  ? 35.255 15.505  -17.142 1.00 42.45  ? 98  TYR A CE1 1 
ATOM   634  C CE2 . TYR A 1 98  ? 36.125 15.075  -19.319 1.00 44.55  ? 98  TYR A CE2 1 
ATOM   635  C CZ  . TYR A 1 98  ? 35.192 14.812  -18.337 1.00 43.66  ? 98  TYR A CZ  1 
ATOM   636  O OH  . TYR A 1 98  ? 34.201 13.906  -18.584 1.00 43.90  ? 98  TYR A OH  1 
ATOM   637  N N   . ALA A 1 99  ? 39.542 20.718  -17.701 1.00 47.95  ? 99  ALA A N   1 
ATOM   638  C CA  . ALA A 1 99  ? 40.859 21.384  -17.686 1.00 44.90  ? 99  ALA A CA  1 
ATOM   639  C C   . ALA A 1 99  ? 40.910 22.501  -18.721 1.00 48.00  ? 99  ALA A C   1 
ATOM   640  O O   . ALA A 1 99  ? 40.249 22.374  -19.764 1.00 38.96  ? 99  ALA A O   1 
ATOM   641  C CB  . ALA A 1 99  ? 41.926 20.372  -17.968 1.00 43.62  ? 99  ALA A CB  1 
ATOM   642  N N   . SER A 1 100 ? 41.732 23.520  -18.460 1.00 45.68  ? 100 SER A N   1 
ATOM   643  C CA  . SER A 1 100 ? 42.026 24.599  -19.438 1.00 47.18  ? 100 SER A CA  1 
ATOM   644  C C   . SER A 1 100 ? 43.496 25.009  -19.302 1.00 49.54  ? 100 SER A C   1 
ATOM   645  O O   . SER A 1 100 ? 43.978 25.171  -18.178 1.00 54.75  ? 100 SER A O   1 
ATOM   646  C CB  . SER A 1 100 ? 41.080 25.753  -19.262 1.00 47.79  ? 100 SER A CB  1 
ATOM   647  O OG  . SER A 1 100 ? 41.565 26.649  -18.285 1.00 51.16  ? 100 SER A OG  1 
ATOM   648  N N   . PHE A 1 101 ? 44.224 25.103  -20.401 1.00 46.12  ? 101 PHE A N   1 
ATOM   649  C CA  . PHE A 1 101 ? 45.649 25.511  -20.358 1.00 49.15  ? 101 PHE A CA  1 
ATOM   650  C C   . PHE A 1 101 ? 45.971 26.225  -21.668 1.00 51.81  ? 101 PHE A C   1 
ATOM   651  O O   . PHE A 1 101 ? 45.266 26.010  -22.702 1.00 48.55  ? 101 PHE A O   1 
ATOM   652  C CB  . PHE A 1 101 ? 46.555 24.298  -20.111 1.00 51.16  ? 101 PHE A CB  1 
ATOM   653  C CG  . PHE A 1 101 ? 46.290 23.131  -21.033 1.00 50.63  ? 101 PHE A CG  1 
ATOM   654  C CD1 . PHE A 1 101 ? 45.263 22.237  -20.775 1.00 53.14  ? 101 PHE A CD1 1 
ATOM   655  C CD2 . PHE A 1 101 ? 47.016 22.965  -22.196 1.00 54.48  ? 101 PHE A CD2 1 
ATOM   656  C CE1 . PHE A 1 101 ? 45.001 21.174  -21.628 1.00 51.08  ? 101 PHE A CE1 1 
ATOM   657  C CE2 . PHE A 1 101 ? 46.736 21.919  -23.066 1.00 55.90  ? 101 PHE A CE2 1 
ATOM   658  C CZ  . PHE A 1 101 ? 45.731 21.026  -22.778 1.00 53.93  ? 101 PHE A CZ  1 
ATOM   659  N N   . ILE A 1 102 ? 47.007 27.055  -21.631 1.00 50.67  ? 102 ILE A N   1 
ATOM   660  C CA  . ILE A 1 102 ? 47.542 27.718  -22.848 1.00 50.41  ? 102 ILE A CA  1 
ATOM   661  C C   . ILE A 1 102 ? 48.701 26.876  -23.370 1.00 50.65  ? 102 ILE A C   1 
ATOM   662  O O   . ILE A 1 102 ? 49.591 26.550  -22.592 1.00 57.97  ? 102 ILE A O   1 
ATOM   663  C CB  . ILE A 1 102 ? 47.910 29.180  -22.543 1.00 54.68  ? 102 ILE A CB  1 
ATOM   664  C CG1 . ILE A 1 102 ? 46.619 29.994  -22.404 1.00 52.59  ? 102 ILE A CG1 1 
ATOM   665  C CG2 . ILE A 1 102 ? 48.843 29.736  -23.619 1.00 53.02  ? 102 ILE A CG2 1 
ATOM   666  C CD1 . ILE A 1 102 ? 46.722 31.196  -21.523 1.00 52.77  ? 102 ILE A CD1 1 
ATOM   667  N N   . GLU A 1 103 ? 48.636 26.491  -24.637 1.00 51.83  ? 103 GLU A N   1 
ATOM   668  C CA  . GLU A 1 103 ? 49.662 25.663  -25.307 1.00 56.58  ? 103 GLU A CA  1 
ATOM   669  C C   . GLU A 1 103 ? 49.432 25.830  -26.811 1.00 55.88  ? 103 GLU A C   1 
ATOM   670  O O   . GLU A 1 103 ? 48.273 26.073  -27.183 1.00 47.99  ? 103 GLU A O   1 
ATOM   671  C CB  . GLU A 1 103 ? 49.586 24.220  -24.803 1.00 62.40  ? 103 GLU A CB  1 
ATOM   672  C CG  . GLU A 1 103 ? 50.622 23.296  -25.435 1.00 65.71  ? 103 GLU A CG  1 
ATOM   673  C CD  . GLU A 1 103 ? 50.586 21.857  -24.952 1.00 66.45  ? 103 GLU A CD  1 
ATOM   674  O OE1 . GLU A 1 103 ? 50.057 21.600  -23.845 1.00 61.42  ? 103 GLU A OE1 1 
ATOM   675  O OE2 . GLU A 1 103 ? 51.097 20.999  -25.685 1.00 74.23  ? 103 GLU A OE2 1 
ATOM   676  N N   . ASP A 1 104 ? 50.510 25.818  -27.607 1.00 61.47  ? 104 ASP A N   1 
ATOM   677  C CA  . ASP A 1 104 ? 50.523 26.202  -29.050 1.00 60.18  ? 104 ASP A CA  1 
ATOM   678  C C   . ASP A 1 104 ? 49.754 27.509  -29.249 1.00 53.67  ? 104 ASP A C   1 
ATOM   679  O O   . ASP A 1 104 ? 49.065 27.637  -30.257 1.00 48.62  ? 104 ASP A O   1 
ATOM   680  C CB  . ASP A 1 104 ? 49.920 25.123  -29.959 1.00 66.70  ? 104 ASP A CB  1 
ATOM   681  C CG  . ASP A 1 104 ? 50.569 23.749  -29.845 1.00 75.32  ? 104 ASP A CG  1 
ATOM   682  O OD1 . ASP A 1 104 ? 51.639 23.640  -29.156 1.00 66.62  ? 104 ASP A OD1 1 
ATOM   683  O OD2 . ASP A 1 104 ? 49.993 22.793  -30.438 1.00 70.46  ? 104 ASP A OD2 1 
ATOM   684  N N   . ASN A 1 105 ? 49.844 28.454  -28.315 1.00 54.89  ? 105 ASN A N   1 
ATOM   685  C CA  . ASN A 1 105 ? 49.268 29.805  -28.537 1.00 58.41  ? 105 ASN A CA  1 
ATOM   686  C C   . ASN A 1 105 ? 47.747 29.767  -28.696 1.00 55.82  ? 105 ASN A C   1 
ATOM   687  O O   . ASN A 1 105 ? 47.201 30.665  -29.356 1.00 53.75  ? 105 ASN A O   1 
ATOM   688  C CB  . ASN A 1 105 ? 49.878 30.450  -29.779 1.00 62.30  ? 105 ASN A CB  1 
ATOM   689  C CG  . ASN A 1 105 ? 50.990 31.382  -29.386 1.00 69.23  ? 105 ASN A CG  1 
ATOM   690  O OD1 . ASN A 1 105 ? 52.049 30.921  -28.943 1.00 60.71  ? 105 ASN A OD1 1 
ATOM   691  N ND2 . ASN A 1 105 ? 50.717 32.677  -29.504 1.00 74.77  ? 105 ASN A ND2 1 
ATOM   692  N N   . GLU A 1 106 ? 47.081 28.780  -28.108 1.00 54.25  ? 106 GLU A N   1 
ATOM   693  C CA  . GLU A 1 106 ? 45.608 28.783  -27.993 1.00 56.85  ? 106 GLU A CA  1 
ATOM   694  C C   . GLU A 1 106 ? 45.258 28.512  -26.528 1.00 51.49  ? 106 GLU A C   1 
ATOM   695  O O   . GLU A 1 106 ? 46.108 27.939  -25.806 1.00 46.80  ? 106 GLU A O   1 
ATOM   696  C CB  . GLU A 1 106 ? 45.000 27.740  -28.937 1.00 68.48  ? 106 GLU A CB  1 
ATOM   697  C CG  . GLU A 1 106 ? 45.433 27.889  -30.387 1.00 75.50  ? 106 GLU A CG  1 
ATOM   698  C CD  . GLU A 1 106 ? 44.893 26.829  -31.338 1.00 76.81  ? 106 GLU A CD  1 
ATOM   699  O OE1 . GLU A 1 106 ? 44.231 27.214  -32.326 1.00 75.41  ? 106 GLU A OE1 1 
ATOM   700  O OE2 . GLU A 1 106 ? 45.160 25.624  -31.104 1.00 75.76  ? 106 GLU A OE2 1 
ATOM   701  N N   . LEU A 1 107 ? 44.058 28.916  -26.116 1.00 46.32  ? 107 LEU A N   1 
ATOM   702  C CA  . LEU A 1 107 ? 43.420 28.413  -24.882 1.00 46.18  ? 107 LEU A CA  1 
ATOM   703  C C   . LEU A 1 107 ? 42.761 27.078  -25.232 1.00 43.28  ? 107 LEU A C   1 
ATOM   704  O O   . LEU A 1 107 ? 41.820 27.091  -26.025 1.00 42.53  ? 107 LEU A O   1 
ATOM   705  C CB  . LEU A 1 107 ? 42.406 29.427  -24.347 1.00 46.94  ? 107 LEU A CB  1 
ATOM   706  C CG  . LEU A 1 107 ? 41.772 29.039  -23.010 1.00 49.97  ? 107 LEU A CG  1 
ATOM   707  C CD1 . LEU A 1 107 ? 42.836 28.882  -21.932 1.00 49.96  ? 107 LEU A CD1 1 
ATOM   708  C CD2 . LEU A 1 107 ? 40.736 30.067  -22.578 1.00 52.37  ? 107 LEU A CD2 1 
ATOM   709  N N   . ASN A 1 108 ? 43.283 25.977  -24.678 1.00 43.01  ? 108 ASN A N   1 
ATOM   710  C CA  . ASN A 1 108 ? 42.777 24.590  -24.857 1.00 41.69  ? 108 ASN A CA  1 
ATOM   711  C C   . ASN A 1 108 ? 41.919 24.191  -23.651 1.00 41.13  ? 108 ASN A C   1 
ATOM   712  O O   . ASN A 1 108 ? 42.356 24.398  -22.531 1.00 44.32  ? 108 ASN A O   1 
ATOM   713  C CB  . ASN A 1 108 ? 43.941 23.612  -24.987 1.00 45.71  ? 108 ASN A CB  1 
ATOM   714  C CG  . ASN A 1 108 ? 44.864 23.966  -26.134 1.00 45.29  ? 108 ASN A CG  1 
ATOM   715  O OD1 . ASN A 1 108 ? 44.588 23.636  -27.280 1.00 48.44  ? 108 ASN A OD1 1 
ATOM   716  N ND2 . ASN A 1 108 ? 45.962 24.629  -25.833 1.00 44.62  ? 108 ASN A ND2 1 
ATOM   717  N N   . ILE A 1 109 ? 40.729 23.653  -23.893 1.00 45.24  ? 109 ILE A N   1 
ATOM   718  C CA  . ILE A 1 109 ? 39.740 23.221  -22.860 1.00 47.30  ? 109 ILE A CA  1 
ATOM   719  C C   . ILE A 1 109 ? 39.425 21.751  -23.107 1.00 42.81  ? 109 ILE A C   1 
ATOM   720  O O   . ILE A 1 109 ? 39.100 21.412  -24.247 1.00 42.71  ? 109 ILE A O   1 
ATOM   721  C CB  . ILE A 1 109 ? 38.447 24.060  -22.929 1.00 49.74  ? 109 ILE A CB  1 
ATOM   722  C CG1 . ILE A 1 109 ? 38.737 25.557  -22.816 1.00 51.47  ? 109 ILE A CG1 1 
ATOM   723  C CG2 . ILE A 1 109 ? 37.448 23.600  -21.874 1.00 48.32  ? 109 ILE A CG2 1 
ATOM   724  C CD1 . ILE A 1 109 ? 37.611 26.420  -23.325 1.00 53.26  ? 109 ILE A CD1 1 
ATOM   725  N N   . VAL A 1 110 ? 39.518 20.924  -22.077 1.00 44.34  ? 110 VAL A N   1 
ATOM   726  C CA  . VAL A 1 110 ? 39.171 19.477  -22.146 1.00 44.85  ? 110 VAL A CA  1 
ATOM   727  C C   . VAL A 1 110 ? 37.826 19.318  -21.439 1.00 46.12  ? 110 VAL A C   1 
ATOM   728  O O   . VAL A 1 110 ? 37.731 19.752  -20.276 1.00 47.76  ? 110 VAL A O   1 
ATOM   729  C CB  . VAL A 1 110 ? 40.289 18.631  -21.523 1.00 44.54  ? 110 VAL A CB  1 
ATOM   730  C CG1 . VAL A 1 110 ? 40.086 17.151  -21.793 1.00 44.30  ? 110 VAL A CG1 1 
ATOM   731  C CG2 . VAL A 1 110 ? 41.653 19.090  -22.019 1.00 46.10  ? 110 VAL A CG2 1 
ATOM   732  N N   . LEU A 1 111 ? 36.820 18.831  -22.168 1.00 46.09  ? 111 LEU A N   1 
ATOM   733  C CA  . LEU A 1 111 ? 35.394 18.771  -21.751 1.00 50.53  ? 111 LEU A CA  1 
ATOM   734  C C   . LEU A 1 111 ? 34.870 17.339  -21.820 1.00 50.10  ? 111 LEU A C   1 
ATOM   735  O O   . LEU A 1 111 ? 35.383 16.538  -22.635 1.00 46.82  ? 111 LEU A O   1 
ATOM   736  C CB  . LEU A 1 111 ? 34.519 19.580  -22.709 1.00 57.76  ? 111 LEU A CB  1 
ATOM   737  C CG  . LEU A 1 111 ? 34.889 21.040  -22.903 1.00 61.74  ? 111 LEU A CG  1 
ATOM   738  C CD1 . LEU A 1 111 ? 35.828 21.180  -24.086 1.00 65.99  ? 111 LEU A CD1 1 
ATOM   739  C CD2 . LEU A 1 111 ? 33.638 21.867  -23.121 1.00 65.08  ? 111 LEU A CD2 1 
ATOM   740  N N   . GLU A 1 112 ? 33.800 17.093  -21.064 1.00 49.13  ? 112 GLU A N   1 
ATOM   741  C CA  . GLU A 1 112 ? 32.962 15.881  -21.147 1.00 50.44  ? 112 GLU A CA  1 
ATOM   742  C C   . GLU A 1 112 ? 32.426 15.808  -22.582 1.00 48.54  ? 112 GLU A C   1 
ATOM   743  O O   . GLU A 1 112 ? 31.907 16.813  -23.106 1.00 44.65  ? 112 GLU A O   1 
ATOM   744  C CB  . GLU A 1 112 ? 31.874 15.966  -20.073 1.00 53.80  ? 112 GLU A CB  1 
ATOM   745  C CG  . GLU A 1 112 ? 31.026 14.714  -19.894 1.00 52.35  ? 112 GLU A CG  1 
ATOM   746  C CD  . GLU A 1 112 ? 29.853 14.908  -18.932 1.00 53.99  ? 112 GLU A CD  1 
ATOM   747  O OE1 . GLU A 1 112 ? 29.055 13.972  -18.779 1.00 57.72  ? 112 GLU A OE1 1 
ATOM   748  O OE2 . GLU A 1 112 ? 29.710 16.017  -18.371 1.00 52.00  ? 112 GLU A OE2 1 
ATOM   749  N N   . LEU A 1 113 ? 32.602 14.664  -23.222 1.00 50.95  ? 113 LEU A N   1 
ATOM   750  C CA  . LEU A 1 113 ? 32.001 14.395  -24.543 1.00 54.37  ? 113 LEU A CA  1 
ATOM   751  C C   . LEU A 1 113 ? 30.615 13.797  -24.299 1.00 54.14  ? 113 LEU A C   1 
ATOM   752  O O   . LEU A 1 113 ? 30.517 12.925  -23.446 1.00 60.05  ? 113 LEU A O   1 
ATOM   753  C CB  . LEU A 1 113 ? 32.930 13.444  -25.301 1.00 54.59  ? 113 LEU A CB  1 
ATOM   754  C CG  . LEU A 1 113 ? 32.569 13.237  -26.769 1.00 57.91  ? 113 LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 113 ? 32.853 14.496  -27.562 1.00 56.52  ? 113 LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 113 ? 33.308 12.038  -27.346 1.00 57.14  ? 113 LEU A CD2 1 
ATOM   757  N N   . ALA A 1 114 ? 29.589 14.275  -24.999 1.00 65.92  ? 114 ALA A N   1 
ATOM   758  C CA  . ALA A 1 114 ? 28.250 13.641  -25.065 1.00 84.46  ? 114 ALA A CA  1 
ATOM   759  C C   . ALA A 1 114 ? 27.978 13.203  -26.512 1.00 92.72  ? 114 ALA A C   1 
ATOM   760  O O   . ALA A 1 114 ? 27.329 13.967  -27.258 1.00 104.08 ? 114 ALA A O   1 
ATOM   761  C CB  . ALA A 1 114 ? 27.210 14.611  -24.560 1.00 85.08  ? 114 ALA A CB  1 
ATOM   762  N N   . ASP A 1 115 ? 28.476 12.035  -26.923 1.00 97.16  ? 115 ASP A N   1 
ATOM   763  C CA  . ASP A 1 115 ? 28.603 11.739  -28.375 1.00 101.23 ? 115 ASP A CA  1 
ATOM   764  C C   . ASP A 1 115 ? 27.348 11.034  -28.901 1.00 93.40  ? 115 ASP A C   1 
ATOM   765  O O   . ASP A 1 115 ? 27.292 10.822  -30.125 1.00 90.40  ? 115 ASP A O   1 
ATOM   766  C CB  . ASP A 1 115 ? 29.872 10.949  -28.710 1.00 108.43 ? 115 ASP A CB  1 
ATOM   767  C CG  . ASP A 1 115 ? 30.491 11.393  -30.030 1.00 117.50 ? 115 ASP A CG  1 
ATOM   768  O OD1 . ASP A 1 115 ? 31.379 10.678  -30.547 1.00 112.55 ? 115 ASP A OD1 1 
ATOM   769  O OD2 . ASP A 1 115 ? 30.079 12.463  -30.537 1.00 123.28 ? 115 ASP A OD2 1 
ATOM   770  N N   . ALA A 1 116 ? 26.378 10.696  -28.045 1.00 74.31  ? 116 ALA A N   1 
ATOM   771  C CA  . ALA A 1 116 ? 25.143 10.000  -28.472 1.00 67.77  ? 116 ALA A CA  1 
ATOM   772  C C   . ALA A 1 116 ? 24.266 11.020  -29.201 1.00 66.96  ? 116 ALA A C   1 
ATOM   773  O O   . ALA A 1 116 ? 24.792 11.679  -30.108 1.00 84.14  ? 116 ALA A O   1 
ATOM   774  C CB  . ALA A 1 116 ? 24.462 9.338   -27.302 1.00 63.54  ? 116 ALA A CB  1 
ATOM   775  N N   . GLY A 1 117 ? 23.008 11.192  -28.804 1.00 58.72  ? 117 GLY A N   1 
ATOM   776  C CA  . GLY A 1 117 ? 22.068 12.094  -29.490 1.00 54.66  ? 117 GLY A CA  1 
ATOM   777  C C   . GLY A 1 117 ? 21.970 13.471  -28.851 1.00 56.30  ? 117 GLY A C   1 
ATOM   778  O O   . GLY A 1 117 ? 22.831 13.831  -28.048 1.00 47.57  ? 117 GLY A O   1 
ATOM   779  N N   . ASP A 1 118 ? 20.927 14.208  -29.228 1.00 51.66  ? 118 ASP A N   1 
ATOM   780  C CA  . ASP A 1 118 ? 20.618 15.582  -28.779 1.00 53.55  ? 118 ASP A CA  1 
ATOM   781  C C   . ASP A 1 118 ? 19.135 15.849  -29.046 1.00 50.88  ? 118 ASP A C   1 
ATOM   782  O O   . ASP A 1 118 ? 18.496 15.046  -29.766 1.00 50.25  ? 118 ASP A O   1 
ATOM   783  C CB  . ASP A 1 118 ? 21.561 16.591  -29.439 1.00 57.21  ? 118 ASP A CB  1 
ATOM   784  C CG  . ASP A 1 118 ? 21.410 16.762  -30.940 1.00 57.19  ? 118 ASP A CG  1 
ATOM   785  O OD1 . ASP A 1 118 ? 20.262 16.918  -31.421 1.00 60.18  ? 118 ASP A OD1 1 
ATOM   786  O OD2 . ASP A 1 118 ? 22.449 16.785  -31.614 1.00 69.49  ? 118 ASP A OD2 1 
ATOM   787  N N   . LEU A 1 119 ? 18.589 16.912  -28.462 1.00 47.10  ? 119 LEU A N   1 
ATOM   788  C CA  . LEU A 1 119 ? 17.134 17.207  -28.557 1.00 44.95  ? 119 LEU A CA  1 
ATOM   789  C C   . LEU A 1 119 ? 16.779 17.497  -30.021 1.00 41.39  ? 119 LEU A C   1 
ATOM   790  O O   . LEU A 1 119 ? 15.679 17.166  -30.463 1.00 45.63  ? 119 LEU A O   1 
ATOM   791  C CB  . LEU A 1 119 ? 16.816 18.392  -27.645 1.00 47.58  ? 119 LEU A CB  1 
ATOM   792  C CG  . LEU A 1 119 ? 15.330 18.701  -27.453 1.00 52.87  ? 119 LEU A CG  1 
ATOM   793  C CD1 . LEU A 1 119 ? 14.547 17.459  -27.020 1.00 51.05  ? 119 LEU A CD1 1 
ATOM   794  C CD2 . LEU A 1 119 ? 15.150 19.839  -26.455 1.00 49.60  ? 119 LEU A CD2 1 
ATOM   795  N N   . SER A 1 120 ? 17.683 18.104  -30.772 1.00 43.59  ? 120 SER A N   1 
ATOM   796  C CA  . SER A 1 120 ? 17.468 18.393  -32.213 1.00 47.43  ? 120 SER A CA  1 
ATOM   797  C C   . SER A 1 120 ? 17.146 17.097  -32.992 1.00 49.59  ? 120 SER A C   1 
ATOM   798  O O   . SER A 1 120 ? 16.162 17.099  -33.751 1.00 49.75  ? 120 SER A O   1 
ATOM   799  C CB  . SER A 1 120 ? 18.672 19.082  -32.767 1.00 48.36  ? 120 SER A CB  1 
ATOM   800  O OG  . SER A 1 120 ? 18.404 19.524  -34.075 1.00 57.08  ? 120 SER A OG  1 
ATOM   801  N N   . ARG A 1 121 ? 17.961 16.042  -32.827 1.00 50.74  ? 121 ARG A N   1 
ATOM   802  C CA  . ARG A 1 121 ? 17.810 14.731  -33.520 1.00 54.34  ? 121 ARG A CA  1 
ATOM   803  C C   . ARG A 1 121 ? 16.510 14.071  -33.047 1.00 49.69  ? 121 ARG A C   1 
ATOM   804  O O   . ARG A 1 121 ? 15.782 13.529  -33.904 1.00 51.77  ? 121 ARG A O   1 
ATOM   805  C CB  . ARG A 1 121 ? 19.029 13.825  -33.289 1.00 57.86  ? 121 ARG A CB  1 
ATOM   806  C CG  . ARG A 1 121 ? 20.300 14.290  -33.995 1.00 65.06  ? 121 ARG A CG  1 
ATOM   807  C CD  . ARG A 1 121 ? 21.588 13.634  -33.486 1.00 70.97  ? 121 ARG A CD  1 
ATOM   808  N NE  . ARG A 1 121 ? 22.075 12.479  -34.247 1.00 78.40  ? 121 ARG A NE  1 
ATOM   809  C CZ  . ARG A 1 121 ? 23.114 11.694  -33.913 1.00 81.95  ? 121 ARG A CZ  1 
ATOM   810  N NH1 . ARG A 1 121 ? 23.791 11.906  -32.799 1.00 77.21  ? 121 ARG A NH1 1 
ATOM   811  N NH2 . ARG A 1 121 ? 23.482 10.689  -34.695 1.00 86.81  ? 121 ARG A NH2 1 
ATOM   812  N N   . MET A 1 122 ? 16.203 14.142  -31.749 1.00 48.14  ? 122 MET A N   1 
ATOM   813  C CA  . MET A 1 122 ? 14.956 13.568  -31.184 1.00 49.32  ? 122 MET A CA  1 
ATOM   814  C C   . MET A 1 122 ? 13.744 14.256  -31.833 1.00 47.38  ? 122 MET A C   1 
ATOM   815  O O   . MET A 1 122 ? 12.858 13.548  -32.333 1.00 49.79  ? 122 MET A O   1 
ATOM   816  C CB  . MET A 1 122 ? 14.908 13.691  -29.656 1.00 52.22  ? 122 MET A CB  1 
ATOM   817  C CG  . MET A 1 122 ? 13.568 13.272  -29.059 1.00 54.38  ? 122 MET A CG  1 
ATOM   818  S SD  . MET A 1 122 ? 13.444 13.524  -27.273 1.00 57.86  ? 122 MET A SD  1 
ATOM   819  C CE  . MET A 1 122 ? 14.123 11.961  -26.717 1.00 75.01  ? 122 MET A CE  1 
ATOM   820  N N   . ILE A 1 123 ? 13.713 15.584  -31.860 1.00 46.23  ? 123 ILE A N   1 
ATOM   821  C CA  . ILE A 1 123 ? 12.571 16.376  -32.416 1.00 45.63  ? 123 ILE A CA  1 
ATOM   822  C C   . ILE A 1 123 ? 12.335 15.974  -33.872 1.00 42.99  ? 123 ILE A C   1 
ATOM   823  O O   . ILE A 1 123 ? 11.165 15.712  -34.217 1.00 48.28  ? 123 ILE A O   1 
ATOM   824  C CB  . ILE A 1 123 ? 12.825 17.892  -32.257 1.00 46.62  ? 123 ILE A CB  1 
ATOM   825  C CG1 . ILE A 1 123 ? 12.538 18.342  -30.820 1.00 44.97  ? 123 ILE A CG1 1 
ATOM   826  C CG2 . ILE A 1 123 ? 12.040 18.707  -33.274 1.00 42.70  ? 123 ILE A CG2 1 
ATOM   827  C CD1 . ILE A 1 123 ? 13.046 19.713  -30.496 1.00 44.87  ? 123 ILE A CD1 1 
ATOM   828  N N   . LYS A 1 124 ? 13.390 15.952  -34.681 1.00 41.03  ? 124 LYS A N   1 
ATOM   829  C CA  . LYS A 1 124 ? 13.353 15.521  -36.107 1.00 52.79  ? 124 LYS A CA  1 
ATOM   830  C C   . LYS A 1 124 ? 12.821 14.095  -36.245 1.00 49.13  ? 124 LYS A C   1 
ATOM   831  O O   . LYS A 1 124 ? 12.083 13.850  -37.195 1.00 46.50  ? 124 LYS A O   1 
ATOM   832  C CB  . LYS A 1 124 ? 14.750 15.543  -36.737 1.00 59.02  ? 124 LYS A CB  1 
ATOM   833  C CG  . LYS A 1 124 ? 15.044 16.788  -37.561 1.00 68.56  ? 124 LYS A CG  1 
ATOM   834  C CD  . LYS A 1 124 ? 16.379 17.420  -37.244 1.00 73.39  ? 124 LYS A CD  1 
ATOM   835  C CE  . LYS A 1 124 ? 16.557 18.779  -37.884 1.00 75.65  ? 124 LYS A CE  1 
ATOM   836  N NZ  . LYS A 1 124 ? 17.888 19.338  -37.554 1.00 76.88  ? 124 LYS A NZ  1 
ATOM   837  N N   . HIS A 1 125 ? 13.266 13.190  -35.373 1.00 53.21  ? 125 HIS A N   1 
ATOM   838  C CA  . HIS A 1 125 ? 12.834 11.771  -35.328 1.00 51.64  ? 125 HIS A CA  1 
ATOM   839  C C   . HIS A 1 125 ? 11.309 11.757  -35.207 1.00 55.81  ? 125 HIS A C   1 
ATOM   840  O O   . HIS A 1 125 ? 10.642 11.106  -36.029 1.00 57.02  ? 125 HIS A O   1 
ATOM   841  C CB  . HIS A 1 125 ? 13.562 11.042  -34.190 1.00 49.80  ? 125 HIS A CB  1 
ATOM   842  C CG  . HIS A 1 125 ? 12.958 9.748   -33.776 0.32 51.92  ? 125 HIS A CG  1 
ATOM   843  N ND1 . HIS A 1 125 ? 13.521 8.534   -34.112 1.00 58.44  ? 125 HIS A ND1 1 
ATOM   844  C CD2 . HIS A 1 125 ? 11.875 9.469   -33.026 0.26 52.39  ? 125 HIS A CD2 1 
ATOM   845  C CE1 . HIS A 1 125 ? 12.796 7.560   -33.609 0.62 54.78  ? 125 HIS A CE1 1 
ATOM   846  N NE2 . HIS A 1 125 ? 11.783 8.110   -32.944 1.00 55.50  ? 125 HIS A NE2 1 
ATOM   847  N N   . PHE A 1 126 ? 10.773 12.468  -34.222 1.00 53.72  ? 126 PHE A N   1 
ATOM   848  C CA  . PHE A 1 126 ? 9.312  12.518  -33.977 1.00 60.19  ? 126 PHE A CA  1 
ATOM   849  C C   . PHE A 1 126 ? 8.617  13.181  -35.176 1.00 57.68  ? 126 PHE A C   1 
ATOM   850  O O   . PHE A 1 126 ? 7.519  12.766  -35.557 1.00 52.18  ? 126 PHE A O   1 
ATOM   851  C CB  . PHE A 1 126 ? 9.020  13.236  -32.656 1.00 59.24  ? 126 PHE A CB  1 
ATOM   852  C CG  . PHE A 1 126 ? 9.099  12.349  -31.441 1.00 52.91  ? 126 PHE A CG  1 
ATOM   853  C CD1 . PHE A 1 126 ? 7.989  11.639  -31.015 1.00 49.62  ? 126 PHE A CD1 1 
ATOM   854  C CD2 . PHE A 1 126 ? 10.280 12.223  -30.728 1.00 48.90  ? 126 PHE A CD2 1 
ATOM   855  C CE1 . PHE A 1 126 ? 8.057  10.829  -29.893 1.00 50.00  ? 126 PHE A CE1 1 
ATOM   856  C CE2 . PHE A 1 126 ? 10.347 11.404  -29.615 1.00 44.56  ? 126 PHE A CE2 1 
ATOM   857  C CZ  . PHE A 1 126 ? 9.241  10.700  -29.206 1.00 48.34  ? 126 PHE A CZ  1 
ATOM   858  N N   . LYS A 1 127 ? 9.245  14.199  -35.749 1.00 56.16  ? 127 LYS A N   1 
ATOM   859  C CA  . LYS A 1 127 ? 8.682  14.975  -36.883 1.00 65.69  ? 127 LYS A CA  1 
ATOM   860  C C   . LYS A 1 127 ? 8.470  14.020  -38.073 1.00 69.28  ? 127 LYS A C   1 
ATOM   861  O O   . LYS A 1 127 ? 7.315  13.943  -38.574 1.00 69.55  ? 127 LYS A O   1 
ATOM   862  C CB  . LYS A 1 127 ? 9.623  16.142  -37.196 1.00 67.36  ? 127 LYS A CB  1 
ATOM   863  C CG  . LYS A 1 127 ? 8.970  17.402  -37.737 1.00 67.32  ? 127 LYS A CG  1 
ATOM   864  C CD  . LYS A 1 127 ? 9.993  18.477  -38.069 1.00 69.54  ? 127 LYS A CD  1 
ATOM   865  C CE  . LYS A 1 127 ? 9.456  19.554  -38.991 1.00 73.22  ? 127 LYS A CE  1 
ATOM   866  N NZ  . LYS A 1 127 ? 8.078  19.966  -38.626 1.00 73.45  ? 127 LYS A NZ  1 
ATOM   867  N N   . LYS A 1 128 ? 9.524  13.296  -38.481 1.00 63.21  ? 128 LYS A N   1 
ATOM   868  C CA  . LYS A 1 128 ? 9.512  12.359  -39.641 1.00 65.86  ? 128 LYS A CA  1 
ATOM   869  C C   . LYS A 1 128 ? 8.516  11.222  -39.384 1.00 64.28  ? 128 LYS A C   1 
ATOM   870  O O   . LYS A 1 128 ? 7.871  10.784  -40.334 1.00 69.72  ? 128 LYS A O   1 
ATOM   871  C CB  . LYS A 1 128 ? 10.892 11.753  -39.914 1.00 69.52  ? 128 LYS A CB  1 
ATOM   872  C CG  . LYS A 1 128 ? 11.966 12.714  -40.409 1.00 77.42  ? 128 LYS A CG  1 
ATOM   873  C CD  . LYS A 1 128 ? 13.374 12.274  -40.013 1.00 87.69  ? 128 LYS A CD  1 
ATOM   874  C CE  . LYS A 1 128 ? 14.481 13.239  -40.393 1.00 87.74  ? 128 LYS A CE  1 
ATOM   875  N NZ  . LYS A 1 128 ? 14.728 13.229  -41.854 1.00 85.96  ? 128 LYS A NZ  1 
ATOM   876  N N   . GLN A 1 129 ? 8.398  10.750  -38.145 1.00 62.46  ? 129 GLN A N   1 
ATOM   877  C CA  . GLN A 1 129 ? 7.427  9.690   -37.771 1.00 59.19  ? 129 GLN A CA  1 
ATOM   878  C C   . GLN A 1 129 ? 6.033  10.292  -37.586 1.00 60.71  ? 129 GLN A C   1 
ATOM   879  O O   . GLN A 1 129 ? 5.147  9.552   -37.105 1.00 68.52  ? 129 GLN A O   1 
ATOM   880  C CB  . GLN A 1 129 ? 7.878  8.976   -36.501 1.00 62.26  ? 129 GLN A CB  1 
ATOM   881  C CG  . GLN A 1 129 ? 8.899  7.883   -36.761 1.00 71.01  ? 129 GLN A CG  1 
ATOM   882  C CD  . GLN A 1 129 ? 9.120  7.049   -35.522 1.00 87.67  ? 129 GLN A CD  1 
ATOM   883  O OE1 . GLN A 1 129 ? 9.256  7.572   -34.414 1.00 90.09  ? 129 GLN A OE1 1 
ATOM   884  N NE2 . GLN A 1 129 ? 9.146  5.736   -35.699 1.00 92.16  ? 129 GLN A NE2 1 
ATOM   885  N N   . LYS A 1 130 ? 5.848  11.578  -37.913 1.00 61.92  ? 130 LYS A N   1 
ATOM   886  C CA  . LYS A 1 130 ? 4.542  12.291  -37.839 1.00 66.18  ? 130 LYS A CA  1 
ATOM   887  C C   . LYS A 1 130 ? 3.891  12.075  -36.464 1.00 60.70  ? 130 LYS A C   1 
ATOM   888  O O   . LYS A 1 130 ? 2.655  11.993  -36.417 1.00 63.41  ? 130 LYS A O   1 
ATOM   889  C CB  . LYS A 1 130 ? 3.633  11.798  -38.969 1.00 71.15  ? 130 LYS A CB  1 
ATOM   890  C CG  . LYS A 1 130 ? 4.114  12.120  -40.378 1.00 79.60  ? 130 LYS A CG  1 
ATOM   891  C CD  . LYS A 1 130 ? 3.872  13.564  -40.787 1.00 88.83  ? 130 LYS A CD  1 
ATOM   892  C CE  . LYS A 1 130 ? 4.663  13.985  -42.011 1.00 91.78  ? 130 LYS A CE  1 
ATOM   893  N NZ  . LYS A 1 130 ? 4.217  13.264  -43.227 1.00 86.87  ? 130 LYS A NZ  1 
ATOM   894  N N   . ARG A 1 131 ? 4.692  11.998  -35.393 1.00 63.64  ? 131 ARG A N   1 
ATOM   895  C CA  . ARG A 1 131 ? 4.258  11.736  -33.986 1.00 65.61  ? 131 ARG A CA  1 
ATOM   896  C C   . ARG A 1 131 ? 4.592  12.950  -33.087 1.00 60.25  ? 131 ARG A C   1 
ATOM   897  O O   . ARG A 1 131 ? 5.690  13.523  -33.236 1.00 61.56  ? 131 ARG A O   1 
ATOM   898  C CB  . ARG A 1 131 ? 4.940  10.468  -33.455 1.00 66.74  ? 131 ARG A CB  1 
ATOM   899  C CG  . ARG A 1 131 ? 4.270  9.160   -33.858 1.00 78.81  ? 131 ARG A CG  1 
ATOM   900  C CD  . ARG A 1 131 ? 4.636  7.999   -32.939 1.00 88.39  ? 131 ARG A CD  1 
ATOM   901  N NE  . ARG A 1 131 ? 6.079  7.767   -32.828 1.00 94.66  ? 131 ARG A NE  1 
ATOM   902  C CZ  . ARG A 1 131 ? 6.812  7.807   -31.704 1.00 100.48 ? 131 ARG A CZ  1 
ATOM   903  N NH1 . ARG A 1 131 ? 6.263  8.073   -30.529 1.00 95.86  ? 131 ARG A NH1 1 
ATOM   904  N NH2 . ARG A 1 131 ? 8.116  7.574   -31.763 1.00 102.24 ? 131 ARG A NH2 1 
ATOM   905  N N   . LEU A 1 132 ? 3.695  13.311  -32.163 1.00 57.43  ? 132 LEU A N   1 
ATOM   906  C CA  . LEU A 1 132 ? 3.943  14.356  -31.126 1.00 57.38  ? 132 LEU A CA  1 
ATOM   907  C C   . LEU A 1 132 ? 4.710  13.727  -29.956 1.00 55.91  ? 132 LEU A C   1 
ATOM   908  O O   . LEU A 1 132 ? 4.551  12.525  -29.720 1.00 54.91  ? 132 LEU A O   1 
ATOM   909  C CB  . LEU A 1 132 ? 2.613  14.974  -30.669 1.00 56.51  ? 132 LEU A CB  1 
ATOM   910  C CG  . LEU A 1 132 ? 1.895  15.870  -31.688 1.00 57.25  ? 132 LEU A CG  1 
ATOM   911  C CD1 . LEU A 1 132 ? 0.694  16.568  -31.061 1.00 56.00  ? 132 LEU A CD1 1 
ATOM   912  C CD2 . LEU A 1 132 ? 2.840  16.909  -32.276 1.00 59.49  ? 132 LEU A CD2 1 
ATOM   913  N N   . ILE A 1 133 ? 5.566  14.498  -29.281 1.00 53.26  ? 133 ILE A N   1 
ATOM   914  C CA  . ILE A 1 133 ? 6.254  14.022  -28.051 1.00 49.88  ? 133 ILE A CA  1 
ATOM   915  C C   . ILE A 1 133 ? 5.241  14.048  -26.913 1.00 50.07  ? 133 ILE A C   1 
ATOM   916  O O   . ILE A 1 133 ? 4.583  15.051  -26.666 1.00 51.05  ? 133 ILE A O   1 
ATOM   917  C CB  . ILE A 1 133 ? 7.527  14.824  -27.733 1.00 43.79  ? 133 ILE A CB  1 
ATOM   918  C CG1 . ILE A 1 133 ? 8.537  14.721  -28.876 1.00 43.53  ? 133 ILE A CG1 1 
ATOM   919  C CG2 . ILE A 1 133 ? 8.132  14.356  -26.422 1.00 42.40  ? 133 ILE A CG2 1 
ATOM   920  C CD1 . ILE A 1 133 ? 9.827  15.467  -28.641 1.00 42.00  ? 133 ILE A CD1 1 
ATOM   921  N N   . PRO A 1 134 ? 5.042  12.920  -26.206 1.00 57.06  ? 134 PRO A N   1 
ATOM   922  C CA  . PRO A 1 134 ? 4.103  12.907  -25.085 1.00 54.33  ? 134 PRO A CA  1 
ATOM   923  C C   . PRO A 1 134 ? 4.598  13.874  -23.998 1.00 49.90  ? 134 PRO A C   1 
ATOM   924  O O   . PRO A 1 134 ? 5.792  13.906  -23.771 1.00 48.46  ? 134 PRO A O   1 
ATOM   925  C CB  . PRO A 1 134 ? 4.098  11.437  -24.612 1.00 54.98  ? 134 PRO A CB  1 
ATOM   926  C CG  . PRO A 1 134 ? 4.724  10.641  -25.754 1.00 56.51  ? 134 PRO A CG  1 
ATOM   927  C CD  . PRO A 1 134 ? 5.658  11.605  -26.463 1.00 55.55  ? 134 PRO A CD  1 
ATOM   928  N N   . GLU A 1 135 ? 3.678  14.602  -23.352 1.00 48.86  ? 135 GLU A N   1 
ATOM   929  C CA  . GLU A 1 135 ? 3.967  15.570  -22.249 1.00 53.73  ? 135 GLU A CA  1 
ATOM   930  C C   . GLU A 1 135 ? 4.831  14.896  -21.158 1.00 53.51  ? 135 GLU A C   1 
ATOM   931  O O   . GLU A 1 135 ? 5.730  15.557  -20.588 1.00 48.13  ? 135 GLU A O   1 
ATOM   932  C CB  . GLU A 1 135 ? 2.658  16.147  -21.687 1.00 51.72  ? 135 GLU A CB  1 
ATOM   933  C CG  . GLU A 1 135 ? 2.873  17.100  -20.512 1.00 54.59  ? 135 GLU A CG  1 
ATOM   934  C CD  . GLU A 1 135 ? 1.745  18.060  -20.147 1.00 51.63  ? 135 GLU A CD  1 
ATOM   935  O OE1 . GLU A 1 135 ? 0.873  18.295  -20.975 1.00 47.01  ? 135 GLU A OE1 1 
ATOM   936  O OE2 . GLU A 1 135 ? 1.768  18.606  -19.026 1.00 56.64  ? 135 GLU A OE2 1 
ATOM   937  N N   . ARG A 1 136 ? 4.575  13.624  -20.867 1.00 51.12  ? 136 ARG A N   1 
ATOM   938  C CA  . ARG A 1 136 ? 5.305  12.854  -19.826 1.00 60.81  ? 136 ARG A CA  1 
ATOM   939  C C   . ARG A 1 136 ? 6.798  12.917  -20.180 1.00 55.34  ? 136 ARG A C   1 
ATOM   940  O O   . ARG A 1 136 ? 7.601  13.297  -19.306 1.00 51.25  ? 136 ARG A O   1 
ATOM   941  C CB  . ARG A 1 136 ? 4.648  11.470  -19.707 1.00 69.07  ? 136 ARG A CB  1 
ATOM   942  C CG  . ARG A 1 136 ? 5.544  10.305  -19.318 1.00 81.88  ? 136 ARG A CG  1 
ATOM   943  C CD  . ARG A 1 136 ? 4.776  8.984   -19.346 1.00 88.98  ? 136 ARG A CD  1 
ATOM   944  N NE  . ARG A 1 136 ? 4.589  8.438   -20.699 1.00 95.83  ? 136 ARG A NE  1 
ATOM   945  C CZ  . ARG A 1 136 ? 3.512  8.600   -21.490 1.00 93.06  ? 136 ARG A CZ  1 
ATOM   946  N NH1 . ARG A 1 136 ? 2.466  9.314   -21.099 1.00 86.21  ? 136 ARG A NH1 1 
ATOM   947  N NH2 . ARG A 1 136 ? 3.487  8.041   -22.692 1.00 87.51  ? 136 ARG A NH2 1 
ATOM   948  N N   . THR A 1 137 ? 7.130  12.664  -21.447 1.00 51.87  ? 137 THR A N   1 
ATOM   949  C CA  . THR A 1 137 ? 8.510  12.643  -21.996 1.00 51.10  ? 137 THR A CA  1 
ATOM   950  C C   . THR A 1 137 ? 9.089  14.072  -22.045 1.00 48.76  ? 137 THR A C   1 
ATOM   951  O O   . THR A 1 137 ? 10.298 14.239  -21.787 1.00 45.11  ? 137 THR A O   1 
ATOM   952  C CB  . THR A 1 137 ? 8.521  11.967  -23.378 1.00 55.24  ? 137 THR A CB  1 
ATOM   953  O OG1 . THR A 1 137 ? 7.802  10.736  -23.305 1.00 50.70  ? 137 THR A OG1 1 
ATOM   954  C CG2 . THR A 1 137 ? 9.917  11.685  -23.899 1.00 52.51  ? 137 THR A CG2 1 
ATOM   955  N N   . VAL A 1 138 ? 8.278  15.076  -22.376 1.00 45.18  ? 138 VAL A N   1 
ATOM   956  C CA  . VAL A 1 138 ? 8.733  16.498  -22.439 1.00 43.59  ? 138 VAL A CA  1 
ATOM   957  C C   . VAL A 1 138 ? 9.265  16.921  -21.063 1.00 43.50  ? 138 VAL A C   1 
ATOM   958  O O   . VAL A 1 138 ? 10.432 17.369  -20.983 1.00 48.54  ? 138 VAL A O   1 
ATOM   959  C CB  . VAL A 1 138 ? 7.610  17.415  -22.939 1.00 43.89  ? 138 VAL A CB  1 
ATOM   960  C CG1 . VAL A 1 138 ? 7.981  18.878  -22.790 1.00 45.65  ? 138 VAL A CG1 1 
ATOM   961  C CG2 . VAL A 1 138 ? 7.211  17.093  -24.379 1.00 41.50  ? 138 VAL A CG2 1 
ATOM   962  N N   . TRP A 1 139 ? 8.484  16.718  -20.009 1.00 40.41  ? 139 TRP A N   1 
ATOM   963  C CA  . TRP A 1 139 ? 8.871  17.041  -18.607 1.00 41.11  ? 139 TRP A CA  1 
ATOM   964  C C   . TRP A 1 139 ? 10.100 16.222  -18.185 1.00 44.25  ? 139 TRP A C   1 
ATOM   965  O O   . TRP A 1 139 ? 10.958 16.782  -17.464 1.00 49.84  ? 139 TRP A O   1 
ATOM   966  C CB  . TRP A 1 139 ? 7.685  16.839  -17.650 1.00 42.37  ? 139 TRP A CB  1 
ATOM   967  C CG  . TRP A 1 139 ? 6.578  17.835  -17.830 1.00 40.24  ? 139 TRP A CG  1 
ATOM   968  C CD1 . TRP A 1 139 ? 5.281  17.582  -18.170 1.00 42.13  ? 139 TRP A CD1 1 
ATOM   969  C CD2 . TRP A 1 139 ? 6.684  19.265  -17.709 1.00 38.12  ? 139 TRP A CD2 1 
ATOM   970  N NE1 . TRP A 1 139 ? 4.579  18.755  -18.280 1.00 43.55  ? 139 TRP A NE1 1 
ATOM   971  C CE2 . TRP A 1 139 ? 5.418  19.803  -18.009 1.00 40.93  ? 139 TRP A CE2 1 
ATOM   972  C CE3 . TRP A 1 139 ? 7.728  20.143  -17.422 1.00 41.40  ? 139 TRP A CE3 1 
ATOM   973  C CZ2 . TRP A 1 139 ? 5.169  21.171  -17.976 1.00 41.54  ? 139 TRP A CZ2 1 
ATOM   974  C CZ3 . TRP A 1 139 ? 7.474  21.500  -17.359 1.00 40.04  ? 139 TRP A CZ3 1 
ATOM   975  C CH2 . TRP A 1 139 ? 6.217  22.004  -17.651 1.00 38.59  ? 139 TRP A CH2 1 
ATOM   976  N N   . LYS A 1 140 ? 10.214 14.969  -18.635 1.00 45.59  ? 140 LYS A N   1 
ATOM   977  C CA  . LYS A 1 140 ? 11.327 14.057  -18.247 1.00 50.37  ? 140 LYS A CA  1 
ATOM   978  C C   . LYS A 1 140 ? 12.653 14.664  -18.721 1.00 46.79  ? 140 LYS A C   1 
ATOM   979  O O   . LYS A 1 140 ? 13.606 14.647  -17.964 1.00 49.29  ? 140 LYS A O   1 
ATOM   980  C CB  . LYS A 1 140 ? 11.160 12.636  -18.814 1.00 54.33  ? 140 LYS A CB  1 
ATOM   981  C CG  . LYS A 1 140 ? 12.141 11.599  -18.257 1.00 60.74  ? 140 LYS A CG  1 
ATOM   982  C CD  . LYS A 1 140 ? 12.692 10.592  -19.253 1.00 68.08  ? 140 LYS A CD  1 
ATOM   983  C CE  . LYS A 1 140 ? 11.696 9.520   -19.647 1.00 80.47  ? 140 LYS A CE  1 
ATOM   984  N NZ  . LYS A 1 140 ? 12.042 8.876   -20.941 1.00 85.32  ? 140 LYS A NZ  1 
ATOM   985  N N   . TYR A 1 141 ? 12.715 15.172  -19.946 1.00 48.76  ? 141 TYR A N   1 
ATOM   986  C CA  . TYR A 1 141 ? 13.929 15.828  -20.487 1.00 46.78  ? 141 TYR A CA  1 
ATOM   987  C C   . TYR A 1 141 ? 13.997 17.270  -19.977 1.00 39.39  ? 141 TYR A C   1 
ATOM   988  O O   . TYR A 1 141 ? 15.048 17.685  -19.547 1.00 39.51  ? 141 TYR A O   1 
ATOM   989  C CB  . TYR A 1 141 ? 13.952 15.663  -22.006 1.00 51.84  ? 141 TYR A CB  1 
ATOM   990  C CG  . TYR A 1 141 ? 14.153 14.231  -22.423 1.00 55.10  ? 141 TYR A CG  1 
ATOM   991  C CD1 . TYR A 1 141 ? 15.311 13.551  -22.082 1.00 58.32  ? 141 TYR A CD1 1 
ATOM   992  C CD2 . TYR A 1 141 ? 13.182 13.547  -23.127 1.00 57.42  ? 141 TYR A CD2 1 
ATOM   993  C CE1 . TYR A 1 141 ? 15.506 12.231  -22.441 1.00 62.10  ? 141 TYR A CE1 1 
ATOM   994  C CE2 . TYR A 1 141 ? 13.367 12.228  -23.506 1.00 59.67  ? 141 TYR A CE2 1 
ATOM   995  C CZ  . TYR A 1 141 ? 14.529 11.565  -23.158 1.00 62.59  ? 141 TYR A CZ  1 
ATOM   996  O OH  . TYR A 1 141 ? 14.711 10.266  -23.536 1.00 67.28  ? 141 TYR A OH  1 
ATOM   997  N N   . PHE A 1 142 ? 12.881 17.993  -19.949 1.00 40.47  ? 142 PHE A N   1 
ATOM   998  C CA  . PHE A 1 142 ? 12.860 19.443  -19.621 1.00 38.33  ? 142 PHE A CA  1 
ATOM   999  C C   . PHE A 1 142 ? 13.280 19.717  -18.167 1.00 40.78  ? 142 PHE A C   1 
ATOM   1000 O O   . PHE A 1 142 ? 13.977 20.711  -17.935 1.00 40.37  ? 142 PHE A O   1 
ATOM   1001 C CB  . PHE A 1 142 ? 11.481 20.037  -19.904 1.00 38.17  ? 142 PHE A CB  1 
ATOM   1002 C CG  . PHE A 1 142 ? 11.488 21.536  -19.802 1.00 39.44  ? 142 PHE A CG  1 
ATOM   1003 C CD1 . PHE A 1 142 ? 12.161 22.298  -20.751 1.00 40.01  ? 142 PHE A CD1 1 
ATOM   1004 C CD2 . PHE A 1 142 ? 10.885 22.182  -18.737 1.00 37.30  ? 142 PHE A CD2 1 
ATOM   1005 C CE1 . PHE A 1 142 ? 12.193 23.676  -20.652 1.00 37.69  ? 142 PHE A CE1 1 
ATOM   1006 C CE2 . PHE A 1 142 ? 10.950 23.561  -18.626 1.00 38.83  ? 142 PHE A CE2 1 
ATOM   1007 C CZ  . PHE A 1 142 ? 11.584 24.305  -19.595 1.00 36.53  ? 142 PHE A CZ  1 
ATOM   1008 N N   . VAL A 1 143 ? 12.860 18.903  -17.196 1.00 36.96  ? 143 VAL A N   1 
ATOM   1009 C CA  . VAL A 1 143 ? 13.267 19.120  -15.778 1.00 36.47  ? 143 VAL A CA  1 
ATOM   1010 C C   . VAL A 1 143 ? 14.790 18.993  -15.690 1.00 38.32  ? 143 VAL A C   1 
ATOM   1011 O O   . VAL A 1 143 ? 15.387 19.712  -14.871 1.00 36.89  ? 143 VAL A O   1 
ATOM   1012 C CB  . VAL A 1 143 ? 12.541 18.154  -14.818 1.00 40.05  ? 143 VAL A CB  1 
ATOM   1013 C CG1 . VAL A 1 143 ? 12.973 16.696  -15.008 1.00 38.65  ? 143 VAL A CG1 1 
ATOM   1014 C CG2 . VAL A 1 143 ? 12.697 18.565  -13.370 1.00 37.86  ? 143 VAL A CG2 1 
ATOM   1015 N N   . GLN A 1 144 ? 15.420 18.135  -16.506 1.00 38.47  ? 144 GLN A N   1 
ATOM   1016 C CA  . GLN A 1 144 ? 16.897 17.949  -16.440 1.00 36.71  ? 144 GLN A CA  1 
ATOM   1017 C C   . GLN A 1 144 ? 17.580 19.218  -16.947 1.00 37.53  ? 144 GLN A C   1 
ATOM   1018 O O   . GLN A 1 144 ? 18.487 19.698  -16.281 1.00 40.46  ? 144 GLN A O   1 
ATOM   1019 C CB  . GLN A 1 144 ? 17.345 16.703  -17.201 1.00 37.96  ? 144 GLN A CB  1 
ATOM   1020 C CG  . GLN A 1 144 ? 16.945 15.392  -16.513 1.00 39.61  ? 144 GLN A CG  1 
ATOM   1021 C CD  . GLN A 1 144 ? 17.378 14.217  -17.355 1.00 39.36  ? 144 GLN A CD  1 
ATOM   1022 O OE1 . GLN A 1 144 ? 18.559 13.921  -17.478 1.00 42.59  ? 144 GLN A OE1 1 
ATOM   1023 N NE2 . GLN A 1 144 ? 16.436 13.590  -18.030 1.00 39.91  ? 144 GLN A NE2 1 
ATOM   1024 N N   . LEU A 1 145 ? 17.149 19.745  -18.089 1.00 37.81  ? 145 LEU A N   1 
ATOM   1025 C CA  . LEU A 1 145 ? 17.642 21.029  -18.649 1.00 37.50  ? 145 LEU A CA  1 
ATOM   1026 C C   . LEU A 1 145 ? 17.435 22.168  -17.635 1.00 36.84  ? 145 LEU A C   1 
ATOM   1027 O O   . LEU A 1 145 ? 18.353 22.971  -17.440 1.00 34.07  ? 145 LEU A O   1 
ATOM   1028 C CB  . LEU A 1 145 ? 16.876 21.284  -19.948 1.00 41.33  ? 145 LEU A CB  1 
ATOM   1029 C CG  . LEU A 1 145 ? 17.234 22.556  -20.697 1.00 40.52  ? 145 LEU A CG  1 
ATOM   1030 C CD1 . LEU A 1 145 ? 18.717 22.597  -20.990 1.00 43.48  ? 145 LEU A CD1 1 
ATOM   1031 C CD2 . LEU A 1 145 ? 16.412 22.646  -21.978 1.00 41.65  ? 145 LEU A CD2 1 
ATOM   1032 N N   . CYS A 1 146 ? 16.292 22.223  -16.961 1.00 37.07  ? 146 CYS A N   1 
ATOM   1033 C CA  . CYS A 1 146 ? 16.030 23.253  -15.928 1.00 38.37  ? 146 CYS A CA  1 
ATOM   1034 C C   . CYS A 1 146 ? 17.022 23.076  -14.785 1.00 39.71  ? 146 CYS A C   1 
ATOM   1035 O O   . CYS A 1 146 ? 17.572 24.105  -14.324 1.00 48.00  ? 146 CYS A O   1 
ATOM   1036 C CB  . CYS A 1 146 ? 14.598 23.221  -15.423 1.00 39.04  ? 146 CYS A CB  1 
ATOM   1037 S SG  . CYS A 1 146 ? 13.428 23.845  -16.657 1.00 44.01  ? 146 CYS A SG  1 
ATOM   1038 N N   . SER A 1 147 ? 17.298 21.831  -14.391 1.00 43.98  ? 147 SER A N   1 
ATOM   1039 C CA  . SER A 1 147 ? 18.252 21.506  -13.293 1.00 43.27  ? 147 SER A CA  1 
ATOM   1040 C C   . SER A 1 147 ? 19.628 22.069  -13.650 1.00 37.51  ? 147 SER A C   1 
ATOM   1041 O O   . SER A 1 147 ? 20.240 22.785  -12.817 1.00 37.89  ? 147 SER A O   1 
ATOM   1042 C CB  . SER A 1 147 ? 18.327 20.022  -13.018 1.00 41.73  ? 147 SER A CB  1 
ATOM   1043 O OG  . SER A 1 147 ? 18.848 19.799  -11.717 1.00 44.41  ? 147 SER A OG  1 
ATOM   1044 N N   . ALA A 1 148 ? 20.098 21.742  -14.845 1.00 34.98  ? 148 ALA A N   1 
ATOM   1045 C CA  . ALA A 1 148 ? 21.374 22.256  -15.394 1.00 37.16  ? 148 ALA A CA  1 
ATOM   1046 C C   . ALA A 1 148 ? 21.397 23.786  -15.286 1.00 38.38  ? 148 ALA A C   1 
ATOM   1047 O O   . ALA A 1 148 ? 22.383 24.315  -14.792 1.00 37.32  ? 148 ALA A O   1 
ATOM   1048 C CB  . ALA A 1 148 ? 21.547 21.816  -16.821 1.00 34.30  ? 148 ALA A CB  1 
ATOM   1049 N N   . LEU A 1 149 ? 20.342 24.481  -15.713 1.00 38.85  ? 149 LEU A N   1 
ATOM   1050 C CA  . LEU A 1 149 ? 20.431 25.949  -15.856 1.00 41.37  ? 149 LEU A CA  1 
ATOM   1051 C C   . LEU A 1 149 ? 20.355 26.612  -14.479 1.00 40.17  ? 149 LEU A C   1 
ATOM   1052 O O   . LEU A 1 149 ? 21.094 27.603  -14.263 1.00 42.04  ? 149 LEU A O   1 
ATOM   1053 C CB  . LEU A 1 149 ? 19.365 26.475  -16.818 1.00 43.42  ? 149 LEU A CB  1 
ATOM   1054 C CG  . LEU A 1 149 ? 19.631 27.906  -17.287 1.00 46.78  ? 149 LEU A CG  1 
ATOM   1055 C CD1 . LEU A 1 149 ? 20.823 27.967  -18.235 1.00 47.04  ? 149 LEU A CD1 1 
ATOM   1056 C CD2 . LEU A 1 149 ? 18.395 28.502  -17.931 1.00 48.06  ? 149 LEU A CD2 1 
ATOM   1057 N N   . GLU A 1 150 ? 19.538 26.077  -13.576 1.00 42.83  ? 150 GLU A N   1 
ATOM   1058 C CA  . GLU A 1 150 ? 19.478 26.533  -12.161 1.00 40.51  ? 150 GLU A CA  1 
ATOM   1059 C C   . GLU A 1 150 ? 20.888 26.480  -11.578 1.00 38.79  ? 150 GLU A C   1 
ATOM   1060 O O   . GLU A 1 150 ? 21.279 27.438  -10.913 1.00 40.18  ? 150 GLU A O   1 
ATOM   1061 C CB  . GLU A 1 150 ? 18.477 25.706  -11.356 1.00 49.43  ? 150 GLU A CB  1 
ATOM   1062 C CG  . GLU A 1 150 ? 18.082 26.353  -10.032 1.00 54.10  ? 150 GLU A CG  1 
ATOM   1063 C CD  . GLU A 1 150 ? 19.063 26.101  -8.909  1.00 56.23  ? 150 GLU A CD  1 
ATOM   1064 O OE1 . GLU A 1 150 ? 19.737 25.053  -8.945  1.00 57.00  ? 150 GLU A OE1 1 
ATOM   1065 O OE2 . GLU A 1 150 ? 19.162 26.956  -8.015  1.00 66.83  ? 150 GLU A OE2 1 
ATOM   1066 N N   . HIS A 1 151 ? 21.664 25.443  -11.874 1.00 36.34  ? 151 HIS A N   1 
ATOM   1067 C CA  . HIS A 1 151 ? 23.055 25.332  -11.359 1.00 37.87  ? 151 HIS A CA  1 
ATOM   1068 C C   . HIS A 1 151 ? 23.912 26.451  -11.948 1.00 40.59  ? 151 HIS A C   1 
ATOM   1069 O O   . HIS A 1 151 ? 24.695 27.099  -11.188 1.00 40.87  ? 151 HIS A O   1 
ATOM   1070 C CB  . HIS A 1 151 ? 23.671 23.964  -11.670 1.00 38.97  ? 151 HIS A CB  1 
ATOM   1071 C CG  . HIS A 1 151 ? 25.076 23.838  -11.211 1.00 35.71  ? 151 HIS A CG  1 
ATOM   1072 N ND1 . HIS A 1 151 ? 25.404 23.817  -9.878  1.00 34.88  ? 151 HIS A ND1 1 
ATOM   1073 C CD2 . HIS A 1 151 ? 26.232 23.741  -11.898 1.00 39.59  ? 151 HIS A CD2 1 
ATOM   1074 C CE1 . HIS A 1 151 ? 26.714 23.699  -9.751  1.00 38.62  ? 151 HIS A CE1 1 
ATOM   1075 N NE2 . HIS A 1 151 ? 27.252 23.631  -10.981 1.00 39.89  ? 151 HIS A NE2 1 
ATOM   1076 N N   . MET A 1 152 ? 23.804 26.659  -13.257 1.00 36.03  ? 152 MET A N   1 
ATOM   1077 C CA  . MET A 1 152 ? 24.625 27.683  -13.932 1.00 37.66  ? 152 MET A CA  1 
ATOM   1078 C C   . MET A 1 152 ? 24.267 29.064  -13.356 1.00 36.69  ? 152 MET A C   1 
ATOM   1079 O O   . MET A 1 152 ? 25.182 29.806  -12.939 1.00 33.85  ? 152 MET A O   1 
ATOM   1080 C CB  . MET A 1 152 ? 24.414 27.628  -15.447 1.00 39.60  ? 152 MET A CB  1 
ATOM   1081 C CG  . MET A 1 152 ? 24.979 26.375  -16.089 1.00 37.39  ? 152 MET A CG  1 
ATOM   1082 S SD  . MET A 1 152 ? 24.793 26.401  -17.909 1.00 42.20  ? 152 MET A SD  1 
ATOM   1083 C CE  . MET A 1 152 ? 26.113 27.557  -18.282 1.00 47.03  ? 152 MET A CE  1 
ATOM   1084 N N   . HIS A 1 153 ? 22.984 29.398  -13.280 1.00 35.82  ? 153 HIS A N   1 
ATOM   1085 C CA  . HIS A 1 153 ? 22.539 30.717  -12.763 1.00 38.60  ? 153 HIS A CA  1 
ATOM   1086 C C   . HIS A 1 153 ? 22.938 30.905  -11.287 1.00 44.27  ? 153 HIS A C   1 
ATOM   1087 O O   . HIS A 1 153 ? 23.332 32.048  -10.933 1.00 48.90  ? 153 HIS A O   1 
ATOM   1088 C CB  . HIS A 1 153 ? 21.040 30.905  -12.982 1.00 39.29  ? 153 HIS A CB  1 
ATOM   1089 C CG  . HIS A 1 153 ? 20.680 31.214  -14.396 1.00 39.89  ? 153 HIS A CG  1 
ATOM   1090 N ND1 . HIS A 1 153 ? 19.444 31.712  -14.742 1.00 42.64  ? 153 HIS A ND1 1 
ATOM   1091 C CD2 . HIS A 1 153 ? 21.370 31.076  -15.545 1.00 37.10  ? 153 HIS A CD2 1 
ATOM   1092 C CE1 . HIS A 1 153 ? 19.390 31.880  -16.041 1.00 40.94  ? 153 HIS A CE1 1 
ATOM   1093 N NE2 . HIS A 1 153 ? 20.552 31.497  -16.555 1.00 41.18  ? 153 HIS A NE2 1 
ATOM   1094 N N   . SER A 1 154 ? 22.832 29.868  -10.448 1.00 43.66  ? 154 SER A N   1 
ATOM   1095 C CA  . SER A 1 154 ? 23.183 29.924  -8.996  1.00 42.46  ? 154 SER A CA  1 
ATOM   1096 C C   . SER A 1 154 ? 24.647 30.336  -8.839  1.00 40.54  ? 154 SER A C   1 
ATOM   1097 O O   . SER A 1 154 ? 24.960 31.007  -7.865  1.00 48.59  ? 154 SER A O   1 
ATOM   1098 C CB  . SER A 1 154 ? 22.910 28.626  -8.276  1.00 43.00  ? 154 SER A CB  1 
ATOM   1099 O OG  . SER A 1 154 ? 23.849 27.622  -8.655  1.00 45.39  ? 154 SER A OG  1 
ATOM   1100 N N   . ARG A 1 155 ? 25.494 29.973  -9.802  1.00 44.58  ? 155 ARG A N   1 
ATOM   1101 C CA  . ARG A 1 155 ? 26.925 30.368  -9.853  1.00 42.29  ? 155 ARG A CA  1 
ATOM   1102 C C   . ARG A 1 155 ? 27.104 31.682  -10.625 1.00 43.68  ? 155 ARG A C   1 
ATOM   1103 O O   . ARG A 1 155 ? 28.260 32.045  -10.902 1.00 42.94  ? 155 ARG A O   1 
ATOM   1104 C CB  . ARG A 1 155 ? 27.739 29.243  -10.496 1.00 43.14  ? 155 ARG A CB  1 
ATOM   1105 C CG  . ARG A 1 155 ? 27.713 27.926  -9.726  1.00 45.11  ? 155 ARG A CG  1 
ATOM   1106 C CD  . ARG A 1 155 ? 28.167 28.027  -8.275  1.00 47.17  ? 155 ARG A CD  1 
ATOM   1107 N NE  . ARG A 1 155 ? 28.219 26.705  -7.662  1.00 48.27  ? 155 ARG A NE  1 
ATOM   1108 C CZ  . ARG A 1 155 ? 29.242 25.862  -7.765  1.00 49.85  ? 155 ARG A CZ  1 
ATOM   1109 N NH1 . ARG A 1 155 ? 30.332 26.200  -8.435  1.00 49.71  ? 155 ARG A NH1 1 
ATOM   1110 N NH2 . ARG A 1 155 ? 29.172 24.675  -7.194  1.00 51.01  ? 155 ARG A NH2 1 
ATOM   1111 N N   . ARG A 1 156 ? 26.022 32.355  -11.017 1.00 48.13  ? 156 ARG A N   1 
ATOM   1112 C CA  . ARG A 1 156 ? 26.107 33.585  -11.857 1.00 57.36  ? 156 ARG A CA  1 
ATOM   1113 C C   . ARG A 1 156 ? 26.877 33.290  -13.166 1.00 54.11  ? 156 ARG A C   1 
ATOM   1114 O O   . ARG A 1 156 ? 27.766 34.078  -13.515 1.00 54.66  ? 156 ARG A O   1 
ATOM   1115 C CB  . ARG A 1 156 ? 26.752 34.722  -11.045 1.00 60.22  ? 156 ARG A CB  1 
ATOM   1116 C CG  . ARG A 1 156 ? 26.177 34.950  -9.646  1.00 71.81  ? 156 ARG A CG  1 
ATOM   1117 C CD  . ARG A 1 156 ? 24.773 35.544  -9.588  1.00 84.10  ? 156 ARG A CD  1 
ATOM   1118 N NE  . ARG A 1 156 ? 24.567 36.643  -10.539 1.00 104.64 ? 156 ARG A NE  1 
ATOM   1119 C CZ  . ARG A 1 156 ? 24.684 37.953  -10.280 1.00 101.20 ? 156 ARG A CZ  1 
ATOM   1120 N NH1 . ARG A 1 156 ? 24.997 38.387  -9.069  1.00 105.73 ? 156 ARG A NH1 1 
ATOM   1121 N NH2 . ARG A 1 156 ? 24.467 38.834  -11.245 1.00 92.30  ? 156 ARG A NH2 1 
ATOM   1122 N N   . VAL A 1 157 ? 26.555 32.190  -13.862 1.00 51.98  ? 157 VAL A N   1 
ATOM   1123 C CA  . VAL A 1 157 ? 27.014 31.879  -15.255 1.00 46.45  ? 157 VAL A CA  1 
ATOM   1124 C C   . VAL A 1 157 ? 25.793 31.805  -16.197 1.00 44.37  ? 157 VAL A C   1 
ATOM   1125 O O   . VAL A 1 157 ? 24.946 30.929  -15.992 1.00 45.64  ? 157 VAL A O   1 
ATOM   1126 C CB  . VAL A 1 157 ? 27.810 30.564  -15.290 1.00 48.37  ? 157 VAL A CB  1 
ATOM   1127 C CG1 . VAL A 1 157 ? 28.226 30.187  -16.707 1.00 50.51  ? 157 VAL A CG1 1 
ATOM   1128 C CG2 . VAL A 1 157 ? 29.029 30.614  -14.395 1.00 47.64  ? 157 VAL A CG2 1 
ATOM   1129 N N   . MET A 1 158 ? 25.697 32.696  -17.193 1.00 48.81  ? 158 MET A N   1 
ATOM   1130 C CA  . MET A 1 158 ? 24.673 32.674  -18.282 1.00 47.50  ? 158 MET A CA  1 
ATOM   1131 C C   . MET A 1 158 ? 25.053 31.566  -19.249 1.00 42.29  ? 158 MET A C   1 
ATOM   1132 O O   . MET A 1 158 ? 26.257 31.341  -19.374 1.00 41.60  ? 158 MET A O   1 
ATOM   1133 C CB  . MET A 1 158 ? 24.690 33.966  -19.094 1.00 51.48  ? 158 MET A CB  1 
ATOM   1134 C CG  . MET A 1 158 ? 24.266 35.155  -18.312 1.00 61.66  ? 158 MET A CG  1 
ATOM   1135 S SD  . MET A 1 158 ? 24.409 36.681  -19.263 1.00 60.24  ? 158 MET A SD  1 
ATOM   1136 C CE  . MET A 1 158 ? 24.626 37.800  -17.876 1.00 61.75  ? 158 MET A CE  1 
ATOM   1137 N N   . HIS A 1 159 ? 24.099 30.941  -19.945 1.00 45.37  ? 159 HIS A N   1 
ATOM   1138 C CA  . HIS A 1 159 ? 24.430 29.960  -21.016 1.00 44.39  ? 159 HIS A CA  1 
ATOM   1139 C C   . HIS A 1 159 ? 24.754 30.695  -22.332 1.00 49.32  ? 159 HIS A C   1 
ATOM   1140 O O   . HIS A 1 159 ? 25.826 30.407  -22.910 1.00 50.70  ? 159 HIS A O   1 
ATOM   1141 C CB  . HIS A 1 159 ? 23.342 28.907  -21.204 1.00 42.20  ? 159 HIS A CB  1 
ATOM   1142 C CG  . HIS A 1 159 ? 23.801 27.809  -22.105 1.00 44.30  ? 159 HIS A CG  1 
ATOM   1143 N ND1 . HIS A 1 159 ? 23.763 27.910  -23.477 1.00 40.86  ? 159 HIS A ND1 1 
ATOM   1144 C CD2 . HIS A 1 159 ? 24.376 26.617  -21.839 1.00 45.86  ? 159 HIS A CD2 1 
ATOM   1145 C CE1 . HIS A 1 159 ? 24.262 26.814  -24.007 1.00 44.17  ? 159 HIS A CE1 1 
ATOM   1146 N NE2 . HIS A 1 159 ? 24.647 26.011  -23.033 1.00 43.17  ? 159 HIS A NE2 1 
ATOM   1147 N N   . ARG A 1 160 ? 23.834 31.536  -22.819 1.00 47.50  ? 160 ARG A N   1 
ATOM   1148 C CA  . ARG A 1 160 ? 24.011 32.424  -24.010 1.00 56.65  ? 160 ARG A CA  1 
ATOM   1149 C C   . ARG A 1 160 ? 23.792 31.698  -25.344 1.00 55.15  ? 160 ARG A C   1 
ATOM   1150 O O   . ARG A 1 160 ? 23.790 32.388  -26.370 1.00 68.29  ? 160 ARG A O   1 
ATOM   1151 C CB  . ARG A 1 160 ? 25.392 33.084  -24.035 1.00 58.78  ? 160 ARG A CB  1 
ATOM   1152 C CG  . ARG A 1 160 ? 25.580 34.126  -22.945 1.00 60.62  ? 160 ARG A CG  1 
ATOM   1153 C CD  . ARG A 1 160 ? 26.512 35.226  -23.390 1.00 67.74  ? 160 ARG A CD  1 
ATOM   1154 N NE  . ARG A 1 160 ? 27.615 35.308  -22.449 1.00 68.02  ? 160 ARG A NE  1 
ATOM   1155 C CZ  . ARG A 1 160 ? 27.871 36.343  -21.670 1.00 77.93  ? 160 ARG A CZ  1 
ATOM   1156 N NH1 . ARG A 1 160 ? 27.118 37.434  -21.730 1.00 87.77  ? 160 ARG A NH1 1 
ATOM   1157 N NH2 . ARG A 1 160 ? 28.889 36.277  -20.832 1.00 77.25  ? 160 ARG A NH2 1 
ATOM   1158 N N   . ASN A 1 161 ? 23.573 30.385  -25.357 1.00 57.08  ? 161 ASN A N   1 
ATOM   1159 C CA  . ASN A 1 161 ? 23.399 29.635  -26.626 1.00 52.23  ? 161 ASN A CA  1 
ATOM   1160 C C   . ASN A 1 161 ? 22.561 28.380  -26.379 1.00 46.90  ? 161 ASN A C   1 
ATOM   1161 O O   . ASN A 1 161 ? 23.038 27.258  -26.655 1.00 40.23  ? 161 ASN A O   1 
ATOM   1162 C CB  . ASN A 1 161 ? 24.750 29.349  -27.283 1.00 55.61  ? 161 ASN A CB  1 
ATOM   1163 C CG  . ASN A 1 161 ? 24.618 29.020  -28.758 1.00 60.91  ? 161 ASN A CG  1 
ATOM   1164 O OD1 . ASN A 1 161 ? 23.583 29.291  -29.389 1.00 63.44  ? 161 ASN A OD1 1 
ATOM   1165 N ND2 . ASN A 1 161 ? 25.663 28.422  -29.310 1.00 56.64  ? 161 ASN A ND2 1 
ATOM   1166 N N   . ILE A 1 162 ? 21.340 28.582  -25.892 1.00 46.62  ? 162 ILE A N   1 
ATOM   1167 C CA  . ILE A 1 162 ? 20.382 27.488  -25.572 1.00 45.40  ? 162 ILE A CA  1 
ATOM   1168 C C   . ILE A 1 162 ? 19.521 27.214  -26.810 1.00 46.52  ? 162 ILE A C   1 
ATOM   1169 O O   . ILE A 1 162 ? 18.738 28.109  -27.198 1.00 47.06  ? 162 ILE A O   1 
ATOM   1170 C CB  . ILE A 1 162 ? 19.519 27.810  -24.338 1.00 40.27  ? 162 ILE A CB  1 
ATOM   1171 C CG1 . ILE A 1 162 ? 20.386 27.945  -23.085 1.00 45.85  ? 162 ILE A CG1 1 
ATOM   1172 C CG2 . ILE A 1 162 ? 18.436 26.750  -24.171 1.00 38.08  ? 162 ILE A CG2 1 
ATOM   1173 C CD1 . ILE A 1 162 ? 19.628 28.349  -21.839 1.00 44.38  ? 162 ILE A CD1 1 
ATOM   1174 N N   . LYS A 1 163 ? 19.605 25.983  -27.322 1.00 45.62  ? 163 LYS A N   1 
ATOM   1175 C CA  . LYS A 1 163 ? 18.889 25.482  -28.528 1.00 44.88  ? 163 LYS A CA  1 
ATOM   1176 C C   . LYS A 1 163 ? 18.945 23.956  -28.521 1.00 39.36  ? 163 LYS A C   1 
ATOM   1177 O O   . LYS A 1 163 ? 19.808 23.373  -27.875 1.00 39.89  ? 163 LYS A O   1 
ATOM   1178 C CB  . LYS A 1 163 ? 19.551 26.059  -29.775 1.00 42.65  ? 163 LYS A CB  1 
ATOM   1179 C CG  . LYS A 1 163 ? 21.000 25.642  -29.970 1.00 49.09  ? 163 LYS A CG  1 
ATOM   1180 C CD  . LYS A 1 163 ? 21.781 26.482  -30.966 1.00 53.95  ? 163 LYS A CD  1 
ATOM   1181 C CE  . LYS A 1 163 ? 23.025 25.760  -31.451 1.00 63.23  ? 163 LYS A CE  1 
ATOM   1182 N NZ  . LYS A 1 163 ? 23.911 26.626  -32.263 1.00 69.03  ? 163 LYS A NZ  1 
ATOM   1183 N N   . PRO A 1 164 ? 18.019 23.257  -29.204 1.00 39.19  ? 164 PRO A N   1 
ATOM   1184 C CA  . PRO A 1 164 ? 17.946 21.798  -29.130 1.00 42.77  ? 164 PRO A CA  1 
ATOM   1185 C C   . PRO A 1 164 ? 19.268 21.051  -29.388 1.00 43.69  ? 164 PRO A C   1 
ATOM   1186 O O   . PRO A 1 164 ? 19.506 20.068  -28.718 1.00 46.98  ? 164 PRO A O   1 
ATOM   1187 C CB  . PRO A 1 164 ? 16.877 21.492  -30.179 1.00 41.52  ? 164 PRO A CB  1 
ATOM   1188 C CG  . PRO A 1 164 ? 15.975 22.686  -30.115 1.00 40.46  ? 164 PRO A CG  1 
ATOM   1189 C CD  . PRO A 1 164 ? 16.949 23.831  -30.027 1.00 41.74  ? 164 PRO A CD  1 
ATOM   1190 N N   . ALA A 1 165 ? 20.136 21.576  -30.251 1.00 42.77  ? 165 ALA A N   1 
ATOM   1191 C CA  . ALA A 1 165 ? 21.395 20.915  -30.661 1.00 47.09  ? 165 ALA A CA  1 
ATOM   1192 C C   . ALA A 1 165 ? 22.442 20.972  -29.543 1.00 46.03  ? 165 ALA A C   1 
ATOM   1193 O O   . ALA A 1 165 ? 23.392 20.169  -29.590 1.00 48.60  ? 165 ALA A O   1 
ATOM   1194 C CB  . ALA A 1 165 ? 21.927 21.553  -31.918 1.00 48.39  ? 165 ALA A CB  1 
ATOM   1195 N N   . ASN A 1 166 ? 22.330 21.932  -28.623 1.00 44.99  ? 166 ASN A N   1 
ATOM   1196 C CA  . ASN A 1 166 ? 23.261 22.077  -27.468 1.00 42.33  ? 166 ASN A CA  1 
ATOM   1197 C C   . ASN A 1 166 ? 22.735 21.303  -26.247 1.00 40.68  ? 166 ASN A C   1 
ATOM   1198 O O   . ASN A 1 166 ? 23.404 21.332  -25.188 1.00 47.12  ? 166 ASN A O   1 
ATOM   1199 C CB  . ASN A 1 166 ? 23.478 23.552  -27.139 1.00 46.92  ? 166 ASN A CB  1 
ATOM   1200 C CG  . ASN A 1 166 ? 24.649 24.136  -27.889 1.00 48.92  ? 166 ASN A CG  1 
ATOM   1201 O OD1 . ASN A 1 166 ? 25.546 23.405  -28.300 1.00 48.00  ? 166 ASN A OD1 1 
ATOM   1202 N ND2 . ASN A 1 166 ? 24.661 25.449  -28.039 1.00 49.72  ? 166 ASN A ND2 1 
ATOM   1203 N N   . VAL A 1 167 ? 21.572 20.666  -26.379 1.00 38.17  ? 167 VAL A N   1 
ATOM   1204 C CA  . VAL A 1 167 ? 20.965 19.793  -25.340 1.00 41.56  ? 167 VAL A CA  1 
ATOM   1205 C C   . VAL A 1 167 ? 21.253 18.333  -25.706 1.00 39.01  ? 167 VAL A C   1 
ATOM   1206 O O   . VAL A 1 167 ? 20.450 17.704  -26.394 1.00 37.07  ? 167 VAL A O   1 
ATOM   1207 C CB  . VAL A 1 167 ? 19.463 20.085  -25.206 1.00 40.97  ? 167 VAL A CB  1 
ATOM   1208 C CG1 . VAL A 1 167 ? 18.813 19.213  -24.138 1.00 43.24  ? 167 VAL A CG1 1 
ATOM   1209 C CG2 . VAL A 1 167 ? 19.226 21.559  -24.929 1.00 36.29  ? 167 VAL A CG2 1 
ATOM   1210 N N   . PHE A 1 168 ? 22.386 17.811  -25.255 1.00 43.95  ? 168 PHE A N   1 
ATOM   1211 C CA  . PHE A 1 168 ? 22.784 16.414  -25.551 1.00 44.17  ? 168 PHE A CA  1 
ATOM   1212 C C   . PHE A 1 168 ? 21.943 15.469  -24.693 1.00 50.07  ? 168 PHE A C   1 
ATOM   1213 O O   . PHE A 1 168 ? 21.384 15.863  -23.620 1.00 50.90  ? 168 PHE A O   1 
ATOM   1214 C CB  . PHE A 1 168 ? 24.296 16.279  -25.400 1.00 47.80  ? 168 PHE A CB  1 
ATOM   1215 C CG  . PHE A 1 168 ? 25.036 17.340  -26.169 1.00 49.22  ? 168 PHE A CG  1 
ATOM   1216 C CD1 . PHE A 1 168 ? 24.908 17.425  -27.547 1.00 52.67  ? 168 PHE A CD1 1 
ATOM   1217 C CD2 . PHE A 1 168 ? 25.825 18.267  -25.524 1.00 50.67  ? 168 PHE A CD2 1 
ATOM   1218 C CE1 . PHE A 1 168 ? 25.569 18.412  -28.262 1.00 55.35  ? 168 PHE A CE1 1 
ATOM   1219 C CE2 . PHE A 1 168 ? 26.483 19.256  -26.242 1.00 53.31  ? 168 PHE A CE2 1 
ATOM   1220 C CZ  . PHE A 1 168 ? 26.347 19.334  -27.608 1.00 52.25  ? 168 PHE A CZ  1 
ATOM   1221 N N   . ILE A 1 169 ? 21.810 14.246  -25.188 1.00 52.56  ? 169 ILE A N   1 
ATOM   1222 C CA  . ILE A 1 169 ? 21.140 13.126  -24.480 1.00 51.74  ? 169 ILE A CA  1 
ATOM   1223 C C   . ILE A 1 169 ? 22.019 11.879  -24.621 1.00 58.86  ? 169 ILE A C   1 
ATOM   1224 O O   . ILE A 1 169 ? 22.271 11.436  -25.768 1.00 63.85  ? 169 ILE A O   1 
ATOM   1225 C CB  . ILE A 1 169 ? 19.720 12.948  -25.041 1.00 51.87  ? 169 ILE A CB  1 
ATOM   1226 C CG1 . ILE A 1 169 ? 18.924 14.250  -24.897 1.00 54.78  ? 169 ILE A CG1 1 
ATOM   1227 C CG2 . ILE A 1 169 ? 19.028 11.772  -24.375 1.00 50.59  ? 169 ILE A CG2 1 
ATOM   1228 C CD1 . ILE A 1 169 ? 17.517 14.197  -25.432 1.00 59.95  ? 169 ILE A CD1 1 
ATOM   1229 N N   . THR A 1 170 ? 22.485 11.363  -23.484 1.00 58.07  ? 170 THR A N   1 
ATOM   1230 C CA  . THR A 1 170 ? 23.208 10.071  -23.347 1.00 64.44  ? 170 THR A CA  1 
ATOM   1231 C C   . THR A 1 170 ? 22.244 8.901   -23.627 1.00 70.10  ? 170 THR A C   1 
ATOM   1232 O O   . THR A 1 170 ? 21.014 9.095   -23.509 1.00 65.66  ? 170 THR A O   1 
ATOM   1233 C CB  . THR A 1 170 ? 23.849 9.943   -21.957 1.00 63.42  ? 170 THR A CB  1 
ATOM   1234 O OG1 . THR A 1 170 ? 22.801 9.761   -21.000 1.00 64.57  ? 170 THR A OG1 1 
ATOM   1235 C CG2 . THR A 1 170 ? 24.723 11.122  -21.572 1.00 61.28  ? 170 THR A CG2 1 
ATOM   1236 N N   . ALA A 1 171 ? 22.794 7.732   -23.987 1.00 74.70  ? 171 ALA A N   1 
ATOM   1237 C CA  . ALA A 1 171 ? 22.103 6.421   -24.122 1.00 73.09  ? 171 ALA A CA  1 
ATOM   1238 C C   . ALA A 1 171 ? 21.077 6.191   -22.998 1.00 75.34  ? 171 ALA A C   1 
ATOM   1239 O O   . ALA A 1 171 ? 19.938 5.810   -23.327 1.00 68.45  ? 171 ALA A O   1 
ATOM   1240 C CB  . ALA A 1 171 ? 23.134 5.324   -24.115 1.00 74.67  ? 171 ALA A CB  1 
ATOM   1241 N N   . THR A 1 172 ? 21.462 6.415   -21.731 1.00 71.82  ? 172 THR A N   1 
ATOM   1242 C CA  . THR A 1 172 ? 20.593 6.263   -20.529 1.00 79.13  ? 172 THR A CA  1 
ATOM   1243 C C   . THR A 1 172 ? 19.490 7.343   -20.472 1.00 79.46  ? 172 THR A C   1 
ATOM   1244 O O   . THR A 1 172 ? 18.630 7.249   -19.583 1.00 82.43  ? 172 THR A O   1 
ATOM   1245 C CB  . THR A 1 172 ? 21.424 6.287   -19.240 1.00 81.25  ? 172 THR A CB  1 
ATOM   1246 O OG1 . THR A 1 172 ? 22.204 7.480   -19.185 1.00 88.35  ? 172 THR A OG1 1 
ATOM   1247 C CG2 . THR A 1 172 ? 22.382 5.126   -19.130 1.00 87.83  ? 172 THR A CG2 1 
ATOM   1248 N N   . GLY A 1 173 ? 19.509 8.353   -21.347 1.00 70.01  ? 173 GLY A N   1 
ATOM   1249 C CA  . GLY A 1 173 ? 18.516 9.445   -21.334 1.00 66.12  ? 173 GLY A CA  1 
ATOM   1250 C C   . GLY A 1 173 ? 18.838 10.521  -20.300 1.00 63.09  ? 173 GLY A C   1 
ATOM   1251 O O   . GLY A 1 173 ? 17.914 11.200  -19.845 1.00 63.33  ? 173 GLY A O   1 
ATOM   1252 N N   . VAL A 1 174 ? 20.104 10.679  -19.922 1.00 58.18  ? 174 VAL A N   1 
ATOM   1253 C CA  . VAL A 1 174 ? 20.568 11.830  -19.105 1.00 58.56  ? 174 VAL A CA  1 
ATOM   1254 C C   . VAL A 1 174 ? 20.819 13.005  -20.061 1.00 58.57  ? 174 VAL A C   1 
ATOM   1255 O O   . VAL A 1 174 ? 21.637 12.850  -20.989 1.00 52.95  ? 174 VAL A O   1 
ATOM   1256 C CB  . VAL A 1 174 ? 21.827 11.486  -18.290 1.00 54.08  ? 174 VAL A CB  1 
ATOM   1257 C CG1 . VAL A 1 174 ? 22.315 12.678  -17.479 1.00 51.70  ? 174 VAL A CG1 1 
ATOM   1258 C CG2 . VAL A 1 174 ? 21.597 10.288  -17.388 1.00 57.65  ? 174 VAL A CG2 1 
ATOM   1259 N N   . VAL A 1 175 ? 20.150 14.135  -19.820 1.00 50.01  ? 175 VAL A N   1 
ATOM   1260 C CA  . VAL A 1 175 ? 20.382 15.427  -20.530 1.00 45.77  ? 175 VAL A CA  1 
ATOM   1261 C C   . VAL A 1 175 ? 21.758 15.968  -20.138 1.00 41.18  ? 175 VAL A C   1 
ATOM   1262 O O   . VAL A 1 175 ? 22.086 15.969  -18.934 1.00 42.66  ? 175 VAL A O   1 
ATOM   1263 C CB  . VAL A 1 175 ? 19.262 16.426  -20.192 1.00 44.87  ? 175 VAL A CB  1 
ATOM   1264 C CG1 . VAL A 1 175 ? 19.568 17.833  -20.680 1.00 44.85  ? 175 VAL A CG1 1 
ATOM   1265 C CG2 . VAL A 1 175 ? 17.922 15.944  -20.711 1.00 42.85  ? 175 VAL A CG2 1 
ATOM   1266 N N   . LYS A 1 176 ? 22.541 16.404  -21.121 1.00 41.18  ? 176 LYS A N   1 
ATOM   1267 C CA  . LYS A 1 176 ? 23.815 17.135  -20.891 1.00 39.40  ? 176 LYS A CA  1 
ATOM   1268 C C   . LYS A 1 176 ? 23.760 18.470  -21.648 1.00 40.34  ? 176 LYS A C   1 
ATOM   1269 O O   . LYS A 1 176 ? 23.892 18.478  -22.898 1.00 37.46  ? 176 LYS A O   1 
ATOM   1270 C CB  . LYS A 1 176 ? 24.997 16.285  -21.346 1.00 39.55  ? 176 LYS A CB  1 
ATOM   1271 C CG  . LYS A 1 176 ? 25.210 14.975  -20.605 1.00 42.94  ? 176 LYS A CG  1 
ATOM   1272 C CD  . LYS A 1 176 ? 25.932 15.112  -19.301 1.00 47.61  ? 176 LYS A CD  1 
ATOM   1273 C CE  . LYS A 1 176 ? 25.941 13.818  -18.520 1.00 48.06  ? 176 LYS A CE  1 
ATOM   1274 N NZ  . LYS A 1 176 ? 26.776 13.930  -17.307 1.00 49.47  ? 176 LYS A NZ  1 
ATOM   1275 N N   . LEU A 1 177 ? 23.556 19.574  -20.932 1.00 41.10  ? 177 LEU A N   1 
ATOM   1276 C CA  . LEU A 1 177 ? 23.547 20.932  -21.541 1.00 40.07  ? 177 LEU A CA  1 
ATOM   1277 C C   . LEU A 1 177 ? 24.992 21.320  -21.850 1.00 43.39  ? 177 LEU A C   1 
ATOM   1278 O O   . LEU A 1 177 ? 25.791 21.438  -20.892 1.00 38.35  ? 177 LEU A O   1 
ATOM   1279 C CB  . LEU A 1 177 ? 22.887 21.938  -20.600 1.00 40.07  ? 177 LEU A CB  1 
ATOM   1280 C CG  . LEU A 1 177 ? 22.838 23.382  -21.103 1.00 42.05  ? 177 LEU A CG  1 
ATOM   1281 C CD1 . LEU A 1 177 ? 22.015 23.496  -22.383 1.00 38.99  ? 177 LEU A CD1 1 
ATOM   1282 C CD2 . LEU A 1 177 ? 22.268 24.301  -20.037 1.00 38.92  ? 177 LEU A CD2 1 
ATOM   1283 N N   . GLY A 1 178 ? 25.332 21.448  -23.138 1.00 42.96  ? 178 GLY A N   1 
ATOM   1284 C CA  . GLY A 1 178 ? 26.659 21.943  -23.556 1.00 45.04  ? 178 GLY A CA  1 
ATOM   1285 C C   . GLY A 1 178 ? 26.576 23.179  -24.444 1.00 46.96  ? 178 GLY A C   1 
ATOM   1286 O O   . GLY A 1 178 ? 25.529 23.860  -24.449 1.00 45.16  ? 178 GLY A O   1 
ATOM   1287 N N   . ASP A 1 179 ? 27.655 23.446  -25.185 1.00 48.11  ? 179 ASP A N   1 
ATOM   1288 C CA  . ASP A 1 179 ? 27.811 24.624  -26.076 1.00 52.54  ? 179 ASP A CA  1 
ATOM   1289 C C   . ASP A 1 179 ? 28.904 24.297  -27.108 1.00 58.08  ? 179 ASP A C   1 
ATOM   1290 O O   . ASP A 1 179 ? 30.069 24.586  -26.832 1.00 60.47  ? 179 ASP A O   1 
ATOM   1291 C CB  . ASP A 1 179 ? 28.060 25.879  -25.231 1.00 54.99  ? 179 ASP A CB  1 
ATOM   1292 C CG  . ASP A 1 179 ? 28.200 27.167  -26.033 1.00 65.91  ? 179 ASP A CG  1 
ATOM   1293 O OD1 . ASP A 1 179 ? 27.769 27.158  -27.221 1.00 62.15  ? 179 ASP A OD1 1 
ATOM   1294 O OD2 . ASP A 1 179 ? 28.762 28.178  -25.469 1.00 60.04  ? 179 ASP A OD2 1 
ATOM   1295 N N   . LEU A 1 180 ? 28.538 23.679  -28.242 1.00 64.96  ? 180 LEU A N   1 
ATOM   1296 C CA  . LEU A 1 180 ? 29.477 23.349  -29.349 1.00 74.19  ? 180 LEU A CA  1 
ATOM   1297 C C   . LEU A 1 180 ? 29.939 24.634  -30.046 1.00 82.04  ? 180 LEU A C   1 
ATOM   1298 O O   . LEU A 1 180 ? 29.122 25.287  -30.730 1.00 76.13  ? 180 LEU A O   1 
ATOM   1299 C CB  . LEU A 1 180 ? 28.815 22.400  -30.350 1.00 74.02  ? 180 LEU A CB  1 
ATOM   1300 C CG  . LEU A 1 180 ? 28.838 20.927  -29.946 1.00 79.87  ? 180 LEU A CG  1 
ATOM   1301 C CD1 . LEU A 1 180 ? 28.216 20.054  -31.031 1.00 85.39  ? 180 LEU A CD1 1 
ATOM   1302 C CD2 . LEU A 1 180 ? 30.250 20.464  -29.622 1.00 72.42  ? 180 LEU A CD2 1 
ATOM   1303 N N   . GLY A 1 181 ? 31.217 24.970  -29.862 1.00 94.86  ? 181 GLY A N   1 
ATOM   1304 C CA  . GLY A 1 181 ? 31.872 26.132  -30.487 1.00 101.59 ? 181 GLY A CA  1 
ATOM   1305 C C   . GLY A 1 181 ? 31.541 27.403  -29.733 1.00 103.33 ? 181 GLY A C   1 
ATOM   1306 O O   . GLY A 1 181 ? 31.227 28.411  -30.397 1.00 112.41 ? 181 GLY A O   1 
ATOM   1307 N N   . LEU A 1 182 ? 31.585 27.341  -28.397 1.00 96.79  ? 182 LEU A N   1 
ATOM   1308 C CA  . LEU A 1 182 ? 31.488 28.507  -27.478 1.00 98.08  ? 182 LEU A CA  1 
ATOM   1309 C C   . LEU A 1 182 ? 30.820 29.694  -28.196 1.00 96.07  ? 182 LEU A C   1 
ATOM   1310 O O   . LEU A 1 182 ? 31.492 30.740  -28.373 1.00 88.09  ? 182 LEU A O   1 
ATOM   1311 C CB  . LEU A 1 182 ? 32.894 28.873  -26.988 1.00 97.00  ? 182 LEU A CB  1 
ATOM   1312 C CG  . LEU A 1 182 ? 33.638 27.804  -26.189 1.00 97.01  ? 182 LEU A CG  1 
ATOM   1313 C CD1 . LEU A 1 182 ? 35.096 28.194  -26.012 1.00 105.80 ? 182 LEU A CD1 1 
ATOM   1314 C CD2 . LEU A 1 182 ? 32.994 27.577  -24.831 1.00 97.21  ? 182 LEU A CD2 1 
ATOM   1315 N N   . GLY A 1 183 ? 29.543 29.539  -28.577 1.00 95.26  ? 183 GLY A N   1 
ATOM   1316 C CA  . GLY A 1 183 ? 28.671 30.615  -29.100 1.00 93.90  ? 183 GLY A CA  1 
ATOM   1317 C C   . GLY A 1 183 ? 28.302 31.646  -28.034 1.00 89.26  ? 183 GLY A C   1 
ATOM   1318 O O   . GLY A 1 183 ? 27.474 32.534  -28.345 1.00 77.31  ? 183 GLY A O   1 
ATOM   1319 N N   . ARG A 1 184 ? 28.923 31.555  -26.844 1.00 88.31  ? 184 ARG A N   1 
ATOM   1320 C CA  . ARG A 1 184 ? 28.686 32.416  -25.649 1.00 94.79  ? 184 ARG A CA  1 
ATOM   1321 C C   . ARG A 1 184 ? 29.520 33.710  -25.727 1.00 101.00 ? 184 ARG A C   1 
ATOM   1322 O O   . ARG A 1 184 ? 29.261 34.622  -24.906 1.00 87.61  ? 184 ARG A O   1 
ATOM   1323 C CB  . ARG A 1 184 ? 28.975 31.638  -24.352 1.00 86.68  ? 184 ARG A CB  1 
ATOM   1324 C CG  . ARG A 1 184 ? 30.433 31.248  -24.108 1.00 80.56  ? 184 ARG A CG  1 
ATOM   1325 C CD  . ARG A 1 184 ? 30.683 30.700  -22.703 1.00 79.22  ? 184 ARG A CD  1 
ATOM   1326 N NE  . ARG A 1 184 ? 30.319 31.622  -21.612 1.00 77.36  ? 184 ARG A NE  1 
ATOM   1327 C CZ  . ARG A 1 184 ? 29.218 31.558  -20.842 1.00 66.34  ? 184 ARG A CZ  1 
ATOM   1328 N NH1 . ARG A 1 184 ? 29.018 32.468  -19.901 1.00 55.54  ? 184 ARG A NH1 1 
ATOM   1329 N NH2 . ARG A 1 184 ? 28.309 30.609  -21.019 1.00 69.19  ? 184 ARG A NH2 1 
ATOM   1330 N N   . PHE A 1 185 ? 30.475 33.794  -26.663 1.00 112.14 ? 185 PHE A N   1 
ATOM   1331 C CA  . PHE A 1 185 ? 31.418 34.938  -26.817 1.00 117.69 ? 185 PHE A CA  1 
ATOM   1332 C C   . PHE A 1 185 ? 31.062 35.787  -28.053 1.00 118.11 ? 185 PHE A C   1 
ATOM   1333 O O   . PHE A 1 185 ? 31.582 36.919  -28.143 1.00 122.61 ? 185 PHE A O   1 
ATOM   1334 C CB  . PHE A 1 185 ? 32.860 34.419  -26.861 1.00 111.89 ? 185 PHE A CB  1 
ATOM   1335 C CG  . PHE A 1 185 ? 33.248 33.543  -25.693 1.00 98.48  ? 185 PHE A CG  1 
ATOM   1336 C CD1 . PHE A 1 185 ? 33.298 34.057  -24.406 1.00 90.33  ? 185 PHE A CD1 1 
ATOM   1337 C CD2 . PHE A 1 185 ? 33.568 32.207  -25.880 1.00 96.67  ? 185 PHE A CD2 1 
ATOM   1338 C CE1 . PHE A 1 185 ? 33.660 33.255  -23.335 1.00 89.33  ? 185 PHE A CE1 1 
ATOM   1339 C CE2 . PHE A 1 185 ? 33.926 31.406  -24.806 1.00 94.10  ? 185 PHE A CE2 1 
ATOM   1340 C CZ  . PHE A 1 185 ? 33.969 31.930  -23.536 1.00 91.03  ? 185 PHE A CZ  1 
ATOM   1341 N N   . PHE A 1 186 ? 30.195 35.285  -28.945 1.00 116.92 ? 186 PHE A N   1 
ATOM   1342 C CA  . PHE A 1 186 ? 29.817 35.908  -30.247 1.00 119.31 ? 186 PHE A CA  1 
ATOM   1343 C C   . PHE A 1 186 ? 29.490 37.399  -30.065 1.00 108.72 ? 186 PHE A C   1 
ATOM   1344 O O   . PHE A 1 186 ? 30.230 38.230  -30.646 1.00 84.79  ? 186 PHE A O   1 
ATOM   1345 C CB  . PHE A 1 186 ? 28.631 35.161  -30.867 1.00 115.46 ? 186 PHE A CB  1 
ATOM   1346 N N   . PRO A 1 200 ? 20.689 34.579  -34.046 1.00 92.48  ? 200 PRO A N   1 
ATOM   1347 C CA  . PRO A 1 200 ? 20.697 33.356  -33.228 1.00 87.08  ? 200 PRO A CA  1 
ATOM   1348 C C   . PRO A 1 200 ? 19.564 32.380  -33.620 1.00 81.54  ? 200 PRO A C   1 
ATOM   1349 O O   . PRO A 1 200 ? 18.642 32.769  -34.367 1.00 68.54  ? 200 PRO A O   1 
ATOM   1350 C CB  . PRO A 1 200 ? 20.561 33.910  -31.790 1.00 84.30  ? 200 PRO A CB  1 
ATOM   1351 C CG  . PRO A 1 200 ? 19.772 35.203  -31.931 1.00 85.64  ? 200 PRO A CG  1 
ATOM   1352 C CD  . PRO A 1 200 ? 19.757 35.529  -33.416 1.00 89.32  ? 200 PRO A CD  1 
ATOM   1353 N N   . TYR A 1 201 ? 19.638 31.136  -33.130 1.00 74.32  ? 201 TYR A N   1 
ATOM   1354 C CA  . TYR A 1 201 ? 18.552 30.123  -33.264 1.00 76.08  ? 201 TYR A CA  1 
ATOM   1355 C C   . TYR A 1 201 ? 17.238 30.743  -32.759 1.00 70.81  ? 201 TYR A C   1 
ATOM   1356 O O   . TYR A 1 201 ? 16.225 30.763  -33.501 1.00 68.62  ? 201 TYR A O   1 
ATOM   1357 C CB  . TYR A 1 201 ? 18.885 28.821  -32.523 1.00 72.36  ? 201 TYR A CB  1 
ATOM   1358 C CG  . TYR A 1 201 ? 17.977 27.659  -32.865 1.00 68.91  ? 201 TYR A CG  1 
ATOM   1359 C CD1 . TYR A 1 201 ? 18.245 26.828  -33.950 1.00 70.67  ? 201 TYR A CD1 1 
ATOM   1360 C CD2 . TYR A 1 201 ? 16.838 27.397  -32.115 1.00 56.48  ? 201 TYR A CD2 1 
ATOM   1361 C CE1 . TYR A 1 201 ? 17.399 25.778  -34.285 1.00 69.39  ? 201 TYR A CE1 1 
ATOM   1362 C CE2 . TYR A 1 201 ? 15.991 26.345  -32.427 1.00 62.29  ? 201 TYR A CE2 1 
ATOM   1363 C CZ  . TYR A 1 201 ? 16.268 25.535  -33.517 1.00 71.74  ? 201 TYR A CZ  1 
ATOM   1364 O OH  . TYR A 1 201 ? 15.426 24.502  -33.808 1.00 63.43  ? 201 TYR A OH  1 
ATOM   1365 N N   . TYR A 1 202 ? 17.259 31.272  -31.537 1.00 61.45  ? 202 TYR A N   1 
ATOM   1366 C CA  . TYR A 1 202 ? 16.120 32.020  -30.957 1.00 60.39  ? 202 TYR A CA  1 
ATOM   1367 C C   . TYR A 1 202 ? 16.451 33.512  -30.883 1.00 66.96  ? 202 TYR A C   1 
ATOM   1368 O O   . TYR A 1 202 ? 17.044 33.971  -29.864 1.00 58.65  ? 202 TYR A O   1 
ATOM   1369 C CB  . TYR A 1 202 ? 15.774 31.473  -29.581 1.00 57.73  ? 202 TYR A CB  1 
ATOM   1370 C CG  . TYR A 1 202 ? 15.376 30.024  -29.601 1.00 62.22  ? 202 TYR A CG  1 
ATOM   1371 C CD1 . TYR A 1 202 ? 14.364 29.566  -30.430 1.00 60.94  ? 202 TYR A CD1 1 
ATOM   1372 C CD2 . TYR A 1 202 ? 16.026 29.109  -28.796 1.00 59.76  ? 202 TYR A CD2 1 
ATOM   1373 C CE1 . TYR A 1 202 ? 14.008 28.228  -30.453 1.00 58.98  ? 202 TYR A CE1 1 
ATOM   1374 C CE2 . TYR A 1 202 ? 15.661 27.775  -28.785 1.00 60.88  ? 202 TYR A CE2 1 
ATOM   1375 C CZ  . TYR A 1 202 ? 14.650 27.333  -29.613 1.00 59.15  ? 202 TYR A CZ  1 
ATOM   1376 O OH  . TYR A 1 202 ? 14.297 26.017  -29.568 1.00 53.00  ? 202 TYR A OH  1 
ATOM   1377 N N   . MET A 1 203 ? 16.048 34.249  -31.927 1.00 68.88  ? 203 MET A N   1 
ATOM   1378 C CA  . MET A 1 203 ? 15.942 35.736  -31.890 1.00 76.82  ? 203 MET A CA  1 
ATOM   1379 C C   . MET A 1 203 ? 15.078 36.119  -30.673 1.00 60.51  ? 203 MET A C   1 
ATOM   1380 O O   . MET A 1 203 ? 13.926 35.676  -30.608 1.00 62.92  ? 203 MET A O   1 
ATOM   1381 C CB  . MET A 1 203 ? 15.349 36.279  -33.200 1.00 85.09  ? 203 MET A CB  1 
ATOM   1382 C CG  . MET A 1 203 ? 15.603 37.770  -33.457 1.00 89.45  ? 203 MET A CG  1 
ATOM   1383 S SD  . MET A 1 203 ? 17.308 38.193  -33.974 1.00 101.02 ? 203 MET A SD  1 
ATOM   1384 C CE  . MET A 1 203 ? 17.248 37.869  -35.738 1.00 106.99 ? 203 MET A CE  1 
ATOM   1385 N N   . SER A 1 204 ? 15.684 36.777  -29.686 1.00 63.17  ? 204 SER A N   1 
ATOM   1386 C CA  . SER A 1 204 ? 15.039 37.378  -28.485 1.00 67.79  ? 204 SER A CA  1 
ATOM   1387 C C   . SER A 1 204 ? 14.798 38.869  -28.726 1.00 70.55  ? 204 SER A C   1 
ATOM   1388 O O   . SER A 1 204 ? 15.513 39.486  -29.518 1.00 74.82  ? 204 SER A O   1 
ATOM   1389 C CB  . SER A 1 204 ? 15.936 37.242  -27.329 1.00 59.27  ? 204 SER A CB  1 
ATOM   1390 O OG  . SER A 1 204 ? 17.112 37.981  -27.621 1.00 55.61  ? 204 SER A OG  1 
ATOM   1391 N N   . PRO A 1 205 ? 13.847 39.525  -28.024 1.00 56.13  ? 205 PRO A N   1 
ATOM   1392 C CA  . PRO A 1 205 ? 13.680 40.968  -28.160 1.00 55.13  ? 205 PRO A CA  1 
ATOM   1393 C C   . PRO A 1 205 ? 14.978 41.729  -27.851 1.00 60.57  ? 205 PRO A C   1 
ATOM   1394 O O   . PRO A 1 205 ? 15.210 42.702  -28.513 1.00 65.88  ? 205 PRO A O   1 
ATOM   1395 C CB  . PRO A 1 205 ? 12.572 41.315  -27.166 1.00 55.82  ? 205 PRO A CB  1 
ATOM   1396 C CG  . PRO A 1 205 ? 11.830 40.011  -26.988 1.00 55.50  ? 205 PRO A CG  1 
ATOM   1397 C CD  . PRO A 1 205 ? 12.886 38.931  -27.096 1.00 55.29  ? 205 PRO A CD  1 
ATOM   1398 N N   . GLU A 1 206 ? 15.822 41.253  -26.924 1.00 63.89  ? 206 GLU A N   1 
ATOM   1399 C CA  . GLU A 1 206 ? 17.047 41.993  -26.496 1.00 66.27  ? 206 GLU A CA  1 
ATOM   1400 C C   . GLU A 1 206 ? 18.182 41.776  -27.502 1.00 75.56  ? 206 GLU A C   1 
ATOM   1401 O O   . GLU A 1 206 ? 19.312 42.218  -27.208 1.00 91.56  ? 206 GLU A O   1 
ATOM   1402 C CB  . GLU A 1 206 ? 17.480 41.655  -25.060 1.00 65.07  ? 206 GLU A CB  1 
ATOM   1403 C CG  . GLU A 1 206 ? 17.497 40.181  -24.704 1.00 67.79  ? 206 GLU A CG  1 
ATOM   1404 C CD  . GLU A 1 206 ? 16.243 39.685  -24.002 1.00 62.63  ? 206 GLU A CD  1 
ATOM   1405 O OE1 . GLU A 1 206 ? 15.149 39.823  -24.589 1.00 60.91  ? 206 GLU A OE1 1 
ATOM   1406 O OE2 . GLU A 1 206 ? 16.359 39.179  -22.867 1.00 56.04  ? 206 GLU A OE2 1 
ATOM   1407 N N   . ARG A 1 207 ? 17.900 41.127  -28.635 1.00 85.44  ? 207 ARG A N   1 
ATOM   1408 C CA  . ARG A 1 207 ? 18.777 41.083  -29.838 1.00 85.21  ? 207 ARG A CA  1 
ATOM   1409 C C   . ARG A 1 207 ? 18.226 42.065  -30.881 1.00 79.48  ? 207 ARG A C   1 
ATOM   1410 O O   . ARG A 1 207 ? 19.020 42.804  -31.479 1.00 70.56  ? 207 ARG A O   1 
ATOM   1411 C CB  . ARG A 1 207 ? 18.843 39.658  -30.391 1.00 92.99  ? 207 ARG A CB  1 
ATOM   1412 C CG  . ARG A 1 207 ? 19.962 39.438  -31.396 1.00 109.53 ? 207 ARG A CG  1 
ATOM   1413 C CD  . ARG A 1 207 ? 21.335 39.317  -30.756 1.00 124.89 ? 207 ARG A CD  1 
ATOM   1414 N NE  . ARG A 1 207 ? 22.372 39.514  -31.765 1.00 142.02 ? 207 ARG A NE  1 
ATOM   1415 C CZ  . ARG A 1 207 ? 22.925 40.685  -32.097 1.00 148.70 ? 207 ARG A CZ  1 
ATOM   1416 N NH1 . ARG A 1 207 ? 22.577 41.809  -31.485 1.00 143.97 ? 207 ARG A NH1 1 
ATOM   1417 N NH2 . ARG A 1 207 ? 23.845 40.720  -33.047 1.00 148.45 ? 207 ARG A NH2 1 
ATOM   1418 N N   . ILE A 1 208 ? 16.902 42.104  -31.051 1.00 77.08  ? 208 ILE A N   1 
ATOM   1419 C CA  . ILE A 1 208 ? 16.185 43.066  -31.946 1.00 74.13  ? 208 ILE A CA  1 
ATOM   1420 C C   . ILE A 1 208 ? 16.418 44.513  -31.492 1.00 71.13  ? 208 ILE A C   1 
ATOM   1421 O O   . ILE A 1 208 ? 16.475 45.383  -32.364 1.00 74.22  ? 208 ILE A O   1 
ATOM   1422 C CB  . ILE A 1 208 ? 14.689 42.717  -32.030 1.00 68.17  ? 208 ILE A CB  1 
ATOM   1423 C CG1 . ILE A 1 208 ? 14.482 41.557  -33.010 1.00 64.04  ? 208 ILE A CG1 1 
ATOM   1424 C CG2 . ILE A 1 208 ? 13.855 43.945  -32.388 1.00 61.65  ? 208 ILE A CG2 1 
ATOM   1425 C CD1 . ILE A 1 208 ? 13.093 40.954  -32.982 1.00 69.22  ? 208 ILE A CD1 1 
ATOM   1426 N N   . HIS A 1 209 ? 16.527 44.762  -30.186 1.00 76.53  ? 209 HIS A N   1 
ATOM   1427 C CA  . HIS A 1 209 ? 16.877 46.083  -29.591 1.00 76.14  ? 209 HIS A CA  1 
ATOM   1428 C C   . HIS A 1 209 ? 18.401 46.165  -29.357 1.00 74.77  ? 209 HIS A C   1 
ATOM   1429 O O   . HIS A 1 209 ? 18.832 47.162  -28.774 1.00 77.24  ? 209 HIS A O   1 
ATOM   1430 C CB  . HIS A 1 209 ? 16.056 46.324  -28.308 1.00 77.60  ? 209 HIS A CB  1 
ATOM   1431 C CG  . HIS A 1 209 ? 14.570 46.381  -28.489 1.00 84.30  ? 209 HIS A CG  1 
ATOM   1432 N ND1 . HIS A 1 209 ? 13.795 45.257  -28.739 1.00 94.58  ? 209 HIS A ND1 1 
ATOM   1433 C CD2 . HIS A 1 209 ? 13.697 47.410  -28.387 1.00 90.99  ? 209 HIS A CD2 1 
ATOM   1434 C CE1 . HIS A 1 209 ? 12.519 45.595  -28.807 1.00 92.66  ? 209 HIS A CE1 1 
ATOM   1435 N NE2 . HIS A 1 209 ? 12.431 46.910  -28.590 1.00 93.82  ? 209 HIS A NE2 1 
ATOM   1436 N N   . GLU A 1 210 ? 19.170 45.146  -29.781 1.00 82.92  ? 210 GLU A N   1 
ATOM   1437 C CA  . GLU A 1 210 ? 20.669 45.032  -29.768 1.00 91.87  ? 210 GLU A CA  1 
ATOM   1438 C C   . GLU A 1 210 ? 21.231 45.031  -28.330 1.00 86.13  ? 210 GLU A C   1 
ATOM   1439 O O   . GLU A 1 210 ? 22.307 44.391  -28.133 1.00 92.30  ? 210 GLU A O   1 
ATOM   1440 C CB  . GLU A 1 210 ? 21.304 46.061  -30.716 1.00 99.17  ? 210 GLU A CB  1 
ATOM   1441 C CG  . GLU A 1 210 ? 21.716 45.442  -32.057 1.00 109.10 ? 210 GLU A CG  1 
ATOM   1442 C CD  . GLU A 1 210 ? 21.853 46.370  -33.261 1.00 117.22 ? 210 GLU A CD  1 
ATOM   1443 O OE1 . GLU A 1 210 ? 22.512 47.420  -33.124 1.00 117.73 ? 210 GLU A OE1 1 
ATOM   1444 O OE2 . GLU A 1 210 ? 21.308 46.033  -34.346 1.00 109.27 ? 210 GLU A OE2 1 
ATOM   1445 N N   . ASN A 1 211 ? 20.561 45.748  -27.413 1.00 67.93  ? 211 ASN A N   1 
ATOM   1446 C CA  . ASN A 1 211 ? 20.437 45.604  -25.924 1.00 73.99  ? 211 ASN A CA  1 
ATOM   1447 C C   . ASN A 1 211 ? 21.295 44.546  -25.194 1.00 76.47  ? 211 ASN A C   1 
ATOM   1448 O O   . ASN A 1 211 ? 21.369 44.677  -23.957 1.00 68.98  ? 211 ASN A O   1 
ATOM   1449 C CB  . ASN A 1 211 ? 18.992 45.275  -25.529 1.00 69.82  ? 211 ASN A CB  1 
ATOM   1450 C CG  . ASN A 1 211 ? 18.209 46.482  -25.064 1.00 67.20  ? 211 ASN A CG  1 
ATOM   1451 O OD1 . ASN A 1 211 ? 18.759 47.569  -24.932 1.00 73.20  ? 211 ASN A OD1 1 
ATOM   1452 N ND2 . ASN A 1 211 ? 16.922 46.302  -24.825 1.00 68.36  ? 211 ASN A ND2 1 
ATOM   1453 N N   . GLY A 1 212 ? 21.826 43.496  -25.835 1.00 81.15  ? 212 GLY A N   1 
ATOM   1454 C CA  . GLY A 1 212 ? 22.755 42.548  -25.179 1.00 82.01  ? 212 GLY A CA  1 
ATOM   1455 C C   . GLY A 1 212 ? 22.058 41.553  -24.250 1.00 78.81  ? 212 GLY A C   1 
ATOM   1456 O O   . GLY A 1 212 ? 20.843 41.661  -24.030 1.00 83.52  ? 212 GLY A O   1 
ATOM   1457 N N   . TYR A 1 213 ? 22.824 40.624  -23.683 1.00 73.60  ? 213 TYR A N   1 
ATOM   1458 C CA  . TYR A 1 213 ? 22.343 39.321  -23.156 1.00 70.07  ? 213 TYR A CA  1 
ATOM   1459 C C   . TYR A 1 213 ? 22.457 39.266  -21.626 1.00 59.07  ? 213 TYR A C   1 
ATOM   1460 O O   . TYR A 1 213 ? 23.528 39.572  -21.087 1.00 55.89  ? 213 TYR A O   1 
ATOM   1461 C CB  . TYR A 1 213 ? 23.140 38.207  -23.837 1.00 72.86  ? 213 TYR A CB  1 
ATOM   1462 C CG  . TYR A 1 213 ? 22.489 36.851  -23.811 1.00 75.64  ? 213 TYR A CG  1 
ATOM   1463 C CD1 . TYR A 1 213 ? 22.617 36.040  -22.693 1.00 75.97  ? 213 TYR A CD1 1 
ATOM   1464 C CD2 . TYR A 1 213 ? 21.759 36.370  -24.894 1.00 65.78  ? 213 TYR A CD2 1 
ATOM   1465 C CE1 . TYR A 1 213 ? 22.030 34.786  -22.641 1.00 74.82  ? 213 TYR A CE1 1 
ATOM   1466 C CE2 . TYR A 1 213 ? 21.172 35.112  -24.859 1.00 72.64  ? 213 TYR A CE2 1 
ATOM   1467 C CZ  . TYR A 1 213 ? 21.307 34.317  -23.726 1.00 73.43  ? 213 TYR A CZ  1 
ATOM   1468 O OH  . TYR A 1 213 ? 20.747 33.072  -23.649 1.00 72.98  ? 213 TYR A OH  1 
ATOM   1469 N N   . ASN A 1 214 ? 21.385 38.857  -20.937 1.00 59.26  ? 214 ASN A N   1 
ATOM   1470 C CA  . ASN A 1 214 ? 21.427 38.582  -19.476 1.00 56.09  ? 214 ASN A CA  1 
ATOM   1471 C C   . ASN A 1 214 ? 20.723 37.251  -19.133 1.00 50.42  ? 214 ASN A C   1 
ATOM   1472 O O   . ASN A 1 214 ? 20.223 36.541  -20.034 1.00 47.44  ? 214 ASN A O   1 
ATOM   1473 C CB  . ASN A 1 214 ? 20.887 39.783  -18.700 1.00 58.65  ? 214 ASN A CB  1 
ATOM   1474 C CG  . ASN A 1 214 ? 19.422 40.060  -18.947 1.00 64.16  ? 214 ASN A CG  1 
ATOM   1475 O OD1 . ASN A 1 214 ? 18.632 39.151  -19.178 1.00 69.64  ? 214 ASN A OD1 1 
ATOM   1476 N ND2 . ASN A 1 214 ? 19.040 41.324  -18.878 1.00 78.70  ? 214 ASN A ND2 1 
ATOM   1477 N N   . PHE A 1 215 ? 20.627 36.968  -17.841 1.00 44.05  ? 215 PHE A N   1 
ATOM   1478 C CA  . PHE A 1 215 ? 20.101 35.717  -17.248 1.00 47.62  ? 215 PHE A CA  1 
ATOM   1479 C C   . PHE A 1 215 ? 18.698 35.439  -17.780 1.00 42.60  ? 215 PHE A C   1 
ATOM   1480 O O   . PHE A 1 215 ? 18.399 34.272  -18.096 1.00 38.17  ? 215 PHE A O   1 
ATOM   1481 C CB  . PHE A 1 215 ? 20.154 35.793  -15.713 1.00 46.48  ? 215 PHE A CB  1 
ATOM   1482 C CG  . PHE A 1 215 ? 21.569 35.729  -15.194 1.00 46.30  ? 215 PHE A CG  1 
ATOM   1483 C CD1 . PHE A 1 215 ? 22.240 34.520  -15.144 1.00 45.88  ? 215 PHE A CD1 1 
ATOM   1484 C CD2 . PHE A 1 215 ? 22.247 36.874  -14.804 1.00 48.24  ? 215 PHE A CD2 1 
ATOM   1485 C CE1 . PHE A 1 215 ? 23.554 34.449  -14.702 1.00 50.01  ? 215 PHE A CE1 1 
ATOM   1486 C CE2 . PHE A 1 215 ? 23.563 36.804  -14.373 1.00 50.62  ? 215 PHE A CE2 1 
ATOM   1487 C CZ  . PHE A 1 215 ? 24.211 35.588  -14.308 1.00 48.48  ? 215 PHE A CZ  1 
ATOM   1488 N N   . LYS A 1 216 ? 17.854 36.464  -17.854 1.00 41.35  ? 216 LYS A N   1 
ATOM   1489 C CA  . LYS A 1 216 ? 16.465 36.302  -18.349 1.00 41.03  ? 216 LYS A CA  1 
ATOM   1490 C C   . LYS A 1 216 ? 16.473 36.097  -19.869 1.00 35.36  ? 216 LYS A C   1 
ATOM   1491 O O   . LYS A 1 216 ? 15.460 35.609  -20.368 1.00 35.48  ? 216 LYS A O   1 
ATOM   1492 C CB  . LYS A 1 216 ? 15.591 37.494  -17.960 1.00 46.83  ? 216 LYS A CB  1 
ATOM   1493 C CG  . LYS A 1 216 ? 15.354 37.674  -16.465 1.00 47.35  ? 216 LYS A CG  1 
ATOM   1494 C CD  . LYS A 1 216 ? 14.406 36.666  -15.876 1.00 48.22  ? 216 LYS A CD  1 
ATOM   1495 C CE  . LYS A 1 216 ? 14.190 36.879  -14.392 1.00 49.51  ? 216 LYS A CE  1 
ATOM   1496 N NZ  . LYS A 1 216 ? 13.055 37.786  -14.146 1.00 52.69  ? 216 LYS A NZ  1 
ATOM   1497 N N   . SER A 1 217 ? 17.568 36.402  -20.573 1.00 32.86  ? 217 SER A N   1 
ATOM   1498 C CA  . SER A 1 217 ? 17.725 36.019  -21.999 1.00 37.57  ? 217 SER A CA  1 
ATOM   1499 C C   . SER A 1 217 ? 17.836 34.485  -22.113 1.00 41.67  ? 217 SER A C   1 
ATOM   1500 O O   . SER A 1 217 ? 17.301 33.943  -23.084 1.00 49.33  ? 217 SER A O   1 
ATOM   1501 C CB  . SER A 1 217 ? 18.871 36.738  -22.662 1.00 39.31  ? 217 SER A CB  1 
ATOM   1502 O OG  . SER A 1 217 ? 18.815 38.154  -22.423 1.00 42.26  ? 217 SER A OG  1 
ATOM   1503 N N   . ASP A 1 218 ? 18.437 33.791  -21.135 1.00 40.27  ? 218 ASP A N   1 
ATOM   1504 C CA  . ASP A 1 218 ? 18.475 32.303  -21.096 1.00 37.55  ? 218 ASP A CA  1 
ATOM   1505 C C   . ASP A 1 218 ? 17.038 31.779  -20.929 1.00 36.63  ? 218 ASP A C   1 
ATOM   1506 O O   . ASP A 1 218 ? 16.690 30.721  -21.475 1.00 36.96  ? 218 ASP A O   1 
ATOM   1507 C CB  . ASP A 1 218 ? 19.364 31.758  -19.977 1.00 36.63  ? 218 ASP A CB  1 
ATOM   1508 C CG  . ASP A 1 218 ? 20.869 31.810  -20.180 1.00 38.47  ? 218 ASP A CG  1 
ATOM   1509 O OD1 . ASP A 1 218 ? 21.304 31.968  -21.335 1.00 42.83  ? 218 ASP A OD1 1 
ATOM   1510 O OD2 . ASP A 1 218 ? 21.612 31.552  -19.169 1.00 40.96  ? 218 ASP A OD2 1 
ATOM   1511 N N   . ILE A 1 219 ? 16.202 32.494  -20.207 1.00 33.74  ? 219 ILE A N   1 
ATOM   1512 C CA  . ILE A 1 219 ? 14.815 32.029  -19.908 1.00 36.24  ? 219 ILE A CA  1 
ATOM   1513 C C   . ILE A 1 219 ? 13.954 32.115  -21.178 1.00 39.05  ? 219 ILE A C   1 
ATOM   1514 O O   . ILE A 1 219 ? 13.078 31.243  -21.393 1.00 37.64  ? 219 ILE A O   1 
ATOM   1515 C CB  . ILE A 1 219 ? 14.237 32.875  -18.758 1.00 33.43  ? 219 ILE A CB  1 
ATOM   1516 C CG1 . ILE A 1 219 ? 15.083 32.730  -17.486 1.00 38.92  ? 219 ILE A CG1 1 
ATOM   1517 C CG2 . ILE A 1 219 ? 12.772 32.540  -18.536 1.00 32.81  ? 219 ILE A CG2 1 
ATOM   1518 C CD1 . ILE A 1 219 ? 15.151 31.300  -16.897 1.00 39.67  ? 219 ILE A CD1 1 
ATOM   1519 N N   . TRP A 1 220 ? 14.154 33.152  -21.985 1.00 40.54  ? 220 TRP A N   1 
ATOM   1520 C CA  . TRP A 1 220 ? 13.444 33.285  -23.277 1.00 40.46  ? 220 TRP A CA  1 
ATOM   1521 C C   . TRP A 1 220 ? 13.734 32.037  -24.111 1.00 37.86  ? 220 TRP A C   1 
ATOM   1522 O O   . TRP A 1 220 ? 12.790 31.419  -24.605 1.00 35.95  ? 220 TRP A O   1 
ATOM   1523 C CB  . TRP A 1 220 ? 13.887 34.560  -23.986 1.00 42.71  ? 220 TRP A CB  1 
ATOM   1524 C CG  . TRP A 1 220 ? 13.463 34.654  -25.417 1.00 42.47  ? 220 TRP A CG  1 
ATOM   1525 C CD1 . TRP A 1 220 ? 14.126 34.159  -26.498 1.00 43.33  ? 220 TRP A CD1 1 
ATOM   1526 C CD2 . TRP A 1 220 ? 12.282 35.307  -25.927 1.00 45.71  ? 220 TRP A CD2 1 
ATOM   1527 N NE1 . TRP A 1 220 ? 13.435 34.454  -27.645 1.00 47.22  ? 220 TRP A NE1 1 
ATOM   1528 C CE2 . TRP A 1 220 ? 12.307 35.163  -27.330 1.00 45.29  ? 220 TRP A CE2 1 
ATOM   1529 C CE3 . TRP A 1 220 ? 11.231 36.023  -25.343 1.00 41.43  ? 220 TRP A CE3 1 
ATOM   1530 C CZ2 . TRP A 1 220 ? 11.310 35.683  -28.150 1.00 44.50  ? 220 TRP A CZ2 1 
ATOM   1531 C CZ3 . TRP A 1 220 ? 10.256 36.553  -26.155 1.00 47.19  ? 220 TRP A CZ3 1 
ATOM   1532 C CH2 . TRP A 1 220 ? 10.292 36.377  -27.539 1.00 44.78  ? 220 TRP A CH2 1 
ATOM   1533 N N   . SER A 1 221 ? 15.016 31.732  -24.289 1.00 38.78  ? 221 SER A N   1 
ATOM   1534 C CA  . SER A 1 221 ? 15.518 30.552  -25.028 1.00 39.16  ? 221 SER A CA  1 
ATOM   1535 C C   . SER A 1 221 ? 14.862 29.281  -24.489 1.00 42.91  ? 221 SER A C   1 
ATOM   1536 O O   . SER A 1 221 ? 14.339 28.481  -25.310 1.00 45.36  ? 221 SER A O   1 
ATOM   1537 C CB  . SER A 1 221 ? 16.984 30.485  -24.932 1.00 39.39  ? 221 SER A CB  1 
ATOM   1538 O OG  . SER A 1 221 ? 17.552 31.447  -25.790 1.00 41.96  ? 221 SER A OG  1 
ATOM   1539 N N   . LEU A 1 222 ? 14.838 29.147  -23.162 1.00 41.36  ? 222 LEU A N   1 
ATOM   1540 C CA  . LEU A 1 222 ? 14.301 27.970  -22.436 1.00 39.33  ? 222 LEU A CA  1 
ATOM   1541 C C   . LEU A 1 222 ? 12.832 27.788  -22.797 1.00 42.93  ? 222 LEU A C   1 
ATOM   1542 O O   . LEU A 1 222 ? 12.435 26.627  -23.069 1.00 44.63  ? 222 LEU A O   1 
ATOM   1543 C CB  . LEU A 1 222 ? 14.481 28.172  -20.926 1.00 40.79  ? 222 LEU A CB  1 
ATOM   1544 C CG  . LEU A 1 222 ? 14.347 26.929  -20.049 1.00 40.20  ? 222 LEU A CG  1 
ATOM   1545 C CD1 . LEU A 1 222 ? 15.400 25.889  -20.412 1.00 43.32  ? 222 LEU A CD1 1 
ATOM   1546 C CD2 . LEU A 1 222 ? 14.477 27.298  -18.580 1.00 38.92  ? 222 LEU A CD2 1 
ATOM   1547 N N   . GLY A 1 223 ? 12.052 28.873  -22.772 1.00 40.59  ? 223 GLY A N   1 
ATOM   1548 C CA  . GLY A 1 223 ? 10.618 28.830  -23.135 1.00 40.16  ? 223 GLY A CA  1 
ATOM   1549 C C   . GLY A 1 223 ? 10.430 28.459  -24.609 1.00 39.16  ? 223 GLY A C   1 
ATOM   1550 O O   . GLY A 1 223 ? 9.455  27.742  -24.929 1.00 34.65  ? 223 GLY A O   1 
ATOM   1551 N N   . CYS A 1 224 ? 11.298 28.947  -25.503 1.00 36.14  ? 224 CYS A N   1 
ATOM   1552 C CA  . CYS A 1 224 ? 11.214 28.628  -26.958 1.00 41.31  ? 224 CYS A CA  1 
ATOM   1553 C C   . CYS A 1 224 ? 11.514 27.127  -27.128 1.00 40.26  ? 224 CYS A C   1 
ATOM   1554 O O   . CYS A 1 224 ? 10.800 26.454  -27.872 1.00 39.40  ? 224 CYS A O   1 
ATOM   1555 C CB  . CYS A 1 224 ? 12.109 29.522  -27.811 1.00 43.00  ? 224 CYS A CB  1 
ATOM   1556 S SG  . CYS A 1 224 ? 11.556 31.250  -27.871 1.00 41.99  ? 224 CYS A SG  1 
ATOM   1557 N N   . LEU A 1 225 ? 12.449 26.587  -26.358 1.00 39.92  ? 225 LEU A N   1 
ATOM   1558 C CA  . LEU A 1 225 ? 12.863 25.169  -26.472 1.00 40.68  ? 225 LEU A CA  1 
ATOM   1559 C C   . LEU A 1 225 ? 11.727 24.256  -25.986 1.00 40.01  ? 225 LEU A C   1 
ATOM   1560 O O   . LEU A 1 225 ? 11.467 23.213  -26.618 1.00 41.32  ? 225 LEU A O   1 
ATOM   1561 C CB  . LEU A 1 225 ? 14.155 25.003  -25.673 1.00 44.06  ? 225 LEU A CB  1 
ATOM   1562 C CG  . LEU A 1 225 ? 14.802 23.628  -25.747 1.00 46.39  ? 225 LEU A CG  1 
ATOM   1563 C CD1 . LEU A 1 225 ? 16.317 23.741  -25.692 1.00 46.35  ? 225 LEU A CD1 1 
ATOM   1564 C CD2 . LEU A 1 225 ? 14.275 22.726  -24.636 1.00 45.07  ? 225 LEU A CD2 1 
ATOM   1565 N N   . LEU A 1 226 ? 11.052 24.635  -24.911 1.00 42.13  ? 226 LEU A N   1 
ATOM   1566 C CA  . LEU A 1 226 ? 9.892  23.883  -24.387 1.00 39.54  ? 226 LEU A CA  1 
ATOM   1567 C C   . LEU A 1 226 ? 8.787  23.887  -25.443 1.00 41.66  ? 226 LEU A C   1 
ATOM   1568 O O   . LEU A 1 226 ? 8.139  22.846  -25.672 1.00 44.11  ? 226 LEU A O   1 
ATOM   1569 C CB  . LEU A 1 226 ? 9.395  24.562  -23.114 1.00 37.56  ? 226 LEU A CB  1 
ATOM   1570 C CG  . LEU A 1 226 ? 8.143  23.938  -22.514 1.00 36.87  ? 226 LEU A CG  1 
ATOM   1571 C CD1 . LEU A 1 226 ? 8.365  22.474  -22.187 1.00 36.46  ? 226 LEU A CD1 1 
ATOM   1572 C CD2 . LEU A 1 226 ? 7.712  24.683  -21.276 1.00 35.86  ? 226 LEU A CD2 1 
ATOM   1573 N N   . TYR A 1 227 ? 8.506  25.047  -26.014 1.00 40.79  ? 227 TYR A N   1 
ATOM   1574 C CA  . TYR A 1 227 ? 7.508  25.146  -27.101 1.00 42.35  ? 227 TYR A CA  1 
ATOM   1575 C C   . TYR A 1 227 ? 7.851  24.130  -28.201 1.00 41.14  ? 227 TYR A C   1 
ATOM   1576 O O   . TYR A 1 227 ? 6.964  23.385  -28.626 1.00 39.01  ? 227 TYR A O   1 
ATOM   1577 C CB  . TYR A 1 227 ? 7.471  26.552  -27.687 1.00 39.49  ? 227 TYR A CB  1 
ATOM   1578 C CG  . TYR A 1 227 ? 6.494  26.686  -28.820 1.00 37.96  ? 227 TYR A CG  1 
ATOM   1579 C CD1 . TYR A 1 227 ? 5.159  26.947  -28.576 1.00 39.72  ? 227 TYR A CD1 1 
ATOM   1580 C CD2 . TYR A 1 227 ? 6.903  26.496  -30.130 1.00 41.44  ? 227 TYR A CD2 1 
ATOM   1581 C CE1 . TYR A 1 227 ? 4.248  27.048  -29.614 1.00 43.41  ? 227 TYR A CE1 1 
ATOM   1582 C CE2 . TYR A 1 227 ? 6.007  26.593  -31.181 1.00 42.36  ? 227 TYR A CE2 1 
ATOM   1583 C CZ  . TYR A 1 227 ? 4.679  26.877  -30.924 1.00 41.44  ? 227 TYR A CZ  1 
ATOM   1584 O OH  . TYR A 1 227 ? 3.807  26.993  -31.962 1.00 46.60  ? 227 TYR A OH  1 
ATOM   1585 N N   . GLU A 1 228 ? 9.096  24.178  -28.672 1.00 43.93  ? 228 GLU A N   1 
ATOM   1586 C CA  . GLU A 1 228 ? 9.581  23.439  -29.851 1.00 48.38  ? 228 GLU A CA  1 
ATOM   1587 C C   . GLU A 1 228 ? 9.496  21.953  -29.534 1.00 49.60  ? 228 GLU A C   1 
ATOM   1588 O O   . GLU A 1 228 ? 9.312  21.173  -30.464 1.00 52.93  ? 228 GLU A O   1 
ATOM   1589 C CB  . GLU A 1 228 ? 11.010 23.844  -30.209 1.00 51.81  ? 228 GLU A CB  1 
ATOM   1590 C CG  . GLU A 1 228 ? 11.474 23.260  -31.538 1.00 50.17  ? 228 GLU A CG  1 
ATOM   1591 C CD  . GLU A 1 228 ? 12.781 23.812  -32.073 1.00 52.74  ? 228 GLU A CD  1 
ATOM   1592 O OE1 . GLU A 1 228 ? 13.173 24.917  -31.659 1.00 63.35  ? 228 GLU A OE1 1 
ATOM   1593 O OE2 . GLU A 1 228 ? 13.417 23.125  -32.894 1.00 61.51  ? 228 GLU A OE2 1 
ATOM   1594 N N   . MET A 1 229 ? 9.645  21.587  -28.264 1.00 48.00  ? 229 MET A N   1 
ATOM   1595 C CA  . MET A 1 229 ? 9.541  20.173  -27.843 1.00 46.55  ? 229 MET A CA  1 
ATOM   1596 C C   . MET A 1 229 ? 8.112  19.698  -28.092 1.00 45.35  ? 229 MET A C   1 
ATOM   1597 O O   . MET A 1 229 ? 7.943  18.532  -28.500 1.00 52.08  ? 229 MET A O   1 
ATOM   1598 C CB  . MET A 1 229 ? 9.921  19.958  -26.374 1.00 45.93  ? 229 MET A CB  1 
ATOM   1599 C CG  . MET A 1 229 ? 11.403 19.804  -26.181 1.00 42.79  ? 229 MET A CG  1 
ATOM   1600 S SD  . MET A 1 229 ? 11.850 19.650  -24.453 1.00 50.60  ? 229 MET A SD  1 
ATOM   1601 C CE  . MET A 1 229 ? 11.667 17.878  -24.278 1.00 50.45  ? 229 MET A CE  1 
ATOM   1602 N N   . ALA A 1 230 ? 7.127  20.562  -27.876 1.00 46.61  ? 230 ALA A N   1 
ATOM   1603 C CA  . ALA A 1 230 ? 5.692  20.200  -27.962 1.00 49.18  ? 230 ALA A CA  1 
ATOM   1604 C C   . ALA A 1 230 ? 5.132  20.389  -29.392 1.00 46.12  ? 230 ALA A C   1 
ATOM   1605 O O   . ALA A 1 230 ? 4.197  19.651  -29.741 1.00 50.19  ? 230 ALA A O   1 
ATOM   1606 C CB  . ALA A 1 230 ? 4.936  20.985  -26.923 1.00 49.21  ? 230 ALA A CB  1 
ATOM   1607 N N   . ALA A 1 231 ? 5.701  21.290  -30.208 1.00 45.78  ? 231 ALA A N   1 
ATOM   1608 C CA  . ALA A 1 231 ? 5.194  21.683  -31.550 1.00 45.40  ? 231 ALA A CA  1 
ATOM   1609 C C   . ALA A 1 231 ? 6.068  21.121  -32.683 1.00 45.41  ? 231 ALA A C   1 
ATOM   1610 O O   . ALA A 1 231 ? 5.591  21.066  -33.831 1.00 45.11  ? 231 ALA A O   1 
ATOM   1611 C CB  . ALA A 1 231 ? 5.117  23.183  -31.636 1.00 44.36  ? 231 ALA A CB  1 
ATOM   1612 N N   . LEU A 1 232 ? 7.307  20.758  -32.365 1.00 46.59  ? 232 LEU A N   1 
ATOM   1613 C CA  . LEU A 1 232 ? 8.318  20.174  -33.281 1.00 49.52  ? 232 LEU A CA  1 
ATOM   1614 C C   . LEU A 1 232 ? 8.796  21.259  -34.240 1.00 51.84  ? 232 LEU A C   1 
ATOM   1615 O O   . LEU A 1 232 ? 9.429  20.919  -35.251 1.00 58.77  ? 232 LEU A O   1 
ATOM   1616 C CB  . LEU A 1 232 ? 7.728  18.940  -33.977 1.00 49.54  ? 232 LEU A CB  1 
ATOM   1617 C CG  . LEU A 1 232 ? 7.317  17.829  -33.006 1.00 48.92  ? 232 LEU A CG  1 
ATOM   1618 C CD1 . LEU A 1 232 ? 6.590  16.689  -33.701 1.00 49.15  ? 232 LEU A CD1 1 
ATOM   1619 C CD2 . LEU A 1 232 ? 8.531  17.290  -32.273 1.00 46.97  ? 232 LEU A CD2 1 
ATOM   1620 N N   . GLN A 1 233 ? 8.567  22.524  -33.879 1.00 51.39  ? 233 GLN A N   1 
ATOM   1621 C CA  . GLN A 1 233 ? 9.169  23.692  -34.570 1.00 51.83  ? 233 GLN A CA  1 
ATOM   1622 C C   . GLN A 1 233 ? 9.292  24.862  -33.592 1.00 48.82  ? 233 GLN A C   1 
ATOM   1623 O O   . GLN A 1 233 ? 8.475  24.957  -32.663 1.00 54.14  ? 233 GLN A O   1 
ATOM   1624 C CB  . GLN A 1 233 ? 8.362  24.086  -35.805 1.00 51.81  ? 233 GLN A CB  1 
ATOM   1625 C CG  . GLN A 1 233 ? 6.918  24.454  -35.513 1.00 60.46  ? 233 GLN A CG  1 
ATOM   1626 C CD  . GLN A 1 233 ? 6.169  24.633  -36.811 1.00 67.13  ? 233 GLN A CD  1 
ATOM   1627 O OE1 . GLN A 1 233 ? 6.134  23.744  -37.657 1.00 71.29  ? 233 GLN A OE1 1 
ATOM   1628 N NE2 . GLN A 1 233 ? 5.585  25.802  -36.997 1.00 69.06  ? 233 GLN A NE2 1 
ATOM   1629 N N   . SER A 1 234 ? 10.313 25.687  -33.798 1.00 46.32  ? 234 SER A N   1 
ATOM   1630 C CA  . SER A 1 234 ? 10.509 26.987  -33.119 1.00 49.58  ? 234 SER A CA  1 
ATOM   1631 C C   . SER A 1 234 ? 9.188  27.741  -33.141 1.00 51.51  ? 234 SER A C   1 
ATOM   1632 O O   . SER A 1 234 ? 8.360  27.543  -34.024 1.00 51.70  ? 234 SER A O   1 
ATOM   1633 C CB  . SER A 1 234 ? 11.608 27.784  -33.754 1.00 47.72  ? 234 SER A CB  1 
ATOM   1634 O OG  . SER A 1 234 ? 12.706 26.938  -34.065 1.00 62.84  ? 234 SER A OG  1 
ATOM   1635 N N   . PRO A 1 235 ? 8.912  28.558  -32.107 1.00 51.15  ? 235 PRO A N   1 
ATOM   1636 C CA  . PRO A 1 235 ? 7.679  29.342  -32.071 1.00 48.90  ? 235 PRO A CA  1 
ATOM   1637 C C   . PRO A 1 235 ? 7.561  30.397  -33.186 1.00 47.15  ? 235 PRO A C   1 
ATOM   1638 O O   . PRO A 1 235 ? 6.454  30.722  -33.543 1.00 43.72  ? 235 PRO A O   1 
ATOM   1639 C CB  . PRO A 1 235 ? 7.730  30.002  -30.680 1.00 47.11  ? 235 PRO A CB  1 
ATOM   1640 C CG  . PRO A 1 235 ? 9.200  29.985  -30.294 1.00 49.58  ? 235 PRO A CG  1 
ATOM   1641 C CD  . PRO A 1 235 ? 9.744  28.715  -30.903 1.00 46.78  ? 235 PRO A CD  1 
ATOM   1642 N N   . PHE A 1 236 ? 8.680  30.905  -33.704 1.00 46.56  ? 236 PHE A N   1 
ATOM   1643 C CA  . PHE A 1 236 ? 8.692  31.965  -34.745 1.00 52.59  ? 236 PHE A CA  1 
ATOM   1644 C C   . PHE A 1 236 ? 9.138  31.417  -36.104 1.00 55.73  ? 236 PHE A C   1 
ATOM   1645 O O   . PHE A 1 236 ? 9.444  32.240  -36.958 1.00 55.68  ? 236 PHE A O   1 
ATOM   1646 C CB  . PHE A 1 236 ? 9.556  33.144  -34.283 1.00 53.24  ? 236 PHE A CB  1 
ATOM   1647 C CG  . PHE A 1 236 ? 9.077  33.672  -32.963 1.00 51.66  ? 236 PHE A CG  1 
ATOM   1648 C CD1 . PHE A 1 236 ? 7.790  34.184  -32.856 1.00 50.59  ? 236 PHE A CD1 1 
ATOM   1649 C CD2 . PHE A 1 236 ? 9.845  33.528  -31.817 1.00 49.79  ? 236 PHE A CD2 1 
ATOM   1650 C CE1 . PHE A 1 236 ? 7.290  34.589  -31.633 1.00 48.14  ? 236 PHE A CE1 1 
ATOM   1651 C CE2 . PHE A 1 236 ? 9.344  33.936  -30.595 1.00 46.21  ? 236 PHE A CE2 1 
ATOM   1652 C CZ  . PHE A 1 236 ? 8.073  34.470  -30.509 1.00 51.41  ? 236 PHE A CZ  1 
ATOM   1653 N N   . TYR A 1 237 ? 9.107  30.100  -36.313 1.00 67.37  ? 237 TYR A N   1 
ATOM   1654 C CA  . TYR A 1 237 ? 9.489  29.450  -37.593 1.00 74.57  ? 237 TYR A CA  1 
ATOM   1655 C C   . TYR A 1 237 ? 8.393  29.717  -38.627 1.00 73.11  ? 237 TYR A C   1 
ATOM   1656 O O   . TYR A 1 237 ? 7.221  29.760  -38.248 1.00 68.34  ? 237 TYR A O   1 
ATOM   1657 C CB  . TYR A 1 237 ? 9.735  27.952  -37.388 1.00 90.96  ? 237 TYR A CB  1 
ATOM   1658 C CG  . TYR A 1 237 ? 9.649  27.113  -38.640 1.00 103.26 ? 237 TYR A CG  1 
ATOM   1659 C CD1 . TYR A 1 237 ? 8.426  26.637  -39.091 1.00 104.51 ? 237 TYR A CD1 1 
ATOM   1660 C CD2 . TYR A 1 237 ? 10.785 26.784  -39.370 1.00 105.13 ? 237 TYR A CD2 1 
ATOM   1661 C CE1 . TYR A 1 237 ? 8.328  25.870  -40.241 1.00 110.44 ? 237 TYR A CE1 1 
ATOM   1662 C CE2 . TYR A 1 237 ? 10.705 26.010  -40.519 1.00 106.12 ? 237 TYR A CE2 1 
ATOM   1663 C CZ  . TYR A 1 237 ? 9.472  25.554  -40.956 1.00 111.70 ? 237 TYR A CZ  1 
ATOM   1664 O OH  . TYR A 1 237 ? 9.381  24.802  -42.092 1.00 118.40 ? 237 TYR A OH  1 
ATOM   1665 N N   . GLY A 1 238 ? 8.781  29.908  -39.889 1.00 77.71  ? 238 GLY A N   1 
ATOM   1666 C CA  . GLY A 1 238 ? 7.868  29.951  -41.049 1.00 82.43  ? 238 GLY A CA  1 
ATOM   1667 C C   . GLY A 1 238 ? 8.525  29.384  -42.301 1.00 88.88  ? 238 GLY A C   1 
ATOM   1668 O O   . GLY A 1 238 ? 9.782  29.285  -42.324 1.00 78.62  ? 238 GLY A O   1 
ATOM   1669 N N   . ASP A 1 239 ? 7.712  29.031  -43.306 1.00 98.06  ? 239 ASP A N   1 
ATOM   1670 C CA  . ASP A 1 239 ? 8.155  28.374  -44.568 1.00 103.53 ? 239 ASP A CA  1 
ATOM   1671 C C   . ASP A 1 239 ? 9.017  29.372  -45.345 1.00 99.68  ? 239 ASP A C   1 
ATOM   1672 O O   . ASP A 1 239 ? 10.261 29.207  -45.365 1.00 91.43  ? 239 ASP A O   1 
ATOM   1673 C CB  . ASP A 1 239 ? 6.954  27.878  -45.381 1.00 110.53 ? 239 ASP A CB  1 
ATOM   1674 C CG  . ASP A 1 239 ? 6.080  26.881  -44.638 1.00 117.09 ? 239 ASP A CG  1 
ATOM   1675 O OD1 . ASP A 1 239 ? 6.360  26.611  -43.442 1.00 123.52 ? 239 ASP A OD1 1 
ATOM   1676 O OD2 . ASP A 1 239 ? 5.116  26.393  -45.256 1.00 125.46 ? 239 ASP A OD2 1 
ATOM   1677 N N   . LYS A 1 240 ? 8.361  30.365  -45.950 1.00 99.32  ? 240 LYS A N   1 
ATOM   1678 C CA  . LYS A 1 240 ? 8.980  31.604  -46.476 1.00 101.14 ? 240 LYS A CA  1 
ATOM   1679 C C   . LYS A 1 240 ? 9.149  32.549  -45.286 1.00 103.18 ? 240 LYS A C   1 
ATOM   1680 O O   . LYS A 1 240 ? 8.372  33.526  -45.198 1.00 105.27 ? 240 LYS A O   1 
ATOM   1681 C CB  . LYS A 1 240 ? 8.106  32.227  -47.572 1.00 95.01  ? 240 LYS A CB  1 
ATOM   1682 N N   . MET A 1 241 ? 10.073 32.225  -44.374 1.00 93.63  ? 241 MET A N   1 
ATOM   1683 C CA  . MET A 1 241 ? 10.396 33.091  -43.213 1.00 89.24  ? 241 MET A CA  1 
ATOM   1684 C C   . MET A 1 241 ? 11.546 34.013  -43.625 1.00 86.17  ? 241 MET A C   1 
ATOM   1685 O O   . MET A 1 241 ? 12.485 33.558  -44.312 1.00 73.47  ? 241 MET A O   1 
ATOM   1686 C CB  . MET A 1 241 ? 10.756 32.293  -41.953 1.00 94.65  ? 241 MET A CB  1 
ATOM   1687 C CG  . MET A 1 241 ? 10.929 33.131  -40.662 1.00 95.45  ? 241 MET A CG  1 
ATOM   1688 S SD  . MET A 1 241 ? 9.576  34.278  -40.172 1.00 97.02  ? 241 MET A SD  1 
ATOM   1689 C CE  . MET A 1 241 ? 8.100  33.338  -40.560 1.00 95.97  ? 241 MET A CE  1 
ATOM   1690 N N   . ASN A 1 242 ? 11.426 35.265  -43.193 1.00 80.21  ? 242 ASN A N   1 
ATOM   1691 C CA  . ASN A 1 242 ? 12.226 36.440  -43.599 1.00 75.56  ? 242 ASN A CA  1 
ATOM   1692 C C   . ASN A 1 242 ? 12.242 37.427  -42.430 1.00 79.09  ? 242 ASN A C   1 
ATOM   1693 O O   . ASN A 1 242 ? 11.242 37.469  -41.670 1.00 83.72  ? 242 ASN A O   1 
ATOM   1694 C CB  . ASN A 1 242 ? 11.603 37.134  -44.805 1.00 75.00  ? 242 ASN A CB  1 
ATOM   1695 C CG  . ASN A 1 242 ? 10.187 37.592  -44.524 1.00 71.16  ? 242 ASN A CG  1 
ATOM   1696 O OD1 . ASN A 1 242 ? 9.957  38.739  -44.143 1.00 71.19  ? 242 ASN A OD1 1 
ATOM   1697 N ND2 . ASN A 1 242 ? 9.234  36.689  -44.673 1.00 73.73  ? 242 ASN A ND2 1 
ATOM   1698 N N   . LEU A 1 243 ? 13.296 38.239  -42.348 1.00 73.02  ? 243 LEU A N   1 
ATOM   1699 C CA  . LEU A 1 243 ? 13.602 39.123  -41.195 1.00 67.17  ? 243 LEU A CA  1 
ATOM   1700 C C   . LEU A 1 243 ? 12.408 40.036  -40.866 1.00 62.47  ? 243 LEU A C   1 
ATOM   1701 O O   . LEU A 1 243 ? 12.106 40.208  -39.671 1.00 57.44  ? 243 LEU A O   1 
ATOM   1702 C CB  . LEU A 1 243 ? 14.860 39.922  -41.528 1.00 65.06  ? 243 LEU A CB  1 
ATOM   1703 C CG  . LEU A 1 243 ? 15.368 40.807  -40.398 1.00 69.59  ? 243 LEU A CG  1 
ATOM   1704 C CD1 . LEU A 1 243 ? 15.768 39.964  -39.197 1.00 72.47  ? 243 LEU A CD1 1 
ATOM   1705 C CD2 . LEU A 1 243 ? 16.537 41.653  -40.872 1.00 68.01  ? 243 LEU A CD2 1 
ATOM   1706 N N   . TYR A 1 244 ? 11.727 40.592  -41.866 1.00 59.88  ? 244 TYR A N   1 
ATOM   1707 C CA  . TYR A 1 244 ? 10.605 41.539  -41.627 1.00 62.18  ? 244 TYR A CA  1 
ATOM   1708 C C   . TYR A 1 244 ? 9.563  40.873  -40.737 1.00 55.16  ? 244 TYR A C   1 
ATOM   1709 O O   . TYR A 1 244 ? 9.228  41.465  -39.697 1.00 52.10  ? 244 TYR A O   1 
ATOM   1710 C CB  . TYR A 1 244 ? 9.902  42.006  -42.908 1.00 64.39  ? 244 TYR A CB  1 
ATOM   1711 C CG  . TYR A 1 244 ? 8.939  43.138  -42.652 1.00 69.13  ? 244 TYR A CG  1 
ATOM   1712 C CD1 . TYR A 1 244 ? 7.633  42.892  -42.250 1.00 68.41  ? 244 TYR A CD1 1 
ATOM   1713 C CD2 . TYR A 1 244 ? 9.349  44.458  -42.760 1.00 68.54  ? 244 TYR A CD2 1 
ATOM   1714 C CE1 . TYR A 1 244 ? 6.753  43.928  -41.977 1.00 71.81  ? 244 TYR A CE1 1 
ATOM   1715 C CE2 . TYR A 1 244 ? 8.479  45.504  -42.508 1.00 71.66  ? 244 TYR A CE2 1 
ATOM   1716 C CZ  . TYR A 1 244 ? 7.180  45.237  -42.113 1.00 70.64  ? 244 TYR A CZ  1 
ATOM   1717 O OH  . TYR A 1 244 ? 6.319  46.259  -41.858 1.00 77.53  ? 244 TYR A OH  1 
ATOM   1718 N N   . SER A 1 245 ? 9.051  39.719  -41.194 1.00 62.27  ? 245 SER A N   1 
ATOM   1719 C CA  . SER A 1 245 ? 7.915  38.965  -40.605 1.00 63.34  ? 245 SER A CA  1 
ATOM   1720 C C   . SER A 1 245 ? 8.315  38.479  -39.212 1.00 58.38  ? 245 SER A C   1 
ATOM   1721 O O   . SER A 1 245 ? 7.464  38.521  -38.304 1.00 52.70  ? 245 SER A O   1 
ATOM   1722 C CB  . SER A 1 245 ? 7.501  37.807  -41.487 1.00 72.17  ? 245 SER A CB  1 
ATOM   1723 O OG  . SER A 1 245 ? 6.345  37.148  -40.965 1.00 80.09  ? 245 SER A OG  1 
ATOM   1724 N N   . LEU A 1 246 ? 9.564  38.035  -39.075 1.00 52.64  ? 246 LEU A N   1 
ATOM   1725 C CA  . LEU A 1 246 ? 10.129 37.531  -37.801 1.00 57.82  ? 246 LEU A CA  1 
ATOM   1726 C C   . LEU A 1 246 ? 10.114 38.649  -36.757 1.00 58.81  ? 246 LEU A C   1 
ATOM   1727 O O   . LEU A 1 246 ? 9.617  38.407  -35.636 1.00 57.24  ? 246 LEU A O   1 
ATOM   1728 C CB  . LEU A 1 246 ? 11.556 37.039  -38.031 1.00 59.55  ? 246 LEU A CB  1 
ATOM   1729 C CG  . LEU A 1 246 ? 12.305 36.668  -36.754 1.00 67.82  ? 246 LEU A CG  1 
ATOM   1730 C CD1 . LEU A 1 246 ? 11.574 35.556  -36.013 1.00 67.34  ? 246 LEU A CD1 1 
ATOM   1731 C CD2 . LEU A 1 246 ? 13.738 36.258  -37.069 1.00 74.71  ? 246 LEU A CD2 1 
ATOM   1732 N N   . CYS A 1 247 ? 10.661 39.815  -37.108 1.00 55.83  ? 247 CYS A N   1 
ATOM   1733 C CA  . CYS A 1 247 ? 10.725 40.998  -36.217 1.00 51.66  ? 247 CYS A CA  1 
ATOM   1734 C C   . CYS A 1 247 ? 9.312  41.362  -35.806 1.00 46.95  ? 247 CYS A C   1 
ATOM   1735 O O   . CYS A 1 247 ? 9.120  41.604  -34.620 1.00 49.98  ? 247 CYS A O   1 
ATOM   1736 C CB  . CYS A 1 247 ? 11.387 42.198  -36.872 1.00 56.09  ? 247 CYS A CB  1 
ATOM   1737 S SG  . CYS A 1 247 ? 13.190 42.059  -36.980 1.00 61.75  ? 247 CYS A SG  1 
ATOM   1738 N N   . LYS A 1 248 ? 8.358  41.337  -36.737 1.00 51.42  ? 248 LYS A N   1 
ATOM   1739 C CA  . LYS A 1 248 ? 6.931  41.642  -36.421 1.00 56.16  ? 248 LYS A CA  1 
ATOM   1740 C C   . LYS A 1 248 ? 6.418  40.628  -35.382 1.00 50.48  ? 248 LYS A C   1 
ATOM   1741 O O   . LYS A 1 248 ? 5.796  41.041  -34.386 1.00 53.16  ? 248 LYS A O   1 
ATOM   1742 C CB  . LYS A 1 248 ? 6.067  41.650  -37.689 1.00 57.40  ? 248 LYS A CB  1 
ATOM   1743 C CG  . LYS A 1 248 ? 4.679  42.267  -37.520 1.00 64.10  ? 248 LYS A CG  1 
ATOM   1744 C CD  . LYS A 1 248 ? 3.601  41.649  -38.393 1.00 71.21  ? 248 LYS A CD  1 
ATOM   1745 C CE  . LYS A 1 248 ? 2.542  42.630  -38.844 1.00 76.06  ? 248 LYS A CE  1 
ATOM   1746 N NZ  . LYS A 1 248 ? 2.941  43.272  -40.121 1.00 88.43  ? 248 LYS A NZ  1 
ATOM   1747 N N   . LYS A 1 249 ? 6.683  39.342  -35.600 1.00 51.53  ? 249 LYS A N   1 
ATOM   1748 C CA  . LYS A 1 249 ? 6.114  38.236  -34.789 1.00 53.54  ? 249 LYS A CA  1 
ATOM   1749 C C   . LYS A 1 249 ? 6.734  38.251  -33.388 1.00 48.92  ? 249 LYS A C   1 
ATOM   1750 O O   . LYS A 1 249 ? 5.999  38.002  -32.423 1.00 50.40  ? 249 LYS A O   1 
ATOM   1751 C CB  . LYS A 1 249 ? 6.255  36.908  -35.541 1.00 55.98  ? 249 LYS A CB  1 
ATOM   1752 C CG  . LYS A 1 249 ? 5.119  36.684  -36.535 1.00 64.80  ? 249 LYS A CG  1 
ATOM   1753 C CD  . LYS A 1 249 ? 5.422  35.708  -37.644 1.00 71.20  ? 249 LYS A CD  1 
ATOM   1754 C CE  . LYS A 1 249 ? 5.413  34.278  -37.165 1.00 75.72  ? 249 LYS A CE  1 
ATOM   1755 N NZ  . LYS A 1 249 ? 6.148  33.390  -38.093 1.00 84.29  ? 249 LYS A NZ  1 
ATOM   1756 N N   . ILE A 1 250 ? 8.010  38.592  -33.259 1.00 46.29  ? 250 ILE A N   1 
ATOM   1757 C CA  . ILE A 1 250 ? 8.645  38.739  -31.924 1.00 50.53  ? 250 ILE A CA  1 
ATOM   1758 C C   . ILE A 1 250 ? 8.064  39.983  -31.246 1.00 52.58  ? 250 ILE A C   1 
ATOM   1759 O O   . ILE A 1 250 ? 7.643  39.862  -30.075 1.00 49.61  ? 250 ILE A O   1 
ATOM   1760 C CB  . ILE A 1 250 ? 10.179 38.741  -32.037 1.00 52.56  ? 250 ILE A CB  1 
ATOM   1761 C CG1 . ILE A 1 250 ? 10.675 37.341  -32.415 1.00 50.13  ? 250 ILE A CG1 1 
ATOM   1762 C CG2 . ILE A 1 250 ? 10.812 39.236  -30.740 1.00 52.61  ? 250 ILE A CG2 1 
ATOM   1763 C CD1 . ILE A 1 250 ? 12.064 37.310  -33.031 1.00 50.54  ? 250 ILE A CD1 1 
ATOM   1764 N N   . GLU A 1 251 ? 7.979  41.112  -31.958 1.00 53.40  ? 251 GLU A N   1 
ATOM   1765 C CA  . GLU A 1 251 ? 7.409  42.356  -31.381 1.00 55.10  ? 251 GLU A CA  1 
ATOM   1766 C C   . GLU A 1 251 ? 6.106  42.019  -30.659 1.00 48.59  ? 251 GLU A C   1 
ATOM   1767 O O   . GLU A 1 251 ? 5.953  42.506  -29.533 1.00 50.73  ? 251 GLU A O   1 
ATOM   1768 C CB  . GLU A 1 251 ? 7.129  43.443  -32.414 1.00 64.05  ? 251 GLU A CB  1 
ATOM   1769 C CG  . GLU A 1 251 ? 6.765  44.762  -31.744 1.00 71.53  ? 251 GLU A CG  1 
ATOM   1770 C CD  . GLU A 1 251 ? 6.425  45.922  -32.663 1.00 72.01  ? 251 GLU A CD  1 
ATOM   1771 O OE1 . GLU A 1 251 ? 5.344  45.879  -33.292 1.00 76.62  ? 251 GLU A OE1 1 
ATOM   1772 O OE2 . GLU A 1 251 ? 7.231  46.876  -32.726 1.00 79.70  ? 251 GLU A OE2 1 
ATOM   1773 N N   . GLN A 1 252 ? 5.232  41.213  -31.285 1.00 48.89  ? 252 GLN A N   1 
ATOM   1774 C CA  . GLN A 1 252 ? 3.865  40.877  -30.785 1.00 47.41  ? 252 GLN A CA  1 
ATOM   1775 C C   . GLN A 1 252 ? 3.836  39.516  -30.084 1.00 43.15  ? 252 GLN A C   1 
ATOM   1776 O O   . GLN A 1 252 ? 2.753  39.103  -29.720 1.00 41.38  ? 252 GLN A O   1 
ATOM   1777 C CB  . GLN A 1 252 ? 2.861  40.829  -31.940 1.00 52.61  ? 252 GLN A CB  1 
ATOM   1778 C CG  . GLN A 1 252 ? 2.974  41.984  -32.939 1.00 53.69  ? 252 GLN A CG  1 
ATOM   1779 C CD  . GLN A 1 252 ? 1.986  41.848  -34.079 1.00 57.18  ? 252 GLN A CD  1 
ATOM   1780 O OE1 . GLN A 1 252 ? 1.721  40.764  -34.596 1.00 55.96  ? 252 GLN A OE1 1 
ATOM   1781 N NE2 . GLN A 1 252 ? 1.412  42.961  -34.491 1.00 57.26  ? 252 GLN A NE2 1 
ATOM   1782 N N   . CYS A 1 253 ? 4.971  38.831  -29.910 1.00 48.16  ? 253 CYS A N   1 
ATOM   1783 C CA  . CYS A 1 253 ? 5.050  37.393  -29.493 1.00 54.05  ? 253 CYS A CA  1 
ATOM   1784 C C   . CYS A 1 253 ? 3.950  36.580  -30.170 1.00 48.96  ? 253 CYS A C   1 
ATOM   1785 O O   . CYS A 1 253 ? 3.082  36.047  -29.455 1.00 45.54  ? 253 CYS A O   1 
ATOM   1786 C CB  . CYS A 1 253 ? 4.935  37.213  -27.982 1.00 57.09  ? 253 CYS A CB  1 
ATOM   1787 S SG  . CYS A 1 253 ? 6.438  37.766  -27.156 1.00 63.66  ? 253 CYS A SG  1 
ATOM   1788 N N   . ASP A 1 254 ? 3.980  36.523  -31.505 1.00 53.60  ? 254 ASP A N   1 
ATOM   1789 C CA  . ASP A 1 254 ? 2.947  35.835  -32.313 1.00 55.42  ? 254 ASP A CA  1 
ATOM   1790 C C   . ASP A 1 254 ? 3.497  34.456  -32.673 1.00 50.00  ? 254 ASP A C   1 
ATOM   1791 O O   . ASP A 1 254 ? 4.288  34.369  -33.636 1.00 49.23  ? 254 ASP A O   1 
ATOM   1792 C CB  . ASP A 1 254 ? 2.549  36.667  -33.535 1.00 60.84  ? 254 ASP A CB  1 
ATOM   1793 C CG  . ASP A 1 254 ? 1.408  36.070  -34.349 1.00 55.27  ? 254 ASP A CG  1 
ATOM   1794 O OD1 . ASP A 1 254 ? 0.670  35.210  -33.810 1.00 56.07  ? 254 ASP A OD1 1 
ATOM   1795 O OD2 . ASP A 1 254 ? 1.250  36.493  -35.505 1.00 57.91  ? 254 ASP A OD2 1 
ATOM   1796 N N   . TYR A 1 255 ? 3.099  33.431  -31.914 1.00 46.72  ? 255 TYR A N   1 
ATOM   1797 C CA  . TYR A 1 255 ? 3.431  32.009  -32.209 1.00 47.92  ? 255 TYR A CA  1 
ATOM   1798 C C   . TYR A 1 255 ? 2.141  31.188  -32.205 1.00 45.70  ? 255 TYR A C   1 
ATOM   1799 O O   . TYR A 1 255 ? 1.169  31.522  -31.525 1.00 43.24  ? 255 TYR A O   1 
ATOM   1800 C CB  . TYR A 1 255 ? 4.526  31.518  -31.256 1.00 48.21  ? 255 TYR A CB  1 
ATOM   1801 C CG  . TYR A 1 255 ? 4.136  31.575  -29.806 1.00 45.45  ? 255 TYR A CG  1 
ATOM   1802 C CD1 . TYR A 1 255 ? 3.363  30.581  -29.245 1.00 39.68  ? 255 TYR A CD1 1 
ATOM   1803 C CD2 . TYR A 1 255 ? 4.523  32.645  -29.011 1.00 47.86  ? 255 TYR A CD2 1 
ATOM   1804 C CE1 . TYR A 1 255 ? 2.975  30.653  -27.918 1.00 46.55  ? 255 TYR A CE1 1 
ATOM   1805 C CE2 . TYR A 1 255 ? 4.155  32.731  -27.682 1.00 42.61  ? 255 TYR A CE2 1 
ATOM   1806 C CZ  . TYR A 1 255 ? 3.372  31.728  -27.134 1.00 47.27  ? 255 TYR A CZ  1 
ATOM   1807 O OH  . TYR A 1 255 ? 2.990  31.797  -25.828 1.00 48.29  ? 255 TYR A OH  1 
ATOM   1808 N N   . PRO A 1 256 ? 2.030  30.163  -33.076 1.00 48.79  ? 256 PRO A N   1 
ATOM   1809 C CA  . PRO A 1 256 ? 0.836  29.323  -33.105 1.00 49.15  ? 256 PRO A CA  1 
ATOM   1810 C C   . PRO A 1 256 ? 0.628  28.692  -31.734 1.00 49.74  ? 256 PRO A C   1 
ATOM   1811 O O   . PRO A 1 256 ? 1.526  28.027  -31.242 1.00 47.10  ? 256 PRO A O   1 
ATOM   1812 C CB  . PRO A 1 256 ? 1.139  28.247  -34.164 1.00 42.78  ? 256 PRO A CB  1 
ATOM   1813 C CG  . PRO A 1 256 ? 2.248  28.822  -35.013 1.00 44.41  ? 256 PRO A CG  1 
ATOM   1814 C CD  . PRO A 1 256 ? 2.988  29.818  -34.135 1.00 47.85  ? 256 PRO A CD  1 
ATOM   1815 N N   . PRO A 1 257 ? -0.534 28.890  -31.077 1.00 53.81  ? 257 PRO A N   1 
ATOM   1816 C CA  . PRO A 1 257 ? -0.838 28.200  -29.827 1.00 52.99  ? 257 PRO A CA  1 
ATOM   1817 C C   . PRO A 1 257 ? -0.694 26.678  -29.940 1.00 60.99  ? 257 PRO A C   1 
ATOM   1818 O O   . PRO A 1 257 ? -0.946 26.127  -31.004 1.00 62.03  ? 257 PRO A O   1 
ATOM   1819 C CB  . PRO A 1 257 ? -2.306 28.530  -29.576 1.00 52.54  ? 257 PRO A CB  1 
ATOM   1820 C CG  . PRO A 1 257 ? -2.473 29.868  -30.245 1.00 57.72  ? 257 PRO A CG  1 
ATOM   1821 C CD  . PRO A 1 257 ? -1.620 29.788  -31.492 1.00 55.10  ? 257 PRO A CD  1 
ATOM   1822 N N   . LEU A 1 258 ? -0.282 26.045  -28.841 1.00 56.79  ? 258 LEU A N   1 
ATOM   1823 C CA  . LEU A 1 258 ? -0.106 24.577  -28.758 1.00 62.84  ? 258 LEU A CA  1 
ATOM   1824 C C   . LEU A 1 258 ? -1.478 23.929  -28.615 1.00 60.24  ? 258 LEU A C   1 
ATOM   1825 O O   . LEU A 1 258 ? -2.369 24.510  -27.998 1.00 57.94  ? 258 LEU A O   1 
ATOM   1826 C CB  . LEU A 1 258 ? 0.787  24.228  -27.560 1.00 60.23  ? 258 LEU A CB  1 
ATOM   1827 C CG  . LEU A 1 258 ? 2.257  24.609  -27.703 1.00 57.75  ? 258 LEU A CG  1 
ATOM   1828 C CD1 . LEU A 1 258 ? 2.989  24.449  -26.381 1.00 56.66  ? 258 LEU A CD1 1 
ATOM   1829 C CD2 . LEU A 1 258 ? 2.925  23.772  -28.775 1.00 56.23  ? 258 LEU A CD2 1 
ATOM   1830 N N   . PRO A 1 259 ? -1.659 22.691  -29.134 1.00 58.30  ? 259 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 259 ? -2.935 21.988  -29.020 1.00 55.53  ? 259 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 259 ? -3.219 21.664  -27.549 1.00 57.75  ? 259 PRO A C   1 
ATOM   1833 O O   . PRO A 1 259 ? -2.480 20.881  -26.949 1.00 57.23  ? 259 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 259 ? -2.760 20.722  -29.873 1.00 54.85  ? 259 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 259 ? -1.258 20.516  -29.947 1.00 57.27  ? 259 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 259 ? -0.633 21.892  -29.824 1.00 55.98  ? 259 PRO A CD  1 
ATOM   1837 N N   . SER A 1 260 ? -4.265 22.283  -26.996 1.00 55.91  ? 260 SER A N   1 
ATOM   1838 C CA  . SER A 1 260 ? -4.730 22.069  -25.601 1.00 55.37  ? 260 SER A CA  1 
ATOM   1839 C C   . SER A 1 260 ? -5.137 20.606  -25.368 1.00 58.39  ? 260 SER A C   1 
ATOM   1840 O O   . SER A 1 260 ? -5.203 20.205  -24.212 1.00 60.71  ? 260 SER A O   1 
ATOM   1841 C CB  . SER A 1 260 ? -5.858 22.988  -25.294 1.00 57.50  ? 260 SER A CB  1 
ATOM   1842 O OG  . SER A 1 260 ? -7.014 22.544  -25.974 1.00 68.98  ? 260 SER A OG  1 
ATOM   1843 N N   . ASP A 1 261 ? -5.429 19.836  -26.416 1.00 64.54  ? 261 ASP A N   1 
ATOM   1844 C CA  . ASP A 1 261 ? -5.831 18.409  -26.296 1.00 67.98  ? 261 ASP A CA  1 
ATOM   1845 C C   . ASP A 1 261 ? -4.634 17.541  -25.900 1.00 60.64  ? 261 ASP A C   1 
ATOM   1846 O O   . ASP A 1 261 ? -4.856 16.534  -25.229 1.00 58.61  ? 261 ASP A O   1 
ATOM   1847 C CB  . ASP A 1 261 ? -6.430 17.885  -27.604 1.00 79.44  ? 261 ASP A CB  1 
ATOM   1848 C CG  . ASP A 1 261 ? -7.826 18.398  -27.912 1.00 85.71  ? 261 ASP A CG  1 
ATOM   1849 O OD1 . ASP A 1 261 ? -8.456 19.020  -27.019 1.00 86.23  ? 261 ASP A OD1 1 
ATOM   1850 O OD2 . ASP A 1 261 ? -8.278 18.153  -29.043 1.00 92.15  ? 261 ASP A OD2 1 
ATOM   1851 N N   . HIS A 1 262 ? -3.421 17.890  -26.338 1.00 62.91  ? 262 HIS A N   1 
ATOM   1852 C CA  . HIS A 1 262 ? -2.193 17.072  -26.136 1.00 64.11  ? 262 HIS A CA  1 
ATOM   1853 C C   . HIS A 1 262 ? -1.320 17.638  -25.005 1.00 60.31  ? 262 HIS A C   1 
ATOM   1854 O O   . HIS A 1 262 ? -0.533 16.861  -24.438 1.00 59.63  ? 262 HIS A O   1 
ATOM   1855 C CB  . HIS A 1 262 ? -1.411 16.947  -27.452 1.00 66.36  ? 262 HIS A CB  1 
ATOM   1856 C CG  . HIS A 1 262 ? -2.154 16.189  -28.499 1.00 74.41  ? 262 HIS A CG  1 
ATOM   1857 N ND1 . HIS A 1 262 ? -2.194 14.807  -28.512 1.00 78.74  ? 262 HIS A ND1 1 
ATOM   1858 C CD2 . HIS A 1 262 ? -2.904 16.608  -29.543 1.00 69.74  ? 262 HIS A CD2 1 
ATOM   1859 C CE1 . HIS A 1 262 ? -2.924 14.407  -29.534 1.00 79.33  ? 262 HIS A CE1 1 
ATOM   1860 N NE2 . HIS A 1 262 ? -3.371 15.497  -30.180 1.00 73.84  ? 262 HIS A NE2 1 
ATOM   1861 N N   . TYR A 1 263 ? -1.412 18.936  -24.698 1.00 56.73  ? 263 TYR A N   1 
ATOM   1862 C CA  . TYR A 1 263 ? -0.467 19.622  -23.779 1.00 52.61  ? 263 TYR A CA  1 
ATOM   1863 C C   . TYR A 1 263 ? -1.263 20.448  -22.770 1.00 52.70  ? 263 TYR A C   1 
ATOM   1864 O O   . TYR A 1 263 ? -2.093 21.290  -23.177 1.00 56.53  ? 263 TYR A O   1 
ATOM   1865 C CB  . TYR A 1 263 ? 0.584  20.422  -24.563 1.00 49.47  ? 263 TYR A CB  1 
ATOM   1866 C CG  . TYR A 1 263 ? 1.444  19.547  -25.436 1.00 47.39  ? 263 TYR A CG  1 
ATOM   1867 C CD1 . TYR A 1 263 ? 2.352  18.661  -24.880 1.00 48.31  ? 263 TYR A CD1 1 
ATOM   1868 C CD2 . TYR A 1 263 ? 1.291  19.542  -26.810 1.00 48.64  ? 263 TYR A CD2 1 
ATOM   1869 C CE1 . TYR A 1 263 ? 3.122  17.824  -25.668 1.00 47.90  ? 263 TYR A CE1 1 
ATOM   1870 C CE2 . TYR A 1 263 ? 2.049  18.710  -27.614 1.00 50.93  ? 263 TYR A CE2 1 
ATOM   1871 C CZ  . TYR A 1 263 ? 2.959  17.841  -27.041 1.00 51.92  ? 263 TYR A CZ  1 
ATOM   1872 O OH  . TYR A 1 263 ? 3.704  17.029  -27.840 1.00 54.53  ? 263 TYR A OH  1 
ATOM   1873 N N   . SER A 1 264 ? -0.980 20.189  -21.490 1.00 50.90  ? 264 SER A N   1 
ATOM   1874 C CA  . SER A 1 264 ? -1.629 20.762  -20.283 1.00 52.09  ? 264 SER A CA  1 
ATOM   1875 C C   . SER A 1 264 ? -1.596 22.298  -20.303 1.00 55.44  ? 264 SER A C   1 
ATOM   1876 O O   . SER A 1 264 ? -0.659 22.900  -20.910 1.00 53.58  ? 264 SER A O   1 
ATOM   1877 C CB  . SER A 1 264 ? -0.948 20.241  -19.033 1.00 51.38  ? 264 SER A CB  1 
ATOM   1878 O OG  . SER A 1 264 ? 0.368  20.789  -18.898 1.00 48.45  ? 264 SER A OG  1 
ATOM   1879 N N   . GLU A 1 265 ? -2.549 22.904  -19.594 1.00 60.34  ? 265 GLU A N   1 
ATOM   1880 C CA  . GLU A 1 265 ? -2.573 24.356  -19.283 1.00 64.95  ? 265 GLU A CA  1 
ATOM   1881 C C   . GLU A 1 265 ? -1.235 24.748  -18.624 1.00 58.79  ? 265 GLU A C   1 
ATOM   1882 O O   . GLU A 1 265 ? -0.716 25.833  -18.928 1.00 47.83  ? 265 GLU A O   1 
ATOM   1883 C CB  . GLU A 1 265 ? -3.789 24.667  -18.407 1.00 72.28  ? 265 GLU A CB  1 
ATOM   1884 C CG  . GLU A 1 265 ? -3.962 26.147  -18.119 1.00 90.08  ? 265 GLU A CG  1 
ATOM   1885 C CD  . GLU A 1 265 ? -4.927 26.486  -16.992 1.00 106.86 ? 265 GLU A CD  1 
ATOM   1886 O OE1 . GLU A 1 265 ? -5.465 25.550  -16.362 1.00 125.24 ? 265 GLU A OE1 1 
ATOM   1887 O OE2 . GLU A 1 265 ? -5.120 27.690  -16.731 1.00 116.83 ? 265 GLU A OE2 1 
ATOM   1888 N N   . GLU A 1 266 ? -0.689 23.895  -17.753 1.00 54.10  ? 266 GLU A N   1 
ATOM   1889 C CA  . GLU A 1 266 ? 0.564  24.184  -17.001 1.00 51.84  ? 266 GLU A CA  1 
ATOM   1890 C C   . GLU A 1 266 ? 1.704  24.400  -18.000 1.00 45.83  ? 266 GLU A C   1 
ATOM   1891 O O   . GLU A 1 266 ? 2.378  25.433  -17.904 1.00 50.98  ? 266 GLU A O   1 
ATOM   1892 C CB  . GLU A 1 266 ? 0.884  23.074  -15.999 1.00 55.57  ? 266 GLU A CB  1 
ATOM   1893 C CG  . GLU A 1 266 ? -0.069 23.030  -14.801 1.00 62.18  ? 266 GLU A CG  1 
ATOM   1894 C CD  . GLU A 1 266 ? -1.428 22.377  -15.039 1.00 61.83  ? 266 GLU A CD  1 
ATOM   1895 O OE1 . GLU A 1 266 ? -1.749 22.060  -16.209 1.00 61.62  ? 266 GLU A OE1 1 
ATOM   1896 O OE2 . GLU A 1 266 ? -2.172 22.191  -14.059 1.00 71.19  ? 266 GLU A OE2 1 
ATOM   1897 N N   . LEU A 1 267 ? 1.863  23.498  -18.965 1.00 44.84  ? 267 LEU A N   1 
ATOM   1898 C CA  . LEU A 1 267 ? 2.969  23.536  -19.956 1.00 43.73  ? 267 LEU A CA  1 
ATOM   1899 C C   . LEU A 1 267 ? 2.836  24.788  -20.825 1.00 43.62  ? 267 LEU A C   1 
ATOM   1900 O O   . LEU A 1 267 ? 3.820  25.544  -20.949 1.00 42.92  ? 267 LEU A O   1 
ATOM   1901 C CB  . LEU A 1 267 ? 2.919  22.261  -20.796 1.00 44.90  ? 267 LEU A CB  1 
ATOM   1902 C CG  . LEU A 1 267 ? 4.149  22.036  -21.666 1.00 46.49  ? 267 LEU A CG  1 
ATOM   1903 C CD1 . LEU A 1 267 ? 4.331  20.553  -21.962 1.00 47.68  ? 267 LEU A CD1 1 
ATOM   1904 C CD2 . LEU A 1 267 ? 4.043  22.844  -22.956 1.00 46.85  ? 267 LEU A CD2 1 
ATOM   1905 N N   . ARG A 1 268 ? 1.634  25.010  -21.358 1.00 47.44  ? 268 ARG A N   1 
ATOM   1906 C CA  . ARG A 1 268 ? 1.253  26.185  -22.189 1.00 45.72  ? 268 ARG A CA  1 
ATOM   1907 C C   . ARG A 1 268 ? 1.446  27.492  -21.412 1.00 43.17  ? 268 ARG A C   1 
ATOM   1908 O O   . ARG A 1 268 ? 2.050  28.441  -21.955 1.00 46.12  ? 268 ARG A O   1 
ATOM   1909 C CB  . ARG A 1 268 ? -0.179 25.967  -22.682 1.00 50.43  ? 268 ARG A CB  1 
ATOM   1910 C CG  . ARG A 1 268 ? -0.283 24.761  -23.608 1.00 48.75  ? 268 ARG A CG  1 
ATOM   1911 C CD  . ARG A 1 268 ? -1.593 24.652  -24.353 1.00 51.67  ? 268 ARG A CD  1 
ATOM   1912 N NE  . ARG A 1 268 ? -2.631 24.121  -23.480 1.00 54.53  ? 268 ARG A NE  1 
ATOM   1913 C CZ  . ARG A 1 268 ? -3.556 24.856  -22.874 1.00 56.93  ? 268 ARG A CZ  1 
ATOM   1914 N NH1 . ARG A 1 268 ? -3.577 26.168  -23.048 1.00 59.46  ? 268 ARG A NH1 1 
ATOM   1915 N NH2 . ARG A 1 268 ? -4.455 24.274  -22.096 1.00 58.12  ? 268 ARG A NH2 1 
ATOM   1916 N N   . GLN A 1 269 ? 1.026  27.543  -20.154 1.00 46.18  ? 269 GLN A N   1 
ATOM   1917 C CA  . GLN A 1 269 ? 1.192  28.773  -19.332 1.00 48.47  ? 269 GLN A CA  1 
ATOM   1918 C C   . GLN A 1 269 ? 2.691  28.984  -19.057 1.00 44.56  ? 269 GLN A C   1 
ATOM   1919 O O   . GLN A 1 269 ? 3.130  30.124  -19.056 1.00 45.57  ? 269 GLN A O   1 
ATOM   1920 C CB  . GLN A 1 269 ? 0.318  28.705  -18.075 1.00 51.98  ? 269 GLN A CB  1 
ATOM   1921 C CG  . GLN A 1 269 ? 0.337  29.974  -17.219 1.00 61.84  ? 269 GLN A CG  1 
ATOM   1922 C CD  . GLN A 1 269 ? 0.263  31.283  -17.983 1.00 65.00  ? 269 GLN A CD  1 
ATOM   1923 O OE1 . GLN A 1 269 ? -0.329 31.394  -19.057 1.00 82.19  ? 269 GLN A OE1 1 
ATOM   1924 N NE2 . GLN A 1 269 ? 0.852  32.321  -17.417 1.00 61.72  ? 269 GLN A NE2 1 
ATOM   1925 N N   . LEU A 1 270 ? 3.477  27.923  -18.892 1.00 44.77  ? 270 LEU A N   1 
ATOM   1926 C CA  . LEU A 1 270 ? 4.924  28.074  -18.584 1.00 47.79  ? 270 LEU A CA  1 
ATOM   1927 C C   . LEU A 1 270 ? 5.664  28.642  -19.804 1.00 46.34  ? 270 LEU A C   1 
ATOM   1928 O O   . LEU A 1 270 ? 6.526  29.536  -19.610 1.00 49.46  ? 270 LEU A O   1 
ATOM   1929 C CB  . LEU A 1 270 ? 5.517  26.730  -18.146 1.00 44.35  ? 270 LEU A CB  1 
ATOM   1930 C CG  . LEU A 1 270 ? 6.976  26.831  -17.713 1.00 40.97  ? 270 LEU A CG  1 
ATOM   1931 C CD1 . LEU A 1 270 ? 7.128  27.857  -16.600 1.00 39.10  ? 270 LEU A CD1 1 
ATOM   1932 C CD2 . LEU A 1 270 ? 7.515  25.478  -17.291 1.00 42.94  ? 270 LEU A CD2 1 
ATOM   1933 N N   . VAL A 1 271 ? 5.347  28.140  -21.006 1.00 48.49  ? 271 VAL A N   1 
ATOM   1934 C CA  . VAL A 1 271 ? 5.825  28.703  -22.308 1.00 48.92  ? 271 VAL A CA  1 
ATOM   1935 C C   . VAL A 1 271 ? 5.435  30.188  -22.380 1.00 44.35  ? 271 VAL A C   1 
ATOM   1936 O O   . VAL A 1 271 ? 6.284  31.023  -22.732 1.00 43.97  ? 271 VAL A O   1 
ATOM   1937 C CB  . VAL A 1 271 ? 5.237  27.925  -23.499 1.00 49.39  ? 271 VAL A CB  1 
ATOM   1938 C CG1 . VAL A 1 271 ? 5.482  28.640  -24.819 1.00 49.18  ? 271 VAL A CG1 1 
ATOM   1939 C CG2 . VAL A 1 271 ? 5.761  26.498  -23.561 1.00 48.72  ? 271 VAL A CG2 1 
ATOM   1940 N N   . ASN A 1 272 ? 4.184  30.490  -22.058 1.00 45.53  ? 272 ASN A N   1 
ATOM   1941 C CA  . ASN A 1 272 ? 3.607  31.849  -22.163 1.00 48.16  ? 272 ASN A CA  1 
ATOM   1942 C C   . ASN A 1 272 ? 4.400  32.828  -21.286 1.00 49.18  ? 272 ASN A C   1 
ATOM   1943 O O   . ASN A 1 272 ? 4.678  33.937  -21.778 1.00 45.39  ? 272 ASN A O   1 
ATOM   1944 C CB  . ASN A 1 272 ? 2.117  31.837  -21.832 1.00 51.96  ? 272 ASN A CB  1 
ATOM   1945 C CG  . ASN A 1 272 ? 1.459  33.193  -22.014 1.00 60.17  ? 272 ASN A CG  1 
ATOM   1946 O OD1 . ASN A 1 272 ? 1.752  33.924  -22.970 1.00 53.77  ? 272 ASN A OD1 1 
ATOM   1947 N ND2 . ASN A 1 272 ? 0.560  33.531  -21.102 1.00 59.28  ? 272 ASN A ND2 1 
ATOM   1948 N N   . MET A 1 273 ? 4.782  32.471  -20.051 1.00 47.30  ? 273 MET A N   1 
ATOM   1949 C CA  . MET A 1 273 ? 5.453  33.472  -19.183 1.00 46.71  ? 273 MET A CA  1 
ATOM   1950 C C   . MET A 1 273 ? 6.925  33.612  -19.579 1.00 46.71  ? 273 MET A C   1 
ATOM   1951 O O   . MET A 1 273 ? 7.516  34.695  -19.367 1.00 45.84  ? 273 MET A O   1 
ATOM   1952 C CB  . MET A 1 273 ? 5.272  33.210  -17.683 1.00 56.18  ? 273 MET A CB  1 
ATOM   1953 C CG  . MET A 1 273 ? 5.746  31.880  -17.136 1.00 63.50  ? 273 MET A CG  1 
ATOM   1954 S SD  . MET A 1 273 ? 5.167  31.628  -15.404 1.00 68.40  ? 273 MET A SD  1 
ATOM   1955 C CE  . MET A 1 273 ? 3.451  31.184  -15.648 1.00 64.17  ? 273 MET A CE  1 
ATOM   1956 N N   . CYS A 1 274 ? 7.509  32.603  -20.207 1.00 47.11  ? 274 CYS A N   1 
ATOM   1957 C CA  . CYS A 1 274 ? 8.947  32.660  -20.571 1.00 46.23  ? 274 CYS A CA  1 
ATOM   1958 C C   . CYS A 1 274 ? 9.080  33.483  -21.841 1.00 43.01  ? 274 CYS A C   1 
ATOM   1959 O O   . CYS A 1 274 ? 10.099 34.174  -21.974 1.00 39.94  ? 274 CYS A O   1 
ATOM   1960 C CB  . CYS A 1 274 ? 9.557  31.279  -20.798 1.00 50.22  ? 274 CYS A CB  1 
ATOM   1961 S SG  . CYS A 1 274 ? 9.698  30.252  -19.313 1.00 46.72  ? 274 CYS A SG  1 
ATOM   1962 N N   . ILE A 1 275 ? 8.111  33.358  -22.752 1.00 45.72  ? 275 ILE A N   1 
ATOM   1963 C CA  . ILE A 1 275 ? 8.137  34.074  -24.062 1.00 50.35  ? 275 ILE A CA  1 
ATOM   1964 C C   . ILE A 1 275 ? 7.381  35.382  -23.850 1.00 50.36  ? 275 ILE A C   1 
ATOM   1965 O O   . ILE A 1 275 ? 6.205  35.458  -24.206 1.00 48.16  ? 275 ILE A O   1 
ATOM   1966 C CB  . ILE A 1 275 ? 7.570  33.237  -25.227 1.00 50.04  ? 275 ILE A CB  1 
ATOM   1967 C CG1 . ILE A 1 275 ? 8.331  31.919  -25.364 1.00 55.47  ? 275 ILE A CG1 1 
ATOM   1968 C CG2 . ILE A 1 275 ? 7.611  34.038  -26.528 1.00 52.03  ? 275 ILE A CG2 1 
ATOM   1969 C CD1 . ILE A 1 275 ? 7.830  31.011  -26.454 1.00 56.12  ? 275 ILE A CD1 1 
ATOM   1970 N N   . ASN A 1 276 ? 8.062  36.333  -23.223 1.00 49.24  ? 276 ASN A N   1 
ATOM   1971 C CA  . ASN A 1 276 ? 7.534  37.661  -22.863 1.00 44.87  ? 276 ASN A CA  1 
ATOM   1972 C C   . ASN A 1 276 ? 8.595  38.674  -23.253 1.00 47.87  ? 276 ASN A C   1 
ATOM   1973 O O   . ASN A 1 276 ? 9.780  38.493  -22.973 1.00 46.38  ? 276 ASN A O   1 
ATOM   1974 C CB  . ASN A 1 276 ? 7.132  37.713  -21.398 1.00 44.07  ? 276 ASN A CB  1 
ATOM   1975 C CG  . ASN A 1 276 ? 6.599  39.067  -20.965 1.00 44.83  ? 276 ASN A CG  1 
ATOM   1976 O OD1 . ASN A 1 276 ? 7.283  40.084  -21.065 1.00 47.28  ? 276 ASN A OD1 1 
ATOM   1977 N ND2 . ASN A 1 276 ? 5.390  39.084  -20.439 1.00 47.21  ? 276 ASN A ND2 1 
ATOM   1978 N N   . PRO A 1 277 ? 8.199  39.753  -23.956 1.00 49.40  ? 277 PRO A N   1 
ATOM   1979 C CA  . PRO A 1 277 ? 9.170  40.671  -24.533 1.00 42.58  ? 277 PRO A CA  1 
ATOM   1980 C C   . PRO A 1 277 ? 10.064 41.288  -23.462 1.00 43.76  ? 277 PRO A C   1 
ATOM   1981 O O   . PRO A 1 277 ? 11.169 41.642  -23.789 1.00 51.86  ? 277 PRO A O   1 
ATOM   1982 C CB  . PRO A 1 277 ? 8.315  41.771  -25.170 1.00 44.52  ? 277 PRO A CB  1 
ATOM   1983 C CG  . PRO A 1 277 ? 6.961  41.125  -25.373 1.00 48.72  ? 277 PRO A CG  1 
ATOM   1984 C CD  . PRO A 1 277 ? 6.805  40.139  -24.236 1.00 46.65  ? 277 PRO A CD  1 
ATOM   1985 N N   . ASP A 1 278 ? 9.528  41.478  -22.251 1.00 45.23  ? 278 ASP A N   1 
ATOM   1986 C CA  . ASP A 1 278 ? 10.225 42.188  -21.151 1.00 44.86  ? 278 ASP A CA  1 
ATOM   1987 C C   . ASP A 1 278 ? 10.974 41.148  -20.324 1.00 45.88  ? 278 ASP A C   1 
ATOM   1988 O O   . ASP A 1 278 ? 10.357 40.339  -19.613 1.00 39.42  ? 278 ASP A O   1 
ATOM   1989 C CB  . ASP A 1 278 ? 9.250  42.986  -20.282 1.00 47.67  ? 278 ASP A CB  1 
ATOM   1990 C CG  . ASP A 1 278 ? 9.918  43.876  -19.234 1.00 48.17  ? 278 ASP A CG  1 
ATOM   1991 O OD1 . ASP A 1 278 ? 11.164 43.923  -19.180 1.00 48.46  ? 278 ASP A OD1 1 
ATOM   1992 O OD2 . ASP A 1 278 ? 9.178  44.550  -18.502 1.00 55.60  ? 278 ASP A OD2 1 
ATOM   1993 N N   . PRO A 1 279 ? 12.321 41.184  -20.357 1.00 47.39  ? 279 PRO A N   1 
ATOM   1994 C CA  . PRO A 1 279 ? 13.127 40.242  -19.590 1.00 47.50  ? 279 PRO A CA  1 
ATOM   1995 C C   . PRO A 1 279 ? 12.743 40.267  -18.094 1.00 50.27  ? 279 PRO A C   1 
ATOM   1996 O O   . PRO A 1 279 ? 12.641 39.207  -17.518 1.00 49.50  ? 279 PRO A O   1 
ATOM   1997 C CB  . PRO A 1 279 ? 14.578 40.682  -19.835 1.00 49.40  ? 279 PRO A CB  1 
ATOM   1998 C CG  . PRO A 1 279 ? 14.539 41.660  -21.006 1.00 48.78  ? 279 PRO A CG  1 
ATOM   1999 C CD  . PRO A 1 279 ? 13.128 42.194  -21.057 1.00 50.79  ? 279 PRO A CD  1 
ATOM   2000 N N   . GLU A 1 280 ? 12.455 41.440  -17.514 1.00 51.26  ? 280 GLU A N   1 
ATOM   2001 C CA  . GLU A 1 280 ? 12.165 41.595  -16.059 1.00 52.44  ? 280 GLU A CA  1 
ATOM   2002 C C   . GLU A 1 280 ? 10.869 40.880  -15.653 1.00 47.03  ? 280 GLU A C   1 
ATOM   2003 O O   . GLU A 1 280 ? 10.700 40.649  -14.454 1.00 49.67  ? 280 GLU A O   1 
ATOM   2004 C CB  . GLU A 1 280 ? 12.097 43.070  -15.657 1.00 62.26  ? 280 GLU A CB  1 
ATOM   2005 C CG  . GLU A 1 280 ? 13.465 43.741  -15.611 1.00 72.23  ? 280 GLU A CG  1 
ATOM   2006 C CD  . GLU A 1 280 ? 13.453 45.183  -15.130 1.00 80.92  ? 280 GLU A CD  1 
ATOM   2007 O OE1 . GLU A 1 280 ? 12.350 45.739  -14.930 1.00 96.78  ? 280 GLU A OE1 1 
ATOM   2008 O OE2 . GLU A 1 280 ? 14.544 45.749  -14.961 1.00 85.18  ? 280 GLU A OE2 1 
ATOM   2009 N N   . LYS A 1 281 ? 9.997  40.510  -16.589 1.00 43.12  ? 281 LYS A N   1 
ATOM   2010 C CA  . LYS A 1 281 ? 8.717  39.839  -16.259 1.00 44.76  ? 281 LYS A CA  1 
ATOM   2011 C C   . LYS A 1 281 ? 8.818  38.344  -16.557 1.00 40.36  ? 281 LYS A C   1 
ATOM   2012 O O   . LYS A 1 281 ? 7.851  37.640  -16.290 1.00 40.70  ? 281 LYS A O   1 
ATOM   2013 C CB  . LYS A 1 281 ? 7.561  40.495  -17.022 1.00 52.09  ? 281 LYS A CB  1 
ATOM   2014 C CG  . LYS A 1 281 ? 7.583  42.017  -16.978 1.00 61.17  ? 281 LYS A CG  1 
ATOM   2015 C CD  . LYS A 1 281 ? 6.299  42.658  -16.525 1.00 74.11  ? 281 LYS A CD  1 
ATOM   2016 C CE  . LYS A 1 281 ? 6.219  44.130  -16.883 1.00 75.78  ? 281 LYS A CE  1 
ATOM   2017 N NZ  . LYS A 1 281 ? 5.592  44.319  -18.216 1.00 74.87  ? 281 LYS A NZ  1 
ATOM   2018 N N   . ARG A 1 282 ? 9.930  37.878  -17.123 1.00 42.37  ? 282 ARG A N   1 
ATOM   2019 C CA  . ARG A 1 282 ? 10.165 36.426  -17.330 1.00 45.10  ? 282 ARG A CA  1 
ATOM   2020 C C   . ARG A 1 282 ? 10.495 35.837  -15.966 1.00 47.04  ? 282 ARG A C   1 
ATOM   2021 O O   . ARG A 1 282 ? 11.099 36.517  -15.136 1.00 49.79  ? 282 ARG A O   1 
ATOM   2022 C CB  . ARG A 1 282 ? 11.275 36.191  -18.356 1.00 42.29  ? 282 ARG A CB  1 
ATOM   2023 C CG  . ARG A 1 282 ? 10.884 36.612  -19.765 1.00 43.19  ? 282 ARG A CG  1 
ATOM   2024 C CD  . ARG A 1 282 ? 12.039 36.444  -20.725 1.00 45.41  ? 282 ARG A CD  1 
ATOM   2025 N NE  . ARG A 1 282 ? 11.966 37.428  -21.784 1.00 44.62  ? 282 ARG A NE  1 
ATOM   2026 C CZ  . ARG A 1 282 ? 13.007 37.996  -22.369 1.00 47.58  ? 282 ARG A CZ  1 
ATOM   2027 N NH1 . ARG A 1 282 ? 14.244 37.674  -22.010 1.00 41.08  ? 282 ARG A NH1 1 
ATOM   2028 N NH2 . ARG A 1 282 ? 12.790 38.902  -23.308 1.00 44.92  ? 282 ARG A NH2 1 
ATOM   2029 N N   . PRO A 1 283 ? 10.061 34.597  -15.655 1.00 45.77  ? 283 PRO A N   1 
ATOM   2030 C CA  . PRO A 1 283 ? 10.380 33.996  -14.361 1.00 48.96  ? 283 PRO A CA  1 
ATOM   2031 C C   . PRO A 1 283 ? 11.883 33.719  -14.294 1.00 46.33  ? 283 PRO A C   1 
ATOM   2032 O O   . PRO A 1 283 ? 12.540 33.700  -15.325 1.00 45.86  ? 283 PRO A O   1 
ATOM   2033 C CB  . PRO A 1 283 ? 9.517  32.733  -14.313 1.00 50.27  ? 283 PRO A CB  1 
ATOM   2034 C CG  . PRO A 1 283 ? 9.297  32.395  -15.764 1.00 50.69  ? 283 PRO A CG  1 
ATOM   2035 C CD  . PRO A 1 283 ? 9.257  33.717  -16.505 1.00 46.33  ? 283 PRO A CD  1 
ATOM   2036 N N   . ASP A 1 284 ? 12.429 33.591  -13.092 1.00 46.50  ? 284 ASP A N   1 
ATOM   2037 C CA  . ASP A 1 284 ? 13.846 33.166  -12.952 1.00 47.48  ? 284 ASP A CA  1 
ATOM   2038 C C   . ASP A 1 284 ? 13.840 31.638  -13.060 1.00 38.42  ? 284 ASP A C   1 
ATOM   2039 O O   . ASP A 1 284 ? 12.769 31.006  -13.003 1.00 32.86  ? 284 ASP A O   1 
ATOM   2040 C CB  . ASP A 1 284 ? 14.542 33.779  -11.724 1.00 57.16  ? 284 ASP A CB  1 
ATOM   2041 C CG  . ASP A 1 284 ? 14.059 33.258  -10.382 1.00 65.40  ? 284 ASP A CG  1 
ATOM   2042 O OD1 . ASP A 1 284 ? 13.565 32.105  -10.329 1.00 72.76  ? 284 ASP A OD1 1 
ATOM   2043 O OD2 . ASP A 1 284 ? 14.194 34.005  -9.400  1.00 77.37  ? 284 ASP A OD2 1 
ATOM   2044 N N   . VAL A 1 285 ? 15.001 31.065  -13.292 1.00 37.68  ? 285 VAL A N   1 
ATOM   2045 C CA  . VAL A 1 285 ? 15.129 29.611  -13.576 1.00 43.80  ? 285 VAL A CA  1 
ATOM   2046 C C   . VAL A 1 285 ? 14.635 28.797  -12.377 1.00 40.93  ? 285 VAL A C   1 
ATOM   2047 O O   . VAL A 1 285 ? 13.949 27.802  -12.614 1.00 42.78  ? 285 VAL A O   1 
ATOM   2048 C CB  . VAL A 1 285 ? 16.576 29.286  -13.963 1.00 46.93  ? 285 VAL A CB  1 
ATOM   2049 C CG1 . VAL A 1 285 ? 17.510 29.410  -12.763 1.00 49.66  ? 285 VAL A CG1 1 
ATOM   2050 C CG2 . VAL A 1 285 ? 16.654 27.931  -14.635 1.00 50.05  ? 285 VAL A CG2 1 
ATOM   2051 N N   . THR A 1 286 ? 14.897 29.231  -11.138 1.00 42.59  ? 286 THR A N   1 
ATOM   2052 C CA  . THR A 1 286 ? 14.418 28.522  -9.917  1.00 43.52  ? 286 THR A CA  1 
ATOM   2053 C C   . THR A 1 286 ? 12.912 28.246  -10.032 1.00 43.83  ? 286 THR A C   1 
ATOM   2054 O O   . THR A 1 286 ? 12.485 27.128  -9.710  1.00 43.01  ? 286 THR A O   1 
ATOM   2055 C CB  . THR A 1 286 ? 14.713 29.307  -8.631  1.00 50.71  ? 286 THR A CB  1 
ATOM   2056 O OG1 . THR A 1 286 ? 16.114 29.493  -8.454  1.00 44.57  ? 286 THR A OG1 1 
ATOM   2057 C CG2 . THR A 1 286 ? 14.201 28.595  -7.402  1.00 52.63  ? 286 THR A CG2 1 
ATOM   2058 N N   . TYR A 1 287 ? 12.123 29.234  -10.464 1.00 42.78  ? 287 TYR A N   1 
ATOM   2059 C CA  . TYR A 1 287 ? 10.654 29.092  -10.617 1.00 41.17  ? 287 TYR A CA  1 
ATOM   2060 C C   . TYR A 1 287 ? 10.349 28.051  -11.713 1.00 44.55  ? 287 TYR A C   1 
ATOM   2061 O O   . TYR A 1 287 ? 9.444  27.192  -11.557 1.00 44.95  ? 287 TYR A O   1 
ATOM   2062 C CB  . TYR A 1 287 ? 10.010 30.451  -10.920 1.00 40.58  ? 287 TYR A CB  1 
ATOM   2063 C CG  . TYR A 1 287 ? 8.547  30.318  -11.240 1.00 39.91  ? 287 TYR A CG  1 
ATOM   2064 C CD1 . TYR A 1 287 ? 8.114  29.999  -12.514 1.00 40.21  ? 287 TYR A CD1 1 
ATOM   2065 C CD2 . TYR A 1 287 ? 7.599  30.419  -10.250 1.00 42.63  ? 287 TYR A CD2 1 
ATOM   2066 C CE1 . TYR A 1 287 ? 6.771  29.822  -12.807 1.00 42.32  ? 287 TYR A CE1 1 
ATOM   2067 C CE2 . TYR A 1 287 ? 6.249  30.239  -10.521 1.00 47.37  ? 287 TYR A CE2 1 
ATOM   2068 C CZ  . TYR A 1 287 ? 5.832  29.944  -11.803 1.00 45.75  ? 287 TYR A CZ  1 
ATOM   2069 O OH  . TYR A 1 287 ? 4.509  29.782  -12.050 1.00 49.18  ? 287 TYR A OH  1 
ATOM   2070 N N   . VAL A 1 288 ? 11.069 28.131  -12.829 1.00 39.39  ? 288 VAL A N   1 
ATOM   2071 C CA  . VAL A 1 288 ? 10.861 27.225  -13.992 1.00 38.88  ? 288 VAL A CA  1 
ATOM   2072 C C   . VAL A 1 288 ? 11.261 25.809  -13.556 1.00 38.15  ? 288 VAL A C   1 
ATOM   2073 O O   . VAL A 1 288 ? 10.472 24.879  -13.803 1.00 39.22  ? 288 VAL A O   1 
ATOM   2074 C CB  . VAL A 1 288 ? 11.606 27.714  -15.253 1.00 38.21  ? 288 VAL A CB  1 
ATOM   2075 C CG1 . VAL A 1 288 ? 11.388 26.799  -16.447 1.00 37.14  ? 288 VAL A CG1 1 
ATOM   2076 C CG2 . VAL A 1 288 ? 11.181 29.123  -15.642 1.00 39.15  ? 288 VAL A CG2 1 
ATOM   2077 N N   . TYR A 1 289 ? 12.380 25.650  -12.846 1.00 40.77  ? 289 TYR A N   1 
ATOM   2078 C CA  . TYR A 1 289 ? 12.853 24.329  -12.337 1.00 41.85  ? 289 TYR A CA  1 
ATOM   2079 C C   . TYR A 1 289 ? 11.774 23.750  -11.405 1.00 45.13  ? 289 TYR A C   1 
ATOM   2080 O O   . TYR A 1 289 ? 11.366 22.560  -11.576 1.00 44.29  ? 289 TYR A O   1 
ATOM   2081 C CB  . TYR A 1 289 ? 14.233 24.503  -11.709 1.00 42.37  ? 289 TYR A CB  1 
ATOM   2082 C CG  . TYR A 1 289 ? 14.907 23.262  -11.186 1.00 46.12  ? 289 TYR A CG  1 
ATOM   2083 C CD1 . TYR A 1 289 ? 14.726 22.023  -11.782 1.00 48.08  ? 289 TYR A CD1 1 
ATOM   2084 C CD2 . TYR A 1 289 ? 15.787 23.343  -10.111 1.00 46.67  ? 289 TYR A CD2 1 
ATOM   2085 C CE1 . TYR A 1 289 ? 15.371 20.890  -11.301 1.00 45.36  ? 289 TYR A CE1 1 
ATOM   2086 C CE2 . TYR A 1 289 ? 16.439 22.222  -9.621  1.00 42.43  ? 289 TYR A CE2 1 
ATOM   2087 C CZ  . TYR A 1 289 ? 16.218 20.986  -10.207 1.00 45.13  ? 289 TYR A CZ  1 
ATOM   2088 O OH  . TYR A 1 289 ? 16.858 19.872  -9.734  1.00 44.05  ? 289 TYR A OH  1 
ATOM   2089 N N   . ASP A 1 290 ? 11.232 24.600  -10.530 1.00 40.51  ? 290 ASP A N   1 
ATOM   2090 C CA  . ASP A 1 290 ? 10.236 24.196  -9.513  1.00 43.85  ? 290 ASP A CA  1 
ATOM   2091 C C   . ASP A 1 290 ? 8.983  23.705  -10.243 1.00 43.66  ? 290 ASP A C   1 
ATOM   2092 O O   . ASP A 1 290 ? 8.466  22.616  -9.896  1.00 47.96  ? 290 ASP A O   1 
ATOM   2093 C CB  . ASP A 1 290 ? 10.022 25.302  -8.463  1.00 46.10  ? 290 ASP A CB  1 
ATOM   2094 C CG  . ASP A 1 290 ? 11.073 25.326  -7.351  1.00 47.64  ? 290 ASP A CG  1 
ATOM   2095 O OD1 . ASP A 1 290 ? 11.707 24.296  -7.118  1.00 50.47  ? 290 ASP A OD1 1 
ATOM   2096 O OD2 . ASP A 1 290 ? 11.260 26.384  -6.721  1.00 63.29  ? 290 ASP A OD2 1 
ATOM   2097 N N   . VAL A 1 291 ? 8.514  24.418  -11.257 1.00 44.37  ? 291 VAL A N   1 
ATOM   2098 C CA  . VAL A 1 291 ? 7.304  23.948  -11.984 1.00 39.79  ? 291 VAL A CA  1 
ATOM   2099 C C   . VAL A 1 291 ? 7.630  22.617  -12.654 1.00 38.93  ? 291 VAL A C   1 
ATOM   2100 O O   . VAL A 1 291 ? 6.834  21.697  -12.558 1.00 36.79  ? 291 VAL A O   1 
ATOM   2101 C CB  . VAL A 1 291 ? 6.824  24.992  -12.999 1.00 41.99  ? 291 VAL A CB  1 
ATOM   2102 C CG1 . VAL A 1 291 ? 5.703  24.459  -13.873 1.00 43.51  ? 291 VAL A CG1 1 
ATOM   2103 C CG2 . VAL A 1 291 ? 6.368  26.257  -12.300 1.00 44.21  ? 291 VAL A CG2 1 
ATOM   2104 N N   . ALA A 1 292 ? 8.766  22.538  -13.337 1.00 44.21  ? 292 ALA A N   1 
ATOM   2105 C CA  . ALA A 1 292 ? 9.176  21.344  -14.111 1.00 48.70  ? 292 ALA A CA  1 
ATOM   2106 C C   . ALA A 1 292 ? 9.255  20.126  -13.179 1.00 46.15  ? 292 ALA A C   1 
ATOM   2107 O O   . ALA A 1 292 ? 8.758  19.055  -13.569 1.00 43.47  ? 292 ALA A O   1 
ATOM   2108 C CB  . ALA A 1 292 ? 10.495 21.595  -14.805 1.00 47.09  ? 292 ALA A CB  1 
ATOM   2109 N N   . LYS A 1 293 ? 9.874  20.295  -12.008 1.00 46.83  ? 293 LYS A N   1 
ATOM   2110 C CA  . LYS A 1 293 ? 10.078 19.221  -10.996 1.00 47.06  ? 293 LYS A CA  1 
ATOM   2111 C C   . LYS A 1 293 ? 8.711  18.706  -10.567 1.00 47.20  ? 293 LYS A C   1 
ATOM   2112 O O   . LYS A 1 293 ? 8.484  17.491  -10.628 1.00 49.32  ? 293 LYS A O   1 
ATOM   2113 C CB  . LYS A 1 293 ? 10.875 19.742  -9.799  1.00 44.73  ? 293 LYS A CB  1 
ATOM   2114 C CG  . LYS A 1 293 ? 12.315 19.278  -9.734  1.00 45.49  ? 293 LYS A CG  1 
ATOM   2115 C CD  . LYS A 1 293 ? 13.240 20.223  -9.013  1.00 48.92  ? 293 LYS A CD  1 
ATOM   2116 C CE  . LYS A 1 293 ? 12.706 20.794  -7.722  1.00 55.81  ? 293 LYS A CE  1 
ATOM   2117 N NZ  . LYS A 1 293 ? 13.747 21.600  -7.035  1.00 60.12  ? 293 LYS A NZ  1 
ATOM   2118 N N   . ARG A 1 294 ? 7.801  19.629  -10.265 1.00 52.43  ? 294 ARG A N   1 
ATOM   2119 C CA  . ARG A 1 294 ? 6.424  19.291  -9.832  1.00 51.33  ? 294 ARG A CA  1 
ATOM   2120 C C   . ARG A 1 294 ? 5.648  18.677  -11.000 1.00 49.65  ? 294 ARG A C   1 
ATOM   2121 O O   . ARG A 1 294 ? 4.893  17.725  -10.755 1.00 54.80  ? 294 ARG A O   1 
ATOM   2122 C CB  . ARG A 1 294 ? 5.790  20.518  -9.173  1.00 55.76  ? 294 ARG A CB  1 
ATOM   2123 C CG  . ARG A 1 294 ? 6.359  20.760  -7.777  1.00 63.38  ? 294 ARG A CG  1 
ATOM   2124 C CD  . ARG A 1 294 ? 6.209  22.182  -7.264  1.00 65.22  ? 294 ARG A CD  1 
ATOM   2125 N NE  . ARG A 1 294 ? 6.990  22.496  -6.070  1.00 63.13  ? 294 ARG A NE  1 
ATOM   2126 C CZ  . ARG A 1 294 ? 8.317  22.625  -6.013  1.00 67.86  ? 294 ARG A CZ  1 
ATOM   2127 N NH1 . ARG A 1 294 ? 9.065  22.415  -7.083  1.00 68.57  ? 294 ARG A NH1 1 
ATOM   2128 N NH2 . ARG A 1 294 ? 8.901  22.966  -4.874  1.00 67.72  ? 294 ARG A NH2 1 
ATOM   2129 N N   . MET A 1 295 ? 5.851  19.129  -12.233 1.00 47.91  ? 295 MET A N   1 
ATOM   2130 C CA  . MET A 1 295 ? 5.079  18.596  -13.384 1.00 50.14  ? 295 MET A CA  1 
ATOM   2131 C C   . MET A 1 295 ? 5.596  17.194  -13.725 1.00 52.38  ? 295 MET A C   1 
ATOM   2132 O O   . MET A 1 295 ? 4.769  16.340  -14.110 1.00 47.28  ? 295 MET A O   1 
ATOM   2133 C CB  . MET A 1 295 ? 5.176  19.505  -14.613 1.00 56.13  ? 295 MET A CB  1 
ATOM   2134 C CG  . MET A 1 295 ? 4.219  20.683  -14.571 1.00 58.26  ? 295 MET A CG  1 
ATOM   2135 S SD  . MET A 1 295 ? 2.528  20.197  -14.095 1.00 53.70  ? 295 MET A SD  1 
ATOM   2136 C CE  . MET A 1 295 ? 1.936  19.444  -15.609 1.00 57.21  ? 295 MET A CE  1 
ATOM   2137 N N   . HIS A 1 296 ? 6.912  16.982  -13.612 1.00 50.20  ? 296 HIS A N   1 
ATOM   2138 C CA  . HIS A 1 296 ? 7.571  15.658  -13.779 1.00 51.89  ? 296 HIS A CA  1 
ATOM   2139 C C   . HIS A 1 296 ? 6.983  14.667  -12.763 1.00 52.17  ? 296 HIS A C   1 
ATOM   2140 O O   . HIS A 1 296 ? 6.482  13.623  -13.198 1.00 46.22  ? 296 HIS A O   1 
ATOM   2141 C CB  . HIS A 1 296 ? 9.103  15.765  -13.640 1.00 48.01  ? 296 HIS A CB  1 
ATOM   2142 C CG  . HIS A 1 296 ? 9.818  14.470  -13.843 1.00 49.20  ? 296 HIS A CG  1 
ATOM   2143 N ND1 . HIS A 1 296 ? 9.494  13.608  -14.889 1.00 48.71  ? 296 HIS A ND1 1 
ATOM   2144 C CD2 . HIS A 1 296 ? 10.825 13.878  -13.155 1.00 44.00  ? 296 HIS A CD2 1 
ATOM   2145 C CE1 . HIS A 1 296 ? 10.292 12.554  -14.847 1.00 47.86  ? 296 HIS A CE1 1 
ATOM   2146 N NE2 . HIS A 1 296 ? 11.110 12.690  -13.790 1.00 43.49  ? 296 HIS A NE2 1 
ATOM   2147 N N   . ALA A 1 297 ? 7.053  14.979  -11.463 1.00 55.01  ? 297 ALA A N   1 
ATOM   2148 C CA  . ALA A 1 297 ? 6.569  14.100  -10.363 1.00 58.91  ? 297 ALA A CA  1 
ATOM   2149 C C   . ALA A 1 297 ? 5.109  13.683  -10.606 1.00 60.04  ? 297 ALA A C   1 
ATOM   2150 O O   . ALA A 1 297 ? 4.766  12.527  -10.349 1.00 67.81  ? 297 ALA A O   1 
ATOM   2151 C CB  . ALA A 1 297 ? 6.726  14.791  -9.031  1.00 57.70  ? 297 ALA A CB  1 
ATOM   2152 N N   . CYS A 1 298 ? 4.294  14.588  -11.134 1.00 64.31  ? 298 CYS A N   1 
ATOM   2153 C CA  . CYS A 1 298 ? 2.844  14.392  -11.355 1.00 71.70  ? 298 CYS A CA  1 
ATOM   2154 C C   . CYS A 1 298 ? 2.587  13.440  -12.538 1.00 84.61  ? 298 CYS A C   1 
ATOM   2155 O O   . CYS A 1 298 ? 1.751  12.527  -12.354 1.00 98.65  ? 298 CYS A O   1 
ATOM   2156 C CB  . CYS A 1 298 ? 2.175  15.743  -11.561 1.00 74.17  ? 298 CYS A CB  1 
ATOM   2157 S SG  . CYS A 1 298 ? 0.507  15.602  -12.238 1.00 88.45  ? 298 CYS A SG  1 
ATOM   2158 N N   . THR A 1 299 ? 3.263  13.625  -13.690 1.00 89.85  ? 299 THR A N   1 
ATOM   2159 C CA  . THR A 1 299 ? 2.974  12.929  -14.991 1.00 89.43  ? 299 THR A CA  1 
ATOM   2160 C C   . THR A 1 299 ? 3.682  11.558  -15.072 1.00 87.89  ? 299 THR A C   1 
ATOM   2161 O O   . THR A 1 299 ? 3.493  10.858  -16.090 1.00 81.11  ? 299 THR A O   1 
ATOM   2162 C CB  . THR A 1 299 ? 3.315  13.804  -16.218 1.00 83.59  ? 299 THR A CB  1 
ATOM   2163 O OG1 . THR A 1 299 ? 4.681  14.224  -16.162 1.00 71.77  ? 299 THR A OG1 1 
ATOM   2164 C CG2 . THR A 1 299 ? 2.430  15.026  -16.354 1.00 78.67  ? 299 THR A CG2 1 
ATOM   2165 N N   . ALA A 1 300 ? 4.455  11.167  -14.052 1.00 96.14  ? 300 ALA A N   1 
ATOM   2166 C CA  . ALA A 1 300 ? 5.118  9.842   -13.960 1.00 100.19 ? 300 ALA A CA  1 
ATOM   2167 C C   . ALA A 1 300 ? 4.352  8.957   -12.967 1.00 91.84  ? 300 ALA A C   1 
ATOM   2168 O O   . ALA A 1 300 ? 3.185  8.628   -13.197 1.00 87.97  ? 300 ALA A O   1 
ATOM   2169 C CB  . ALA A 1 300 ? 6.567  10.015  -13.566 1.00 97.61  ? 300 ALA A CB  1 
ATOM   2170 N N   . LYS B 1 20  ? 38.482 38.509  5.719   1.00 94.79  ? 20  LYS B N   1 
ATOM   2171 C CA  . LYS B 1 20  ? 38.885 38.748  4.295   1.00 95.18  ? 20  LYS B CA  1 
ATOM   2172 C C   . LYS B 1 20  ? 37.625 39.032  3.464   1.00 94.75  ? 20  LYS B C   1 
ATOM   2173 O O   . LYS B 1 20  ? 36.556 38.543  3.848   1.00 89.46  ? 20  LYS B O   1 
ATOM   2174 C CB  . LYS B 1 20  ? 39.681 37.551  3.764   1.00 92.30  ? 20  LYS B CB  1 
ATOM   2175 N N   . ALA B 1 21  ? 37.760 39.786  2.366   1.00 93.19  ? 21  ALA B N   1 
ATOM   2176 C CA  . ALA B 1 21  ? 36.653 40.367  1.559   1.00 86.58  ? 21  ALA B CA  1 
ATOM   2177 C C   . ALA B 1 21  ? 36.274 39.464  0.372   1.00 76.16  ? 21  ALA B C   1 
ATOM   2178 O O   . ALA B 1 21  ? 37.182 38.892  -0.268  1.00 72.43  ? 21  ALA B O   1 
ATOM   2179 C CB  . ALA B 1 21  ? 37.059 41.740  1.066   1.00 90.99  ? 21  ALA B CB  1 
ATOM   2180 N N   . LEU B 1 22  ? 34.977 39.409  0.046   1.00 66.09  ? 22  LEU B N   1 
ATOM   2181 C CA  . LEU B 1 22  ? 34.396 38.559  -1.029  1.00 68.78  ? 22  LEU B CA  1 
ATOM   2182 C C   . LEU B 1 22  ? 35.114 38.822  -2.356  1.00 66.80  ? 22  LEU B C   1 
ATOM   2183 O O   . LEU B 1 22  ? 35.506 39.962  -2.576  1.00 76.54  ? 22  LEU B O   1 
ATOM   2184 C CB  . LEU B 1 22  ? 32.893 38.836  -1.158  1.00 68.51  ? 22  LEU B CB  1 
ATOM   2185 C CG  . LEU B 1 22  ? 31.990 37.858  -0.411  1.00 74.56  ? 22  LEU B CG  1 
ATOM   2186 C CD1 . LEU B 1 22  ? 32.315 37.849  1.075   1.00 76.72  ? 22  LEU B CD1 1 
ATOM   2187 C CD2 . LEU B 1 22  ? 30.525 38.196  -0.643  1.00 79.16  ? 22  LEU B CD2 1 
ATOM   2188 N N   . ARG B 1 23  ? 35.252 37.800  -3.204  1.00 66.47  ? 23  ARG B N   1 
ATOM   2189 C CA  . ARG B 1 23  ? 35.864 37.907  -4.555  1.00 69.33  ? 23  ARG B CA  1 
ATOM   2190 C C   . ARG B 1 23  ? 35.113 37.031  -5.551  1.00 62.87  ? 23  ARG B C   1 
ATOM   2191 O O   . ARG B 1 23  ? 35.615 35.986  -5.955  1.00 64.08  ? 23  ARG B O   1 
ATOM   2192 C CB  . ARG B 1 23  ? 37.329 37.482  -4.496  1.00 76.41  ? 23  ARG B CB  1 
ATOM   2193 C CG  . ARG B 1 23  ? 38.202 38.416  -3.672  1.00 77.12  ? 23  ARG B CG  1 
ATOM   2194 C CD  . ARG B 1 23  ? 39.603 38.392  -4.231  1.00 77.31  ? 23  ARG B CD  1 
ATOM   2195 N NE  . ARG B 1 23  ? 40.497 37.597  -3.415  1.00 76.71  ? 23  ARG B NE  1 
ATOM   2196 C CZ  . ARG B 1 23  ? 41.490 36.840  -3.876  1.00 76.39  ? 23  ARG B CZ  1 
ATOM   2197 N NH1 . ARG B 1 23  ? 41.707 36.706  -5.177  1.00 71.91  ? 23  ARG B NH1 1 
ATOM   2198 N NH2 . ARG B 1 23  ? 42.260 36.199  -3.013  1.00 73.13  ? 23  ARG B NH2 1 
ATOM   2199 N N   . PRO B 1 24  ? 33.903 37.449  -5.983  1.00 63.32  ? 24  PRO B N   1 
ATOM   2200 C CA  . PRO B 1 24  ? 33.072 36.664  -6.904  1.00 65.44  ? 24  PRO B CA  1 
ATOM   2201 C C   . PRO B 1 24  ? 33.758 36.084  -8.150  1.00 67.04  ? 24  PRO B C   1 
ATOM   2202 O O   . PRO B 1 24  ? 33.288 35.073  -8.631  1.00 81.85  ? 24  PRO B O   1 
ATOM   2203 C CB  . PRO B 1 24  ? 32.011 37.683  -7.353  1.00 63.28  ? 24  PRO B CB  1 
ATOM   2204 C CG  . PRO B 1 24  ? 31.846 38.589  -6.144  1.00 66.05  ? 24  PRO B CG  1 
ATOM   2205 C CD  . PRO B 1 24  ? 33.236 38.689  -5.547  1.00 64.26  ? 24  PRO B CD  1 
ATOM   2206 N N   . ASP B 1 25  ? 34.811 36.739  -8.650  1.00 63.58  ? 25  ASP B N   1 
ATOM   2207 C CA  . ASP B 1 25  ? 35.628 36.292  -9.814  1.00 64.62  ? 25  ASP B CA  1 
ATOM   2208 C C   . ASP B 1 25  ? 36.278 34.928  -9.510  1.00 62.95  ? 25  ASP B C   1 
ATOM   2209 O O   . ASP B 1 25  ? 36.544 34.164  -10.480 1.00 56.46  ? 25  ASP B O   1 
ATOM   2210 C CB  . ASP B 1 25  ? 36.660 37.363  -10.211 1.00 72.87  ? 25  ASP B CB  1 
ATOM   2211 C CG  . ASP B 1 25  ? 37.407 38.034  -9.051  1.00 79.41  ? 25  ASP B CG  1 
ATOM   2212 O OD1 . ASP B 1 25  ? 36.748 38.505  -8.086  1.00 72.29  ? 25  ASP B OD1 1 
ATOM   2213 O OD2 . ASP B 1 25  ? 38.648 38.113  -9.126  1.00 81.42  ? 25  ASP B OD2 1 
ATOM   2214 N N   . MET B 1 26  ? 36.522 34.627  -8.224  1.00 54.53  ? 26  MET B N   1 
ATOM   2215 C CA  . MET B 1 26  ? 37.220 33.397  -7.750  1.00 55.92  ? 26  MET B CA  1 
ATOM   2216 C C   . MET B 1 26  ? 36.217 32.242  -7.572  1.00 52.40  ? 26  MET B C   1 
ATOM   2217 O O   . MET B 1 26  ? 36.647 31.062  -7.607  1.00 51.26  ? 26  MET B O   1 
ATOM   2218 C CB  . MET B 1 26  ? 37.933 33.647  -6.413  1.00 60.22  ? 26  MET B CB  1 
ATOM   2219 C CG  . MET B 1 26  ? 39.104 34.629  -6.481  1.00 59.65  ? 26  MET B CG  1 
ATOM   2220 S SD  . MET B 1 26  ? 40.438 34.148  -7.613  1.00 65.71  ? 26  MET B SD  1 
ATOM   2221 C CE  . MET B 1 26  ? 40.651 32.406  -7.245  1.00 69.95  ? 26  MET B CE  1 
ATOM   2222 N N   . GLY B 1 27  ? 34.935 32.552  -7.377  1.00 51.68  ? 27  GLY B N   1 
ATOM   2223 C CA  . GLY B 1 27  ? 33.891 31.557  -7.066  1.00 50.34  ? 27  GLY B CA  1 
ATOM   2224 C C   . GLY B 1 27  ? 34.315 30.640  -5.930  1.00 48.99  ? 27  GLY B C   1 
ATOM   2225 O O   . GLY B 1 27  ? 34.639 31.136  -4.835  1.00 51.03  ? 27  GLY B O   1 
ATOM   2226 N N   . TYR B 1 28  ? 34.367 29.334  -6.170  1.00 47.69  ? 28  TYR B N   1 
ATOM   2227 C CA  . TYR B 1 28  ? 34.595 28.349  -5.084  1.00 46.87  ? 28  TYR B CA  1 
ATOM   2228 C C   . TYR B 1 28  ? 36.098 28.179  -4.824  1.00 47.95  ? 28  TYR B C   1 
ATOM   2229 O O   . TYR B 1 28  ? 36.413 27.320  -3.987  1.00 49.50  ? 28  TYR B O   1 
ATOM   2230 C CB  . TYR B 1 28  ? 33.870 27.032  -5.390  1.00 45.32  ? 28  TYR B CB  1 
ATOM   2231 C CG  . TYR B 1 28  ? 32.416 26.994  -4.984  1.00 44.47  ? 28  TYR B CG  1 
ATOM   2232 C CD1 . TYR B 1 28  ? 31.549 28.051  -5.255  1.00 49.04  ? 28  TYR B CD1 1 
ATOM   2233 C CD2 . TYR B 1 28  ? 31.881 25.878  -4.367  1.00 45.46  ? 28  TYR B CD2 1 
ATOM   2234 C CE1 . TYR B 1 28  ? 30.206 28.010  -4.895  1.00 46.88  ? 28  TYR B CE1 1 
ATOM   2235 C CE2 . TYR B 1 28  ? 30.537 25.813  -4.022  1.00 49.84  ? 28  TYR B CE2 1 
ATOM   2236 C CZ  . TYR B 1 28  ? 29.698 26.887  -4.261  1.00 48.06  ? 28  TYR B CZ  1 
ATOM   2237 O OH  . TYR B 1 28  ? 28.380 26.808  -3.894  1.00 50.61  ? 28  TYR B OH  1 
ATOM   2238 N N   . ASN B 1 29  ? 36.983 28.986  -5.428  1.00 46.29  ? 29  ASN B N   1 
ATOM   2239 C CA  . ASN B 1 29  ? 38.452 28.724  -5.414  1.00 50.20  ? 29  ASN B CA  1 
ATOM   2240 C C   . ASN B 1 29  ? 39.217 29.698  -4.520  1.00 44.94  ? 29  ASN B C   1 
ATOM   2241 O O   . ASN B 1 29  ? 40.421 29.913  -4.789  1.00 51.87  ? 29  ASN B O   1 
ATOM   2242 C CB  . ASN B 1 29  ? 39.045 28.773  -6.824  1.00 57.76  ? 29  ASN B CB  1 
ATOM   2243 C CG  . ASN B 1 29  ? 38.986 27.424  -7.496  1.00 58.31  ? 29  ASN B CG  1 
ATOM   2244 O OD1 . ASN B 1 29  ? 39.997 26.760  -7.656  1.00 73.80  ? 29  ASN B OD1 1 
ATOM   2245 N ND2 . ASN B 1 29  ? 37.794 26.990  -7.839  1.00 67.45  ? 29  ASN B ND2 1 
ATOM   2246 N N   . THR B 1 30  ? 38.577 30.265  -3.501  1.00 43.71  ? 30  THR B N   1 
ATOM   2247 C CA  . THR B 1 30  ? 39.262 31.071  -2.452  1.00 47.85  ? 30  THR B CA  1 
ATOM   2248 C C   . THR B 1 30  ? 38.499 30.963  -1.122  1.00 46.54  ? 30  THR B C   1 
ATOM   2249 O O   . THR B 1 30  ? 37.235 30.925  -1.142  1.00 45.34  ? 30  THR B O   1 
ATOM   2250 C CB  . THR B 1 30  ? 39.475 32.517  -2.936  1.00 51.39  ? 30  THR B CB  1 
ATOM   2251 O OG1 . THR B 1 30  ? 40.602 33.071  -2.246  1.00 57.08  ? 30  THR B OG1 1 
ATOM   2252 C CG2 . THR B 1 30  ? 38.261 33.405  -2.756  1.00 51.46  ? 30  THR B CG2 1 
ATOM   2253 N N   . LEU B 1 31  ? 39.225 30.935  -0.001  1.00 48.19  ? 31  LEU B N   1 
ATOM   2254 C CA  . LEU B 1 31  ? 38.614 30.803  1.355   1.00 53.50  ? 31  LEU B CA  1 
ATOM   2255 C C   . LEU B 1 31  ? 37.777 32.035  1.713   1.00 52.33  ? 31  LEU B C   1 
ATOM   2256 O O   . LEU B 1 31  ? 36.807 31.885  2.487   1.00 53.52  ? 31  LEU B O   1 
ATOM   2257 C CB  . LEU B 1 31  ? 39.703 30.541  2.395   1.00 53.21  ? 31  LEU B CB  1 
ATOM   2258 C CG  . LEU B 1 31  ? 40.359 29.166  2.286   1.00 53.38  ? 31  LEU B CG  1 
ATOM   2259 C CD1 . LEU B 1 31  ? 41.496 29.033  3.277   1.00 48.38  ? 31  LEU B CD1 1 
ATOM   2260 C CD2 . LEU B 1 31  ? 39.330 28.066  2.487   1.00 53.61  ? 31  LEU B CD2 1 
ATOM   2261 N N   . ALA B 1 32  ? 38.104 33.196  1.160   1.00 53.32  ? 32  ALA B N   1 
ATOM   2262 C CA  . ALA B 1 32  ? 37.377 34.463  1.427   1.00 58.71  ? 32  ALA B CA  1 
ATOM   2263 C C   . ALA B 1 32  ? 35.898 34.342  1.036   1.00 53.32  ? 32  ALA B C   1 
ATOM   2264 O O   . ALA B 1 32  ? 35.108 35.167  1.517   1.00 54.10  ? 32  ALA B O   1 
ATOM   2265 C CB  . ALA B 1 32  ? 38.033 35.612  0.684   1.00 60.17  ? 32  ALA B CB  1 
ATOM   2266 N N   . ASN B 1 33  ? 35.530 33.400  0.161   1.00 51.92  ? 33  ASN B N   1 
ATOM   2267 C CA  . ASN B 1 33  ? 34.127 33.264  -0.321  1.00 45.09  ? 33  ASN B CA  1 
ATOM   2268 C C   . ASN B 1 33  ? 33.351 32.235  0.519   1.00 44.03  ? 33  ASN B C   1 
ATOM   2269 O O   . ASN B 1 33  ? 32.215 31.867  0.114   1.00 45.70  ? 33  ASN B O   1 
ATOM   2270 C CB  . ASN B 1 33  ? 34.113 32.973  -1.818  1.00 48.11  ? 33  ASN B CB  1 
ATOM   2271 C CG  . ASN B 1 33  ? 34.531 34.171  -2.645  1.00 53.23  ? 33  ASN B CG  1 
ATOM   2272 O OD1 . ASN B 1 33  ? 34.463 35.313  -2.182  1.00 56.25  ? 33  ASN B OD1 1 
ATOM   2273 N ND2 . ASN B 1 33  ? 34.962 33.923  -3.871  1.00 51.22  ? 33  ASN B ND2 1 
ATOM   2274 N N   . PHE B 1 34  ? 33.905 31.809  1.657   1.00 44.03  ? 34  PHE B N   1 
ATOM   2275 C CA  . PHE B 1 34  ? 33.292 30.820  2.584   1.00 47.62  ? 34  PHE B CA  1 
ATOM   2276 C C   . PHE B 1 34  ? 33.386 31.332  4.028   1.00 49.01  ? 34  PHE B C   1 
ATOM   2277 O O   . PHE B 1 34  ? 34.456 31.857  4.406   1.00 48.43  ? 34  PHE B O   1 
ATOM   2278 C CB  . PHE B 1 34  ? 33.987 29.456  2.444   1.00 46.83  ? 34  PHE B CB  1 
ATOM   2279 C CG  . PHE B 1 34  ? 33.894 28.846  1.066   1.00 46.86  ? 34  PHE B CG  1 
ATOM   2280 C CD1 . PHE B 1 34  ? 32.811 28.060  0.711   1.00 45.58  ? 34  PHE B CD1 1 
ATOM   2281 C CD2 . PHE B 1 34  ? 34.884 29.068  0.117   1.00 47.53  ? 34  PHE B CD2 1 
ATOM   2282 C CE1 . PHE B 1 34  ? 32.716 27.525  -0.564  1.00 48.73  ? 34  PHE B CE1 1 
ATOM   2283 C CE2 . PHE B 1 34  ? 34.794 28.512  -1.152  1.00 45.74  ? 34  PHE B CE2 1 
ATOM   2284 C CZ  . PHE B 1 34  ? 33.712 27.743  -1.489  1.00 46.04  ? 34  PHE B CZ  1 
ATOM   2285 N N   . ARG B 1 35  ? 32.312 31.166  4.810   1.00 49.83  ? 35  ARG B N   1 
ATOM   2286 C CA  . ARG B 1 35  ? 32.356 31.253  6.295   1.00 57.26  ? 35  ARG B CA  1 
ATOM   2287 C C   . ARG B 1 35  ? 32.446 29.835  6.863   1.00 52.02  ? 35  ARG B C   1 
ATOM   2288 O O   . ARG B 1 35  ? 31.506 29.074  6.683   1.00 47.04  ? 35  ARG B O   1 
ATOM   2289 C CB  . ARG B 1 35  ? 31.131 31.988  6.859   1.00 67.11  ? 35  ARG B CB  1 
ATOM   2290 C CG  . ARG B 1 35  ? 31.178 32.190  8.371   1.00 75.45  ? 35  ARG B CG  1 
ATOM   2291 C CD  . ARG B 1 35  ? 29.988 32.928  8.962   1.00 87.97  ? 35  ARG B CD  1 
ATOM   2292 N NE  . ARG B 1 35  ? 28.759 32.163  8.785   1.00 96.93  ? 35  ARG B NE  1 
ATOM   2293 C CZ  . ARG B 1 35  ? 27.795 32.446  7.909   1.00 97.16  ? 35  ARG B CZ  1 
ATOM   2294 N NH1 . ARG B 1 35  ? 27.877 33.516  7.133   1.00 101.31 ? 35  ARG B NH1 1 
ATOM   2295 N NH2 . ARG B 1 35  ? 26.743 31.651  7.811   1.00 93.75  ? 35  ARG B NH2 1 
ATOM   2296 N N   . ILE B 1 36  ? 33.545 29.508  7.529   1.00 54.91  ? 36  ILE B N   1 
ATOM   2297 C CA  . ILE B 1 36  ? 33.694 28.255  8.318   1.00 58.97  ? 36  ILE B CA  1 
ATOM   2298 C C   . ILE B 1 36  ? 32.772 28.345  9.544   1.00 60.59  ? 36  ILE B C   1 
ATOM   2299 O O   . ILE B 1 36  ? 32.753 29.396  10.181  1.00 57.92  ? 36  ILE B O   1 
ATOM   2300 C CB  . ILE B 1 36  ? 35.180 28.029  8.676   1.00 63.89  ? 36  ILE B CB  1 
ATOM   2301 C CG1 . ILE B 1 36  ? 35.987 27.609  7.441   1.00 63.05  ? 36  ILE B CG1 1 
ATOM   2302 C CG2 . ILE B 1 36  ? 35.343 27.029  9.817   1.00 60.87  ? 36  ILE B CG2 1 
ATOM   2303 C CD1 . ILE B 1 36  ? 37.226 28.441  7.185   1.00 71.08  ? 36  ILE B CD1 1 
ATOM   2304 N N   . GLU B 1 37  ? 31.997 27.291  9.811   1.00 62.15  ? 37  GLU B N   1 
ATOM   2305 C CA  . GLU B 1 37  ? 31.096 27.166  10.987  1.00 68.37  ? 37  GLU B CA  1 
ATOM   2306 C C   . GLU B 1 37  ? 31.836 26.399  12.095  1.00 75.91  ? 37  GLU B C   1 
ATOM   2307 O O   . GLU B 1 37  ? 32.354 27.070  13.008  1.00 84.48  ? 37  GLU B O   1 
ATOM   2308 C CB  . GLU B 1 37  ? 29.771 26.536  10.562  1.00 73.91  ? 37  GLU B CB  1 
ATOM   2309 C CG  . GLU B 1 37  ? 29.008 27.367  9.528   1.00 81.84  ? 37  GLU B CG  1 
ATOM   2310 C CD  . GLU B 1 37  ? 27.724 26.740  8.993   1.00 88.34  ? 37  GLU B CD  1 
ATOM   2311 O OE1 . GLU B 1 37  ? 27.157 25.854  9.685   1.00 100.91 ? 37  GLU B OE1 1 
ATOM   2312 O OE2 . GLU B 1 37  ? 27.286 27.135  7.885   1.00 79.39  ? 37  GLU B OE2 1 
ATOM   2313 N N   . LYS B 1 38  ? 31.938 25.067  12.018  1.00 70.99  ? 38  LYS B N   1 
ATOM   2314 C CA  . LYS B 1 38  ? 32.619 24.243  13.055  1.00 71.47  ? 38  LYS B CA  1 
ATOM   2315 C C   . LYS B 1 38  ? 33.437 23.117  12.413  1.00 69.52  ? 38  LYS B C   1 
ATOM   2316 O O   . LYS B 1 38  ? 33.031 22.586  11.367  1.00 62.99  ? 38  LYS B O   1 
ATOM   2317 C CB  . LYS B 1 38  ? 31.604 23.656  14.045  1.00 83.39  ? 38  LYS B CB  1 
ATOM   2318 C CG  . LYS B 1 38  ? 30.355 23.043  13.420  1.00 94.12  ? 38  LYS B CG  1 
ATOM   2319 C CD  . LYS B 1 38  ? 29.390 22.415  14.420  1.00 101.93 ? 38  LYS B CD  1 
ATOM   2320 C CE  . LYS B 1 38  ? 27.960 22.312  13.908  1.00 111.41 ? 38  LYS B CE  1 
ATOM   2321 N NZ  . LYS B 1 38  ? 27.445 23.589  13.345  1.00 112.56 ? 38  LYS B NZ  1 
ATOM   2322 N N   . LYS B 1 39  ? 34.557 22.768  13.043  1.00 68.89  ? 39  LYS B N   1 
ATOM   2323 C CA  . LYS B 1 39  ? 35.261 21.474  12.856  1.00 68.99  ? 39  LYS B CA  1 
ATOM   2324 C C   . LYS B 1 39  ? 34.243 20.340  13.024  1.00 69.03  ? 39  LYS B C   1 
ATOM   2325 O O   . LYS B 1 39  ? 33.440 20.402  13.973  1.00 72.36  ? 39  LYS B O   1 
ATOM   2326 C CB  . LYS B 1 39  ? 36.396 21.372  13.874  1.00 71.75  ? 39  LYS B CB  1 
ATOM   2327 C CG  . LYS B 1 39  ? 37.554 20.481  13.467  1.00 75.86  ? 39  LYS B CG  1 
ATOM   2328 C CD  . LYS B 1 39  ? 38.802 20.750  14.276  1.00 84.44  ? 39  LYS B CD  1 
ATOM   2329 C CE  . LYS B 1 39  ? 39.373 22.134  14.047  1.00 88.33  ? 39  LYS B CE  1 
ATOM   2330 N NZ  . LYS B 1 39  ? 40.832 22.087  13.782  1.00 91.54  ? 39  LYS B NZ  1 
ATOM   2331 N N   . ILE B 1 40  ? 34.222 19.380  12.101  1.00 65.73  ? 40  ILE B N   1 
ATOM   2332 C CA  . ILE B 1 40  ? 33.293 18.213  12.147  1.00 61.48  ? 40  ILE B CA  1 
ATOM   2333 C C   . ILE B 1 40  ? 34.067 16.915  11.927  1.00 62.94  ? 40  ILE B C   1 
ATOM   2334 O O   . ILE B 1 40  ? 33.387 15.875  11.763  1.00 63.71  ? 40  ILE B O   1 
ATOM   2335 C CB  . ILE B 1 40  ? 32.156 18.340  11.112  1.00 64.20  ? 40  ILE B CB  1 
ATOM   2336 C CG1 . ILE B 1 40  ? 32.687 18.466  9.681   1.00 62.92  ? 40  ILE B CG1 1 
ATOM   2337 C CG2 . ILE B 1 40  ? 31.228 19.479  11.494  1.00 70.44  ? 40  ILE B CG2 1 
ATOM   2338 C CD1 . ILE B 1 40  ? 31.616 18.639  8.617   1.00 59.65  ? 40  ILE B CD1 1 
ATOM   2339 N N   . GLY B 1 41  ? 35.405 16.950  11.934  1.00 55.00  ? 41  GLY B N   1 
ATOM   2340 C CA  . GLY B 1 41  ? 36.201 15.783  11.516  1.00 55.45  ? 41  GLY B CA  1 
ATOM   2341 C C   . GLY B 1 41  ? 37.685 16.043  11.594  1.00 51.49  ? 41  GLY B C   1 
ATOM   2342 O O   . GLY B 1 41  ? 38.100 17.157  11.290  1.00 54.99  ? 41  GLY B O   1 
ATOM   2343 N N   . ARG B 1 42  ? 38.456 15.039  11.993  1.00 49.76  ? 42  ARG B N   1 
ATOM   2344 C CA  . ARG B 1 42  ? 39.935 15.089  11.945  1.00 56.55  ? 42  ARG B CA  1 
ATOM   2345 C C   . ARG B 1 42  ? 40.391 13.750  11.360  1.00 53.14  ? 42  ARG B C   1 
ATOM   2346 O O   . ARG B 1 42  ? 39.785 12.747  11.679  1.00 53.16  ? 42  ARG B O   1 
ATOM   2347 C CB  . ARG B 1 42  ? 40.492 15.416  13.334  1.00 58.92  ? 42  ARG B CB  1 
ATOM   2348 C CG  . ARG B 1 42  ? 41.958 15.838  13.366  1.00 66.04  ? 42  ARG B CG  1 
ATOM   2349 C CD  . ARG B 1 42  ? 42.491 15.702  14.780  1.00 71.72  ? 42  ARG B CD  1 
ATOM   2350 N NE  . ARG B 1 42  ? 43.608 16.559  15.137  1.00 71.82  ? 42  ARG B NE  1 
ATOM   2351 C CZ  . ARG B 1 42  ? 43.515 17.844  15.422  1.00 70.77  ? 42  ARG B CZ  1 
ATOM   2352 N NH1 . ARG B 1 42  ? 42.355 18.469  15.360  1.00 78.68  ? 42  ARG B NH1 1 
ATOM   2353 N NH2 . ARG B 1 42  ? 44.592 18.518  15.758  1.00 84.04  ? 42  ARG B NH2 1 
ATOM   2354 N N   . GLY B 1 43  ? 41.360 13.775  10.457  1.00 54.49  ? 43  GLY B N   1 
ATOM   2355 C CA  . GLY B 1 43  ? 41.942 12.573  9.844   1.00 59.47  ? 43  GLY B CA  1 
ATOM   2356 C C   . GLY B 1 43  ? 43.448 12.595  9.976   1.00 57.69  ? 43  GLY B C   1 
ATOM   2357 O O   . GLY B 1 43  ? 43.969 13.508  10.616  1.00 47.49  ? 43  GLY B O   1 
ATOM   2358 N N   . GLN B 1 44  ? 44.129 11.618  9.390   1.00 61.28  ? 44  GLN B N   1 
ATOM   2359 C CA  . GLN B 1 44  ? 45.598 11.496  9.527   1.00 64.38  ? 44  GLN B CA  1 
ATOM   2360 C C   . GLN B 1 44  ? 46.223 12.784  9.002   1.00 63.12  ? 44  GLN B C   1 
ATOM   2361 O O   . GLN B 1 44  ? 47.212 13.260  9.597   1.00 58.64  ? 44  GLN B O   1 
ATOM   2362 C CB  . GLN B 1 44  ? 46.105 10.295  8.736   1.00 71.61  ? 44  GLN B CB  1 
ATOM   2363 C CG  . GLN B 1 44  ? 47.351 9.669   9.331   1.00 82.83  ? 44  GLN B CG  1 
ATOM   2364 C CD  . GLN B 1 44  ? 47.327 8.195   9.026   1.00 91.93  ? 44  GLN B CD  1 
ATOM   2365 O OE1 . GLN B 1 44  ? 47.457 7.788   7.871   1.00 83.70  ? 44  GLN B OE1 1 
ATOM   2366 N NE2 . GLN B 1 44  ? 47.086 7.395   10.056  1.00 96.41  ? 44  GLN B NE2 1 
ATOM   2367 N N   . PHE B 1 45  ? 45.650 13.322  7.922   1.00 53.30  ? 45  PHE B N   1 
ATOM   2368 C CA  . PHE B 1 45  ? 46.303 14.374  7.117   1.00 52.49  ? 45  PHE B CA  1 
ATOM   2369 C C   . PHE B 1 45  ? 45.447 15.629  7.041   1.00 47.58  ? 45  PHE B C   1 
ATOM   2370 O O   . PHE B 1 45  ? 45.890 16.609  6.398   1.00 48.17  ? 45  PHE B O   1 
ATOM   2371 C CB  . PHE B 1 45  ? 46.559 13.856  5.710   1.00 54.86  ? 45  PHE B CB  1 
ATOM   2372 C CG  . PHE B 1 45  ? 47.418 12.627  5.637   1.00 59.18  ? 45  PHE B CG  1 
ATOM   2373 C CD1 . PHE B 1 45  ? 48.680 12.618  6.214   1.00 59.17  ? 45  PHE B CD1 1 
ATOM   2374 C CD2 . PHE B 1 45  ? 46.979 11.496  4.960   1.00 61.31  ? 45  PHE B CD2 1 
ATOM   2375 C CE1 . PHE B 1 45  ? 49.480 11.488  6.130   1.00 64.91  ? 45  PHE B CE1 1 
ATOM   2376 C CE2 . PHE B 1 45  ? 47.787 10.370  4.868   1.00 62.05  ? 45  PHE B CE2 1 
ATOM   2377 C CZ  . PHE B 1 45  ? 49.035 10.371  5.450   1.00 64.11  ? 45  PHE B CZ  1 
ATOM   2378 N N   . SER B 1 46  ? 44.254 15.603  7.623   1.00 46.32  ? 46  SER B N   1 
ATOM   2379 C CA  . SER B 1 46  ? 43.210 16.600  7.277   1.00 51.44  ? 46  SER B CA  1 
ATOM   2380 C C   . SER B 1 46  ? 42.354 16.964  8.490   1.00 47.92  ? 46  SER B C   1 
ATOM   2381 O O   . SER B 1 46  ? 42.316 16.181  9.454   1.00 47.11  ? 46  SER B O   1 
ATOM   2382 C CB  . SER B 1 46  ? 42.363 16.101  6.124   1.00 49.99  ? 46  SER B CB  1 
ATOM   2383 O OG  . SER B 1 46  ? 41.652 14.919  6.478   1.00 47.73  ? 46  SER B OG  1 
ATOM   2384 N N   . GLU B 1 47  ? 41.721 18.134  8.413   1.00 50.83  ? 47  GLU B N   1 
ATOM   2385 C CA  . GLU B 1 47  ? 40.583 18.579  9.254   1.00 55.53  ? 47  GLU B CA  1 
ATOM   2386 C C   . GLU B 1 47  ? 39.433 18.876  8.294   1.00 52.39  ? 47  GLU B C   1 
ATOM   2387 O O   . GLU B 1 47  ? 39.711 19.318  7.173   1.00 52.53  ? 47  GLU B O   1 
ATOM   2388 C CB  . GLU B 1 47  ? 40.940 19.831  10.065  1.00 68.63  ? 47  GLU B CB  1 
ATOM   2389 C CG  . GLU B 1 47  ? 42.356 19.822  10.643  1.00 81.85  ? 47  GLU B CG  1 
ATOM   2390 C CD  . GLU B 1 47  ? 42.473 19.516  12.129  1.00 90.58  ? 47  GLU B CD  1 
ATOM   2391 O OE1 . GLU B 1 47  ? 41.434 19.504  12.825  1.00 83.19  ? 47  GLU B OE1 1 
ATOM   2392 O OE2 . GLU B 1 47  ? 43.616 19.287  12.586  1.00 117.60 ? 47  GLU B OE2 1 
ATOM   2393 N N   . VAL B 1 48  ? 38.202 18.607  8.704   1.00 47.31  ? 48  VAL B N   1 
ATOM   2394 C CA  . VAL B 1 48  ? 36.995 18.855  7.884   1.00 48.54  ? 48  VAL B CA  1 
ATOM   2395 C C   . VAL B 1 48  ? 36.104 19.804  8.671   1.00 48.34  ? 48  VAL B C   1 
ATOM   2396 O O   . VAL B 1 48  ? 35.975 19.579  9.888   1.00 46.85  ? 48  VAL B O   1 
ATOM   2397 C CB  . VAL B 1 48  ? 36.258 17.547  7.551   1.00 53.04  ? 48  VAL B CB  1 
ATOM   2398 C CG1 . VAL B 1 48  ? 35.286 17.763  6.411   1.00 54.20  ? 48  VAL B CG1 1 
ATOM   2399 C CG2 . VAL B 1 48  ? 37.220 16.410  7.227   1.00 57.66  ? 48  VAL B CG2 1 
ATOM   2400 N N   . TYR B 1 49  ? 35.524 20.797  7.988   1.00 46.11  ? 49  TYR B N   1 
ATOM   2401 C CA  . TYR B 1 49  ? 34.616 21.824  8.558   1.00 47.49  ? 49  TYR B CA  1 
ATOM   2402 C C   . TYR B 1 49  ? 33.302 21.833  7.789   1.00 45.01  ? 49  TYR B C   1 
ATOM   2403 O O   . TYR B 1 49  ? 33.256 21.418  6.608   1.00 46.80  ? 49  TYR B O   1 
ATOM   2404 C CB  . TYR B 1 49  ? 35.220 23.231  8.523   1.00 51.01  ? 49  TYR B CB  1 
ATOM   2405 C CG  . TYR B 1 49  ? 36.563 23.367  9.194   1.00 56.99  ? 49  TYR B CG  1 
ATOM   2406 C CD1 . TYR B 1 49  ? 37.724 22.976  8.545   1.00 57.54  ? 49  TYR B CD1 1 
ATOM   2407 C CD2 . TYR B 1 49  ? 36.676 23.902  10.470  1.00 56.89  ? 49  TYR B CD2 1 
ATOM   2408 C CE1 . TYR B 1 49  ? 38.966 23.112  9.140   1.00 59.22  ? 49  TYR B CE1 1 
ATOM   2409 C CE2 . TYR B 1 49  ? 37.911 24.040  11.083  1.00 62.01  ? 49  TYR B CE2 1 
ATOM   2410 C CZ  . TYR B 1 49  ? 39.058 23.634  10.419  1.00 64.77  ? 49  TYR B CZ  1 
ATOM   2411 O OH  . TYR B 1 49  ? 40.275 23.736  11.024  1.00 59.69  ? 49  TYR B OH  1 
ATOM   2412 N N   . ARG B 1 50  ? 32.264 22.276  8.488   1.00 46.93  ? 50  ARG B N   1 
ATOM   2413 C CA  . ARG B 1 50  ? 30.975 22.713  7.917   1.00 49.71  ? 50  ARG B CA  1 
ATOM   2414 C C   . ARG B 1 50  ? 31.181 24.204  7.637   1.00 46.04  ? 50  ARG B C   1 
ATOM   2415 O O   . ARG B 1 50  ? 31.800 24.879  8.441   1.00 43.05  ? 50  ARG B O   1 
ATOM   2416 C CB  . ARG B 1 50  ? 29.838 22.299  8.862   1.00 59.29  ? 50  ARG B CB  1 
ATOM   2417 C CG  . ARG B 1 50  ? 28.509 22.977  8.596   1.00 70.63  ? 50  ARG B CG  1 
ATOM   2418 C CD  . ARG B 1 50  ? 27.234 22.148  8.735   1.00 70.83  ? 50  ARG B CD  1 
ATOM   2419 N NE  . ARG B 1 50  ? 26.280 22.989  8.012   1.00 79.14  ? 50  ARG B NE  1 
ATOM   2420 C CZ  . ARG B 1 50  ? 25.062 22.670  7.589   1.00 77.72  ? 50  ARG B CZ  1 
ATOM   2421 N NH1 . ARG B 1 50  ? 24.352 23.592  6.968   1.00 84.23  ? 50  ARG B NH1 1 
ATOM   2422 N NH2 . ARG B 1 50  ? 24.542 21.473  7.790   1.00 84.63  ? 50  ARG B NH2 1 
ATOM   2423 N N   . ALA B 1 51  ? 30.869 24.638  6.428   1.00 44.55  ? 51  ALA B N   1 
ATOM   2424 C CA  . ALA B 1 51  ? 31.026 26.033  5.978   1.00 45.27  ? 51  ALA B CA  1 
ATOM   2425 C C   . ALA B 1 51  ? 29.811 26.369  5.127   1.00 43.08  ? 51  ALA B C   1 
ATOM   2426 O O   . ALA B 1 51  ? 29.109 25.440  4.694   1.00 50.02  ? 51  ALA B O   1 
ATOM   2427 C CB  . ALA B 1 51  ? 32.321 26.220  5.203   1.00 45.92  ? 51  ALA B CB  1 
ATOM   2428 N N   . ALA B 1 52  ? 29.591 27.649  4.878   1.00 44.63  ? 52  ALA B N   1 
ATOM   2429 C CA  . ALA B 1 52  ? 28.613 28.098  3.877   1.00 48.74  ? 52  ALA B CA  1 
ATOM   2430 C C   . ALA B 1 52  ? 29.376 28.916  2.854   1.00 46.42  ? 52  ALA B C   1 
ATOM   2431 O O   . ALA B 1 52  ? 30.217 29.716  3.264   1.00 49.39  ? 52  ALA B O   1 
ATOM   2432 C CB  . ALA B 1 52  ? 27.511 28.895  4.527   1.00 51.41  ? 52  ALA B CB  1 
ATOM   2433 N N   . CYS B 1 53  ? 29.075 28.732  1.576   1.00 48.02  ? 53  CYS B N   1 
ATOM   2434 C CA  . CYS B 1 53  ? 29.523 29.674  0.521   1.00 50.01  ? 53  CYS B CA  1 
ATOM   2435 C C   . CYS B 1 53  ? 28.825 31.032  0.697   1.00 47.09  ? 53  CYS B C   1 
ATOM   2436 O O   . CYS B 1 53  ? 27.592 31.048  0.874   1.00 48.85  ? 53  CYS B O   1 
ATOM   2437 C CB  . CYS B 1 53  ? 29.221 29.124  -0.858  1.00 49.67  ? 53  CYS B CB  1 
ATOM   2438 S SG  . CYS B 1 53  ? 29.917 30.194  -2.130  1.00 55.98  ? 53  CYS B SG  1 
ATOM   2439 N N   . LEU B 1 54  ? 29.579 32.130  0.650   1.00 48.71  ? 54  LEU B N   1 
ATOM   2440 C CA  . LEU B 1 54  ? 29.037 33.497  0.880   1.00 53.11  ? 54  LEU B CA  1 
ATOM   2441 C C   . LEU B 1 54  ? 28.413 34.018  -0.419  1.00 59.85  ? 54  LEU B C   1 
ATOM   2442 O O   . LEU B 1 54  ? 27.632 34.980  -0.345  1.00 68.04  ? 54  LEU B O   1 
ATOM   2443 C CB  . LEU B 1 54  ? 30.134 34.432  1.407   1.00 52.09  ? 54  LEU B CB  1 
ATOM   2444 C CG  . LEU B 1 54  ? 30.680 34.066  2.793   1.00 52.12  ? 54  LEU B CG  1 
ATOM   2445 C CD1 . LEU B 1 54  ? 31.866 34.918  3.188   1.00 54.01  ? 54  LEU B CD1 1 
ATOM   2446 C CD2 . LEU B 1 54  ? 29.597 34.175  3.850   1.00 55.35  ? 54  LEU B CD2 1 
ATOM   2447 N N   . LEU B 1 55  ? 28.718 33.399  -1.561  1.00 55.88  ? 55  LEU B N   1 
ATOM   2448 C CA  . LEU B 1 55  ? 28.222 33.864  -2.880  1.00 57.74  ? 55  LEU B CA  1 
ATOM   2449 C C   . LEU B 1 55  ? 26.773 33.411  -3.081  1.00 60.72  ? 55  LEU B C   1 
ATOM   2450 O O   . LEU B 1 55  ? 26.033 34.103  -3.794  1.00 64.68  ? 55  LEU B O   1 
ATOM   2451 C CB  . LEU B 1 55  ? 29.120 33.310  -3.989  1.00 56.61  ? 55  LEU B CB  1 
ATOM   2452 C CG  . LEU B 1 55  ? 30.599 33.699  -3.928  1.00 61.34  ? 55  LEU B CG  1 
ATOM   2453 C CD1 . LEU B 1 55  ? 31.255 33.510  -5.281  1.00 65.55  ? 55  LEU B CD1 1 
ATOM   2454 C CD2 . LEU B 1 55  ? 30.792 35.135  -3.465  1.00 67.00  ? 55  LEU B CD2 1 
ATOM   2455 N N   . ASP B 1 56  ? 26.392 32.268  -2.522  1.00 58.97  ? 56  ASP B N   1 
ATOM   2456 C CA  . ASP B 1 56  ? 25.119 31.605  -2.892  1.00 55.84  ? 56  ASP B CA  1 
ATOM   2457 C C   . ASP B 1 56  ? 24.451 30.957  -1.670  1.00 56.56  ? 56  ASP B C   1 
ATOM   2458 O O   . ASP B 1 56  ? 23.321 30.460  -1.847  1.00 54.05  ? 56  ASP B O   1 
ATOM   2459 C CB  . ASP B 1 56  ? 25.385 30.627  -4.042  1.00 60.36  ? 56  ASP B CB  1 
ATOM   2460 C CG  . ASP B 1 56  ? 26.340 29.495  -3.693  1.00 62.60  ? 56  ASP B CG  1 
ATOM   2461 O OD1 . ASP B 1 56  ? 26.641 29.332  -2.490  1.00 63.43  ? 56  ASP B OD1 1 
ATOM   2462 O OD2 . ASP B 1 56  ? 26.750 28.762  -4.620  1.00 55.29  ? 56  ASP B OD2 1 
ATOM   2463 N N   . GLY B 1 57  ? 25.107 30.933  -0.498  1.00 53.75  ? 57  GLY B N   1 
ATOM   2464 C CA  . GLY B 1 57  ? 24.519 30.468  0.780   1.00 53.47  ? 57  GLY B CA  1 
ATOM   2465 C C   . GLY B 1 57  ? 24.486 28.948  0.919   1.00 56.44  ? 57  GLY B C   1 
ATOM   2466 O O   . GLY B 1 57  ? 23.888 28.453  1.896   1.00 58.57  ? 57  GLY B O   1 
ATOM   2467 N N   . VAL B 1 58  ? 25.111 28.216  -0.006  1.00 53.93  ? 58  VAL B N   1 
ATOM   2468 C CA  . VAL B 1 58  ? 25.077 26.728  -0.043  1.00 54.06  ? 58  VAL B CA  1 
ATOM   2469 C C   . VAL B 1 58  ? 25.948 26.179  1.090   1.00 54.28  ? 58  VAL B C   1 
ATOM   2470 O O   . VAL B 1 58  ? 27.115 26.549  1.235   1.00 51.61  ? 58  VAL B O   1 
ATOM   2471 C CB  . VAL B 1 58  ? 25.516 26.213  -1.428  1.00 56.20  ? 58  VAL B CB  1 
ATOM   2472 C CG1 . VAL B 1 58  ? 25.654 24.696  -1.461  1.00 51.77  ? 58  VAL B CG1 1 
ATOM   2473 C CG2 . VAL B 1 58  ? 24.556 26.687  -2.521  1.00 57.26  ? 58  VAL B CG2 1 
ATOM   2474 N N   . PRO B 1 59  ? 25.408 25.290  1.951   1.00 51.35  ? 59  PRO B N   1 
ATOM   2475 C CA  . PRO B 1 59  ? 26.226 24.593  2.938   1.00 50.93  ? 59  PRO B CA  1 
ATOM   2476 C C   . PRO B 1 59  ? 27.171 23.609  2.241   1.00 47.19  ? 59  PRO B C   1 
ATOM   2477 O O   . PRO B 1 59  ? 26.726 22.931  1.357   1.00 48.83  ? 59  PRO B O   1 
ATOM   2478 C CB  . PRO B 1 59  ? 25.215 23.836  3.808   1.00 51.98  ? 59  PRO B CB  1 
ATOM   2479 C CG  . PRO B 1 59  ? 24.014 23.664  2.906   1.00 57.70  ? 59  PRO B CG  1 
ATOM   2480 C CD  . PRO B 1 59  ? 23.994 24.899  2.025   1.00 58.43  ? 59  PRO B CD  1 
ATOM   2481 N N   . VAL B 1 60  ? 28.437 23.566  2.653   1.00 46.48  ? 60  VAL B N   1 
ATOM   2482 C CA  . VAL B 1 60  ? 29.472 22.690  2.038   1.00 44.12  ? 60  VAL B CA  1 
ATOM   2483 C C   . VAL B 1 60  ? 30.351 22.149  3.148   1.00 47.10  ? 60  VAL B C   1 
ATOM   2484 O O   . VAL B 1 60  ? 30.382 22.779  4.230   1.00 46.51  ? 60  VAL B O   1 
ATOM   2485 C CB  . VAL B 1 60  ? 30.345 23.444  1.026   1.00 46.34  ? 60  VAL B CB  1 
ATOM   2486 C CG1 . VAL B 1 60  ? 29.527 24.032  -0.107  1.00 48.35  ? 60  VAL B CG1 1 
ATOM   2487 C CG2 . VAL B 1 60  ? 31.163 24.518  1.719   1.00 50.42  ? 60  VAL B CG2 1 
ATOM   2488 N N   . ALA B 1 61  ? 31.058 21.056  2.850   1.00 45.77  ? 61  ALA B N   1 
ATOM   2489 C CA  . ALA B 1 61  ? 32.166 20.510  3.663   1.00 44.34  ? 61  ALA B CA  1 
ATOM   2490 C C   . ALA B 1 61  ? 33.466 21.131  3.155   1.00 42.91  ? 61  ALA B C   1 
ATOM   2491 O O   . ALA B 1 61  ? 33.640 21.226  1.936   1.00 41.52  ? 61  ALA B O   1 
ATOM   2492 C CB  . ALA B 1 61  ? 32.199 19.004  3.583   1.00 47.80  ? 61  ALA B CB  1 
ATOM   2493 N N   . LEU B 1 62  ? 34.324 21.580  4.062   1.00 44.99  ? 62  LEU B N   1 
ATOM   2494 C CA  . LEU B 1 62  ? 35.632 22.161  3.694   1.00 42.76  ? 62  LEU B CA  1 
ATOM   2495 C C   . LEU B 1 62  ? 36.735 21.323  4.356   1.00 45.30  ? 62  LEU B C   1 
ATOM   2496 O O   . LEU B 1 62  ? 36.809 21.253  5.596   1.00 42.90  ? 62  LEU B O   1 
ATOM   2497 C CB  . LEU B 1 62  ? 35.632 23.633  4.081   1.00 46.50  ? 62  LEU B CB  1 
ATOM   2498 C CG  . LEU B 1 62  ? 36.979 24.338  3.991   1.00 53.00  ? 62  LEU B CG  1 
ATOM   2499 C CD1 . LEU B 1 62  ? 37.669 24.024  2.677   1.00 56.47  ? 62  LEU B CD1 1 
ATOM   2500 C CD2 . LEU B 1 62  ? 36.788 25.839  4.150   1.00 57.16  ? 62  LEU B CD2 1 
ATOM   2501 N N   . LYS B 1 63  ? 37.481 20.602  3.524   1.00 44.81  ? 63  LYS B N   1 
ATOM   2502 C CA  . LYS B 1 63  ? 38.544 19.660  3.934   1.00 49.02  ? 63  LYS B CA  1 
ATOM   2503 C C   . LYS B 1 63  ? 39.863 20.396  3.702   1.00 46.77  ? 63  LYS B C   1 
ATOM   2504 O O   . LYS B 1 63  ? 40.100 20.794  2.551   1.00 45.37  ? 63  LYS B O   1 
ATOM   2505 C CB  . LYS B 1 63  ? 38.388 18.353  3.149   1.00 44.86  ? 63  LYS B CB  1 
ATOM   2506 C CG  . LYS B 1 63  ? 39.247 17.196  3.625   1.00 48.79  ? 63  LYS B CG  1 
ATOM   2507 C CD  . LYS B 1 63  ? 38.848 15.863  3.028   1.00 52.93  ? 63  LYS B CD  1 
ATOM   2508 C CE  . LYS B 1 63  ? 39.400 14.671  3.770   1.00 56.71  ? 63  LYS B CE  1 
ATOM   2509 N NZ  . LYS B 1 63  ? 39.922 13.643  2.843   1.00 61.20  ? 63  LYS B NZ  1 
ATOM   2510 N N   . LYS B 1 64  ? 40.601 20.678  4.778   1.00 45.49  ? 64  LYS B N   1 
ATOM   2511 C CA  . LYS B 1 64  ? 41.962 21.281  4.737   1.00 47.57  ? 64  LYS B CA  1 
ATOM   2512 C C   . LYS B 1 64  ? 42.969 20.143  4.900   1.00 46.42  ? 64  LYS B C   1 
ATOM   2513 O O   . LYS B 1 64  ? 42.910 19.461  5.939   1.00 46.45  ? 64  LYS B O   1 
ATOM   2514 C CB  . LYS B 1 64  ? 42.131 22.340  5.829   1.00 49.84  ? 64  LYS B CB  1 
ATOM   2515 C CG  . LYS B 1 64  ? 41.139 23.497  5.775   1.00 51.56  ? 64  LYS B CG  1 
ATOM   2516 C CD  . LYS B 1 64  ? 41.411 24.559  6.817   1.00 58.61  ? 64  LYS B CD  1 
ATOM   2517 C CE  . LYS B 1 64  ? 40.420 25.704  6.824   1.00 60.80  ? 64  LYS B CE  1 
ATOM   2518 N NZ  . LYS B 1 64  ? 40.851 26.782  5.905   1.00 67.75  ? 64  LYS B NZ  1 
ATOM   2519 N N   . VAL B 1 65  ? 43.777 19.882  3.872   1.00 45.08  ? 65  VAL B N   1 
ATOM   2520 C CA  . VAL B 1 65  ? 44.739 18.740  3.852   1.00 46.15  ? 65  VAL B CA  1 
ATOM   2521 C C   . VAL B 1 65  ? 46.141 19.333  3.987   1.00 48.36  ? 65  VAL B C   1 
ATOM   2522 O O   . VAL B 1 65  ? 46.482 20.229  3.199   1.00 54.95  ? 65  VAL B O   1 
ATOM   2523 C CB  . VAL B 1 65  ? 44.601 17.858  2.596   1.00 42.90  ? 65  VAL B CB  1 
ATOM   2524 C CG1 . VAL B 1 65  ? 45.545 16.665  2.609   1.00 40.91  ? 65  VAL B CG1 1 
ATOM   2525 C CG2 . VAL B 1 65  ? 43.181 17.369  2.398   1.00 44.19  ? 65  VAL B CG2 1 
ATOM   2526 N N   . GLN B 1 66  ? 46.907 18.872  4.975   1.00 50.75  ? 66  GLN B N   1 
ATOM   2527 C CA  . GLN B 1 66  ? 48.278 19.379  5.224   1.00 51.27  ? 66  GLN B CA  1 
ATOM   2528 C C   . GLN B 1 66  ? 49.220 18.634  4.286   1.00 47.18  ? 66  GLN B C   1 
ATOM   2529 O O   . GLN B 1 66  ? 49.893 17.710  4.729   1.00 49.57  ? 66  GLN B O   1 
ATOM   2530 C CB  . GLN B 1 66  ? 48.647 19.234  6.698   1.00 57.15  ? 66  GLN B CB  1 
ATOM   2531 C CG  . GLN B 1 66  ? 48.513 20.529  7.482   1.00 66.58  ? 66  GLN B CG  1 
ATOM   2532 C CD  . GLN B 1 66  ? 47.163 20.672  8.133   1.00 75.05  ? 66  GLN B CD  1 
ATOM   2533 O OE1 . GLN B 1 66  ? 46.211 21.163  7.529   1.00 77.07  ? 66  GLN B OE1 1 
ATOM   2534 N NE2 . GLN B 1 66  ? 47.084 20.278  9.397   1.00 77.42  ? 66  GLN B NE2 1 
ATOM   2535 N N   . ILE B 1 67  ? 49.238 19.021  3.015   1.00 48.71  ? 67  ILE B N   1 
ATOM   2536 C CA  . ILE B 1 67  ? 50.055 18.335  1.976   1.00 48.10  ? 67  ILE B CA  1 
ATOM   2537 C C   . ILE B 1 67  ? 51.534 18.676  2.180   1.00 48.16  ? 67  ILE B C   1 
ATOM   2538 O O   . ILE B 1 67  ? 52.362 17.944  1.643   1.00 47.49  ? 67  ILE B O   1 
ATOM   2539 C CB  . ILE B 1 67  ? 49.554 18.654  0.548   1.00 47.16  ? 67  ILE B CB  1 
ATOM   2540 C CG1 . ILE B 1 67  ? 49.458 20.150  0.250   1.00 46.08  ? 67  ILE B CG1 1 
ATOM   2541 C CG2 . ILE B 1 67  ? 48.227 17.949  0.300   1.00 46.26  ? 67  ILE B CG2 1 
ATOM   2542 C CD1 . ILE B 1 67  ? 49.209 20.445  -1.211  1.00 45.76  ? 67  ILE B CD1 1 
ATOM   2543 N N   . PHE B 1 68  ? 51.846 19.745  2.918   1.00 48.73  ? 68  PHE B N   1 
ATOM   2544 C CA  . PHE B 1 68  ? 53.232 20.209  3.194   1.00 50.02  ? 68  PHE B CA  1 
ATOM   2545 C C   . PHE B 1 68  ? 53.688 19.685  4.560   1.00 49.58  ? 68  PHE B C   1 
ATOM   2546 O O   . PHE B 1 68  ? 54.694 18.961  4.630   1.00 53.84  ? 68  PHE B O   1 
ATOM   2547 C CB  . PHE B 1 68  ? 53.293 21.737  3.093   1.00 48.61  ? 68  PHE B CB  1 
ATOM   2548 C CG  . PHE B 1 68  ? 52.841 22.240  1.747   1.00 47.26  ? 68  PHE B CG  1 
ATOM   2549 C CD1 . PHE B 1 68  ? 53.442 21.771  0.592   1.00 44.34  ? 68  PHE B CD1 1 
ATOM   2550 C CD2 . PHE B 1 68  ? 51.787 23.132  1.633   1.00 48.50  ? 68  PHE B CD2 1 
ATOM   2551 C CE1 . PHE B 1 68  ? 53.023 22.206  -0.651  1.00 47.57  ? 68  PHE B CE1 1 
ATOM   2552 C CE2 . PHE B 1 68  ? 51.359 23.564  0.389   1.00 47.53  ? 68  PHE B CE2 1 
ATOM   2553 C CZ  . PHE B 1 68  ? 51.983 23.104  -0.748  1.00 51.57  ? 68  PHE B CZ  1 
ATOM   2554 N N   . ASP B 1 69  ? 52.926 20.006  5.601   1.00 52.61  ? 69  ASP B N   1 
ATOM   2555 C CA  . ASP B 1 69  ? 53.305 19.792  7.021   1.00 57.12  ? 69  ASP B CA  1 
ATOM   2556 C C   . ASP B 1 69  ? 53.152 18.310  7.414   1.00 58.66  ? 69  ASP B C   1 
ATOM   2557 O O   . ASP B 1 69  ? 53.782 17.950  8.414   1.00 65.67  ? 69  ASP B O   1 
ATOM   2558 C CB  . ASP B 1 69  ? 52.497 20.723  7.934   1.00 55.98  ? 69  ASP B CB  1 
ATOM   2559 C CG  . ASP B 1 69  ? 52.600 22.206  7.588   1.00 66.00  ? 69  ASP B CG  1 
ATOM   2560 O OD1 . ASP B 1 69  ? 53.546 22.594  6.870   1.00 69.29  ? 69  ASP B OD1 1 
ATOM   2561 O OD2 . ASP B 1 69  ? 51.742 22.975  8.053   1.00 74.33  ? 69  ASP B OD2 1 
ATOM   2562 N N   . LEU B 1 70  ? 52.366 17.474  6.702   1.00 56.86  ? 70  LEU B N   1 
ATOM   2563 C CA  . LEU B 1 70  ? 52.044 16.081  7.159   1.00 53.80  ? 70  LEU B CA  1 
ATOM   2564 C C   . LEU B 1 70  ? 52.262 15.007  6.086   1.00 52.99  ? 70  LEU B C   1 
ATOM   2565 O O   . LEU B 1 70  ? 51.947 13.828  6.372   1.00 55.22  ? 70  LEU B O   1 
ATOM   2566 C CB  . LEU B 1 70  ? 50.595 16.019  7.657   1.00 54.48  ? 70  LEU B CB  1 
ATOM   2567 C CG  . LEU B 1 70  ? 50.323 16.738  8.974   1.00 60.20  ? 70  LEU B CG  1 
ATOM   2568 C CD1 . LEU B 1 70  ? 48.841 16.661  9.359   1.00 56.61  ? 70  LEU B CD1 1 
ATOM   2569 C CD2 . LEU B 1 70  ? 51.196 16.171  10.085  1.00 57.81  ? 70  LEU B CD2 1 
ATOM   2570 N N   . MET B 1 71  ? 52.796 15.337  4.913   1.00 55.70  ? 71  MET B N   1 
ATOM   2571 C CA  . MET B 1 71  ? 53.029 14.323  3.848   1.00 57.32  ? 71  MET B CA  1 
ATOM   2572 C C   . MET B 1 71  ? 54.443 14.486  3.309   1.00 52.21  ? 71  MET B C   1 
ATOM   2573 O O   . MET B 1 71  ? 54.914 15.613  3.325   1.00 49.95  ? 71  MET B O   1 
ATOM   2574 C CB  . MET B 1 71  ? 52.052 14.517  2.688   1.00 57.04  ? 71  MET B CB  1 
ATOM   2575 C CG  . MET B 1 71  ? 50.610 14.329  3.078   1.00 58.82  ? 71  MET B CG  1 
ATOM   2576 S SD  . MET B 1 71  ? 49.541 14.439  1.626   1.00 59.63  ? 71  MET B SD  1 
ATOM   2577 C CE  . MET B 1 71  ? 48.005 13.828  2.318   1.00 60.23  ? 71  MET B CE  1 
ATOM   2578 N N   . ASP B 1 72  ? 55.052 13.414  2.805   1.00 54.93  ? 72  ASP B N   1 
ATOM   2579 C CA  . ASP B 1 72  ? 56.306 13.528  2.018   1.00 62.89  ? 72  ASP B CA  1 
ATOM   2580 C C   . ASP B 1 72  ? 55.926 14.014  0.617   1.00 62.00  ? 72  ASP B C   1 
ATOM   2581 O O   . ASP B 1 72  ? 54.774 14.390  0.433   1.00 62.67  ? 72  ASP B O   1 
ATOM   2582 C CB  . ASP B 1 72  ? 57.123 12.233  2.029   1.00 67.82  ? 72  ASP B CB  1 
ATOM   2583 C CG  . ASP B 1 72  ? 56.577 11.129  1.150   1.00 76.20  ? 72  ASP B CG  1 
ATOM   2584 O OD1 . ASP B 1 72  ? 55.435 10.701  1.412   1.00 74.90  ? 72  ASP B OD1 1 
ATOM   2585 O OD2 . ASP B 1 72  ? 57.312 10.703  0.216   1.00 88.44  ? 72  ASP B OD2 1 
ATOM   2586 N N   . ALA B 1 73  ? 56.878 14.040  -0.314  1.00 66.41  ? 73  ALA B N   1 
ATOM   2587 C CA  . ALA B 1 73  ? 56.694 14.566  -1.681  1.00 64.95  ? 73  ALA B CA  1 
ATOM   2588 C C   . ALA B 1 73  ? 55.776 13.616  -2.458  1.00 68.37  ? 73  ALA B C   1 
ATOM   2589 O O   . ALA B 1 73  ? 54.889 14.134  -3.179  1.00 64.78  ? 73  ALA B O   1 
ATOM   2590 C CB  . ALA B 1 73  ? 58.026 14.740  -2.362  1.00 67.44  ? 73  ALA B CB  1 
ATOM   2591 N N   . LYS B 1 74  ? 55.967 12.297  -2.283  1.00 66.68  ? 74  LYS B N   1 
ATOM   2592 C CA  . LYS B 1 74  ? 55.227 11.205  -2.986  1.00 65.19  ? 74  LYS B CA  1 
ATOM   2593 C C   . LYS B 1 74  ? 53.748 11.287  -2.592  1.00 54.66  ? 74  LYS B C   1 
ATOM   2594 O O   . LYS B 1 74  ? 52.916 11.487  -3.481  1.00 51.63  ? 74  LYS B O   1 
ATOM   2595 C CB  . LYS B 1 74  ? 55.843 9.832   -2.682  1.00 69.70  ? 74  LYS B CB  1 
ATOM   2596 C CG  . LYS B 1 74  ? 55.211 8.619   -3.366  1.00 72.06  ? 74  LYS B CG  1 
ATOM   2597 C CD  . LYS B 1 74  ? 55.262 8.631   -4.881  1.00 80.61  ? 74  LYS B CD  1 
ATOM   2598 C CE  . LYS B 1 74  ? 54.949 7.288   -5.520  1.00 84.48  ? 74  LYS B CE  1 
ATOM   2599 N NZ  . LYS B 1 74  ? 53.566 6.823   -5.243  1.00 84.64  ? 74  LYS B NZ  1 
ATOM   2600 N N   . ALA B 1 75  ? 53.445 11.210  -1.302  1.00 52.38  ? 75  ALA B N   1 
ATOM   2601 C CA  . ALA B 1 75  ? 52.080 11.391  -0.759  1.00 54.44  ? 75  ALA B CA  1 
ATOM   2602 C C   . ALA B 1 75  ? 51.415 12.650  -1.333  1.00 54.56  ? 75  ALA B C   1 
ATOM   2603 O O   . ALA B 1 75  ? 50.213 12.577  -1.628  1.00 56.70  ? 75  ALA B O   1 
ATOM   2604 C CB  . ALA B 1 75  ? 52.138 11.478  0.745   1.00 58.82  ? 75  ALA B CB  1 
ATOM   2605 N N   . ARG B 1 76  ? 52.137 13.777  -1.414  1.00 47.95  ? 76  ARG B N   1 
ATOM   2606 C CA  . ARG B 1 76  ? 51.540 15.101  -1.753  1.00 49.79  ? 76  ARG B CA  1 
ATOM   2607 C C   . ARG B 1 76  ? 51.083 15.046  -3.211  1.00 45.98  ? 76  ARG B C   1 
ATOM   2608 O O   . ARG B 1 76  ? 49.913 15.359  -3.491  1.00 50.82  ? 76  ARG B O   1 
ATOM   2609 C CB  . ARG B 1 76  ? 52.531 16.236  -1.475  1.00 48.31  ? 76  ARG B CB  1 
ATOM   2610 C CG  . ARG B 1 76  ? 52.239 17.574  -2.146  1.00 50.42  ? 76  ARG B CG  1 
ATOM   2611 C CD  . ARG B 1 76  ? 53.514 18.426  -2.182  1.00 55.88  ? 76  ARG B CD  1 
ATOM   2612 N NE  . ARG B 1 76  ? 54.031 18.360  -0.836  1.00 62.01  ? 76  ARG B NE  1 
ATOM   2613 C CZ  . ARG B 1 76  ? 55.269 18.144  -0.451  1.00 52.31  ? 76  ARG B CZ  1 
ATOM   2614 N NH1 . ARG B 1 76  ? 56.271 18.074  -1.303  1.00 55.13  ? 76  ARG B NH1 1 
ATOM   2615 N NH2 . ARG B 1 76  ? 55.492 18.039  0.845   1.00 62.16  ? 76  ARG B NH2 1 
ATOM   2616 N N   . ALA B 1 77  ? 51.984 14.634  -4.089  1.00 41.91  ? 77  ALA B N   1 
ATOM   2617 C CA  . ALA B 1 77  ? 51.756 14.517  -5.540  1.00 45.75  ? 77  ALA B CA  1 
ATOM   2618 C C   . ALA B 1 77  ? 50.607 13.537  -5.813  1.00 47.93  ? 77  ALA B C   1 
ATOM   2619 O O   . ALA B 1 77  ? 49.717 13.873  -6.601  1.00 53.21  ? 77  ALA B O   1 
ATOM   2620 C CB  . ALA B 1 77  ? 53.033 14.091  -6.214  1.00 40.31  ? 77  ALA B CB  1 
ATOM   2621 N N   . ASP B 1 78  ? 50.622 12.373  -5.183  1.00 50.36  ? 78  ASP B N   1 
ATOM   2622 C CA  . ASP B 1 78  ? 49.596 11.320  -5.401  1.00 56.49  ? 78  ASP B CA  1 
ATOM   2623 C C   . ASP B 1 78  ? 48.243 11.881  -4.943  1.00 56.50  ? 78  ASP B C   1 
ATOM   2624 O O   . ASP B 1 78  ? 47.245 11.693  -5.667  1.00 54.84  ? 78  ASP B O   1 
ATOM   2625 C CB  . ASP B 1 78  ? 49.968 10.014  -4.688  1.00 60.98  ? 78  ASP B CB  1 
ATOM   2626 C CG  . ASP B 1 78  ? 51.144 9.249   -5.292  1.00 65.24  ? 78  ASP B CG  1 
ATOM   2627 O OD1 . ASP B 1 78  ? 51.789 9.744   -6.260  1.00 67.01  ? 78  ASP B OD1 1 
ATOM   2628 O OD2 . ASP B 1 78  ? 51.418 8.152   -4.779  1.00 77.55  ? 78  ASP B OD2 1 
ATOM   2629 N N   . CYS B 1 79  ? 48.219 12.588  -3.812  1.00 51.25  ? 79  CYS B N   1 
ATOM   2630 C CA  . CYS B 1 79  ? 46.992 13.196  -3.244  1.00 48.64  ? 79  CYS B CA  1 
ATOM   2631 C C   . CYS B 1 79  ? 46.467 14.278  -4.195  1.00 52.70  ? 79  CYS B C   1 
ATOM   2632 O O   . CYS B 1 79  ? 45.240 14.333  -4.418  1.00 51.80  ? 79  CYS B O   1 
ATOM   2633 C CB  . CYS B 1 79  ? 47.254 13.776  -1.866  1.00 51.15  ? 79  CYS B CB  1 
ATOM   2634 S SG  . CYS B 1 79  ? 45.940 14.878  -1.279  1.00 52.09  ? 79  CYS B SG  1 
ATOM   2635 N N   . ILE B 1 80  ? 47.347 15.105  -4.756  1.00 51.86  ? 80  ILE B N   1 
ATOM   2636 C CA  . ILE B 1 80  ? 46.918 16.172  -5.702  1.00 56.03  ? 80  ILE B CA  1 
ATOM   2637 C C   . ILE B 1 80  ? 46.341 15.497  -6.955  1.00 56.34  ? 80  ILE B C   1 
ATOM   2638 O O   . ILE B 1 80  ? 45.251 15.928  -7.366  1.00 57.09  ? 80  ILE B O   1 
ATOM   2639 C CB  . ILE B 1 80  ? 48.059 17.158  -6.015  1.00 55.62  ? 80  ILE B CB  1 
ATOM   2640 C CG1 . ILE B 1 80  ? 48.300 18.112  -4.846  1.00 52.88  ? 80  ILE B CG1 1 
ATOM   2641 C CG2 . ILE B 1 80  ? 47.779 17.920  -7.302  1.00 54.75  ? 80  ILE B CG2 1 
ATOM   2642 C CD1 . ILE B 1 80  ? 49.554 18.942  -4.992  1.00 52.50  ? 80  ILE B CD1 1 
ATOM   2643 N N   . LYS B 1 81  ? 47.016 14.482  -7.514  1.00 51.46  ? 81  LYS B N   1 
ATOM   2644 C CA  . LYS B 1 81  ? 46.543 13.758  -8.727  1.00 63.28  ? 81  LYS B CA  1 
ATOM   2645 C C   . LYS B 1 81  ? 45.135 13.215  -8.459  1.00 58.88  ? 81  LYS B C   1 
ATOM   2646 O O   . LYS B 1 81  ? 44.286 13.344  -9.347  1.00 57.81  ? 81  LYS B O   1 
ATOM   2647 C CB  . LYS B 1 81  ? 47.421 12.566  -9.131  1.00 67.86  ? 81  LYS B CB  1 
ATOM   2648 C CG  . LYS B 1 81  ? 48.875 12.857  -9.474  1.00 82.58  ? 81  LYS B CG  1 
ATOM   2649 C CD  . LYS B 1 81  ? 49.150 14.212  -10.110 1.00 98.41  ? 81  LYS B CD  1 
ATOM   2650 C CE  . LYS B 1 81  ? 50.609 14.616  -10.019 1.00 106.22 ? 81  LYS B CE  1 
ATOM   2651 N NZ  . LYS B 1 81  ? 51.513 13.485  -10.352 1.00 110.49 ? 81  LYS B NZ  1 
ATOM   2652 N N   . GLU B 1 82  ? 44.926 12.624  -7.281  1.00 49.55  ? 82  GLU B N   1 
ATOM   2653 C CA  . GLU B 1 82  ? 43.675 11.944  -6.881  1.00 52.76  ? 82  GLU B CA  1 
ATOM   2654 C C   . GLU B 1 82  ? 42.561 13.000  -6.819  1.00 50.49  ? 82  GLU B C   1 
ATOM   2655 O O   . GLU B 1 82  ? 41.487 12.742  -7.388  1.00 45.97  ? 82  GLU B O   1 
ATOM   2656 C CB  . GLU B 1 82  ? 43.901 11.194  -5.563  1.00 63.66  ? 82  GLU B CB  1 
ATOM   2657 C CG  . GLU B 1 82  ? 42.728 10.346  -5.086  1.00 76.88  ? 82  GLU B CG  1 
ATOM   2658 C CD  . GLU B 1 82  ? 42.797 8.868   -5.443  1.00 96.95  ? 82  GLU B CD  1 
ATOM   2659 O OE1 . GLU B 1 82  ? 42.004 8.066   -4.857  1.00 99.82  ? 82  GLU B OE1 1 
ATOM   2660 O OE2 . GLU B 1 82  ? 43.640 8.515   -6.309  1.00 99.63  ? 82  GLU B OE2 1 
ATOM   2661 N N   . ILE B 1 83  ? 42.803 14.158  -6.191  1.00 44.83  ? 83  ILE B N   1 
ATOM   2662 C CA  . ILE B 1 83  ? 41.750 15.192  -5.993  1.00 45.78  ? 83  ILE B CA  1 
ATOM   2663 C C   . ILE B 1 83  ? 41.392 15.789  -7.362  1.00 44.42  ? 83  ILE B C   1 
ATOM   2664 O O   . ILE B 1 83  ? 40.209 16.080  -7.570  1.00 43.87  ? 83  ILE B O   1 
ATOM   2665 C CB  . ILE B 1 83  ? 42.146 16.278  -4.968  1.00 48.60  ? 83  ILE B CB  1 
ATOM   2666 C CG1 . ILE B 1 83  ? 42.463 15.725  -3.571  1.00 54.56  ? 83  ILE B CG1 1 
ATOM   2667 C CG2 . ILE B 1 83  ? 41.066 17.347  -4.898  1.00 47.18  ? 83  ILE B CG2 1 
ATOM   2668 C CD1 . ILE B 1 83  ? 41.582 14.583  -3.093  1.00 54.95  ? 83  ILE B CD1 1 
ATOM   2669 N N   . ASP B 1 84  ? 42.369 15.958  -8.251  1.00 44.82  ? 84  ASP B N   1 
ATOM   2670 C CA  . ASP B 1 84  ? 42.167 16.455  -9.639  1.00 48.09  ? 84  ASP B CA  1 
ATOM   2671 C C   . ASP B 1 84  ? 41.162 15.570  -10.380 1.00 48.76  ? 84  ASP B C   1 
ATOM   2672 O O   . ASP B 1 84  ? 40.245 16.136  -11.005 1.00 52.06  ? 84  ASP B O   1 
ATOM   2673 C CB  . ASP B 1 84  ? 43.489 16.524  -10.398 1.00 51.27  ? 84  ASP B CB  1 
ATOM   2674 C CG  . ASP B 1 84  ? 44.323 17.748  -10.049 1.00 58.45  ? 84  ASP B CG  1 
ATOM   2675 O OD1 . ASP B 1 84  ? 43.774 18.675  -9.384  1.00 52.74  ? 84  ASP B OD1 1 
ATOM   2676 O OD2 . ASP B 1 84  ? 45.513 17.779  -10.462 1.00 65.13  ? 84  ASP B OD2 1 
ATOM   2677 N N   . LEU B 1 85  ? 41.311 14.244  -10.278 1.00 47.08  ? 85  LEU B N   1 
ATOM   2678 C CA  . LEU B 1 85  ? 40.408 13.245  -10.906 1.00 48.08  ? 85  LEU B CA  1 
ATOM   2679 C C   . LEU B 1 85  ? 39.021 13.307  -10.262 1.00 47.41  ? 85  LEU B C   1 
ATOM   2680 O O   . LEU B 1 85  ? 38.034 13.201  -10.983 1.00 48.33  ? 85  LEU B O   1 
ATOM   2681 C CB  . LEU B 1 85  ? 40.998 11.843  -10.741 1.00 52.48  ? 85  LEU B CB  1 
ATOM   2682 C CG  . LEU B 1 85  ? 42.275 11.536  -11.527 1.00 55.31  ? 85  LEU B CG  1 
ATOM   2683 C CD1 . LEU B 1 85  ? 42.665 10.082  -11.323 1.00 57.37  ? 85  LEU B CD1 1 
ATOM   2684 C CD2 . LEU B 1 85  ? 42.111 11.838  -13.013 1.00 56.91  ? 85  LEU B CD2 1 
ATOM   2685 N N   . LEU B 1 86  ? 38.946 13.449  -8.942  1.00 46.68  ? 86  LEU B N   1 
ATOM   2686 C CA  . LEU B 1 86  ? 37.666 13.339  -8.214  1.00 45.00  ? 86  LEU B CA  1 
ATOM   2687 C C   . LEU B 1 86  ? 36.815 14.530  -8.607  1.00 45.29  ? 86  LEU B C   1 
ATOM   2688 O O   . LEU B 1 86  ? 35.595 14.361  -8.757  1.00 47.22  ? 86  LEU B O   1 
ATOM   2689 C CB  . LEU B 1 86  ? 37.898 13.316  -6.703  1.00 45.98  ? 86  LEU B CB  1 
ATOM   2690 C CG  . LEU B 1 86  ? 38.378 11.988  -6.125  1.00 47.80  ? 86  LEU B CG  1 
ATOM   2691 C CD1 . LEU B 1 86  ? 38.851 12.184  -4.682  1.00 47.02  ? 86  LEU B CD1 1 
ATOM   2692 C CD2 . LEU B 1 86  ? 37.277 10.929  -6.192  1.00 44.84  ? 86  LEU B CD2 1 
ATOM   2693 N N   . LYS B 1 87  ? 37.425 15.698  -8.750  1.00 47.29  ? 87  LYS B N   1 
ATOM   2694 C CA  . LYS B 1 87  ? 36.632 16.920  -9.032  1.00 57.71  ? 87  LYS B CA  1 
ATOM   2695 C C   . LYS B 1 87  ? 36.282 16.993  -10.537 1.00 55.51  ? 87  LYS B C   1 
ATOM   2696 O O   . LYS B 1 87  ? 35.565 17.942  -10.898 1.00 54.83  ? 87  LYS B O   1 
ATOM   2697 C CB  . LYS B 1 87  ? 37.289 18.136  -8.370  1.00 56.84  ? 87  LYS B CB  1 
ATOM   2698 C CG  . LYS B 1 87  ? 38.433 18.828  -9.093  1.00 58.19  ? 87  LYS B CG  1 
ATOM   2699 C CD  . LYS B 1 87  ? 38.782 20.126  -8.387  1.00 57.16  ? 87  LYS B CD  1 
ATOM   2700 C CE  . LYS B 1 87  ? 39.729 21.016  -9.153  1.00 61.63  ? 87  LYS B CE  1 
ATOM   2701 N NZ  . LYS B 1 87  ? 41.039 20.349  -9.333  1.00 70.83  ? 87  LYS B NZ  1 
ATOM   2702 N N   . GLN B 1 88  ? 36.645 15.973  -11.332 1.00 54.47  ? 88  GLN B N   1 
ATOM   2703 C CA  . GLN B 1 88  ? 36.224 15.772  -12.752 1.00 60.92  ? 88  GLN B CA  1 
ATOM   2704 C C   . GLN B 1 88  ? 34.982 14.865  -12.833 1.00 63.26  ? 88  GLN B C   1 
ATOM   2705 O O   . GLN B 1 88  ? 34.348 14.824  -13.890 1.00 75.29  ? 88  GLN B O   1 
ATOM   2706 C CB  . GLN B 1 88  ? 37.324 15.103  -13.583 1.00 61.30  ? 88  GLN B CB  1 
ATOM   2707 C CG  . GLN B 1 88  ? 38.491 16.016  -13.933 1.00 74.54  ? 88  GLN B CG  1 
ATOM   2708 C CD  . GLN B 1 88  ? 39.638 15.284  -14.603 1.00 87.64  ? 88  GLN B CD  1 
ATOM   2709 O OE1 . GLN B 1 88  ? 39.506 14.145  -15.068 1.00 85.20  ? 88  GLN B OE1 1 
ATOM   2710 N NE2 . GLN B 1 88  ? 40.790 15.944  -14.664 1.00 86.17  ? 88  GLN B NE2 1 
ATOM   2711 N N   . LEU B 1 89  ? 34.652 14.120  -11.784 1.00 56.58  ? 89  LEU B N   1 
ATOM   2712 C CA  . LEU B 1 89  ? 33.471 13.226  -11.793 1.00 53.34  ? 89  LEU B CA  1 
ATOM   2713 C C   . LEU B 1 89  ? 32.205 14.075  -11.833 1.00 56.69  ? 89  LEU B C   1 
ATOM   2714 O O   . LEU B 1 89  ? 32.123 15.071  -11.114 1.00 67.59  ? 89  LEU B O   1 
ATOM   2715 C CB  . LEU B 1 89  ? 33.452 12.355  -10.543 1.00 49.14  ? 89  LEU B CB  1 
ATOM   2716 C CG  . LEU B 1 89  ? 34.680 11.489  -10.366 1.00 48.47  ? 89  LEU B CG  1 
ATOM   2717 C CD1 . LEU B 1 89  ? 34.497 10.589  -9.164  1.00 49.24  ? 89  LEU B CD1 1 
ATOM   2718 C CD2 . LEU B 1 89  ? 34.942 10.692  -11.636 1.00 50.97  ? 89  LEU B CD2 1 
ATOM   2719 N N   . ASN B 1 90  ? 31.230 13.593  -12.587 1.00 53.69  ? 90  ASN B N   1 
ATOM   2720 C CA  . ASN B 1 90  ? 30.019 14.332  -12.986 1.00 56.91  ? 90  ASN B CA  1 
ATOM   2721 C C   . ASN B 1 90  ? 28.871 13.334  -13.146 1.00 55.28  ? 90  ASN B C   1 
ATOM   2722 O O   . ASN B 1 90  ? 28.564 12.939  -14.316 1.00 62.76  ? 90  ASN B O   1 
ATOM   2723 C CB  . ASN B 1 90  ? 30.266 15.064  -14.303 1.00 56.10  ? 90  ASN B CB  1 
ATOM   2724 C CG  . ASN B 1 90  ? 29.157 16.048  -14.486 1.00 56.53  ? 90  ASN B CG  1 
ATOM   2725 O OD1 . ASN B 1 90  ? 28.633 16.521  -13.479 1.00 65.68  ? 90  ASN B OD1 1 
ATOM   2726 N ND2 . ASN B 1 90  ? 28.766 16.289  -15.722 1.00 57.17  ? 90  ASN B ND2 1 
ATOM   2727 N N   . HIS B 1 91  ? 28.323 12.875  -12.028 1.00 45.44  ? 91  HIS B N   1 
ATOM   2728 C CA  . HIS B 1 91  ? 27.409 11.713  -12.002 1.00 46.22  ? 91  HIS B CA  1 
ATOM   2729 C C   . HIS B 1 91  ? 26.316 11.973  -10.984 1.00 48.74  ? 91  HIS B C   1 
ATOM   2730 O O   . HIS B 1 91  ? 26.606 12.401  -9.868  1.00 44.10  ? 91  HIS B O   1 
ATOM   2731 C CB  . HIS B 1 91  ? 28.193 10.434  -11.710 1.00 48.97  ? 91  HIS B CB  1 
ATOM   2732 C CG  . HIS B 1 91  ? 27.440 9.187   -12.032 1.00 47.38  ? 91  HIS B CG  1 
ATOM   2733 N ND1 . HIS B 1 91  ? 26.499 8.650   -11.170 1.00 45.03  ? 91  HIS B ND1 1 
ATOM   2734 C CD2 . HIS B 1 91  ? 27.481 8.375   -13.113 1.00 46.71  ? 91  HIS B CD2 1 
ATOM   2735 C CE1 . HIS B 1 91  ? 25.987 7.560   -11.715 1.00 46.55  ? 91  HIS B CE1 1 
ATOM   2736 N NE2 . HIS B 1 91  ? 26.570 7.371   -12.908 1.00 47.48  ? 91  HIS B NE2 1 
ATOM   2737 N N   . PRO B 1 92  ? 25.044 11.677  -11.337 1.00 52.02  ? 92  PRO B N   1 
ATOM   2738 C CA  . PRO B 1 92  ? 23.916 11.893  -10.432 1.00 49.70  ? 92  PRO B CA  1 
ATOM   2739 C C   . PRO B 1 92  ? 24.163 11.280  -9.042  1.00 48.74  ? 92  PRO B C   1 
ATOM   2740 O O   . PRO B 1 92  ? 23.708 11.855  -8.068  1.00 42.58  ? 92  PRO B O   1 
ATOM   2741 C CB  . PRO B 1 92  ? 22.721 11.195  -11.113 1.00 49.03  ? 92  PRO B CB  1 
ATOM   2742 C CG  . PRO B 1 92  ? 23.115 10.978  -12.560 1.00 51.65  ? 92  PRO B CG  1 
ATOM   2743 C CD  . PRO B 1 92  ? 24.633 11.069  -12.618 1.00 53.79  ? 92  PRO B CD  1 
ATOM   2744 N N   . ASN B 1 93  ? 24.885 10.150  -8.976  1.00 48.72  ? 93  ASN B N   1 
ATOM   2745 C CA  . ASN B 1 93  ? 24.978 9.316   -7.744  1.00 48.36  ? 93  ASN B CA  1 
ATOM   2746 C C   . ASN B 1 93  ? 26.335 9.460   -7.037  1.00 45.73  ? 93  ASN B C   1 
ATOM   2747 O O   . ASN B 1 93  ? 26.615 8.632   -6.149  1.00 46.51  ? 93  ASN B O   1 
ATOM   2748 C CB  . ASN B 1 93  ? 24.703 7.848   -8.067  1.00 50.21  ? 93  ASN B CB  1 
ATOM   2749 C CG  . ASN B 1 93  ? 23.401 7.640   -8.807  1.00 44.47  ? 93  ASN B CG  1 
ATOM   2750 O OD1 . ASN B 1 93  ? 23.401 7.258   -9.971  1.00 43.63  ? 93  ASN B OD1 1 
ATOM   2751 N ND2 . ASN B 1 93  ? 22.297 7.917   -8.146  1.00 41.93  ? 93  ASN B ND2 1 
ATOM   2752 N N   . VAL B 1 94  ? 27.136 10.474  -7.364  1.00 43.58  ? 94  VAL B N   1 
ATOM   2753 C CA  . VAL B 1 94  ? 28.414 10.747  -6.639  1.00 47.61  ? 94  VAL B CA  1 
ATOM   2754 C C   . VAL B 1 94  ? 28.305 12.104  -5.944  1.00 47.73  ? 94  VAL B C   1 
ATOM   2755 O O   . VAL B 1 94  ? 27.859 13.060  -6.601  1.00 50.86  ? 94  VAL B O   1 
ATOM   2756 C CB  . VAL B 1 94  ? 29.616 10.720  -7.595  1.00 51.18  ? 94  VAL B CB  1 
ATOM   2757 C CG1 . VAL B 1 94  ? 30.884 11.004  -6.837  1.00 55.60  ? 94  VAL B CG1 1 
ATOM   2758 C CG2 . VAL B 1 94  ? 29.727 9.401   -8.349  1.00 54.78  ? 94  VAL B CG2 1 
ATOM   2759 N N   . ILE B 1 95  ? 28.730 12.179  -4.683  1.00 41.89  ? 95  ILE B N   1 
ATOM   2760 C CA  . ILE B 1 95  ? 28.891 13.455  -3.925  1.00 42.84  ? 95  ILE B CA  1 
ATOM   2761 C C   . ILE B 1 95  ? 29.926 14.293  -4.684  1.00 41.48  ? 95  ILE B C   1 
ATOM   2762 O O   . ILE B 1 95  ? 30.999 13.749  -4.981  1.00 40.73  ? 95  ILE B O   1 
ATOM   2763 C CB  . ILE B 1 95  ? 29.285 13.188  -2.448  1.00 46.95  ? 95  ILE B CB  1 
ATOM   2764 C CG1 . ILE B 1 95  ? 28.168 12.450  -1.705  1.00 54.54  ? 95  ILE B CG1 1 
ATOM   2765 C CG2 . ILE B 1 95  ? 29.686 14.450  -1.696  1.00 43.38  ? 95  ILE B CG2 1 
ATOM   2766 C CD1 . ILE B 1 95  ? 26.891 13.252  -1.558  1.00 59.15  ? 95  ILE B CD1 1 
ATOM   2767 N N   . LYS B 1 96  ? 29.606 15.560  -4.968  1.00 42.96  ? 96  LYS B N   1 
ATOM   2768 C CA  . LYS B 1 96  ? 30.444 16.475  -5.796  1.00 48.58  ? 96  LYS B CA  1 
ATOM   2769 C C   . LYS B 1 96  ? 31.668 16.918  -5.003  1.00 42.48  ? 96  LYS B C   1 
ATOM   2770 O O   . LYS B 1 96  ? 31.521 17.196  -3.806  1.00 46.57  ? 96  LYS B O   1 
ATOM   2771 C CB  . LYS B 1 96  ? 29.664 17.706  -6.280  1.00 50.38  ? 96  LYS B CB  1 
ATOM   2772 C CG  . LYS B 1 96  ? 28.371 17.397  -7.015  1.00 54.36  ? 96  LYS B CG  1 
ATOM   2773 C CD  . LYS B 1 96  ? 28.565 16.435  -8.159  1.00 63.74  ? 96  LYS B CD  1 
ATOM   2774 C CE  . LYS B 1 96  ? 27.327 16.210  -9.002  1.00 66.17  ? 96  LYS B CE  1 
ATOM   2775 N NZ  . LYS B 1 96  ? 27.708 15.784  -10.364 1.00 72.25  ? 96  LYS B NZ  1 
ATOM   2776 N N   . TYR B 1 97  ? 32.830 16.925  -5.656  1.00 40.12  ? 97  TYR B N   1 
ATOM   2777 C CA  . TYR B 1 97  ? 34.002 17.755  -5.295  1.00 40.26  ? 97  TYR B CA  1 
ATOM   2778 C C   . TYR B 1 97  ? 33.910 19.055  -6.093  1.00 41.01  ? 97  TYR B C   1 
ATOM   2779 O O   . TYR B 1 97  ? 34.059 19.034  -7.330  1.00 46.60  ? 97  TYR B O   1 
ATOM   2780 C CB  . TYR B 1 97  ? 35.292 17.006  -5.582  1.00 39.99  ? 97  TYR B CB  1 
ATOM   2781 C CG  . TYR B 1 97  ? 35.617 15.954  -4.560  1.00 48.45  ? 97  TYR B CG  1 
ATOM   2782 C CD1 . TYR B 1 97  ? 34.869 14.789  -4.423  1.00 48.20  ? 97  TYR B CD1 1 
ATOM   2783 C CD2 . TYR B 1 97  ? 36.715 16.124  -3.732  1.00 55.62  ? 97  TYR B CD2 1 
ATOM   2784 C CE1 . TYR B 1 97  ? 35.199 13.839  -3.468  1.00 50.35  ? 97  TYR B CE1 1 
ATOM   2785 C CE2 . TYR B 1 97  ? 37.069 15.174  -2.792  1.00 58.56  ? 97  TYR B CE2 1 
ATOM   2786 C CZ  . TYR B 1 97  ? 36.304 14.033  -2.651  1.00 59.76  ? 97  TYR B CZ  1 
ATOM   2787 O OH  . TYR B 1 97  ? 36.709 13.144  -1.694  1.00 66.41  ? 97  TYR B OH  1 
ATOM   2788 N N   . TYR B 1 98  ? 33.600 20.146  -5.404  1.00 39.61  ? 98  TYR B N   1 
ATOM   2789 C CA  . TYR B 1 98  ? 33.293 21.464  -6.017  1.00 43.71  ? 98  TYR B CA  1 
ATOM   2790 C C   . TYR B 1 98  ? 34.606 22.209  -6.289  1.00 42.97  ? 98  TYR B C   1 
ATOM   2791 O O   . TYR B 1 98  ? 34.684 22.909  -7.291  1.00 50.06  ? 98  TYR B O   1 
ATOM   2792 C CB  . TYR B 1 98  ? 32.311 22.264  -5.150  1.00 43.35  ? 98  TYR B CB  1 
ATOM   2793 C CG  . TYR B 1 98  ? 30.884 21.778  -5.222  1.00 46.96  ? 98  TYR B CG  1 
ATOM   2794 C CD1 . TYR B 1 98  ? 30.290 21.517  -6.449  1.00 47.26  ? 98  TYR B CD1 1 
ATOM   2795 C CD2 . TYR B 1 98  ? 30.098 21.620  -4.083  1.00 50.48  ? 98  TYR B CD2 1 
ATOM   2796 C CE1 . TYR B 1 98  ? 28.970 21.101  -6.549  1.00 51.92  ? 98  TYR B CE1 1 
ATOM   2797 C CE2 . TYR B 1 98  ? 28.770 21.200  -4.165  1.00 52.10  ? 98  TYR B CE2 1 
ATOM   2798 C CZ  . TYR B 1 98  ? 28.208 20.927  -5.406  1.00 55.29  ? 98  TYR B CZ  1 
ATOM   2799 O OH  . TYR B 1 98  ? 26.926 20.473  -5.558  1.00 54.88  ? 98  TYR B OH  1 
ATOM   2800 N N   . ALA B 1 99  ? 35.642 22.020  -5.473  1.00 41.28  ? 99  ALA B N   1 
ATOM   2801 C CA  . ALA B 1 99  ? 36.890 22.790  -5.641  1.00 37.08  ? 99  ALA B CA  1 
ATOM   2802 C C   . ALA B 1 99  ? 38.032 22.162  -4.862  1.00 38.05  ? 99  ALA B C   1 
ATOM   2803 O O   . ALA B 1 99  ? 37.799 21.417  -3.900  1.00 40.13  ? 99  ALA B O   1 
ATOM   2804 C CB  . ALA B 1 99  ? 36.671 24.215  -5.226  1.00 40.52  ? 99  ALA B CB  1 
ATOM   2805 N N   . SER B 1 100 ? 39.238 22.428  -5.330  1.00 38.33  ? 100 SER B N   1 
ATOM   2806 C CA  . SER B 1 100 ? 40.482 22.178  -4.589  1.00 43.33  ? 100 SER B CA  1 
ATOM   2807 C C   . SER B 1 100 ? 41.477 23.256  -5.006  1.00 45.81  ? 100 SER B C   1 
ATOM   2808 O O   . SER B 1 100 ? 41.619 23.512  -6.198  1.00 54.46  ? 100 SER B O   1 
ATOM   2809 C CB  . SER B 1 100 ? 40.981 20.802  -4.839  1.00 42.77  ? 100 SER B CB  1 
ATOM   2810 O OG  . SER B 1 100 ? 41.471 20.731  -6.152  1.00 53.96  ? 100 SER B OG  1 
ATOM   2811 N N   . PHE B 1 101 ? 42.110 23.900  -4.041  1.00 50.20  ? 101 PHE B N   1 
ATOM   2812 C CA  . PHE B 1 101 ? 43.101 24.972  -4.293  1.00 48.79  ? 101 PHE B CA  1 
ATOM   2813 C C   . PHE B 1 101 ? 44.040 25.051  -3.095  1.00 44.71  ? 101 PHE B C   1 
ATOM   2814 O O   . PHE B 1 101 ? 43.669 24.574  -2.009  1.00 43.43  ? 101 PHE B O   1 
ATOM   2815 C CB  . PHE B 1 101 ? 42.372 26.286  -4.570  1.00 47.53  ? 101 PHE B CB  1 
ATOM   2816 C CG  . PHE B 1 101 ? 41.436 26.706  -3.472  1.00 43.47  ? 101 PHE B CG  1 
ATOM   2817 C CD1 . PHE B 1 101 ? 40.143 26.219  -3.417  1.00 40.33  ? 101 PHE B CD1 1 
ATOM   2818 C CD2 . PHE B 1 101 ? 41.852 27.602  -2.496  1.00 45.49  ? 101 PHE B CD2 1 
ATOM   2819 C CE1 . PHE B 1 101 ? 39.280 26.627  -2.410  1.00 44.68  ? 101 PHE B CE1 1 
ATOM   2820 C CE2 . PHE B 1 101 ? 40.991 27.999  -1.484  1.00 43.67  ? 101 PHE B CE2 1 
ATOM   2821 C CZ  . PHE B 1 101 ? 39.703 27.512  -1.440  1.00 42.74  ? 101 PHE B CZ  1 
ATOM   2822 N N   . ILE B 1 102 ? 45.226 25.618  -3.302  1.00 48.62  ? 102 ILE B N   1 
ATOM   2823 C CA  . ILE B 1 102 ? 46.231 25.841  -2.226  1.00 47.49  ? 102 ILE B CA  1 
ATOM   2824 C C   . ILE B 1 102 ? 46.097 27.276  -1.703  1.00 47.94  ? 102 ILE B C   1 
ATOM   2825 O O   . ILE B 1 102 ? 46.196 28.193  -2.513  1.00 51.31  ? 102 ILE B O   1 
ATOM   2826 C CB  . ILE B 1 102 ? 47.633 25.513  -2.757  1.00 47.32  ? 102 ILE B CB  1 
ATOM   2827 C CG1 . ILE B 1 102 ? 47.721 24.031  -3.132  1.00 45.71  ? 102 ILE B CG1 1 
ATOM   2828 C CG2 . ILE B 1 102 ? 48.676 25.893  -1.719  1.00 49.96  ? 102 ILE B CG2 1 
ATOM   2829 C CD1 . ILE B 1 102 ? 48.900 23.652  -3.963  1.00 47.69  ? 102 ILE B CD1 1 
ATOM   2830 N N   . GLU B 1 103 ? 45.879 27.445  -0.396  1.00 51.57  ? 103 GLU B N   1 
ATOM   2831 C CA  . GLU B 1 103 ? 45.850 28.764  0.293   1.00 47.10  ? 103 GLU B CA  1 
ATOM   2832 C C   . GLU B 1 103 ? 46.138 28.536  1.786   1.00 49.49  ? 103 GLU B C   1 
ATOM   2833 O O   . GLU B 1 103 ? 45.822 27.451  2.295   1.00 43.99  ? 103 GLU B O   1 
ATOM   2834 C CB  . GLU B 1 103 ? 44.512 29.444  -0.009  1.00 51.62  ? 103 GLU B CB  1 
ATOM   2835 C CG  . GLU B 1 103 ? 44.299 30.765  0.709   1.00 56.82  ? 103 GLU B CG  1 
ATOM   2836 C CD  . GLU B 1 103 ? 43.080 31.577  0.283   1.00 62.71  ? 103 GLU B CD  1 
ATOM   2837 O OE1 . GLU B 1 103 ? 42.544 31.303  -0.824  1.00 61.22  ? 103 GLU B OE1 1 
ATOM   2838 O OE2 . GLU B 1 103 ? 42.682 32.506  1.055   1.00 53.80  ? 103 GLU B OE2 1 
ATOM   2839 N N   . ASP B 1 104 ? 46.761 29.500  2.467   1.00 49.83  ? 104 ASP B N   1 
ATOM   2840 C CA  . ASP B 1 104 ? 47.219 29.355  3.876   1.00 53.30  ? 104 ASP B CA  1 
ATOM   2841 C C   . ASP B 1 104 ? 47.987 28.035  4.045   1.00 46.32  ? 104 ASP B C   1 
ATOM   2842 O O   . ASP B 1 104 ? 47.828 27.366  5.085   1.00 50.01  ? 104 ASP B O   1 
ATOM   2843 C CB  . ASP B 1 104 ? 46.056 29.422  4.873   1.00 59.34  ? 104 ASP B CB  1 
ATOM   2844 C CG  . ASP B 1 104 ? 45.191 30.666  4.778   1.00 65.53  ? 104 ASP B CG  1 
ATOM   2845 O OD1 . ASP B 1 104 ? 45.671 31.686  4.227   1.00 70.09  ? 104 ASP B OD1 1 
ATOM   2846 O OD2 . ASP B 1 104 ? 44.037 30.603  5.264   1.00 72.00  ? 104 ASP B OD2 1 
ATOM   2847 N N   . ASN B 1 105 ? 48.743 27.622  3.037   1.00 46.71  ? 105 ASN B N   1 
ATOM   2848 C CA  . ASN B 1 105 ? 49.690 26.480  3.149   1.00 53.27  ? 105 ASN B CA  1 
ATOM   2849 C C   . ASN B 1 105 ? 48.996 25.111  3.282   1.00 51.90  ? 105 ASN B C   1 
ATOM   2850 O O   . ASN B 1 105 ? 49.642 24.154  3.770   1.00 48.03  ? 105 ASN B O   1 
ATOM   2851 C CB  . ASN B 1 105 ? 50.632 26.721  4.328   1.00 56.97  ? 105 ASN B CB  1 
ATOM   2852 C CG  . ASN B 1 105 ? 52.044 26.404  3.913   1.00 61.96  ? 105 ASN B CG  1 
ATOM   2853 O OD1 . ASN B 1 105 ? 52.494 26.978  2.923   1.00 65.40  ? 105 ASN B OD1 1 
ATOM   2854 N ND2 . ASN B 1 105 ? 52.697 25.471  4.604   1.00 61.28  ? 105 ASN B ND2 1 
ATOM   2855 N N   . GLU B 1 106 ? 47.744 24.989  2.851   1.00 51.24  ? 106 GLU B N   1 
ATOM   2856 C CA  . GLU B 1 106 ? 46.994 23.711  2.887   1.00 54.05  ? 106 GLU B CA  1 
ATOM   2857 C C   . GLU B 1 106 ? 46.346 23.486  1.516   1.00 49.75  ? 106 GLU B C   1 
ATOM   2858 O O   . GLU B 1 106 ? 46.152 24.474  0.775   1.00 49.06  ? 106 GLU B O   1 
ATOM   2859 C CB  . GLU B 1 106 ? 45.970 23.755  4.024   1.00 58.76  ? 106 GLU B CB  1 
ATOM   2860 C CG  . GLU B 1 106 ? 46.604 23.868  5.398   1.00 65.05  ? 106 GLU B CG  1 
ATOM   2861 C CD  . GLU B 1 106 ? 45.709 24.385  6.516   1.00 75.08  ? 106 GLU B CD  1 
ATOM   2862 O OE1 . GLU B 1 106 ? 45.913 23.958  7.676   1.00 83.03  ? 106 GLU B OE1 1 
ATOM   2863 O OE2 . GLU B 1 106 ? 44.839 25.239  6.242   1.00 81.06  ? 106 GLU B OE2 1 
ATOM   2864 N N   . LEU B 1 107 ? 46.035 22.233  1.184   1.00 43.29  ? 107 LEU B N   1 
ATOM   2865 C CA  . LEU B 1 107 ? 45.108 21.909  0.080   1.00 42.42  ? 107 LEU B CA  1 
ATOM   2866 C C   . LEU B 1 107 ? 43.681 22.035  0.623   1.00 40.17  ? 107 LEU B C   1 
ATOM   2867 O O   . LEU B 1 107 ? 43.323 21.280  1.531   1.00 45.34  ? 107 LEU B O   1 
ATOM   2868 C CB  . LEU B 1 107 ? 45.376 20.506  -0.474  1.00 44.42  ? 107 LEU B CB  1 
ATOM   2869 C CG  . LEU B 1 107 ? 44.492 20.140  -1.665  1.00 45.01  ? 107 LEU B CG  1 
ATOM   2870 C CD1 . LEU B 1 107 ? 44.754 21.084  -2.820  1.00 43.73  ? 107 LEU B CD1 1 
ATOM   2871 C CD2 . LEU B 1 107 ? 44.692 18.702  -2.107  1.00 52.89  ? 107 LEU B CD2 1 
ATOM   2872 N N   . ASN B 1 108 ? 42.914 22.991  0.114   1.00 37.62  ? 108 ASN B N   1 
ATOM   2873 C CA  . ASN B 1 108 ? 41.495 23.210  0.503   1.00 40.48  ? 108 ASN B CA  1 
ATOM   2874 C C   . ASN B 1 108 ? 40.583 22.489  -0.489  1.00 39.82  ? 108 ASN B C   1 
ATOM   2875 O O   . ASN B 1 108 ? 40.691 22.740  -1.685  1.00 41.50  ? 108 ASN B O   1 
ATOM   2876 C CB  . ASN B 1 108 ? 41.172 24.697  0.563   1.00 41.45  ? 108 ASN B CB  1 
ATOM   2877 C CG  . ASN B 1 108 ? 42.033 25.392  1.592   1.00 44.61  ? 108 ASN B CG  1 
ATOM   2878 O OD1 . ASN B 1 108 ? 41.684 25.412  2.763   1.00 48.91  ? 108 ASN B OD1 1 
ATOM   2879 N ND2 . ASN B 1 108 ? 43.150 25.951  1.160   1.00 44.01  ? 108 ASN B ND2 1 
ATOM   2880 N N   . ILE B 1 109 ? 39.715 21.615  -0.007  1.00 40.58  ? 109 ILE B N   1 
ATOM   2881 C CA  . ILE B 1 109 ? 38.777 20.858  -0.877  1.00 39.17  ? 109 ILE B CA  1 
ATOM   2882 C C   . ILE B 1 109 ? 37.372 21.231  -0.446  1.00 35.27  ? 109 ILE B C   1 
ATOM   2883 O O   . ILE B 1 109 ? 37.091 21.099  0.731   1.00 41.95  ? 109 ILE B O   1 
ATOM   2884 C CB  . ILE B 1 109 ? 39.041 19.351  -0.767  1.00 39.69  ? 109 ILE B CB  1 
ATOM   2885 C CG1 . ILE B 1 109 ? 40.526 19.054  -0.932  1.00 40.80  ? 109 ILE B CG1 1 
ATOM   2886 C CG2 . ILE B 1 109 ? 38.203 18.572  -1.760  1.00 42.45  ? 109 ILE B CG2 1 
ATOM   2887 C CD1 . ILE B 1 109 ? 40.872 17.593  -0.721  1.00 46.01  ? 109 ILE B CD1 1 
ATOM   2888 N N   . VAL B 1 110 ? 36.551 21.716  -1.364  1.00 33.75  ? 110 VAL B N   1 
ATOM   2889 C CA  . VAL B 1 110 ? 35.121 22.025  -1.096  1.00 38.32  ? 110 VAL B CA  1 
ATOM   2890 C C   . VAL B 1 110 ? 34.272 20.877  -1.658  1.00 40.72  ? 110 VAL B C   1 
ATOM   2891 O O   . VAL B 1 110 ? 34.411 20.589  -2.871  1.00 45.29  ? 110 VAL B O   1 
ATOM   2892 C CB  . VAL B 1 110 ? 34.705 23.378  -1.698  1.00 37.14  ? 110 VAL B CB  1 
ATOM   2893 C CG1 . VAL B 1 110 ? 33.279 23.743  -1.290  1.00 40.16  ? 110 VAL B CG1 1 
ATOM   2894 C CG2 . VAL B 1 110 ? 35.676 24.480  -1.318  1.00 36.03  ? 110 VAL B CG2 1 
ATOM   2895 N N   . LEU B 1 111 ? 33.424 20.277  -0.813  1.00 42.09  ? 111 LEU B N   1 
ATOM   2896 C CA  . LEU B 1 111 ? 32.568 19.099  -1.119  1.00 45.54  ? 111 LEU B CA  1 
ATOM   2897 C C   . LEU B 1 111 ? 31.110 19.401  -0.799  1.00 43.85  ? 111 LEU B C   1 
ATOM   2898 O O   . LEU B 1 111 ? 30.846 20.091  0.204   1.00 44.11  ? 111 LEU B O   1 
ATOM   2899 C CB  . LEU B 1 111 ? 32.977 17.906  -0.254  1.00 49.30  ? 111 LEU B CB  1 
ATOM   2900 C CG  . LEU B 1 111 ? 34.412 17.433  -0.394  1.00 50.85  ? 111 LEU B CG  1 
ATOM   2901 C CD1 . LEU B 1 111 ? 35.289 18.049  0.682   1.00 53.44  ? 111 LEU B CD1 1 
ATOM   2902 C CD2 . LEU B 1 111 ? 34.454 15.925  -0.308  1.00 56.21  ? 111 LEU B CD2 1 
ATOM   2903 N N   . GLU B 1 112 ? 30.223 18.780  -1.569  1.00 43.22  ? 112 GLU B N   1 
ATOM   2904 C CA  . GLU B 1 112 ? 28.763 18.710  -1.330  1.00 48.53  ? 112 GLU B CA  1 
ATOM   2905 C C   . GLU B 1 112 ? 28.497 18.012  0.009   1.00 45.63  ? 112 GLU B C   1 
ATOM   2906 O O   . GLU B 1 112 ? 29.156 17.006  0.258   1.00 46.72  ? 112 GLU B O   1 
ATOM   2907 C CB  . GLU B 1 112 ? 28.111 17.954  -2.489  1.00 47.33  ? 112 GLU B CB  1 
ATOM   2908 C CG  . GLU B 1 112 ? 26.695 17.509  -2.195  1.00 51.36  ? 112 GLU B CG  1 
ATOM   2909 C CD  . GLU B 1 112 ? 25.953 16.942  -3.397  1.00 52.78  ? 112 GLU B CD  1 
ATOM   2910 O OE1 . GLU B 1 112 ? 24.711 17.106  -3.445  1.00 58.63  ? 112 GLU B OE1 1 
ATOM   2911 O OE2 . GLU B 1 112 ? 26.612 16.360  -4.285  1.00 48.42  ? 112 GLU B OE2 1 
ATOM   2912 N N   . LEU B 1 113 ? 27.605 18.584  0.823   1.00 52.63  ? 113 LEU B N   1 
ATOM   2913 C CA  . LEU B 1 113 ? 26.799 17.918  1.890   1.00 54.36  ? 113 LEU B CA  1 
ATOM   2914 C C   . LEU B 1 113 ? 25.372 17.740  1.367   1.00 55.37  ? 113 LEU B C   1 
ATOM   2915 O O   . LEU B 1 113 ? 24.714 18.767  1.101   1.00 56.70  ? 113 LEU B O   1 
ATOM   2916 C CB  . LEU B 1 113 ? 26.757 18.812  3.130   1.00 54.67  ? 113 LEU B CB  1 
ATOM   2917 C CG  . LEU B 1 113 ? 28.093 19.086  3.802   1.00 55.23  ? 113 LEU B CG  1 
ATOM   2918 C CD1 . LEU B 1 113 ? 27.955 20.231  4.799   1.00 54.30  ? 113 LEU B CD1 1 
ATOM   2919 C CD2 . LEU B 1 113 ? 28.611 17.819  4.479   1.00 52.83  ? 113 LEU B CD2 1 
ATOM   2920 N N   . ALA B 1 114 ? 24.915 16.499  1.201   1.00 63.59  ? 114 ALA B N   1 
ATOM   2921 C CA  . ALA B 1 114 ? 23.599 16.169  0.601   1.00 67.28  ? 114 ALA B CA  1 
ATOM   2922 C C   . ALA B 1 114 ? 22.502 16.158  1.680   1.00 64.46  ? 114 ALA B C   1 
ATOM   2923 O O   . ALA B 1 114 ? 22.742 15.610  2.789   1.00 65.07  ? 114 ALA B O   1 
ATOM   2924 C CB  . ALA B 1 114 ? 23.670 14.842  -0.116  1.00 72.32  ? 114 ALA B CB  1 
ATOM   2925 N N   . ASP B 1 115 ? 21.346 16.748  1.352   1.00 64.94  ? 115 ASP B N   1 
ATOM   2926 C CA  . ASP B 1 115 ? 20.074 16.629  2.116   1.00 71.58  ? 115 ASP B CA  1 
ATOM   2927 C C   . ASP B 1 115 ? 19.536 15.208  1.891   1.00 70.05  ? 115 ASP B C   1 
ATOM   2928 O O   . ASP B 1 115 ? 18.693 15.004  0.984   1.00 70.10  ? 115 ASP B O   1 
ATOM   2929 C CB  . ASP B 1 115 ? 19.070 17.732  1.740   1.00 74.95  ? 115 ASP B CB  1 
ATOM   2930 C CG  . ASP B 1 115 ? 17.709 17.636  2.430   1.00 72.61  ? 115 ASP B CG  1 
ATOM   2931 O OD1 . ASP B 1 115 ? 17.621 16.958  3.469   1.00 64.37  ? 115 ASP B OD1 1 
ATOM   2932 O OD2 . ASP B 1 115 ? 16.733 18.232  1.910   1.00 70.84  ? 115 ASP B OD2 1 
ATOM   2933 N N   . ALA B 1 116 ? 20.016 14.267  2.706   1.00 68.03  ? 116 ALA B N   1 
ATOM   2934 C CA  . ALA B 1 116 ? 19.793 12.814  2.547   1.00 68.71  ? 116 ALA B CA  1 
ATOM   2935 C C   . ALA B 1 116 ? 20.274 12.103  3.815   1.00 61.55  ? 116 ALA B C   1 
ATOM   2936 O O   . ALA B 1 116 ? 21.263 12.571  4.420   1.00 70.52  ? 116 ALA B O   1 
ATOM   2937 C CB  . ALA B 1 116 ? 20.521 12.329  1.308   1.00 67.29  ? 116 ALA B CB  1 
ATOM   2938 N N   . GLY B 1 117 ? 19.579 11.032  4.190   1.00 57.43  ? 117 GLY B N   1 
ATOM   2939 C CA  . GLY B 1 117 ? 19.983 10.090  5.250   1.00 61.39  ? 117 GLY B CA  1 
ATOM   2940 C C   . GLY B 1 117 ? 20.937 9.023   4.729   1.00 62.25  ? 117 GLY B C   1 
ATOM   2941 O O   . GLY B 1 117 ? 20.826 8.630   3.561   1.00 54.65  ? 117 GLY B O   1 
ATOM   2942 N N   . ASP B 1 118 ? 21.867 8.580   5.574   1.00 71.07  ? 118 ASP B N   1 
ATOM   2943 C CA  . ASP B 1 118 ? 22.832 7.506   5.233   1.00 75.22  ? 118 ASP B CA  1 
ATOM   2944 C C   . ASP B 1 118 ? 22.155 6.148   5.426   1.00 74.87  ? 118 ASP B C   1 
ATOM   2945 O O   . ASP B 1 118 ? 21.378 6.008   6.388   1.00 80.23  ? 118 ASP B O   1 
ATOM   2946 C CB  . ASP B 1 118 ? 24.122 7.595   6.046   1.00 77.34  ? 118 ASP B CB  1 
ATOM   2947 C CG  . ASP B 1 118 ? 23.889 7.776   7.524   1.00 80.00  ? 118 ASP B CG  1 
ATOM   2948 O OD1 . ASP B 1 118 ? 23.329 8.842   7.902   1.00 89.42  ? 118 ASP B OD1 1 
ATOM   2949 O OD2 . ASP B 1 118 ? 24.272 6.866   8.274   1.00 77.66  ? 118 ASP B OD2 1 
ATOM   2950 N N   . LEU B 1 119 ? 22.488 5.199   4.544   1.00 64.52  ? 119 LEU B N   1 
ATOM   2951 C CA  . LEU B 1 119 ? 21.972 3.806   4.500   1.00 60.00  ? 119 LEU B CA  1 
ATOM   2952 C C   . LEU B 1 119 ? 22.138 3.133   5.869   1.00 57.69  ? 119 LEU B C   1 
ATOM   2953 O O   . LEU B 1 119 ? 21.329 2.245   6.193   1.00 51.57  ? 119 LEU B O   1 
ATOM   2954 C CB  . LEU B 1 119 ? 22.736 3.056   3.412   1.00 59.03  ? 119 LEU B CB  1 
ATOM   2955 C CG  . LEU B 1 119 ? 22.420 1.573   3.270   1.00 58.90  ? 119 LEU B CG  1 
ATOM   2956 C CD1 . LEU B 1 119 ? 20.960 1.370   2.912   1.00 63.26  ? 119 LEU B CD1 1 
ATOM   2957 C CD2 . LEU B 1 119 ? 23.320 0.940   2.217   1.00 59.39  ? 119 LEU B CD2 1 
ATOM   2958 N N   . SER B 1 120 ? 23.139 3.539   6.647   1.00 55.07  ? 120 SER B N   1 
ATOM   2959 C CA  . SER B 1 120 ? 23.312 3.100   8.051   1.00 55.42  ? 120 SER B CA  1 
ATOM   2960 C C   . SER B 1 120 ? 22.013 3.337   8.827   1.00 60.24  ? 120 SER B C   1 
ATOM   2961 O O   . SER B 1 120 ? 21.427 2.340   9.321   1.00 65.45  ? 120 SER B O   1 
ATOM   2962 C CB  . SER B 1 120 ? 24.440 3.804   8.682   1.00 51.34  ? 120 SER B CB  1 
ATOM   2963 O OG  . SER B 1 120 ? 24.651 3.287   9.969   1.00 64.57  ? 120 SER B OG  1 
ATOM   2964 N N   . ARG B 1 121 ? 21.570 4.598   8.890   1.00 65.04  ? 121 ARG B N   1 
ATOM   2965 C CA  . ARG B 1 121 ? 20.322 5.042   9.574   1.00 71.23  ? 121 ARG B CA  1 
ATOM   2966 C C   . ARG B 1 121 ? 19.124 4.226   9.076   1.00 63.28  ? 121 ARG B C   1 
ATOM   2967 O O   . ARG B 1 121 ? 18.382 3.696   9.906   1.00 68.02  ? 121 ARG B O   1 
ATOM   2968 C CB  . ARG B 1 121 ? 20.074 6.541   9.369   1.00 80.38  ? 121 ARG B CB  1 
ATOM   2969 C CG  . ARG B 1 121 ? 20.308 7.360   10.630  1.00 96.53  ? 121 ARG B CG  1 
ATOM   2970 C CD  . ARG B 1 121 ? 20.390 8.863   10.412  1.00 104.57 ? 121 ARG B CD  1 
ATOM   2971 N NE  . ARG B 1 121 ? 21.118 9.475   11.519  1.00 106.85 ? 121 ARG B NE  1 
ATOM   2972 C CZ  . ARG B 1 121 ? 22.443 9.432   11.679  1.00 106.75 ? 121 ARG B CZ  1 
ATOM   2973 N NH1 . ARG B 1 121 ? 23.205 8.818   10.787  1.00 111.63 ? 121 ARG B NH1 1 
ATOM   2974 N NH2 . ARG B 1 121 ? 23.007 10.005  12.731  1.00 102.83 ? 121 ARG B NH2 1 
ATOM   2975 N N   . MET B 1 122 ? 18.931 4.145   7.766   1.00 60.50  ? 122 MET B N   1 
ATOM   2976 C CA  . MET B 1 122 ? 17.813 3.381   7.158   1.00 60.49  ? 122 MET B CA  1 
ATOM   2977 C C   . MET B 1 122 ? 17.874 1.909   7.607   1.00 64.32  ? 122 MET B C   1 
ATOM   2978 O O   . MET B 1 122 ? 16.802 1.309   7.823   1.00 66.84  ? 122 MET B O   1 
ATOM   2979 C CB  . MET B 1 122 ? 17.878 3.457   5.634   1.00 60.60  ? 122 MET B CB  1 
ATOM   2980 C CG  . MET B 1 122 ? 16.691 2.808   4.975   1.00 68.45  ? 122 MET B CG  1 
ATOM   2981 S SD  . MET B 1 122 ? 17.002 2.386   3.256   1.00 74.59  ? 122 MET B SD  1 
ATOM   2982 C CE  . MET B 1 122 ? 16.259 3.817   2.466   1.00 79.76  ? 122 MET B CE  1 
ATOM   2983 N N   . ILE B 1 123 ? 19.078 1.345   7.738   1.00 63.88  ? 123 ILE B N   1 
ATOM   2984 C CA  . ILE B 1 123 ? 19.296 -0.074  8.149   1.00 61.31  ? 123 ILE B CA  1 
ATOM   2985 C C   . ILE B 1 123 ? 18.867 -0.231  9.610   1.00 67.95  ? 123 ILE B C   1 
ATOM   2986 O O   . ILE B 1 123 ? 18.108 -1.183  9.880   1.00 65.15  ? 123 ILE B O   1 
ATOM   2987 C CB  . ILE B 1 123 ? 20.751 -0.535  7.916   1.00 57.07  ? 123 ILE B CB  1 
ATOM   2988 C CG1 . ILE B 1 123 ? 20.933 -1.073  6.496   1.00 55.50  ? 123 ILE B CG1 1 
ATOM   2989 C CG2 . ILE B 1 123 ? 21.193 -1.561  8.958   1.00 56.68  ? 123 ILE B CG2 1 
ATOM   2990 C CD1 . ILE B 1 123 ? 22.370 -1.095  6.027   1.00 57.12  ? 123 ILE B CD1 1 
ATOM   2991 N N   . LYS B 1 124 ? 19.336 0.635   10.517  1.00 66.71  ? 124 LYS B N   1 
ATOM   2992 C CA  . LYS B 1 124 ? 19.000 0.497   11.957  1.00 74.69  ? 124 LYS B CA  1 
ATOM   2993 C C   . LYS B 1 124 ? 17.518 0.840   12.160  1.00 74.42  ? 124 LYS B C   1 
ATOM   2994 O O   . LYS B 1 124 ? 16.958 0.370   13.154  1.00 88.76  ? 124 LYS B O   1 
ATOM   2995 C CB  . LYS B 1 124 ? 19.943 1.309   12.843  1.00 80.08  ? 124 LYS B CB  1 
ATOM   2996 C CG  . LYS B 1 124 ? 19.811 2.814   12.724  1.00 96.81  ? 124 LYS B CG  1 
ATOM   2997 C CD  . LYS B 1 124 ? 20.736 3.565   13.653  1.00 113.93 ? 124 LYS B CD  1 
ATOM   2998 C CE  . LYS B 1 124 ? 20.710 5.065   13.419  1.00 127.09 ? 124 LYS B CE  1 
ATOM   2999 N NZ  . LYS B 1 124 ? 21.657 5.797   14.297  1.00 126.95 ? 124 LYS B NZ  1 
ATOM   3000 N N   . HIS B 1 125 ? 16.898 1.576   11.231  1.00 72.26  ? 125 HIS B N   1 
ATOM   3001 C CA  . HIS B 1 125 ? 15.438 1.869   11.231  1.00 77.43  ? 125 HIS B CA  1 
ATOM   3002 C C   . HIS B 1 125 ? 14.689 0.544   11.066  1.00 77.70  ? 125 HIS B C   1 
ATOM   3003 O O   . HIS B 1 125 ? 14.076 0.107   12.050  1.00 85.14  ? 125 HIS B O   1 
ATOM   3004 C CB  . HIS B 1 125 ? 15.080 2.930   10.172  1.00 78.45  ? 125 HIS B CB  1 
ATOM   3005 C CG  . HIS B 1 125 ? 13.632 3.287   10.098  0.32 77.23  ? 125 HIS B CG  1 
ATOM   3006 N ND1 . HIS B 1 125 ? 13.028 4.142   11.002  1.00 78.91  ? 125 HIS B ND1 1 
ATOM   3007 C CD2 . HIS B 1 125 ? 12.676 2.940   9.211   0.26 78.89  ? 125 HIS B CD2 1 
ATOM   3008 C CE1 . HIS B 1 125 ? 11.759 4.287   10.692  0.62 76.21  ? 125 HIS B CE1 1 
ATOM   3009 N NE2 . HIS B 1 125 ? 11.517 3.559   9.595   1.00 82.98  ? 125 HIS B NE2 1 
ATOM   3010 N N   . PHE B 1 126 ? 14.801 -0.087  9.889   1.00 74.76  ? 126 PHE B N   1 
ATOM   3011 C CA  . PHE B 1 126 ? 14.212 -1.410  9.547   1.00 70.48  ? 126 PHE B CA  1 
ATOM   3012 C C   . PHE B 1 126 ? 14.485 -2.444  10.650  1.00 72.80  ? 126 PHE B C   1 
ATOM   3013 O O   . PHE B 1 126 ? 13.614 -3.310  10.868  1.00 77.53  ? 126 PHE B O   1 
ATOM   3014 C CB  . PHE B 1 126 ? 14.778 -1.938  8.227   1.00 66.74  ? 126 PHE B CB  1 
ATOM   3015 C CG  . PHE B 1 126 ? 14.028 -1.540  6.983   1.00 65.01  ? 126 PHE B CG  1 
ATOM   3016 C CD1 . PHE B 1 126 ? 14.260 -0.317  6.373   1.00 66.10  ? 126 PHE B CD1 1 
ATOM   3017 C CD2 . PHE B 1 126 ? 13.111 -2.409  6.400   1.00 73.37  ? 126 PHE B CD2 1 
ATOM   3018 C CE1 . PHE B 1 126 ? 13.585 0.035   5.213   1.00 64.42  ? 126 PHE B CE1 1 
ATOM   3019 C CE2 . PHE B 1 126 ? 12.426 -2.055  5.245   1.00 69.34  ? 126 PHE B CE2 1 
ATOM   3020 C CZ  . PHE B 1 126 ? 12.663 -0.828  4.657   1.00 70.58  ? 126 PHE B CZ  1 
ATOM   3021 N N   . LYS B 1 127 ? 15.656 -2.381  11.290  1.00 69.43  ? 127 LYS B N   1 
ATOM   3022 C CA  . LYS B 1 127 ? 16.083 -3.302  12.379  1.00 76.01  ? 127 LYS B CA  1 
ATOM   3023 C C   . LYS B 1 127 ? 15.155 -3.127  13.596  1.00 83.51  ? 127 LYS B C   1 
ATOM   3024 O O   . LYS B 1 127 ? 14.607 -4.147  14.063  1.00 83.89  ? 127 LYS B O   1 
ATOM   3025 C CB  . LYS B 1 127 ? 17.554 -3.053  12.736  1.00 77.55  ? 127 LYS B CB  1 
ATOM   3026 C CG  . LYS B 1 127 ? 18.293 -4.222  13.375  1.00 83.80  ? 127 LYS B CG  1 
ATOM   3027 C CD  . LYS B 1 127 ? 19.715 -3.877  13.791  1.00 91.25  ? 127 LYS B CD  1 
ATOM   3028 C CE  . LYS B 1 127 ? 20.425 -5.004  14.514  1.00 92.78  ? 127 LYS B CE  1 
ATOM   3029 N NZ  . LYS B 1 127 ? 20.781 -6.104  13.587  1.00 86.79  ? 127 LYS B NZ  1 
ATOM   3030 N N   . LYS B 1 128 ? 14.960 -1.895  14.084  1.00 90.52  ? 128 LYS B N   1 
ATOM   3031 C CA  . LYS B 1 128 ? 14.043 -1.594  15.222  1.00 94.09  ? 128 LYS B CA  1 
ATOM   3032 C C   . LYS B 1 128 ? 12.640 -2.120  14.895  1.00 89.97  ? 128 LYS B C   1 
ATOM   3033 O O   . LYS B 1 128 ? 12.055 -2.788  15.760  1.00 87.02  ? 128 LYS B O   1 
ATOM   3034 C CB  . LYS B 1 128 ? 13.981 -0.096  15.530  1.00 98.79  ? 128 LYS B CB  1 
ATOM   3035 C CG  . LYS B 1 128 ? 15.279 0.520   16.036  1.00 109.34 ? 128 LYS B CG  1 
ATOM   3036 C CD  . LYS B 1 128 ? 15.695 0.056   17.416  1.00 119.06 ? 128 LYS B CD  1 
ATOM   3037 C CE  . LYS B 1 128 ? 16.938 0.759   17.922  1.00 125.16 ? 128 LYS B CE  1 
ATOM   3038 N NZ  . LYS B 1 128 ? 18.117 0.464   17.072  1.00 136.57 ? 128 LYS B NZ  1 
ATOM   3039 N N   . GLN B 1 129 ? 12.154 -1.869  13.674  1.00 87.22  ? 129 GLN B N   1 
ATOM   3040 C CA  . GLN B 1 129 ? 10.799 -2.263  13.190  1.00 91.48  ? 129 GLN B CA  1 
ATOM   3041 C C   . GLN B 1 129 ? 10.783 -3.740  12.768  1.00 87.38  ? 129 GLN B C   1 
ATOM   3042 O O   . GLN B 1 129 ? 9.799  -4.157  12.129  1.00 84.15  ? 129 GLN B O   1 
ATOM   3043 C CB  . GLN B 1 129 ? 10.362 -1.366  12.026  1.00 97.58  ? 129 GLN B CB  1 
ATOM   3044 C CG  . GLN B 1 129 ? 10.186 0.096   12.422  1.00 108.80 ? 129 GLN B CG  1 
ATOM   3045 C CD  . GLN B 1 129 ? 9.975  0.993   11.225  1.00 119.42 ? 129 GLN B CD  1 
ATOM   3046 O OE1 . GLN B 1 129 ? 10.754 0.986   10.274  1.00 123.33 ? 129 GLN B OE1 1 
ATOM   3047 N NE2 . GLN B 1 129 ? 8.912  1.782   11.260  1.00 123.85 ? 129 GLN B NE2 1 
ATOM   3048 N N   . LYS B 1 130 ? 11.827 -4.501  13.107  1.00 90.51  ? 130 LYS B N   1 
ATOM   3049 C CA  . LYS B 1 130 ? 11.925 -5.969  12.874  1.00 95.80  ? 130 LYS B CA  1 
ATOM   3050 C C   . LYS B 1 130 ? 11.389 -6.320  11.475  1.00 94.91  ? 130 LYS B C   1 
ATOM   3051 O O   . LYS B 1 130 ? 10.726 -7.361  11.337  1.00 94.78  ? 130 LYS B O   1 
ATOM   3052 C CB  . LYS B 1 130 ? 11.185 -6.708  13.996  1.00 97.04  ? 130 LYS B CB  1 
ATOM   3053 C CG  . LYS B 1 130 ? 11.805 -6.566  15.381  1.00 101.38 ? 130 LYS B CG  1 
ATOM   3054 C CD  . LYS B 1 130 ? 11.010 -7.252  16.476  1.00 105.88 ? 130 LYS B CD  1 
ATOM   3055 C CE  . LYS B 1 130 ? 11.644 -7.135  17.847  1.00 102.31 ? 130 LYS B CE  1 
ATOM   3056 N NZ  . LYS B 1 130 ? 10.837 -7.829  18.877  1.00 105.70 ? 130 LYS B NZ  1 
ATOM   3057 N N   . ARG B 1 131 ? 11.687 -5.496  10.465  1.00 100.31 ? 131 ARG B N   1 
ATOM   3058 C CA  . ARG B 1 131 ? 11.282 -5.729  9.050   1.00 100.59 ? 131 ARG B CA  1 
ATOM   3059 C C   . ARG B 1 131 ? 12.546 -5.869  8.194   1.00 89.91  ? 131 ARG B C   1 
ATOM   3060 O O   . ARG B 1 131 ? 13.632 -5.532  8.677   1.00 82.95  ? 131 ARG B O   1 
ATOM   3061 C CB  . ARG B 1 131 ? 10.391 -4.588  8.549   1.00 106.86 ? 131 ARG B CB  1 
ATOM   3062 C CG  . ARG B 1 131 ? 9.296  -5.020  7.583   1.00 115.69 ? 131 ARG B CG  1 
ATOM   3063 C CD  . ARG B 1 131 ? 8.721  -3.854  6.790   1.00 120.65 ? 131 ARG B CD  1 
ATOM   3064 N NE  . ARG B 1 131 ? 8.287  -2.749  7.643   1.00 122.98 ? 131 ARG B NE  1 
ATOM   3065 C CZ  . ARG B 1 131 ? 7.158  -2.719  8.354   1.00 117.85 ? 131 ARG B CZ  1 
ATOM   3066 N NH1 . ARG B 1 131 ? 6.872  -1.660  9.094   1.00 111.50 ? 131 ARG B NH1 1 
ATOM   3067 N NH2 . ARG B 1 131 ? 6.316  -3.738  8.329   1.00 119.90 ? 131 ARG B NH2 1 
ATOM   3068 N N   . LEU B 1 132 ? 12.402 -6.377  6.973   1.00 85.96  ? 132 LEU B N   1 
ATOM   3069 C CA  . LEU B 1 132 ? 13.510 -6.543  5.998   1.00 81.22  ? 132 LEU B CA  1 
ATOM   3070 C C   . LEU B 1 132 ? 13.294 -5.571  4.837   1.00 72.99  ? 132 LEU B C   1 
ATOM   3071 O O   . LEU B 1 132 ? 12.131 -5.241  4.556   1.00 69.74  ? 132 LEU B O   1 
ATOM   3072 C CB  . LEU B 1 132 ? 13.539 -7.992  5.507   1.00 79.27  ? 132 LEU B CB  1 
ATOM   3073 C CG  . LEU B 1 132 ? 13.928 -9.034  6.556   1.00 83.03  ? 132 LEU B CG  1 
ATOM   3074 C CD1 . LEU B 1 132 ? 13.585 -10.433 6.067   1.00 86.48  ? 132 LEU B CD1 1 
ATOM   3075 C CD2 . LEU B 1 132 ? 15.408 -8.931  6.909   1.00 83.24  ? 132 LEU B CD2 1 
ATOM   3076 N N   . ILE B 1 133 ? 14.378 -5.119  4.207   1.00 61.81  ? 133 ILE B N   1 
ATOM   3077 C CA  . ILE B 1 133 ? 14.295 -4.330  2.946   1.00 60.81  ? 133 ILE B CA  1 
ATOM   3078 C C   . ILE B 1 133 ? 13.955 -5.324  1.843   1.00 58.92  ? 133 ILE B C   1 
ATOM   3079 O O   . ILE B 1 133 ? 14.678 -6.302  1.630   1.00 59.55  ? 133 ILE B O   1 
ATOM   3080 C CB  . ILE B 1 133 ? 15.580 -3.523  2.663   1.00 62.78  ? 133 ILE B CB  1 
ATOM   3081 C CG1 . ILE B 1 133 ? 15.993 -2.686  3.879   1.00 56.02  ? 133 ILE B CG1 1 
ATOM   3082 C CG2 . ILE B 1 133 ? 15.428 -2.659  1.406   1.00 63.64  ? 133 ILE B CG2 1 
ATOM   3083 C CD1 . ILE B 1 133 ? 17.373 -2.101  3.774   1.00 57.68  ? 133 ILE B CD1 1 
ATOM   3084 N N   . PRO B 1 134 ? 12.809 -5.145  1.153   1.00 57.46  ? 134 PRO B N   1 
ATOM   3085 C CA  . PRO B 1 134 ? 12.433 -6.055  0.079   1.00 57.29  ? 134 PRO B CA  1 
ATOM   3086 C C   . PRO B 1 134 ? 13.478 -5.972  -1.037  1.00 56.07  ? 134 PRO B C   1 
ATOM   3087 O O   . PRO B 1 134 ? 13.927 -4.850  -1.342  1.00 50.41  ? 134 PRO B O   1 
ATOM   3088 C CB  . PRO B 1 134 ? 11.057 -5.567  -0.397  1.00 62.10  ? 134 PRO B CB  1 
ATOM   3089 C CG  . PRO B 1 134 ? 10.943 -4.141  0.131   1.00 63.39  ? 134 PRO B CG  1 
ATOM   3090 C CD  . PRO B 1 134 ? 11.822 -4.078  1.367   1.00 59.99  ? 134 PRO B CD  1 
ATOM   3091 N N   . GLU B 1 135 ? 13.822 -7.137  -1.604  1.00 53.23  ? 135 GLU B N   1 
ATOM   3092 C CA  . GLU B 1 135 ? 14.762 -7.303  -2.748  1.00 56.31  ? 135 GLU B CA  1 
ATOM   3093 C C   . GLU B 1 135 ? 14.573 -6.192  -3.804  1.00 55.58  ? 135 GLU B C   1 
ATOM   3094 O O   . GLU B 1 135 ? 15.576 -5.798  -4.444  1.00 56.66  ? 135 GLU B O   1 
ATOM   3095 C CB  . GLU B 1 135 ? 14.580 -8.689  -3.374  1.00 53.88  ? 135 GLU B CB  1 
ATOM   3096 C CG  . GLU B 1 135 ? 15.387 -8.889  -4.653  1.00 50.58  ? 135 GLU B CG  1 
ATOM   3097 C CD  . GLU B 1 135 ? 15.818 -10.313 -4.925  1.00 54.34  ? 135 GLU B CD  1 
ATOM   3098 O OE1 . GLU B 1 135 ? 15.606 -11.154 -4.030  1.00 61.09  ? 135 GLU B OE1 1 
ATOM   3099 O OE2 . GLU B 1 135 ? 16.359 -10.582 -6.031  1.00 53.34  ? 135 GLU B OE2 1 
ATOM   3100 N N   . ARG B 1 136 ? 13.345 -5.713  -3.997  1.00 60.49  ? 136 ARG B N   1 
ATOM   3101 C CA  . ARG B 1 136 ? 12.976 -4.723  -5.046  1.00 70.99  ? 136 ARG B CA  1 
ATOM   3102 C C   . ARG B 1 136 ? 13.632 -3.365  -4.731  1.00 67.25  ? 136 ARG B C   1 
ATOM   3103 O O   . ARG B 1 136 ? 14.204 -2.758  -5.665  1.00 57.46  ? 136 ARG B O   1 
ATOM   3104 C CB  . ARG B 1 136 ? 11.448 -4.666  -5.132  1.00 79.91  ? 136 ARG B CB  1 
ATOM   3105 C CG  . ARG B 1 136 ? 10.890 -3.747  -6.207  1.00 95.82  ? 136 ARG B CG  1 
ATOM   3106 C CD  . ARG B 1 136 ? 9.377  -3.886  -6.283  1.00 108.36 ? 136 ARG B CD  1 
ATOM   3107 N NE  . ARG B 1 136 ? 8.764  -3.454  -5.031  1.00 123.23 ? 136 ARG B NE  1 
ATOM   3108 C CZ  . ARG B 1 136 ? 8.473  -2.192  -4.708  1.00 124.11 ? 136 ARG B CZ  1 
ATOM   3109 N NH1 . ARG B 1 136 ? 7.933  -1.925  -3.531  1.00 125.26 ? 136 ARG B NH1 1 
ATOM   3110 N NH2 . ARG B 1 136 ? 8.712  -1.202  -5.551  1.00 120.82 ? 136 ARG B NH2 1 
ATOM   3111 N N   . THR B 1 137 ? 13.560 -2.919  -3.469  1.00 59.31  ? 137 THR B N   1 
ATOM   3112 C CA  . THR B 1 137 ? 14.169 -1.657  -2.967  1.00 63.85  ? 137 THR B CA  1 
ATOM   3113 C C   . THR B 1 137 ? 15.701 -1.787  -2.992  1.00 57.70  ? 137 THR B C   1 
ATOM   3114 O O   . THR B 1 137 ? 16.383 -0.830  -3.401  1.00 53.42  ? 137 THR B O   1 
ATOM   3115 C CB  . THR B 1 137 ? 13.702 -1.321  -1.542  1.00 63.28  ? 137 THR B CB  1 
ATOM   3116 O OG1 . THR B 1 137 ? 12.285 -1.207  -1.529  1.00 64.77  ? 137 THR B OG1 1 
ATOM   3117 C CG2 . THR B 1 137 ? 14.285 -0.029  -1.012  1.00 66.15  ? 137 THR B CG2 1 
ATOM   3118 N N   . VAL B 1 138 ? 16.214 -2.930  -2.550  1.00 51.43  ? 138 VAL B N   1 
ATOM   3119 C CA  . VAL B 1 138 ? 17.674 -3.191  -2.495  1.00 55.36  ? 138 VAL B CA  1 
ATOM   3120 C C   . VAL B 1 138 ? 18.234 -2.944  -3.896  1.00 53.66  ? 138 VAL B C   1 
ATOM   3121 O O   . VAL B 1 138 ? 19.207 -2.198  -3.976  1.00 53.76  ? 138 VAL B O   1 
ATOM   3122 C CB  . VAL B 1 138 ? 18.000 -4.602  -1.964  1.00 53.27  ? 138 VAL B CB  1 
ATOM   3123 C CG1 . VAL B 1 138 ? 19.438 -5.014  -2.257  1.00 50.16  ? 138 VAL B CG1 1 
ATOM   3124 C CG2 . VAL B 1 138 ? 17.719 -4.695  -0.473  1.00 56.60  ? 138 VAL B CG2 1 
ATOM   3125 N N   . TRP B 1 139 ? 17.639 -3.525  -4.946  1.00 50.40  ? 139 TRP B N   1 
ATOM   3126 C CA  . TRP B 1 139 ? 18.123 -3.348  -6.340  1.00 56.34  ? 139 TRP B CA  1 
ATOM   3127 C C   . TRP B 1 139 ? 17.985 -1.879  -6.774  1.00 60.84  ? 139 TRP B C   1 
ATOM   3128 O O   . TRP B 1 139 ? 18.870 -1.406  -7.531  1.00 57.41  ? 139 TRP B O   1 
ATOM   3129 C CB  . TRP B 1 139 ? 17.400 -4.276  -7.317  1.00 58.86  ? 139 TRP B CB  1 
ATOM   3130 C CG  . TRP B 1 139 ? 17.742 -5.725  -7.175  1.00 61.91  ? 139 TRP B CG  1 
ATOM   3131 C CD1 . TRP B 1 139 ? 16.870 -6.746  -6.931  1.00 60.12  ? 139 TRP B CD1 1 
ATOM   3132 C CD2 . TRP B 1 139 ? 19.044 -6.328  -7.295  1.00 62.19  ? 139 TRP B CD2 1 
ATOM   3133 N NE1 . TRP B 1 139 ? 17.535 -7.940  -6.897  1.00 60.50  ? 139 TRP B NE1 1 
ATOM   3134 C CE2 . TRP B 1 139 ? 18.871 -7.716  -7.103  1.00 61.35  ? 139 TRP B CE2 1 
ATOM   3135 C CE3 . TRP B 1 139 ? 20.332 -5.840  -7.544  1.00 61.96  ? 139 TRP B CE3 1 
ATOM   3136 C CZ2 . TRP B 1 139 ? 19.937 -8.615  -7.171  1.00 58.28  ? 139 TRP B CZ2 1 
ATOM   3137 C CZ3 . TRP B 1 139 ? 21.386 -6.727  -7.594  1.00 56.39  ? 139 TRP B CZ3 1 
ATOM   3138 C CH2 . TRP B 1 139 ? 21.189 -8.096  -7.415  1.00 58.21  ? 139 TRP B CH2 1 
ATOM   3139 N N   . LYS B 1 140 ? 16.921 -1.192  -6.342  1.00 65.54  ? 140 LYS B N   1 
ATOM   3140 C CA  . LYS B 1 140 ? 16.676 0.239   -6.672  1.00 69.84  ? 140 LYS B CA  1 
ATOM   3141 C C   . LYS B 1 140 ? 17.902 1.039   -6.216  1.00 63.66  ? 140 LYS B C   1 
ATOM   3142 O O   . LYS B 1 140 ? 18.436 1.835   -7.055  1.00 48.33  ? 140 LYS B O   1 
ATOM   3143 C CB  . LYS B 1 140 ? 15.376 0.761   -6.041  1.00 79.32  ? 140 LYS B CB  1 
ATOM   3144 C CG  . LYS B 1 140 ? 14.876 2.098   -6.581  1.00 83.98  ? 140 LYS B CG  1 
ATOM   3145 C CD  . LYS B 1 140 ? 13.431 2.410   -6.211  1.00 95.24  ? 140 LYS B CD  1 
ATOM   3146 C CE  . LYS B 1 140 ? 13.271 3.242   -4.951  1.00 97.10  ? 140 LYS B CE  1 
ATOM   3147 N NZ  . LYS B 1 140 ? 13.463 4.687   -5.217  1.00 92.30  ? 140 LYS B NZ  1 
ATOM   3148 N N   . TYR B 1 141 ? 18.361 0.797   -4.978  1.00 55.62  ? 141 TYR B N   1 
ATOM   3149 C CA  . TYR B 1 141 ? 19.507 1.523   -4.359  1.00 60.63  ? 141 TYR B CA  1 
ATOM   3150 C C   . TYR B 1 141 ? 20.840 1.041   -4.949  1.00 53.74  ? 141 TYR B C   1 
ATOM   3151 O O   . TYR B 1 141 ? 21.704 1.872   -5.305  1.00 48.39  ? 141 TYR B O   1 
ATOM   3152 C CB  . TYR B 1 141 ? 19.485 1.393   -2.833  1.00 59.88  ? 141 TYR B CB  1 
ATOM   3153 C CG  . TYR B 1 141 ? 18.273 2.008   -2.188  1.00 63.02  ? 141 TYR B CG  1 
ATOM   3154 C CD1 . TYR B 1 141 ? 17.575 3.024   -2.814  1.00 66.14  ? 141 TYR B CD1 1 
ATOM   3155 C CD2 . TYR B 1 141 ? 17.824 1.579   -0.950  1.00 67.71  ? 141 TYR B CD2 1 
ATOM   3156 C CE1 . TYR B 1 141 ? 16.451 3.592   -2.239  1.00 72.14  ? 141 TYR B CE1 1 
ATOM   3157 C CE2 . TYR B 1 141 ? 16.704 2.139   -0.359  1.00 72.05  ? 141 TYR B CE2 1 
ATOM   3158 C CZ  . TYR B 1 141 ? 16.013 3.149   -1.007  1.00 72.37  ? 141 TYR B CZ  1 
ATOM   3159 O OH  . TYR B 1 141 ? 14.909 3.729   -0.454  1.00 80.80  ? 141 TYR B OH  1 
ATOM   3160 N N   . PHE B 1 142 ? 20.998 -0.272  -5.073  1.00 47.20  ? 142 PHE B N   1 
ATOM   3161 C CA  . PHE B 1 142 ? 22.295 -0.908  -5.403  1.00 47.14  ? 142 PHE B CA  1 
ATOM   3162 C C   . PHE B 1 142 ? 22.670 -0.531  -6.845  1.00 48.51  ? 142 PHE B C   1 
ATOM   3163 O O   . PHE B 1 142 ? 23.874 -0.314  -7.104  1.00 46.47  ? 142 PHE B O   1 
ATOM   3164 C CB  . PHE B 1 142 ? 22.239 -2.418  -5.125  1.00 42.50  ? 142 PHE B CB  1 
ATOM   3165 C CG  . PHE B 1 142 ? 23.564 -3.129  -5.227  1.00 43.08  ? 142 PHE B CG  1 
ATOM   3166 C CD1 . PHE B 1 142 ? 24.482 -3.080  -4.189  1.00 41.72  ? 142 PHE B CD1 1 
ATOM   3167 C CD2 . PHE B 1 142 ? 23.906 -3.818  -6.380  1.00 43.92  ? 142 PHE B CD2 1 
ATOM   3168 C CE1 . PHE B 1 142 ? 25.714 -3.689  -4.315  1.00 41.38  ? 142 PHE B CE1 1 
ATOM   3169 C CE2 . PHE B 1 142 ? 25.126 -4.463  -6.486  1.00 45.94  ? 142 PHE B CE2 1 
ATOM   3170 C CZ  . PHE B 1 142 ? 26.029 -4.392  -5.450  1.00 41.87  ? 142 PHE B CZ  1 
ATOM   3171 N N   . VAL B 1 143 ? 21.689 -0.431  -7.755  1.00 46.33  ? 143 VAL B N   1 
ATOM   3172 C CA  . VAL B 1 143 ? 21.968 -0.089  -9.182  1.00 49.22  ? 143 VAL B CA  1 
ATOM   3173 C C   . VAL B 1 143 ? 22.596 1.307   -9.240  1.00 48.31  ? 143 VAL B C   1 
ATOM   3174 O O   . VAL B 1 143 ? 23.405 1.529   -10.147 1.00 49.00  ? 143 VAL B O   1 
ATOM   3175 C CB  . VAL B 1 143 ? 20.735 -0.190  -10.110 1.00 51.36  ? 143 VAL B CB  1 
ATOM   3176 C CG1 . VAL B 1 143 ? 19.674 0.855   -9.808  1.00 49.78  ? 143 VAL B CG1 1 
ATOM   3177 C CG2 . VAL B 1 143 ? 21.139 -0.124  -11.585 1.00 54.79  ? 143 VAL B CG2 1 
ATOM   3178 N N   . GLN B 1 144 ? 22.226 2.210   -8.329  1.00 44.84  ? 144 GLN B N   1 
ATOM   3179 C CA  . GLN B 1 144 ? 22.711 3.611   -8.364  1.00 53.18  ? 144 GLN B CA  1 
ATOM   3180 C C   . GLN B 1 144 ? 24.157 3.667   -7.856  1.00 51.46  ? 144 GLN B C   1 
ATOM   3181 O O   . GLN B 1 144 ? 24.998 4.304   -8.527  1.00 48.47  ? 144 GLN B O   1 
ATOM   3182 C CB  . GLN B 1 144 ? 21.755 4.495   -7.568  1.00 55.94  ? 144 GLN B CB  1 
ATOM   3183 C CG  . GLN B 1 144 ? 20.400 4.624   -8.246  1.00 56.81  ? 144 GLN B CG  1 
ATOM   3184 C CD  . GLN B 1 144 ? 19.479 5.509   -7.452  1.00 54.59  ? 144 GLN B CD  1 
ATOM   3185 O OE1 . GLN B 1 144 ? 19.555 6.730   -7.552  1.00 52.17  ? 144 GLN B OE1 1 
ATOM   3186 N NE2 . GLN B 1 144 ? 18.616 4.897   -6.650  1.00 57.72  ? 144 GLN B NE2 1 
ATOM   3187 N N   . LEU B 1 145 ? 24.418 3.034   -6.713  1.00 49.59  ? 145 LEU B N   1 
ATOM   3188 C CA  . LEU B 1 145 ? 25.784 2.793   -6.190  1.00 47.86  ? 145 LEU B CA  1 
ATOM   3189 C C   . LEU B 1 145 ? 26.680 2.219   -7.280  1.00 47.59  ? 145 LEU B C   1 
ATOM   3190 O O   . LEU B 1 145 ? 27.806 2.749   -7.442  1.00 47.23  ? 145 LEU B O   1 
ATOM   3191 C CB  . LEU B 1 145 ? 25.693 1.831   -5.025  1.00 53.36  ? 145 LEU B CB  1 
ATOM   3192 C CG  . LEU B 1 145 ? 25.574 2.524   -3.683  1.00 62.46  ? 145 LEU B CG  1 
ATOM   3193 C CD1 . LEU B 1 145 ? 25.027 1.553   -2.651  1.00 70.69  ? 145 LEU B CD1 1 
ATOM   3194 C CD2 . LEU B 1 145 ? 26.933 3.077   -3.268  1.00 66.77  ? 145 LEU B CD2 1 
ATOM   3195 N N   . CYS B 1 146 ? 26.203 1.207   -8.003  1.00 39.83  ? 146 CYS B N   1 
ATOM   3196 C CA  . CYS B 1 146 ? 26.993 0.532   -9.064  1.00 44.41  ? 146 CYS B CA  1 
ATOM   3197 C C   . CYS B 1 146 ? 27.246 1.514   -10.217 1.00 45.36  ? 146 CYS B C   1 
ATOM   3198 O O   . CYS B 1 146 ? 28.401 1.505   -10.773 1.00 39.68  ? 146 CYS B O   1 
ATOM   3199 C CB  . CYS B 1 146 ? 26.328 -0.735  -9.589  1.00 51.79  ? 146 CYS B CB  1 
ATOM   3200 S SG  . CYS B 1 146 ? 26.106 -2.033  -8.345  1.00 50.89  ? 146 CYS B SG  1 
ATOM   3201 N N   . SER B 1 147 ? 26.232 2.321   -10.571 1.00 41.47  ? 147 SER B N   1 
ATOM   3202 C CA  . SER B 1 147 ? 26.340 3.393   -11.601 1.00 43.30  ? 147 SER B CA  1 
ATOM   3203 C C   . SER B 1 147 ? 27.474 4.350   -11.199 1.00 41.63  ? 147 SER B C   1 
ATOM   3204 O O   . SER B 1 147 ? 28.443 4.508   -11.998 1.00 45.78  ? 147 SER B O   1 
ATOM   3205 C CB  . SER B 1 147 ? 25.035 4.123   -11.828 1.00 44.61  ? 147 SER B CB  1 
ATOM   3206 O OG  . SER B 1 147 ? 25.079 4.824   -13.065 1.00 45.87  ? 147 SER B OG  1 
ATOM   3207 N N   . ALA B 1 148 ? 27.411 4.883   -9.978  1.00 35.88  ? 148 ALA B N   1 
ATOM   3208 C CA  . ALA B 1 148 ? 28.500 5.665   -9.338  1.00 39.75  ? 148 ALA B CA  1 
ATOM   3209 C C   . ALA B 1 148 ? 29.864 4.967   -9.464  1.00 40.78  ? 148 ALA B C   1 
ATOM   3210 O O   . ALA B 1 148 ? 30.810 5.561   -10.005 1.00 41.47  ? 148 ALA B O   1 
ATOM   3211 C CB  . ALA B 1 148 ? 28.161 5.902   -7.897  1.00 43.49  ? 148 ALA B CB  1 
ATOM   3212 N N   . LEU B 1 149 ? 29.996 3.740   -8.977  1.00 45.70  ? 149 LEU B N   1 
ATOM   3213 C CA  . LEU B 1 149 ? 31.317 3.074   -8.956  1.00 43.35  ? 149 LEU B CA  1 
ATOM   3214 C C   . LEU B 1 149 ? 31.766 2.853   -10.404 1.00 43.46  ? 149 LEU B C   1 
ATOM   3215 O O   . LEU B 1 149 ? 32.976 3.052   -10.691 1.00 39.91  ? 149 LEU B O   1 
ATOM   3216 C CB  . LEU B 1 149 ? 31.228 1.774   -8.147  1.00 46.38  ? 149 LEU B CB  1 
ATOM   3217 C CG  . LEU B 1 149 ? 32.550 1.233   -7.593  1.00 45.88  ? 149 LEU B CG  1 
ATOM   3218 C CD1 . LEU B 1 149 ? 33.191 2.209   -6.605  1.00 49.55  ? 149 LEU B CD1 1 
ATOM   3219 C CD2 . LEU B 1 149 ? 32.335 -0.106  -6.907  1.00 47.66  ? 149 LEU B CD2 1 
ATOM   3220 N N   . GLU B 1 150 ? 30.856 2.504   -11.316 1.00 42.07  ? 150 GLU B N   1 
ATOM   3221 C CA  . GLU B 1 150 ? 31.279 2.271   -12.724 1.00 42.33  ? 150 GLU B CA  1 
ATOM   3222 C C   . GLU B 1 150 ? 31.879 3.578   -13.250 1.00 45.28  ? 150 GLU B C   1 
ATOM   3223 O O   . GLU B 1 150 ? 32.991 3.554   -13.853 1.00 46.07  ? 150 GLU B O   1 
ATOM   3224 C CB  . GLU B 1 150 ? 30.142 1.775   -13.612 1.00 49.30  ? 150 GLU B CB  1 
ATOM   3225 C CG  . GLU B 1 150 ? 30.621 1.289   -14.978 1.00 53.21  ? 150 GLU B CG  1 
ATOM   3226 C CD  . GLU B 1 150 ? 30.943 2.395   -15.980 1.00 58.54  ? 150 GLU B CD  1 
ATOM   3227 O OE1 . GLU B 1 150 ? 30.255 3.464   -15.968 1.00 64.33  ? 150 GLU B OE1 1 
ATOM   3228 O OE2 . GLU B 1 150 ? 31.898 2.211   -16.751 1.00 56.68  ? 150 GLU B OE2 1 
ATOM   3229 N N   . HIS B 1 151 ? 31.204 4.694   -12.986 1.00 43.49  ? 151 HIS B N   1 
ATOM   3230 C CA  . HIS B 1 151 ? 31.687 6.039   -13.381 1.00 42.42  ? 151 HIS B CA  1 
ATOM   3231 C C   . HIS B 1 151 ? 33.109 6.249   -12.845 1.00 42.46  ? 151 HIS B C   1 
ATOM   3232 O O   . HIS B 1 151 ? 34.023 6.591   -13.639 1.00 45.84  ? 151 HIS B O   1 
ATOM   3233 C CB  . HIS B 1 151 ? 30.683 7.097   -12.929 1.00 47.79  ? 151 HIS B CB  1 
ATOM   3234 C CG  . HIS B 1 151 ? 31.114 8.445   -13.373 1.00 50.93  ? 151 HIS B CG  1 
ATOM   3235 N ND1 . HIS B 1 151 ? 31.291 8.733   -14.708 1.00 49.83  ? 151 HIS B ND1 1 
ATOM   3236 C CD2 . HIS B 1 151 ? 31.478 9.538   -12.674 1.00 52.19  ? 151 HIS B CD2 1 
ATOM   3237 C CE1 . HIS B 1 151 ? 31.716 9.963   -14.828 1.00 50.76  ? 151 HIS B CE1 1 
ATOM   3238 N NE2 . HIS B 1 151 ? 31.842 10.478  -13.591 1.00 61.89  ? 151 HIS B NE2 1 
ATOM   3239 N N   . MET B 1 152 ? 33.302 6.029   -11.544 1.00 42.26  ? 152 MET B N   1 
ATOM   3240 C CA  . MET B 1 152 ? 34.605 6.204   -10.848 1.00 40.82  ? 152 MET B CA  1 
ATOM   3241 C C   . MET B 1 152 ? 35.687 5.305   -11.477 1.00 39.92  ? 152 MET B C   1 
ATOM   3242 O O   . MET B 1 152 ? 36.767 5.834   -11.843 1.00 37.77  ? 152 MET B O   1 
ATOM   3243 C CB  . MET B 1 152 ? 34.452 5.886   -9.362  1.00 41.87  ? 152 MET B CB  1 
ATOM   3244 C CG  . MET B 1 152 ? 33.635 6.916   -8.631  1.00 42.51  ? 152 MET B CG  1 
ATOM   3245 S SD  . MET B 1 152 ? 33.478 6.651   -6.845  1.00 45.12  ? 152 MET B SD  1 
ATOM   3246 C CE  . MET B 1 152 ? 35.174 6.866   -6.317  1.00 43.11  ? 152 MET B CE  1 
ATOM   3247 N N   . HIS B 1 153 ? 35.446 4.000   -11.612 1.00 41.57  ? 153 HIS B N   1 
ATOM   3248 C CA  . HIS B 1 153 ? 36.474 3.043   -12.130 1.00 45.05  ? 153 HIS B CA  1 
ATOM   3249 C C   . HIS B 1 153 ? 36.822 3.360   -13.595 1.00 43.98  ? 153 HIS B C   1 
ATOM   3250 O O   . HIS B 1 153 ? 38.015 3.184   -13.974 1.00 42.49  ? 153 HIS B O   1 
ATOM   3251 C CB  . HIS B 1 153 ? 36.044 1.585   -11.936 1.00 42.38  ? 153 HIS B CB  1 
ATOM   3252 C CG  . HIS B 1 153 ? 36.072 1.123   -10.519 1.00 42.12  ? 153 HIS B CG  1 
ATOM   3253 N ND1 . HIS B 1 153 ? 35.810 -0.174  -10.169 1.00 44.54  ? 153 HIS B ND1 1 
ATOM   3254 C CD2 . HIS B 1 153 ? 36.299 1.784   -9.363  1.00 43.81  ? 153 HIS B CD2 1 
ATOM   3255 C CE1 . HIS B 1 153 ? 35.870 -0.294  -8.856  1.00 48.02  ? 153 HIS B CE1 1 
ATOM   3256 N NE2 . HIS B 1 153 ? 36.171 0.893   -8.341  1.00 43.26  ? 153 HIS B NE2 1 
ATOM   3257 N N   . SER B 1 154 ? 35.861 3.875   -14.365 1.00 44.81  ? 154 SER B N   1 
ATOM   3258 C CA  . SER B 1 154 ? 36.061 4.277   -15.787 1.00 50.32  ? 154 SER B CA  1 
ATOM   3259 C C   . SER B 1 154 ? 37.039 5.466   -15.876 1.00 52.66  ? 154 SER B C   1 
ATOM   3260 O O   . SER B 1 154 ? 37.639 5.626   -16.931 1.00 51.57  ? 154 SER B O   1 
ATOM   3261 C CB  . SER B 1 154 ? 34.759 4.601   -16.454 1.00 48.57  ? 154 SER B CB  1 
ATOM   3262 O OG  . SER B 1 154 ? 34.423 5.962   -16.218 1.00 55.48  ? 154 SER B OG  1 
ATOM   3263 N N   . ARG B 1 155 ? 37.195 6.275   -14.817 1.00 54.29  ? 155 ARG B N   1 
ATOM   3264 C CA  . ARG B 1 155 ? 38.176 7.395   -14.783 1.00 53.30  ? 155 ARG B CA  1 
ATOM   3265 C C   . ARG B 1 155 ? 39.393 6.988   -13.947 1.00 50.46  ? 155 ARG B C   1 
ATOM   3266 O O   . ARG B 1 155 ? 40.143 7.898   -13.532 1.00 48.08  ? 155 ARG B O   1 
ATOM   3267 C CB  . ARG B 1 155 ? 37.564 8.687   -14.221 1.00 57.88  ? 155 ARG B CB  1 
ATOM   3268 C CG  . ARG B 1 155 ? 36.246 9.116   -14.851 1.00 64.72  ? 155 ARG B CG  1 
ATOM   3269 C CD  . ARG B 1 155 ? 36.236 8.986   -16.353 1.00 77.13  ? 155 ARG B CD  1 
ATOM   3270 N NE  . ARG B 1 155 ? 35.017 9.492   -16.956 1.00 88.67  ? 155 ARG B NE  1 
ATOM   3271 C CZ  . ARG B 1 155 ? 34.769 10.776  -17.182 1.00 104.79 ? 155 ARG B CZ  1 
ATOM   3272 N NH1 . ARG B 1 155 ? 35.644 11.704  -16.825 1.00 111.28 ? 155 ARG B NH1 1 
ATOM   3273 N NH2 . ARG B 1 155 ? 33.633 11.132  -17.757 1.00 112.71 ? 155 ARG B NH2 1 
ATOM   3274 N N   . ARG B 1 156 ? 39.565 5.686   -13.690 1.00 54.13  ? 156 ARG B N   1 
ATOM   3275 C CA  . ARG B 1 156 ? 40.682 5.105   -12.889 1.00 57.65  ? 156 ARG B CA  1 
ATOM   3276 C C   . ARG B 1 156 ? 40.708 5.692   -11.469 1.00 55.12  ? 156 ARG B C   1 
ATOM   3277 O O   . ARG B 1 156 ? 41.817 5.995   -10.987 1.00 61.46  ? 156 ARG B O   1 
ATOM   3278 C CB  . ARG B 1 156 ? 42.023 5.341   -13.596 1.00 67.56  ? 156 ARG B CB  1 
ATOM   3279 C CG  . ARG B 1 156 ? 42.059 4.826   -15.029 1.00 77.91  ? 156 ARG B CG  1 
ATOM   3280 C CD  . ARG B 1 156 ? 43.440 4.442   -15.532 1.00 89.98  ? 156 ARG B CD  1 
ATOM   3281 N NE  . ARG B 1 156 ? 43.304 3.582   -16.703 1.00 109.13 ? 156 ARG B NE  1 
ATOM   3282 C CZ  . ARG B 1 156 ? 43.069 2.269   -16.675 1.00 126.24 ? 156 ARG B CZ  1 
ATOM   3283 N NH1 . ARG B 1 156 ? 42.952 1.600   -17.812 1.00 127.53 ? 156 ARG B NH1 1 
ATOM   3284 N NH2 . ARG B 1 156 ? 42.959 1.622   -15.523 1.00 129.09 ? 156 ARG B NH2 1 
ATOM   3285 N N   . VAL B 1 157 ? 39.552 5.815   -10.803 1.00 49.67  ? 157 VAL B N   1 
ATOM   3286 C CA  . VAL B 1 157 ? 39.474 6.297   -9.393  1.00 49.58  ? 157 VAL B CA  1 
ATOM   3287 C C   . VAL B 1 157 ? 38.913 5.189   -8.507  1.00 47.37  ? 157 VAL B C   1 
ATOM   3288 O O   . VAL B 1 157 ? 37.740 4.822   -8.740  1.00 44.03  ? 157 VAL B O   1 
ATOM   3289 C CB  . VAL B 1 157 ? 38.611 7.559   -9.248  1.00 51.61  ? 157 VAL B CB  1 
ATOM   3290 C CG1 . VAL B 1 157 ? 38.694 8.107   -7.836  1.00 50.13  ? 157 VAL B CG1 1 
ATOM   3291 C CG2 . VAL B 1 157 ? 38.975 8.619   -10.262 1.00 52.57  ? 157 VAL B CG2 1 
ATOM   3292 N N   . MET B 1 158 ? 39.692 4.720   -7.520  1.00 43.09  ? 158 MET B N   1 
ATOM   3293 C CA  . MET B 1 158 ? 39.190 3.790   -6.475  1.00 46.28  ? 158 MET B CA  1 
ATOM   3294 C C   . MET B 1 158 ? 38.443 4.605   -5.431  1.00 44.20  ? 158 MET B C   1 
ATOM   3295 O O   . MET B 1 158 ? 38.951 5.693   -5.052  1.00 46.04  ? 158 MET B O   1 
ATOM   3296 C CB  . MET B 1 158 ? 40.296 3.045   -5.727  1.00 49.55  ? 158 MET B CB  1 
ATOM   3297 C CG  . MET B 1 158 ? 41.215 2.253   -6.596  1.00 55.62  ? 158 MET B CG  1 
ATOM   3298 S SD  . MET B 1 158 ? 42.508 1.549   -5.564  1.00 56.77  ? 158 MET B SD  1 
ATOM   3299 C CE  . MET B 1 158 ? 43.879 1.629   -6.716  1.00 63.18  ? 158 MET B CE  1 
ATOM   3300 N N   . HIS B 1 159 ? 37.335 4.061   -4.929  1.00 43.85  ? 159 HIS B N   1 
ATOM   3301 C CA  . HIS B 1 159 ? 36.578 4.662   -3.805  1.00 43.53  ? 159 HIS B CA  1 
ATOM   3302 C C   . HIS B 1 159 ? 37.315 4.475   -2.471  1.00 44.63  ? 159 HIS B C   1 
ATOM   3303 O O   . HIS B 1 159 ? 37.463 5.464   -1.771  1.00 46.36  ? 159 HIS B O   1 
ATOM   3304 C CB  . HIS B 1 159 ? 35.154 4.138   -3.720  1.00 42.88  ? 159 HIS B CB  1 
ATOM   3305 C CG  . HIS B 1 159 ? 34.372 4.962   -2.761  1.00 44.62  ? 159 HIS B CG  1 
ATOM   3306 N ND1 . HIS B 1 159 ? 34.478 4.792   -1.405  1.00 41.86  ? 159 HIS B ND1 1 
ATOM   3307 C CD2 . HIS B 1 159 ? 33.554 6.017   -2.957  1.00 44.27  ? 159 HIS B CD2 1 
ATOM   3308 C CE1 . HIS B 1 159 ? 33.695 5.664   -0.802  1.00 44.81  ? 159 HIS B CE1 1 
ATOM   3309 N NE2 . HIS B 1 159 ? 33.108 6.415   -1.730  1.00 41.21  ? 159 HIS B NE2 1 
ATOM   3310 N N   . ARG B 1 160 ? 37.729 3.260   -2.121  1.00 46.67  ? 160 ARG B N   1 
ATOM   3311 C CA  . ARG B 1 160 ? 38.593 2.979   -0.935  1.00 52.13  ? 160 ARG B CA  1 
ATOM   3312 C C   . ARG B 1 160 ? 37.833 2.917   0.403   1.00 52.22  ? 160 ARG B C   1 
ATOM   3313 O O   . ARG B 1 160 ? 38.400 2.361   1.340   1.00 51.17  ? 160 ARG B O   1 
ATOM   3314 C CB  . ARG B 1 160 ? 39.703 4.019   -0.820  1.00 57.85  ? 160 ARG B CB  1 
ATOM   3315 C CG  . ARG B 1 160 ? 40.765 3.899   -1.898  1.00 66.81  ? 160 ARG B CG  1 
ATOM   3316 C CD  . ARG B 1 160 ? 41.928 4.793   -1.528  1.00 74.42  ? 160 ARG B CD  1 
ATOM   3317 N NE  . ARG B 1 160 ? 42.520 5.368   -2.722  1.00 75.69  ? 160 ARG B NE  1 
ATOM   3318 C CZ  . ARG B 1 160 ? 43.595 4.900   -3.331  1.00 76.00  ? 160 ARG B CZ  1 
ATOM   3319 N NH1 . ARG B 1 160 ? 44.226 3.834   -2.858  1.00 74.03  ? 160 ARG B NH1 1 
ATOM   3320 N NH2 . ARG B 1 160 ? 44.031 5.510   -4.419  1.00 75.23  ? 160 ARG B NH2 1 
ATOM   3321 N N   . ASN B 1 161 ? 36.609 3.430   0.541   1.00 54.17  ? 161 ASN B N   1 
ATOM   3322 C CA  A ASN B 1 161 ? 35.841 3.253   1.809   0.50 53.20  ? 161 ASN B CA  1 
ATOM   3323 C CA  B ASN B 1 161 ? 35.840 3.300   1.806   0.50 55.82  ? 161 ASN B CA  1 
ATOM   3324 C C   . ASN B 1 161 ? 34.341 3.201   1.491   1.00 51.37  ? 161 ASN B C   1 
ATOM   3325 O O   . ASN B 1 161 ? 33.609 4.147   1.817   1.00 51.43  ? 161 ASN B O   1 
ATOM   3326 C CB  A ASN B 1 161 ? 36.237 4.309   2.850   0.50 56.74  ? 161 ASN B CB  1 
ATOM   3327 C CB  B ASN B 1 161 ? 36.225 4.406   2.802   0.50 62.82  ? 161 ASN B CB  1 
ATOM   3328 C CG  A ASN B 1 161 ? 35.929 3.935   4.291   0.50 52.85  ? 161 ASN B CG  1 
ATOM   3329 C CG  B ASN B 1 161 ? 36.243 5.819   2.248   0.50 63.31  ? 161 ASN B CG  1 
ATOM   3330 O OD1 A ASN B 1 161 ? 35.768 2.763   4.646   0.50 45.50  ? 161 ASN B OD1 1 
ATOM   3331 O OD1 B ASN B 1 161 ? 36.839 6.105   1.204   0.50 57.33  ? 161 ASN B OD1 1 
ATOM   3332 N ND2 A ASN B 1 161 ? 35.862 4.950   5.135   0.50 51.15  ? 161 ASN B ND2 1 
ATOM   3333 N ND2 B ASN B 1 161 ? 35.648 6.734   3.000   0.50 65.59  ? 161 ASN B ND2 1 
ATOM   3334 N N   . ILE B 1 162 ? 33.914 2.095   0.876   1.00 49.99  ? 162 ILE B N   1 
ATOM   3335 C CA  . ILE B 1 162 ? 32.479 1.798   0.602   1.00 45.36  ? 162 ILE B CA  1 
ATOM   3336 C C   . ILE B 1 162 ? 31.934 1.189   1.892   1.00 43.24  ? 162 ILE B C   1 
ATOM   3337 O O   . ILE B 1 162 ? 32.502 0.201   2.344   1.00 44.05  ? 162 ILE B O   1 
ATOM   3338 C CB  . ILE B 1 162 ? 32.310 0.901   -0.646  1.00 44.46  ? 162 ILE B CB  1 
ATOM   3339 C CG1 . ILE B 1 162 ? 32.764 1.638   -1.908  1.00 43.32  ? 162 ILE B CG1 1 
ATOM   3340 C CG2 . ILE B 1 162 ? 30.888 0.375   -0.810  1.00 43.63  ? 162 ILE B CG2 1 
ATOM   3341 C CD1 . ILE B 1 162 ? 32.878 0.753   -3.115  1.00 43.55  ? 162 ILE B CD1 1 
ATOM   3342 N N   . LYS B 1 163 ? 30.929 1.826   2.486   1.00 46.19  ? 163 LYS B N   1 
ATOM   3343 C CA  . LYS B 1 163 ? 30.256 1.397   3.744   1.00 52.39  ? 163 LYS B CA  1 
ATOM   3344 C C   . LYS B 1 163 ? 28.918 2.130   3.864   1.00 50.42  ? 163 LYS B C   1 
ATOM   3345 O O   . LYS B 1 163 ? 28.729 3.186   3.254   1.00 48.49  ? 163 LYS B O   1 
ATOM   3346 C CB  . LYS B 1 163 ? 31.170 1.659   4.942   1.00 54.59  ? 163 LYS B CB  1 
ATOM   3347 C CG  . LYS B 1 163 ? 31.587 3.111   5.141   1.00 61.08  ? 163 LYS B CG  1 
ATOM   3348 C CD  . LYS B 1 163 ? 32.496 3.326   6.331   1.00 61.09  ? 163 LYS B CD  1 
ATOM   3349 C CE  . LYS B 1 163 ? 32.567 4.776   6.760   1.00 66.48  ? 163 LYS B CE  1 
ATOM   3350 N NZ  . LYS B 1 163 ? 33.787 5.079   7.550   1.00 68.37  ? 163 LYS B NZ  1 
ATOM   3351 N N   . PRO B 1 164 ? 27.948 1.596   4.638   1.00 51.99  ? 164 PRO B N   1 
ATOM   3352 C CA  . PRO B 1 164 ? 26.625 2.219   4.743   1.00 53.23  ? 164 PRO B CA  1 
ATOM   3353 C C   . PRO B 1 164 ? 26.679 3.704   5.143   1.00 48.65  ? 164 PRO B C   1 
ATOM   3354 O O   . PRO B 1 164 ? 25.953 4.470   4.580   1.00 47.14  ? 164 PRO B O   1 
ATOM   3355 C CB  . PRO B 1 164 ? 25.901 1.364   5.797   1.00 52.19  ? 164 PRO B CB  1 
ATOM   3356 C CG  . PRO B 1 164 ? 26.596 0.004   5.712   1.00 52.84  ? 164 PRO B CG  1 
ATOM   3357 C CD  . PRO B 1 164 ? 28.044 0.342   5.411   1.00 56.37  ? 164 PRO B CD  1 
ATOM   3358 N N   . ALA B 1 165 ? 27.575 4.085   6.045   1.00 46.28  ? 165 ALA B N   1 
ATOM   3359 C CA  . ALA B 1 165 ? 27.739 5.490   6.484   1.00 52.63  ? 165 ALA B CA  1 
ATOM   3360 C C   . ALA B 1 165 ? 28.125 6.428   5.331   1.00 52.55  ? 165 ALA B C   1 
ATOM   3361 O O   . ALA B 1 165 ? 27.956 7.645   5.491   1.00 57.52  ? 165 ALA B O   1 
ATOM   3362 C CB  . ALA B 1 165 ? 28.755 5.557   7.586   1.00 54.63  ? 165 ALA B CB  1 
ATOM   3363 N N   . ASN B 1 166 ? 28.613 5.919   4.199   1.00 54.44  ? 166 ASN B N   1 
ATOM   3364 C CA  . ASN B 1 166 ? 29.085 6.782   3.079   1.00 49.87  ? 166 ASN B CA  1 
ATOM   3365 C C   . ASN B 1 166 ? 28.078 6.760   1.944   1.00 49.06  ? 166 ASN B C   1 
ATOM   3366 O O   . ASN B 1 166 ? 28.417 7.263   0.869   1.00 55.15  ? 166 ASN B O   1 
ATOM   3367 C CB  . ASN B 1 166 ? 30.434 6.334   2.520   1.00 54.12  ? 166 ASN B CB  1 
ATOM   3368 C CG  . ASN B 1 166 ? 31.602 6.910   3.281   1.00 51.69  ? 166 ASN B CG  1 
ATOM   3369 O OD1 . ASN B 1 166 ? 31.537 8.037   3.719   1.00 63.16  ? 166 ASN B OD1 1 
ATOM   3370 N ND2 . ASN B 1 166 ? 32.677 6.161   3.420   1.00 60.38  ? 166 ASN B ND2 1 
ATOM   3371 N N   . VAL B 1 167 ? 26.913 6.157   2.152   1.00 50.59  ? 167 VAL B N   1 
ATOM   3372 C CA  . VAL B 1 167 ? 25.853 6.045   1.104   1.00 56.29  ? 167 VAL B CA  1 
ATOM   3373 C C   . VAL B 1 167 ? 24.657 6.882   1.556   1.00 55.87  ? 167 VAL B C   1 
ATOM   3374 O O   . VAL B 1 167 ? 24.124 6.592   2.624   1.00 55.01  ? 167 VAL B O   1 
ATOM   3375 C CB  . VAL B 1 167 ? 25.456 4.582   0.853   1.00 57.59  ? 167 VAL B CB  1 
ATOM   3376 C CG1 . VAL B 1 167 ? 24.302 4.470   -0.134  1.00 62.68  ? 167 VAL B CG1 1 
ATOM   3377 C CG2 . VAL B 1 167 ? 26.647 3.773   0.374   1.00 61.70  ? 167 VAL B CG2 1 
ATOM   3378 N N   . PHE B 1 168 ? 24.284 7.901   0.781   1.00 57.92  ? 168 PHE B N   1 
ATOM   3379 C CA  . PHE B 1 168 ? 23.220 8.865   1.144   1.00 55.11  ? 168 PHE B CA  1 
ATOM   3380 C C   . PHE B 1 168 ? 22.046 8.648   0.198   1.00 58.84  ? 168 PHE B C   1 
ATOM   3381 O O   . PHE B 1 168 ? 22.251 8.332   -1.002  1.00 55.21  ? 168 PHE B O   1 
ATOM   3382 C CB  . PHE B 1 168 ? 23.792 10.276  1.162   1.00 53.46  ? 168 PHE B CB  1 
ATOM   3383 C CG  . PHE B 1 168 ? 24.990 10.420  2.065   1.00 52.86  ? 168 PHE B CG  1 
ATOM   3384 C CD1 . PHE B 1 168 ? 24.833 10.600  3.426   1.00 49.66  ? 168 PHE B CD1 1 
ATOM   3385 C CD2 . PHE B 1 168 ? 26.281 10.369  1.547   1.00 60.97  ? 168 PHE B CD2 1 
ATOM   3386 C CE1 . PHE B 1 168 ? 25.944 10.754  4.245   1.00 56.67  ? 168 PHE B CE1 1 
ATOM   3387 C CE2 . PHE B 1 168 ? 27.391 10.528  2.368   1.00 57.13  ? 168 PHE B CE2 1 
ATOM   3388 C CZ  . PHE B 1 168 ? 27.221 10.706  3.720   1.00 52.72  ? 168 PHE B CZ  1 
ATOM   3389 N N   . ILE B 1 169 ? 20.843 8.704   0.768   1.00 65.66  ? 169 ILE B N   1 
ATOM   3390 C CA  . ILE B 1 169 ? 19.570 8.473   0.025   1.00 75.92  ? 169 ILE B CA  1 
ATOM   3391 C C   . ILE B 1 169 ? 18.707 9.716   0.230   1.00 70.65  ? 169 ILE B C   1 
ATOM   3392 O O   . ILE B 1 169 ? 18.573 10.163  1.393   1.00 71.56  ? 169 ILE B O   1 
ATOM   3393 C CB  . ILE B 1 169 ? 18.875 7.157   0.454   1.00 77.82  ? 169 ILE B CB  1 
ATOM   3394 C CG1 . ILE B 1 169 ? 19.853 5.975   0.472   1.00 78.41  ? 169 ILE B CG1 1 
ATOM   3395 C CG2 . ILE B 1 169 ? 17.678 6.859   -0.442  1.00 75.63  ? 169 ILE B CG2 1 
ATOM   3396 C CD1 . ILE B 1 169 ? 19.279 4.701   1.037   1.00 77.16  ? 169 ILE B CD1 1 
ATOM   3397 N N   . THR B 1 170 ? 18.201 10.274  -0.868  1.00 70.82  ? 170 THR B N   1 
ATOM   3398 C CA  . THR B 1 170 ? 17.407 11.528  -0.875  1.00 78.68  ? 170 THR B CA  1 
ATOM   3399 C C   . THR B 1 170 ? 15.964 11.227  -0.456  1.00 75.49  ? 170 THR B C   1 
ATOM   3400 O O   . THR B 1 170 ? 15.599 10.031  -0.332  1.00 64.85  ? 170 THR B O   1 
ATOM   3401 C CB  . THR B 1 170 ? 17.457 12.191  -2.256  1.00 75.40  ? 170 THR B CB  1 
ATOM   3402 O OG1 . THR B 1 170 ? 16.962 11.194  -3.145  1.00 72.63  ? 170 THR B OG1 1 
ATOM   3403 C CG2 . THR B 1 170 ? 18.841 12.652  -2.661  1.00 72.39  ? 170 THR B CG2 1 
ATOM   3404 N N   . ALA B 1 171 ? 15.200 12.292  -0.213  1.00 86.89  ? 171 ALA B N   1 
ATOM   3405 C CA  . ALA B 1 171 ? 13.721 12.316  -0.240  1.00 91.25  ? 171 ALA B CA  1 
ATOM   3406 C C   . ALA B 1 171 ? 13.223 11.308  -1.286  1.00 92.84  ? 171 ALA B C   1 
ATOM   3407 O O   . ALA B 1 171 ? 12.584 10.308  -0.887  1.00 78.94  ? 171 ALA B O   1 
ATOM   3408 C CB  . ALA B 1 171 ? 13.266 13.723  -0.563  1.00 93.37  ? 171 ALA B CB  1 
ATOM   3409 N N   . THR B 1 172 ? 13.589 11.539  -2.558  1.00 93.83  ? 172 THR B N   1 
ATOM   3410 C CA  . THR B 1 172 ? 13.039 10.888  -3.783  1.00 94.72  ? 172 THR B CA  1 
ATOM   3411 C C   . THR B 1 172 ? 13.646 9.493   -4.026  1.00 91.05  ? 172 THR B C   1 
ATOM   3412 O O   . THR B 1 172 ? 13.223 8.835   -5.005  1.00 87.04  ? 172 THR B O   1 
ATOM   3413 C CB  . THR B 1 172 ? 13.265 11.774  -5.020  1.00 96.17  ? 172 THR B CB  1 
ATOM   3414 O OG1 . THR B 1 172 ? 14.643 12.138  -5.114  1.00 93.91  ? 172 THR B OG1 1 
ATOM   3415 C CG2 . THR B 1 172 ? 12.460 13.053  -4.989  1.00 95.09  ? 172 THR B CG2 1 
ATOM   3416 N N   . GLY B 1 173 ? 14.612 9.059   -3.210  1.00 82.24  ? 173 GLY B N   1 
ATOM   3417 C CA  . GLY B 1 173 ? 15.269 7.744   -3.352  1.00 74.36  ? 173 GLY B CA  1 
ATOM   3418 C C   . GLY B 1 173 ? 16.411 7.736   -4.369  1.00 71.13  ? 173 GLY B C   1 
ATOM   3419 O O   . GLY B 1 173 ? 16.738 6.639   -4.887  1.00 62.71  ? 173 GLY B O   1 
ATOM   3420 N N   . VAL B 1 174 ? 17.054 8.876   -4.646  1.00 68.44  ? 174 VAL B N   1 
ATOM   3421 C CA  . VAL B 1 174 ? 18.313 8.866   -5.452  1.00 66.71  ? 174 VAL B CA  1 
ATOM   3422 C C   . VAL B 1 174 ? 19.489 8.698   -4.480  1.00 59.93  ? 174 VAL B C   1 
ATOM   3423 O O   . VAL B 1 174 ? 19.515 9.335   -3.407  1.00 53.75  ? 174 VAL B O   1 
ATOM   3424 C CB  . VAL B 1 174 ? 18.470 10.060  -6.426  1.00 71.33  ? 174 VAL B CB  1 
ATOM   3425 C CG1 . VAL B 1 174 ? 17.151 10.425  -7.109  1.00 71.00  ? 174 VAL B CG1 1 
ATOM   3426 C CG2 . VAL B 1 174 ? 19.092 11.285  -5.781  1.00 75.85  ? 174 VAL B CG2 1 
ATOM   3427 N N   . VAL B 1 175 ? 20.413 7.815   -4.843  1.00 58.71  ? 175 VAL B N   1 
ATOM   3428 C CA  . VAL B 1 175 ? 21.589 7.439   -4.015  1.00 64.62  ? 175 VAL B CA  1 
ATOM   3429 C C   . VAL B 1 175 ? 22.753 8.358   -4.381  1.00 61.94  ? 175 VAL B C   1 
ATOM   3430 O O   . VAL B 1 175 ? 22.915 8.606   -5.592  1.00 61.21  ? 175 VAL B O   1 
ATOM   3431 C CB  . VAL B 1 175 ? 21.936 5.962   -4.249  1.00 65.83  ? 175 VAL B CB  1 
ATOM   3432 C CG1 . VAL B 1 175 ? 23.211 5.559   -3.529  1.00 69.76  ? 175 VAL B CG1 1 
ATOM   3433 C CG2 . VAL B 1 175 ? 20.766 5.075   -3.849  1.00 72.40  ? 175 VAL B CG2 1 
ATOM   3434 N N   . LYS B 1 176 ? 23.492 8.836   -3.369  1.00 55.16  ? 176 LYS B N   1 
ATOM   3435 C CA  . LYS B 1 176 ? 24.745 9.625   -3.500  1.00 61.08  ? 176 LYS B CA  1 
ATOM   3436 C C   . LYS B 1 176 ? 25.849 8.916   -2.707  1.00 54.83  ? 176 LYS B C   1 
ATOM   3437 O O   . LYS B 1 176 ? 25.749 8.876   -1.455  1.00 43.73  ? 176 LYS B O   1 
ATOM   3438 C CB  . LYS B 1 176 ? 24.601 11.054  -2.960  1.00 69.48  ? 176 LYS B CB  1 
ATOM   3439 C CG  . LYS B 1 176 ? 23.460 11.891  -3.524  1.00 75.71  ? 176 LYS B CG  1 
ATOM   3440 C CD  . LYS B 1 176 ? 23.615 12.273  -4.976  1.00 79.65  ? 176 LYS B CD  1 
ATOM   3441 C CE  . LYS B 1 176 ? 24.086 13.696  -5.177  1.00 82.78  ? 176 LYS B CE  1 
ATOM   3442 N NZ  . LYS B 1 176 ? 23.006 14.687  -4.955  1.00 81.81  ? 176 LYS B NZ  1 
ATOM   3443 N N   . LEU B 1 177 ? 26.899 8.448   -3.394  1.00 46.83  ? 177 LEU B N   1 
ATOM   3444 C CA  . LEU B 1 177 ? 28.092 7.844   -2.738  1.00 44.64  ? 177 LEU B CA  1 
ATOM   3445 C C   . LEU B 1 177 ? 29.138 8.931   -2.458  1.00 41.97  ? 177 LEU B C   1 
ATOM   3446 O O   . LEU B 1 177 ? 29.530 9.621   -3.405  1.00 43.47  ? 177 LEU B O   1 
ATOM   3447 C CB  . LEU B 1 177 ? 28.621 6.731   -3.645  1.00 44.60  ? 177 LEU B CB  1 
ATOM   3448 C CG  . LEU B 1 177 ? 29.945 6.085   -3.245  1.00 46.58  ? 177 LEU B CG  1 
ATOM   3449 C CD1 . LEU B 1 177 ? 29.842 5.354   -1.924  1.00 43.90  ? 177 LEU B CD1 1 
ATOM   3450 C CD2 . LEU B 1 177 ? 30.403 5.135   -4.348  1.00 51.70  ? 177 LEU B CD2 1 
ATOM   3451 N N   . GLY B 1 178 ? 29.571 9.056   -1.198  1.00 38.67  ? 178 GLY B N   1 
ATOM   3452 C CA  . GLY B 1 178 ? 30.577 10.027  -0.725  1.00 41.51  ? 178 GLY B CA  1 
ATOM   3453 C C   . GLY B 1 178 ? 31.737 9.312   -0.078  1.00 41.06  ? 178 GLY B C   1 
ATOM   3454 O O   . GLY B 1 178 ? 31.678 8.079   -0.071  1.00 48.66  ? 178 GLY B O   1 
ATOM   3455 N N   . ASP B 1 179 ? 32.746 10.016  0.452   1.00 45.43  ? 179 ASP B N   1 
ATOM   3456 C CA  . ASP B 1 179 ? 33.851 9.352   1.212   1.00 58.98  ? 179 ASP B CA  1 
ATOM   3457 C C   . ASP B 1 179 ? 34.117 10.032  2.560   1.00 60.29  ? 179 ASP B C   1 
ATOM   3458 O O   . ASP B 1 179 ? 35.173 9.740   3.157   1.00 68.13  ? 179 ASP B O   1 
ATOM   3459 C CB  . ASP B 1 179 ? 35.150 9.251   0.403   1.00 60.16  ? 179 ASP B CB  1 
ATOM   3460 C CG  . ASP B 1 179 ? 35.564 10.531  -0.295  1.00 67.62  ? 179 ASP B CG  1 
ATOM   3461 O OD1 . ASP B 1 179 ? 34.981 11.614  0.033   1.00 65.00  ? 179 ASP B OD1 1 
ATOM   3462 O OD2 . ASP B 1 179 ? 36.461 10.430  -1.172  1.00 70.05  ? 179 ASP B OD2 1 
ATOM   3463 N N   . LEU B 1 180 ? 33.175 10.842  3.041   1.00 66.42  ? 180 LEU B N   1 
ATOM   3464 C CA  . LEU B 1 180 ? 33.299 11.715  4.244   1.00 71.35  ? 180 LEU B CA  1 
ATOM   3465 C C   . LEU B 1 180 ? 32.432 11.200  5.400   1.00 70.71  ? 180 LEU B C   1 
ATOM   3466 O O   . LEU B 1 180 ? 32.783 11.492  6.559   1.00 75.75  ? 180 LEU B O   1 
ATOM   3467 C CB  . LEU B 1 180 ? 32.875 13.138  3.864   1.00 73.62  ? 180 LEU B CB  1 
ATOM   3468 C CG  . LEU B 1 180 ? 33.966 14.203  3.943   1.00 79.39  ? 180 LEU B CG  1 
ATOM   3469 C CD1 . LEU B 1 180 ? 35.176 13.827  3.091   1.00 83.14  ? 180 LEU B CD1 1 
ATOM   3470 C CD2 . LEU B 1 180 ? 33.404 15.557  3.528   1.00 84.29  ? 180 LEU B CD2 1 
ATOM   3471 N N   . GLY B 1 181 ? 31.310 10.537  5.104   1.00 67.18  ? 181 GLY B N   1 
ATOM   3472 C CA  . GLY B 1 181 ? 30.378 10.009  6.115   1.00 66.17  ? 181 GLY B CA  1 
ATOM   3473 C C   . GLY B 1 181 ? 29.558 11.116  6.754   1.00 70.84  ? 181 GLY B C   1 
ATOM   3474 O O   . GLY B 1 181 ? 29.080 10.898  7.889   1.00 71.42  ? 181 GLY B O   1 
ATOM   3475 N N   . LEU B 1 182 ? 29.372 12.236  6.037   1.00 69.57  ? 182 LEU B N   1 
ATOM   3476 C CA  . LEU B 1 182 ? 28.716 13.475  6.533   1.00 76.05  ? 182 LEU B CA  1 
ATOM   3477 C C   . LEU B 1 182 ? 27.622 13.900  5.549   1.00 76.05  ? 182 LEU B C   1 
ATOM   3478 O O   . LEU B 1 182 ? 27.961 14.249  4.400   1.00 75.70  ? 182 LEU B O   1 
ATOM   3479 C CB  . LEU B 1 182 ? 29.758 14.594  6.665   1.00 79.19  ? 182 LEU B CB  1 
ATOM   3480 C CG  . LEU B 1 182 ? 30.980 14.283  7.526   1.00 82.37  ? 182 LEU B CG  1 
ATOM   3481 C CD1 . LEU B 1 182 ? 32.020 15.381  7.374   1.00 88.51  ? 182 LEU B CD1 1 
ATOM   3482 C CD2 . LEU B 1 182 ? 30.604 14.095  8.989   1.00 80.12  ? 182 LEU B CD2 1 
ATOM   3483 N N   . GLY B 1 183 ? 26.364 13.905  5.993   1.00 70.21  ? 183 GLY B N   1 
ATOM   3484 C CA  . GLY B 1 183 ? 25.265 14.544  5.249   1.00 71.48  ? 183 GLY B CA  1 
ATOM   3485 C C   . GLY B 1 183 ? 25.120 15.997  5.661   1.00 64.05  ? 183 GLY B C   1 
ATOM   3486 O O   . GLY B 1 183 ? 25.758 16.411  6.664   1.00 56.46  ? 183 GLY B O   1 
ATOM   3487 N N   . ARG B 1 184 ? 24.277 16.739  4.948   1.00 59.94  ? 184 ARG B N   1 
ATOM   3488 C CA  . ARG B 1 184 ? 23.917 18.131  5.316   1.00 64.36  ? 184 ARG B CA  1 
ATOM   3489 C C   . ARG B 1 184 ? 23.470 18.188  6.784   1.00 67.03  ? 184 ARG B C   1 
ATOM   3490 O O   . ARG B 1 184 ? 23.945 19.107  7.477   1.00 63.47  ? 184 ARG B O   1 
ATOM   3491 C CB  . ARG B 1 184 ? 22.821 18.666  4.396   1.00 63.28  ? 184 ARG B CB  1 
ATOM   3492 C CG  . ARG B 1 184 ? 22.554 20.157  4.548   1.00 68.72  ? 184 ARG B CG  1 
ATOM   3493 C CD  . ARG B 1 184 ? 21.732 20.673  3.384   1.00 73.06  ? 184 ARG B CD  1 
ATOM   3494 N NE  . ARG B 1 184 ? 22.499 20.532  2.153   1.00 81.84  ? 184 ARG B NE  1 
ATOM   3495 C CZ  . ARG B 1 184 ? 22.123 20.968  0.955   1.00 82.87  ? 184 ARG B CZ  1 
ATOM   3496 N NH1 . ARG B 1 184 ? 22.932 20.801  -0.080  1.00 80.11  ? 184 ARG B NH1 1 
ATOM   3497 N NH2 . ARG B 1 184 ? 20.952 21.564  0.797   1.00 77.77  ? 184 ARG B NH2 1 
ATOM   3498 N N   . PHE B 1 185 ? 22.611 17.258  7.244   1.00 68.86  ? 185 PHE B N   1 
ATOM   3499 C CA  . PHE B 1 185 ? 21.894 17.364  8.554   1.00 73.43  ? 185 PHE B CA  1 
ATOM   3500 C C   . PHE B 1 185 ? 22.353 16.276  9.536   1.00 69.74  ? 185 PHE B C   1 
ATOM   3501 O O   . PHE B 1 185 ? 22.667 16.646  10.683  1.00 75.46  ? 185 PHE B O   1 
ATOM   3502 C CB  . PHE B 1 185 ? 20.377 17.456  8.340   1.00 66.42  ? 185 PHE B CB  1 
ATOM   3503 C CG  . PHE B 1 185 ? 19.991 18.678  7.543   1.00 65.59  ? 185 PHE B CG  1 
ATOM   3504 C CD1 . PHE B 1 185 ? 20.361 19.952  7.970   1.00 65.39  ? 185 PHE B CD1 1 
ATOM   3505 C CD2 . PHE B 1 185 ? 19.332 18.558  6.329   1.00 62.42  ? 185 PHE B CD2 1 
ATOM   3506 C CE1 . PHE B 1 185 ? 20.061 21.078  7.212   1.00 66.49  ? 185 PHE B CE1 1 
ATOM   3507 C CE2 . PHE B 1 185 ? 19.026 19.686  5.576   1.00 65.13  ? 185 PHE B CE2 1 
ATOM   3508 C CZ  . PHE B 1 185 ? 19.389 20.942  6.016   1.00 65.81  ? 185 PHE B CZ  1 
ATOM   3509 N N   . PHE B 1 186 ? 22.431 15.014  9.109   1.00 75.09  ? 186 PHE B N   1 
ATOM   3510 C CA  . PHE B 1 186 ? 22.880 13.867  9.947   1.00 81.34  ? 186 PHE B CA  1 
ATOM   3511 C C   . PHE B 1 186 ? 24.194 13.289  9.397   1.00 85.47  ? 186 PHE B C   1 
ATOM   3512 O O   . PHE B 1 186 ? 24.375 13.212  8.148   1.00 91.49  ? 186 PHE B O   1 
ATOM   3513 C CB  . PHE B 1 186 ? 21.794 12.785  10.053  1.00 77.48  ? 186 PHE B CB  1 
ATOM   3514 C CG  . PHE B 1 186 ? 20.387 13.314  10.201  1.00 81.21  ? 186 PHE B CG  1 
ATOM   3515 C CD1 . PHE B 1 186 ? 19.913 13.725  11.437  1.00 76.20  ? 186 PHE B CD1 1 
ATOM   3516 C CD2 . PHE B 1 186 ? 19.545 13.424  9.100   1.00 81.25  ? 186 PHE B CD2 1 
ATOM   3517 C CE1 . PHE B 1 186 ? 18.628 14.224  11.567  1.00 73.97  ? 186 PHE B CE1 1 
ATOM   3518 C CE2 . PHE B 1 186 ? 18.264 13.932  9.235   1.00 77.09  ? 186 PHE B CE2 1 
ATOM   3519 C CZ  . PHE B 1 186 ? 17.812 14.332  10.468  1.00 77.75  ? 186 PHE B CZ  1 
ATOM   3520 N N   . SER B 1 187 ? 25.076 12.904  10.332  1.00 92.89  ? 187 SER B N   1 
ATOM   3521 C CA  . SER B 1 187 ? 26.231 11.983  10.156  1.00 89.51  ? 187 SER B CA  1 
ATOM   3522 C C   . SER B 1 187 ? 26.051 10.760  11.067  1.00 75.73  ? 187 SER B C   1 
ATOM   3523 O O   . SER B 1 187 ? 26.833 9.799   10.911  1.00 86.99  ? 187 SER B O   1 
ATOM   3524 C CB  . SER B 1 187 ? 27.520 12.690  10.452  1.00 94.17  ? 187 SER B CB  1 
ATOM   3525 O OG  . SER B 1 187 ? 27.851 12.578  11.831  1.00 97.01  ? 187 SER B OG  1 
ATOM   3526 N N   . THR B 1 199 ? 40.919 0.204   11.969  1.00 126.82 ? 199 THR B N   1 
ATOM   3527 C CA  . THR B 1 199 ? 40.440 -0.942  11.145  1.00 126.50 ? 199 THR B CA  1 
ATOM   3528 C C   . THR B 1 199 ? 39.233 -0.510  10.306  1.00 120.80 ? 199 THR B C   1 
ATOM   3529 O O   . THR B 1 199 ? 38.134 -0.381  10.848  1.00 97.05  ? 199 THR B O   1 
ATOM   3530 C CB  . THR B 1 199 ? 40.107 -2.152  12.032  1.00 117.11 ? 199 THR B CB  1 
ATOM   3531 N N   . PRO B 1 200 ? 39.383 -0.299  8.967   1.00 120.90 ? 200 PRO B N   1 
ATOM   3532 C CA  . PRO B 1 200 ? 38.273 0.144   8.113   1.00 107.94 ? 200 PRO B CA  1 
ATOM   3533 C C   . PRO B 1 200 ? 37.095 -0.844  8.126   1.00 92.01  ? 200 PRO B C   1 
ATOM   3534 O O   . PRO B 1 200 ? 37.270 -1.973  8.548   1.00 90.55  ? 200 PRO B O   1 
ATOM   3535 C CB  . PRO B 1 200 ? 38.873 0.276   6.702   1.00 108.34 ? 200 PRO B CB  1 
ATOM   3536 C CG  . PRO B 1 200 ? 40.142 -0.553  6.748   1.00 115.06 ? 200 PRO B CG  1 
ATOM   3537 C CD  . PRO B 1 200 ? 40.620 -0.494  8.188   1.00 118.49 ? 200 PRO B CD  1 
ATOM   3538 N N   . TYR B 1 201 ? 35.919 -0.388  7.690   1.00 74.49  ? 201 TYR B N   1 
ATOM   3539 C CA  . TYR B 1 201 ? 34.606 -0.991  8.046   1.00 70.09  ? 201 TYR B CA  1 
ATOM   3540 C C   . TYR B 1 201 ? 34.520 -2.426  7.498   1.00 68.22  ? 201 TYR B C   1 
ATOM   3541 O O   . TYR B 1 201 ? 34.334 -3.355  8.290   1.00 68.61  ? 201 TYR B O   1 
ATOM   3542 C CB  . TYR B 1 201 ? 33.459 -0.093  7.575   1.00 67.06  ? 201 TYR B CB  1 
ATOM   3543 C CG  . TYR B 1 201 ? 32.094 -0.481  8.092   1.00 61.50  ? 201 TYR B CG  1 
ATOM   3544 C CD1 . TYR B 1 201 ? 31.627 -0.022  9.315   1.00 59.00  ? 201 TYR B CD1 1 
ATOM   3545 C CD2 . TYR B 1 201 ? 31.274 -1.319  7.353   1.00 56.06  ? 201 TYR B CD2 1 
ATOM   3546 C CE1 . TYR B 1 201 ? 30.374 -0.386  9.792   1.00 61.04  ? 201 TYR B CE1 1 
ATOM   3547 C CE2 . TYR B 1 201 ? 30.017 -1.680  7.805   1.00 59.90  ? 201 TYR B CE2 1 
ATOM   3548 C CZ  . TYR B 1 201 ? 29.563 -1.213  9.029   1.00 64.50  ? 201 TYR B CZ  1 
ATOM   3549 O OH  . TYR B 1 201 ? 28.321 -1.583  9.464   1.00 63.39  ? 201 TYR B OH  1 
ATOM   3550 N N   . TYR B 1 202 ? 34.656 -2.613  6.185   1.00 59.43  ? 202 TYR B N   1 
ATOM   3551 C CA  . TYR B 1 202 ? 34.770 -3.957  5.563   1.00 55.56  ? 202 TYR B CA  1 
ATOM   3552 C C   . TYR B 1 202 ? 36.241 -4.260  5.253   1.00 54.41  ? 202 TYR B C   1 
ATOM   3553 O O   . TYR B 1 202 ? 36.789 -3.724  4.303   1.00 57.75  ? 202 TYR B O   1 
ATOM   3554 C CB  . TYR B 1 202 ? 33.949 -4.028  4.279   1.00 49.02  ? 202 TYR B CB  1 
ATOM   3555 C CG  . TYR B 1 202 ? 32.481 -3.738  4.411   1.00 46.33  ? 202 TYR B CG  1 
ATOM   3556 C CD1 . TYR B 1 202 ? 31.680 -4.401  5.328   1.00 46.06  ? 202 TYR B CD1 1 
ATOM   3557 C CD2 . TYR B 1 202 ? 31.876 -2.845  3.554   1.00 44.93  ? 202 TYR B CD2 1 
ATOM   3558 C CE1 . TYR B 1 202 ? 30.322 -4.144  5.412   1.00 46.21  ? 202 TYR B CE1 1 
ATOM   3559 C CE2 . TYR B 1 202 ? 30.516 -2.600  3.600   1.00 48.26  ? 202 TYR B CE2 1 
ATOM   3560 C CZ  . TYR B 1 202 ? 29.735 -3.252  4.530   1.00 47.75  ? 202 TYR B CZ  1 
ATOM   3561 O OH  . TYR B 1 202 ? 28.404 -2.966  4.557   1.00 46.82  ? 202 TYR B OH  1 
ATOM   3562 N N   . MET B 1 203 ? 36.864 -5.143  6.021   1.00 63.08  ? 203 MET B N   1 
ATOM   3563 C CA  . MET B 1 203 ? 38.277 -5.530  5.801   1.00 58.86  ? 203 MET B CA  1 
ATOM   3564 C C   . MET B 1 203 ? 38.318 -6.601  4.709   1.00 50.91  ? 203 MET B C   1 
ATOM   3565 O O   . MET B 1 203 ? 37.579 -7.601  4.860   1.00 45.53  ? 203 MET B O   1 
ATOM   3566 C CB  . MET B 1 203 ? 38.853 -6.098  7.095   1.00 70.66  ? 203 MET B CB  1 
ATOM   3567 C CG  . MET B 1 203 ? 40.352 -5.929  7.211   1.00 78.67  ? 203 MET B CG  1 
ATOM   3568 S SD  . MET B 1 203 ? 40.733 -4.931  8.647   1.00 75.73  ? 203 MET B SD  1 
ATOM   3569 C CE  . MET B 1 203 ? 40.094 -6.004  9.937   1.00 75.22  ? 203 MET B CE  1 
ATOM   3570 N N   . SER B 1 204 ? 39.104 -6.400  3.645   1.00 48.68  ? 204 SER B N   1 
ATOM   3571 C CA  . SER B 1 204 ? 39.292 -7.427  2.585   1.00 51.99  ? 204 SER B CA  1 
ATOM   3572 C C   . SER B 1 204 ? 40.443 -8.345  2.965   1.00 47.39  ? 204 SER B C   1 
ATOM   3573 O O   . SER B 1 204 ? 41.291 -7.999  3.772   1.00 47.52  ? 204 SER B O   1 
ATOM   3574 C CB  . SER B 1 204 ? 39.526 -6.848  1.219   1.00 52.31  ? 204 SER B CB  1 
ATOM   3575 O OG  . SER B 1 204 ? 40.708 -6.070  1.198   1.00 62.11  ? 204 SER B OG  1 
ATOM   3576 N N   . PRO B 1 205 ? 40.499 -9.550  2.386   1.00 45.68  ? 205 PRO B N   1 
ATOM   3577 C CA  . PRO B 1 205 ? 41.653 -10.418 2.562   1.00 50.71  ? 205 PRO B CA  1 
ATOM   3578 C C   . PRO B 1 205 ? 42.977 -9.745  2.169   1.00 55.67  ? 205 PRO B C   1 
ATOM   3579 O O   . PRO B 1 205 ? 43.963 -9.891  2.887   1.00 54.57  ? 205 PRO B O   1 
ATOM   3580 C CB  . PRO B 1 205 ? 41.299 -11.593 1.651   1.00 53.69  ? 205 PRO B CB  1 
ATOM   3581 C CG  . PRO B 1 205 ? 39.796 -11.635 1.709   1.00 52.69  ? 205 PRO B CG  1 
ATOM   3582 C CD  . PRO B 1 205 ? 39.404 -10.180 1.637   1.00 50.52  ? 205 PRO B CD  1 
ATOM   3583 N N   . GLU B 1 206 ? 42.985 -9.006  1.064   1.00 57.78  ? 206 GLU B N   1 
ATOM   3584 C CA  . GLU B 1 206 ? 44.219 -8.337  0.575   1.00 61.76  ? 206 GLU B CA  1 
ATOM   3585 C C   . GLU B 1 206 ? 44.626 -7.213  1.552   1.00 60.93  ? 206 GLU B C   1 
ATOM   3586 O O   . GLU B 1 206 ? 45.847 -6.920  1.618   1.00 55.97  ? 206 GLU B O   1 
ATOM   3587 C CB  . GLU B 1 206 ? 44.062 -7.878  -0.879  1.00 63.31  ? 206 GLU B CB  1 
ATOM   3588 C CG  . GLU B 1 206 ? 42.974 -6.839  -1.103  1.00 61.36  ? 206 GLU B CG  1 
ATOM   3589 C CD  . GLU B 1 206 ? 41.661 -7.387  -1.632  1.00 56.56  ? 206 GLU B CD  1 
ATOM   3590 O OE1 . GLU B 1 206 ? 41.265 -8.496  -1.210  1.00 51.75  ? 206 GLU B OE1 1 
ATOM   3591 O OE2 . GLU B 1 206 ? 41.043 -6.705  -2.472  1.00 55.01  ? 206 GLU B OE2 1 
ATOM   3592 N N   . ARG B 1 207 ? 43.689 -6.623  2.307   1.00 52.16  ? 207 ARG B N   1 
ATOM   3593 C CA  . ARG B 1 207 ? 44.044 -5.677  3.407   1.00 57.89  ? 207 ARG B CA  1 
ATOM   3594 C C   . ARG B 1 207 ? 44.688 -6.448  4.568   1.00 57.36  ? 207 ARG B C   1 
ATOM   3595 O O   . ARG B 1 207 ? 45.731 -6.006  5.053   1.00 55.83  ? 207 ARG B O   1 
ATOM   3596 C CB  . ARG B 1 207 ? 42.838 -4.911  3.954   1.00 59.99  ? 207 ARG B CB  1 
ATOM   3597 C CG  . ARG B 1 207 ? 43.183 -3.933  5.076   1.00 66.55  ? 207 ARG B CG  1 
ATOM   3598 C CD  . ARG B 1 207 ? 43.363 -2.511  4.587   1.00 87.23  ? 207 ARG B CD  1 
ATOM   3599 N NE  . ARG B 1 207 ? 42.122 -2.063  3.975   1.00 112.25 ? 207 ARG B NE  1 
ATOM   3600 C CZ  . ARG B 1 207 ? 41.988 -1.009  3.177   1.00 124.63 ? 207 ARG B CZ  1 
ATOM   3601 N NH1 . ARG B 1 207 ? 43.028 -0.248  2.867   1.00 125.40 ? 207 ARG B NH1 1 
ATOM   3602 N NH2 . ARG B 1 207 ? 40.793 -0.729  2.683   1.00 128.33 ? 207 ARG B NH2 1 
ATOM   3603 N N   . ILE B 1 208 ? 44.032 -7.514  5.031   1.00 58.56  ? 208 ILE B N   1 
ATOM   3604 C CA  . ILE B 1 208 ? 44.468 -8.387  6.160   1.00 63.19  ? 208 ILE B CA  1 
ATOM   3605 C C   . ILE B 1 208 ? 45.907 -8.849  5.919   1.00 66.27  ? 208 ILE B C   1 
ATOM   3606 O O   . ILE B 1 208 ? 46.730 -8.713  6.836   1.00 59.91  ? 208 ILE B O   1 
ATOM   3607 C CB  . ILE B 1 208 ? 43.535 -9.607  6.267   1.00 65.29  ? 208 ILE B CB  1 
ATOM   3608 C CG1 . ILE B 1 208 ? 42.235 -9.281  6.985   1.00 68.78  ? 208 ILE B CG1 1 
ATOM   3609 C CG2 . ILE B 1 208 ? 44.227 -10.782 6.927   1.00 73.82  ? 208 ILE B CG2 1 
ATOM   3610 C CD1 . ILE B 1 208 ? 41.277 -10.442 6.936   1.00 73.43  ? 208 ILE B CD1 1 
ATOM   3611 N N   . HIS B 1 209 ? 46.161 -9.390  4.723   1.00 72.28  ? 209 HIS B N   1 
ATOM   3612 C CA  . HIS B 1 209 ? 47.335 -10.229 4.377   1.00 74.69  ? 209 HIS B CA  1 
ATOM   3613 C C   . HIS B 1 209 ? 48.500 -9.380  3.861   1.00 76.45  ? 209 HIS B C   1 
ATOM   3614 O O   . HIS B 1 209 ? 49.644 -9.703  4.215   1.00 81.25  ? 209 HIS B O   1 
ATOM   3615 C CB  . HIS B 1 209 ? 46.928 -11.327 3.383   1.00 70.19  ? 209 HIS B CB  1 
ATOM   3616 C CG  . HIS B 1 209 ? 46.267 -12.476 4.061   1.00 76.09  ? 209 HIS B CG  1 
ATOM   3617 N ND1 . HIS B 1 209 ? 44.967 -12.850 3.787   1.00 86.99  ? 209 HIS B ND1 1 
ATOM   3618 C CD2 . HIS B 1 209 ? 46.704 -13.307 5.035   1.00 83.39  ? 209 HIS B CD2 1 
ATOM   3619 C CE1 . HIS B 1 209 ? 44.632 -13.872 4.554   1.00 87.92  ? 209 HIS B CE1 1 
ATOM   3620 N NE2 . HIS B 1 209 ? 45.682 -14.171 5.332   1.00 84.06  ? 209 HIS B NE2 1 
ATOM   3621 N N   . GLU B 1 210 ? 48.245 -8.373  3.027   1.00 84.44  ? 210 GLU B N   1 
ATOM   3622 C CA  . GLU B 1 210 ? 49.314 -7.687  2.245   1.00 89.17  ? 210 GLU B CA  1 
ATOM   3623 C C   . GLU B 1 210 ? 49.215 -6.173  2.393   1.00 82.07  ? 210 GLU B C   1 
ATOM   3624 O O   . GLU B 1 210 ? 50.015 -5.477  1.743   1.00 79.44  ? 210 GLU B O   1 
ATOM   3625 C CB  . GLU B 1 210 ? 49.212 -8.053  0.762   1.00 94.53  ? 210 GLU B CB  1 
ATOM   3626 C CG  . GLU B 1 210 ? 49.554 -9.505  0.486   1.00 105.84 ? 210 GLU B CG  1 
ATOM   3627 C CD  . GLU B 1 210 ? 48.490 -10.253 -0.299  1.00 118.87 ? 210 GLU B CD  1 
ATOM   3628 O OE1 . GLU B 1 210 ? 47.912 -9.650  -1.227  1.00 124.74 ? 210 GLU B OE1 1 
ATOM   3629 O OE2 . GLU B 1 210 ? 48.226 -11.429 0.039   1.00 125.41 ? 210 GLU B OE2 1 
ATOM   3630 N N   . ASN B 1 211 ? 48.268 -5.684  3.193   1.00 78.85  ? 211 ASN B N   1 
ATOM   3631 C CA  . ASN B 1 211 ? 47.917 -4.239  3.232   1.00 87.60  ? 211 ASN B CA  1 
ATOM   3632 C C   . ASN B 1 211 ? 47.811 -3.709  1.786   1.00 76.63  ? 211 ASN B C   1 
ATOM   3633 O O   . ASN B 1 211 ? 48.394 -2.656  1.514   1.00 80.63  ? 211 ASN B O   1 
ATOM   3634 C CB  . ASN B 1 211 ? 48.939 -3.469  4.081   1.00 95.26  ? 211 ASN B CB  1 
ATOM   3635 C CG  . ASN B 1 211 ? 49.460 -4.283  5.249   1.00 100.30 ? 211 ASN B CG  1 
ATOM   3636 O OD1 . ASN B 1 211 ? 48.765 -4.450  6.252   1.00 103.66 ? 211 ASN B OD1 1 
ATOM   3637 N ND2 . ASN B 1 211 ? 50.667 -4.815  5.123   1.00 93.08  ? 211 ASN B ND2 1 
ATOM   3638 N N   . GLY B 1 212 ? 47.141 -4.436  0.882   1.00 68.21  ? 212 GLY B N   1 
ATOM   3639 C CA  . GLY B 1 212 ? 46.896 -4.016  -0.514  1.00 66.56  ? 212 GLY B CA  1 
ATOM   3640 C C   . GLY B 1 212 ? 45.485 -3.458  -0.676  1.00 64.19  ? 212 GLY B C   1 
ATOM   3641 O O   . GLY B 1 212 ? 44.585 -3.946  0.020   1.00 64.58  ? 212 GLY B O   1 
ATOM   3642 N N   . TYR B 1 213 ? 45.290 -2.438  -1.522  1.00 58.33  ? 213 TYR B N   1 
ATOM   3643 C CA  . TYR B 1 213 ? 43.947 -1.971  -1.966  1.00 56.91  ? 213 TYR B CA  1 
ATOM   3644 C C   . TYR B 1 213 ? 43.972 -1.652  -3.464  1.00 51.01  ? 213 TYR B C   1 
ATOM   3645 O O   . TYR B 1 213 ? 44.700 -0.747  -3.868  1.00 53.15  ? 213 TYR B O   1 
ATOM   3646 C CB  . TYR B 1 213 ? 43.441 -0.755  -1.176  1.00 51.03  ? 213 TYR B CB  1 
ATOM   3647 C CG  . TYR B 1 213 ? 41.934 -0.611  -1.190  1.00 51.71  ? 213 TYR B CG  1 
ATOM   3648 C CD1 . TYR B 1 213 ? 41.267 -0.035  -2.264  1.00 50.14  ? 213 TYR B CD1 1 
ATOM   3649 C CD2 . TYR B 1 213 ? 41.153 -1.099  -0.152  1.00 51.33  ? 213 TYR B CD2 1 
ATOM   3650 C CE1 . TYR B 1 213 ? 39.881 0.061   -2.296  1.00 49.84  ? 213 TYR B CE1 1 
ATOM   3651 C CE2 . TYR B 1 213 ? 39.768 -0.973  -0.144  1.00 47.50  ? 213 TYR B CE2 1 
ATOM   3652 C CZ  . TYR B 1 213 ? 39.125 -0.396  -1.227  1.00 50.82  ? 213 TYR B CZ  1 
ATOM   3653 O OH  . TYR B 1 213 ? 37.761 -0.290  -1.257  1.00 49.13  ? 213 TYR B OH  1 
ATOM   3654 N N   . ASN B 1 214 ? 43.142 -2.340  -4.244  1.00 46.53  ? 214 ASN B N   1 
ATOM   3655 C CA  . ASN B 1 214 ? 42.982 -2.105  -5.701  1.00 47.71  ? 214 ASN B CA  1 
ATOM   3656 C C   . ASN B 1 214 ? 41.481 -1.965  -6.029  1.00 46.10  ? 214 ASN B C   1 
ATOM   3657 O O   . ASN B 1 214 ? 40.640 -2.029  -5.099  1.00 44.18  ? 214 ASN B O   1 
ATOM   3658 C CB  . ASN B 1 214 ? 43.687 -3.216  -6.481  1.00 52.07  ? 214 ASN B CB  1 
ATOM   3659 C CG  . ASN B 1 214 ? 43.100 -4.588  -6.211  1.00 61.22  ? 214 ASN B CG  1 
ATOM   3660 O OD1 . ASN B 1 214 ? 41.909 -4.732  -5.931  1.00 68.20  ? 214 ASN B OD1 1 
ATOM   3661 N ND2 . ASN B 1 214 ? 43.936 -5.610  -6.263  1.00 73.47  ? 214 ASN B ND2 1 
ATOM   3662 N N   . PHE B 1 215 ? 41.147 -1.842  -7.316  1.00 41.84  ? 215 PHE B N   1 
ATOM   3663 C CA  . PHE B 1 215 ? 39.765 -1.646  -7.835  1.00 43.49  ? 215 PHE B CA  1 
ATOM   3664 C C   . PHE B 1 215 ? 38.850 -2.798  -7.372  1.00 41.50  ? 215 PHE B C   1 
ATOM   3665 O O   . PHE B 1 215 ? 37.678 -2.553  -7.059  1.00 37.96  ? 215 PHE B O   1 
ATOM   3666 C CB  . PHE B 1 215 ? 39.796 -1.456  -9.362  1.00 42.49  ? 215 PHE B CB  1 
ATOM   3667 C CG  . PHE B 1 215 ? 40.497 -0.195  -9.800  1.00 41.52  ? 215 PHE B CG  1 
ATOM   3668 C CD1 . PHE B 1 215 ? 39.825 1.025   -9.811  1.00 43.53  ? 215 PHE B CD1 1 
ATOM   3669 C CD2 . PHE B 1 215 ? 41.837 -0.218  -10.180 1.00 42.47  ? 215 PHE B CD2 1 
ATOM   3670 C CE1 . PHE B 1 215 ? 40.475 2.194   -10.195 1.00 42.69  ? 215 PHE B CE1 1 
ATOM   3671 C CE2 . PHE B 1 215 ? 42.493 0.955   -10.539 1.00 42.55  ? 215 PHE B CE2 1 
ATOM   3672 C CZ  . PHE B 1 215 ? 41.810 2.159   -10.553 1.00 42.76  ? 215 PHE B CZ  1 
ATOM   3673 N N   . LYS B 1 216 ? 39.375 -4.017  -7.298  1.00 42.40  ? 216 LYS B N   1 
ATOM   3674 C CA  . LYS B 1 216 ? 38.611 -5.220  -6.871  1.00 45.47  ? 216 LYS B CA  1 
ATOM   3675 C C   . LYS B 1 216 ? 38.362 -5.167  -5.356  1.00 44.16  ? 216 LYS B C   1 
ATOM   3676 O O   . LYS B 1 216 ? 37.342 -5.743  -4.910  1.00 43.82  ? 216 LYS B O   1 
ATOM   3677 C CB  . LYS B 1 216 ? 39.336 -6.484  -7.350  1.00 47.16  ? 216 LYS B CB  1 
ATOM   3678 C CG  . LYS B 1 216 ? 39.442 -6.614  -8.872  1.00 48.36  ? 216 LYS B CG  1 
ATOM   3679 C CD  . LYS B 1 216 ? 38.118 -6.954  -9.540  1.00 52.71  ? 216 LYS B CD  1 
ATOM   3680 C CE  . LYS B 1 216 ? 38.250 -7.420  -10.985 1.00 57.29  ? 216 LYS B CE  1 
ATOM   3681 N NZ  . LYS B 1 216 ? 38.933 -8.733  -11.120 1.00 53.82  ? 216 LYS B NZ  1 
ATOM   3682 N N   . SER B 1 217 ? 39.189 -4.447  -4.593  1.00 40.94  ? 217 SER B N   1 
ATOM   3683 C CA  . SER B 1 217 ? 38.885 -4.188  -3.158  1.00 44.93  ? 217 SER B CA  1 
ATOM   3684 C C   . SER B 1 217 ? 37.556 -3.416  -3.070  1.00 39.55  ? 217 SER B C   1 
ATOM   3685 O O   . SER B 1 217 ? 36.742 -3.748  -2.203  1.00 40.58  ? 217 SER B O   1 
ATOM   3686 C CB  . SER B 1 217 ? 40.020 -3.498  -2.404  1.00 44.45  ? 217 SER B CB  1 
ATOM   3687 O OG  . SER B 1 217 ? 41.291 -4.098  -2.672  1.00 45.76  ? 217 SER B OG  1 
ATOM   3688 N N   . ASP B 1 218 ? 37.262 -2.489  -3.987  1.00 39.10  ? 218 ASP B N   1 
ATOM   3689 C CA  . ASP B 1 218 ? 35.944 -1.792  -3.955  1.00 37.47  ? 218 ASP B CA  1 
ATOM   3690 C C   . ASP B 1 218 ? 34.808 -2.819  -4.143  1.00 37.60  ? 218 ASP B C   1 
ATOM   3691 O O   . ASP B 1 218 ? 33.720 -2.648  -3.509  1.00 36.85  ? 218 ASP B O   1 
ATOM   3692 C CB  . ASP B 1 218 ? 35.857 -0.659  -4.977  1.00 42.13  ? 218 ASP B CB  1 
ATOM   3693 C CG  . ASP B 1 218 ? 36.570 0.645   -4.643  1.00 40.69  ? 218 ASP B CG  1 
ATOM   3694 O OD1 . ASP B 1 218 ? 36.849 0.891   -3.448  1.00 45.59  ? 218 ASP B OD1 1 
ATOM   3695 O OD2 . ASP B 1 218 ? 36.809 1.431   -5.605  1.00 39.37  ? 218 ASP B OD2 1 
ATOM   3696 N N   . ILE B 1 219 ? 35.049 -3.872  -4.942  1.00 37.85  ? 219 ILE B N   1 
ATOM   3697 C CA  . ILE B 1 219 ? 34.014 -4.884  -5.309  1.00 42.64  ? 219 ILE B CA  1 
ATOM   3698 C C   . ILE B 1 219 ? 33.697 -5.719  -4.064  1.00 42.79  ? 219 ILE B C   1 
ATOM   3699 O O   . ILE B 1 219 ? 32.486 -5.953  -3.783  1.00 38.97  ? 219 ILE B O   1 
ATOM   3700 C CB  . ILE B 1 219 ? 34.452 -5.776  -6.500  1.00 44.38  ? 219 ILE B CB  1 
ATOM   3701 C CG1 . ILE B 1 219 ? 34.828 -4.960  -7.741  1.00 44.12  ? 219 ILE B CG1 1 
ATOM   3702 C CG2 . ILE B 1 219 ? 33.362 -6.799  -6.812  1.00 44.70  ? 219 ILE B CG2 1 
ATOM   3703 C CD1 . ILE B 1 219 ? 33.691 -4.113  -8.313  1.00 46.07  ? 219 ILE B CD1 1 
ATOM   3704 N N   . TRP B 1 220 ? 34.748 -6.177  -3.377  1.00 39.50  ? 220 TRP B N   1 
ATOM   3705 C CA  . TRP B 1 220 ? 34.623 -6.831  -2.055  1.00 39.75  ? 220 TRP B CA  1 
ATOM   3706 C C   . TRP B 1 220 ? 33.663 -6.024  -1.179  1.00 38.24  ? 220 TRP B C   1 
ATOM   3707 O O   . TRP B 1 220 ? 32.663 -6.601  -0.693  1.00 36.89  ? 220 TRP B O   1 
ATOM   3708 C CB  . TRP B 1 220 ? 35.994 -6.986  -1.385  1.00 42.69  ? 220 TRP B CB  1 
ATOM   3709 C CG  . TRP B 1 220 ? 35.889 -7.470  0.028   1.00 42.10  ? 220 TRP B CG  1 
ATOM   3710 C CD1 . TRP B 1 220 ? 35.691 -6.717  1.148   1.00 42.04  ? 220 TRP B CD1 1 
ATOM   3711 C CD2 . TRP B 1 220 ? 35.951 -8.836  0.467   1.00 45.89  ? 220 TRP B CD2 1 
ATOM   3712 N NE1 . TRP B 1 220 ? 35.623 -7.518  2.253   1.00 45.01  ? 220 TRP B NE1 1 
ATOM   3713 C CE2 . TRP B 1 220 ? 35.797 -8.822  1.872   1.00 46.82  ? 220 TRP B CE2 1 
ATOM   3714 C CE3 . TRP B 1 220 ? 36.140 -10.063 -0.182  1.00 45.07  ? 220 TRP B CE3 1 
ATOM   3715 C CZ2 . TRP B 1 220 ? 35.820 -9.991  2.628   1.00 45.47  ? 220 TRP B CZ2 1 
ATOM   3716 C CZ3 . TRP B 1 220 ? 36.166 -11.219 0.570   1.00 46.64  ? 220 TRP B CZ3 1 
ATOM   3717 C CH2 . TRP B 1 220 ? 36.010 -11.180 1.957   1.00 47.14  ? 220 TRP B CH2 1 
ATOM   3718 N N   . SER B 1 221 ? 33.988 -4.755  -0.925  1.00 39.87  ? 221 SER B N   1 
ATOM   3719 C CA  . SER B 1 221 ? 33.172 -3.864  -0.059  1.00 40.64  ? 221 SER B CA  1 
ATOM   3720 C C   . SER B 1 221 ? 31.730 -3.807  -0.584  1.00 42.45  ? 221 SER B C   1 
ATOM   3721 O O   . SER B 1 221 ? 30.791 -3.856  0.235   1.00 40.49  ? 221 SER B O   1 
ATOM   3722 C CB  . SER B 1 221 ? 33.751 -2.491  0.002   1.00 39.77  ? 221 SER B CB  1 
ATOM   3723 O OG  . SER B 1 221 ? 34.897 -2.488  0.814   1.00 41.51  ? 221 SER B OG  1 
ATOM   3724 N N   . LEU B 1 222 ? 31.570 -3.667  -1.901  1.00 42.34  ? 222 LEU B N   1 
ATOM   3725 C CA  . LEU B 1 222 ? 30.239 -3.517  -2.558  1.00 45.32  ? 222 LEU B CA  1 
ATOM   3726 C C   . LEU B 1 222 ? 29.431 -4.795  -2.301  1.00 46.28  ? 222 LEU B C   1 
ATOM   3727 O O   . LEU B 1 222 ? 28.220 -4.706  -1.997  1.00 41.28  ? 222 LEU B O   1 
ATOM   3728 C CB  . LEU B 1 222 ? 30.487 -3.266  -4.051  1.00 48.93  ? 222 LEU B CB  1 
ATOM   3729 C CG  . LEU B 1 222 ? 29.322 -2.755  -4.893  1.00 48.67  ? 222 LEU B CG  1 
ATOM   3730 C CD1 . LEU B 1 222 ? 28.924 -1.337  -4.504  1.00 52.03  ? 222 LEU B CD1 1 
ATOM   3731 C CD2 . LEU B 1 222 ? 29.705 -2.809  -6.361  1.00 46.50  ? 222 LEU B CD2 1 
ATOM   3732 N N   . GLY B 1 223 ? 30.089 -5.953  -2.430  1.00 42.92  ? 223 GLY B N   1 
ATOM   3733 C CA  . GLY B 1 223 ? 29.516 -7.245  -2.026  1.00 42.21  ? 223 GLY B CA  1 
ATOM   3734 C C   . GLY B 1 223 ? 29.052 -7.234  -0.580  1.00 39.98  ? 223 GLY B C   1 
ATOM   3735 O O   . GLY B 1 223 ? 27.926 -7.679  -0.313  1.00 36.32  ? 223 GLY B O   1 
ATOM   3736 N N   . CYS B 1 224 ? 29.894 -6.771  0.340   1.00 37.62  ? 224 CYS B N   1 
ATOM   3737 C CA  . CYS B 1 224 ? 29.547 -6.711  1.778   1.00 40.25  ? 224 CYS B CA  1 
ATOM   3738 C C   . CYS B 1 224 ? 28.356 -5.779  1.997   1.00 49.28  ? 224 CYS B C   1 
ATOM   3739 O O   . CYS B 1 224 ? 27.544 -6.045  2.933   1.00 51.06  ? 224 CYS B O   1 
ATOM   3740 C CB  . CYS B 1 224 ? 30.722 -6.243  2.618   1.00 39.58  ? 224 CYS B CB  1 
ATOM   3741 S SG  . CYS B 1 224 ? 32.104 -7.411  2.545   1.00 44.68  ? 224 CYS B SG  1 
ATOM   3742 N N   . LEU B 1 225 ? 28.256 -4.710  1.198   1.00 50.45  ? 225 LEU B N   1 
ATOM   3743 C CA  . LEU B 1 225 ? 27.194 -3.700  1.408   1.00 51.52  ? 225 LEU B CA  1 
ATOM   3744 C C   . LEU B 1 225 ? 25.869 -4.273  0.889   1.00 52.13  ? 225 LEU B C   1 
ATOM   3745 O O   . LEU B 1 225 ? 24.828 -4.054  1.548   1.00 47.60  ? 225 LEU B O   1 
ATOM   3746 C CB  . LEU B 1 225 ? 27.586 -2.392  0.723   1.00 51.88  ? 225 LEU B CB  1 
ATOM   3747 C CG  . LEU B 1 225 ? 26.624 -1.241  0.992   1.00 53.86  ? 225 LEU B CG  1 
ATOM   3748 C CD1 . LEU B 1 225 ? 27.365 0.032   1.340   1.00 53.80  ? 225 LEU B CD1 1 
ATOM   3749 C CD2 . LEU B 1 225 ? 25.721 -1.027  -0.211  1.00 62.83  ? 225 LEU B CD2 1 
ATOM   3750 N N   . LEU B 1 226 ? 25.910 -5.018  -0.220  1.00 46.53  ? 226 LEU B N   1 
ATOM   3751 C CA  . LEU B 1 226 ? 24.709 -5.726  -0.731  1.00 49.93  ? 226 LEU B CA  1 
ATOM   3752 C C   . LEU B 1 226 ? 24.257 -6.748  0.322   1.00 49.44  ? 226 LEU B C   1 
ATOM   3753 O O   . LEU B 1 226 ? 23.049 -6.794  0.587   1.00 50.85  ? 226 LEU B O   1 
ATOM   3754 C CB  . LEU B 1 226 ? 25.001 -6.375  -2.089  1.00 50.05  ? 226 LEU B CB  1 
ATOM   3755 C CG  . LEU B 1 226 ? 23.849 -7.173  -2.705  1.00 48.11  ? 226 LEU B CG  1 
ATOM   3756 C CD1 . LEU B 1 226 ? 22.621 -6.308  -2.935  1.00 47.76  ? 226 LEU B CD1 1 
ATOM   3757 C CD2 . LEU B 1 226 ? 24.278 -7.832  -3.999  1.00 48.99  ? 226 LEU B CD2 1 
ATOM   3758 N N   . TYR B 1 227 ? 25.170 -7.507  0.940   1.00 49.03  ? 227 TYR B N   1 
ATOM   3759 C CA  . TYR B 1 227 ? 24.816 -8.417  2.067   1.00 48.44  ? 227 TYR B CA  1 
ATOM   3760 C C   . TYR B 1 227 ? 24.163 -7.621  3.204   1.00 44.65  ? 227 TYR B C   1 
ATOM   3761 O O   . TYR B 1 227 ? 23.112 -8.045  3.675   1.00 46.60  ? 227 TYR B O   1 
ATOM   3762 C CB  . TYR B 1 227 ? 26.019 -9.208  2.583   1.00 51.01  ? 227 TYR B CB  1 
ATOM   3763 C CG  . TYR B 1 227 ? 25.718 -10.139 3.735   1.00 49.46  ? 227 TYR B CG  1 
ATOM   3764 C CD1 . TYR B 1 227 ? 25.735 -9.684  5.042   1.00 51.15  ? 227 TYR B CD1 1 
ATOM   3765 C CD2 . TYR B 1 227 ? 25.421 -11.473 3.526   1.00 47.13  ? 227 TYR B CD2 1 
ATOM   3766 C CE1 . TYR B 1 227 ? 25.457 -10.521 6.111   1.00 53.46  ? 227 TYR B CE1 1 
ATOM   3767 C CE2 . TYR B 1 227 ? 25.136 -12.322 4.583   1.00 56.16  ? 227 TYR B CE2 1 
ATOM   3768 C CZ  . TYR B 1 227 ? 25.162 -11.848 5.885   1.00 54.08  ? 227 TYR B CZ  1 
ATOM   3769 O OH  . TYR B 1 227 ? 24.914 -12.657 6.955   1.00 60.48  ? 227 TYR B OH  1 
ATOM   3770 N N   . GLU B 1 228 ? 24.773 -6.516  3.634   1.00 46.66  ? 228 GLU B N   1 
ATOM   3771 C CA  . GLU B 1 228 ? 24.311 -5.725  4.805   1.00 49.09  ? 228 GLU B CA  1 
ATOM   3772 C C   . GLU B 1 228 ? 22.905 -5.144  4.557   1.00 48.74  ? 228 GLU B C   1 
ATOM   3773 O O   . GLU B 1 228 ? 22.149 -4.993  5.532   1.00 47.35  ? 228 GLU B O   1 
ATOM   3774 C CB  . GLU B 1 228 ? 25.323 -4.626  5.140   1.00 48.34  ? 228 GLU B CB  1 
ATOM   3775 C CG  . GLU B 1 228 ? 25.034 -3.934  6.472   1.00 48.66  ? 228 GLU B CG  1 
ATOM   3776 C CD  . GLU B 1 228 ? 26.227 -3.465  7.296   1.00 52.23  ? 228 GLU B CD  1 
ATOM   3777 O OE1 . GLU B 1 228 ? 27.397 -3.738  6.915   1.00 53.57  ? 228 GLU B OE1 1 
ATOM   3778 O OE2 . GLU B 1 228 ? 25.985 -2.842  8.337   1.00 59.57  ? 228 GLU B OE2 1 
ATOM   3779 N N   . MET B 1 229 ? 22.561 -4.797  3.317   1.00 51.54  ? 229 MET B N   1 
ATOM   3780 C CA  . MET B 1 229 ? 21.219 -4.236  2.988   1.00 56.82  ? 229 MET B CA  1 
ATOM   3781 C C   . MET B 1 229 ? 20.160 -5.329  3.199   1.00 55.96  ? 229 MET B C   1 
ATOM   3782 O O   . MET B 1 229 ? 19.059 -4.997  3.670   1.00 60.21  ? 229 MET B O   1 
ATOM   3783 C CB  . MET B 1 229 ? 21.145 -3.722  1.544   1.00 55.05  ? 229 MET B CB  1 
ATOM   3784 C CG  . MET B 1 229 ? 21.770 -2.344  1.338   1.00 59.47  ? 229 MET B CG  1 
ATOM   3785 S SD  . MET B 1 229 ? 21.529 -1.710  -0.362  1.00 60.12  ? 229 MET B SD  1 
ATOM   3786 C CE  . MET B 1 229 ? 22.451 -2.892  -1.338  1.00 74.77  ? 229 MET B CE  1 
ATOM   3787 N N   . ALA B 1 230 ? 20.493 -6.579  2.850   1.00 52.79  ? 230 ALA B N   1 
ATOM   3788 C CA  . ALA B 1 230 ? 19.597 -7.764  2.902   1.00 51.58  ? 230 ALA B CA  1 
ATOM   3789 C C   . ALA B 1 230 ? 19.551 -8.363  4.320   1.00 54.02  ? 230 ALA B C   1 
ATOM   3790 O O   . ALA B 1 230 ? 18.433 -8.717  4.765   1.00 59.42  ? 230 ALA B O   1 
ATOM   3791 C CB  . ALA B 1 230 ? 20.037 -8.776  1.871   1.00 50.53  ? 230 ALA B CB  1 
ATOM   3792 N N   . ALA B 1 231 ? 20.701 -8.433  5.013   1.00 51.01  ? 231 ALA B N   1 
ATOM   3793 C CA  . ALA B 1 231 ? 20.874 -9.070  6.342   1.00 53.84  ? 231 ALA B CA  1 
ATOM   3794 C C   . ALA B 1 231 ? 20.678 -8.069  7.494   1.00 47.55  ? 231 ALA B C   1 
ATOM   3795 O O   . ALA B 1 231 ? 20.475 -8.548  8.608   1.00 52.68  ? 231 ALA B O   1 
ATOM   3796 C CB  . ALA B 1 231 ? 22.235 -9.734  6.423   1.00 52.37  ? 231 ALA B CB  1 
ATOM   3797 N N   . LEU B 1 232 ? 20.809 -6.758  7.245   1.00 51.79  ? 232 LEU B N   1 
ATOM   3798 C CA  . LEU B 1 232 ? 20.779 -5.636  8.237   1.00 52.32  ? 232 LEU B CA  1 
ATOM   3799 C C   . LEU B 1 232 ? 21.950 -5.702  9.223   1.00 51.56  ? 232 LEU B C   1 
ATOM   3800 O O   . LEU B 1 232 ? 21.890 -5.058  10.288  1.00 50.73  ? 232 LEU B O   1 
ATOM   3801 C CB  . LEU B 1 232 ? 19.438 -5.627  8.979   1.00 60.08  ? 232 LEU B CB  1 
ATOM   3802 C CG  . LEU B 1 232 ? 18.194 -5.486  8.096   1.00 63.10  ? 232 LEU B CG  1 
ATOM   3803 C CD1 . LEU B 1 232 ? 16.949 -5.298  8.950   1.00 61.78  ? 232 LEU B CD1 1 
ATOM   3804 C CD2 . LEU B 1 232 ? 18.340 -4.338  7.096   1.00 61.43  ? 232 LEU B CD2 1 
ATOM   3805 N N   . GLN B 1 233 ? 23.025 -6.387  8.862   1.00 57.00  ? 233 GLN B N   1 
ATOM   3806 C CA  . GLN B 1 233 ? 24.305 -6.308  9.614   1.00 59.38  ? 233 GLN B CA  1 
ATOM   3807 C C   . GLN B 1 233 ? 25.445 -6.752  8.693   1.00 54.67  ? 233 GLN B C   1 
ATOM   3808 O O   . GLN B 1 233 ? 25.180 -7.438  7.671   1.00 55.00  ? 233 GLN B O   1 
ATOM   3809 C CB  . GLN B 1 233 ? 24.219 -7.136  10.898  1.00 61.22  ? 233 GLN B CB  1 
ATOM   3810 C CG  . GLN B 1 233 ? 24.009 -8.626  10.666  1.00 60.36  ? 233 GLN B CG  1 
ATOM   3811 C CD  . GLN B 1 233 ? 23.500 -9.292  11.923  1.00 68.44  ? 233 GLN B CD  1 
ATOM   3812 O OE1 . GLN B 1 233 ? 22.389 -9.027  12.376  1.00 81.00  ? 233 GLN B OE1 1 
ATOM   3813 N NE2 . GLN B 1 233 ? 24.307 -10.160 12.510  1.00 66.59  ? 233 GLN B NE2 1 
ATOM   3814 N N   . SER B 1 234 ? 26.670 -6.369  9.026   1.00 47.67  ? 234 SER B N   1 
ATOM   3815 C CA  A SER B 1 234 ? 27.875 -6.737  8.242   0.50 48.34  ? 234 SER B CA  1 
ATOM   3816 C CA  B SER B 1 234 ? 27.869 -6.738  8.230   0.50 48.37  ? 234 SER B CA  1 
ATOM   3817 C C   . SER B 1 234 ? 27.956 -8.259  8.134   1.00 48.47  ? 234 SER B C   1 
ATOM   3818 O O   . SER B 1 234 ? 27.490 -8.969  9.019   1.00 50.35  ? 234 SER B O   1 
ATOM   3819 C CB  A SER B 1 234 ? 29.119 -6.147  8.855   0.50 47.21  ? 234 SER B CB  1 
ATOM   3820 C CB  B SER B 1 234 ? 29.131 -6.152  8.803   0.50 47.28  ? 234 SER B CB  1 
ATOM   3821 O OG  A SER B 1 234 ? 29.066 -4.726  8.855   0.50 46.95  ? 234 SER B OG  1 
ATOM   3822 O OG  B SER B 1 234 ? 30.273 -6.625  8.098   0.50 47.18  ? 234 SER B OG  1 
ATOM   3823 N N   . PRO B 1 235 ? 28.516 -8.801  7.033   1.00 48.43  ? 235 PRO B N   1 
ATOM   3824 C CA  . PRO B 1 235 ? 28.714 -10.243 6.899   1.00 49.91  ? 235 PRO B CA  1 
ATOM   3825 C C   . PRO B 1 235 ? 29.674 -10.872 7.917   1.00 52.81  ? 235 PRO B C   1 
ATOM   3826 O O   . PRO B 1 235 ? 29.497 -12.038 8.230   1.00 55.47  ? 235 PRO B O   1 
ATOM   3827 C CB  . PRO B 1 235 ? 29.322 -10.440 5.507   1.00 45.66  ? 235 PRO B CB  1 
ATOM   3828 C CG  . PRO B 1 235 ? 29.677 -9.056  5.009   1.00 47.38  ? 235 PRO B CG  1 
ATOM   3829 C CD  . PRO B 1 235 ? 28.887 -8.059  5.819   1.00 47.26  ? 235 PRO B CD  1 
ATOM   3830 N N   . PHE B 1 236 ? 30.654 -10.104 8.391   1.00 52.25  ? 236 PHE B N   1 
ATOM   3831 C CA  . PHE B 1 236 ? 31.679 -10.573 9.352   1.00 57.01  ? 236 PHE B CA  1 
ATOM   3832 C C   . PHE B 1 236 ? 31.450 -9.922  10.723  1.00 68.31  ? 236 PHE B C   1 
ATOM   3833 O O   . PHE B 1 236 ? 32.412 -9.643  11.427  1.00 69.71  ? 236 PHE B O   1 
ATOM   3834 C CB  . PHE B 1 236 ? 33.041 -10.330 8.709   1.00 56.00  ? 236 PHE B CB  1 
ATOM   3835 C CG  . PHE B 1 236 ? 33.162 -10.961 7.345   1.00 55.22  ? 236 PHE B CG  1 
ATOM   3836 C CD1 . PHE B 1 236 ? 33.161 -12.339 7.207   1.00 52.84  ? 236 PHE B CD1 1 
ATOM   3837 C CD2 . PHE B 1 236 ? 33.219 -10.187 6.196   1.00 52.33  ? 236 PHE B CD2 1 
ATOM   3838 C CE1 . PHE B 1 236 ? 33.253 -12.927 5.955   1.00 55.52  ? 236 PHE B CE1 1 
ATOM   3839 C CE2 . PHE B 1 236 ? 33.320 -10.776 4.948   1.00 48.68  ? 236 PHE B CE2 1 
ATOM   3840 C CZ  . PHE B 1 236 ? 33.342 -12.143 4.827   1.00 54.11  ? 236 PHE B CZ  1 
ATOM   3841 N N   . TYR B 1 237 ? 30.184 -9.748  11.114  1.00 91.93  ? 237 TYR B N   1 
ATOM   3842 C CA  . TYR B 1 237 ? 29.760 -8.981  12.317  1.00 104.70 ? 237 TYR B CA  1 
ATOM   3843 C C   . TYR B 1 237 ? 30.204 -9.738  13.578  1.00 107.07 ? 237 TYR B C   1 
ATOM   3844 O O   . TYR B 1 237 ? 31.281 -9.392  14.083  1.00 123.67 ? 237 TYR B O   1 
ATOM   3845 C CB  . TYR B 1 237 ? 28.261 -8.657  12.251  1.00 109.66 ? 237 TYR B CB  1 
ATOM   3846 C CG  . TYR B 1 237 ? 27.697 -7.970  13.471  1.00 125.14 ? 237 TYR B CG  1 
ATOM   3847 C CD1 . TYR B 1 237 ? 28.196 -6.753  13.911  1.00 129.64 ? 237 TYR B CD1 1 
ATOM   3848 C CD2 . TYR B 1 237 ? 26.650 -8.534  14.189  1.00 131.10 ? 237 TYR B CD2 1 
ATOM   3849 C CE1 . TYR B 1 237 ? 27.677 -6.124  15.034  1.00 129.69 ? 237 TYR B CE1 1 
ATOM   3850 C CE2 . TYR B 1 237 ? 26.121 -7.919  15.313  1.00 125.59 ? 237 TYR B CE2 1 
ATOM   3851 C CZ  . TYR B 1 237 ? 26.635 -6.708  15.736  1.00 124.70 ? 237 TYR B CZ  1 
ATOM   3852 O OH  . TYR B 1 237 ? 26.111 -6.099  16.838  1.00 121.40 ? 237 TYR B OH  1 
ATOM   3853 N N   . GLY B 1 238 ? 29.429 -10.723 14.054  1.00 109.05 ? 238 GLY B N   1 
ATOM   3854 C CA  . GLY B 1 238 ? 29.656 -11.424 15.341  1.00 119.04 ? 238 GLY B CA  1 
ATOM   3855 C C   . GLY B 1 238 ? 29.277 -10.580 16.560  1.00 123.45 ? 238 GLY B C   1 
ATOM   3856 O O   . GLY B 1 238 ? 28.522 -9.597  16.395  1.00 121.43 ? 238 GLY B O   1 
ATOM   3857 N N   . ASP B 1 239 ? 29.763 -10.958 17.753  1.00 124.61 ? 239 ASP B N   1 
ATOM   3858 C CA  . ASP B 1 239 ? 29.557 -10.223 19.035  1.00 126.48 ? 239 ASP B CA  1 
ATOM   3859 C C   . ASP B 1 239 ? 30.915 -10.014 19.723  1.00 131.53 ? 239 ASP B C   1 
ATOM   3860 O O   . ASP B 1 239 ? 31.473 -8.909  19.559  1.00 133.99 ? 239 ASP B O   1 
ATOM   3861 C CB  . ASP B 1 239 ? 28.546 -10.929 19.948  1.00 124.92 ? 239 ASP B CB  1 
ATOM   3862 C CG  . ASP B 1 239 ? 27.124 -10.388 19.861  1.00 126.75 ? 239 ASP B CG  1 
ATOM   3863 O OD1 . ASP B 1 239 ? 26.730 -9.895  18.780  1.00 124.62 ? 239 ASP B OD1 1 
ATOM   3864 O OD2 . ASP B 1 239 ? 26.415 -10.465 20.879  1.00 121.62 ? 239 ASP B OD2 1 
ATOM   3865 N N   . LYS B 1 240 ? 31.419 -11.019 20.459  1.00 129.89 ? 240 LYS B N   1 
ATOM   3866 C CA  . LYS B 1 240 ? 32.736 -10.979 21.159  1.00 126.43 ? 240 LYS B CA  1 
ATOM   3867 C C   . LYS B 1 240 ? 33.761 -10.365 20.198  1.00 118.16 ? 240 LYS B C   1 
ATOM   3868 O O   . LYS B 1 240 ? 34.072 -9.173  20.342  1.00 106.33 ? 240 LYS B O   1 
ATOM   3869 C CB  . LYS B 1 240 ? 33.142 -12.383 21.629  1.00 131.87 ? 240 LYS B CB  1 
ATOM   3870 C CG  . LYS B 1 240 ? 34.598 -12.543 22.067  1.00 139.09 ? 240 LYS B CG  1 
ATOM   3871 C CD  . LYS B 1 240 ? 35.119 -13.978 22.034  1.00 140.40 ? 240 LYS B CD  1 
ATOM   3872 C CE  . LYS B 1 240 ? 35.123 -14.625 20.659  1.00 132.35 ? 240 LYS B CE  1 
ATOM   3873 N NZ  . LYS B 1 240 ? 36.329 -14.274 19.874  1.00 124.42 ? 240 LYS B NZ  1 
ATOM   3874 N N   . MET B 1 241 ? 34.225 -11.156 19.230  1.00 118.38 ? 241 MET B N   1 
ATOM   3875 C CA  . MET B 1 241 ? 35.010 -10.704 18.052  1.00 111.40 ? 241 MET B CA  1 
ATOM   3876 C C   . MET B 1 241 ? 36.381 -10.163 18.486  1.00 94.18  ? 241 MET B C   1 
ATOM   3877 O O   . MET B 1 241 ? 36.572 -8.924  18.566  1.00 78.90  ? 241 MET B O   1 
ATOM   3878 C CB  . MET B 1 241 ? 34.236 -9.663  17.229  1.00 113.76 ? 241 MET B CB  1 
ATOM   3879 C CG  . MET B 1 241 ? 34.269 -9.934  15.722  1.00 108.50 ? 241 MET B CG  1 
ATOM   3880 S SD  . MET B 1 241 ? 34.093 -11.698 15.296  1.00 99.08  ? 241 MET B SD  1 
ATOM   3881 C CE  . MET B 1 241 ? 33.513 -11.560 13.608  1.00 89.97  ? 241 MET B CE  1 
ATOM   3882 N N   . ASN B 1 242 ? 37.283 -11.100 18.781  1.00 76.83  ? 242 ASN B N   1 
ATOM   3883 C CA  . ASN B 1 242 ? 38.725 -11.010 18.466  1.00 70.47  ? 242 ASN B CA  1 
ATOM   3884 C C   . ASN B 1 242 ? 38.883 -10.402 17.067  1.00 66.39  ? 242 ASN B C   1 
ATOM   3885 O O   . ASN B 1 242 ? 38.114 -10.811 16.161  1.00 67.27  ? 242 ASN B O   1 
ATOM   3886 C CB  . ASN B 1 242 ? 39.362 -12.400 18.419  1.00 70.07  ? 242 ASN B CB  1 
ATOM   3887 C CG  . ASN B 1 242 ? 40.209 -12.726 19.618  1.00 81.12  ? 242 ASN B CG  1 
ATOM   3888 O OD1 . ASN B 1 242 ? 39.821 -12.416 20.739  1.00 109.88 ? 242 ASN B OD1 1 
ATOM   3889 N ND2 . ASN B 1 242 ? 41.355 -13.350 19.391  1.00 86.78  ? 242 ASN B ND2 1 
ATOM   3890 N N   . LEU B 1 243 ? 39.875 -9.533  16.864  1.00 58.96  ? 243 LEU B N   1 
ATOM   3891 C CA  . LEU B 1 243 ? 40.402 -9.202  15.508  1.00 61.03  ? 243 LEU B CA  1 
ATOM   3892 C C   . LEU B 1 243 ? 40.897 -10.479 14.811  1.00 52.45  ? 243 LEU B C   1 
ATOM   3893 O O   . LEU B 1 243 ? 40.805 -10.556 13.574  1.00 51.46  ? 243 LEU B O   1 
ATOM   3894 C CB  . LEU B 1 243 ? 41.521 -8.163  15.594  1.00 66.63  ? 243 LEU B CB  1 
ATOM   3895 C CG  . LEU B 1 243 ? 41.074 -6.722  15.362  1.00 80.33  ? 243 LEU B CG  1 
ATOM   3896 C CD1 . LEU B 1 243 ? 40.163 -6.245  16.489  1.00 88.28  ? 243 LEU B CD1 1 
ATOM   3897 C CD2 . LEU B 1 243 ? 42.281 -5.810  15.230  1.00 82.35  ? 243 LEU B CD2 1 
ATOM   3898 N N   . TYR B 1 244 ? 41.409 -11.445 15.561  1.00 49.85  ? 244 TYR B N   1 
ATOM   3899 C CA  . TYR B 1 244 ? 41.976 -12.697 15.002  1.00 55.15  ? 244 TYR B CA  1 
ATOM   3900 C C   . TYR B 1 244 ? 40.848 -13.622 14.498  1.00 54.66  ? 244 TYR B C   1 
ATOM   3901 O O   . TYR B 1 244 ? 40.957 -14.170 13.409  1.00 51.55  ? 244 TYR B O   1 
ATOM   3902 C CB  . TYR B 1 244 ? 42.881 -13.360 16.040  1.00 52.45  ? 244 TYR B CB  1 
ATOM   3903 C CG  . TYR B 1 244 ? 43.674 -14.525 15.509  1.00 56.17  ? 244 TYR B CG  1 
ATOM   3904 C CD1 . TYR B 1 244 ? 44.230 -14.484 14.244  1.00 55.96  ? 244 TYR B CD1 1 
ATOM   3905 C CD2 . TYR B 1 244 ? 43.887 -15.661 16.276  1.00 58.05  ? 244 TYR B CD2 1 
ATOM   3906 C CE1 . TYR B 1 244 ? 44.953 -15.550 13.741  1.00 60.79  ? 244 TYR B CE1 1 
ATOM   3907 C CE2 . TYR B 1 244 ? 44.612 -16.734 15.789  1.00 54.51  ? 244 TYR B CE2 1 
ATOM   3908 C CZ  . TYR B 1 244 ? 45.148 -16.672 14.518  1.00 55.00  ? 244 TYR B CZ  1 
ATOM   3909 O OH  . TYR B 1 244 ? 45.860 -17.706 14.003  1.00 71.01  ? 244 TYR B OH  1 
ATOM   3910 N N   . SER B 1 245 ? 39.784 -13.798 15.272  1.00 53.72  ? 245 SER B N   1 
ATOM   3911 C CA  . SER B 1 245 ? 38.547 -14.478 14.830  1.00 54.45  ? 245 SER B CA  1 
ATOM   3912 C C   . SER B 1 245 ? 38.022 -13.772 13.573  1.00 55.29  ? 245 SER B C   1 
ATOM   3913 O O   . SER B 1 245 ? 37.703 -14.484 12.622  1.00 52.47  ? 245 SER B O   1 
ATOM   3914 C CB  . SER B 1 245 ? 37.529 -14.513 15.930  1.00 56.92  ? 245 SER B CB  1 
ATOM   3915 O OG  . SER B 1 245 ? 36.281 -14.990 15.447  1.00 72.75  ? 245 SER B OG  1 
ATOM   3916 N N   . LEU B 1 246 ? 37.945 -12.432 13.560  1.00 53.60  ? 246 LEU B N   1 
ATOM   3917 C CA  . LEU B 1 246 ? 37.454 -11.658 12.388  1.00 50.81  ? 246 LEU B CA  1 
ATOM   3918 C C   . LEU B 1 246 ? 38.343 -11.929 11.151  1.00 50.81  ? 246 LEU B C   1 
ATOM   3919 O O   . LEU B 1 246 ? 37.780 -12.143 10.068  1.00 54.95  ? 246 LEU B O   1 
ATOM   3920 C CB  . LEU B 1 246 ? 37.366 -10.165 12.715  1.00 56.88  ? 246 LEU B CB  1 
ATOM   3921 C CG  . LEU B 1 246 ? 36.931 -9.264  11.543  1.00 65.69  ? 246 LEU B CG  1 
ATOM   3922 C CD1 . LEU B 1 246 ? 35.476 -9.504  11.163  1.00 60.50  ? 246 LEU B CD1 1 
ATOM   3923 C CD2 . LEU B 1 246 ? 37.135 -7.785  11.856  1.00 62.31  ? 246 LEU B CD2 1 
ATOM   3924 N N   . CYS B 1 247 ? 39.670 -11.975 11.275  1.00 43.66  ? 247 CYS B N   1 
ATOM   3925 C CA  . CYS B 1 247 ? 40.569 -12.351 10.150  1.00 46.75  ? 247 CYS B CA  1 
ATOM   3926 C C   . CYS B 1 247 ? 40.364 -13.799 9.697   1.00 48.00  ? 247 CYS B C   1 
ATOM   3927 O O   . CYS B 1 247 ? 40.482 -14.039 8.496   1.00 55.72  ? 247 CYS B O   1 
ATOM   3928 C CB  . CYS B 1 247 ? 42.034 -12.172 10.507  1.00 50.59  ? 247 CYS B CB  1 
ATOM   3929 S SG  . CYS B 1 247 ? 42.443 -10.439 10.789  1.00 59.19  ? 247 CYS B SG  1 
ATOM   3930 N N   . LYS B 1 248 ? 40.109 -14.737 10.610  1.00 55.12  ? 248 LYS B N   1 
ATOM   3931 C CA  . LYS B 1 248 ? 39.902 -16.175 10.280  1.00 54.50  ? 248 LYS B CA  1 
ATOM   3932 C C   . LYS B 1 248 ? 38.635 -16.329 9.437   1.00 52.41  ? 248 LYS B C   1 
ATOM   3933 O O   . LYS B 1 248 ? 38.674 -17.116 8.478   1.00 61.32  ? 248 LYS B O   1 
ATOM   3934 C CB  . LYS B 1 248 ? 39.798 -17.043 11.537  1.00 58.34  ? 248 LYS B CB  1 
ATOM   3935 C CG  . LYS B 1 248 ? 41.108 -17.310 12.267  1.00 69.99  ? 248 LYS B CG  1 
ATOM   3936 C CD  . LYS B 1 248 ? 40.900 -18.053 13.591  1.00 80.88  ? 248 LYS B CD  1 
ATOM   3937 C CE  . LYS B 1 248 ? 42.148 -18.115 14.441  1.00 84.37  ? 248 LYS B CE  1 
ATOM   3938 N NZ  . LYS B 1 248 ? 41.923 -18.844 15.709  1.00 86.49  ? 248 LYS B NZ  1 
ATOM   3939 N N   . LYS B 1 249 ? 37.554 -15.639 9.816   1.00 52.40  ? 249 LYS B N   1 
ATOM   3940 C CA  . LYS B 1 249 ? 36.236 -15.680 9.125   1.00 57.38  ? 249 LYS B CA  1 
ATOM   3941 C C   . LYS B 1 249 ? 36.354 -15.061 7.722   1.00 50.79  ? 249 LYS B C   1 
ATOM   3942 O O   . LYS B 1 249 ? 35.750 -15.607 6.799   1.00 47.91  ? 249 LYS B O   1 
ATOM   3943 C CB  . LYS B 1 249 ? 35.162 -15.006 9.990   1.00 57.95  ? 249 LYS B CB  1 
ATOM   3944 C CG  . LYS B 1 249 ? 34.684 -15.872 11.152  1.00 65.39  ? 249 LYS B CG  1 
ATOM   3945 C CD  . LYS B 1 249 ? 34.060 -15.100 12.282  1.00 72.88  ? 249 LYS B CD  1 
ATOM   3946 C CE  . LYS B 1 249 ? 32.603 -15.423 12.541  1.00 83.13  ? 249 LYS B CE  1 
ATOM   3947 N NZ  . LYS B 1 249 ? 31.958 -14.373 13.374  1.00 85.82  ? 249 LYS B NZ  1 
ATOM   3948 N N   . ILE B 1 250 ? 37.088 -13.958 7.571   1.00 51.47  ? 250 ILE B N   1 
ATOM   3949 C CA  . ILE B 1 250 ? 37.317 -13.274 6.262   1.00 53.86  ? 250 ILE B CA  1 
ATOM   3950 C C   . ILE B 1 250 ? 38.069 -14.214 5.313   1.00 58.46  ? 250 ILE B C   1 
ATOM   3951 O O   . ILE B 1 250 ? 37.589 -14.381 4.185   1.00 66.42  ? 250 ILE B O   1 
ATOM   3952 C CB  . ILE B 1 250 ? 38.042 -11.937 6.470   1.00 49.07  ? 250 ILE B CB  1 
ATOM   3953 C CG1 . ILE B 1 250 ? 37.086 -10.923 7.095   1.00 45.60  ? 250 ILE B CG1 1 
ATOM   3954 C CG2 . ILE B 1 250 ? 38.643 -11.439 5.168   1.00 45.89  ? 250 ILE B CG2 1 
ATOM   3955 C CD1 . ILE B 1 250 ? 37.737 -9.652  7.535   1.00 46.97  ? 250 ILE B CD1 1 
ATOM   3956 N N   . GLU B 1 251 ? 39.169 -14.814 5.778   1.00 60.72  ? 251 GLU B N   1 
ATOM   3957 C CA  . GLU B 1 251 ? 39.986 -15.832 5.063   1.00 62.60  ? 251 GLU B CA  1 
ATOM   3958 C C   . GLU B 1 251 ? 39.072 -16.895 4.441   1.00 63.78  ? 251 GLU B C   1 
ATOM   3959 O O   . GLU B 1 251 ? 39.255 -17.218 3.246   1.00 77.89  ? 251 GLU B O   1 
ATOM   3960 C CB  . GLU B 1 251 ? 40.954 -16.497 6.046   1.00 74.09  ? 251 GLU B CB  1 
ATOM   3961 C CG  . GLU B 1 251 ? 42.270 -16.949 5.433   1.00 85.17  ? 251 GLU B CG  1 
ATOM   3962 C CD  . GLU B 1 251 ? 43.033 -17.977 6.261   1.00 95.58  ? 251 GLU B CD  1 
ATOM   3963 O OE1 . GLU B 1 251 ? 44.018 -17.581 6.941   1.00 86.94  ? 251 GLU B OE1 1 
ATOM   3964 O OE2 . GLU B 1 251 ? 42.651 -19.179 6.213   1.00 92.11  ? 251 GLU B OE2 1 
ATOM   3965 N N   . GLN B 1 252 ? 38.153 -17.435 5.244   1.00 58.79  ? 252 GLN B N   1 
ATOM   3966 C CA  . GLN B 1 252 ? 37.219 -18.539 4.893   1.00 58.80  ? 252 GLN B CA  1 
ATOM   3967 C C   . GLN B 1 252 ? 35.925 -18.009 4.246   1.00 54.62  ? 252 GLN B C   1 
ATOM   3968 O O   . GLN B 1 252 ? 35.032 -18.841 4.006   1.00 54.07  ? 252 GLN B O   1 
ATOM   3969 C CB  . GLN B 1 252 ? 36.795 -19.299 6.158   1.00 59.22  ? 252 GLN B CB  1 
ATOM   3970 C CG  . GLN B 1 252 ? 37.833 -20.250 6.728   1.00 61.68  ? 252 GLN B CG  1 
ATOM   3971 C CD  . GLN B 1 252 ? 37.263 -21.109 7.837   1.00 68.61  ? 252 GLN B CD  1 
ATOM   3972 O OE1 . GLN B 1 252 ? 36.058 -21.154 8.088   1.00 73.15  ? 252 GLN B OE1 1 
ATOM   3973 N NE2 . GLN B 1 252 ? 38.140 -21.805 8.538   1.00 77.90  ? 252 GLN B NE2 1 
ATOM   3974 N N   . CYS B 1 253 ? 35.785 -16.691 4.045   1.00 49.30  ? 253 CYS B N   1 
ATOM   3975 C CA  . CYS B 1 253 ? 34.498 -16.015 3.716   1.00 50.31  ? 253 CYS B CA  1 
ATOM   3976 C C   . CYS B 1 253 ? 33.350 -16.687 4.485   1.00 48.37  ? 253 CYS B C   1 
ATOM   3977 O O   . CYS B 1 253 ? 32.356 -17.094 3.874   1.00 47.34  ? 253 CYS B O   1 
ATOM   3978 C CB  . CYS B 1 253 ? 34.232 -15.994 2.209   1.00 52.85  ? 253 CYS B CB  1 
ATOM   3979 S SG  . CYS B 1 253 ? 35.421 -14.967 1.304   1.00 58.17  ? 253 CYS B SG  1 
ATOM   3980 N N   . ASP B 1 254 ? 33.482 -16.766 5.805   1.00 53.49  ? 254 ASP B N   1 
ATOM   3981 C CA  . ASP B 1 254 ? 32.511 -17.432 6.708   1.00 52.82  ? 254 ASP B CA  1 
ATOM   3982 C C   . ASP B 1 254 ? 31.523 -16.372 7.208   1.00 48.00  ? 254 ASP B C   1 
ATOM   3983 O O   . ASP B 1 254 ? 31.819 -15.745 8.234   1.00 49.25  ? 254 ASP B O   1 
ATOM   3984 C CB  . ASP B 1 254 ? 33.275 -18.145 7.830   1.00 58.58  ? 254 ASP B CB  1 
ATOM   3985 C CG  . ASP B 1 254 ? 32.408 -18.787 8.900   1.00 59.29  ? 254 ASP B CG  1 
ATOM   3986 O OD1 . ASP B 1 254 ? 31.178 -18.926 8.678   1.00 53.92  ? 254 ASP B OD1 1 
ATOM   3987 O OD2 . ASP B 1 254 ? 32.977 -19.140 9.953   1.00 60.73  ? 254 ASP B OD2 1 
ATOM   3988 N N   . TYR B 1 255 ? 30.417 -16.170 6.487   1.00 43.91  ? 255 TYR B N   1 
ATOM   3989 C CA  . TYR B 1 255 ? 29.301 -15.256 6.849   1.00 46.06  ? 255 TYR B CA  1 
ATOM   3990 C C   . TYR B 1 255 ? 28.006 -16.061 6.906   1.00 44.43  ? 255 TYR B C   1 
ATOM   3991 O O   . TYR B 1 255 ? 27.860 -17.071 6.240   1.00 46.66  ? 255 TYR B O   1 
ATOM   3992 C CB  . TYR B 1 255 ? 29.204 -14.055 5.892   1.00 45.10  ? 255 TYR B CB  1 
ATOM   3993 C CG  . TYR B 1 255 ? 29.025 -14.354 4.421   1.00 42.79  ? 255 TYR B CG  1 
ATOM   3994 C CD1 . TYR B 1 255 ? 27.769 -14.482 3.848   1.00 48.18  ? 255 TYR B CD1 1 
ATOM   3995 C CD2 . TYR B 1 255 ? 30.118 -14.478 3.582   1.00 43.93  ? 255 TYR B CD2 1 
ATOM   3996 C CE1 . TYR B 1 255 ? 27.602 -14.740 2.492   1.00 45.67  ? 255 TYR B CE1 1 
ATOM   3997 C CE2 . TYR B 1 255 ? 29.972 -14.727 2.226   1.00 44.90  ? 255 TYR B CE2 1 
ATOM   3998 C CZ  . TYR B 1 255 ? 28.709 -14.857 1.672   1.00 45.17  ? 255 TYR B CZ  1 
ATOM   3999 O OH  . TYR B 1 255 ? 28.574 -15.137 0.339   1.00 47.89  ? 255 TYR B OH  1 
ATOM   4000 N N   . PRO B 1 256 ? 27.027 -15.660 7.731   1.00 45.08  ? 256 PRO B N   1 
ATOM   4001 C CA  . PRO B 1 256 ? 25.715 -16.303 7.708   1.00 52.62  ? 256 PRO B CA  1 
ATOM   4002 C C   . PRO B 1 256 ? 25.046 -16.186 6.337   1.00 53.16  ? 256 PRO B C   1 
ATOM   4003 O O   . PRO B 1 256 ? 24.869 -15.084 5.831   1.00 51.65  ? 256 PRO B O   1 
ATOM   4004 C CB  . PRO B 1 256 ? 24.907 -15.525 8.762   1.00 47.76  ? 256 PRO B CB  1 
ATOM   4005 C CG  . PRO B 1 256 ? 25.961 -14.891 9.655   1.00 45.68  ? 256 PRO B CG  1 
ATOM   4006 C CD  . PRO B 1 256 ? 27.137 -14.608 8.748   1.00 44.87  ? 256 PRO B CD  1 
ATOM   4007 N N   . PRO B 1 257 ? 24.638 -17.301 5.685   1.00 60.37  ? 257 PRO B N   1 
ATOM   4008 C CA  . PRO B 1 257 ? 23.904 -17.207 4.424   1.00 58.16  ? 257 PRO B CA  1 
ATOM   4009 C C   . PRO B 1 257 ? 22.645 -16.351 4.577   1.00 57.51  ? 257 PRO B C   1 
ATOM   4010 O O   . PRO B 1 257 ? 22.041 -16.383 5.629   1.00 67.53  ? 257 PRO B O   1 
ATOM   4011 C CB  . PRO B 1 257 ? 23.549 -18.661 4.093   1.00 60.16  ? 257 PRO B CB  1 
ATOM   4012 C CG  . PRO B 1 257 ? 24.603 -19.468 4.819   1.00 62.25  ? 257 PRO B CG  1 
ATOM   4013 C CD  . PRO B 1 257 ? 24.871 -18.696 6.094   1.00 61.50  ? 257 PRO B CD  1 
ATOM   4014 N N   . LEU B 1 258 ? 22.291 -15.594 3.542   1.00 58.67  ? 258 LEU B N   1 
ATOM   4015 C CA  . LEU B 1 258 ? 20.999 -14.861 3.485   1.00 66.91  ? 258 LEU B CA  1 
ATOM   4016 C C   . LEU B 1 258 ? 19.843 -15.854 3.352   1.00 69.45  ? 258 LEU B C   1 
ATOM   4017 O O   . LEU B 1 258 ? 20.011 -16.911 2.739   1.00 65.60  ? 258 LEU B O   1 
ATOM   4018 C CB  . LEU B 1 258 ? 21.015 -13.899 2.297   1.00 68.47  ? 258 LEU B CB  1 
ATOM   4019 C CG  . LEU B 1 258 ? 21.952 -12.704 2.434   1.00 68.45  ? 258 LEU B CG  1 
ATOM   4020 C CD1 . LEU B 1 258 ? 22.092 -11.969 1.104   1.00 64.36  ? 258 LEU B CD1 1 
ATOM   4021 C CD2 . LEU B 1 258 ? 21.452 -11.774 3.530   1.00 63.61  ? 258 LEU B CD2 1 
ATOM   4022 N N   . PRO B 1 259 ? 18.632 -15.520 3.872   1.00 71.99  ? 259 PRO B N   1 
ATOM   4023 C CA  . PRO B 1 259 ? 17.451 -16.383 3.732   1.00 68.50  ? 259 PRO B CA  1 
ATOM   4024 C C   . PRO B 1 259 ? 16.937 -16.520 2.283   1.00 66.90  ? 259 PRO B C   1 
ATOM   4025 O O   . PRO B 1 259 ? 16.453 -15.555 1.745   1.00 67.45  ? 259 PRO B O   1 
ATOM   4026 C CB  . PRO B 1 259 ? 16.383 -15.690 4.601   1.00 67.07  ? 259 PRO B CB  1 
ATOM   4027 C CG  . PRO B 1 259 ? 17.137 -14.687 5.444   1.00 70.82  ? 259 PRO B CG  1 
ATOM   4028 C CD  . PRO B 1 259 ? 18.327 -14.281 4.608   1.00 70.11  ? 259 PRO B CD  1 
ATOM   4029 N N   . SER B 1 260 ? 17.014 -17.713 1.681   1.00 73.57  ? 260 SER B N   1 
ATOM   4030 C CA  . SER B 1 260 ? 16.612 -17.956 0.267   1.00 72.13  ? 260 SER B CA  1 
ATOM   4031 C C   . SER B 1 260 ? 15.095 -17.773 0.081   1.00 72.07  ? 260 SER B C   1 
ATOM   4032 O O   . SER B 1 260 ? 14.644 -17.663 -1.086  1.00 60.91  ? 260 SER B O   1 
ATOM   4033 C CB  . SER B 1 260 ? 17.077 -19.300 -0.210  1.00 73.96  ? 260 SER B CB  1 
ATOM   4034 O OG  . SER B 1 260 ? 16.642 -20.325 0.663   1.00 88.00  ? 260 SER B OG  1 
ATOM   4035 N N   . ASP B 1 261 ? 14.321 -17.685 1.166   1.00 74.89  ? 261 ASP B N   1 
ATOM   4036 C CA  . ASP B 1 261 ? 12.864 -17.399 1.061   1.00 84.49  ? 261 ASP B CA  1 
ATOM   4037 C C   . ASP B 1 261 ? 12.642 -15.906 0.738   1.00 79.07  ? 261 ASP B C   1 
ATOM   4038 O O   . ASP B 1 261 ? 11.649 -15.609 0.055   1.00 82.14  ? 261 ASP B O   1 
ATOM   4039 C CB  . ASP B 1 261 ? 12.082 -17.929 2.273   1.00 92.88  ? 261 ASP B CB  1 
ATOM   4040 C CG  . ASP B 1 261 ? 12.676 -17.607 3.636   1.00 102.60 ? 261 ASP B CG  1 
ATOM   4041 O OD1 . ASP B 1 261 ? 13.896 -17.818 3.815   1.00 98.54  ? 261 ASP B OD1 1 
ATOM   4042 O OD2 . ASP B 1 261 ? 11.907 -17.163 4.517   1.00 112.94 ? 261 ASP B OD2 1 
ATOM   4043 N N   . HIS B 1 262 ? 13.528 -14.996 1.158   1.00 74.07  ? 262 HIS B N   1 
ATOM   4044 C CA  . HIS B 1 262 ? 13.344 -13.516 1.043   1.00 73.42  ? 262 HIS B CA  1 
ATOM   4045 C C   . HIS B 1 262 ? 14.140 -12.914 -0.130  1.00 66.58  ? 262 HIS B C   1 
ATOM   4046 O O   . HIS B 1 262 ? 13.742 -11.845 -0.612  1.00 69.66  ? 262 HIS B O   1 
ATOM   4047 C CB  . HIS B 1 262 ? 13.707 -12.825 2.367   1.00 74.54  ? 262 HIS B CB  1 
ATOM   4048 C CG  . HIS B 1 262 ? 12.741 -13.100 3.472   1.00 85.02  ? 262 HIS B CG  1 
ATOM   4049 N ND1 . HIS B 1 262 ? 11.701 -12.236 3.780   1.00 93.12  ? 262 HIS B ND1 1 
ATOM   4050 C CD2 . HIS B 1 262 ? 12.651 -14.128 4.345   1.00 83.94  ? 262 HIS B CD2 1 
ATOM   4051 C CE1 . HIS B 1 262 ? 11.013 -12.723 4.797   1.00 91.43  ? 262 HIS B CE1 1 
ATOM   4052 N NE2 . HIS B 1 262 ? 11.576 -13.884 5.160   1.00 93.95  ? 262 HIS B NE2 1 
ATOM   4053 N N   . TYR B 1 263 ? 15.228 -13.549 -0.568  1.00 58.44  ? 263 TYR B N   1 
ATOM   4054 C CA  . TYR B 1 263 ? 16.197 -12.969 -1.532  1.00 54.50  ? 263 TYR B CA  1 
ATOM   4055 C C   . TYR B 1 263 ? 16.554 -14.004 -2.606  1.00 53.93  ? 263 TYR B C   1 
ATOM   4056 O O   . TYR B 1 263 ? 17.034 -15.091 -2.261  1.00 50.53  ? 263 TYR B O   1 
ATOM   4057 C CB  . TYR B 1 263 ? 17.426 -12.429 -0.782  1.00 56.88  ? 263 TYR B CB  1 
ATOM   4058 C CG  . TYR B 1 263 ? 17.074 -11.338 0.203   1.00 55.45  ? 263 TYR B CG  1 
ATOM   4059 C CD1 . TYR B 1 263 ? 16.640 -10.095 -0.243  1.00 51.22  ? 263 TYR B CD1 1 
ATOM   4060 C CD2 . TYR B 1 263 ? 17.103 -11.559 1.571   1.00 49.17  ? 263 TYR B CD2 1 
ATOM   4061 C CE1 . TYR B 1 263 ? 16.267 -9.098  0.644   1.00 50.90  ? 263 TYR B CE1 1 
ATOM   4062 C CE2 . TYR B 1 263 ? 16.731 -10.570 2.470   1.00 51.19  ? 263 TYR B CE2 1 
ATOM   4063 C CZ  . TYR B 1 263 ? 16.304 -9.337  2.004   1.00 50.55  ? 263 TYR B CZ  1 
ATOM   4064 O OH  . TYR B 1 263 ? 15.934 -8.342  2.862   1.00 50.72  ? 263 TYR B OH  1 
ATOM   4065 N N   . SER B 1 264 ? 16.350 -13.627 -3.873  1.00 55.62  ? 264 SER B N   1 
ATOM   4066 C CA  . SER B 1 264 ? 16.616 -14.417 -5.099  1.00 53.74  ? 264 SER B CA  1 
ATOM   4067 C C   . SER B 1 264 ? 18.007 -15.047 -5.055  1.00 55.20  ? 264 SER B C   1 
ATOM   4068 O O   . SER B 1 264 ? 18.876 -14.581 -4.295  1.00 51.79  ? 264 SER B O   1 
ATOM   4069 C CB  . SER B 1 264 ? 16.433 -13.581 -6.353  1.00 56.93  ? 264 SER B CB  1 
ATOM   4070 O OG  . SER B 1 264 ? 17.489 -12.651 -6.548  1.00 56.81  ? 264 SER B OG  1 
ATOM   4071 N N   . GLU B 1 265 ? 18.171 -16.117 -5.827  1.00 61.96  ? 265 GLU B N   1 
ATOM   4072 C CA  . GLU B 1 265 ? 19.455 -16.825 -6.038  1.00 69.08  ? 265 GLU B CA  1 
ATOM   4073 C C   . GLU B 1 265 ? 20.437 -15.867 -6.747  1.00 68.03  ? 265 GLU B C   1 
ATOM   4074 O O   . GLU B 1 265 ? 21.665 -15.988 -6.511  1.00 68.41  ? 265 GLU B O   1 
ATOM   4075 C CB  . GLU B 1 265 ? 19.186 -18.110 -6.828  1.00 70.70  ? 265 GLU B CB  1 
ATOM   4076 C CG  . GLU B 1 265 ? 20.319 -19.123 -6.756  1.00 82.00  ? 265 GLU B CG  1 
ATOM   4077 C CD  . GLU B 1 265 ? 20.016 -20.450 -7.436  1.00 91.36  ? 265 GLU B CD  1 
ATOM   4078 O OE1 . GLU B 1 265 ? 20.973 -21.101 -7.919  1.00 90.33  ? 265 GLU B OE1 1 
ATOM   4079 O OE2 . GLU B 1 265 ? 18.824 -20.835 -7.481  1.00 94.47  ? 265 GLU B OE2 1 
ATOM   4080 N N   . GLU B 1 266 ? 19.928 -14.944 -7.574  1.00 63.23  ? 266 GLU B N   1 
ATOM   4081 C CA  . GLU B 1 266 ? 20.771 -14.004 -8.371  1.00 69.12  ? 266 GLU B CA  1 
ATOM   4082 C C   . GLU B 1 266 ? 21.308 -12.897 -7.443  1.00 57.97  ? 266 GLU B C   1 
ATOM   4083 O O   . GLU B 1 266 ? 22.470 -12.534 -7.621  1.00 55.27  ? 266 GLU B O   1 
ATOM   4084 C CB  . GLU B 1 266 ? 20.098 -13.484 -9.660  1.00 75.45  ? 266 GLU B CB  1 
ATOM   4085 C CG  . GLU B 1 266 ? 18.569 -13.503 -9.701  1.00 86.77  ? 266 GLU B CG  1 
ATOM   4086 C CD  . GLU B 1 266 ? 17.892 -14.803 -10.126 1.00 77.51  ? 266 GLU B CD  1 
ATOM   4087 O OE1 . GLU B 1 266 ? 17.136 -15.355 -9.314  1.00 76.11  ? 266 GLU B OE1 1 
ATOM   4088 O OE2 . GLU B 1 266 ? 18.101 -15.249 -11.269 1.00 79.81  ? 266 GLU B OE2 1 
ATOM   4089 N N   . LEU B 1 267 ? 20.558 -12.431 -6.441  1.00 46.60  ? 267 LEU B N   1 
ATOM   4090 C CA  . LEU B 1 267 ? 21.138 -11.560 -5.388  1.00 49.16  ? 267 LEU B CA  1 
ATOM   4091 C C   . LEU B 1 267 ? 22.222 -12.337 -4.613  1.00 51.39  ? 267 LEU B C   1 
ATOM   4092 O O   . LEU B 1 267 ? 23.368 -11.809 -4.464  1.00 46.25  ? 267 LEU B O   1 
ATOM   4093 C CB  . LEU B 1 267 ? 20.036 -11.049 -4.457  1.00 52.20  ? 267 LEU B CB  1 
ATOM   4094 C CG  . LEU B 1 267 ? 20.508 -9.993  -3.451  1.00 52.32  ? 267 LEU B CG  1 
ATOM   4095 C CD1 . LEU B 1 267 ? 19.359 -9.109  -3.008  1.00 52.65  ? 267 LEU B CD1 1 
ATOM   4096 C CD2 . LEU B 1 267 ? 21.178 -10.627 -2.235  1.00 47.00  ? 267 LEU B CD2 1 
ATOM   4097 N N   . ARG B 1 268 ? 21.892 -13.539 -4.127  1.00 49.62  ? 268 ARG B N   1 
ATOM   4098 C CA  . ARG B 1 268 ? 22.759 -14.323 -3.205  1.00 47.85  ? 268 ARG B CA  1 
ATOM   4099 C C   . ARG B 1 268 ? 24.036 -14.697 -3.947  1.00 47.26  ? 268 ARG B C   1 
ATOM   4100 O O   . ARG B 1 268 ? 25.096 -14.710 -3.313  1.00 57.82  ? 268 ARG B O   1 
ATOM   4101 C CB  . ARG B 1 268 ? 22.015 -15.542 -2.648  1.00 50.35  ? 268 ARG B CB  1 
ATOM   4102 C CG  . ARG B 1 268 ? 21.008 -15.185 -1.561  1.00 52.57  ? 268 ARG B CG  1 
ATOM   4103 C CD  . ARG B 1 268 ? 20.362 -16.405 -0.908  1.00 59.25  ? 268 ARG B CD  1 
ATOM   4104 N NE  . ARG B 1 268 ? 19.287 -16.970 -1.720  1.00 55.76  ? 268 ARG B NE  1 
ATOM   4105 C CZ  . ARG B 1 268 ? 19.349 -18.084 -2.445  1.00 55.66  ? 268 ARG B CZ  1 
ATOM   4106 N NH1 . ARG B 1 268 ? 20.432 -18.845 -2.464  1.00 56.10  ? 268 ARG B NH1 1 
ATOM   4107 N NH2 . ARG B 1 268 ? 18.296 -18.437 -3.160  1.00 67.17  ? 268 ARG B NH2 1 
ATOM   4108 N N   . GLN B 1 269 ? 23.941 -14.938 -5.249  1.00 49.19  ? 269 GLN B N   1 
ATOM   4109 C CA  . GLN B 1 269 ? 25.100 -15.298 -6.107  1.00 59.82  ? 269 GLN B CA  1 
ATOM   4110 C C   . GLN B 1 269 ? 26.004 -14.074 -6.322  1.00 54.52  ? 269 GLN B C   1 
ATOM   4111 O O   . GLN B 1 269 ? 27.250 -14.235 -6.351  1.00 49.28  ? 269 GLN B O   1 
ATOM   4112 C CB  . GLN B 1 269 ? 24.623 -15.844 -7.459  1.00 70.30  ? 269 GLN B CB  1 
ATOM   4113 C CG  . GLN B 1 269 ? 24.858 -17.334 -7.624  1.00 85.68  ? 269 GLN B CG  1 
ATOM   4114 C CD  . GLN B 1 269 ? 26.299 -17.580 -7.993  1.00 92.18  ? 269 GLN B CD  1 
ATOM   4115 O OE1 . GLN B 1 269 ? 26.673 -17.491 -9.162  1.00 109.26 ? 269 GLN B OE1 1 
ATOM   4116 N NE2 . GLN B 1 269 ? 27.123 -17.864 -6.994  1.00 86.85  ? 269 GLN B NE2 1 
ATOM   4117 N N   . LEU B 1 270 ? 25.412 -12.913 -6.605  1.00 51.96  ? 270 LEU B N   1 
ATOM   4118 C CA  . LEU B 1 270 ? 26.183 -11.661 -6.837  1.00 52.79  ? 270 LEU B CA  1 
ATOM   4119 C C   . LEU B 1 270 ? 27.016 -11.390 -5.579  1.00 53.58  ? 270 LEU B C   1 
ATOM   4120 O O   . LEU B 1 270 ? 28.236 -11.169 -5.729  1.00 52.34  ? 270 LEU B O   1 
ATOM   4121 C CB  . LEU B 1 270 ? 25.231 -10.501 -7.139  1.00 53.06  ? 270 LEU B CB  1 
ATOM   4122 C CG  . LEU B 1 270 ? 25.910 -9.184  -7.496  1.00 51.97  ? 270 LEU B CG  1 
ATOM   4123 C CD1 . LEU B 1 270 ? 26.744 -9.336  -8.760  1.00 53.64  ? 270 LEU B CD1 1 
ATOM   4124 C CD2 . LEU B 1 270 ? 24.875 -8.084  -7.659  1.00 51.93  ? 270 LEU B CD2 1 
ATOM   4125 N N   . VAL B 1 271 ? 26.385 -11.503 -4.398  1.00 48.37  ? 271 VAL B N   1 
ATOM   4126 C CA  . VAL B 1 271 ? 27.064 -11.400 -3.078  1.00 48.23  ? 271 VAL B CA  1 
ATOM   4127 C C   . VAL B 1 271 ? 28.219 -12.410 -3.036  1.00 45.94  ? 271 VAL B C   1 
ATOM   4128 O O   . VAL B 1 271 ? 29.341 -11.989 -2.729  1.00 43.17  ? 271 VAL B O   1 
ATOM   4129 C CB  . VAL B 1 271 ? 26.086 -11.566 -1.904  1.00 47.42  ? 271 VAL B CB  1 
ATOM   4130 C CG1 . VAL B 1 271 ? 26.843 -11.684 -0.598  1.00 47.23  ? 271 VAL B CG1 1 
ATOM   4131 C CG2 . VAL B 1 271 ? 25.092 -10.417 -1.841  1.00 46.03  ? 271 VAL B CG2 1 
ATOM   4132 N N   . ASN B 1 272 ? 27.977 -13.671 -3.397  1.00 46.43  ? 272 ASN B N   1 
ATOM   4133 C CA  . ASN B 1 272 ? 29.013 -14.735 -3.328  1.00 46.39  ? 272 ASN B CA  1 
ATOM   4134 C C   . ASN B 1 272 ? 30.157 -14.450 -4.313  1.00 45.09  ? 272 ASN B C   1 
ATOM   4135 O O   . ASN B 1 272 ? 31.336 -14.737 -3.972  1.00 46.57  ? 272 ASN B O   1 
ATOM   4136 C CB  . ASN B 1 272 ? 28.438 -16.134 -3.546  1.00 47.96  ? 272 ASN B CB  1 
ATOM   4137 C CG  . ASN B 1 272 ? 29.453 -17.205 -3.206  1.00 52.45  ? 272 ASN B CG  1 
ATOM   4138 O OD1 . ASN B 1 272 ? 29.990 -17.227 -2.099  1.00 52.15  ? 272 ASN B OD1 1 
ATOM   4139 N ND2 . ASN B 1 272 ? 29.741 -18.082 -4.154  1.00 58.42  ? 272 ASN B ND2 1 
ATOM   4140 N N   . MET B 1 273 ? 29.858 -13.909 -5.494  1.00 41.97  ? 273 MET B N   1 
ATOM   4141 C CA  . MET B 1 273 ? 30.912 -13.590 -6.487  1.00 43.21  ? 273 MET B CA  1 
ATOM   4142 C C   . MET B 1 273 ? 31.774 -12.449 -5.946  1.00 43.01  ? 273 MET B C   1 
ATOM   4143 O O   . MET B 1 273 ? 32.985 -12.432 -6.216  1.00 44.88  ? 273 MET B O   1 
ATOM   4144 C CB  . MET B 1 273 ? 30.310 -13.177 -7.835  1.00 52.98  ? 273 MET B CB  1 
ATOM   4145 C CG  . MET B 1 273 ? 29.929 -14.346 -8.728  1.00 57.29  ? 273 MET B CG  1 
ATOM   4146 S SD  . MET B 1 273 ? 29.016 -13.825 -10.208 1.00 64.37  ? 273 MET B SD  1 
ATOM   4147 C CE  . MET B 1 273 ? 27.339 -13.937 -9.601  1.00 68.21  ? 273 MET B CE  1 
ATOM   4148 N N   . CYS B 1 274 ? 31.172 -11.495 -5.236  1.00 42.38  ? 274 CYS B N   1 
ATOM   4149 C CA  . CYS B 1 274 ? 31.876 -10.265 -4.807  1.00 43.01  ? 274 CYS B CA  1 
ATOM   4150 C C   . CYS B 1 274 ? 32.720 -10.577 -3.576  1.00 43.68  ? 274 CYS B C   1 
ATOM   4151 O O   . CYS B 1 274 ? 33.867 -10.070 -3.500  1.00 49.50  ? 274 CYS B O   1 
ATOM   4152 C CB  . CYS B 1 274 ? 30.896 -9.125  -4.575  1.00 45.05  ? 274 CYS B CB  1 
ATOM   4153 S SG  . CYS B 1 274 ? 30.191 -8.518  -6.131  1.00 48.24  ? 274 CYS B SG  1 
ATOM   4154 N N   . ILE B 1 275 ? 32.193 -11.398 -2.673  1.00 41.58  ? 275 ILE B N   1 
ATOM   4155 C CA  . ILE B 1 275 ? 32.884 -11.773 -1.407  1.00 48.20  ? 275 ILE B CA  1 
ATOM   4156 C C   . ILE B 1 275 ? 33.723 -13.038 -1.680  1.00 44.48  ? 275 ILE B C   1 
ATOM   4157 O O   . ILE B 1 275 ? 33.356 -14.133 -1.268  1.00 42.57  ? 275 ILE B O   1 
ATOM   4158 C CB  . ILE B 1 275 ? 31.858 -11.881 -0.267  1.00 51.79  ? 275 ILE B CB  1 
ATOM   4159 C CG1 . ILE B 1 275 ? 31.129 -10.546 -0.099  1.00 52.86  ? 275 ILE B CG1 1 
ATOM   4160 C CG2 . ILE B 1 275 ? 32.516 -12.350 1.028   1.00 55.48  ? 275 ILE B CG2 1 
ATOM   4161 C CD1 . ILE B 1 275 ? 30.096 -10.533 1.017   1.00 59.63  ? 275 ILE B CD1 1 
ATOM   4162 N N   . ASN B 1 276 ? 34.805 -12.856 -2.432  1.00 43.67  ? 276 ASN B N   1 
ATOM   4163 C CA  . ASN B 1 276 ? 35.731 -13.908 -2.887  1.00 41.81  ? 276 ASN B CA  1 
ATOM   4164 C C   . ASN B 1 276 ? 37.114 -13.502 -2.421  1.00 44.73  ? 276 ASN B C   1 
ATOM   4165 O O   . ASN B 1 276 ? 37.516 -12.377 -2.641  1.00 48.40  ? 276 ASN B O   1 
ATOM   4166 C CB  . ASN B 1 276 ? 35.695 -14.074 -4.399  1.00 42.83  ? 276 ASN B CB  1 
ATOM   4167 C CG  . ASN B 1 276 ? 36.453 -15.299 -4.882  1.00 46.12  ? 276 ASN B CG  1 
ATOM   4168 O OD1 . ASN B 1 276 ? 37.685 -15.372 -4.797  1.00 42.47  ? 276 ASN B OD1 1 
ATOM   4169 N ND2 . ASN B 1 276 ? 35.726 -16.250 -5.444  1.00 45.82  ? 276 ASN B ND2 1 
ATOM   4170 N N   . PRO B 1 277 ? 37.891 -14.383 -1.765  1.00 46.54  ? 277 PRO B N   1 
ATOM   4171 C CA  . PRO B 1 277 ? 39.189 -13.973 -1.237  1.00 47.00  ? 277 PRO B CA  1 
ATOM   4172 C C   . PRO B 1 277 ? 40.200 -13.478 -2.289  1.00 45.98  ? 277 PRO B C   1 
ATOM   4173 O O   . PRO B 1 277 ? 41.066 -12.696 -1.944  1.00 49.26  ? 277 PRO B O   1 
ATOM   4174 C CB  . PRO B 1 277 ? 39.710 -15.234 -0.539  1.00 44.75  ? 277 PRO B CB  1 
ATOM   4175 C CG  . PRO B 1 277 ? 38.467 -16.077 -0.304  1.00 50.22  ? 277 PRO B CG  1 
ATOM   4176 C CD  . PRO B 1 277 ? 37.567 -15.789 -1.483  1.00 45.91  ? 277 PRO B CD  1 
ATOM   4177 N N   . ASP B 1 278 ? 40.078 -13.928 -3.536  1.00 45.93  ? 278 ASP B N   1 
ATOM   4178 C CA  . ASP B 1 278 ? 41.008 -13.555 -4.631  1.00 49.70  ? 278 ASP B CA  1 
ATOM   4179 C C   . ASP B 1 278 ? 40.412 -12.372 -5.390  1.00 50.44  ? 278 ASP B C   1 
ATOM   4180 O O   . ASP B 1 278 ? 39.352 -12.496 -6.015  1.00 46.04  ? 278 ASP B O   1 
ATOM   4181 C CB  . ASP B 1 278 ? 41.272 -14.763 -5.521  1.00 54.91  ? 278 ASP B CB  1 
ATOM   4182 C CG  . ASP B 1 278 ? 42.373 -14.576 -6.537  1.00 57.68  ? 278 ASP B CG  1 
ATOM   4183 O OD1 . ASP B 1 278 ? 42.971 -13.473 -6.581  1.00 63.15  ? 278 ASP B OD1 1 
ATOM   4184 O OD2 . ASP B 1 278 ? 42.627 -15.551 -7.265  1.00 66.28  ? 278 ASP B OD2 1 
ATOM   4185 N N   . PRO B 1 279 ? 41.073 -11.192 -5.334  1.00 51.60  ? 279 PRO B N   1 
ATOM   4186 C CA  . PRO B 1 279 ? 40.650 -10.018 -6.093  1.00 53.11  ? 279 PRO B CA  1 
ATOM   4187 C C   . PRO B 1 279 ? 40.467 -10.305 -7.594  1.00 51.70  ? 279 PRO B C   1 
ATOM   4188 O O   . PRO B 1 279 ? 39.489 -9.838  -8.144  1.00 54.40  ? 279 PRO B O   1 
ATOM   4189 C CB  . PRO B 1 279 ? 41.779 -8.988  -5.912  1.00 55.92  ? 279 PRO B CB  1 
ATOM   4190 C CG  . PRO B 1 279 ? 42.611 -9.473  -4.754  1.00 55.00  ? 279 PRO B CG  1 
ATOM   4191 C CD  . PRO B 1 279 ? 42.277 -10.936 -4.539  1.00 54.23  ? 279 PRO B CD  1 
ATOM   4192 N N   . GLU B 1 280 ? 41.376 -11.080 -8.197  1.00 49.70  ? 280 GLU B N   1 
ATOM   4193 C CA  . GLU B 1 280 ? 41.314 -11.467 -9.636  1.00 53.74  ? 280 GLU B CA  1 
ATOM   4194 C C   . GLU B 1 280 ? 40.030 -12.251 -9.926  1.00 47.27  ? 280 GLU B C   1 
ATOM   4195 O O   . GLU B 1 280 ? 39.612 -12.194 -11.046 1.00 50.18  ? 280 GLU B O   1 
ATOM   4196 C CB  . GLU B 1 280 ? 42.492 -12.325 -10.102 1.00 58.68  ? 280 GLU B CB  1 
ATOM   4197 C CG  . GLU B 1 280 ? 43.867 -11.739 -9.822  1.00 69.62  ? 280 GLU B CG  1 
ATOM   4198 C CD  . GLU B 1 280 ? 44.332 -10.645 -10.769 1.00 83.34  ? 280 GLU B CD  1 
ATOM   4199 O OE1 . GLU B 1 280 ? 45.534 -10.311 -10.722 1.00 94.11  ? 280 GLU B OE1 1 
ATOM   4200 O OE2 . GLU B 1 280 ? 43.499 -10.117 -11.539 1.00 89.53  ? 280 GLU B OE2 1 
ATOM   4201 N N   . LYS B 1 281 ? 39.423 -12.956 -8.972  1.00 49.39  ? 281 LYS B N   1 
ATOM   4202 C CA  . LYS B 1 281 ? 38.233 -13.812 -9.265  1.00 53.83  ? 281 LYS B CA  1 
ATOM   4203 C C   . LYS B 1 281 ? 36.943 -13.013 -9.055  1.00 51.58  ? 281 LYS B C   1 
ATOM   4204 O O   . LYS B 1 281 ? 35.863 -13.523 -9.391  1.00 47.78  ? 281 LYS B O   1 
ATOM   4205 C CB  . LYS B 1 281 ? 38.238 -15.079 -8.400  1.00 59.41  ? 281 LYS B CB  1 
ATOM   4206 C CG  . LYS B 1 281 ? 39.386 -16.035 -8.678  1.00 59.63  ? 281 LYS B CG  1 
ATOM   4207 C CD  . LYS B 1 281 ? 39.179 -16.867 -9.921  1.00 67.70  ? 281 LYS B CD  1 
ATOM   4208 C CE  . LYS B 1 281 ? 40.464 -17.463 -10.467 1.00 74.45  ? 281 LYS B CE  1 
ATOM   4209 N NZ  . LYS B 1 281 ? 41.266 -18.123 -9.404  1.00 79.04  ? 281 LYS B NZ  1 
ATOM   4210 N N   . ARG B 1 282 ? 37.046 -11.810 -8.493  1.00 48.03  ? 282 ARG B N   1 
ATOM   4211 C CA  . ARG B 1 282 ? 35.877 -10.930 -8.279  1.00 46.98  ? 282 ARG B CA  1 
ATOM   4212 C C   . ARG B 1 282 ? 35.487 -10.333 -9.630  1.00 41.35  ? 282 ARG B C   1 
ATOM   4213 O O   . ARG B 1 282 ? 36.352 -9.981  -10.421 1.00 44.90  ? 282 ARG B O   1 
ATOM   4214 C CB  . ARG B 1 282 ? 36.218 -9.852  -7.244  1.00 52.67  ? 282 ARG B CB  1 
ATOM   4215 C CG  . ARG B 1 282 ? 36.440 -10.380 -5.832  1.00 50.74  ? 282 ARG B CG  1 
ATOM   4216 C CD  . ARG B 1 282 ? 36.737 -9.295  -4.815  1.00 48.22  ? 282 ARG B CD  1 
ATOM   4217 N NE  . ARG B 1 282 ? 37.551 -9.870  -3.758  1.00 47.44  ? 282 ARG B NE  1 
ATOM   4218 C CZ  . ARG B 1 282 ? 38.559 -9.266  -3.146  1.00 44.36  ? 282 ARG B CZ  1 
ATOM   4219 N NH1 . ARG B 1 282 ? 38.886 -8.024  -3.458  1.00 46.19  ? 282 ARG B NH1 1 
ATOM   4220 N NH2 . ARG B 1 282 ? 39.248 -9.916  -2.228  1.00 43.07  ? 282 ARG B NH2 1 
ATOM   4221 N N   . PRO B 1 283 ? 34.190 -10.158 -9.933  1.00 37.52  ? 283 PRO B N   1 
ATOM   4222 C CA  . PRO B 1 283 ? 33.806 -9.467  -11.156 1.00 46.35  ? 283 PRO B CA  1 
ATOM   4223 C C   . PRO B 1 283 ? 34.291 -8.001  -11.146 1.00 53.50  ? 283 PRO B C   1 
ATOM   4224 O O   . PRO B 1 283 ? 34.457 -7.407  -10.067 1.00 48.93  ? 283 PRO B O   1 
ATOM   4225 C CB  . PRO B 1 283 ? 32.272 -9.554  -11.167 1.00 42.85  ? 283 PRO B CB  1 
ATOM   4226 C CG  . PRO B 1 283 ? 31.890 -9.767  -9.716  1.00 42.55  ? 283 PRO B CG  1 
ATOM   4227 C CD  . PRO B 1 283 ? 33.038 -10.519 -9.091  1.00 39.23  ? 283 PRO B CD  1 
ATOM   4228 N N   . ASP B 1 284 ? 34.510 -7.438  -12.339 1.00 50.76  ? 284 ASP B N   1 
ATOM   4229 C CA  . ASP B 1 284 ? 34.649 -5.971  -12.523 1.00 52.90  ? 284 ASP B CA  1 
ATOM   4230 C C   . ASP B 1 284 ? 33.271 -5.328  -12.273 1.00 49.68  ? 284 ASP B C   1 
ATOM   4231 O O   . ASP B 1 284 ? 32.231 -6.045  -12.324 1.00 42.27  ? 284 ASP B O   1 
ATOM   4232 C CB  . ASP B 1 284 ? 35.353 -5.643  -13.851 1.00 60.98  ? 284 ASP B CB  1 
ATOM   4233 C CG  . ASP B 1 284 ? 34.635 -6.038  -15.130 1.00 61.22  ? 284 ASP B CG  1 
ATOM   4234 O OD1 . ASP B 1 284 ? 33.400 -6.177  -15.100 1.00 65.43  ? 284 ASP B OD1 1 
ATOM   4235 O OD2 . ASP B 1 284 ? 35.325 -6.160  -16.163 1.00 71.96  ? 284 ASP B OD2 1 
ATOM   4236 N N   . VAL B 1 285 ? 33.259 -4.030  -11.943 1.00 48.06  ? 285 VAL B N   1 
ATOM   4237 C CA  . VAL B 1 285 ? 32.021 -3.250  -11.636 1.00 47.40  ? 285 VAL B CA  1 
ATOM   4238 C C   . VAL B 1 285 ? 31.081 -3.219  -12.855 1.00 47.93  ? 285 VAL B C   1 
ATOM   4239 O O   . VAL B 1 285 ? 29.867 -3.155  -12.647 1.00 44.75  ? 285 VAL B O   1 
ATOM   4240 C CB  . VAL B 1 285 ? 32.373 -1.827  -11.168 1.00 49.40  ? 285 VAL B CB  1 
ATOM   4241 C CG1 . VAL B 1 285 ? 33.054 -1.019  -12.263 1.00 50.18  ? 285 VAL B CG1 1 
ATOM   4242 C CG2 . VAL B 1 285 ? 31.157 -1.095  -10.632 1.00 46.54  ? 285 VAL B CG2 1 
ATOM   4243 N N   . THR B 1 286 ? 31.596 -3.222  -14.086 1.00 50.20  ? 286 THR B N   1 
ATOM   4244 C CA  . THR B 1 286 ? 30.738 -3.257  -15.303 1.00 52.54  ? 286 THR B CA  1 
ATOM   4245 C C   . THR B 1 286 ? 29.774 -4.440  -15.141 1.00 53.53  ? 286 THR B C   1 
ATOM   4246 O O   . THR B 1 286 ? 28.557 -4.240  -15.291 1.00 49.02  ? 286 THR B O   1 
ATOM   4247 C CB  . THR B 1 286 ? 31.572 -3.333  -16.593 1.00 56.08  ? 286 THR B CB  1 
ATOM   4248 O OG1 . THR B 1 286 ? 32.368 -2.152  -16.668 1.00 57.30  ? 286 THR B OG1 1 
ATOM   4249 C CG2 . THR B 1 286 ? 30.747 -3.440  -17.861 1.00 53.89  ? 286 THR B CG2 1 
ATOM   4250 N N   . TYR B 1 287 ? 30.307 -5.618  -14.807 1.00 48.55  ? 287 TYR B N   1 
ATOM   4251 C CA  . TYR B 1 287 ? 29.524 -6.869  -14.651 1.00 50.44  ? 287 TYR B CA  1 
ATOM   4252 C C   . TYR B 1 287 ? 28.501 -6.708  -13.520 1.00 45.34  ? 287 TYR B C   1 
ATOM   4253 O O   . TYR B 1 287 ? 27.364 -7.166  -13.703 1.00 45.40  ? 287 TYR B O   1 
ATOM   4254 C CB  . TYR B 1 287 ? 30.428 -8.086  -14.422 1.00 53.45  ? 287 TYR B CB  1 
ATOM   4255 C CG  . TYR B 1 287 ? 29.668 -9.377  -14.219 1.00 61.68  ? 287 TYR B CG  1 
ATOM   4256 C CD1 . TYR B 1 287 ? 29.209 -9.751  -12.960 1.00 58.65  ? 287 TYR B CD1 1 
ATOM   4257 C CD2 . TYR B 1 287 ? 29.375 -10.210 -15.289 1.00 62.88  ? 287 TYR B CD2 1 
ATOM   4258 C CE1 . TYR B 1 287 ? 28.513 -10.931 -12.766 1.00 61.69  ? 287 TYR B CE1 1 
ATOM   4259 C CE2 . TYR B 1 287 ? 28.666 -11.388 -15.114 1.00 64.16  ? 287 TYR B CE2 1 
ATOM   4260 C CZ  . TYR B 1 287 ? 28.243 -11.751 -13.847 1.00 63.65  ? 287 TYR B CZ  1 
ATOM   4261 O OH  . TYR B 1 287 ? 27.552 -12.908 -13.656 1.00 74.78  ? 287 TYR B OH  1 
ATOM   4262 N N   . VAL B 1 288 ? 28.896 -6.122  -12.390 1.00 41.12  ? 288 VAL B N   1 
ATOM   4263 C CA  . VAL B 1 288 ? 28.016 -6.004  -11.194 1.00 44.15  ? 288 VAL B CA  1 
ATOM   4264 C C   . VAL B 1 288 ? 26.875 -5.047  -11.548 1.00 46.24  ? 288 VAL B C   1 
ATOM   4265 O O   . VAL B 1 288 ? 25.710 -5.370  -11.227 1.00 49.75  ? 288 VAL B O   1 
ATOM   4266 C CB  . VAL B 1 288 ? 28.783 -5.542  -9.941  1.00 45.25  ? 288 VAL B CB  1 
ATOM   4267 C CG1 . VAL B 1 288 ? 27.866 -5.462  -8.720  1.00 48.73  ? 288 VAL B CG1 1 
ATOM   4268 C CG2 . VAL B 1 288 ? 29.972 -6.440  -9.656  1.00 49.92  ? 288 VAL B CG2 1 
ATOM   4269 N N   . TYR B 1 289 ? 27.216 -3.919  -12.180 1.00 49.98  ? 289 TYR B N   1 
ATOM   4270 C CA  . TYR B 1 289 ? 26.280 -2.878  -12.697 1.00 48.69  ? 289 TYR B CA  1 
ATOM   4271 C C   . TYR B 1 289 ? 25.280 -3.522  -13.668 1.00 44.99  ? 289 TYR B C   1 
ATOM   4272 O O   . TYR B 1 289 ? 24.040 -3.343  -13.542 1.00 41.05  ? 289 TYR B O   1 
ATOM   4273 C CB  . TYR B 1 289 ? 27.083 -1.746  -13.355 1.00 51.60  ? 289 TYR B CB  1 
ATOM   4274 C CG  . TYR B 1 289 ? 26.305 -0.525  -13.793 1.00 49.00  ? 289 TYR B CG  1 
ATOM   4275 C CD1 . TYR B 1 289 ? 25.189 -0.096  -13.096 1.00 42.99  ? 289 TYR B CD1 1 
ATOM   4276 C CD2 . TYR B 1 289 ? 26.707 0.224   -14.892 1.00 47.71  ? 289 TYR B CD2 1 
ATOM   4277 C CE1 . TYR B 1 289 ? 24.478 1.026   -13.485 1.00 46.26  ? 289 TYR B CE1 1 
ATOM   4278 C CE2 . TYR B 1 289 ? 26.010 1.358   -15.285 1.00 45.27  ? 289 TYR B CE2 1 
ATOM   4279 C CZ  . TYR B 1 289 ? 24.889 1.756   -14.581 1.00 44.92  ? 289 TYR B CZ  1 
ATOM   4280 O OH  . TYR B 1 289 ? 24.166 2.856   -14.932 1.00 52.62  ? 289 TYR B OH  1 
ATOM   4281 N N   . ASP B 1 290 ? 25.789 -4.326  -14.592 1.00 47.30  ? 290 ASP B N   1 
ATOM   4282 C CA  . ASP B 1 290 ? 24.926 -5.013  -15.584 1.00 51.87  ? 290 ASP B CA  1 
ATOM   4283 C C   . ASP B 1 290 ? 23.891 -5.888  -14.848 1.00 51.02  ? 290 ASP B C   1 
ATOM   4284 O O   . ASP B 1 290 ? 22.705 -5.862  -15.228 1.00 49.79  ? 290 ASP B O   1 
ATOM   4285 C CB  . ASP B 1 290 ? 25.758 -5.777  -16.615 1.00 58.58  ? 290 ASP B CB  1 
ATOM   4286 C CG  . ASP B 1 290 ? 24.899 -6.127  -17.815 1.00 73.41  ? 290 ASP B CG  1 
ATOM   4287 O OD1 . ASP B 1 290 ? 24.623 -5.187  -18.630 1.00 72.98  ? 290 ASP B OD1 1 
ATOM   4288 O OD2 . ASP B 1 290 ? 24.418 -7.300  -17.859 1.00 69.76  ? 290 ASP B OD2 1 
ATOM   4289 N N   . VAL B 1 291 ? 24.287 -6.578  -13.779 1.00 51.57  ? 291 VAL B N   1 
ATOM   4290 C CA  . VAL B 1 291 ? 23.380 -7.493  -13.022 1.00 54.52  ? 291 VAL B CA  1 
ATOM   4291 C C   . VAL B 1 291 ? 22.342 -6.640  -12.286 1.00 55.18  ? 291 VAL B C   1 
ATOM   4292 O O   . VAL B 1 291 ? 21.133 -6.858  -12.458 1.00 51.86  ? 291 VAL B O   1 
ATOM   4293 C CB  . VAL B 1 291 ? 24.173 -8.395  -12.056 1.00 52.99  ? 291 VAL B CB  1 
ATOM   4294 C CG1 . VAL B 1 291 ? 23.248 -9.138  -11.097 1.00 50.67  ? 291 VAL B CG1 1 
ATOM   4295 C CG2 . VAL B 1 291 ? 25.088 -9.361  -12.815 1.00 50.97  ? 291 VAL B CG2 1 
ATOM   4296 N N   . ALA B 1 292 ? 22.817 -5.684  -11.497 1.00 60.87  ? 292 ALA B N   1 
ATOM   4297 C CA  . ALA B 1 292 ? 21.972 -4.684  -10.812 1.00 61.61  ? 292 ALA B CA  1 
ATOM   4298 C C   . ALA B 1 292 ? 20.956 -4.101  -11.810 1.00 53.06  ? 292 ALA B C   1 
ATOM   4299 O O   . ALA B 1 292 ? 19.799 -3.962  -11.406 1.00 48.77  ? 292 ALA B O   1 
ATOM   4300 C CB  . ALA B 1 292 ? 22.846 -3.618  -10.190 1.00 59.98  ? 292 ALA B CB  1 
ATOM   4301 N N   . LYS B 1 293 ? 21.356 -3.805  -13.058 1.00 49.67  ? 293 LYS B N   1 
ATOM   4302 C CA  . LYS B 1 293 ? 20.444 -3.172  -14.063 1.00 56.30  ? 293 LYS B CA  1 
ATOM   4303 C C   . LYS B 1 293 ? 19.383 -4.180  -14.528 1.00 58.74  ? 293 LYS B C   1 
ATOM   4304 O O   . LYS B 1 293 ? 18.193 -3.804  -14.507 1.00 52.58  ? 293 LYS B O   1 
ATOM   4305 C CB  . LYS B 1 293 ? 21.187 -2.545  -15.246 1.00 53.28  ? 293 LYS B CB  1 
ATOM   4306 C CG  . LYS B 1 293 ? 21.652 -1.114  -14.991 1.00 57.99  ? 293 LYS B CG  1 
ATOM   4307 C CD  . LYS B 1 293 ? 22.312 -0.439  -16.167 1.00 57.80  ? 293 LYS B CD  1 
ATOM   4308 C CE  . LYS B 1 293 ? 23.472 -1.243  -16.700 1.00 58.52  ? 293 LYS B CE  1 
ATOM   4309 N NZ  . LYS B 1 293 ? 24.071 -0.565  -17.866 1.00 68.48  ? 293 LYS B NZ  1 
ATOM   4310 N N   . ARG B 1 294 ? 19.775 -5.408  -14.886 1.00 60.75  ? 294 ARG B N   1 
ATOM   4311 C CA  . ARG B 1 294 ? 18.815 -6.485  -15.261 1.00 60.12  ? 294 ARG B CA  1 
ATOM   4312 C C   . ARG B 1 294 ? 17.850 -6.760  -14.092 1.00 61.88  ? 294 ARG B C   1 
ATOM   4313 O O   . ARG B 1 294 ? 16.640 -6.963  -14.348 1.00 58.31  ? 294 ARG B O   1 
ATOM   4314 C CB  . ARG B 1 294 ? 19.567 -7.748  -15.681 1.00 59.61  ? 294 ARG B CB  1 
ATOM   4315 C CG  . ARG B 1 294 ? 20.236 -7.624  -17.041 1.00 64.68  ? 294 ARG B CG  1 
ATOM   4316 C CD  . ARG B 1 294 ? 21.345 -8.646  -17.234 1.00 66.19  ? 294 ARG B CD  1 
ATOM   4317 N NE  . ARG B 1 294 ? 21.927 -8.546  -18.572 1.00 76.67  ? 294 ARG B NE  1 
ATOM   4318 C CZ  . ARG B 1 294 ? 21.432 -9.121  -19.672 1.00 73.08  ? 294 ARG B CZ  1 
ATOM   4319 N NH1 . ARG B 1 294 ? 22.035 -8.929  -20.834 1.00 68.20  ? 294 ARG B NH1 1 
ATOM   4320 N NH2 . ARG B 1 294 ? 20.340 -9.870  -19.609 1.00 70.04  ? 294 ARG B NH2 1 
ATOM   4321 N N   . MET B 1 295 ? 18.341 -6.756  -12.848 1.00 61.30  ? 295 MET B N   1 
ATOM   4322 C CA  . MET B 1 295 ? 17.524 -7.140  -11.662 1.00 63.85  ? 295 MET B CA  1 
ATOM   4323 C C   . MET B 1 295 ? 16.605 -5.979  -11.264 1.00 57.28  ? 295 MET B C   1 
ATOM   4324 O O   . MET B 1 295 ? 15.454 -6.242  -10.919 1.00 58.85  ? 295 MET B O   1 
ATOM   4325 C CB  . MET B 1 295 ? 18.401 -7.573  -10.482 1.00 59.17  ? 295 MET B CB  1 
ATOM   4326 C CG  . MET B 1 295 ? 19.164 -8.861  -10.753 1.00 58.45  ? 295 MET B CG  1 
ATOM   4327 S SD  . MET B 1 295 ? 18.089 -10.260 -11.190 1.00 55.04  ? 295 MET B SD  1 
ATOM   4328 C CE  . MET B 1 295 ? 17.185 -10.455 -9.652  1.00 52.44  ? 295 MET B CE  1 
ATOM   4329 N N   . HIS B 1 296 ? 17.077 -4.742  -11.346 1.00 56.10  ? 296 HIS B N   1 
ATOM   4330 C CA  . HIS B 1 296 ? 16.213 -3.545  -11.185 1.00 58.86  ? 296 HIS B CA  1 
ATOM   4331 C C   . HIS B 1 296 ? 15.063 -3.642  -12.191 1.00 60.01  ? 296 HIS B C   1 
ATOM   4332 O O   . HIS B 1 296 ? 13.897 -3.525  -11.769 1.00 65.08  ? 296 HIS B O   1 
ATOM   4333 C CB  . HIS B 1 296 ? 17.021 -2.255  -11.358 1.00 58.74  ? 296 HIS B CB  1 
ATOM   4334 C CG  . HIS B 1 296 ? 16.217 -1.031  -11.083 1.00 62.80  ? 296 HIS B CG  1 
ATOM   4335 N ND1 . HIS B 1 296 ? 15.419 -0.915  -9.935  1.00 60.28  ? 296 HIS B ND1 1 
ATOM   4336 C CD2 . HIS B 1 296 ? 16.072 0.117   -11.785 1.00 53.56  ? 296 HIS B CD2 1 
ATOM   4337 C CE1 . HIS B 1 296 ? 14.818 0.254   -9.949  1.00 59.78  ? 296 HIS B CE1 1 
ATOM   4338 N NE2 . HIS B 1 296 ? 15.199 0.903   -11.079 1.00 62.77  ? 296 HIS B NE2 1 
ATOM   4339 N N   . ALA B 1 297 ? 15.390 -3.900  -13.460 1.00 60.06  ? 297 ALA B N   1 
ATOM   4340 C CA  . ALA B 1 297 ? 14.440 -3.937  -14.596 1.00 65.73  ? 297 ALA B CA  1 
ATOM   4341 C C   . ALA B 1 297 ? 13.362 -5.004  -14.337 1.00 68.88  ? 297 ALA B C   1 
ATOM   4342 O O   . ALA B 1 297 ? 12.171 -4.666  -14.481 1.00 65.86  ? 297 ALA B O   1 
ATOM   4343 C CB  . ALA B 1 297 ? 15.164 -4.157  -15.912 1.00 58.83  ? 297 ALA B CB  1 
ATOM   4344 N N   . CYS B 1 298 ? 13.735 -6.227  -13.934 1.00 75.03  ? 298 CYS B N   1 
ATOM   4345 C CA  . CYS B 1 298 ? 12.768 -7.357  -13.776 1.00 78.65  ? 298 CYS B CA  1 
ATOM   4346 C C   . CYS B 1 298 ? 12.152 -7.404  -12.360 1.00 80.18  ? 298 CYS B C   1 
ATOM   4347 O O   . CYS B 1 298 ? 11.269 -8.263  -12.148 1.00 74.87  ? 298 CYS B O   1 
ATOM   4348 C CB  . CYS B 1 298 ? 13.364 -8.695  -14.225 1.00 78.26  ? 298 CYS B CB  1 
ATOM   4349 S SG  . CYS B 1 298 ? 14.553 -9.489  -13.107 1.00 88.89  ? 298 CYS B SG  1 
ATOM   4350 N N   . THR B 1 299 ? 12.531 -6.500  -11.440 1.00 77.51  ? 299 THR B N   1 
ATOM   4351 C CA  . THR B 1 299 ? 11.969 -6.452  -10.055 1.00 81.11  ? 299 THR B CA  1 
ATOM   4352 C C   . THR B 1 299 ? 11.006 -5.266  -9.906  1.00 75.58  ? 299 THR B C   1 
ATOM   4353 O O   . THR B 1 299 ? 10.129 -5.356  -9.026  1.00 72.35  ? 299 THR B O   1 
ATOM   4354 C CB  . THR B 1 299 ? 13.053 -6.481  -8.958  1.00 78.19  ? 299 THR B CB  1 
ATOM   4355 O OG1 . THR B 1 299 ? 14.101 -5.536  -9.216  1.00 72.05  ? 299 THR B OG1 1 
ATOM   4356 C CG2 . THR B 1 299 ? 13.638 -7.868  -8.778  1.00 71.69  ? 299 THR B CG2 1 
ATOM   4357 N N   . ALA B 1 300 ? 11.152 -4.230  -10.739 1.00 79.00  ? 300 ALA B N   1 
ATOM   4358 C CA  . ALA B 1 300 ? 10.294 -3.020  -10.765 1.00 87.43  ? 300 ALA B CA  1 
ATOM   4359 C C   . ALA B 1 300 ? 9.005  -3.311  -11.540 1.00 85.07  ? 300 ALA B C   1 
ATOM   4360 O O   . ALA B 1 300 ? 7.962  -2.859  -11.086 1.00 83.02  ? 300 ALA B O   1 
ATOM   4361 C CB  . ALA B 1 300 ? 11.051 -1.869  -11.381 1.00 85.69  ? 300 ALA B CB  1 
HETATM 4362 C C1  . EDO C 2 .   ? 1.129  27.965  -26.240 1.00 65.68  ? 401 EDO A C1  1 
HETATM 4363 O O1  . EDO C 2 .   ? -0.218 27.584  -26.474 1.00 59.32  ? 401 EDO A O1  1 
HETATM 4364 C C2  . EDO C 2 .   ? 1.382  28.531  -24.880 1.00 67.55  ? 401 EDO A C2  1 
HETATM 4365 O O2  . EDO C 2 .   ? 1.726  29.906  -24.833 1.00 72.53  ? 401 EDO A O2  1 
HETATM 4366 C C1  . EDO D 2 .   ? 25.279 -15.629 -0.284  1.00 82.40  ? 401 EDO B C1  1 
HETATM 4367 O O1  . EDO D 2 .   ? 26.440 -16.298 -0.756  1.00 82.89  ? 401 EDO B O1  1 
HETATM 4368 C C2  . EDO D 2 .   ? 24.586 -16.397 0.788   1.00 83.83  ? 401 EDO B C2  1 
HETATM 4369 O O2  . EDO D 2 .   ? 23.358 -15.833 1.194   1.00 75.76  ? 401 EDO B O2  1 
HETATM 4370 C C1  . EDO E 2 .   ? 24.761 -13.629 -12.251 1.00 97.28  ? 402 EDO B C1  1 
HETATM 4371 O O1  . EDO E 2 .   ? 25.683 -12.559 -12.330 1.00 98.04  ? 402 EDO B O1  1 
HETATM 4372 C C2  . EDO E 2 .   ? 23.619 -13.299 -11.364 1.00 89.69  ? 402 EDO B C2  1 
HETATM 4373 O O2  . EDO E 2 .   ? 23.950 -13.376 -9.995  1.00 83.70  ? 402 EDO B O2  1 
HETATM 4374 C C1  . EDO F 2 .   ? 33.115 10.968  -4.189  1.00 79.55  ? 403 EDO B C1  1 
HETATM 4375 O O1  . EDO F 2 .   ? 32.313 11.925  -3.520  1.00 77.55  ? 403 EDO B O1  1 
HETATM 4376 C C2  . EDO F 2 .   ? 33.016 9.604   -3.618  1.00 80.17  ? 403 EDO B C2  1 
HETATM 4377 O O2  . EDO F 2 .   ? 34.271 9.108   -3.171  1.00 94.41  ? 403 EDO B O2  1 
HETATM 4378 C C1  . EDO G 2 .   ? 22.351 -11.727 -14.431 1.00 84.47  ? 404 EDO B C1  1 
HETATM 4379 O O1  . EDO G 2 .   ? 21.766 -10.640 -15.165 1.00 63.61  ? 404 EDO B O1  1 
HETATM 4380 C C2  . EDO G 2 .   ? 21.361 -12.795 -14.160 1.00 82.56  ? 404 EDO B C2  1 
HETATM 4381 O O2  . EDO G 2 .   ? 20.196 -12.188 -13.652 1.00 75.18  ? 404 EDO B O2  1 
HETATM 4382 O O   . HOH H 3 .   ? 25.969 20.348  -8.277  1.00 45.87  ? 501 HOH A O   1 
HETATM 4383 O O   . HOH H 3 .   ? 37.653 40.634  -30.195 1.00 49.38  ? 502 HOH A O   1 
HETATM 4384 O O   . HOH H 3 .   ? 43.990 40.585  -22.042 1.00 46.23  ? 503 HOH A O   1 
HETATM 4385 O O   . HOH H 3 .   ? 29.101 19.662  -14.897 1.00 42.59  ? 504 HOH A O   1 
HETATM 4386 O O   . HOH H 3 .   ? 27.982 28.549  -23.062 1.00 61.51  ? 505 HOH A O   1 
HETATM 4387 O O   . HOH H 3 .   ? 6.177  36.344  -17.735 1.00 52.04  ? 506 HOH A O   1 
HETATM 4388 O O   . HOH H 3 .   ? 35.490 37.383  -24.501 1.00 59.98  ? 507 HOH A O   1 
HETATM 4389 O O   . HOH H 3 .   ? 15.939 7.738   -34.699 1.00 61.46  ? 508 HOH A O   1 
HETATM 4390 O O   . HOH H 3 .   ? 56.024 16.117  -17.885 1.00 65.55  ? 509 HOH A O   1 
HETATM 4391 O O   . HOH H 3 .   ? 7.494  13.032  -16.509 1.00 49.88  ? 510 HOH A O   1 
HETATM 4392 O O   . HOH H 3 .   ? 5.133  32.411  -35.192 1.00 53.86  ? 511 HOH A O   1 
HETATM 4393 O O   . HOH H 3 .   ? 14.687 24.008  -6.494  1.00 55.29  ? 512 HOH A O   1 
HETATM 4394 O O   . HOH H 3 .   ? 20.287 31.269  -25.529 1.00 47.44  ? 513 HOH A O   1 
HETATM 4395 O O   . HOH H 3 .   ? 32.790 22.455  -15.207 1.00 41.11  ? 514 HOH A O   1 
HETATM 4396 O O   . HOH H 3 .   ? 2.891  39.045  -36.249 1.00 53.28  ? 515 HOH A O   1 
HETATM 4397 O O   . HOH H 3 .   ? 19.263 20.454  -8.765  1.00 41.50  ? 516 HOH A O   1 
HETATM 4398 O O   . HOH H 3 .   ? 15.873 17.524  -10.518 1.00 38.71  ? 517 HOH A O   1 
HETATM 4399 O O   . HOH H 3 .   ? 7.360  43.933  -27.743 1.00 44.25  ? 518 HOH A O   1 
HETATM 4400 O O   . HOH H 3 .   ? 11.297 30.723  -33.072 1.00 52.50  ? 519 HOH A O   1 
HETATM 4401 O O   . HOH H 3 .   ? 32.235 23.939  -7.845  1.00 74.82  ? 520 HOH A O   1 
HETATM 4402 O O   . HOH H 3 .   ? 33.541 30.650  -30.216 1.00 51.41  ? 521 HOH A O   1 
HETATM 4403 O O   . HOH H 3 .   ? -0.507 31.168  -23.950 1.00 57.20  ? 522 HOH A O   1 
HETATM 4404 O O   . HOH H 3 .   ? 8.388  9.124   -25.408 1.00 52.74  ? 523 HOH A O   1 
HETATM 4405 O O   . HOH H 3 .   ? 47.561 32.290  -36.583 1.00 61.20  ? 524 HOH A O   1 
HETATM 4406 O O   . HOH H 3 .   ? 31.544 28.717  -9.082  1.00 47.29  ? 525 HOH A O   1 
HETATM 4407 O O   . HOH H 3 .   ? 5.471  34.904  -42.276 1.00 59.75  ? 526 HOH A O   1 
HETATM 4408 O O   . HOH H 3 .   ? 5.692  17.185  -29.841 1.00 56.19  ? 527 HOH A O   1 
HETATM 4409 O O   . HOH H 3 .   ? 12.481 27.045  -4.347  1.00 66.46  ? 528 HOH A O   1 
HETATM 4410 O O   . HOH H 3 .   ? 23.897 14.448  -31.502 1.00 61.99  ? 529 HOH A O   1 
HETATM 4411 O O   . HOH H 3 .   ? 32.386 13.521  -16.543 1.00 51.63  ? 530 HOH A O   1 
HETATM 4412 O O   . HOH H 3 .   ? 25.557 7.802   -23.986 1.00 58.06  ? 531 HOH A O   1 
HETATM 4413 O O   . HOH H 3 .   ? 20.559 22.521  -10.084 1.00 43.19  ? 532 HOH A O   1 
HETATM 4414 O O   . HOH H 3 .   ? 11.999 8.700   -23.709 1.00 62.95  ? 533 HOH A O   1 
HETATM 4415 O O   . HOH H 3 .   ? 17.179 32.951  -13.700 1.00 43.73  ? 534 HOH A O   1 
HETATM 4416 O O   . HOH H 3 .   ? -0.753 33.744  -31.887 1.00 62.23  ? 535 HOH A O   1 
HETATM 4417 O O   . HOH H 3 .   ? 42.926 23.217  -15.797 1.00 52.11  ? 536 HOH A O   1 
HETATM 4418 O O   . HOH H 3 .   ? 16.715 12.141  -36.182 1.00 61.06  ? 537 HOH A O   1 
HETATM 4419 O O   . HOH H 3 .   ? 4.026  36.417  -20.506 1.00 51.99  ? 538 HOH A O   1 
HETATM 4420 O O   . HOH H 3 .   ? 54.515 30.872  -27.461 1.00 59.00  ? 539 HOH A O   1 
HETATM 4421 O O   . HOH H 3 .   ? 44.584 31.889  -33.398 1.00 75.55  ? 540 HOH A O   1 
HETATM 4422 O O   . HOH H 3 .   ? 29.619 9.725   -25.598 1.00 63.07  ? 541 HOH A O   1 
HETATM 4423 O O   . HOH H 3 .   ? 0.228  38.151  -30.784 1.00 49.81  ? 542 HOH A O   1 
HETATM 4424 O O   . HOH H 3 .   ? 26.120 9.488   -35.117 1.00 63.12  ? 543 HOH A O   1 
HETATM 4425 O O   . HOH H 3 .   ? 24.649 40.053  -6.679  1.00 67.33  ? 544 HOH A O   1 
HETATM 4426 O O   . HOH H 3 .   ? 19.438 30.689  -36.282 1.00 68.13  ? 545 HOH A O   1 
HETATM 4427 O O   . HOH H 3 .   ? 11.714 25.012  -36.301 1.00 48.74  ? 546 HOH A O   1 
HETATM 4428 O O   . HOH H 3 .   ? 23.089 23.913  -8.038  1.00 49.10  ? 547 HOH A O   1 
HETATM 4429 O O   . HOH H 3 .   ? 19.352 23.383  -32.459 1.00 52.85  ? 548 HOH A O   1 
HETATM 4430 O O   . HOH H 3 .   ? 30.850 18.544  -25.311 1.00 44.23  ? 549 HOH A O   1 
HETATM 4431 O O   . HOH H 3 .   ? 1.396  32.582  -35.150 1.00 49.88  ? 550 HOH A O   1 
HETATM 4432 O O   . HOH H 3 .   ? 28.441 34.369  -17.596 1.00 51.08  ? 551 HOH A O   1 
HETATM 4433 O O   . HOH H 3 .   ? 43.440 29.037  -18.585 1.00 57.37  ? 552 HOH A O   1 
HETATM 4434 O O   . HOH H 3 .   ? 12.290 37.647  -11.189 1.00 56.65  ? 553 HOH A O   1 
HETATM 4435 O O   . HOH H 3 .   ? 12.241 41.571  -11.944 1.00 61.66  ? 554 HOH A O   1 
HETATM 4436 O O   . HOH H 3 .   ? 18.925 11.926  -29.869 1.00 45.40  ? 555 HOH A O   1 
HETATM 4437 O O   . HOH H 3 .   ? 14.993 40.297  -14.118 1.00 50.07  ? 556 HOH A O   1 
HETATM 4438 O O   . HOH H 3 .   ? 13.665 30.678  -35.402 1.00 55.96  ? 557 HOH A O   1 
HETATM 4439 O O   . HOH H 3 .   ? 0.752  11.982  -32.192 1.00 58.30  ? 558 HOH A O   1 
HETATM 4440 O O   . HOH H 3 .   ? -6.858 21.097  -29.335 1.00 62.97  ? 559 HOH A O   1 
HETATM 4441 O O   . HOH H 3 .   ? 1.540  12.494  -21.428 1.00 55.33  ? 560 HOH A O   1 
HETATM 4442 O O   . HOH H 3 .   ? 2.348  27.113  -15.078 1.00 43.44  ? 561 HOH A O   1 
HETATM 4443 O O   . HOH H 3 .   ? 37.764 19.004  -13.293 1.00 58.73  ? 562 HOH A O   1 
HETATM 4444 O O   . HOH H 3 .   ? 19.874 30.583  -29.052 1.00 49.75  ? 563 HOH A O   1 
HETATM 4445 O O   . HOH H 3 .   ? 11.569 30.025  -7.260  1.00 62.62  ? 564 HOH A O   1 
HETATM 4446 O O   . HOH H 3 .   ? 30.398 33.343  -38.593 1.00 68.00  ? 565 HOH A O   1 
HETATM 4447 O O   . HOH H 3 .   ? 24.876 11.738  -15.616 1.00 89.40  ? 566 HOH A O   1 
HETATM 4448 O O   . HOH H 3 .   ? 3.391  15.289  -36.206 1.00 62.09  ? 567 HOH A O   1 
HETATM 4449 O O   . HOH H 3 .   ? 19.030 39.090  -15.713 1.00 49.22  ? 568 HOH A O   1 
HETATM 4450 O O   . HOH H 3 .   ? 21.440 35.326  -10.804 1.00 51.21  ? 569 HOH A O   1 
HETATM 4451 O O   . HOH H 3 .   ? 36.611 9.862   -36.868 1.00 58.71  ? 570 HOH A O   1 
HETATM 4452 O O   . HOH H 3 .   ? 10.145 19.484  -5.642  1.00 57.86  ? 571 HOH A O   1 
HETATM 4453 O O   . HOH H 3 .   ? 19.698 13.385  -13.958 1.00 66.70  ? 572 HOH A O   1 
HETATM 4454 O O   . HOH H 3 .   ? 1.082  14.296  -26.890 1.00 61.76  ? 573 HOH A O   1 
HETATM 4455 O O   . HOH H 3 .   ? 20.038 16.476  -10.682 1.00 48.85  ? 574 HOH A O   1 
HETATM 4456 O O   . HOH H 3 .   ? -3.875 17.585  -21.776 1.00 57.70  ? 575 HOH A O   1 
HETATM 4457 O O   . HOH H 3 .   ? 18.656 31.271  -6.260  1.00 62.25  ? 576 HOH A O   1 
HETATM 4458 O O   . HOH H 3 .   ? 21.747 24.307  -34.373 1.00 53.92  ? 577 HOH A O   1 
HETATM 4459 O O   . HOH H 3 .   ? 31.551 31.336  -37.372 1.00 58.50  ? 578 HOH A O   1 
HETATM 4460 O O   . HOH H 3 .   ? 27.838 25.056  -21.090 1.00 54.96  ? 579 HOH A O   1 
HETATM 4461 O O   . HOH H 3 .   ? 16.003 16.575  -12.688 1.00 47.57  ? 580 HOH A O   1 
HETATM 4462 O O   . HOH H 3 .   ? 1.632  23.611  -32.698 1.00 49.52  ? 581 HOH A O   1 
HETATM 4463 O O   . HOH H 3 .   ? 39.879 30.864  -10.031 1.00 57.14  ? 582 HOH A O   1 
HETATM 4464 O O   . HOH H 3 .   ? 30.646 30.697  -7.763  1.00 48.01  ? 583 HOH A O   1 
HETATM 4465 O O   . HOH H 3 .   ? 14.762 9.233   -30.061 1.00 64.86  ? 584 HOH A O   1 
HETATM 4466 O O   . HOH H 3 .   ? 17.229 35.321  -13.188 1.00 49.84  ? 585 HOH A O   1 
HETATM 4467 O O   . HOH H 3 .   ? 12.899 19.768  -38.988 1.00 66.83  ? 586 HOH A O   1 
HETATM 4468 O O   . HOH H 3 .   ? 19.653 38.186  -10.370 1.00 64.47  ? 587 HOH A O   1 
HETATM 4469 O O   . HOH I 3 .   ? 32.317 -7.251  7.461   1.00 64.46  ? 501 HOH B O   1 
HETATM 4470 O O   . HOH I 3 .   ? 37.926 12.762  -15.946 1.00 55.03  ? 502 HOH B O   1 
HETATM 4471 O O   . HOH I 3 .   ? 34.776 37.474  2.813   1.00 64.97  ? 503 HOH B O   1 
HETATM 4472 O O   . HOH I 3 .   ? 48.928 28.644  0.842   1.00 57.81  ? 504 HOH B O   1 
HETATM 4473 O O   . HOH I 3 .   ? 31.167 33.881  -8.863  1.00 57.27  ? 505 HOH B O   1 
HETATM 4474 O O   . HOH I 3 .   ? 16.757 -6.791  4.595   1.00 59.21  ? 506 HOH B O   1 
HETATM 4475 O O   . HOH I 3 .   ? 36.070 0.026   0.557   1.00 43.39  ? 507 HOH B O   1 
HETATM 4476 O O   . HOH I 3 .   ? 45.794 20.343  11.787  1.00 65.62  ? 508 HOH B O   1 
HETATM 4477 O O   . HOH I 3 .   ? 43.510 31.546  -3.185  1.00 55.40  ? 509 HOH B O   1 
HETATM 4478 O O   . HOH I 3 .   ? 27.532 26.054  12.643  1.00 68.06  ? 510 HOH B O   1 
HETATM 4479 O O   . HOH I 3 .   ? 30.624 5.920   -16.639 1.00 57.09  ? 511 HOH B O   1 
HETATM 4480 O O   . HOH I 3 .   ? 40.624 33.915  0.417   1.00 64.27  ? 512 HOH B O   1 
HETATM 4481 O O   . HOH I 3 .   ? 16.177 14.970  0.299   1.00 62.85  ? 513 HOH B O   1 
HETATM 4482 O O   . HOH I 3 .   ? 27.147 24.697  -4.856  1.00 50.58  ? 514 HOH B O   1 
HETATM 4483 O O   . HOH I 3 .   ? 21.993 11.811  6.832   1.00 84.66  ? 515 HOH B O   1 
HETATM 4484 O O   . HOH I 3 .   ? 26.508 21.061  -0.487  1.00 40.37  ? 516 HOH B O   1 
HETATM 4485 O O   . HOH I 3 .   ? 37.172 13.165  0.905   1.00 67.84  ? 517 HOH B O   1 
HETATM 4486 O O   . HOH I 3 .   ? 42.864 29.895  -5.801  1.00 52.86  ? 518 HOH B O   1 
HETATM 4487 O O   . HOH I 3 .   ? 32.610 12.602  -0.645  1.00 66.88  ? 519 HOH B O   1 
HETATM 4488 O O   . HOH I 3 .   ? 40.123 38.812  -7.020  1.00 65.49  ? 520 HOH B O   1 
HETATM 4489 O O   . HOH I 3 .   ? 25.731 15.253  -6.547  1.00 59.44  ? 521 HOH B O   1 
HETATM 4490 O O   . HOH I 3 .   ? 27.192 11.318  -15.950 1.00 63.31  ? 522 HOH B O   1 
HETATM 4491 O O   . HOH I 3 .   ? 28.268 4.906   -14.858 1.00 43.51  ? 523 HOH B O   1 
HETATM 4492 O O   . HOH I 3 .   ? 48.580 10.655  -0.638  1.00 51.93  ? 524 HOH B O   1 
HETATM 4493 O O   . HOH I 3 .   ? 25.297 27.233  -6.327  1.00 56.67  ? 525 HOH B O   1 
HETATM 4494 O O   . HOH I 3 .   ? 35.398 31.499  7.648   1.00 58.55  ? 526 HOH B O   1 
HETATM 4495 O O   . HOH I 3 .   ? 13.782 -2.916  -8.545  1.00 50.10  ? 527 HOH B O   1 
HETATM 4496 O O   . HOH I 3 .   ? 39.608 8.039   -3.531  1.00 64.37  ? 528 HOH B O   1 
HETATM 4497 O O   . HOH I 3 .   ? 21.721 3.394   -13.803 1.00 50.51  ? 529 HOH B O   1 
HETATM 4498 O O   . HOH I 3 .   ? 37.237 30.933  5.034   1.00 55.86  ? 530 HOH B O   1 
HETATM 4499 O O   . HOH I 3 .   ? 46.545 7.185   12.768  1.00 62.66  ? 531 HOH B O   1 
HETATM 4500 O O   . HOH I 3 .   ? 43.083 12.550  6.269   1.00 37.52  ? 532 HOH B O   1 
HETATM 4501 O O   . HOH I 3 .   ? 21.377 14.891  5.944   1.00 44.55  ? 533 HOH B O   1 
HETATM 4502 O O   . HOH I 3 .   ? 11.172 -0.253  0.845   1.00 56.79  ? 534 HOH B O   1 
HETATM 4503 O O   . HOH I 3 .   ? 39.139 24.109  -7.826  1.00 43.36  ? 535 HOH B O   1 
HETATM 4504 O O   . HOH I 3 .   ? 55.172 16.527  -4.589  1.00 42.30  ? 536 HOH B O   1 
HETATM 4505 O O   . HOH I 3 .   ? 33.500 -22.266 7.948   1.00 54.96  ? 537 HOH B O   1 
HETATM 4506 O O   . HOH I 3 .   ? 25.498 23.226  11.355  1.00 64.74  ? 538 HOH B O   1 
HETATM 4507 O O   . HOH I 3 .   ? 45.822 25.993  -6.024  1.00 51.18  ? 539 HOH B O   1 
HETATM 4508 O O   . HOH I 3 .   ? 42.481 6.150   -7.301  1.00 51.24  ? 540 HOH B O   1 
HETATM 4509 O O   . HOH I 3 .   ? 36.639 -17.589 14.338  1.00 54.72  ? 541 HOH B O   1 
HETATM 4510 O O   . HOH I 3 .   ? 39.942 -3.452  2.531   1.00 61.21  ? 542 HOH B O   1 
HETATM 4511 O O   . HOH I 3 .   ? 50.340 21.649  4.961   1.00 53.06  ? 543 HOH B O   1 
HETATM 4512 O O   . HOH I 3 .   ? 32.714 15.673  -8.374  1.00 49.23  ? 544 HOH B O   1 
HETATM 4513 O O   . HOH I 3 .   ? 30.926 -13.890 10.240  1.00 55.41  ? 545 HOH B O   1 
HETATM 4514 O O   . HOH I 3 .   ? 30.065 13.980  -9.419  1.00 73.85  ? 546 HOH B O   1 
HETATM 4515 O O   . HOH I 3 .   ? 33.990 -9.274  -14.541 1.00 47.87  ? 547 HOH B O   1 
HETATM 4516 O O   . HOH I 3 .   ? 42.552 25.445  -8.261  1.00 53.36  ? 548 HOH B O   1 
HETATM 4517 O O   . HOH I 3 .   ? 24.427 25.805  10.783  1.00 49.00  ? 549 HOH B O   1 
HETATM 4518 O O   . HOH I 3 .   ? 45.164 13.947  -12.098 1.00 50.11  ? 550 HOH B O   1 
HETATM 4519 O O   . HOH I 3 .   ? 10.809 -7.156  -3.561  1.00 54.29  ? 551 HOH B O   1 
HETATM 4520 O O   . HOH I 3 .   ? 25.966 4.737   -16.374 1.00 50.09  ? 552 HOH B O   1 
HETATM 4521 O O   . HOH I 3 .   ? 36.044 -2.777  -11.619 1.00 43.09  ? 553 HOH B O   1 
HETATM 4522 O O   . HOH I 3 .   ? 36.823 -23.746 10.436  1.00 58.31  ? 554 HOH B O   1 
HETATM 4523 O O   . HOH I 3 .   ? 29.055 2.167   7.848   1.00 52.07  ? 555 HOH B O   1 
HETATM 4524 O O   . HOH I 3 .   ? 28.469 30.591  -6.304  1.00 52.52  ? 556 HOH B O   1 
HETATM 4525 O O   . HOH I 3 .   ? 44.352 -19.060 3.697   1.00 57.03  ? 557 HOH B O   1 
HETATM 4526 O O   . HOH I 3 .   ? 49.711 19.966  10.951  1.00 56.76  ? 558 HOH B O   1 
HETATM 4527 O O   . HOH I 3 .   ? 46.972 0.524   -2.242  1.00 60.17  ? 559 HOH B O   1 
HETATM 4528 O O   . HOH I 3 .   ? 44.593 6.900   -11.953 1.00 68.44  ? 560 HOH B O   1 
HETATM 4529 O O   . HOH I 3 .   ? 24.338 2.499   -18.007 1.00 47.06  ? 561 HOH B O   1 
HETATM 4530 O O   . HOH I 3 .   ? 23.719 -5.411  14.387  1.00 74.38  ? 562 HOH B O   1 
HETATM 4531 O O   . HOH I 3 .   ? 43.007 39.467  -3.398  1.00 65.87  ? 563 HOH B O   1 
HETATM 4532 O O   . HOH I 3 .   ? 34.004 21.409  -9.965  1.00 55.66  ? 564 HOH B O   1 
HETATM 4533 O O   . HOH I 3 .   ? 26.866 18.616  8.659   1.00 57.09  ? 565 HOH B O   1 
HETATM 4534 O O   . HOH I 3 .   ? 33.075 -20.957 5.334   1.00 57.54  ? 566 HOH B O   1 
HETATM 4535 O O   . HOH I 3 .   ? 42.885 12.876  1.984   1.00 48.22  ? 567 HOH B O   1 
HETATM 4536 O O   . HOH I 3 .   ? 49.176 24.681  7.206   1.00 60.03  ? 568 HOH B O   1 
HETATM 4537 O O   . HOH I 3 .   ? 17.910 -10.262 -17.514 1.00 62.83  ? 569 HOH B O   1 
HETATM 4538 O O   . HOH I 3 .   ? 14.347 -16.768 6.840   1.00 76.75  ? 570 HOH B O   1 
HETATM 4539 O O   . HOH I 3 .   ? 36.373 13.052  13.511  1.00 55.28  ? 571 HOH B O   1 
HETATM 4540 O O   . HOH I 3 .   ? 42.338 -4.226  -9.472  1.00 55.34  ? 572 HOH B O   1 
HETATM 4541 O O   . HOH I 3 .   ? 43.215 2.717   1.090   1.00 62.25  ? 573 HOH B O   1 
HETATM 4542 O O   . HOH I 3 .   ? 39.625 0.096   -13.932 1.00 48.99  ? 574 HOH B O   1 
HETATM 4543 O O   . HOH I 3 .   ? 13.091 -14.856 -4.093  1.00 55.74  ? 575 HOH B O   1 
HETATM 4544 O O   . HOH I 3 .   ? 33.501 -14.808 17.657  1.00 65.37  ? 576 HOH B O   1 
HETATM 4545 O O   . HOH I 3 .   ? 23.093 -18.993 -4.825  1.00 79.55  ? 577 HOH B O   1 
HETATM 4546 O O   . HOH I 3 .   ? 52.947 -8.845  3.032   1.00 63.15  ? 578 HOH B O   1 
HETATM 4547 O O   . HOH I 3 .   ? 53.184 10.664  4.306   1.00 59.33  ? 579 HOH B O   1 
HETATM 4548 O O   . HOH I 3 .   ? 30.928 36.454  -11.056 1.00 56.28  ? 580 HOH B O   1 
HETATM 4549 O O   . HOH I 3 .   ? 23.226 7.410   -15.190 1.00 63.58  ? 581 HOH B O   1 
HETATM 4550 O O   . HOH I 3 .   ? 17.379 9.854   10.745  1.00 60.46  ? 582 HOH B O   1 
HETATM 4551 O O   . HOH I 3 .   ? 26.208 -18.837 10.048  1.00 61.68  ? 583 HOH B O   1 
HETATM 4552 O O   . HOH I 3 .   ? 38.391 25.094  14.869  1.00 82.68  ? 584 HOH B O   1 
HETATM 4553 O O   . HOH I 3 .   ? 16.992 12.912  6.766   1.00 60.35  ? 585 HOH B O   1 
HETATM 4554 O O   . HOH I 3 .   ? 20.335 -12.613 7.388   1.00 52.35  ? 586 HOH B O   1 
HETATM 4555 O O   . HOH I 3 .   ? 18.761 -0.970  -17.875 1.00 59.38  ? 587 HOH B O   1 
HETATM 4556 O O   . HOH I 3 .   ? 40.158 -25.357 6.713   1.00 56.30  ? 588 HOH B O   1 
HETATM 4557 O O   . HOH I 3 .   ? 38.109 -4.098  -11.979 1.00 53.87  ? 589 HOH B O   1 
# 
