data_8Y12
# 
_entry.id   8Y12 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8Y12         pdb_00008y12 10.2210/pdb8y12/pdb 
WWPDB D_1300044293 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        8Y12 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gaoweizheng@ecust.edu.cn 
_pdbx_contact_author.name_first         GaoWei 
_pdbx_contact_author.name_last          Zheng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5918-6047 
# 
_audit_author.name               'Shi, M.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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                     'NADPH complex of Imine Reductase from Pochonia chlamydosporia 170' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Shi, M.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 Oxidoreductase                                     30754.488 2   ? ? ? ? 
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                            106.120   2   ? ? ? ? 
3 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 743.405   2   ? ? ? ? 
4 water       nat water                                              18.015    336 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Imine reductase' 
# 
_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       
;MSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSASKAASLVAQGVTVAATPAECVASSPTIVICLLSYDVTQQTL
DEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMVPPILLGQPSSVTLISGPKTAYESQKELLSSIGTTRH
VSDDIAKASLLDNALLSIMGGVFEGWVQALAIVGKAGEDEVDFAALASPFVKSMADWLPRIAGHVREKQYVGGSPLTMQL
EALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSASKAASLVAQGVTVAATPAECVASSPTIVICLLSYDVTQQTL
DEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMVPPILLGQPSSVTLISGPKTAYESQKELLSSIGTTRH
VSDDIAKASLLDNALLSIMGGVFEGWVQALAIVGKAGEDEVDFAALASPFVKSMADWLPRIAGHVREKQYVGGSPLTMQL
EALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_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 'DI(HYDROXYETHYL)ETHER'                            PEG 
3 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
4 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   SER n 
1 3   SER n 
1 4   SER n 
1 5   ASN n 
1 6   LYS n 
1 7   PRO n 
1 8   HIS n 
1 9   VAL n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLY n 
1 14  LEU n 
1 15  GLY n 
1 16  ASN n 
1 17  MET n 
1 18  GLY n 
1 19  LEU n 
1 20  ALA n 
1 21  ILE n 
1 22  ALA n 
1 23  ASN n 
1 24  CYS n 
1 25  LEU n 
1 26  ILE n 
1 27  LYS n 
1 28  SER n 
1 29  GLY n 
1 30  CYS n 
1 31  LYS n 
1 32  LEU n 
1 33  THR n 
1 34  VAL n 
1 35  TRP n 
1 36  ASN n 
1 37  ARG n 
1 38  SER n 
1 39  ALA n 
1 40  SER n 
1 41  LYS n 
1 42  ALA n 
1 43  ALA n 
1 44  SER n 
1 45  LEU n 
1 46  VAL n 
1 47  ALA n 
1 48  GLN n 
1 49  GLY n 
1 50  VAL n 
1 51  THR n 
1 52  VAL n 
1 53  ALA n 
1 54  ALA n 
1 55  THR n 
1 56  PRO n 
1 57  ALA n 
1 58  GLU n 
1 59  CYS n 
1 60  VAL n 
1 61  ALA n 
1 62  SER n 
1 63  SER n 
1 64  PRO n 
1 65  THR n 
1 66  ILE n 
1 67  VAL n 
1 68  ILE n 
1 69  CYS n 
1 70  LEU n 
1 71  LEU n 
1 72  SER n 
1 73  TYR n 
1 74  ASP n 
1 75  VAL n 
1 76  THR n 
1 77  GLN n 
1 78  GLN n 
1 79  THR n 
1 80  LEU n 
1 81  ASP n 
1 82  GLU n 
1 83  VAL n 
1 84  ILE n 
1 85  ASP n 
1 86  LEU n 
1 87  SER n 
1 88  GLY n 
1 89  LYS n 
1 90  THR n 
1 91  ILE n 
1 92  ILE n 
1 93  ASN n 
1 94  LEU n 
1 95  THR n 
1 96  ASN n 
1 97  GLY n 
1 98  THR n 
1 99  PRO n 
1 100 GLN n 
1 101 GLN n 
1 102 ALA n 
1 103 VAL n 
1 104 LYS n 
1 105 VAL n 
1 106 ALA n 
1 107 THR n 
1 108 LEU n 
1 109 VAL n 
1 110 GLN n 
1 111 GLN n 
1 112 ARG n 
1 113 GLY n 
1 114 ALA n 
1 115 GLU n 
1 116 SER n 
1 117 TYR n 
1 118 ILE n 
1 119 HIS n 
1 120 GLY n 
1 121 ALA n 
1 122 ILE n 
1 123 MET n 
1 124 VAL n 
1 125 PRO n 
1 126 PRO n 
1 127 ILE n 
1 128 LEU n 
1 129 LEU n 
1 130 GLY n 
1 131 GLN n 
1 132 PRO n 
1 133 SER n 
1 134 SER n 
1 135 VAL n 
1 136 THR n 
1 137 LEU n 
1 138 ILE n 
1 139 SER n 
1 140 GLY n 
1 141 PRO n 
1 142 LYS n 
1 143 THR n 
1 144 ALA n 
1 145 TYR n 
1 146 GLU n 
1 147 SER n 
1 148 GLN n 
1 149 LYS n 
1 150 GLU n 
1 151 LEU n 
1 152 LEU n 
1 153 SER n 
1 154 SER n 
1 155 ILE n 
1 156 GLY n 
1 157 THR n 
1 158 THR n 
1 159 ARG n 
1 160 HIS n 
1 161 VAL n 
1 162 SER n 
1 163 ASP n 
1 164 ASP n 
1 165 ILE n 
1 166 ALA n 
1 167 LYS n 
1 168 ALA n 
1 169 SER n 
1 170 LEU n 
1 171 LEU n 
1 172 ASP n 
1 173 ASN n 
1 174 ALA n 
1 175 LEU n 
1 176 LEU n 
1 177 SER n 
1 178 ILE n 
1 179 MET n 
1 180 GLY n 
1 181 GLY n 
1 182 VAL n 
1 183 PHE n 
1 184 GLU n 
1 185 GLY n 
1 186 TRP n 
1 187 VAL n 
1 188 GLN n 
1 189 ALA n 
1 190 LEU n 
1 191 ALA n 
1 192 ILE n 
1 193 VAL n 
1 194 GLY n 
1 195 LYS n 
1 196 ALA n 
1 197 GLY n 
1 198 GLU n 
1 199 ASP n 
1 200 GLU n 
1 201 VAL n 
1 202 ASP n 
1 203 PHE n 
1 204 ALA n 
1 205 ALA n 
1 206 LEU n 
1 207 ALA n 
1 208 SER n 
1 209 PRO n 
1 210 PHE n 
1 211 VAL n 
1 212 LYS n 
1 213 SER n 
1 214 MET n 
1 215 ALA n 
1 216 ASP n 
1 217 TRP n 
1 218 LEU n 
1 219 PRO n 
1 220 ARG n 
1 221 ILE n 
1 222 ALA n 
1 223 GLY n 
1 224 HIS n 
1 225 VAL n 
1 226 ARG n 
1 227 GLU n 
1 228 LYS n 
1 229 GLN n 
1 230 TYR n 
1 231 VAL n 
1 232 GLY n 
1 233 GLY n 
1 234 SER n 
1 235 PRO n 
1 236 LEU n 
1 237 THR n 
1 238 MET n 
1 239 GLN n 
1 240 LEU n 
1 241 GLU n 
1 242 ALA n 
1 243 LEU n 
1 244 GLU n 
1 245 ASN n 
1 246 ILE n 
1 247 SER n 
1 248 GLU n 
1 249 THR n 
1 250 SER n 
1 251 ARG n 
1 252 GLU n 
1 253 LEU n 
1 254 GLY n 
1 255 VAL n 
1 256 GLY n 
1 257 VAL n 
1 258 LEU n 
1 259 LEU n 
1 260 GLY n 
1 261 SER n 
1 262 MET n 
1 263 ARG n 
1 264 GLU n 
1 265 VAL n 
1 266 MET n 
1 267 SER n 
1 268 GLU n 
1 269 ALA n 
1 270 VAL n 
1 271 LYS n 
1 272 LYS n 
1 273 GLY n 
1 274 LYS n 
1 275 GLY n 
1 276 GLY n 
1 277 GLU n 
1 278 SER n 
1 279 ILE n 
1 280 ALA n 
1 281 GLY n 
1 282 LEU n 
1 283 VAL n 
1 284 PRO n 
1 285 MET n 
1 286 LEU n 
1 287 THR n 
1 288 GLU n 
1 289 LEU n 
1 290 ASP n 
1 291 LYS n 
1 292 LYS n 
1 293 TRP 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                   293 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 VFPPC_03305 
_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      'Pochonia chlamydosporia 170' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1380566 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                            ?                                            
'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                           ?                                            
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                         ?                                            
'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                    ?                                            
'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                           ?                                            
'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                          ?                                            
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                    ?                                            
'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                            ?                                            
'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                          ?                                            
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                              ?                                            'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                         ?                                            
'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                            ?                                            
'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                             ?                                            
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                         ?                                            
'C5 H11 N O2 S'     149.211 
NAP non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                            ?                                            
'C4 H10 O3'         106.120 
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   SER 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   ASN 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   PRO 7   7   7   PRO PRO A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  ILE 12  12  12  ILE ILE A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  LEU 19  19  19  LEU LEU A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  CYS 24  24  24  CYS CYS A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  CYS 30  30  30  CYS CYS A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  ASN 36  36  36  ASN ASN A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  SER 38  38  38  SER SER A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  CYS 59  59  59  CYS CYS 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  SER 62  62  62  SER SER A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  ILE 66  66  66  ILE ILE A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  CYS 69  69  69  CYS CYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  GLN 78  78  78  GLN GLN A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  VAL 83  83  83  VAL VAL A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  LEU 94  94  94  LEU LEU A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 GLN 100 100 100 GLN GLN A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 GLN 111 111 111 GLN GLN A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ILE 122 122 122 ILE ILE A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 LEU 137 137 137 LEU LEU A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 LYS 142 142 142 LYS LYS A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 GLN 148 148 148 GLN GLN A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 THR 157 157 157 THR THR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 ARG 159 159 159 ARG ARG A . n 
A 1 160 HIS 160 160 160 HIS HIS A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 LEU 170 170 170 LEU LEU A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 ASN 173 173 173 ASN ASN A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 ILE 178 178 178 ILE ILE A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 GLY 181 181 181 GLY GLY A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 TRP 186 186 186 TRP TRP A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 LYS 195 195 195 LYS LYS A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 GLU 200 200 200 GLU GLU A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 SER 213 213 213 SER SER A . n 
A 1 214 MET 214 214 214 MET MET A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 TRP 217 217 217 TRP TRP A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 HIS 224 224 224 HIS HIS A . n 
A 1 225 VAL 225 225 225 VAL VAL A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLY 233 233 233 GLY GLY 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 LEU 236 236 236 LEU LEU A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 MET 238 238 238 MET MET A . n 
A 1 239 GLN 239 239 239 GLN GLN A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 ILE 246 246 246 ILE ILE A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 ARG 251 251 251 ARG ARG A . n 
A 1 252 GLU 252 252 252 GLU GLU A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 GLY 254 254 254 GLY GLY A . n 
A 1 255 VAL 255 255 255 VAL VAL A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 MET 262 262 262 MET MET A . n 
A 1 263 ARG 263 263 263 ARG ARG A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 MET 266 266 266 MET MET A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 LYS 271 271 271 LYS LYS A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 LYS 274 274 274 LYS LYS A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 SER 278 278 278 SER SER A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 PRO 284 284 284 PRO PRO A . n 
A 1 285 MET 285 285 285 MET MET A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 THR 287 287 287 THR THR A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 ASP 290 290 290 ASP ASP A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 LYS 292 292 292 LYS LYS A . n 
A 1 293 TRP 293 293 293 TRP TRP A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   SER 4   4   ?   ?   ?   B . n 
B 1 5   ASN 5   5   ?   ?   ?   B . n 
B 1 6   LYS 6   6   ?   ?   ?   B . n 
B 1 7   PRO 7   7   7   PRO PRO B . n 
B 1 8   HIS 8   8   8   HIS HIS B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  ILE 12  12  12  ILE ILE B . n 
B 1 13  GLY 13  13  13  GLY GLY B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  ASN 16  16  16  ASN ASN B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  LEU 19  19  19  LEU LEU B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ILE 21  21  21  ILE ILE B . n 
B 1 22  ALA 22  22  22  ALA ALA B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  CYS 24  24  24  CYS CYS B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  CYS 30  30  30  CYS CYS B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  TRP 35  35  35  TRP TRP B . n 
B 1 36  ASN 36  36  36  ASN ASN B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  SER 38  38  38  SER SER B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  SER 40  40  40  SER SER B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  VAL 46  46  46  VAL VAL B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  THR 51  51  51  THR THR B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  THR 55  55  55  THR THR B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  ALA 57  57  57  ALA ALA B . n 
B 1 58  GLU 58  58  58  GLU GLU B . n 
B 1 59  CYS 59  59  59  CYS CYS 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  SER 62  62  62  SER SER B . n 
B 1 63  SER 63  63  63  SER SER B . n 
B 1 64  PRO 64  64  64  PRO PRO B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  ILE 66  66  66  ILE ILE B . n 
B 1 67  VAL 67  67  67  VAL VAL B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  CYS 69  69  69  CYS CYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  TYR 73  73  73  TYR TYR B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  THR 76  76  76  THR THR B . n 
B 1 77  GLN 77  77  77  GLN GLN B . n 
B 1 78  GLN 78  78  78  GLN GLN B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  LEU 80  80  80  LEU LEU B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  GLU 82  82  82  GLU GLU B . n 
B 1 83  VAL 83  83  83  VAL VAL B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  SER 87  87  87  SER SER B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  ILE 91  91  91  ILE ILE B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  ASN 93  93  93  ASN ASN B . n 
B 1 94  LEU 94  94  94  LEU LEU B . n 
B 1 95  THR 95  95  95  THR THR B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 GLN 100 100 100 GLN GLN B . n 
B 1 101 GLN 101 101 101 GLN GLN B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 LYS 104 104 104 LYS LYS B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 ALA 106 106 106 ALA ALA B . n 
B 1 107 THR 107 107 107 THR THR B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 VAL 109 109 109 VAL VAL B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 GLN 111 111 111 GLN GLN B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 SER 116 116 116 SER SER B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ILE 122 122 122 ILE ILE B . n 
B 1 123 MET 123 123 123 MET MET B . n 
B 1 124 VAL 124 124 124 VAL VAL B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 VAL 135 135 135 VAL VAL B . n 
B 1 136 THR 136 136 136 THR THR B . n 
B 1 137 LEU 137 137 137 LEU LEU B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 LYS 142 142 142 LYS LYS B . n 
B 1 143 THR 143 143 143 THR THR B . n 
B 1 144 ALA 144 144 144 ALA ALA B . n 
B 1 145 TYR 145 145 145 TYR TYR B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 GLN 148 148 148 GLN GLN B . n 
B 1 149 LYS 149 149 149 LYS LYS B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 GLY 156 156 156 GLY GLY B . n 
B 1 157 THR 157 157 157 THR THR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 ARG 159 159 159 ARG ARG B . n 
B 1 160 HIS 160 160 160 HIS HIS B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 ALA 166 166 166 ALA ALA B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 LEU 170 170 170 LEU LEU B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 ASP 172 172 172 ASP ASP B . n 
B 1 173 ASN 173 173 173 ASN ASN B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 LEU 175 175 175 LEU LEU B . n 
B 1 176 LEU 176 176 176 LEU LEU B . n 
B 1 177 SER 177 177 177 SER SER B . n 
B 1 178 ILE 178 178 178 ILE ILE B . n 
B 1 179 MET 179 179 179 MET MET B . n 
B 1 180 GLY 180 180 180 GLY GLY B . n 
B 1 181 GLY 181 181 181 GLY GLY B . n 
B 1 182 VAL 182 182 182 VAL VAL B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 GLY 185 185 185 GLY GLY B . n 
B 1 186 TRP 186 186 186 TRP TRP B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 GLY 194 194 194 GLY GLY B . n 
B 1 195 LYS 195 195 195 LYS LYS B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 GLU 198 198 198 GLU GLU B . n 
B 1 199 ASP 199 199 199 ASP ASP B . n 
B 1 200 GLU 200 200 200 GLU GLU B . n 
B 1 201 VAL 201 201 201 VAL VAL B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 LEU 206 206 206 LEU LEU B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 SER 208 208 208 SER SER B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 PHE 210 210 210 PHE PHE B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 SER 213 213 213 SER SER B . n 
B 1 214 MET 214 214 214 MET MET B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 TRP 217 217 217 TRP TRP B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 ARG 220 220 220 ARG ARG B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 HIS 224 224 224 HIS HIS B . n 
B 1 225 VAL 225 225 225 VAL VAL B . n 
B 1 226 ARG 226 226 226 ARG ARG B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 LYS 228 228 228 LYS LYS B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 VAL 231 231 231 VAL VAL B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 GLY 233 233 233 GLY GLY 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 LEU 236 236 236 LEU LEU B . n 
B 1 237 THR 237 237 237 THR THR B . n 
B 1 238 MET 238 238 238 MET MET B . n 
B 1 239 GLN 239 239 239 GLN GLN B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 ALA 242 242 242 ALA ALA B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 ILE 246 246 246 ILE ILE B . n 
B 1 247 SER 247 247 247 SER SER B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 SER 250 250 250 SER SER B . n 
B 1 251 ARG 251 251 251 ARG ARG B . n 
B 1 252 GLU 252 252 252 GLU GLU B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 GLY 254 254 254 GLY GLY B . n 
B 1 255 VAL 255 255 255 VAL VAL B . n 
B 1 256 GLY 256 256 256 GLY GLY B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 MET 262 262 262 MET MET B . n 
B 1 263 ARG 263 263 263 ARG ARG B . n 
B 1 264 GLU 264 264 264 GLU GLU B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 MET 266 266 266 MET MET B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 GLU 268 268 268 GLU GLU B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 LYS 271 271 271 LYS LYS B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 LYS 274 274 274 LYS LYS B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 GLY 276 276 276 GLY GLY B . n 
B 1 277 GLU 277 277 277 GLU GLU B . n 
B 1 278 SER 278 278 278 SER SER B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 PRO 284 284 284 PRO PRO B . n 
B 1 285 MET 285 285 285 MET MET B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 THR 287 287 287 THR THR B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 LEU 289 289 289 LEU LEU B . n 
B 1 290 ASP 290 290 290 ASP ASP B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 LYS 292 292 292 LYS LYS B . n 
B 1 293 TRP 293 293 293 TRP TRP B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PEG 1   2901 2901 PEG PEG A . 
D 3 NAP 1   2902 3401 NAP NAP A . 
E 2 PEG 1   3601 3601 PEG PEG B . 
F 3 NAP 1   3602 4101 NAP NAP B . 
G 4 HOH 1   3001 325  HOH HOH A . 
G 4 HOH 2   3002 68   HOH HOH A . 
G 4 HOH 3   3003 39   HOH HOH A . 
G 4 HOH 4   3004 85   HOH HOH A . 
G 4 HOH 5   3005 287  HOH HOH A . 
G 4 HOH 6   3006 101  HOH HOH A . 
G 4 HOH 7   3007 269  HOH HOH A . 
G 4 HOH 8   3008 309  HOH HOH A . 
G 4 HOH 9   3009 202  HOH HOH A . 
G 4 HOH 10  3010 247  HOH HOH A . 
G 4 HOH 11  3011 314  HOH HOH A . 
G 4 HOH 12  3012 69   HOH HOH A . 
G 4 HOH 13  3013 316  HOH HOH A . 
G 4 HOH 14  3014 92   HOH HOH A . 
G 4 HOH 15  3015 189  HOH HOH A . 
G 4 HOH 16  3016 124  HOH HOH A . 
G 4 HOH 17  3017 164  HOH HOH A . 
G 4 HOH 18  3018 108  HOH HOH A . 
G 4 HOH 19  3019 2    HOH HOH A . 
G 4 HOH 20  3020 236  HOH HOH A . 
G 4 HOH 21  3021 147  HOH HOH A . 
G 4 HOH 22  3022 275  HOH HOH A . 
G 4 HOH 23  3023 187  HOH HOH A . 
G 4 HOH 24  3024 79   HOH HOH A . 
G 4 HOH 25  3025 6    HOH HOH A . 
G 4 HOH 26  3026 266  HOH HOH A . 
G 4 HOH 27  3027 67   HOH HOH A . 
G 4 HOH 28  3028 308  HOH HOH A . 
G 4 HOH 29  3029 245  HOH HOH A . 
G 4 HOH 30  3030 191  HOH HOH A . 
G 4 HOH 31  3031 15   HOH HOH A . 
G 4 HOH 32  3032 66   HOH HOH A . 
G 4 HOH 33  3033 240  HOH HOH A . 
G 4 HOH 34  3034 81   HOH HOH A . 
G 4 HOH 35  3035 272  HOH HOH A . 
G 4 HOH 36  3036 244  HOH HOH A . 
G 4 HOH 37  3037 213  HOH HOH A . 
G 4 HOH 38  3038 27   HOH HOH A . 
G 4 HOH 39  3039 268  HOH HOH A . 
G 4 HOH 40  3040 167  HOH HOH A . 
G 4 HOH 41  3041 23   HOH HOH A . 
G 4 HOH 42  3042 106  HOH HOH A . 
G 4 HOH 43  3043 145  HOH HOH A . 
G 4 HOH 44  3044 264  HOH HOH A . 
G 4 HOH 45  3045 212  HOH HOH A . 
G 4 HOH 46  3046 30   HOH HOH A . 
G 4 HOH 47  3047 168  HOH HOH A . 
G 4 HOH 48  3048 42   HOH HOH A . 
G 4 HOH 49  3049 256  HOH HOH A . 
G 4 HOH 50  3050 1    HOH HOH A . 
G 4 HOH 51  3051 179  HOH HOH A . 
G 4 HOH 52  3052 32   HOH HOH A . 
G 4 HOH 53  3053 194  HOH HOH A . 
G 4 HOH 54  3054 65   HOH HOH A . 
G 4 HOH 55  3055 192  HOH HOH A . 
G 4 HOH 56  3056 28   HOH HOH A . 
G 4 HOH 57  3057 159  HOH HOH A . 
G 4 HOH 58  3058 265  HOH HOH A . 
G 4 HOH 59  3059 284  HOH HOH A . 
G 4 HOH 60  3060 76   HOH HOH A . 
G 4 HOH 61  3061 267  HOH HOH A . 
G 4 HOH 62  3062 201  HOH HOH A . 
G 4 HOH 63  3063 80   HOH HOH A . 
G 4 HOH 64  3064 196  HOH HOH A . 
G 4 HOH 65  3065 171  HOH HOH A . 
G 4 HOH 66  3066 20   HOH HOH A . 
G 4 HOH 67  3067 208  HOH HOH A . 
G 4 HOH 68  3068 29   HOH HOH A . 
G 4 HOH 69  3069 103  HOH HOH A . 
G 4 HOH 70  3070 200  HOH HOH A . 
G 4 HOH 71  3071 151  HOH HOH A . 
G 4 HOH 72  3072 139  HOH HOH A . 
G 4 HOH 73  3073 43   HOH HOH A . 
G 4 HOH 74  3074 10   HOH HOH A . 
G 4 HOH 75  3075 150  HOH HOH A . 
G 4 HOH 76  3076 170  HOH HOH A . 
G 4 HOH 77  3077 173  HOH HOH A . 
G 4 HOH 78  3078 239  HOH HOH A . 
G 4 HOH 79  3079 231  HOH HOH A . 
G 4 HOH 80  3080 313  HOH HOH A . 
G 4 HOH 81  3081 3    HOH HOH A . 
G 4 HOH 82  3082 281  HOH HOH A . 
G 4 HOH 83  3083 13   HOH HOH A . 
G 4 HOH 84  3084 153  HOH HOH A . 
G 4 HOH 85  3085 115  HOH HOH A . 
G 4 HOH 86  3086 161  HOH HOH A . 
G 4 HOH 87  3087 135  HOH HOH A . 
G 4 HOH 88  3088 304  HOH HOH A . 
G 4 HOH 89  3089 49   HOH HOH A . 
G 4 HOH 90  3090 282  HOH HOH A . 
G 4 HOH 91  3091 37   HOH HOH A . 
G 4 HOH 92  3092 25   HOH HOH A . 
G 4 HOH 93  3093 158  HOH HOH A . 
G 4 HOH 94  3094 86   HOH HOH A . 
G 4 HOH 95  3095 255  HOH HOH A . 
G 4 HOH 96  3096 109  HOH HOH A . 
G 4 HOH 97  3097 113  HOH HOH A . 
G 4 HOH 98  3098 46   HOH HOH A . 
G 4 HOH 99  3099 182  HOH HOH A . 
G 4 HOH 100 3100 125  HOH HOH A . 
G 4 HOH 101 3101 107  HOH HOH A . 
G 4 HOH 102 3102 140  HOH HOH A . 
G 4 HOH 103 3103 175  HOH HOH A . 
G 4 HOH 104 3104 230  HOH HOH A . 
G 4 HOH 105 3105 104  HOH HOH A . 
G 4 HOH 106 3106 274  HOH HOH A . 
G 4 HOH 107 3107 100  HOH HOH A . 
G 4 HOH 108 3108 146  HOH HOH A . 
G 4 HOH 109 3109 178  HOH HOH A . 
G 4 HOH 110 3110 271  HOH HOH A . 
G 4 HOH 111 3111 184  HOH HOH A . 
G 4 HOH 112 3112 12   HOH HOH A . 
G 4 HOH 113 3113 317  HOH HOH A . 
G 4 HOH 114 3114 127  HOH HOH A . 
G 4 HOH 115 3115 50   HOH HOH A . 
G 4 HOH 116 3116 254  HOH HOH A . 
G 4 HOH 117 3117 279  HOH HOH A . 
G 4 HOH 118 3118 273  HOH HOH A . 
G 4 HOH 119 3119 203  HOH HOH A . 
G 4 HOH 120 3120 58   HOH HOH A . 
G 4 HOH 121 3121 98   HOH HOH A . 
G 4 HOH 122 3122 210  HOH HOH A . 
G 4 HOH 123 3123 237  HOH HOH A . 
G 4 HOH 124 3124 138  HOH HOH A . 
G 4 HOH 125 3125 52   HOH HOH A . 
G 4 HOH 126 3126 105  HOH HOH A . 
G 4 HOH 127 3127 283  HOH HOH A . 
G 4 HOH 128 3128 300  HOH HOH A . 
G 4 HOH 129 3129 259  HOH HOH A . 
G 4 HOH 130 3130 312  HOH HOH A . 
G 4 HOH 131 3131 131  HOH HOH A . 
G 4 HOH 132 3132 41   HOH HOH A . 
G 4 HOH 133 3133 8    HOH HOH A . 
G 4 HOH 134 3134 22   HOH HOH A . 
G 4 HOH 135 3135 112  HOH HOH A . 
G 4 HOH 136 3136 330  HOH HOH A . 
G 4 HOH 137 3137 207  HOH HOH A . 
G 4 HOH 138 3138 324  HOH HOH A . 
G 4 HOH 139 3139 72   HOH HOH A . 
G 4 HOH 140 3140 329  HOH HOH A . 
G 4 HOH 141 3141 73   HOH HOH A . 
G 4 HOH 142 3142 36   HOH HOH A . 
G 4 HOH 143 3143 197  HOH HOH A . 
G 4 HOH 144 3144 84   HOH HOH A . 
G 4 HOH 145 3145 320  HOH HOH A . 
G 4 HOH 146 3146 87   HOH HOH A . 
G 4 HOH 147 3147 83   HOH HOH A . 
G 4 HOH 148 3148 206  HOH HOH A . 
G 4 HOH 149 3149 217  HOH HOH A . 
G 4 HOH 150 3150 82   HOH HOH A . 
G 4 HOH 151 3151 193  HOH HOH A . 
G 4 HOH 152 3152 290  HOH HOH A . 
G 4 HOH 153 3153 261  HOH HOH A . 
G 4 HOH 154 3154 257  HOH HOH A . 
G 4 HOH 155 3155 93   HOH HOH A . 
G 4 HOH 156 3156 78   HOH HOH A . 
G 4 HOH 157 3157 216  HOH HOH A . 
G 4 HOH 158 3158 327  HOH HOH A . 
G 4 HOH 159 3159 323  HOH HOH A . 
G 4 HOH 160 3160 328  HOH HOH A . 
G 4 HOH 161 3161 205  HOH HOH A . 
G 4 HOH 162 3162 303  HOH HOH A . 
G 4 HOH 163 3163 44   HOH HOH A . 
H 4 HOH 1   3701 19   HOH HOH B . 
H 4 HOH 2   3702 56   HOH HOH B . 
H 4 HOH 3   3703 144  HOH HOH B . 
H 4 HOH 4   3704 89   HOH HOH B . 
H 4 HOH 5   3705 227  HOH HOH B . 
H 4 HOH 6   3706 295  HOH HOH B . 
H 4 HOH 7   3707 143  HOH HOH B . 
H 4 HOH 8   3708 38   HOH HOH B . 
H 4 HOH 9   3709 116  HOH HOH B . 
H 4 HOH 10  3710 294  HOH HOH B . 
H 4 HOH 11  3711 126  HOH HOH B . 
H 4 HOH 12  3712 152  HOH HOH B . 
H 4 HOH 13  3713 286  HOH HOH B . 
H 4 HOH 14  3714 70   HOH HOH B . 
H 4 HOH 15  3715 280  HOH HOH B . 
H 4 HOH 16  3716 296  HOH HOH B . 
H 4 HOH 17  3717 64   HOH HOH B . 
H 4 HOH 18  3718 188  HOH HOH B . 
H 4 HOH 19  3719 96   HOH HOH B . 
H 4 HOH 20  3720 121  HOH HOH B . 
H 4 HOH 21  3721 123  HOH HOH B . 
H 4 HOH 22  3722 31   HOH HOH B . 
H 4 HOH 23  3723 228  HOH HOH B . 
H 4 HOH 24  3724 61   HOH HOH B . 
H 4 HOH 25  3725 183  HOH HOH B . 
H 4 HOH 26  3726 57   HOH HOH B . 
H 4 HOH 27  3727 74   HOH HOH B . 
H 4 HOH 28  3728 311  HOH HOH B . 
H 4 HOH 29  3729 94   HOH HOH B . 
H 4 HOH 30  3730 60   HOH HOH B . 
H 4 HOH 31  3731 285  HOH HOH B . 
H 4 HOH 32  3732 218  HOH HOH B . 
H 4 HOH 33  3733 198  HOH HOH B . 
H 4 HOH 34  3734 133  HOH HOH B . 
H 4 HOH 35  3735 26   HOH HOH B . 
H 4 HOH 36  3736 4    HOH HOH B . 
H 4 HOH 37  3737 141  HOH HOH B . 
H 4 HOH 38  3738 243  HOH HOH B . 
H 4 HOH 39  3739 299  HOH HOH B . 
H 4 HOH 40  3740 253  HOH HOH B . 
H 4 HOH 41  3741 172  HOH HOH B . 
H 4 HOH 42  3742 185  HOH HOH B . 
H 4 HOH 43  3743 226  HOH HOH B . 
H 4 HOH 44  3744 235  HOH HOH B . 
H 4 HOH 45  3745 214  HOH HOH B . 
H 4 HOH 46  3746 176  HOH HOH B . 
H 4 HOH 47  3747 88   HOH HOH B . 
H 4 HOH 48  3748 34   HOH HOH B . 
H 4 HOH 49  3749 177  HOH HOH B . 
H 4 HOH 50  3750 169  HOH HOH B . 
H 4 HOH 51  3751 250  HOH HOH B . 
H 4 HOH 52  3752 91   HOH HOH B . 
H 4 HOH 53  3753 181  HOH HOH B . 
H 4 HOH 54  3754 162  HOH HOH B . 
H 4 HOH 55  3755 252  HOH HOH B . 
H 4 HOH 56  3756 9    HOH HOH B . 
H 4 HOH 57  3757 334  HOH HOH B . 
H 4 HOH 58  3758 136  HOH HOH B . 
H 4 HOH 59  3759 118  HOH HOH B . 
H 4 HOH 60  3760 246  HOH HOH B . 
H 4 HOH 61  3761 102  HOH HOH B . 
H 4 HOH 62  3762 157  HOH HOH B . 
H 4 HOH 63  3763 160  HOH HOH B . 
H 4 HOH 64  3764 14   HOH HOH B . 
H 4 HOH 65  3765 336  HOH HOH B . 
H 4 HOH 66  3766 18   HOH HOH B . 
H 4 HOH 67  3767 142  HOH HOH B . 
H 4 HOH 68  3768 234  HOH HOH B . 
H 4 HOH 69  3769 190  HOH HOH B . 
H 4 HOH 70  3770 204  HOH HOH B . 
H 4 HOH 71  3771 122  HOH HOH B . 
H 4 HOH 72  3772 130  HOH HOH B . 
H 4 HOH 73  3773 156  HOH HOH B . 
H 4 HOH 74  3774 59   HOH HOH B . 
H 4 HOH 75  3775 258  HOH HOH B . 
H 4 HOH 76  3776 225  HOH HOH B . 
H 4 HOH 77  3777 114  HOH HOH B . 
H 4 HOH 78  3778 35   HOH HOH B . 
H 4 HOH 79  3779 5    HOH HOH B . 
H 4 HOH 80  3780 62   HOH HOH B . 
H 4 HOH 81  3781 129  HOH HOH B . 
H 4 HOH 82  3782 199  HOH HOH B . 
H 4 HOH 83  3783 238  HOH HOH B . 
H 4 HOH 84  3784 209  HOH HOH B . 
H 4 HOH 85  3785 137  HOH HOH B . 
H 4 HOH 86  3786 51   HOH HOH B . 
H 4 HOH 87  3787 53   HOH HOH B . 
H 4 HOH 88  3788 241  HOH HOH B . 
H 4 HOH 89  3789 302  HOH HOH B . 
H 4 HOH 90  3790 40   HOH HOH B . 
H 4 HOH 91  3791 24   HOH HOH B . 
H 4 HOH 92  3792 132  HOH HOH B . 
H 4 HOH 93  3793 163  HOH HOH B . 
H 4 HOH 94  3794 154  HOH HOH B . 
H 4 HOH 95  3795 278  HOH HOH B . 
H 4 HOH 96  3796 223  HOH HOH B . 
H 4 HOH 97  3797 75   HOH HOH B . 
H 4 HOH 98  3798 17   HOH HOH B . 
H 4 HOH 99  3799 301  HOH HOH B . 
H 4 HOH 100 3800 180  HOH HOH B . 
H 4 HOH 101 3801 7    HOH HOH B . 
H 4 HOH 102 3802 166  HOH HOH B . 
H 4 HOH 103 3803 249  HOH HOH B . 
H 4 HOH 104 3804 224  HOH HOH B . 
H 4 HOH 105 3805 155  HOH HOH B . 
H 4 HOH 106 3806 77   HOH HOH B . 
H 4 HOH 107 3807 186  HOH HOH B . 
H 4 HOH 108 3808 149  HOH HOH B . 
H 4 HOH 109 3809 332  HOH HOH B . 
H 4 HOH 110 3810 242  HOH HOH B . 
H 4 HOH 111 3811 134  HOH HOH B . 
H 4 HOH 112 3812 128  HOH HOH B . 
H 4 HOH 113 3813 229  HOH HOH B . 
H 4 HOH 114 3814 232  HOH HOH B . 
H 4 HOH 115 3815 95   HOH HOH B . 
H 4 HOH 116 3816 55   HOH HOH B . 
H 4 HOH 117 3817 16   HOH HOH B . 
H 4 HOH 118 3818 215  HOH HOH B . 
H 4 HOH 119 3819 63   HOH HOH B . 
H 4 HOH 120 3820 220  HOH HOH B . 
H 4 HOH 121 3821 211  HOH HOH B . 
H 4 HOH 122 3822 48   HOH HOH B . 
H 4 HOH 123 3823 315  HOH HOH B . 
H 4 HOH 124 3824 110  HOH HOH B . 
H 4 HOH 125 3825 248  HOH HOH B . 
H 4 HOH 126 3826 47   HOH HOH B . 
H 4 HOH 127 3827 21   HOH HOH B . 
H 4 HOH 128 3828 263  HOH HOH B . 
H 4 HOH 129 3829 260  HOH HOH B . 
H 4 HOH 130 3830 117  HOH HOH B . 
H 4 HOH 131 3831 71   HOH HOH B . 
H 4 HOH 132 3832 233  HOH HOH B . 
H 4 HOH 133 3833 174  HOH HOH B . 
H 4 HOH 134 3834 54   HOH HOH B . 
H 4 HOH 135 3835 11   HOH HOH B . 
H 4 HOH 136 3836 298  HOH HOH B . 
H 4 HOH 137 3837 276  HOH HOH B . 
H 4 HOH 138 3838 120  HOH HOH B . 
H 4 HOH 139 3839 326  HOH HOH B . 
H 4 HOH 140 3840 310  HOH HOH B . 
H 4 HOH 141 3841 222  HOH HOH B . 
H 4 HOH 142 3842 195  HOH HOH B . 
H 4 HOH 143 3843 321  HOH HOH B . 
H 4 HOH 144 3844 219  HOH HOH B . 
H 4 HOH 145 3845 319  HOH HOH B . 
H 4 HOH 146 3846 165  HOH HOH B . 
H 4 HOH 147 3847 318  HOH HOH B . 
H 4 HOH 148 3848 305  HOH HOH B . 
H 4 HOH 149 3849 288  HOH HOH B . 
H 4 HOH 150 3850 322  HOH HOH B . 
H 4 HOH 151 3851 90   HOH HOH B . 
H 4 HOH 152 3852 251  HOH HOH B . 
H 4 HOH 153 3853 33   HOH HOH B . 
H 4 HOH 154 3854 306  HOH HOH B . 
H 4 HOH 155 3855 221  HOH HOH B . 
H 4 HOH 156 3856 292  HOH HOH B . 
H 4 HOH 157 3857 335  HOH HOH B . 
H 4 HOH 158 3858 148  HOH HOH B . 
H 4 HOH 159 3859 97   HOH HOH B . 
H 4 HOH 160 3860 111  HOH HOH B . 
H 4 HOH 161 3861 333  HOH HOH B . 
H 4 HOH 162 3862 291  HOH HOH B . 
H 4 HOH 163 3863 99   HOH HOH B . 
H 4 HOH 164 3864 262  HOH HOH B . 
H 4 HOH 165 3865 331  HOH HOH B . 
H 4 HOH 166 3866 289  HOH HOH B . 
H 4 HOH 167 3867 297  HOH HOH B . 
H 4 HOH 168 3868 119  HOH HOH B . 
H 4 HOH 169 3869 307  HOH HOH B . 
H 4 HOH 170 3870 270  HOH HOH B . 
H 4 HOH 171 3871 277  HOH HOH B . 
H 4 HOH 172 3872 45   HOH HOH B . 
H 4 HOH 173 3873 293  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? SAINT  ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   99.34 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Y12 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.802 
_cell.length_a_esd                 ? 
_cell.length_b                     114.091 
_cell.length_b_esd                 ? 
_cell.length_c                     62.870 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8Y12 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8Y12 
_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             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.45 
_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    'PEG 3350, magnesium chloride, Tris-Hcl 8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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                         'Bruker PHOTON III' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-07-25 
_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   1.34138 
_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                      'LIQUID ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER METALJET' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.34138 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Y12 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.09 
_reflns.d_resolution_low                               33.08 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     30773 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.29 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.53 
_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                                   0.0538 
_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                                    2.09 
_reflns_shell.d_res_low                                     2.13 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.33 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1428 
_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                               2.67 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          88.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.1537 
_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]                            4.54 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.65 
_refine.aniso_B[2][2]                            -1.85 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -2.75 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.787 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.916 
_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                                 8Y12 
_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                            2.10 
_refine.ls_d_res_low                             33.08 
_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                     28926 
_refine.ls_number_reflns_R_free                  1540 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.44 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18502 
_refine.ls_R_factor_R_free                       0.25489 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18128 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.262 
_refine.pdbx_overall_ESU_R_Free                  0.219 
_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                             6.715 
_refine.overall_SU_ML                            0.170 
_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                       2.10 
_refine_hist.d_res_low                        33.08 
_refine_hist.number_atoms_solvent             336 
_refine_hist.number_atoms_total               4667 
_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        4221 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         110 
_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' ? 0.008  0.013  4397 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  4254 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.579  1.659  5980 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.297  1.582  9892 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.315  5.000  573  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 36.847 24.267 150  ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.296 15.000 760  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.525 15.000 14   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.068  0.200  609  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  4774 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  774  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.088  3.124  2298 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.088  3.124  2297 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.116  4.682  2869 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.115  4.682  2870 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.554  3.437  2099 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.554  3.437  2100 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.953  5.011  3112 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.460  38.826 5078 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.455  38.711 5031 ? 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                       2.100 
_refine_ls_shell.d_res_low                        2.155 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             105 
_refine_ls_shell.number_reflns_R_work             2050 
_refine_ls_shell.percent_reflns_obs               97.60 
_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                  0.247 
_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                  0.385 
# 
_struct.entry_id                     8Y12 
_struct.title                        'NADPH complex of Imine Reductase from Pochonia chlamydosporia 170' 
_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        8Y12 
_struct_keywords.text            'NADPH Complex, Reductive aminase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A179FZ20_METCM 
_struct_ref.pdbx_db_accession          A0A179FZ20 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSSSNKPHVSLIGLGNMGLAIANCLIKSGCKLTVWNRSASKAASLVAQGVTVAATPAECVASSPTIVICLLSYDVTQQTL
DEVIDLSGKTIINLTNGTPQQAVKVATLVQQRGAESYIHGAIMVPPILLGQPSSVTLISGPKTAYESQKELLSSIGTTRH
VSDDIAKASLLDNALLSIMGGVFEGWVQALAIVGKAGEDEVDFAALASPFVKSMADWLPRIAGHVREKQYVGGSPLTMQL
EALENISETSRELGVGVLLGSMREVMSEAVKKGKGGESIAGLVPMLTELDKKW
;
_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 8Y12 A 1 ? 293 ? A0A179FZ20 1 ? 293 ? 1 293 
2 1 8Y12 B 1 ? 293 ? A0A179FZ20 1 ? 293 ? 1 293 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 13040 ? 
1 MORE         -86   ? 
1 'SSA (A^2)'  20540 ? 
# 
_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 
# 
_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 GLY A 15  ? GLY A 29  ? GLY A 15  GLY A 29  1 ? 15 
HELX_P HELX_P2  AA2 SER A 38  ? GLY A 49  ? SER A 38  GLY A 49  5 ? 12 
HELX_P HELX_P3  AA3 THR A 55  ? SER A 62  ? THR A 55  SER A 62  1 ? 8  
HELX_P HELX_P4  AA4 SER A 72  ? ASP A 81  ? SER A 72  ASP A 81  1 ? 10 
HELX_P HELX_P5  AA5 THR A 98  ? GLN A 111 ? THR A 98  GLN A 111 1 ? 14 
HELX_P HELX_P6  AA6 PRO A 125 ? LEU A 129 ? PRO A 125 LEU A 129 5 ? 5  
HELX_P HELX_P7  AA7 PRO A 141 ? SER A 153 ? PRO A 141 SER A 153 1 ? 13 
HELX_P HELX_P8  AA8 SER A 154 ? GLY A 156 ? SER A 154 GLY A 156 5 ? 3  
HELX_P HELX_P9  AA9 ALA A 166 ? ALA A 196 ? ALA A 166 ALA A 196 1 ? 31 
HELX_P HELX_P10 AB1 ASP A 199 ? GLU A 227 ? ASP A 199 GLU A 227 1 ? 29 
HELX_P HELX_P11 AB2 PRO A 235 ? GLY A 254 ? PRO A 235 GLY A 254 1 ? 20 
HELX_P HELX_P12 AB3 LEU A 259 ? LYS A 272 ? LEU A 259 LYS A 272 1 ? 14 
HELX_P HELX_P13 AB4 SER A 278 ? ALA A 280 ? SER A 278 ALA A 280 5 ? 3  
HELX_P HELX_P14 AB5 GLY A 281 ? GLU A 288 ? GLY A 281 GLU A 288 1 ? 8  
HELX_P HELX_P15 AB6 GLY B 15  ? SER B 28  ? GLY B 15  SER B 28  1 ? 14 
HELX_P HELX_P16 AB7 SER B 38  ? LYS B 41  ? SER B 38  LYS B 41  5 ? 4  
HELX_P HELX_P17 AB8 ALA B 42  ? ALA B 47  ? ALA B 42  ALA B 47  1 ? 6  
HELX_P HELX_P18 AB9 THR B 55  ? SER B 62  ? THR B 55  SER B 62  1 ? 8  
HELX_P HELX_P19 AC1 SER B 72  ? LEU B 80  ? SER B 72  LEU B 80  1 ? 9  
HELX_P HELX_P20 AC2 THR B 98  ? GLN B 111 ? THR B 98  GLN B 111 1 ? 14 
HELX_P HELX_P21 AC3 PRO B 125 ? LEU B 129 ? PRO B 125 LEU B 129 5 ? 5  
HELX_P HELX_P22 AC4 PRO B 141 ? SER B 153 ? PRO B 141 SER B 153 1 ? 13 
HELX_P HELX_P23 AC5 SER B 154 ? GLY B 156 ? SER B 154 GLY B 156 5 ? 3  
HELX_P HELX_P24 AC6 ALA B 166 ? ALA B 196 ? ALA B 166 ALA B 196 1 ? 31 
HELX_P HELX_P25 AC7 ASP B 199 ? LYS B 228 ? ASP B 199 LYS B 228 1 ? 30 
HELX_P HELX_P26 AC8 PRO B 235 ? LEU B 253 ? PRO B 235 LEU B 253 1 ? 19 
HELX_P HELX_P27 AC9 LEU B 259 ? LYS B 272 ? LEU B 259 LYS B 272 1 ? 14 
HELX_P HELX_P28 AD1 SER B 278 ? ALA B 280 ? SER B 278 ALA B 280 5 ? 3  
HELX_P HELX_P29 AD2 GLY B 281 ? GLU B 288 ? GLY B 281 GLU B 288 1 ? 8  
# 
_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 ? 8 ? 
AA2 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? 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 THR A 51  ? VAL A 52  ? THR A 51  VAL A 52  
AA1 2 LYS A 31  ? TRP A 35  ? LYS A 31  TRP A 35  
AA1 3 HIS A 8   ? ILE A 12  ? HIS A 8   ILE A 12  
AA1 4 THR A 65  ? ILE A 68  ? THR A 65  ILE A 68  
AA1 5 THR A 90  ? ASN A 93  ? THR A 90  ASN A 93  
AA1 6 SER A 116 ? ILE A 122 ? SER A 116 ILE A 122 
AA1 7 VAL A 135 ? SER A 139 ? VAL A 135 SER A 139 
AA1 8 THR A 157 ? SER A 162 ? THR A 157 SER A 162 
AA2 1 THR B 51  ? VAL B 52  ? THR B 51  VAL B 52  
AA2 2 LYS B 31  ? TRP B 35  ? LYS B 31  TRP B 35  
AA2 3 HIS B 8   ? ILE B 12  ? HIS B 8   ILE B 12  
AA2 4 THR B 65  ? ILE B 68  ? THR B 65  ILE B 68  
AA2 5 THR B 90  ? ASN B 93  ? THR B 90  ASN B 93  
AA2 6 TYR B 117 ? ILE B 122 ? TYR B 117 ILE B 122 
AA2 7 VAL B 135 ? SER B 139 ? VAL B 135 SER B 139 
AA2 8 THR B 157 ? SER B 162 ? THR B 157 SER B 162 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O THR A 51  ? O THR A 51  N VAL A 34  ? N VAL A 34  
AA1 2 3 O LYS A 31  ? O LYS A 31  N VAL A 9   ? N VAL A 9   
AA1 3 4 N SER A 10  ? N SER A 10  O VAL A 67  ? O VAL A 67  
AA1 4 5 N ILE A 66  ? N ILE A 66  O ILE A 92  ? O ILE A 92  
AA1 5 6 N ILE A 91  ? N ILE A 91  O SER A 116 ? O SER A 116 
AA1 6 7 N HIS A 119 ? N HIS A 119 O SER A 139 ? O SER A 139 
AA1 7 8 N ILE A 138 ? N ILE A 138 O ARG A 159 ? O ARG A 159 
AA2 1 2 O THR B 51  ? O THR B 51  N VAL B 34  ? N VAL B 34  
AA2 2 3 O THR B 33  ? O THR B 33  N LEU B 11  ? N LEU B 11  
AA2 3 4 N SER B 10  ? N SER B 10  O VAL B 67  ? O VAL B 67  
AA2 4 5 N ILE B 66  ? N ILE B 66  O ILE B 92  ? O ILE B 92  
AA2 5 6 N ASN B 93  ? N ASN B 93  O ILE B 118 ? O ILE B 118 
AA2 6 7 N HIS B 119 ? N HIS B 119 O SER B 139 ? O SER B 139 
AA2 7 8 N ILE B 138 ? N ILE B 138 O ARG B 159 ? O ARG B 159 
# 
_pdbx_entry_details.entry_id                   8Y12 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    150 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   OG 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    153 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
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 LEU B 258 ? ? -98.16 -151.98 
2 1 ASP B 290 ? ? -62.40 99.71   
# 
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 SER 2 ? A SER 2 
3  1 Y 1 A SER 3 ? A SER 3 
4  1 Y 1 A SER 4 ? A SER 4 
5  1 Y 1 A ASN 5 ? A ASN 5 
6  1 Y 1 B MET 1 ? B MET 1 
7  1 Y 1 B SER 2 ? B SER 2 
8  1 Y 1 B SER 3 ? B SER 3 
9  1 Y 1 B SER 4 ? B SER 4 
10 1 Y 1 B ASN 5 ? B ASN 5 
11 1 Y 1 B LYS 6 ? B LYS 6 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAP PA   P N R 250 
NAP O1A  O N N 251 
NAP O2A  O N N 252 
NAP O5B  O N N 253 
NAP C5B  C N N 254 
NAP C4B  C N R 255 
NAP O4B  O N N 256 
NAP C3B  C N R 257 
NAP O3B  O N N 258 
NAP C2B  C N R 259 
NAP O2B  O N N 260 
NAP C1B  C N R 261 
NAP N9A  N Y N 262 
NAP C8A  C Y N 263 
NAP N7A  N Y N 264 
NAP C5A  C Y N 265 
NAP C6A  C Y N 266 
NAP N6A  N N N 267 
NAP N1A  N Y N 268 
NAP C2A  C Y N 269 
NAP N3A  N Y N 270 
NAP C4A  C Y N 271 
NAP O3   O N N 272 
NAP PN   P N N 273 
NAP O1N  O N N 274 
NAP O2N  O N N 275 
NAP O5D  O N N 276 
NAP C5D  C N N 277 
NAP C4D  C N R 278 
NAP O4D  O N N 279 
NAP C3D  C N S 280 
NAP O3D  O N N 281 
NAP C2D  C N R 282 
NAP O2D  O N N 283 
NAP C1D  C N R 284 
NAP N1N  N Y N 285 
NAP C2N  C Y N 286 
NAP C3N  C Y N 287 
NAP C7N  C N N 288 
NAP O7N  O N N 289 
NAP N7N  N N N 290 
NAP C4N  C Y N 291 
NAP C5N  C Y N 292 
NAP C6N  C Y N 293 
NAP P2B  P N N 294 
NAP O1X  O N N 295 
NAP O2X  O N N 296 
NAP O3X  O N N 297 
NAP HOA2 H N N 298 
NAP H51A H N N 299 
NAP H52A H N N 300 
NAP H4B  H N N 301 
NAP H3B  H N N 302 
NAP HO3A H N N 303 
NAP H2B  H N N 304 
NAP H1B  H N N 305 
NAP H8A  H N N 306 
NAP H61A H N N 307 
NAP H62A H N N 308 
NAP H2A  H N N 309 
NAP H51N H N N 310 
NAP H52N H N N 311 
NAP H4D  H N N 312 
NAP H3D  H N N 313 
NAP HO3N H N N 314 
NAP H2D  H N N 315 
NAP HO2N H N N 316 
NAP H1D  H N N 317 
NAP H2N  H N N 318 
NAP H71N H N N 319 
NAP H72N H N N 320 
NAP H4N  H N N 321 
NAP H5N  H N N 322 
NAP H6N  H N N 323 
NAP HOP2 H N N 324 
NAP HOP3 H N N 325 
PEG C1   C N N 326 
PEG O1   O N N 327 
PEG C2   C N N 328 
PEG O2   O N N 329 
PEG C3   C N N 330 
PEG C4   C N N 331 
PEG O4   O N N 332 
PEG H11  H N N 333 
PEG H12  H N N 334 
PEG HO1  H N N 335 
PEG H21  H N N 336 
PEG H22  H N N 337 
PEG H31  H N N 338 
PEG H32  H N N 339 
PEG H41  H N N 340 
PEG H42  H N N 341 
PEG HO4  H N N 342 
PHE N    N N N 343 
PHE CA   C N S 344 
PHE C    C N N 345 
PHE O    O N N 346 
PHE CB   C N N 347 
PHE CG   C Y N 348 
PHE CD1  C Y N 349 
PHE CD2  C Y N 350 
PHE CE1  C Y N 351 
PHE CE2  C Y N 352 
PHE CZ   C Y N 353 
PHE OXT  O N N 354 
PHE H    H N N 355 
PHE H2   H N N 356 
PHE HA   H N N 357 
PHE HB2  H N N 358 
PHE HB3  H N N 359 
PHE HD1  H N N 360 
PHE HD2  H N N 361 
PHE HE1  H N N 362 
PHE HE2  H N N 363 
PHE HZ   H N N 364 
PHE HXT  H N N 365 
PRO N    N N N 366 
PRO CA   C N S 367 
PRO C    C N N 368 
PRO O    O N N 369 
PRO CB   C N N 370 
PRO CG   C N N 371 
PRO CD   C N N 372 
PRO OXT  O N N 373 
PRO H    H N N 374 
PRO HA   H N N 375 
PRO HB2  H N N 376 
PRO HB3  H N N 377 
PRO HG2  H N N 378 
PRO HG3  H N N 379 
PRO HD2  H N N 380 
PRO HD3  H N N 381 
PRO HXT  H N N 382 
SER N    N N N 383 
SER CA   C N S 384 
SER C    C N N 385 
SER O    O N N 386 
SER CB   C N N 387 
SER OG   O N N 388 
SER OXT  O N N 389 
SER H    H N N 390 
SER H2   H N N 391 
SER HA   H N N 392 
SER HB2  H N N 393 
SER HB3  H N N 394 
SER HG   H N N 395 
SER HXT  H N N 396 
THR N    N N N 397 
THR CA   C N S 398 
THR C    C N N 399 
THR O    O N N 400 
THR CB   C N R 401 
THR OG1  O N N 402 
THR CG2  C N N 403 
THR OXT  O N N 404 
THR H    H N N 405 
THR H2   H N N 406 
THR HA   H N N 407 
THR HB   H N N 408 
THR HG1  H N N 409 
THR HG21 H N N 410 
THR HG22 H N N 411 
THR HG23 H N N 412 
THR HXT  H N N 413 
TRP N    N N N 414 
TRP CA   C N S 415 
TRP C    C N N 416 
TRP O    O N N 417 
TRP CB   C N N 418 
TRP CG   C Y N 419 
TRP CD1  C Y N 420 
TRP CD2  C Y N 421 
TRP NE1  N Y N 422 
TRP CE2  C Y N 423 
TRP CE3  C Y N 424 
TRP CZ2  C Y N 425 
TRP CZ3  C Y N 426 
TRP CH2  C Y N 427 
TRP OXT  O N N 428 
TRP H    H N N 429 
TRP H2   H N N 430 
TRP HA   H N N 431 
TRP HB2  H N N 432 
TRP HB3  H N N 433 
TRP HD1  H N N 434 
TRP HE1  H N N 435 
TRP HE3  H N N 436 
TRP HZ2  H N N 437 
TRP HZ3  H N N 438 
TRP HH2  H N N 439 
TRP HXT  H N N 440 
TYR N    N N N 441 
TYR CA   C N S 442 
TYR C    C N N 443 
TYR O    O N N 444 
TYR CB   C N N 445 
TYR CG   C Y N 446 
TYR CD1  C Y N 447 
TYR CD2  C Y N 448 
TYR CE1  C Y N 449 
TYR CE2  C Y N 450 
TYR CZ   C Y N 451 
TYR OH   O N N 452 
TYR OXT  O N N 453 
TYR H    H N N 454 
TYR H2   H N N 455 
TYR HA   H N N 456 
TYR HB2  H N N 457 
TYR HB3  H N N 458 
TYR HD1  H N N 459 
TYR HD2  H N N 460 
TYR HE1  H N N 461 
TYR HE2  H N N 462 
TYR HH   H N N 463 
TYR HXT  H N N 464 
VAL N    N N N 465 
VAL CA   C N S 466 
VAL C    C N N 467 
VAL O    O N N 468 
VAL CB   C N N 469 
VAL CG1  C N N 470 
VAL CG2  C N N 471 
VAL OXT  O N N 472 
VAL H    H N N 473 
VAL H2   H N N 474 
VAL HA   H N N 475 
VAL HB   H N N 476 
VAL HG11 H N N 477 
VAL HG12 H N N 478 
VAL HG13 H N N 479 
VAL HG21 H N N 480 
VAL HG22 H N N 481 
VAL HG23 H N N 482 
VAL HXT  H N N 483 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAP PA  O1A  doub N N 237 
NAP PA  O2A  sing N N 238 
NAP PA  O5B  sing N N 239 
NAP PA  O3   sing N N 240 
NAP O2A HOA2 sing N N 241 
NAP O5B C5B  sing N N 242 
NAP C5B C4B  sing N N 243 
NAP C5B H51A sing N N 244 
NAP C5B H52A sing N N 245 
NAP C4B O4B  sing N N 246 
NAP C4B C3B  sing N N 247 
NAP C4B H4B  sing N N 248 
NAP O4B C1B  sing N N 249 
NAP C3B O3B  sing N N 250 
NAP C3B C2B  sing N N 251 
NAP C3B H3B  sing N N 252 
NAP O3B HO3A sing N N 253 
NAP C2B O2B  sing N N 254 
NAP C2B C1B  sing N N 255 
NAP C2B H2B  sing N N 256 
NAP O2B P2B  sing N N 257 
NAP C1B N9A  sing N N 258 
NAP C1B H1B  sing N N 259 
NAP N9A C8A  sing Y N 260 
NAP N9A C4A  sing Y N 261 
NAP C8A N7A  doub Y N 262 
NAP C8A H8A  sing N N 263 
NAP N7A C5A  sing Y N 264 
NAP C5A C6A  sing Y N 265 
NAP C5A C4A  doub Y N 266 
NAP C6A N6A  sing N N 267 
NAP C6A N1A  doub Y N 268 
NAP N6A H61A sing N N 269 
NAP N6A H62A sing N N 270 
NAP N1A C2A  sing Y N 271 
NAP C2A N3A  doub Y N 272 
NAP C2A H2A  sing N N 273 
NAP N3A C4A  sing Y N 274 
NAP O3  PN   sing N N 275 
NAP PN  O1N  doub N N 276 
NAP PN  O2N  sing N N 277 
NAP PN  O5D  sing N N 278 
NAP O5D C5D  sing N N 279 
NAP C5D C4D  sing N N 280 
NAP C5D H51N sing N N 281 
NAP C5D H52N sing N N 282 
NAP C4D O4D  sing N N 283 
NAP C4D C3D  sing N N 284 
NAP C4D H4D  sing N N 285 
NAP O4D C1D  sing N N 286 
NAP C3D O3D  sing N N 287 
NAP C3D C2D  sing N N 288 
NAP C3D H3D  sing N N 289 
NAP O3D HO3N sing N N 290 
NAP C2D O2D  sing N N 291 
NAP C2D C1D  sing N N 292 
NAP C2D H2D  sing N N 293 
NAP O2D HO2N sing N N 294 
NAP C1D N1N  sing N N 295 
NAP C1D H1D  sing N N 296 
NAP N1N C2N  sing Y N 297 
NAP N1N C6N  doub Y N 298 
NAP C2N C3N  doub Y N 299 
NAP C2N H2N  sing N N 300 
NAP C3N C7N  sing N N 301 
NAP C3N C4N  sing Y N 302 
NAP C7N O7N  doub N N 303 
NAP C7N N7N  sing N N 304 
NAP N7N H71N sing N N 305 
NAP N7N H72N sing N N 306 
NAP C4N C5N  doub Y N 307 
NAP C4N H4N  sing N N 308 
NAP C5N C6N  sing Y N 309 
NAP C5N H5N  sing N N 310 
NAP C6N H6N  sing N N 311 
NAP P2B O1X  doub N N 312 
NAP P2B O2X  sing N N 313 
NAP P2B O3X  sing N N 314 
NAP O2X HOP2 sing N N 315 
NAP O3X HOP3 sing N N 316 
PEG C1  O1   sing N N 317 
PEG C1  C2   sing N N 318 
PEG C1  H11  sing N N 319 
PEG C1  H12  sing N N 320 
PEG O1  HO1  sing N N 321 
PEG C2  O2   sing N N 322 
PEG C2  H21  sing N N 323 
PEG C2  H22  sing N N 324 
PEG O2  C3   sing N N 325 
PEG C3  C4   sing N N 326 
PEG C3  H31  sing N N 327 
PEG C3  H32  sing N N 328 
PEG C4  O4   sing N N 329 
PEG C4  H41  sing N N 330 
PEG C4  H42  sing N N 331 
PEG O4  HO4  sing N N 332 
PHE N   CA   sing N N 333 
PHE N   H    sing N N 334 
PHE N   H2   sing N N 335 
PHE CA  C    sing N N 336 
PHE CA  CB   sing N N 337 
PHE CA  HA   sing N N 338 
PHE C   O    doub N N 339 
PHE C   OXT  sing N N 340 
PHE CB  CG   sing N N 341 
PHE CB  HB2  sing N N 342 
PHE CB  HB3  sing N N 343 
PHE CG  CD1  doub Y N 344 
PHE CG  CD2  sing Y N 345 
PHE CD1 CE1  sing Y N 346 
PHE CD1 HD1  sing N N 347 
PHE CD2 CE2  doub Y N 348 
PHE CD2 HD2  sing N N 349 
PHE CE1 CZ   doub Y N 350 
PHE CE1 HE1  sing N N 351 
PHE CE2 CZ   sing Y N 352 
PHE CE2 HE2  sing N N 353 
PHE CZ  HZ   sing N N 354 
PHE OXT HXT  sing N N 355 
PRO N   CA   sing N N 356 
PRO N   CD   sing N N 357 
PRO N   H    sing N N 358 
PRO CA  C    sing N N 359 
PRO CA  CB   sing N N 360 
PRO CA  HA   sing N N 361 
PRO C   O    doub N N 362 
PRO C   OXT  sing N N 363 
PRO CB  CG   sing N N 364 
PRO CB  HB2  sing N N 365 
PRO CB  HB3  sing N N 366 
PRO CG  CD   sing N N 367 
PRO CG  HG2  sing N N 368 
PRO CG  HG3  sing N N 369 
PRO CD  HD2  sing N N 370 
PRO CD  HD3  sing N N 371 
PRO OXT HXT  sing N N 372 
SER N   CA   sing N N 373 
SER N   H    sing N N 374 
SER N   H2   sing N N 375 
SER CA  C    sing N N 376 
SER CA  CB   sing N N 377 
SER CA  HA   sing N N 378 
SER C   O    doub N N 379 
SER C   OXT  sing N N 380 
SER CB  OG   sing N N 381 
SER CB  HB2  sing N N 382 
SER CB  HB3  sing N N 383 
SER OG  HG   sing N N 384 
SER OXT HXT  sing N N 385 
THR N   CA   sing N N 386 
THR N   H    sing N N 387 
THR N   H2   sing N N 388 
THR CA  C    sing N N 389 
THR CA  CB   sing N N 390 
THR CA  HA   sing N N 391 
THR C   O    doub N N 392 
THR C   OXT  sing N N 393 
THR CB  OG1  sing N N 394 
THR CB  CG2  sing N N 395 
THR CB  HB   sing N N 396 
THR OG1 HG1  sing N N 397 
THR CG2 HG21 sing N N 398 
THR CG2 HG22 sing N N 399 
THR CG2 HG23 sing N N 400 
THR OXT HXT  sing N N 401 
TRP N   CA   sing N N 402 
TRP N   H    sing N N 403 
TRP N   H2   sing N N 404 
TRP CA  C    sing N N 405 
TRP CA  CB   sing N N 406 
TRP CA  HA   sing N N 407 
TRP C   O    doub N N 408 
TRP C   OXT  sing N N 409 
TRP CB  CG   sing N N 410 
TRP CB  HB2  sing N N 411 
TRP CB  HB3  sing N N 412 
TRP CG  CD1  doub Y N 413 
TRP CG  CD2  sing Y N 414 
TRP CD1 NE1  sing Y N 415 
TRP CD1 HD1  sing N N 416 
TRP CD2 CE2  doub Y N 417 
TRP CD2 CE3  sing Y N 418 
TRP NE1 CE2  sing Y N 419 
TRP NE1 HE1  sing N N 420 
TRP CE2 CZ2  sing Y N 421 
TRP CE3 CZ3  doub Y N 422 
TRP CE3 HE3  sing N N 423 
TRP CZ2 CH2  doub Y N 424 
TRP CZ2 HZ2  sing N N 425 
TRP CZ3 CH2  sing Y N 426 
TRP CZ3 HZ3  sing N N 427 
TRP CH2 HH2  sing N N 428 
TRP OXT HXT  sing N N 429 
TYR N   CA   sing N N 430 
TYR N   H    sing N N 431 
TYR N   H2   sing N N 432 
TYR CA  C    sing N N 433 
TYR CA  CB   sing N N 434 
TYR CA  HA   sing N N 435 
TYR C   O    doub N N 436 
TYR C   OXT  sing N N 437 
TYR CB  CG   sing N N 438 
TYR CB  HB2  sing N N 439 
TYR CB  HB3  sing N N 440 
TYR CG  CD1  doub Y N 441 
TYR CG  CD2  sing Y N 442 
TYR CD1 CE1  sing Y N 443 
TYR CD1 HD1  sing N N 444 
TYR CD2 CE2  doub Y N 445 
TYR CD2 HD2  sing N N 446 
TYR CE1 CZ   doub Y N 447 
TYR CE1 HE1  sing N N 448 
TYR CE2 CZ   sing Y N 449 
TYR CE2 HE2  sing N N 450 
TYR CZ  OH   sing N N 451 
TYR OH  HH   sing N N 452 
TYR OXT HXT  sing N N 453 
VAL N   CA   sing N N 454 
VAL N   H    sing N N 455 
VAL N   H2   sing N N 456 
VAL CA  C    sing N N 457 
VAL CA  CB   sing N N 458 
VAL CA  HA   sing N N 459 
VAL C   O    doub N N 460 
VAL C   OXT  sing N N 461 
VAL CB  CG1  sing N N 462 
VAL CB  CG2  sing N N 463 
VAL CB  HB   sing N N 464 
VAL CG1 HG11 sing N N 465 
VAL CG1 HG12 sing N N 466 
VAL CG1 HG13 sing N N 467 
VAL CG2 HG21 sing N N 468 
VAL CG2 HG22 sing N N 469 
VAL CG2 HG23 sing N N 470 
VAL OXT HXT  sing N N 471 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8Y12 
_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]   0.026454 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004350 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008765 
_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]   0.016119 
_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 
P 
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 6   ? 24.324  21.306  47.233  1.00 69.93 ? 6    LYS A N   1 
ATOM   2    C CA  . LYS A 1 6   ? 22.879  21.076  47.577  1.00 67.23 ? 6    LYS A CA  1 
ATOM   3    C C   . LYS A 1 6   ? 22.055  22.321  47.215  1.00 64.82 ? 6    LYS A C   1 
ATOM   4    O O   . LYS A 1 6   ? 21.408  22.935  48.072  1.00 58.59 ? 6    LYS A O   1 
ATOM   5    C CB  . LYS A 1 6   ? 22.758  20.638  49.045  1.00 68.12 ? 6    LYS A CB  1 
ATOM   6    C CG  . LYS A 1 6   ? 22.870  21.729  50.109  1.00 69.65 ? 6    LYS A CG  1 
ATOM   7    C CD  . LYS A 1 6   ? 23.895  22.827  49.831  1.00 73.02 ? 6    LYS A CD  1 
ATOM   8    C CE  . LYS A 1 6   ? 23.755  24.012  50.760  1.00 73.97 ? 6    LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 6   ? 24.088  23.640  52.154  1.00 76.38 ? 6    LYS A NZ  1 
ATOM   10   N N   . PRO A 1 7   ? 22.019  22.728  45.921  1.00 60.69 ? 7    PRO A N   1 
ATOM   11   C CA  . PRO A 1 7   ? 21.145  23.824  45.499  1.00 55.89 ? 7    PRO A CA  1 
ATOM   12   C C   . PRO A 1 7   ? 19.680  23.354  45.580  1.00 48.99 ? 7    PRO A C   1 
ATOM   13   O O   . PRO A 1 7   ? 19.443  22.161  45.441  1.00 45.05 ? 7    PRO A O   1 
ATOM   14   C CB  . PRO A 1 7   ? 21.624  24.134  44.072  1.00 58.67 ? 7    PRO A CB  1 
ATOM   15   C CG  . PRO A 1 7   ? 22.170  22.805  43.567  1.00 61.78 ? 7    PRO A CG  1 
ATOM   16   C CD  . PRO A 1 7   ? 22.755  22.129  44.792  1.00 61.91 ? 7    PRO A CD  1 
ATOM   17   N N   . HIS A 1 8   ? 18.761  24.282  45.864  1.00 45.44 ? 8    HIS A N   1 
ATOM   18   C CA  . HIS A 1 8   ? 17.293  24.052  45.951  1.00 43.02 ? 8    HIS A CA  1 
ATOM   19   C C   . HIS A 1 8   ? 16.706  23.950  44.536  1.00 40.64 ? 8    HIS A C   1 
ATOM   20   O O   . HIS A 1 8   ? 16.876  24.907  43.737  1.00 38.79 ? 8    HIS A O   1 
ATOM   21   C CB  . HIS A 1 8   ? 16.603  25.164  46.747  1.00 45.21 ? 8    HIS A CB  1 
ATOM   22   C CG  . HIS A 1 8   ? 16.944  25.187  48.199  1.00 51.95 ? 8    HIS A CG  1 
ATOM   23   N ND1 . HIS A 1 8   ? 15.975  25.283  49.181  1.00 58.18 ? 8    HIS A ND1 1 
ATOM   24   C CD2 . HIS A 1 8   ? 18.131  25.141  48.842  1.00 54.89 ? 8    HIS A CD2 1 
ATOM   25   C CE1 . HIS A 1 8   ? 16.550  25.292  50.367  1.00 57.37 ? 8    HIS A CE1 1 
ATOM   26   N NE2 . HIS A 1 8   ? 17.871  25.208  50.184  1.00 58.45 ? 8    HIS A NE2 1 
ATOM   27   N N   . VAL A 1 9   ? 16.041  22.834  44.235  1.00 36.61 ? 9    VAL A N   1 
ATOM   28   C CA  . VAL A 1 9   ? 15.310  22.631  42.955  1.00 32.46 ? 9    VAL A CA  1 
ATOM   29   C C   . VAL A 1 9   ? 13.870  22.238  43.276  1.00 32.42 ? 9    VAL A C   1 
ATOM   30   O O   . VAL A 1 9   ? 13.649  21.441  44.213  1.00 33.27 ? 9    VAL A O   1 
ATOM   31   C CB  . VAL A 1 9   ? 16.009  21.602  42.050  1.00 30.44 ? 9    VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 9   ? 15.227  21.358  40.770  1.00 29.42 ? 9    VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 9   ? 17.417  22.045  41.713  1.00 31.16 ? 9    VAL A CG2 1 
ATOM   34   N N   . SER A 1 10  ? 12.916  22.800  42.535  1.00 29.39 ? 10   SER A N   1 
ATOM   35   C CA  . SER A 1 10  ? 11.493  22.395  42.606  1.00 29.55 ? 10   SER A CA  1 
ATOM   36   C C   . SER A 1 10  ? 11.162  21.598  41.342  1.00 29.74 ? 10   SER A C   1 
ATOM   37   O O   . SER A 1 10  ? 11.729  21.933  40.278  1.00 28.69 ? 10   SER A O   1 
ATOM   38   C CB  . SER A 1 10  ? 10.604  23.583  42.782  1.00 30.88 ? 10   SER A CB  1 
ATOM   39   O OG  . SER A 1 10  ? 10.621  24.004  44.132  1.00 30.66 ? 10   SER A OG  1 
ATOM   40   N N   . LEU A 1 11  ? 10.326  20.561  41.462  1.00 28.58 ? 11   LEU A N   1 
ATOM   41   C CA  . LEU A 1 11  ? 9.871   19.721  40.321  1.00 26.90 ? 11   LEU A CA  1 
ATOM   42   C C   . LEU A 1 11  ? 8.347   19.628  40.361  1.00 27.18 ? 11   LEU A C   1 
ATOM   43   O O   . LEU A 1 11  ? 7.820   19.168  41.380  1.00 28.86 ? 11   LEU A O   1 
ATOM   44   C CB  . LEU A 1 11  ? 10.523  18.344  40.406  1.00 27.99 ? 11   LEU A CB  1 
ATOM   45   C CG  . LEU A 1 11  ? 9.918   17.253  39.522  1.00 26.97 ? 11   LEU A CG  1 
ATOM   46   C CD1 . LEU A 1 11  ? 9.960   17.646  38.053  1.00 28.92 ? 11   LEU A CD1 1 
ATOM   47   C CD2 . LEU A 1 11  ? 10.648  15.934  39.731  1.00 25.33 ? 11   LEU A CD2 1 
ATOM   48   N N   . ILE A 1 12  ? 7.680   20.069  39.290  1.00 25.75 ? 12   ILE A N   1 
ATOM   49   C CA  . ILE A 1 12  ? 6.204   19.975  39.113  1.00 25.16 ? 12   ILE A CA  1 
ATOM   50   C C   . ILE A 1 12  ? 5.927   18.840  38.130  1.00 22.80 ? 12   ILE A C   1 
ATOM   51   O O   . ILE A 1 12  ? 6.358   18.943  36.983  1.00 23.27 ? 12   ILE A O   1 
ATOM   52   C CB  . ILE A 1 12  ? 5.601   21.324  38.663  1.00 25.45 ? 12   ILE A CB  1 
ATOM   53   C CG1 . ILE A 1 12  ? 5.748   22.380  39.761  1.00 28.07 ? 12   ILE A CG1 1 
ATOM   54   C CG2 . ILE A 1 12  ? 4.156   21.143  38.228  1.00 25.77 ? 12   ILE A CG2 1 
ATOM   55   C CD1 . ILE A 1 12  ? 5.113   23.713  39.452  1.00 30.98 ? 12   ILE A CD1 1 
ATOM   56   N N   . GLY A 1 13  ? 5.227   17.802  38.584  1.00 22.62 ? 13   GLY A N   1 
ATOM   57   C CA  . GLY A 1 13  ? 4.918   16.601  37.793  1.00 21.71 ? 13   GLY A CA  1 
ATOM   58   C C   . GLY A 1 13  ? 5.734   15.404  38.237  1.00 21.72 ? 13   GLY A C   1 
ATOM   59   O O   . GLY A 1 13  ? 6.984   15.426  38.137  1.00 23.16 ? 13   GLY A O   1 
ATOM   60   N N   . LEU A 1 14  ? 5.047   14.370  38.693  1.00 22.04 ? 14   LEU A N   1 
ATOM   61   C CA  . LEU A 1 14  ? 5.650   13.109  39.175  1.00 21.22 ? 14   LEU A CA  1 
ATOM   62   C C   . LEU A 1 14  ? 4.984   11.938  38.464  1.00 21.51 ? 14   LEU A C   1 
ATOM   63   O O   . LEU A 1 14  ? 4.760   10.933  39.110  1.00 21.88 ? 14   LEU A O   1 
ATOM   64   C CB  . LEU A 1 14  ? 5.482   13.021  40.693  1.00 21.35 ? 14   LEU A CB  1 
ATOM   65   C CG  . LEU A 1 14  ? 6.232   14.076  41.500  1.00 21.39 ? 14   LEU A CG  1 
ATOM   66   C CD1 . LEU A 1 14  ? 5.847   13.977  42.968  1.00 22.01 ? 14   LEU A CD1 1 
ATOM   67   C CD2 . LEU A 1 14  ? 7.750   13.947  41.311  1.00 22.51 ? 14   LEU A CD2 1 
ATOM   68   N N   . GLY A 1 15  ? 4.748   12.065  37.152  1.00 23.80 ? 15   GLY A N   1 
ATOM   69   C CA  . GLY A 1 15  ? 4.257   10.983  36.282  1.00 22.99 ? 15   GLY A CA  1 
ATOM   70   C C   . GLY A 1 15  ? 5.364   9.981   36.000  1.00 24.11 ? 15   GLY A C   1 
ATOM   71   O O   . GLY A 1 15  ? 6.341   9.932   36.769  1.00 26.48 ? 15   GLY A O   1 
ATOM   72   N N   . ASN A 1 16  ? 5.236   9.190   34.946  1.00 22.54 ? 16   ASN A N   1 
ATOM   73   C CA  . ASN A 1 16  ? 6.323   8.272   34.523  1.00 24.49 ? 16   ASN A CA  1 
ATOM   74   C C   . ASN A 1 16  ? 7.629   9.074   34.395  1.00 24.70 ? 16   ASN A C   1 
ATOM   75   O O   . ASN A 1 16  ? 8.634   8.677   35.038  1.00 24.88 ? 16   ASN A O   1 
ATOM   76   C CB  . ASN A 1 16  ? 5.952   7.516   33.253  1.00 24.05 ? 16   ASN A CB  1 
ATOM   77   C CG  . ASN A 1 16  ? 4.939   6.430   33.542  1.00 25.75 ? 16   ASN A CG  1 
ATOM   78   O OD1 . ASN A 1 16  ? 3.761   6.555   33.197  1.00 27.41 ? 16   ASN A OD1 1 
ATOM   79   N ND2 . ASN A 1 16  ? 5.391   5.392   34.208  1.00 25.29 ? 16   ASN A ND2 1 
ATOM   80   N N   . MET A 1 17  ? 7.624   10.192  33.656  1.00 23.29 ? 17   MET A N   1 
ATOM   81   C CA  . MET A 1 17  ? 8.900   10.922  33.391  1.00 23.64 ? 17   MET A CA  1 
ATOM   82   C C   . MET A 1 17  ? 9.271   11.829  34.586  1.00 23.62 ? 17   MET A C   1 
ATOM   83   O O   . MET A 1 17  ? 10.500  11.867  34.975  1.00 23.93 ? 17   MET A O   1 
ATOM   84   C CB  . MET A 1 17  ? 8.840   11.718  32.082  1.00 22.91 ? 17   MET A CB  1 
ATOM   85   C CG  . MET A 1 17  ? 10.179  12.361  31.735  1.00 21.68 ? 17   MET A CG  1 
ATOM   86   S SD  . MET A 1 17  ? 11.485  11.121  31.588  1.00 21.75 ? 17   MET A SD  1 
ATOM   87   C CE  . MET A 1 17  ? 10.958  10.311  30.079  1.00 20.19 ? 17   MET A CE  1 
ATOM   88   N N   . GLY A 1 18  ? 8.287   12.508  35.176  1.00 20.42 ? 18   GLY A N   1 
ATOM   89   C CA  . GLY A 1 18  ? 8.484   13.336  36.378  1.00 22.19 ? 18   GLY A CA  1 
ATOM   90   C C   . GLY A 1 18  ? 9.223   12.595  37.483  1.00 23.42 ? 18   GLY A C   1 
ATOM   91   O O   . GLY A 1 18  ? 10.091  13.186  38.119  1.00 22.29 ? 18   GLY A O   1 
ATOM   92   N N   . LEU A 1 19  ? 8.868   11.339  37.741  1.00 25.20 ? 19   LEU A N   1 
ATOM   93   C CA  . LEU A 1 19  ? 9.467   10.556  38.853  1.00 27.62 ? 19   LEU A CA  1 
ATOM   94   C C   . LEU A 1 19  ? 10.917  10.172  38.481  1.00 26.24 ? 19   LEU A C   1 
ATOM   95   O O   . LEU A 1 19  ? 11.810  10.270  39.343  1.00 24.78 ? 19   LEU A O   1 
ATOM   96   C CB  . LEU A 1 19  ? 8.563   9.350   39.151  1.00 29.78 ? 19   LEU A CB  1 
ATOM   97   C CG  . LEU A 1 19  ? 8.987   8.521   40.357  1.00 35.21 ? 19   LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 19  ? 9.104   9.396   41.599  1.00 38.45 ? 19   LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 19  ? 8.018   7.369   40.597  1.00 37.53 ? 19   LEU A CD2 1 
ATOM   100  N N   . ALA A 1 20  ? 11.168  9.805   37.225  1.00 24.34 ? 20   ALA A N   1 
ATOM   101  C CA  . ALA A 1 20  ? 12.532  9.553   36.726  1.00 22.65 ? 20   ALA A CA  1 
ATOM   102  C C   . ALA A 1 20  ? 13.341  10.837  36.879  1.00 23.65 ? 20   ALA A C   1 
ATOM   103  O O   . ALA A 1 20  ? 14.518  10.760  37.345  1.00 25.34 ? 20   ALA A O   1 
ATOM   104  C CB  . ALA A 1 20  ? 12.483  9.056   35.310  1.00 23.44 ? 20   ALA A CB  1 
ATOM   105  N N   . ILE A 1 21  ? 12.760  11.992  36.538  1.00 22.90 ? 21   ILE A N   1 
ATOM   106  C CA  . ILE A 1 21  ? 13.478  13.288  36.728  1.00 24.01 ? 21   ILE A CA  1 
ATOM   107  C C   . ILE A 1 21  ? 13.809  13.449  38.218  1.00 25.62 ? 21   ILE A C   1 
ATOM   108  O O   . ILE A 1 21  ? 14.941  13.874  38.535  1.00 24.96 ? 21   ILE A O   1 
ATOM   109  C CB  . ILE A 1 21  ? 12.694  14.504  36.213  1.00 24.24 ? 21   ILE A CB  1 
ATOM   110  C CG1 . ILE A 1 21  ? 12.492  14.461  34.696  1.00 24.67 ? 21   ILE A CG1 1 
ATOM   111  C CG2 . ILE A 1 21  ? 13.375  15.794  36.658  1.00 23.99 ? 21   ILE A CG2 1 
ATOM   112  C CD1 . ILE A 1 21  ? 11.401  15.410  34.204  1.00 25.90 ? 21   ILE A CD1 1 
ATOM   113  N N   . ALA A 1 22  ? 12.833  13.227  39.099  1.00 26.41 ? 22   ALA A N   1 
ATOM   114  C CA  . ALA A 1 22  ? 13.009  13.417  40.558  1.00 29.45 ? 22   ALA A CA  1 
ATOM   115  C C   . ALA A 1 22  ? 14.241  12.610  41.011  1.00 29.88 ? 22   ALA A C   1 
ATOM   116  O O   . ALA A 1 22  ? 15.162  13.184  41.632  1.00 28.83 ? 22   ALA A O   1 
ATOM   117  C CB  . ALA A 1 22  ? 11.734  13.027  41.283  1.00 29.98 ? 22   ALA A CB  1 
ATOM   118  N N   . ASN A 1 23  ? 14.296  11.329  40.644  1.00 30.55 ? 23   ASN A N   1 
ATOM   119  C CA  . ASN A 1 23  ? 15.385  10.406  41.064  1.00 31.00 ? 23   ASN A CA  1 
ATOM   120  C C   . ASN A 1 23  ? 16.739  10.926  40.556  1.00 30.32 ? 23   ASN A C   1 
ATOM   121  O O   . ASN A 1 23  ? 17.678  10.943  41.345  1.00 29.18 ? 23   ASN A O   1 
ATOM   122  C CB  . ASN A 1 23  ? 15.094  8.971   40.641  1.00 29.02 ? 23   ASN A CB  1 
ATOM   123  C CG  . ASN A 1 23  ? 14.106  8.311   41.576  1.00 31.61 ? 23   ASN A CG  1 
ATOM   124  O OD1 . ASN A 1 23  ? 14.307  8.332   42.786  1.00 33.35 ? 23   ASN A OD1 1 
ATOM   125  N ND2 . ASN A 1 23  ? 13.063  7.712   41.027  1.00 27.89 ? 23   ASN A ND2 1 
ATOM   126  N N   . CYS A 1 24  ? 16.824  11.367  39.307  1.00 29.36 ? 24   CYS A N   1 
ATOM   127  C CA  . CYS A 1 24  ? 18.057  11.960  38.735  1.00 32.06 ? 24   CYS A CA  1 
ATOM   128  C C   . CYS A 1 24  ? 18.481  13.165  39.594  1.00 33.08 ? 24   CYS A C   1 
ATOM   129  O O   . CYS A 1 24  ? 19.656  13.221  39.994  1.00 35.03 ? 24   CYS A O   1 
ATOM   130  C CB  . CYS A 1 24  ? 17.867  12.328  37.269  1.00 30.84 ? 24   CYS A CB  1 
ATOM   131  S SG  . CYS A 1 24  ? 17.783  10.893  36.166  1.00 31.51 ? 24   CYS A SG  1 
ATOM   132  N N   . LEU A 1 25  ? 17.565  14.087  39.883  1.00 33.87 ? 25   LEU A N   1 
ATOM   133  C CA  . LEU A 1 25  ? 17.876  15.341  40.610  1.00 34.61 ? 25   LEU A CA  1 
ATOM   134  C C   . LEU A 1 25  ? 18.350  14.977  42.028  1.00 38.69 ? 25   LEU A C   1 
ATOM   135  O O   . LEU A 1 25  ? 19.343  15.581  42.499  1.00 33.85 ? 25   LEU A O   1 
ATOM   136  C CB  . LEU A 1 25  ? 16.643  16.251  40.626  1.00 35.82 ? 25   LEU A CB  1 
ATOM   137  C CG  . LEU A 1 25  ? 16.173  16.793  39.271  1.00 36.51 ? 25   LEU A CG  1 
ATOM   138  C CD1 . LEU A 1 25  ? 14.833  17.502  39.399  1.00 34.28 ? 25   LEU A CD1 1 
ATOM   139  C CD2 . LEU A 1 25  ? 17.204  17.732  38.665  1.00 36.50 ? 25   LEU A CD2 1 
ATOM   140  N N   . ILE A 1 26  ? 17.706  13.994  42.663  1.00 39.88 ? 26   ILE A N   1 
ATOM   141  C CA  . ILE A 1 26  ? 18.069  13.523  44.036  1.00 41.38 ? 26   ILE A CA  1 
ATOM   142  C C   . ILE A 1 26  ? 19.512  13.016  44.029  1.00 45.77 ? 26   ILE A C   1 
ATOM   143  O O   . ILE A 1 26  ? 20.270  13.433  44.926  1.00 45.29 ? 26   ILE A O   1 
ATOM   144  C CB  . ILE A 1 26  ? 17.126  12.427  44.567  1.00 38.35 ? 26   ILE A CB  1 
ATOM   145  C CG1 . ILE A 1 26  ? 15.759  12.995  44.959  1.00 37.15 ? 26   ILE A CG1 1 
ATOM   146  C CG2 . ILE A 1 26  ? 17.787  11.691  45.737  1.00 38.86 ? 26   ILE A CG2 1 
ATOM   147  C CD1 . ILE A 1 26  ? 14.667  11.945  45.057  1.00 36.47 ? 26   ILE A CD1 1 
ATOM   148  N N   . LYS A 1 27  ? 19.845  12.127  43.084  1.00 47.77 ? 27   LYS A N   1 
ATOM   149  C CA  . LYS A 1 27  ? 21.188  11.501  42.958  1.00 52.98 ? 27   LYS A CA  1 
ATOM   150  C C   . LYS A 1 27  ? 22.247  12.586  42.749  1.00 51.80 ? 27   LYS A C   1 
ATOM   151  O O   . LYS A 1 27  ? 23.351  12.420  43.279  1.00 57.67 ? 27   LYS A O   1 
ATOM   152  C CB  . LYS A 1 27  ? 21.219  10.490  41.811  1.00 55.37 ? 27   LYS A CB  1 
ATOM   153  C CG  . LYS A 1 27  ? 20.786  9.082   42.194  1.00 61.93 ? 27   LYS A CG  1 
ATOM   154  C CD  . LYS A 1 27  ? 20.710  8.128   41.016  1.00 66.00 ? 27   LYS A CD  1 
ATOM   155  C CE  . LYS A 1 27  ? 21.963  8.149   40.164  1.00 67.61 ? 27   LYS A CE  1 
ATOM   156  N NZ  . LYS A 1 27  ? 22.019  6.981   39.257  1.00 71.98 ? 27   LYS A NZ  1 
ATOM   157  N N   . SER A 1 28  ? 21.909  13.650  42.011  1.00 54.21 ? 28   SER A N   1 
ATOM   158  C CA  . SER A 1 28  ? 22.804  14.793  41.686  1.00 54.92 ? 28   SER A CA  1 
ATOM   159  C C   . SER A 1 28  ? 23.239  15.498  42.970  1.00 52.54 ? 28   SER A C   1 
ATOM   160  O O   . SER A 1 28  ? 24.266  16.204  42.912  1.00 53.50 ? 28   SER A O   1 
ATOM   161  C CB  . SER A 1 28  ? 22.142  15.781  40.746  1.00 59.66 ? 28   SER A CB  1 
ATOM   162  O OG  . SER A 1 28  ? 21.361  16.740  41.459  1.00 59.34 ? 28   SER A OG  1 
ATOM   163  N N   . GLY A 1 29  ? 22.442  15.372  44.041  1.00 49.48 ? 29   GLY A N   1 
ATOM   164  C CA  . GLY A 1 29  ? 22.770  15.861  45.397  1.00 50.76 ? 29   GLY A CA  1 
ATOM   165  C C   . GLY A 1 29  ? 22.046  17.153  45.762  1.00 53.22 ? 29   GLY A C   1 
ATOM   166  O O   . GLY A 1 29  ? 22.538  17.874  46.654  1.00 56.50 ? 29   GLY A O   1 
ATOM   167  N N   . CYS A 1 30  ? 20.891  17.428  45.148  1.00 51.24 ? 30   CYS A N   1 
ATOM   168  C CA  . CYS A 1 30  ? 20.139  18.701  45.320  1.00 47.52 ? 30   CYS A CA  1 
ATOM   169  C C   . CYS A 1 30  ? 19.057  18.521  46.389  1.00 43.48 ? 30   CYS A C   1 
ATOM   170  O O   . CYS A 1 30  ? 18.701  17.371  46.697  1.00 40.94 ? 30   CYS A O   1 
ATOM   171  C CB  . CYS A 1 30  ? 19.518  19.150  44.001  1.00 52.81 ? 30   CYS A CB  1 
ATOM   172  S SG  . CYS A 1 30  ? 17.815  18.579  43.763  1.00 51.08 ? 30   CYS A SG  1 
ATOM   173  N N   . LYS A 1 31  ? 18.537  19.638  46.895  1.00 41.73 ? 31   LYS A N   1 
ATOM   174  C CA  . LYS A 1 31  ? 17.432  19.689  47.883  1.00 43.24 ? 31   LYS A CA  1 
ATOM   175  C C   . LYS A 1 31  ? 16.136  19.909  47.087  1.00 38.14 ? 31   LYS A C   1 
ATOM   176  O O   . LYS A 1 31  ? 15.920  21.026  46.527  1.00 37.24 ? 31   LYS A O   1 
ATOM   177  C CB  . LYS A 1 31  ? 17.821  20.698  48.972  1.00 45.84 ? 31   LYS A CB  1 
ATOM   178  C CG  . LYS A 1 31  ? 16.752  21.668  49.451  1.00 52.53 ? 31   LYS A CG  1 
ATOM   179  C CD  . LYS A 1 31  ? 15.624  21.053  50.252  1.00 56.00 ? 31   LYS A CD  1 
ATOM   180  C CE  . LYS A 1 31  ? 14.537  22.065  50.552  1.00 55.68 ? 31   LYS A CE  1 
ATOM   181  N NZ  . LYS A 1 31  ? 13.381  21.441  51.233  1.00 57.59 ? 31   LYS A NZ  1 
ATOM   182  N N   . LEU A 1 32  ? 15.315  18.863  47.002  1.00 34.46 ? 32   LEU A N   1 
ATOM   183  C CA  . LEU A 1 32  ? 14.201  18.765  46.019  1.00 34.63 ? 32   LEU A CA  1 
ATOM   184  C C   . LEU A 1 32  ? 12.855  19.001  46.706  1.00 34.82 ? 32   LEU A C   1 
ATOM   185  O O   . LEU A 1 32  ? 12.505  18.297  47.681  1.00 35.53 ? 32   LEU A O   1 
ATOM   186  C CB  . LEU A 1 32  ? 14.235  17.399  45.325  1.00 36.11 ? 32   LEU A CB  1 
ATOM   187  C CG  . LEU A 1 32  ? 13.239  17.232  44.173  1.00 34.73 ? 32   LEU A CG  1 
ATOM   188  C CD1 . LEU A 1 32  ? 13.554  18.212  43.055  1.00 36.67 ? 32   LEU A CD1 1 
ATOM   189  C CD2 . LEU A 1 32  ? 13.239  15.799  43.635  1.00 34.30 ? 32   LEU A CD2 1 
ATOM   190  N N   . THR A 1 33  ? 12.108  19.963  46.195  1.00 32.92 ? 33   THR A N   1 
ATOM   191  C CA  . THR A 1 33  ? 10.684  20.153  46.544  1.00 32.13 ? 33   THR A CA  1 
ATOM   192  C C   . THR A 1 33  ? 9.856   19.676  45.356  1.00 29.06 ? 33   THR A C   1 
ATOM   193  O O   . THR A 1 33  ? 10.102  20.118  44.243  1.00 29.02 ? 33   THR A O   1 
ATOM   194  C CB  . THR A 1 33  ? 10.407  21.611  46.933  1.00 30.49 ? 33   THR A CB  1 
ATOM   195  O OG1 . THR A 1 33  ? 11.248  21.882  48.056  1.00 28.25 ? 33   THR A OG1 1 
ATOM   196  C CG2 . THR A 1 33  ? 8.945   21.865  47.244  1.00 30.54 ? 33   THR A CG2 1 
ATOM   197  N N   . VAL A 1 34  ? 8.877   18.824  45.604  1.00 30.24 ? 34   VAL A N   1 
ATOM   198  C CA  . VAL A 1 34  ? 8.022   18.237  44.542  1.00 28.38 ? 34   VAL A CA  1 
ATOM   199  C C   . VAL A 1 34  ? 6.563   18.671  44.763  1.00 26.93 ? 34   VAL A C   1 
ATOM   200  O O   . VAL A 1 34  ? 6.182   19.021  45.870  1.00 25.87 ? 34   VAL A O   1 
ATOM   201  C CB  . VAL A 1 34  ? 8.195   16.705  44.462  1.00 29.11 ? 34   VAL A CB  1 
ATOM   202  C CG1 . VAL A 1 34  ? 9.618   16.343  44.087  1.00 30.52 ? 34   VAL A CG1 1 
ATOM   203  C CG2 . VAL A 1 34  ? 7.775   15.985  45.735  1.00 29.50 ? 34   VAL A CG2 1 
ATOM   204  N N   . TRP A 1 35  ? 5.795   18.705  43.686  1.00 26.62 ? 35   TRP A N   1 
ATOM   205  C CA  . TRP A 1 35  ? 4.323   18.799  43.726  1.00 27.80 ? 35   TRP A CA  1 
ATOM   206  C C   . TRP A 1 35  ? 3.787   17.965  42.577  1.00 29.03 ? 35   TRP A C   1 
ATOM   207  O O   . TRP A 1 35  ? 4.402   17.954  41.491  1.00 27.50 ? 35   TRP A O   1 
ATOM   208  C CB  . TRP A 1 35  ? 3.793   20.241  43.667  1.00 27.30 ? 35   TRP A CB  1 
ATOM   209  C CG  . TRP A 1 35  ? 2.295   20.255  43.650  1.00 28.34 ? 35   TRP A CG  1 
ATOM   210  C CD1 . TRP A 1 35  ? 1.459   20.382  44.718  1.00 29.24 ? 35   TRP A CD1 1 
ATOM   211  C CD2 . TRP A 1 35  ? 1.448   20.088  42.501  1.00 28.47 ? 35   TRP A CD2 1 
ATOM   212  N NE1 . TRP A 1 35  ? 0.158   20.320  44.314  1.00 28.86 ? 35   TRP A NE1 1 
ATOM   213  C CE2 . TRP A 1 35  ? 0.117   20.136  42.962  1.00 27.93 ? 35   TRP A CE2 1 
ATOM   214  C CE3 . TRP A 1 35  ? 1.688   19.907  41.135  1.00 28.34 ? 35   TRP A CE3 1 
ATOM   215  C CZ2 . TRP A 1 35  ? -0.972  19.985  42.112  1.00 27.99 ? 35   TRP A CZ2 1 
ATOM   216  C CZ3 . TRP A 1 35  ? 0.607   19.788  40.286  1.00 30.49 ? 35   TRP A CZ3 1 
ATOM   217  C CH2 . TRP A 1 35  ? -0.701  19.815  40.770  1.00 29.48 ? 35   TRP A CH2 1 
ATOM   218  N N   . ASN A 1 36  ? 2.661   17.309  42.835  1.00 28.27 ? 36   ASN A N   1 
ATOM   219  C CA  . ASN A 1 36  ? 1.950   16.494  41.836  1.00 27.82 ? 36   ASN A CA  1 
ATOM   220  C C   . ASN A 1 36  ? 0.495   16.529  42.247  1.00 27.35 ? 36   ASN A C   1 
ATOM   221  O O   . ASN A 1 36  ? 0.279   16.492  43.436  1.00 27.67 ? 36   ASN A O   1 
ATOM   222  C CB  . ASN A 1 36  ? 2.503   15.068  41.799  1.00 26.65 ? 36   ASN A CB  1 
ATOM   223  C CG  . ASN A 1 36  ? 2.013   14.330  40.579  1.00 27.20 ? 36   ASN A CG  1 
ATOM   224  O OD1 . ASN A 1 36  ? 2.172   14.828  39.468  1.00 26.12 ? 36   ASN A OD1 1 
ATOM   225  N ND2 . ASN A 1 36  ? 1.390   13.177  40.783  1.00 24.80 ? 36   ASN A ND2 1 
ATOM   226  N N   . ARG A 1 37  ? -0.433  16.547  41.294  1.00 29.36 ? 37   ARG A N   1 
ATOM   227  C CA  . ARG A 1 37  ? -1.891  16.451  41.552  1.00 29.59 ? 37   ARG A CA  1 
ATOM   228  C C   . ARG A 1 37  ? -2.169  15.261  42.483  1.00 31.40 ? 37   ARG A C   1 
ATOM   229  O O   . ARG A 1 37  ? -2.895  15.431  43.468  1.00 31.80 ? 37   ARG A O   1 
ATOM   230  C CB  . ARG A 1 37  ? -2.640  16.315  40.223  1.00 30.00 ? 37   ARG A CB  1 
ATOM   231  C CG  . ARG A 1 37  ? -4.099  15.915  40.382  1.00 28.99 ? 37   ARG A CG  1 
ATOM   232  C CD  . ARG A 1 37  ? -4.776  15.794  39.047  1.00 29.56 ? 37   ARG A CD  1 
ATOM   233  N NE  . ARG A 1 37  ? -4.258  14.699  38.247  1.00 27.70 ? 37   ARG A NE  1 
ATOM   234  C CZ  . ARG A 1 37  ? -4.759  14.336  37.074  1.00 28.46 ? 37   ARG A CZ  1 
ATOM   235  N NH1 . ARG A 1 37  ? -4.225  13.339  36.392  1.00 27.36 ? 37   ARG A NH1 1 
ATOM   236  N NH2 . ARG A 1 37  ? -5.812  14.967  36.592  1.00 32.25 ? 37   ARG A NH2 1 
ATOM   237  N N   . SER A 1 38  ? -1.613  14.086  42.174  1.00 30.36 ? 38   SER A N   1 
ATOM   238  C CA  . SER A 1 38  ? -1.674  12.875  43.033  1.00 28.73 ? 38   SER A CA  1 
ATOM   239  C C   . SER A 1 38  ? -0.407  12.812  43.900  1.00 27.49 ? 38   SER A C   1 
ATOM   240  O O   . SER A 1 38  ? 0.625   12.336  43.395  1.00 24.18 ? 38   SER A O   1 
ATOM   241  C CB  . SER A 1 38  ? -1.850  11.641  42.188  1.00 28.43 ? 38   SER A CB  1 
ATOM   242  O OG  . SER A 1 38  ? -2.839  11.845  41.193  1.00 29.62 ? 38   SER A OG  1 
ATOM   243  N N   . ALA A 1 39  ? -0.482  13.334  45.133  1.00 29.60 ? 39   ALA A N   1 
ATOM   244  C CA  . ALA A 1 39  ? 0.662   13.547  46.057  1.00 29.73 ? 39   ALA A CA  1 
ATOM   245  C C   . ALA A 1 39  ? 1.305   12.200  46.411  1.00 29.51 ? 39   ALA A C   1 
ATOM   246  O O   . ALA A 1 39  ? 2.524   12.169  46.691  1.00 29.24 ? 39   ALA A O   1 
ATOM   247  C CB  . ALA A 1 39  ? 0.235   14.298  47.304  1.00 29.84 ? 39   ALA A CB  1 
ATOM   248  N N   . SER A 1 40  ? 0.531   11.119  46.360  1.00 30.48 ? 40   SER A N   1 
ATOM   249  C CA  . SER A 1 40  ? 0.999   9.743   46.662  1.00 32.19 ? 40   SER A CA  1 
ATOM   250  C C   . SER A 1 40  ? 2.171   9.355   45.750  1.00 31.42 ? 40   SER A C   1 
ATOM   251  O O   . SER A 1 40  ? 2.936   8.440   46.140  1.00 29.97 ? 40   SER A O   1 
ATOM   252  C CB  . SER A 1 40  ? -0.109  8.760   46.515  1.00 31.80 ? 40   SER A CB  1 
ATOM   253  O OG  . SER A 1 40  ? -0.401  8.606   45.135  1.00 34.81 ? 40   SER A OG  1 
ATOM   254  N N   . LYS A 1 41  ? 2.302   9.969   44.566  1.00 29.11 ? 41   LYS A N   1 
ATOM   255  C CA  . LYS A 1 41  ? 3.407   9.606   43.640  1.00 31.23 ? 41   LYS A CA  1 
ATOM   256  C C   . LYS A 1 41  ? 4.750   10.108  44.191  1.00 28.86 ? 41   LYS A C   1 
ATOM   257  O O   . LYS A 1 41  ? 5.782   9.788   43.575  1.00 24.63 ? 41   LYS A O   1 
ATOM   258  C CB  . LYS A 1 41  ? 3.088   10.088  42.225  1.00 33.06 ? 41   LYS A CB  1 
ATOM   259  C CG  . LYS A 1 41  ? 2.022   9.235   41.550  1.00 34.91 ? 41   LYS A CG  1 
ATOM   260  C CD  . LYS A 1 41  ? 1.539   9.804   40.258  1.00 38.57 ? 41   LYS A CD  1 
ATOM   261  C CE  . LYS A 1 41  ? 0.433   8.976   39.629  1.00 39.26 ? 41   LYS A CE  1 
ATOM   262  N NZ  . LYS A 1 41  ? 0.253   9.319   38.197  1.00 39.12 ? 41   LYS A NZ  1 
ATOM   263  N N   . ALA A 1 42  ? 4.746   10.870  45.295  1.00 26.81 ? 42   ALA A N   1 
ATOM   264  C CA  . ALA A 1 42  ? 5.983   11.353  45.957  1.00 27.75 ? 42   ALA A CA  1 
ATOM   265  C C   . ALA A 1 42  ? 6.467   10.325  46.993  1.00 27.64 ? 42   ALA A C   1 
ATOM   266  O O   . ALA A 1 42  ? 7.628   10.451  47.450  1.00 28.67 ? 42   ALA A O   1 
ATOM   267  C CB  . ALA A 1 42  ? 5.740   12.704  46.582  1.00 26.64 ? 42   ALA A CB  1 
ATOM   268  N N   . ALA A 1 43  ? 5.632   9.332   47.331  1.00 27.47 ? 43   ALA A N   1 
ATOM   269  C CA  . ALA A 1 43  ? 5.877   8.323   48.389  1.00 28.02 ? 43   ALA A CA  1 
ATOM   270  C C   . ALA A 1 43  ? 7.283   7.714   48.268  1.00 29.32 ? 43   ALA A C   1 
ATOM   271  O O   . ALA A 1 43  ? 7.957   7.625   49.316  1.00 30.97 ? 43   ALA A O   1 
ATOM   272  C CB  . ALA A 1 43  ? 4.797   7.266   48.352  1.00 29.41 ? 43   ALA A CB  1 
ATOM   273  N N   . SER A 1 44  ? 7.752   7.357   47.061  1.00 28.81 ? 44   SER A N   1 
ATOM   274  C CA  . SER A 1 44  ? 9.079   6.706   46.862  1.00 30.68 ? 44   SER A CA  1 
ATOM   275  C C   . SER A 1 44  ? 10.227  7.713   47.060  1.00 31.83 ? 44   SER A C   1 
ATOM   276  O O   . SER A 1 44  ? 11.382  7.281   47.075  1.00 31.64 ? 44   SER A O   1 
ATOM   277  C CB  . SER A 1 44  ? 9.170   6.005   45.526  1.00 31.82 ? 44   SER A CB  1 
ATOM   278  O OG  . SER A 1 44  ? 9.068   6.929   44.452  1.00 31.26 ? 44   SER A OG  1 
ATOM   279  N N   . LEU A 1 45  ? 9.932   9.006   47.216  1.00 34.51 ? 45   LEU A N   1 
ATOM   280  C CA  . LEU A 1 45  ? 10.953  10.090  47.289  1.00 35.14 ? 45   LEU A CA  1 
ATOM   281  C C   . LEU A 1 45  ? 11.146  10.579  48.732  1.00 34.87 ? 45   LEU A C   1 
ATOM   282  O O   . LEU A 1 45  ? 12.213  11.152  49.015  1.00 33.61 ? 45   LEU A O   1 
ATOM   283  C CB  . LEU A 1 45  ? 10.508  11.250  46.394  1.00 36.12 ? 45   LEU A CB  1 
ATOM   284  C CG  . LEU A 1 45  ? 10.087  10.873  44.977  1.00 34.94 ? 45   LEU A CG  1 
ATOM   285  C CD1 . LEU A 1 45  ? 9.547   12.094  44.252  1.00 35.60 ? 45   LEU A CD1 1 
ATOM   286  C CD2 . LEU A 1 45  ? 11.249  10.251  44.219  1.00 34.52 ? 45   LEU A CD2 1 
ATOM   287  N N   . VAL A 1 46  ? 10.149  10.399  49.602  1.00 37.10 ? 46   VAL A N   1 
ATOM   288  C CA  . VAL A 1 46  ? 10.147  10.931  50.999  1.00 38.02 ? 46   VAL A CA  1 
ATOM   289  C C   . VAL A 1 46  ? 11.380  10.409  51.766  1.00 39.35 ? 46   VAL A C   1 
ATOM   290  O O   . VAL A 1 46  ? 12.056  11.229  52.420  1.00 40.71 ? 46   VAL A O   1 
ATOM   291  C CB  . VAL A 1 46  ? 8.805   10.600  51.677  1.00 39.09 ? 46   VAL A CB  1 
ATOM   292  C CG1 . VAL A 1 46  ? 8.852   10.716  53.195  1.00 38.95 ? 46   VAL A CG1 1 
ATOM   293  C CG2 . VAL A 1 46  ? 7.698   11.473  51.098  1.00 41.96 ? 46   VAL A CG2 1 
ATOM   294  N N   . ALA A 1 47  ? 11.710  9.121   51.640  1.00 39.30 ? 47   ALA A N   1 
ATOM   295  C CA  . ALA A 1 47  ? 12.878  8.493   52.301  1.00 41.40 ? 47   ALA A CA  1 
ATOM   296  C C   . ALA A 1 47  ? 14.173  9.152   51.817  1.00 46.01 ? 47   ALA A C   1 
ATOM   297  O O   . ALA A 1 47  ? 15.130  9.201   52.615  1.00 47.66 ? 47   ALA A O   1 
ATOM   298  C CB  . ALA A 1 47  ? 12.913  7.010   52.033  1.00 42.20 ? 47   ALA A CB  1 
ATOM   299  N N   . GLN A 1 48  ? 14.228  9.610   50.558  1.00 45.91 ? 48   GLN A N   1 
ATOM   300  C CA  . GLN A 1 48  ? 15.474  10.140  49.931  1.00 42.48 ? 48   GLN A CA  1 
ATOM   301  C C   . GLN A 1 48  ? 15.647  11.619  50.312  1.00 40.08 ? 48   GLN A C   1 
ATOM   302  O O   . GLN A 1 48  ? 16.589  12.237  49.796  1.00 42.75 ? 48   GLN A O   1 
ATOM   303  C CB  . GLN A 1 48  ? 15.474  9.953   48.408  1.00 43.61 ? 48   GLN A CB  1 
ATOM   304  C CG  . GLN A 1 48  ? 15.046  8.565   47.916  1.00 43.28 ? 48   GLN A CG  1 
ATOM   305  C CD  . GLN A 1 48  ? 15.252  8.411   46.426  1.00 43.27 ? 48   GLN A CD  1 
ATOM   306  O OE1 . GLN A 1 48  ? 16.327  8.697   45.898  1.00 44.06 ? 48   GLN A OE1 1 
ATOM   307  N NE2 . GLN A 1 48  ? 14.217  7.970   45.724  1.00 36.66 ? 48   GLN A NE2 1 
ATOM   308  N N   . GLY A 1 49  ? 14.774  12.151  51.178  1.00 40.46 ? 49   GLY A N   1 
ATOM   309  C CA  . GLY A 1 49  ? 14.882  13.494  51.788  1.00 41.66 ? 49   GLY A CA  1 
ATOM   310  C C   . GLY A 1 49  ? 14.164  14.570  50.986  1.00 43.22 ? 49   GLY A C   1 
ATOM   311  O O   . GLY A 1 49  ? 14.572  15.750  51.088  1.00 42.49 ? 49   GLY A O   1 
ATOM   312  N N   . VAL A 1 50  ? 13.130  14.196  50.222  1.00 42.06 ? 50   VAL A N   1 
ATOM   313  C CA  . VAL A 1 50  ? 12.366  15.128  49.339  1.00 39.16 ? 50   VAL A CA  1 
ATOM   314  C C   . VAL A 1 50  ? 11.236  15.745  50.167  1.00 35.71 ? 50   VAL A C   1 
ATOM   315  O O   . VAL A 1 50  ? 10.563  14.979  50.898  1.00 32.17 ? 50   VAL A O   1 
ATOM   316  C CB  . VAL A 1 50  ? 11.807  14.425  48.083  1.00 44.29 ? 50   VAL A CB  1 
ATOM   317  C CG1 . VAL A 1 50  ? 10.445  13.808  48.336  1.00 49.27 ? 50   VAL A CG1 1 
ATOM   318  C CG2 . VAL A 1 50  ? 11.694  15.374  46.901  1.00 46.40 ? 50   VAL A CG2 1 
ATOM   319  N N   . THR A 1 51  ? 11.011  17.054  50.011  1.00 28.94 ? 51   THR A N   1 
ATOM   320  C CA  . THR A 1 51  ? 9.850   17.796  50.584  1.00 32.70 ? 51   THR A CA  1 
ATOM   321  C C   . THR A 1 51  ? 8.682   17.790  49.584  1.00 31.23 ? 51   THR A C   1 
ATOM   322  O O   . THR A 1 51  ? 8.917   18.066  48.406  1.00 29.95 ? 51   THR A O   1 
ATOM   323  C CB  . THR A 1 51  ? 10.246  19.227  50.969  1.00 32.44 ? 51   THR A CB  1 
ATOM   324  O OG1 . THR A 1 51  ? 11.392  19.143  51.827  1.00 30.27 ? 51   THR A OG1 1 
ATOM   325  C CG2 . THR A 1 51  ? 9.100   19.971  51.622  1.00 32.93 ? 51   THR A CG2 1 
ATOM   326  N N   . VAL A 1 52  ? 7.480   17.424  50.028  1.00 29.68 ? 52   VAL A N   1 
ATOM   327  C CA  . VAL A 1 52  ? 6.237   17.524  49.223  1.00 29.05 ? 52   VAL A CA  1 
ATOM   328  C C   . VAL A 1 52  ? 5.547   18.837  49.582  1.00 31.90 ? 52   VAL A C   1 
ATOM   329  O O   . VAL A 1 52  ? 5.080   18.973  50.713  1.00 31.99 ? 52   VAL A O   1 
ATOM   330  C CB  . VAL A 1 52  ? 5.307   16.320  49.430  1.00 27.81 ? 52   VAL A CB  1 
ATOM   331  C CG1 . VAL A 1 52  ? 4.043   16.451  48.605  1.00 28.95 ? 52   VAL A CG1 1 
ATOM   332  C CG2 . VAL A 1 52  ? 6.008   15.018  49.094  1.00 30.46 ? 52   VAL A CG2 1 
ATOM   333  N N   . ALA A 1 53  ? 5.492   19.770  48.641  1.00 33.16 ? 53   ALA A N   1 
ATOM   334  C CA  . ALA A 1 53  ? 4.747   21.032  48.799  1.00 31.24 ? 53   ALA A CA  1 
ATOM   335  C C   . ALA A 1 53  ? 3.274   20.755  48.478  1.00 30.76 ? 53   ALA A C   1 
ATOM   336  O O   . ALA A 1 53  ? 2.970   19.896  47.587  1.00 31.57 ? 53   ALA A O   1 
ATOM   337  C CB  . ALA A 1 53  ? 5.362   22.096  47.933  1.00 30.91 ? 53   ALA A CB  1 
ATOM   338  N N   . ALA A 1 54  ? 2.391   21.432  49.212  1.00 31.41 ? 54   ALA A N   1 
ATOM   339  C CA  . ALA A 1 54  ? 0.929   21.210  49.209  1.00 31.44 ? 54   ALA A CA  1 
ATOM   340  C C   . ALA A 1 54  ? 0.355   21.767  47.904  1.00 31.18 ? 54   ALA A C   1 
ATOM   341  O O   . ALA A 1 54  ? -0.583  21.157  47.371  1.00 30.66 ? 54   ALA A O   1 
ATOM   342  C CB  . ALA A 1 54  ? 0.312   21.848  50.433  1.00 33.63 ? 54   ALA A CB  1 
ATOM   343  N N   . THR A 1 55  ? 0.925   22.859  47.377  1.00 28.60 ? 55   THR A N   1 
ATOM   344  C CA  . THR A 1 55  ? 0.388   23.556  46.180  1.00 29.31 ? 55   THR A CA  1 
ATOM   345  C C   . THR A 1 55  ? 1.529   23.896  45.220  1.00 29.67 ? 55   THR A C   1 
ATOM   346  O O   . THR A 1 55  ? 2.683   24.015  45.618  1.00 29.47 ? 55   THR A O   1 
ATOM   347  C CB  . THR A 1 55  ? -0.433  24.799  46.567  1.00 30.81 ? 55   THR A CB  1 
ATOM   348  O OG1 . THR A 1 55  ? 0.385   25.783  47.200  1.00 31.34 ? 55   THR A OG1 1 
ATOM   349  C CG2 . THR A 1 55  ? -1.600  24.490  47.480  1.00 31.41 ? 55   THR A CG2 1 
ATOM   350  N N   . PRO A 1 56  ? 1.228   24.047  43.914  1.00 28.61 ? 56   PRO A N   1 
ATOM   351  C CA  . PRO A 1 56  ? 2.196   24.563  42.945  1.00 28.60 ? 56   PRO A CA  1 
ATOM   352  C C   . PRO A 1 56  ? 2.915   25.829  43.418  1.00 27.44 ? 56   PRO A C   1 
ATOM   353  O O   . PRO A 1 56  ? 4.094   25.916  43.238  1.00 26.97 ? 56   PRO A O   1 
ATOM   354  C CB  . PRO A 1 56  ? 1.304   24.841  41.722  1.00 28.97 ? 56   PRO A CB  1 
ATOM   355  C CG  . PRO A 1 56  ? 0.264   23.737  41.809  1.00 29.84 ? 56   PRO A CG  1 
ATOM   356  C CD  . PRO A 1 56  ? -0.065  23.704  43.290  1.00 29.47 ? 56   PRO A CD  1 
ATOM   357  N N   . ALA A 1 57  ? 2.181   26.766  44.019  1.00 27.84 ? 57   ALA A N   1 
ATOM   358  C CA  . ALA A 1 57  ? 2.723   28.045  44.526  1.00 28.02 ? 57   ALA A CA  1 
ATOM   359  C C   . ALA A 1 57  ? 3.794   27.743  45.575  1.00 28.19 ? 57   ALA A C   1 
ATOM   360  O O   . ALA A 1 57  ? 4.926   28.223  45.436  1.00 28.93 ? 57   ALA A O   1 
ATOM   361  C CB  . ALA A 1 57  ? 1.617   28.892  45.100  1.00 29.47 ? 57   ALA A CB  1 
ATOM   362  N N   . GLU A 1 58  ? 3.460   26.977  46.604  1.00 31.33 ? 58   GLU A N   1 
ATOM   363  C CA  . GLU A 1 58  ? 4.422   26.698  47.697  1.00 32.40 ? 58   GLU A CA  1 
ATOM   364  C C   . GLU A 1 58  ? 5.597   25.935  47.078  1.00 32.19 ? 58   GLU A C   1 
ATOM   365  O O   . GLU A 1 58  ? 6.750   26.208  47.463  1.00 36.64 ? 58   GLU A O   1 
ATOM   366  C CB  . GLU A 1 58  ? 3.726   26.006  48.874  1.00 37.30 ? 58   GLU A CB  1 
ATOM   367  C CG  . GLU A 1 58  ? 2.682   26.882  49.564  1.00 41.27 ? 58   GLU A CG  1 
ATOM   368  C CD  . GLU A 1 58  ? 1.638   26.150  50.407  1.00 45.93 ? 58   GLU A CD  1 
ATOM   369  O OE1 . GLU A 1 58  ? 1.986   25.109  51.008  1.00 44.39 ? 58   GLU A OE1 1 
ATOM   370  O OE2 . GLU A 1 58  ? 0.457   26.612  50.446  1.00 51.57 ? 58   GLU A OE2 1 
ATOM   371  N N   . CYS A 1 59  ? 5.347   25.083  46.078  1.00 30.44 ? 59   CYS A N   1 
ATOM   372  C CA  . CYS A 1 59  ? 6.431   24.324  45.405  1.00 28.65 ? 59   CYS A CA  1 
ATOM   373  C C   . CYS A 1 59  ? 7.425   25.310  44.770  1.00 29.54 ? 59   CYS A C   1 
ATOM   374  O O   . CYS A 1 59  ? 8.645   25.132  44.955  1.00 29.61 ? 59   CYS A O   1 
ATOM   375  C CB  . CYS A 1 59  ? 5.877   23.344  44.380  1.00 28.88 ? 59   CYS A CB  1 
ATOM   376  S SG  . CYS A 1 59  ? 7.176   22.331  43.632  1.00 31.84 ? 59   CYS A SG  1 
ATOM   377  N N   . VAL A 1 60  ? 6.927   26.330  44.071  1.00 31.14 ? 60   VAL A N   1 
ATOM   378  C CA  . VAL A 1 60  ? 7.763   27.291  43.282  1.00 32.49 ? 60   VAL A CA  1 
ATOM   379  C C   . VAL A 1 60  ? 8.493   28.252  44.231  1.00 32.40 ? 60   VAL A C   1 
ATOM   380  O O   . VAL A 1 60  ? 9.677   28.537  43.977  1.00 30.83 ? 60   VAL A O   1 
ATOM   381  C CB  . VAL A 1 60  ? 6.905   28.040  42.242  1.00 33.77 ? 60   VAL A CB  1 
ATOM   382  C CG1 . VAL A 1 60  ? 7.600   29.285  41.728  1.00 32.96 ? 60   VAL A CG1 1 
ATOM   383  C CG2 . VAL A 1 60  ? 6.527   27.121  41.088  1.00 33.40 ? 60   VAL A CG2 1 
ATOM   384  N N   . ALA A 1 61  ? 7.832   28.700  45.303  1.00 32.98 ? 61   ALA A N   1 
ATOM   385  C CA  . ALA A 1 61  ? 8.437   29.518  46.385  1.00 34.93 ? 61   ALA A CA  1 
ATOM   386  C C   . ALA A 1 61  ? 9.728   28.876  46.923  1.00 37.41 ? 61   ALA A C   1 
ATOM   387  O O   . ALA A 1 61  ? 10.646  29.635  47.267  1.00 39.07 ? 61   ALA A O   1 
ATOM   388  C CB  . ALA A 1 61  ? 7.435   29.710  47.490  1.00 36.34 ? 61   ALA A CB  1 
ATOM   389  N N   . SER A 1 62  ? 9.801   27.536  46.967  1.00 37.15 ? 62   SER A N   1 
ATOM   390  C CA  . SER A 1 62  ? 10.806  26.738  47.715  1.00 35.53 ? 62   SER A CA  1 
ATOM   391  C C   . SER A 1 62  ? 12.189  26.763  47.054  1.00 36.14 ? 62   SER A C   1 
ATOM   392  O O   . SER A 1 62  ? 13.158  26.454  47.770  1.00 35.53 ? 62   SER A O   1 
ATOM   393  C CB  . SER A 1 62  ? 10.336  25.314  47.901  1.00 36.09 ? 62   SER A CB  1 
ATOM   394  O OG  . SER A 1 62  ? 9.189   25.270  48.731  1.00 36.07 ? 62   SER A OG  1 
ATOM   395  N N   . SER A 1 63  ? 12.292  27.085  45.757  1.00 36.66 ? 63   SER A N   1 
ATOM   396  C CA  . SER A 1 63  ? 13.557  26.986  44.973  1.00 33.29 ? 63   SER A CA  1 
ATOM   397  C C   . SER A 1 63  ? 13.665  28.106  43.936  1.00 32.19 ? 63   SER A C   1 
ATOM   398  O O   . SER A 1 63  ? 12.662  28.651  43.479  1.00 32.37 ? 63   SER A O   1 
ATOM   399  C CB  . SER A 1 63  ? 13.657  25.634  44.305  1.00 34.56 ? 63   SER A CB  1 
ATOM   400  O OG  . SER A 1 63  ? 13.147  24.591  45.137  1.00 35.20 ? 63   SER A OG  1 
ATOM   401  N N   . PRO A 1 64  ? 14.895  28.509  43.543  1.00 32.74 ? 64   PRO A N   1 
ATOM   402  C CA  . PRO A 1 64  ? 15.091  29.404  42.393  1.00 32.82 ? 64   PRO A CA  1 
ATOM   403  C C   . PRO A 1 64  ? 15.051  28.752  40.997  1.00 31.53 ? 64   PRO A C   1 
ATOM   404  O O   . PRO A 1 64  ? 15.140  29.456  40.032  1.00 29.90 ? 64   PRO A O   1 
ATOM   405  C CB  . PRO A 1 64  ? 16.514  29.964  42.619  1.00 33.60 ? 64   PRO A CB  1 
ATOM   406  C CG  . PRO A 1 64  ? 17.220  28.896  43.417  1.00 34.65 ? 64   PRO A CG  1 
ATOM   407  C CD  . PRO A 1 64  ? 16.148  28.224  44.260  1.00 34.19 ? 64   PRO A CD  1 
ATOM   408  N N   . THR A 1 65  ? 14.993  27.421  40.928  1.00 31.77 ? 65   THR A N   1 
ATOM   409  C CA  . THR A 1 65  ? 15.042  26.624  39.681  1.00 29.87 ? 65   THR A CA  1 
ATOM   410  C C   . THR A 1 65  ? 13.839  25.674  39.681  1.00 29.99 ? 65   THR A C   1 
ATOM   411  O O   . THR A 1 65  ? 13.821  24.751  40.516  1.00 32.32 ? 65   THR A O   1 
ATOM   412  C CB  . THR A 1 65  ? 16.356  25.839  39.581  1.00 32.37 ? 65   THR A CB  1 
ATOM   413  O OG1 . THR A 1 65  ? 17.431  26.761  39.745  1.00 32.35 ? 65   THR A OG1 1 
ATOM   414  C CG2 . THR A 1 65  ? 16.485  25.087  38.274  1.00 32.31 ? 65   THR A CG2 1 
ATOM   415  N N   . ILE A 1 66  ? 12.871  25.909  38.801  1.00 27.41 ? 66   ILE A N   1 
ATOM   416  C CA  . ILE A 1 66  ? 11.617  25.107  38.684  1.00 28.16 ? 66   ILE A CA  1 
ATOM   417  C C   . ILE A 1 66  ? 11.732  24.181  37.474  1.00 27.64 ? 66   ILE A C   1 
ATOM   418  O O   . ILE A 1 66  ? 11.860  24.697  36.366  1.00 30.26 ? 66   ILE A O   1 
ATOM   419  C CB  . ILE A 1 66  ? 10.381  26.006  38.524  1.00 27.53 ? 66   ILE A CB  1 
ATOM   420  C CG1 . ILE A 1 66  ? 10.432  27.235  39.438  1.00 25.76 ? 66   ILE A CG1 1 
ATOM   421  C CG2 . ILE A 1 66  ? 9.123   25.172  38.729  1.00 27.83 ? 66   ILE A CG2 1 
ATOM   422  C CD1 . ILE A 1 66  ? 10.625  26.908  40.883  1.00 26.41 ? 66   ILE A CD1 1 
ATOM   423  N N   . VAL A 1 67  ? 11.665  22.870  37.681  1.00 26.27 ? 67   VAL A N   1 
ATOM   424  C CA  . VAL A 1 67  ? 11.505  21.882  36.578  1.00 23.82 ? 67   VAL A CA  1 
ATOM   425  C C   . VAL A 1 67  ? 10.023  21.517  36.478  1.00 23.33 ? 67   VAL A C   1 
ATOM   426  O O   . VAL A 1 67  ? 9.387   21.255  37.536  1.00 23.43 ? 67   VAL A O   1 
ATOM   427  C CB  . VAL A 1 67  ? 12.422  20.664  36.779  1.00 23.83 ? 67   VAL A CB  1 
ATOM   428  C CG1 . VAL A 1 67  ? 12.362  19.709  35.590  1.00 24.69 ? 67   VAL A CG1 1 
ATOM   429  C CG2 . VAL A 1 67  ? 13.866  21.102  37.043  1.00 24.38 ? 67   VAL A CG2 1 
ATOM   430  N N   . ILE A 1 68  ? 9.475   21.567  35.267  1.00 22.43 ? 68   ILE A N   1 
ATOM   431  C CA  . ILE A 1 68  ? 8.061   21.175  34.998  1.00 22.79 ? 68   ILE A CA  1 
ATOM   432  C C   . ILE A 1 68  ? 8.083   19.970  34.063  1.00 21.35 ? 68   ILE A C   1 
ATOM   433  O O   . ILE A 1 68  ? 8.700   20.057  33.023  1.00 22.88 ? 68   ILE A O   1 
ATOM   434  C CB  . ILE A 1 68  ? 7.215   22.328  34.419  1.00 21.43 ? 68   ILE A CB  1 
ATOM   435  C CG1 . ILE A 1 68  ? 7.257   23.574  35.303  1.00 22.32 ? 68   ILE A CG1 1 
ATOM   436  C CG2 . ILE A 1 68  ? 5.782   21.861  34.195  1.00 21.40 ? 68   ILE A CG2 1 
ATOM   437  C CD1 . ILE A 1 68  ? 6.778   24.846  34.613  1.00 21.91 ? 68   ILE A CD1 1 
ATOM   438  N N   . CYS A 1 69  ? 7.408   18.894  34.425  1.00 20.93 ? 69   CYS A N   1 
ATOM   439  C CA  . CYS A 1 69  ? 7.222   17.747  33.513  1.00 21.39 ? 69   CYS A CA  1 
ATOM   440  C C   . CYS A 1 69  ? 5.811   17.191  33.696  1.00 21.93 ? 69   CYS A C   1 
ATOM   441  O O   . CYS A 1 69  ? 5.632   16.217  34.467  1.00 23.68 ? 69   CYS A O   1 
ATOM   442  C CB  . CYS A 1 69  ? 8.313   16.713  33.738  1.00 20.87 ? 69   CYS A CB  1 
ATOM   443  S SG  . CYS A 1 69  ? 8.261   15.450  32.448  1.00 22.72 ? 69   CYS A SG  1 
ATOM   444  N N   . LEU A 1 70  ? 4.846   17.837  33.041  1.00 22.79 ? 70   LEU A N   1 
ATOM   445  C CA  . LEU A 1 70  ? 3.397   17.513  33.106  1.00 22.49 ? 70   LEU A CA  1 
ATOM   446  C C   . LEU A 1 70  ? 2.926   16.914  31.775  1.00 22.71 ? 70   LEU A C   1 
ATOM   447  O O   . LEU A 1 70  ? 3.716   16.881  30.830  1.00 20.81 ? 70   LEU A O   1 
ATOM   448  C CB  . LEU A 1 70  ? 2.616   18.785  33.439  1.00 21.41 ? 70   LEU A CB  1 
ATOM   449  C CG  . LEU A 1 70  ? 2.821   19.306  34.854  1.00 21.19 ? 70   LEU A CG  1 
ATOM   450  C CD1 . LEU A 1 70  ? 2.303   20.735  34.979  1.00 19.43 ? 70   LEU A CD1 1 
ATOM   451  C CD2 . LEU A 1 70  ? 2.172   18.375  35.870  1.00 20.92 ? 70   LEU A CD2 1 
ATOM   452  N N   . LEU A 1 71  ? 1.676   16.442  31.714  1.00 23.45 ? 71   LEU A N   1 
ATOM   453  C CA  . LEU A 1 71  ? 1.114   15.786  30.495  1.00 25.08 ? 71   LEU A CA  1 
ATOM   454  C C   . LEU A 1 71  ? 1.293   16.703  29.279  1.00 25.45 ? 71   LEU A C   1 
ATOM   455  O O   . LEU A 1 71  ? 1.729   16.222  28.216  1.00 28.29 ? 71   LEU A O   1 
ATOM   456  C CB  . LEU A 1 71  ? -0.373  15.493  30.695  1.00 27.21 ? 71   LEU A CB  1 
ATOM   457  C CG  . LEU A 1 71  ? -0.913  14.184  30.114  1.00 30.01 ? 71   LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 71  ? -2.346  14.375  29.641  1.00 29.31 ? 71   LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 71  ? -0.042  13.623  28.998  1.00 28.09 ? 71   LEU A CD2 1 
ATOM   460  N N   . SER A 1 72  ? 0.948   17.978  29.422  1.00 23.00 ? 72   SER A N   1 
ATOM   461  C CA  . SER A 1 72  ? 0.658   18.862  28.273  1.00 25.34 ? 72   SER A CA  1 
ATOM   462  C C   . SER A 1 72  ? 0.671   20.333  28.693  1.00 24.71 ? 72   SER A C   1 
ATOM   463  O O   . SER A 1 72  ? 0.596   20.624  29.903  1.00 22.04 ? 72   SER A O   1 
ATOM   464  C CB  . SER A 1 72  ? -0.677  18.521  27.698  1.00 25.41 ? 72   SER A CB  1 
ATOM   465  O OG  . SER A 1 72  ? -1.683  18.994  28.576  1.00 27.44 ? 72   SER A OG  1 
ATOM   466  N N   . TYR A 1 73  ? 0.714   21.212  27.688  1.00 24.34 ? 73   TYR A N   1 
ATOM   467  C CA  . TYR A 1 73  ? 0.566   22.676  27.846  1.00 25.42 ? 73   TYR A CA  1 
ATOM   468  C C   . TYR A 1 73  ? -0.685  23.009  28.673  1.00 25.01 ? 73   TYR A C   1 
ATOM   469  O O   . TYR A 1 73  ? -0.560  23.737  29.631  1.00 26.67 ? 73   TYR A O   1 
ATOM   470  C CB  . TYR A 1 73  ? 0.486   23.343  26.475  1.00 26.36 ? 73   TYR A CB  1 
ATOM   471  C CG  . TYR A 1 73  ? -0.002  24.759  26.544  1.00 27.22 ? 73   TYR A CG  1 
ATOM   472  C CD1 . TYR A 1 73  ? 0.813   25.754  27.045  1.00 28.22 ? 73   TYR A CD1 1 
ATOM   473  C CD2 . TYR A 1 73  ? -1.277  25.097  26.131  1.00 28.79 ? 73   TYR A CD2 1 
ATOM   474  C CE1 . TYR A 1 73  ? 0.383   27.066  27.128  1.00 30.26 ? 73   TYR A CE1 1 
ATOM   475  C CE2 . TYR A 1 73  ? -1.719  26.409  26.190  1.00 30.29 ? 73   TYR A CE2 1 
ATOM   476  C CZ  . TYR A 1 73  ? -0.885  27.395  26.690  1.00 31.28 ? 73   TYR A CZ  1 
ATOM   477  O OH  . TYR A 1 73  ? -1.281  28.697  26.754  1.00 32.39 ? 73   TYR A OH  1 
ATOM   478  N N   . ASP A 1 74  ? -1.854  22.511  28.274  1.00 26.38 ? 74   ASP A N   1 
ATOM   479  C CA  . ASP A 1 74  ? -3.130  22.831  28.957  1.00 29.24 ? 74   ASP A CA  1 
ATOM   480  C C   . ASP A 1 74  ? -2.957  22.531  30.439  1.00 28.59 ? 74   ASP A C   1 
ATOM   481  O O   . ASP A 1 74  ? -3.348  23.371  31.257  1.00 28.76 ? 74   ASP A O   1 
ATOM   482  C CB  . ASP A 1 74  ? -4.316  22.087  28.350  1.00 32.31 ? 74   ASP A CB  1 
ATOM   483  C CG  . ASP A 1 74  ? -4.863  22.742  27.092  1.00 35.01 ? 74   ASP A CG  1 
ATOM   484  O OD1 . ASP A 1 74  ? -4.434  23.886  26.770  1.00 36.00 ? 74   ASP A OD1 1 
ATOM   485  O OD2 . ASP A 1 74  ? -5.734  22.125  26.464  1.00 34.48 ? 74   ASP A OD2 1 
ATOM   486  N N   . VAL A 1 75  ? -2.387  21.374  30.771  1.00 26.33 ? 75   VAL A N   1 
ATOM   487  C CA  . VAL A 1 75  ? -2.199  20.988  32.197  1.00 25.71 ? 75   VAL A CA  1 
ATOM   488  C C   . VAL A 1 75  ? -1.182  21.947  32.832  1.00 24.19 ? 75   VAL A C   1 
ATOM   489  O O   . VAL A 1 75  ? -1.375  22.326  33.982  1.00 24.18 ? 75   VAL A O   1 
ATOM   490  C CB  . VAL A 1 75  ? -1.811  19.509  32.335  1.00 25.86 ? 75   VAL A CB  1 
ATOM   491  C CG1 . VAL A 1 75  ? -1.427  19.174  33.769  1.00 27.58 ? 75   VAL A CG1 1 
ATOM   492  C CG2 . VAL A 1 75  ? -2.942  18.602  31.843  1.00 27.09 ? 75   VAL A CG2 1 
ATOM   493  N N   . THR A 1 76  ? -0.156  22.351  32.089  1.00 23.58 ? 76   THR A N   1 
ATOM   494  C CA  . THR A 1 76  ? 0.866   23.314  32.563  1.00 25.76 ? 76   THR A CA  1 
ATOM   495  C C   . THR A 1 76  ? 0.217   24.675  32.876  1.00 27.37 ? 76   THR A C   1 
ATOM   496  O O   . THR A 1 76  ? 0.475   25.184  33.967  1.00 25.48 ? 76   THR A O   1 
ATOM   497  C CB  . THR A 1 76  ? 2.012   23.457  31.560  1.00 24.35 ? 76   THR A CB  1 
ATOM   498  O OG1 . THR A 1 76  ? 2.552   22.169  31.262  1.00 23.54 ? 76   THR A OG1 1 
ATOM   499  C CG2 . THR A 1 76  ? 3.073   24.398  32.089  1.00 25.99 ? 76   THR A CG2 1 
ATOM   500  N N   . GLN A 1 77  ? -0.571  25.237  31.948  1.00 28.08 ? 77   GLN A N   1 
ATOM   501  C CA  . GLN A 1 77  ? -1.365  26.486  32.157  1.00 31.40 ? 77   GLN A CA  1 
ATOM   502  C C   . GLN A 1 77  ? -2.253  26.342  33.408  1.00 29.93 ? 77   GLN A C   1 
ATOM   503  O O   . GLN A 1 77  ? -2.296  27.294  34.202  1.00 26.61 ? 77   GLN A O   1 
ATOM   504  C CB  . GLN A 1 77  ? -2.157  26.841  30.885  1.00 35.16 ? 77   GLN A CB  1 
ATOM   505  C CG  . GLN A 1 77  ? -3.468  27.595  31.113  1.00 40.85 ? 77   GLN A CG  1 
ATOM   506  C CD  . GLN A 1 77  ? -4.662  26.698  31.377  1.00 43.89 ? 77   GLN A CD  1 
ATOM   507  O OE1 . GLN A 1 77  ? -4.816  25.642  30.760  1.00 43.54 ? 77   GLN A OE1 1 
ATOM   508  N NE2 . GLN A 1 77  ? -5.535  27.117  32.293  1.00 45.59 ? 77   GLN A NE2 1 
ATOM   509  N N   . GLN A 1 78  ? -2.958  25.217  33.582  1.00 32.27 ? 78   GLN A N   1 
ATOM   510  C CA  . GLN A 1 78  ? -3.885  25.005  34.735  1.00 35.12 ? 78   GLN A CA  1 
ATOM   511  C C   . GLN A 1 78  ? -3.068  25.029  36.033  1.00 33.95 ? 78   GLN A C   1 
ATOM   512  O O   . GLN A 1 78  ? -3.492  25.671  37.003  1.00 31.32 ? 78   GLN A O   1 
ATOM   513  C CB  . GLN A 1 78  ? -4.649  23.684  34.611  1.00 37.77 ? 78   GLN A CB  1 
ATOM   514  C CG  . GLN A 1 78  ? -5.664  23.659  33.478  1.00 46.73 ? 78   GLN A CG  1 
ATOM   515  C CD  . GLN A 1 78  ? -6.036  22.263  33.022  1.00 52.34 ? 78   GLN A CD  1 
ATOM   516  O OE1 . GLN A 1 78  ? -5.817  21.265  33.715  1.00 55.47 ? 78   GLN A OE1 1 
ATOM   517  N NE2 . GLN A 1 78  ? -6.617  22.182  31.834  1.00 58.04 ? 78   GLN A NE2 1 
ATOM   518  N N   . THR A 1 79  ? -1.906  24.370  36.021  1.00 34.18 ? 79   THR A N   1 
ATOM   519  C CA  . THR A 1 79  ? -1.043  24.179  37.210  1.00 33.00 ? 79   THR A CA  1 
ATOM   520  C C   . THR A 1 79  ? -0.419  25.526  37.581  1.00 32.14 ? 79   THR A C   1 
ATOM   521  O O   . THR A 1 79  ? -0.290  25.799  38.789  1.00 29.53 ? 79   THR A O   1 
ATOM   522  C CB  . THR A 1 79  ? -0.055  23.027  36.981  1.00 31.88 ? 79   THR A CB  1 
ATOM   523  O OG1 . THR A 1 79  ? -0.829  21.863  36.692  1.00 29.70 ? 79   THR A OG1 1 
ATOM   524  C CG2 . THR A 1 79  ? 0.831   22.749  38.177  1.00 32.51 ? 79   THR A CG2 1 
ATOM   525  N N   . LEU A 1 80  ? -0.080  26.353  36.593  1.00 33.58 ? 80   LEU A N   1 
ATOM   526  C CA  . LEU A 1 80  ? 0.637   27.629  36.847  1.00 34.57 ? 80   LEU A CA  1 
ATOM   527  C C   . LEU A 1 80  ? -0.351  28.748  37.186  1.00 35.30 ? 80   LEU A C   1 
ATOM   528  O O   . LEU A 1 80  ? 0.124   29.823  37.580  1.00 33.50 ? 80   LEU A O   1 
ATOM   529  C CB  . LEU A 1 80  ? 1.490   27.990  35.633  1.00 35.13 ? 80   LEU A CB  1 
ATOM   530  C CG  . LEU A 1 80  ? 2.759   27.159  35.461  1.00 34.66 ? 80   LEU A CG  1 
ATOM   531  C CD1 . LEU A 1 80  ? 3.599   27.742  34.347  1.00 35.03 ? 80   LEU A CD1 1 
ATOM   532  C CD2 . LEU A 1 80  ? 3.566   27.067  36.752  1.00 34.88 ? 80   LEU A CD2 1 
ATOM   533  N N   . ASP A 1 81  ? -1.656  28.476  37.094  1.00 38.98 ? 81   ASP A N   1 
ATOM   534  C CA  . ASP A 1 81  ? -2.764  29.464  37.154  1.00 39.35 ? 81   ASP A CA  1 
ATOM   535  C C   . ASP A 1 81  ? -2.578  30.392  38.357  1.00 42.43 ? 81   ASP A C   1 
ATOM   536  O O   . ASP A 1 81  ? -2.556  31.613  38.152  1.00 40.82 ? 81   ASP A O   1 
ATOM   537  C CB  . ASP A 1 81  ? -4.118  28.760  37.242  1.00 44.50 ? 81   ASP A CB  1 
ATOM   538  C CG  . ASP A 1 81  ? -5.284  29.720  37.131  1.00 47.09 ? 81   ASP A CG  1 
ATOM   539  O OD1 . ASP A 1 81  ? -5.316  30.473  36.133  1.00 45.36 ? 81   ASP A OD1 1 
ATOM   540  O OD2 . ASP A 1 81  ? -6.136  29.718  38.046  1.00 52.80 ? 81   ASP A OD2 1 
ATOM   541  N N   . GLU A 1 82  ? -2.398  29.825  39.555  1.00 44.45 ? 82   GLU A N   1 
ATOM   542  C CA  . GLU A 1 82  ? -2.315  30.586  40.830  1.00 44.88 ? 82   GLU A CA  1 
ATOM   543  C C   . GLU A 1 82  ? -0.860  30.789  41.257  1.00 44.05 ? 82   GLU A C   1 
ATOM   544  O O   . GLU A 1 82  ? -0.644  31.295  42.360  1.00 44.32 ? 82   GLU A O   1 
ATOM   545  C CB  . GLU A 1 82  ? -3.083  29.853  41.924  1.00 48.28 ? 82   GLU A CB  1 
ATOM   546  C CG  . GLU A 1 82  ? -4.514  29.553  41.535  1.00 47.71 ? 82   GLU A CG  1 
ATOM   547  C CD  . GLU A 1 82  ? -5.441  29.272  42.699  1.00 47.32 ? 82   GLU A CD  1 
ATOM   548  O OE1 . GLU A 1 82  ? -6.577  28.870  42.441  1.00 54.47 ? 82   GLU A OE1 1 
ATOM   549  O OE2 . GLU A 1 82  ? -5.029  29.466  43.853  1.00 51.30 ? 82   GLU A OE2 1 
ATOM   550  N N   . VAL A 1 83  ? 0.108   30.378  40.444  1.00 44.06 ? 83   VAL A N   1 
ATOM   551  C CA  . VAL A 1 83  ? 1.542   30.658  40.718  1.00 42.65 ? 83   VAL A CA  1 
ATOM   552  C C   . VAL A 1 83  ? 1.777   32.110  40.297  1.00 45.36 ? 83   VAL A C   1 
ATOM   553  O O   . VAL A 1 83  ? 2.013   32.346  39.113  1.00 46.14 ? 83   VAL A O   1 
ATOM   554  C CB  . VAL A 1 83  ? 2.473   29.684  39.985  1.00 43.26 ? 83   VAL A CB  1 
ATOM   555  C CG1 . VAL A 1 83  ? 3.936   30.011  40.268  1.00 41.75 ? 83   VAL A CG1 1 
ATOM   556  C CG2 . VAL A 1 83  ? 2.148   28.237  40.339  1.00 43.66 ? 83   VAL A CG2 1 
ATOM   557  N N   . ILE A 1 84  ? 1.719   33.035  41.249  1.00 49.55 ? 84   ILE A N   1 
ATOM   558  C CA  . ILE A 1 84  ? 1.575   34.498  40.990  1.00 52.62 ? 84   ILE A CA  1 
ATOM   559  C C   . ILE A 1 84  ? 2.966   35.150  40.854  1.00 52.17 ? 84   ILE A C   1 
ATOM   560  O O   . ILE A 1 84  ? 3.099   36.130  40.068  1.00 50.48 ? 84   ILE A O   1 
ATOM   561  C CB  . ILE A 1 84  ? 0.687   35.102  42.104  1.00 57.40 ? 84   ILE A CB  1 
ATOM   562  C CG1 . ILE A 1 84  ? -0.452  35.939  41.518  1.00 61.95 ? 84   ILE A CG1 1 
ATOM   563  C CG2 . ILE A 1 84  ? 1.491   35.864  43.153  1.00 57.35 ? 84   ILE A CG2 1 
ATOM   564  C CD1 . ILE A 1 84  ? -1.527  35.112  40.833  1.00 63.84 ? 84   ILE A CD1 1 
ATOM   565  N N   . ASP A 1 85  ? 3.974   34.610  41.550  1.00 48.67 ? 85   ASP A N   1 
ATOM   566  C CA  . ASP A 1 85  ? 5.288   35.274  41.768  1.00 49.01 ? 85   ASP A CA  1 
ATOM   567  C C   . ASP A 1 85  ? 6.422   34.335  41.354  1.00 46.95 ? 85   ASP A C   1 
ATOM   568  O O   . ASP A 1 85  ? 6.635   33.325  42.050  1.00 40.84 ? 85   ASP A O   1 
ATOM   569  C CB  . ASP A 1 85  ? 5.443   35.669  43.239  1.00 51.23 ? 85   ASP A CB  1 
ATOM   570  C CG  . ASP A 1 85  ? 6.752   36.369  43.554  1.00 52.75 ? 85   ASP A CG  1 
ATOM   571  O OD1 . ASP A 1 85  ? 7.328   36.966  42.625  1.00 58.38 ? 85   ASP A OD1 1 
ATOM   572  O OD2 . ASP A 1 85  ? 7.188   36.304  44.728  1.00 54.99 ? 85   ASP A OD2 1 
ATOM   573  N N   . LEU A 1 86  ? 7.126   34.659  40.266  1.00 46.89 ? 86   LEU A N   1 
ATOM   574  C CA  . LEU A 1 86  ? 8.265   33.845  39.764  1.00 45.69 ? 86   LEU A CA  1 
ATOM   575  C C   . LEU A 1 86  ? 9.561   34.666  39.767  1.00 44.66 ? 86   LEU A C   1 
ATOM   576  O O   . LEU A 1 86  ? 10.514  34.235  39.106  1.00 41.25 ? 86   LEU A O   1 
ATOM   577  C CB  . LEU A 1 86  ? 7.930   33.310  38.367  1.00 45.82 ? 86   LEU A CB  1 
ATOM   578  C CG  . LEU A 1 86  ? 6.785   32.297  38.313  1.00 46.02 ? 86   LEU A CG  1 
ATOM   579  C CD1 . LEU A 1 86  ? 6.585   31.749  36.913  1.00 48.24 ? 86   LEU A CD1 1 
ATOM   580  C CD2 . LEU A 1 86  ? 7.031   31.156  39.278  1.00 47.13 ? 86   LEU A CD2 1 
ATOM   581  N N   . SER A 1 87  ? 9.634   35.758  40.539  1.00 44.94 ? 87   SER A N   1 
ATOM   582  C CA  . SER A 1 87  ? 10.845  36.620  40.616  1.00 46.38 ? 87   SER A CA  1 
ATOM   583  C C   . SER A 1 87  ? 12.048  35.743  40.947  1.00 43.75 ? 87   SER A C   1 
ATOM   584  O O   . SER A 1 87  ? 11.906  34.903  41.839  1.00 47.33 ? 87   SER A O   1 
ATOM   585  C CB  . SER A 1 87  ? 10.697  37.717  41.630  1.00 46.41 ? 87   SER A CB  1 
ATOM   586  O OG  . SER A 1 87  ? 9.382   38.244  41.590  1.00 54.58 ? 87   SER A OG  1 
ATOM   587  N N   . GLY A 1 88  ? 13.164  35.931  40.234  1.00 42.46 ? 88   GLY A N   1 
ATOM   588  C CA  . GLY A 1 88  ? 14.454  35.264  40.506  1.00 43.25 ? 88   GLY A CA  1 
ATOM   589  C C   . GLY A 1 88  ? 14.430  33.767  40.220  1.00 43.39 ? 88   GLY A C   1 
ATOM   590  O O   . GLY A 1 88  ? 15.391  33.090  40.631  1.00 45.99 ? 88   GLY A O   1 
ATOM   591  N N   . LYS A 1 89  ? 13.390  33.263  39.545  1.00 38.36 ? 89   LYS A N   1 
ATOM   592  C CA  . LYS A 1 89  ? 13.245  31.826  39.184  1.00 39.98 ? 89   LYS A CA  1 
ATOM   593  C C   . LYS A 1 89  ? 13.604  31.602  37.713  1.00 35.97 ? 89   LYS A C   1 
ATOM   594  O O   . LYS A 1 89  ? 13.148  32.376  36.845  1.00 33.01 ? 89   LYS A O   1 
ATOM   595  C CB  . LYS A 1 89  ? 11.806  31.325  39.360  1.00 40.85 ? 89   LYS A CB  1 
ATOM   596  C CG  . LYS A 1 89  ? 11.065  31.801  40.600  1.00 41.53 ? 89   LYS A CG  1 
ATOM   597  C CD  . LYS A 1 89  ? 11.247  30.914  41.784  1.00 42.27 ? 89   LYS A CD  1 
ATOM   598  C CE  . LYS A 1 89  ? 10.509  31.402  43.010  1.00 40.60 ? 89   LYS A CE  1 
ATOM   599  N NZ  . LYS A 1 89  ? 11.204  30.932  44.231  1.00 40.47 ? 89   LYS A NZ  1 
ATOM   600  N N   . THR A 1 90  ? 14.336  30.524  37.446  1.00 38.91 ? 90   THR A N   1 
ATOM   601  C CA  . THR A 1 90  ? 14.507  29.920  36.101  1.00 35.21 ? 90   THR A CA  1 
ATOM   602  C C   . THR A 1 90  ? 13.547  28.734  35.999  1.00 32.70 ? 90   THR A C   1 
ATOM   603  O O   . THR A 1 90  ? 13.559  27.855  36.896  1.00 30.30 ? 90   THR A O   1 
ATOM   604  C CB  . THR A 1 90  ? 15.965  29.521  35.845  1.00 38.30 ? 90   THR A CB  1 
ATOM   605  O OG1 . THR A 1 90  ? 16.762  30.671  36.114  1.00 35.98 ? 90   THR A OG1 1 
ATOM   606  C CG2 . THR A 1 90  ? 16.210  29.028  34.434  1.00 40.84 ? 90   THR A CG2 1 
ATOM   607  N N   . ILE A 1 91  ? 12.720  28.753  34.963  1.00 30.05 ? 91   ILE A N   1 
ATOM   608  C CA  . ILE A 1 91  ? 11.788  27.654  34.595  1.00 30.03 ? 91   ILE A CA  1 
ATOM   609  C C   . ILE A 1 91  ? 12.497  26.778  33.564  1.00 27.60 ? 91   ILE A C   1 
ATOM   610  O O   . ILE A 1 91  ? 12.976  27.312  32.536  1.00 27.27 ? 91   ILE A O   1 
ATOM   611  C CB  . ILE A 1 91  ? 10.466  28.211  34.035  1.00 29.98 ? 91   ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 91  ? 9.903   29.358  34.878  1.00 30.19 ? 91   ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 91  ? 9.469   27.088  33.828  1.00 30.17 ? 91   ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 91  ? 9.592   29.005  36.302  1.00 32.08 ? 91   ILE A CD1 1 
ATOM   615  N N   . ILE A 1 92  ? 12.541  25.479  33.824  1.00 27.10 ? 92   ILE A N   1 
ATOM   616  C CA  . ILE A 1 92  ? 13.012  24.444  32.869  1.00 26.58 ? 92   ILE A CA  1 
ATOM   617  C C   . ILE A 1 92  ? 11.805  23.583  32.530  1.00 26.28 ? 92   ILE A C   1 
ATOM   618  O O   . ILE A 1 92  ? 11.399  22.748  33.377  1.00 26.95 ? 92   ILE A O   1 
ATOM   619  C CB  . ILE A 1 92  ? 14.168  23.642  33.485  1.00 27.89 ? 92   ILE A CB  1 
ATOM   620  C CG1 . ILE A 1 92  ? 15.221  24.592  34.056  1.00 28.43 ? 92   ILE A CG1 1 
ATOM   621  C CG2 . ILE A 1 92  ? 14.750  22.667  32.475  1.00 27.90 ? 92   ILE A CG2 1 
ATOM   622  C CD1 . ILE A 1 92  ? 16.405  23.903  34.675  1.00 28.86 ? 92   ILE A CD1 1 
ATOM   623  N N   . ASN A 1 93  ? 11.226  23.800  31.356  1.00 24.30 ? 93   ASN A N   1 
ATOM   624  C CA  . ASN A 1 93  ? 9.967   23.126  30.968  1.00 23.46 ? 93   ASN A CA  1 
ATOM   625  C C   . ASN A 1 93  ? 10.269  21.885  30.138  1.00 23.06 ? 93   ASN A C   1 
ATOM   626  O O   . ASN A 1 93  ? 10.690  22.068  29.011  1.00 22.01 ? 93   ASN A O   1 
ATOM   627  C CB  . ASN A 1 93  ? 9.043   24.055  30.195  1.00 25.23 ? 93   ASN A CB  1 
ATOM   628  C CG  . ASN A 1 93  ? 7.624   23.531  30.192  1.00 23.90 ? 93   ASN A CG  1 
ATOM   629  O OD1 . ASN A 1 93  ? 7.364   22.473  30.756  1.00 26.37 ? 93   ASN A OD1 1 
ATOM   630  N ND2 . ASN A 1 93  ? 6.708   24.261  29.588  1.00 24.77 ? 93   ASN A ND2 1 
ATOM   631  N N   . LEU A 1 94  ? 10.005  20.681  30.664  1.00 24.03 ? 94   LEU A N   1 
ATOM   632  C CA  . LEU A 1 94  ? 10.300  19.400  29.962  1.00 23.78 ? 94   LEU A CA  1 
ATOM   633  C C   . LEU A 1 94  ? 8.977   18.758  29.536  1.00 24.22 ? 94   LEU A C   1 
ATOM   634  O O   . LEU A 1 94  ? 8.942   17.544  29.315  1.00 25.20 ? 94   LEU A O   1 
ATOM   635  C CB  . LEU A 1 94  ? 11.127  18.478  30.865  1.00 23.29 ? 94   LEU A CB  1 
ATOM   636  C CG  . LEU A 1 94  ? 12.461  19.035  31.373  1.00 23.32 ? 94   LEU A CG  1 
ATOM   637  C CD1 . LEU A 1 94  ? 13.257  17.971  32.123  1.00 25.01 ? 94   LEU A CD1 1 
ATOM   638  C CD2 . LEU A 1 94  ? 13.315  19.628  30.265  1.00 22.13 ? 94   LEU A CD2 1 
ATOM   639  N N   . THR A 1 95  ? 7.925   19.567  29.400  1.00 23.62 ? 95   THR A N   1 
ATOM   640  C CA  . THR A 1 95  ? 6.567   19.122  28.974  1.00 22.58 ? 95   THR A CA  1 
ATOM   641  C C   . THR A 1 95  ? 6.467   19.176  27.448  1.00 20.97 ? 95   THR A C   1 
ATOM   642  O O   . THR A 1 95  ? 6.610   20.258  26.897  1.00 22.13 ? 95   THR A O   1 
ATOM   643  C CB  . THR A 1 95  ? 5.478   19.992  29.606  1.00 22.37 ? 95   THR A CB  1 
ATOM   644  O OG1 . THR A 1 95  ? 5.626   19.859  31.020  1.00 23.57 ? 95   THR A OG1 1 
ATOM   645  C CG2 . THR A 1 95  ? 4.086   19.625  29.148  1.00 22.66 ? 95   THR A CG2 1 
ATOM   646  N N   . ASN A 1 96  ? 6.188   18.046  26.811  1.00 22.59 ? 96   ASN A N   1 
ATOM   647  C CA  . ASN A 1 96  ? 5.906   17.941  25.357  1.00 21.43 ? 96   ASN A CA  1 
ATOM   648  C C   . ASN A 1 96  ? 4.803   18.933  24.992  1.00 21.47 ? 96   ASN A C   1 
ATOM   649  O O   . ASN A 1 96  ? 3.745   18.989  25.687  1.00 20.95 ? 96   ASN A O   1 
ATOM   650  C CB  . ASN A 1 96  ? 5.447   16.551  24.925  1.00 21.94 ? 96   ASN A CB  1 
ATOM   651  C CG  . ASN A 1 96  ? 4.885   16.544  23.514  1.00 22.81 ? 96   ASN A CG  1 
ATOM   652  O OD1 . ASN A 1 96  ? 5.645   16.564  22.536  1.00 23.27 ? 96   ASN A OD1 1 
ATOM   653  N ND2 . ASN A 1 96  ? 3.569   16.497  23.393  1.00 17.85 ? 96   ASN A ND2 1 
ATOM   654  N N   . GLY A 1 97  ? 5.034   19.674  23.920  1.00 21.43 ? 97   GLY A N   1 
ATOM   655  C CA  . GLY A 1 97  ? 4.041   20.612  23.362  1.00 21.04 ? 97   GLY A CA  1 
ATOM   656  C C   . GLY A 1 97  ? 4.504   21.144  22.030  1.00 20.68 ? 97   GLY A C   1 
ATOM   657  O O   . GLY A 1 97  ? 5.550   20.712  21.551  1.00 21.16 ? 97   GLY A O   1 
ATOM   658  N N   . THR A 1 98  ? 3.716   22.027  21.439  1.00 22.44 ? 98   THR A N   1 
ATOM   659  C CA  . THR A 1 98  ? 3.977   22.638  20.124  1.00 23.22 ? 98   THR A CA  1 
ATOM   660  C C   . THR A 1 98  ? 4.899   23.821  20.346  1.00 24.65 ? 98   THR A C   1 
ATOM   661  O O   . THR A 1 98  ? 4.996   24.298  21.473  1.00 23.52 ? 98   THR A O   1 
ATOM   662  C CB  . THR A 1 98  ? 2.697   23.170  19.501  1.00 24.82 ? 98   THR A CB  1 
ATOM   663  O OG1 . THR A 1 98  ? 2.514   24.455  20.089  1.00 23.27 ? 98   THR A OG1 1 
ATOM   664  C CG2 . THR A 1 98  ? 1.508   22.281  19.769  1.00 25.24 ? 98   THR A CG2 1 
ATOM   665  N N   . PRO A 1 99  ? 5.608   24.299  19.298  1.00 25.22 ? 99   PRO A N   1 
ATOM   666  C CA  . PRO A 1 99  ? 6.421   25.507  19.403  1.00 24.85 ? 99   PRO A CA  1 
ATOM   667  C C   . PRO A 1 99  ? 5.664   26.683  20.025  1.00 25.15 ? 99   PRO A C   1 
ATOM   668  O O   . PRO A 1 99  ? 6.173   27.253  20.941  1.00 26.15 ? 99   PRO A O   1 
ATOM   669  C CB  . PRO A 1 99  ? 6.850   25.752  17.951  1.00 26.33 ? 99   PRO A CB  1 
ATOM   670  C CG  . PRO A 1 99  ? 6.957   24.337  17.398  1.00 25.95 ? 99   PRO A CG  1 
ATOM   671  C CD  . PRO A 1 99  ? 5.734   23.653  17.977  1.00 25.92 ? 99   PRO A CD  1 
ATOM   672  N N   . GLN A 1 100 ? 4.445   26.984  19.598  1.00 27.07 ? 100  GLN A N   1 
ATOM   673  C CA  . GLN A 1 100 ? 3.747   28.159  20.186  1.00 28.15 ? 100  GLN A CA  1 
ATOM   674  C C   . GLN A 1 100 ? 3.416   27.905  21.669  1.00 28.21 ? 100  GLN A C   1 
ATOM   675  O O   . GLN A 1 100 ? 3.372   28.880  22.447  1.00 26.54 ? 100  GLN A O   1 
ATOM   676  C CB  . GLN A 1 100 ? 2.486   28.522  19.403  1.00 29.41 ? 100  GLN A CB  1 
ATOM   677  C CG  . GLN A 1 100 ? 1.935   29.899  19.764  1.00 30.72 ? 100  GLN A CG  1 
ATOM   678  C CD  . GLN A 1 100 ? 2.928   31.022  19.559  1.00 30.82 ? 100  GLN A CD  1 
ATOM   679  O OE1 . GLN A 1 100 ? 3.905   30.884  18.819  1.00 33.66 ? 100  GLN A OE1 1 
ATOM   680  N NE2 . GLN A 1 100 ? 2.697   32.145  20.236  1.00 31.65 ? 100  GLN A NE2 1 
ATOM   681  N N   . GLN A 1 101 ? 3.164   26.655  22.070  1.00 25.91 ? 101  GLN A N   1 
ATOM   682  C CA  . GLN A 1 101 ? 2.864   26.343  23.490  1.00 23.65 ? 101  GLN A CA  1 
ATOM   683  C C   . GLN A 1 101 ? 4.097   26.697  24.327  1.00 24.21 ? 101  GLN A C   1 
ATOM   684  O O   . GLN A 1 101 ? 3.903   27.214  25.417  1.00 24.74 ? 101  GLN A O   1 
ATOM   685  C CB  . GLN A 1 101 ? 2.422   24.889  23.630  1.00 24.11 ? 101  GLN A CB  1 
ATOM   686  C CG  . GLN A 1 101 ? 1.028   24.650  23.053  1.00 24.12 ? 101  GLN A CG  1 
ATOM   687  C CD  . GLN A 1 101 ? 0.617   23.202  23.107  1.00 25.08 ? 101  GLN A CD  1 
ATOM   688  O OE1 . GLN A 1 101 ? 1.454   22.314  23.358  1.00 21.43 ? 101  GLN A OE1 1 
ATOM   689  N NE2 . GLN A 1 101 ? -0.669  22.966  22.841  1.00 19.08 ? 101  GLN A NE2 1 
ATOM   690  N N   . ALA A 1 102 ? 5.312   26.447  23.833  1.00 24.20 ? 102  ALA A N   1 
ATOM   691  C CA  . ALA A 1 102 ? 6.555   26.841  24.529  1.00 24.52 ? 102  ALA A CA  1 
ATOM   692  C C   . ALA A 1 102 ? 6.542   28.364  24.679  1.00 25.55 ? 102  ALA A C   1 
ATOM   693  O O   . ALA A 1 102 ? 6.796   28.838  25.794  1.00 25.82 ? 102  ALA A O   1 
ATOM   694  C CB  . ALA A 1 102 ? 7.780   26.382  23.793  1.00 24.57 ? 102  ALA A CB  1 
ATOM   695  N N   . VAL A 1 103 ? 6.223   29.093  23.608  1.00 25.31 ? 103  VAL A N   1 
ATOM   696  C CA  . VAL A 1 103 ? 6.216   30.588  23.603  1.00 27.82 ? 103  VAL A CA  1 
ATOM   697  C C   . VAL A 1 103 ? 5.168   31.076  24.611  1.00 28.32 ? 103  VAL A C   1 
ATOM   698  O O   . VAL A 1 103 ? 5.481   31.998  25.417  1.00 28.48 ? 103  VAL A O   1 
ATOM   699  C CB  . VAL A 1 103 ? 5.959   31.145  22.189  1.00 30.61 ? 103  VAL A CB  1 
ATOM   700  C CG1 . VAL A 1 103 ? 5.809   32.663  22.196  1.00 31.60 ? 103  VAL A CG1 1 
ATOM   701  C CG2 . VAL A 1 103 ? 7.059   30.719  21.230  1.00 31.83 ? 103  VAL A CG2 1 
ATOM   702  N N   . LYS A 1 104 ? 3.992   30.445  24.612  1.00 27.60 ? 104  LYS A N   1 
ATOM   703  C CA  . LYS A 1 104 ? 2.873   30.763  25.550  1.00 27.17 ? 104  LYS A CA  1 
ATOM   704  C C   . LYS A 1 104 ? 3.315   30.577  27.010  1.00 28.39 ? 104  LYS A C   1 
ATOM   705  O O   . LYS A 1 104 ? 2.992   31.493  27.818  1.00 26.82 ? 104  LYS A O   1 
ATOM   706  C CB  . LYS A 1 104 ? 1.619   29.958  25.191  1.00 26.24 ? 104  LYS A CB  1 
ATOM   707  C CG  . LYS A 1 104 ? 0.830   30.558  24.034  1.00 26.86 ? 104  LYS A CG  1 
ATOM   708  C CD  . LYS A 1 104 ? 0.202   29.601  23.053  1.00 29.46 ? 104  LYS A CD  1 
ATOM   709  C CE  . LYS A 1 104 ? -0.699  28.561  23.660  1.00 32.02 ? 104  LYS A CE  1 
ATOM   710  N NZ  . LYS A 1 104 ? -1.728  28.105  22.692  1.00 34.42 ? 104  LYS A NZ  1 
ATOM   711  N N   . VAL A 1 105 ? 4.025   29.487  27.365  1.00 27.60 ? 105  VAL A N   1 
ATOM   712  C CA  . VAL A 1 105 ? 4.465   29.264  28.779  1.00 27.59 ? 105  VAL A CA  1 
ATOM   713  C C   . VAL A 1 105 ? 5.588   30.253  29.093  1.00 27.92 ? 105  VAL A C   1 
ATOM   714  O O   . VAL A 1 105 ? 5.589   30.806  30.197  1.00 28.78 ? 105  VAL A O   1 
ATOM   715  C CB  . VAL A 1 105 ? 4.902   27.830  29.125  1.00 25.36 ? 105  VAL A CB  1 
ATOM   716  C CG1 . VAL A 1 105 ? 5.106   27.689  30.626  1.00 24.28 ? 105  VAL A CG1 1 
ATOM   717  C CG2 . VAL A 1 105 ? 3.924   26.785  28.625  1.00 26.03 ? 105  VAL A CG2 1 
ATOM   718  N N   . ALA A 1 106 ? 6.499   30.482  28.159  1.00 30.08 ? 106  ALA A N   1 
ATOM   719  C CA  . ALA A 1 106 ? 7.589   31.471  28.335  1.00 32.28 ? 106  ALA A CA  1 
ATOM   720  C C   . ALA A 1 106 ? 6.956   32.819  28.697  1.00 33.99 ? 106  ALA A C   1 
ATOM   721  O O   . ALA A 1 106 ? 7.473   33.499  29.618  1.00 32.84 ? 106  ALA A O   1 
ATOM   722  C CB  . ALA A 1 106 ? 8.455   31.551  27.100  1.00 30.29 ? 106  ALA A CB  1 
ATOM   723  N N   . THR A 1 107 ? 5.848   33.156  28.032  1.00 34.94 ? 107  THR A N   1 
ATOM   724  C CA  . THR A 1 107 ? 5.135   34.447  28.210  1.00 37.99 ? 107  THR A CA  1 
ATOM   725  C C   . THR A 1 107 ? 4.428   34.456  29.565  1.00 36.54 ? 107  THR A C   1 
ATOM   726  O O   . THR A 1 107 ? 4.531   35.467  30.270  1.00 34.70 ? 107  THR A O   1 
ATOM   727  C CB  . THR A 1 107 ? 4.161   34.710  27.059  1.00 36.13 ? 107  THR A CB  1 
ATOM   728  O OG1 . THR A 1 107 ? 4.987   34.907  25.919  1.00 35.43 ? 107  THR A OG1 1 
ATOM   729  C CG2 . THR A 1 107 ? 3.279   35.917  27.274  1.00 37.56 ? 107  THR A CG2 1 
ATOM   730  N N   . LEU A 1 108 ? 3.718   33.376  29.894  1.00 38.18 ? 108  LEU A N   1 
ATOM   731  C CA  . LEU A 1 108 ? 3.018   33.236  31.198  1.00 38.61 ? 108  LEU A CA  1 
ATOM   732  C C   . LEU A 1 108 ? 4.044   33.487  32.309  1.00 37.27 ? 108  LEU A C   1 
ATOM   733  O O   . LEU A 1 108 ? 3.763   34.374  33.114  1.00 39.66 ? 108  LEU A O   1 
ATOM   734  C CB  . LEU A 1 108 ? 2.354   31.856  31.305  1.00 44.44 ? 108  LEU A CB  1 
ATOM   735  C CG  . LEU A 1 108 ? 1.004   31.812  32.018  1.00 48.86 ? 108  LEU A CG  1 
ATOM   736  C CD1 . LEU A 1 108 ? 1.084   32.519  33.354  1.00 52.23 ? 108  LEU A CD1 1 
ATOM   737  C CD2 . LEU A 1 108 ? -0.111  32.421  31.172  1.00 49.40 ? 108  LEU A CD2 1 
ATOM   738  N N   . VAL A 1 109 ? 5.208   32.813  32.310  1.00 33.21 ? 109  VAL A N   1 
ATOM   739  C CA  . VAL A 1 109 ? 6.206   32.897  33.428  1.00 33.88 ? 109  VAL A CA  1 
ATOM   740  C C   . VAL A 1 109 ? 6.922   34.259  33.400  1.00 36.61 ? 109  VAL A C   1 
ATOM   741  O O   . VAL A 1 109 ? 7.295   34.739  34.487  1.00 36.35 ? 109  VAL A O   1 
ATOM   742  C CB  . VAL A 1 109 ? 7.220   31.726  33.458  1.00 28.68 ? 109  VAL A CB  1 
ATOM   743  C CG1 . VAL A 1 109 ? 6.546   30.371  33.599  1.00 29.02 ? 109  VAL A CG1 1 
ATOM   744  C CG2 . VAL A 1 109 ? 8.146   31.708  32.270  1.00 29.11 ? 109  VAL A CG2 1 
ATOM   745  N N   . GLN A 1 110 ? 7.148   34.858  32.226  1.00 41.38 ? 110  GLN A N   1 
ATOM   746  C CA  . GLN A 1 110 ? 7.810   36.196  32.120  1.00 44.39 ? 110  GLN A CA  1 
ATOM   747  C C   . GLN A 1 110 ? 6.910   37.243  32.792  1.00 42.38 ? 110  GLN A C   1 
ATOM   748  O O   . GLN A 1 110 ? 7.394   37.937  33.669  1.00 44.27 ? 110  GLN A O   1 
ATOM   749  C CB  . GLN A 1 110 ? 8.130   36.546  30.663  1.00 48.10 ? 110  GLN A CB  1 
ATOM   750  C CG  . GLN A 1 110 ? 8.660   37.964  30.460  1.00 52.03 ? 110  GLN A CG  1 
ATOM   751  C CD  . GLN A 1 110 ? 7.548   38.967  30.244  1.00 54.82 ? 110  GLN A CD  1 
ATOM   752  O OE1 . GLN A 1 110 ? 6.812   38.901  29.263  1.00 64.58 ? 110  GLN A OE1 1 
ATOM   753  N NE2 . GLN A 1 110 ? 7.412   39.908  31.164  1.00 52.91 ? 110  GLN A NE2 1 
ATOM   754  N N   . GLN A 1 111 ? 5.628   37.294  32.430  1.00 42.67 ? 111  GLN A N   1 
ATOM   755  C CA  . GLN A 1 111 ? 4.605   38.215  32.999  1.00 45.69 ? 111  GLN A CA  1 
ATOM   756  C C   . GLN A 1 111 ? 4.505   38.081  34.523  1.00 47.93 ? 111  GLN A C   1 
ATOM   757  O O   . GLN A 1 111 ? 3.869   38.958  35.137  1.00 48.32 ? 111  GLN A O   1 
ATOM   758  C CB  . GLN A 1 111 ? 3.224   37.904  32.429  1.00 46.50 ? 111  GLN A CB  1 
ATOM   759  C CG  . GLN A 1 111 ? 3.102   38.269  30.964  1.00 47.07 ? 111  GLN A CG  1 
ATOM   760  C CD  . GLN A 1 111 ? 1.883   37.663  30.322  1.00 48.28 ? 111  GLN A CD  1 
ATOM   761  O OE1 . GLN A 1 111 ? 1.296   36.706  30.825  1.00 50.10 ? 111  GLN A OE1 1 
ATOM   762  N NE2 . GLN A 1 111 ? 1.503   38.223  29.184  1.00 49.43 ? 111  GLN A NE2 1 
ATOM   763  N N   . ARG A 1 112 ? 5.056   37.008  35.098  1.00 44.53 ? 112  ARG A N   1 
ATOM   764  C CA  . ARG A 1 112 ? 4.970   36.716  36.548  1.00 40.38 ? 112  ARG A CA  1 
ATOM   765  C C   . ARG A 1 112 ? 6.351   36.882  37.185  1.00 37.42 ? 112  ARG A C   1 
ATOM   766  O O   . ARG A 1 112 ? 6.489   36.529  38.357  1.00 36.97 ? 112  ARG A O   1 
ATOM   767  C CB  . ARG A 1 112 ? 4.320   35.343  36.731  1.00 39.22 ? 112  ARG A CB  1 
ATOM   768  C CG  . ARG A 1 112 ? 2.891   35.340  36.200  1.00 40.20 ? 112  ARG A CG  1 
ATOM   769  C CD  . ARG A 1 112 ? 2.165   34.032  36.357  1.00 40.99 ? 112  ARG A CD  1 
ATOM   770  N NE  . ARG A 1 112 ? 0.807   34.128  35.840  1.00 40.83 ? 112  ARG A NE  1 
ATOM   771  C CZ  . ARG A 1 112 ? -0.190  33.317  36.171  1.00 44.24 ? 112  ARG A CZ  1 
ATOM   772  N NH1 . ARG A 1 112 ? 0.014   32.324  37.020  1.00 50.49 ? 112  ARG A NH1 1 
ATOM   773  N NH2 . ARG A 1 112 ? -1.395  33.489  35.655  1.00 44.72 ? 112  ARG A NH2 1 
ATOM   774  N N   . GLY A 1 113 ? 7.316   37.442  36.452  1.00 36.12 ? 113  GLY A N   1 
ATOM   775  C CA  . GLY A 1 113 ? 8.604   37.896  37.005  1.00 36.14 ? 113  GLY A CA  1 
ATOM   776  C C   . GLY A 1 113 ? 9.714   36.872  36.861  1.00 35.58 ? 113  GLY A C   1 
ATOM   777  O O   . GLY A 1 113 ? 10.802  37.104  37.412  1.00 41.93 ? 113  GLY A O   1 
ATOM   778  N N   . ALA A 1 114 ? 9.492   35.773  36.145  1.00 34.27 ? 114  ALA A N   1 
ATOM   779  C CA  . ALA A 1 114 ? 10.514  34.716  35.971  1.00 31.51 ? 114  ALA A CA  1 
ATOM   780  C C   . ALA A 1 114 ? 11.742  35.361  35.345  1.00 33.22 ? 114  ALA A C   1 
ATOM   781  O O   . ALA A 1 114 ? 11.551  36.160  34.408  1.00 30.05 ? 114  ALA A O   1 
ATOM   782  C CB  . ALA A 1 114 ? 10.003  33.587  35.115  1.00 33.08 ? 114  ALA A CB  1 
ATOM   783  N N   . GLU A 1 115 ? 12.926  35.032  35.864  1.00 34.85 ? 115  GLU A N   1 
ATOM   784  C CA  . GLU A 1 115 ? 14.235  35.482  35.337  1.00 38.75 ? 115  GLU A CA  1 
ATOM   785  C C   . GLU A 1 115 ? 14.450  34.887  33.940  1.00 36.77 ? 115  GLU A C   1 
ATOM   786  O O   . GLU A 1 115 ? 14.919  35.625  33.077  1.00 34.69 ? 115  GLU A O   1 
ATOM   787  C CB  . GLU A 1 115 ? 15.379  35.074  36.274  1.00 44.53 ? 115  GLU A CB  1 
ATOM   788  C CG  . GLU A 1 115 ? 16.388  36.189  36.531  1.00 51.94 ? 115  GLU A CG  1 
ATOM   789  C CD  . GLU A 1 115 ? 15.740  37.485  37.002  1.00 56.16 ? 115  GLU A CD  1 
ATOM   790  O OE1 . GLU A 1 115 ? 14.957  37.439  37.982  1.00 62.10 ? 115  GLU A OE1 1 
ATOM   791  O OE2 . GLU A 1 115 ? 15.968  38.527  36.356  1.00 58.50 ? 115  GLU A OE2 1 
ATOM   792  N N   . SER A 1 116 ? 14.167  33.592  33.732  1.00 34.59 ? 116  SER A N   1 
ATOM   793  C CA  . SER A 1 116 ? 14.309  32.942  32.404  1.00 32.71 ? 116  SER A CA  1 
ATOM   794  C C   . SER A 1 116 ? 13.509  31.641  32.266  1.00 31.47 ? 116  SER A C   1 
ATOM   795  O O   . SER A 1 116 ? 13.070  31.052  33.270  1.00 31.54 ? 116  SER A O   1 
ATOM   796  C CB  . SER A 1 116 ? 15.738  32.684  32.111  1.00 34.36 ? 116  SER A CB  1 
ATOM   797  O OG  . SER A 1 116 ? 16.162  31.572  32.847  1.00 39.42 ? 116  SER A OG  1 
ATOM   798  N N   . TYR A 1 117 ? 13.372  31.220  31.014  1.00 29.87 ? 117  TYR A N   1 
ATOM   799  C CA  . TYR A 1 117 ? 12.679  30.001  30.541  1.00 28.39 ? 117  TYR A CA  1 
ATOM   800  C C   . TYR A 1 117 ? 13.606  29.297  29.556  1.00 28.12 ? 117  TYR A C   1 
ATOM   801  O O   . TYR A 1 117 ? 14.182  29.951  28.648  1.00 29.09 ? 117  TYR A O   1 
ATOM   802  C CB  . TYR A 1 117 ? 11.342  30.363  29.889  1.00 26.96 ? 117  TYR A CB  1 
ATOM   803  C CG  . TYR A 1 117 ? 10.506  29.203  29.416  1.00 25.69 ? 117  TYR A CG  1 
ATOM   804  C CD1 . TYR A 1 117 ? 10.732  28.622  28.187  1.00 26.29 ? 117  TYR A CD1 1 
ATOM   805  C CD2 . TYR A 1 117 ? 9.495   28.678  30.195  1.00 24.14 ? 117  TYR A CD2 1 
ATOM   806  C CE1 . TYR A 1 117 ? 9.968   27.557  27.736  1.00 26.63 ? 117  TYR A CE1 1 
ATOM   807  C CE2 . TYR A 1 117 ? 8.719   27.614  29.766  1.00 25.72 ? 117  TYR A CE2 1 
ATOM   808  C CZ  . TYR A 1 117 ? 8.948   27.057  28.522  1.00 25.74 ? 117  TYR A CZ  1 
ATOM   809  O OH  . TYR A 1 117 ? 8.169   26.036  28.058  1.00 23.24 ? 117  TYR A OH  1 
ATOM   810  N N   . ILE A 1 118 ? 13.805  28.003  29.761  1.00 28.02 ? 118  ILE A N   1 
ATOM   811  C CA  . ILE A 1 118 ? 14.398  27.113  28.730  1.00 26.20 ? 118  ILE A CA  1 
ATOM   812  C C   . ILE A 1 118 ? 13.429  25.943  28.579  1.00 28.13 ? 118  ILE A C   1 
ATOM   813  O O   . ILE A 1 118 ? 12.686  25.646  29.548  1.00 25.48 ? 118  ILE A O   1 
ATOM   814  C CB  . ILE A 1 118 ? 15.851  26.714  29.061  1.00 28.70 ? 118  ILE A CB  1 
ATOM   815  C CG1 . ILE A 1 118 ? 16.001  25.897  30.341  1.00 27.86 ? 118  ILE A CG1 1 
ATOM   816  C CG2 . ILE A 1 118 ? 16.736  27.955  29.101  1.00 30.73 ? 118  ILE A CG2 1 
ATOM   817  C CD1 . ILE A 1 118 ? 17.422  25.454  30.590  1.00 29.37 ? 118  ILE A CD1 1 
ATOM   818  N N   . HIS A 1 119 ? 13.361  25.378  27.377  1.00 25.25 ? 119  HIS A N   1 
ATOM   819  C CA  . HIS A 1 119 ? 12.451  24.255  27.076  1.00 25.63 ? 119  HIS A CA  1 
ATOM   820  C C   . HIS A 1 119 ? 13.330  23.066  26.742  1.00 25.07 ? 119  HIS A C   1 
ATOM   821  O O   . HIS A 1 119 ? 14.424  23.290  26.213  1.00 25.99 ? 119  HIS A O   1 
ATOM   822  C CB  . HIS A 1 119 ? 11.439  24.587  25.976  1.00 25.04 ? 119  HIS A CB  1 
ATOM   823  C CG  . HIS A 1 119 ? 10.270  23.674  26.045  1.00 22.36 ? 119  HIS A CG  1 
ATOM   824  N ND1 . HIS A 1 119 ? 9.077   24.052  26.612  1.00 22.75 ? 119  HIS A ND1 1 
ATOM   825  C CD2 . HIS A 1 119 ? 10.148  22.381  25.704  1.00 20.94 ? 119  HIS A CD2 1 
ATOM   826  C CE1 . HIS A 1 119 ? 8.244   23.037  26.569  1.00 24.08 ? 119  HIS A CE1 1 
ATOM   827  N NE2 . HIS A 1 119 ? 8.890   21.987  26.036  1.00 22.88 ? 119  HIS A NE2 1 
ATOM   828  N N   . GLY A 1 120 ? 12.900  21.888  27.174  1.00 23.68 ? 120  GLY A N   1 
ATOM   829  C CA  . GLY A 1 120 ? 13.614  20.622  26.963  1.00 23.38 ? 120  GLY A CA  1 
ATOM   830  C C   . GLY A 1 120 ? 12.656  19.565  26.474  1.00 23.18 ? 120  GLY A C   1 
ATOM   831  O O   . GLY A 1 120 ? 11.502  19.518  26.965  1.00 22.46 ? 120  GLY A O   1 
ATOM   832  N N   . ALA A 1 121 ? 13.105  18.792  25.494  1.00 22.41 ? 121  ALA A N   1 
ATOM   833  C CA  . ALA A 1 121 ? 12.478  17.554  25.005  1.00 21.77 ? 121  ALA A CA  1 
ATOM   834  C C   . ALA A 1 121 ? 13.409  16.389  25.355  1.00 23.04 ? 121  ALA A C   1 
ATOM   835  O O   . ALA A 1 121 ? 14.498  16.254  24.733  1.00 24.63 ? 121  ALA A O   1 
ATOM   836  C CB  . ALA A 1 121 ? 12.215  17.664  23.526  1.00 20.54 ? 121  ALA A CB  1 
ATOM   837  N N   . ILE A 1 122 ? 12.993  15.593  26.339  1.00 23.22 ? 122  ILE A N   1 
ATOM   838  C CA  . ILE A 1 122 ? 13.608  14.285  26.710  1.00 22.82 ? 122  ILE A CA  1 
ATOM   839  C C   . ILE A 1 122 ? 13.272  13.275  25.616  1.00 22.63 ? 122  ILE A C   1 
ATOM   840  O O   . ILE A 1 122 ? 12.067  13.077  25.327  1.00 23.53 ? 122  ILE A O   1 
ATOM   841  C CB  . ILE A 1 122 ? 13.105  13.849  28.087  1.00 22.55 ? 122  ILE A CB  1 
ATOM   842  C CG1 . ILE A 1 122 ? 13.490  14.874  29.155  1.00 23.25 ? 122  ILE A CG1 1 
ATOM   843  C CG2 . ILE A 1 122 ? 13.611  12.461  28.426  1.00 23.52 ? 122  ILE A CG2 1 
ATOM   844  C CD1 . ILE A 1 122 ? 12.651  14.787  30.403  1.00 22.98 ? 122  ILE A CD1 1 
ATOM   845  N N   . MET A 1 123 ? 14.289  12.726  24.949  1.00 24.63 ? 123  MET A N   1 
ATOM   846  C CA  . MET A 1 123 ? 14.083  11.863  23.754  1.00 26.74 ? 123  MET A CA  1 
ATOM   847  C C   . MET A 1 123 ? 14.210  10.373  24.121  1.00 26.27 ? 123  MET A C   1 
ATOM   848  O O   . MET A 1 123 ? 14.301  9.547   23.193  1.00 31.24 ? 123  MET A O   1 
ATOM   849  C CB  . MET A 1 123 ? 15.067  12.253  22.642  1.00 29.24 ? 123  MET A CB  1 
ATOM   850  C CG  . MET A 1 123 ? 14.912  13.706  22.148  1.00 30.36 ? 123  MET A CG  1 
ATOM   851  S SD  . MET A 1 123 ? 13.173  14.304  22.028  1.00 30.67 ? 123  MET A SD  1 
ATOM   852  C CE  . MET A 1 123 ? 12.488  13.196  20.799  1.00 31.39 ? 123  MET A CE  1 
ATOM   853  N N   . VAL A 1 124 ? 14.082  10.012  25.399  1.00 25.38 ? 124  VAL A N   1 
ATOM   854  C CA  . VAL A 1 124 ? 14.181  8.595   25.873  1.00 25.56 ? 124  VAL A CA  1 
ATOM   855  C C   . VAL A 1 124 ? 13.026  8.331   26.827  1.00 25.28 ? 124  VAL A C   1 
ATOM   856  O O   . VAL A 1 124 ? 12.486  9.266   27.423  1.00 23.81 ? 124  VAL A O   1 
ATOM   857  C CB  . VAL A 1 124 ? 15.548  8.306   26.534  1.00 27.21 ? 124  VAL A CB  1 
ATOM   858  C CG1 . VAL A 1 124 ? 16.689  8.363   25.522  1.00 27.79 ? 124  VAL A CG1 1 
ATOM   859  C CG2 . VAL A 1 124 ? 15.852  9.231   27.704  1.00 27.65 ? 124  VAL A CG2 1 
ATOM   860  N N   . PRO A 1 125 ? 12.610  7.055   26.984  1.00 24.85 ? 125  PRO A N   1 
ATOM   861  C CA  . PRO A 1 125 ? 11.733  6.665   28.083  1.00 25.82 ? 125  PRO A CA  1 
ATOM   862  C C   . PRO A 1 125 ? 12.382  6.803   29.461  1.00 24.77 ? 125  PRO A C   1 
ATOM   863  O O   . PRO A 1 125 ? 13.606  6.870   29.586  1.00 25.31 ? 125  PRO A O   1 
ATOM   864  C CB  . PRO A 1 125 ? 11.376  5.212   27.777  1.00 26.75 ? 125  PRO A CB  1 
ATOM   865  C CG  . PRO A 1 125 ? 12.563  4.730   26.966  1.00 26.85 ? 125  PRO A CG  1 
ATOM   866  C CD  . PRO A 1 125 ? 12.970  5.921   26.122  1.00 26.62 ? 125  PRO A CD  1 
ATOM   867  N N   . PRO A 1 126 ? 11.567  6.875   30.537  1.00 24.61 ? 126  PRO A N   1 
ATOM   868  C CA  . PRO A 1 126 ? 12.075  7.161   31.878  1.00 26.34 ? 126  PRO A CA  1 
ATOM   869  C C   . PRO A 1 126 ? 13.272  6.306   32.337  1.00 26.63 ? 126  PRO A C   1 
ATOM   870  O O   . PRO A 1 126 ? 14.144  6.855   32.981  1.00 26.11 ? 126  PRO A O   1 
ATOM   871  C CB  . PRO A 1 126 ? 10.840  6.896   32.747  1.00 26.66 ? 126  PRO A CB  1 
ATOM   872  C CG  . PRO A 1 126 ? 9.687   7.310   31.860  1.00 26.47 ? 126  PRO A CG  1 
ATOM   873  C CD  . PRO A 1 126 ? 10.100  6.796   30.495  1.00 25.78 ? 126  PRO A CD  1 
ATOM   874  N N   . ILE A 1 127 ? 13.264  5.010   32.003  1.00 25.75 ? 127  ILE A N   1 
ATOM   875  C CA  . ILE A 1 127 ? 14.268  4.001   32.446  1.00 28.20 ? 127  ILE A CA  1 
ATOM   876  C C   . ILE A 1 127 ? 15.672  4.401   31.947  1.00 28.09 ? 127  ILE A C   1 
ATOM   877  O O   . ILE A 1 127 ? 16.639  3.982   32.564  1.00 23.48 ? 127  ILE A O   1 
ATOM   878  C CB  . ILE A 1 127 ? 13.861  2.575   31.996  1.00 29.94 ? 127  ILE A CB  1 
ATOM   879  C CG1 . ILE A 1 127 ? 14.887  1.530   32.446  1.00 31.15 ? 127  ILE A CG1 1 
ATOM   880  C CG2 . ILE A 1 127 ? 13.617  2.496   30.491  1.00 31.32 ? 127  ILE A CG2 1 
ATOM   881  C CD1 . ILE A 1 127 ? 15.238  1.611   33.917  1.00 32.41 ? 127  ILE A CD1 1 
ATOM   882  N N   . LEU A 1 128 ? 15.762  5.209   30.890  1.00 26.35 ? 128  LEU A N   1 
ATOM   883  C CA  . LEU A 1 128 ? 17.033  5.608   30.267  1.00 26.43 ? 128  LEU A CA  1 
ATOM   884  C C   . LEU A 1 128 ? 17.447  6.978   30.799  1.00 28.84 ? 128  LEU A C   1 
ATOM   885  O O   . LEU A 1 128 ? 18.642  7.371   30.580  1.00 28.09 ? 128  LEU A O   1 
ATOM   886  C CB  . LEU A 1 128 ? 16.873  5.603   28.744  1.00 25.83 ? 128  LEU A CB  1 
ATOM   887  C CG  . LEU A 1 128 ? 16.767  4.214   28.110  1.00 26.60 ? 128  LEU A CG  1 
ATOM   888  C CD1 . LEU A 1 128 ? 16.810  4.304   26.601  1.00 29.27 ? 128  LEU A CD1 1 
ATOM   889  C CD2 . LEU A 1 128 ? 17.860  3.285   28.618  1.00 27.84 ? 128  LEU A CD2 1 
ATOM   890  N N   . LEU A 1 129 ? 16.554  7.676   31.503  1.00 25.13 ? 129  LEU A N   1 
ATOM   891  C CA  . LEU A 1 129 ? 16.913  9.031   31.974  1.00 26.83 ? 129  LEU A CA  1 
ATOM   892  C C   . LEU A 1 129 ? 18.132  8.927   32.902  1.00 29.83 ? 129  LEU A C   1 
ATOM   893  O O   . LEU A 1 129 ? 18.179  8.035   33.752  1.00 31.20 ? 129  LEU A O   1 
ATOM   894  C CB  . LEU A 1 129 ? 15.739  9.732   32.661  1.00 25.39 ? 129  LEU A CB  1 
ATOM   895  C CG  . LEU A 1 129 ? 15.916  11.244  32.680  1.00 22.40 ? 129  LEU A CG  1 
ATOM   896  C CD1 . LEU A 1 129 ? 15.763  11.782  31.275  1.00 21.86 ? 129  LEU A CD1 1 
ATOM   897  C CD2 . LEU A 1 129 ? 14.975  11.909  33.662  1.00 24.19 ? 129  LEU A CD2 1 
ATOM   898  N N   . GLY A 1 130 ? 19.113  9.798   32.704  1.00 33.75 ? 130  GLY A N   1 
ATOM   899  C CA  . GLY A 1 130 ? 20.326  9.835   33.541  1.00 37.69 ? 130  GLY A CA  1 
ATOM   900  C C   . GLY A 1 130 ? 21.496  9.050   32.967  1.00 37.65 ? 130  GLY A C   1 
ATOM   901  O O   . GLY A 1 130 ? 22.553  9.134   33.574  1.00 37.00 ? 130  GLY A O   1 
ATOM   902  N N   . GLN A 1 131 ? 21.335  8.315   31.863  1.00 41.55 ? 131  GLN A N   1 
ATOM   903  C CA  . GLN A 1 131 ? 22.495  7.755   31.099  1.00 46.71 ? 131  GLN A CA  1 
ATOM   904  C C   . GLN A 1 131 ? 23.117  8.885   30.277  1.00 47.03 ? 131  GLN A C   1 
ATOM   905  O O   . GLN A 1 131 ? 22.399  9.575   29.564  1.00 45.14 ? 131  GLN A O   1 
ATOM   906  C CB  . GLN A 1 131 ? 22.092  6.611   30.163  1.00 49.82 ? 131  GLN A CB  1 
ATOM   907  C CG  . GLN A 1 131 ? 21.139  5.583   30.772  1.00 53.88 ? 131  GLN A CG  1 
ATOM   908  C CD  . GLN A 1 131 ? 21.737  4.838   31.935  1.00 58.29 ? 131  GLN A CD  1 
ATOM   909  O OE1 . GLN A 1 131 ? 22.948  4.642   32.013  1.00 68.68 ? 131  GLN A OE1 1 
ATOM   910  N NE2 . GLN A 1 131 ? 20.881  4.402   32.846  1.00 63.61 ? 131  GLN A NE2 1 
ATOM   911  N N   . PRO A 1 132 ? 24.447  9.153   30.355  1.00 51.89 ? 132  PRO A N   1 
ATOM   912  C CA  . PRO A 1 132 ? 25.084  10.134  29.465  1.00 51.59 ? 132  PRO A CA  1 
ATOM   913  C C   . PRO A 1 132 ? 24.652  10.020  27.990  1.00 54.13 ? 132  PRO A C   1 
ATOM   914  O O   . PRO A 1 132 ? 24.577  11.043  27.315  1.00 50.58 ? 132  PRO A O   1 
ATOM   915  C CB  . PRO A 1 132 ? 26.574  9.800   29.601  1.00 50.88 ? 132  PRO A CB  1 
ATOM   916  C CG  . PRO A 1 132 ? 26.698  9.302   31.030  1.00 51.37 ? 132  PRO A CG  1 
ATOM   917  C CD  . PRO A 1 132 ? 25.396  8.576   31.324  1.00 49.15 ? 132  PRO A CD  1 
ATOM   918  N N   . SER A 1 133 ? 24.415  8.783   27.528  1.00 50.34 ? 133  SER A N   1 
ATOM   919  C CA  . SER A 1 133 ? 23.920  8.428   26.174  1.00 52.63 ? 133  SER A CA  1 
ATOM   920  C C   . SER A 1 133 ? 22.574  9.109   25.897  1.00 52.66 ? 133  SER A C   1 
ATOM   921  O O   . SER A 1 133 ? 22.388  9.635   24.781  1.00 48.98 ? 133  SER A O   1 
ATOM   922  C CB  . SER A 1 133 ? 23.781  6.932   26.047  1.00 58.79 ? 133  SER A CB  1 
ATOM   923  O OG  . SER A 1 133 ? 23.176  6.371   27.211  1.00 59.43 ? 133  SER A OG  1 
ATOM   924  N N   . SER A 1 134 ? 21.662  9.045   26.872  1.00 47.77 ? 134  SER A N   1 
ATOM   925  C CA  . SER A 1 134 ? 20.269  9.546   26.773  1.00 42.81 ? 134  SER A CA  1 
ATOM   926  C C   . SER A 1 134 ? 20.319  11.068  26.579  1.00 38.21 ? 134  SER A C   1 
ATOM   927  O O   . SER A 1 134 ? 20.958  11.772  27.393  1.00 40.98 ? 134  SER A O   1 
ATOM   928  C CB  . SER A 1 134 ? 19.463  9.111   27.963  1.00 37.25 ? 134  SER A CB  1 
ATOM   929  O OG  . SER A 1 134 ? 19.475  10.108  28.976  1.00 41.72 ? 134  SER A OG  1 
ATOM   930  N N   . VAL A 1 135 ? 19.733  11.550  25.491  1.00 34.58 ? 135  VAL A N   1 
ATOM   931  C CA  . VAL A 1 135 ? 19.855  12.971  25.072  1.00 35.75 ? 135  VAL A CA  1 
ATOM   932  C C   . VAL A 1 135 ? 18.536  13.684  25.390  1.00 35.93 ? 135  VAL A C   1 
ATOM   933  O O   . VAL A 1 135 ? 17.433  13.124  25.114  1.00 33.90 ? 135  VAL A O   1 
ATOM   934  C CB  . VAL A 1 135 ? 20.225  13.099  23.581  1.00 38.23 ? 135  VAL A CB  1 
ATOM   935  C CG1 . VAL A 1 135 ? 20.200  14.545  23.112  1.00 38.56 ? 135  VAL A CG1 1 
ATOM   936  C CG2 . VAL A 1 135 ? 21.581  12.472  23.279  1.00 42.91 ? 135  VAL A CG2 1 
ATOM   937  N N   . THR A 1 136 ? 18.663  14.881  25.951  1.00 32.09 ? 136  THR A N   1 
ATOM   938  C CA  . THR A 1 136 ? 17.576  15.872  26.072  1.00 30.00 ? 136  THR A CA  1 
ATOM   939  C C   . THR A 1 136 ? 17.949  17.097  25.234  1.00 29.31 ? 136  THR A C   1 
ATOM   940  O O   . THR A 1 136 ? 19.022  17.675  25.505  1.00 32.54 ? 136  THR A O   1 
ATOM   941  C CB  . THR A 1 136 ? 17.372  16.186  27.556  1.00 29.07 ? 136  THR A CB  1 
ATOM   942  O OG1 . THR A 1 136 ? 17.010  14.926  28.132  1.00 28.11 ? 136  THR A OG1 1 
ATOM   943  C CG2 . THR A 1 136 ? 16.354  17.285  27.793  1.00 26.04 ? 136  THR A CG2 1 
ATOM   944  N N   . LEU A 1 137 ? 17.090  17.499  24.291  1.00 28.33 ? 137  LEU A N   1 
ATOM   945  C CA  . LEU A 1 137 ? 17.261  18.724  23.453  1.00 28.24 ? 137  LEU A CA  1 
ATOM   946  C C   . LEU A 1 137 ? 16.790  19.927  24.264  1.00 30.04 ? 137  LEU A C   1 
ATOM   947  O O   . LEU A 1 137 ? 15.716  19.823  24.871  1.00 30.76 ? 137  LEU A O   1 
ATOM   948  C CB  . LEU A 1 137 ? 16.431  18.609  22.168  1.00 29.57 ? 137  LEU A CB  1 
ATOM   949  C CG  . LEU A 1 137 ? 16.635  17.325  21.366  1.00 29.98 ? 137  LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 137 ? 15.805  17.336  20.089  1.00 30.48 ? 137  LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 137 ? 18.115  17.117  21.055  1.00 29.97 ? 137  LEU A CD2 1 
ATOM   952  N N   . ILE A 1 138 ? 17.593  20.991  24.310  1.00 26.93 ? 138  ILE A N   1 
ATOM   953  C CA  . ILE A 1 138 ? 17.342  22.216  25.112  1.00 29.14 ? 138  ILE A CA  1 
ATOM   954  C C   . ILE A 1 138 ? 17.317  23.387  24.138  1.00 27.86 ? 138  ILE A C   1 
ATOM   955  O O   . ILE A 1 138 ? 18.139  23.377  23.203  1.00 29.03 ? 138  ILE A O   1 
ATOM   956  C CB  . ILE A 1 138 ? 18.407  22.379  26.222  1.00 31.78 ? 138  ILE A CB  1 
ATOM   957  C CG1 . ILE A 1 138 ? 18.452  21.153  27.141  1.00 33.75 ? 138  ILE A CG1 1 
ATOM   958  C CG2 . ILE A 1 138 ? 18.192  23.661  27.014  1.00 31.80 ? 138  ILE A CG2 1 
ATOM   959  C CD1 . ILE A 1 138 ? 17.183  20.928  27.930  1.00 34.97 ? 138  ILE A CD1 1 
ATOM   960  N N   . SER A 1 139 ? 16.357  24.303  24.304  1.00 28.49 ? 139  SER A N   1 
ATOM   961  C CA  . SER A 1 139 ? 16.294  25.590  23.562  1.00 27.95 ? 139  SER A CA  1 
ATOM   962  C C   . SER A 1 139 ? 15.872  26.727  24.496  1.00 28.11 ? 139  SER A C   1 
ATOM   963  O O   . SER A 1 139 ? 15.146  26.460  25.446  1.00 26.13 ? 139  SER A O   1 
ATOM   964  C CB  . SER A 1 139 ? 15.401  25.502  22.361  1.00 26.93 ? 139  SER A CB  1 
ATOM   965  O OG  . SER A 1 139 ? 14.078  25.170  22.733  1.00 25.05 ? 139  SER A OG  1 
ATOM   966  N N   . GLY A 1 140 ? 16.300  27.953  24.170  1.00 29.77 ? 140  GLY A N   1 
ATOM   967  C CA  . GLY A 1 140 ? 16.222  29.164  25.011  1.00 30.32 ? 140  GLY A CA  1 
ATOM   968  C C   . GLY A 1 140 ? 17.597  29.830  25.094  1.00 32.31 ? 140  GLY A C   1 
ATOM   969  O O   . GLY A 1 140 ? 18.574  29.288  24.587  1.00 27.33 ? 140  GLY A O   1 
ATOM   970  N N   . PRO A 1 141 ? 17.697  31.038  25.700  1.00 36.16 ? 141  PRO A N   1 
ATOM   971  C CA  . PRO A 1 141 ? 18.969  31.761  25.826  1.00 37.22 ? 141  PRO A CA  1 
ATOM   972  C C   . PRO A 1 141 ? 20.195  30.936  26.250  1.00 35.28 ? 141  PRO A C   1 
ATOM   973  O O   . PRO A 1 141 ? 20.108  30.210  27.204  1.00 36.49 ? 141  PRO A O   1 
ATOM   974  C CB  . PRO A 1 141 ? 18.630  32.794  26.907  1.00 38.37 ? 141  PRO A CB  1 
ATOM   975  C CG  . PRO A 1 141 ? 17.170  33.138  26.617  1.00 39.41 ? 141  PRO A CG  1 
ATOM   976  C CD  . PRO A 1 141 ? 16.552  31.821  26.195  1.00 37.49 ? 141  PRO A CD  1 
ATOM   977  N N   . LYS A 1 142 ? 21.298  31.091  25.513  1.00 36.84 ? 142  LYS A N   1 
ATOM   978  C CA  . LYS A 1 142 ? 22.609  30.418  25.724  1.00 40.87 ? 142  LYS A CA  1 
ATOM   979  C C   . LYS A 1 142 ? 23.074  30.581  27.183  1.00 40.79 ? 142  LYS A C   1 
ATOM   980  O O   . LYS A 1 142 ? 23.553  29.569  27.772  1.00 33.67 ? 142  LYS A O   1 
ATOM   981  C CB  . LYS A 1 142 ? 23.636  30.985  24.732  1.00 47.12 ? 142  LYS A CB  1 
ATOM   982  C CG  . LYS A 1 142 ? 25.020  30.343  24.750  1.00 50.50 ? 142  LYS A CG  1 
ATOM   983  C CD  . LYS A 1 142 ? 25.012  28.879  24.369  1.00 55.89 ? 142  LYS A CD  1 
ATOM   984  C CE  . LYS A 1 142 ? 26.350  28.194  24.570  1.00 59.23 ? 142  LYS A CE  1 
ATOM   985  N NZ  . LYS A 1 142 ? 26.313  26.798  24.062  1.00 59.77 ? 142  LYS A NZ  1 
ATOM   986  N N   . THR A 1 143 ? 22.955  31.783  27.759  1.00 40.10 ? 143  THR A N   1 
ATOM   987  C CA  . THR A 1 143 ? 23.407  32.065  29.149  1.00 44.45 ? 143  THR A CA  1 
ATOM   988  C C   . THR A 1 143 ? 22.544  31.251  30.123  1.00 42.74 ? 143  THR A C   1 
ATOM   989  O O   . THR A 1 143 ? 23.124  30.698  31.083  1.00 37.03 ? 143  THR A O   1 
ATOM   990  C CB  . THR A 1 143 ? 23.411  33.568  29.479  1.00 49.60 ? 143  THR A CB  1 
ATOM   991  O OG1 . THR A 1 143 ? 24.360  34.229  28.635  1.00 49.19 ? 143  THR A OG1 1 
ATOM   992  C CG2 . THR A 1 143 ? 23.760  33.847  30.929  1.00 49.15 ? 143  THR A CG2 1 
ATOM   993  N N   . ALA A 1 144 ? 21.229  31.158  29.873  1.00 41.86 ? 144  ALA A N   1 
ATOM   994  C CA  . ALA A 1 144 ? 20.272  30.382  30.706  1.00 43.60 ? 144  ALA A CA  1 
ATOM   995  C C   . ALA A 1 144 ? 20.629  28.885  30.647  1.00 41.95 ? 144  ALA A C   1 
ATOM   996  O O   . ALA A 1 144 ? 20.898  28.313  31.712  1.00 42.84 ? 144  ALA A O   1 
ATOM   997  C CB  . ALA A 1 144 ? 18.850  30.654  30.277  1.00 42.96 ? 144  ALA A CB  1 
ATOM   998  N N   . TYR A 1 145 ? 20.676  28.270  29.462  1.00 42.26 ? 145  TYR A N   1 
ATOM   999  C CA  . TYR A 1 145 ? 21.229  26.896  29.282  1.00 42.82 ? 145  TYR A CA  1 
ATOM   1000 C C   . TYR A 1 145 ? 22.513  26.765  30.109  1.00 43.14 ? 145  TYR A C   1 
ATOM   1001 O O   . TYR A 1 145 ? 22.640  25.797  30.888  1.00 42.27 ? 145  TYR A O   1 
ATOM   1002 C CB  . TYR A 1 145 ? 21.555  26.558  27.820  1.00 39.27 ? 145  TYR A CB  1 
ATOM   1003 C CG  . TYR A 1 145 ? 22.215  25.212  27.628  1.00 39.66 ? 145  TYR A CG  1 
ATOM   1004 C CD1 . TYR A 1 145 ? 21.563  24.041  27.989  1.00 40.31 ? 145  TYR A CD1 1 
ATOM   1005 C CD2 . TYR A 1 145 ? 23.501  25.095  27.118  1.00 41.30 ? 145  TYR A CD2 1 
ATOM   1006 C CE1 . TYR A 1 145 ? 22.162  22.799  27.838  1.00 41.61 ? 145  TYR A CE1 1 
ATOM   1007 C CE2 . TYR A 1 145 ? 24.118  23.862  26.960  1.00 39.39 ? 145  TYR A CE2 1 
ATOM   1008 C CZ  . TYR A 1 145 ? 23.441  22.705  27.312  1.00 43.15 ? 145  TYR A CZ  1 
ATOM   1009 O OH  . TYR A 1 145 ? 24.023  21.478  27.163  1.00 41.69 ? 145  TYR A OH  1 
ATOM   1010 N N   . GLU A 1 146 ? 23.450  27.701  29.929  1.00 44.89 ? 146  GLU A N   1 
ATOM   1011 C CA  . GLU A 1 146 ? 24.822  27.585  30.497  1.00 44.10 ? 146  GLU A CA  1 
ATOM   1012 C C   . GLU A 1 146 ? 24.729  27.535  32.025  1.00 38.80 ? 146  GLU A C   1 
ATOM   1013 O O   . GLU A 1 146 ? 25.485  26.755  32.639  1.00 35.05 ? 146  GLU A O   1 
ATOM   1014 C CB  . GLU A 1 146 ? 25.739  28.699  29.984  1.00 46.36 ? 146  GLU A CB  1 
ATOM   1015 C CG  . GLU A 1 146 ? 26.271  28.437  28.580  1.00 48.91 ? 146  GLU A CG  1 
ATOM   1016 C CD  . GLU A 1 146 ? 27.240  27.273  28.450  1.00 53.14 ? 146  GLU A CD  1 
ATOM   1017 O OE1 . GLU A 1 146 ? 28.036  27.060  29.388  1.00 59.34 ? 146  GLU A OE1 1 
ATOM   1018 O OE2 . GLU A 1 146 ? 27.211  26.587  27.401  1.00 55.28 ? 146  GLU A OE2 1 
ATOM   1019 N N   . SER A 1 147 ? 23.834  28.313  32.628  1.00 40.02 ? 147  SER A N   1 
ATOM   1020 C CA  . SER A 1 147 ? 23.662  28.340  34.107  1.00 41.66 ? 147  SER A CA  1 
ATOM   1021 C C   . SER A 1 147 ? 23.022  27.037  34.610  1.00 40.12 ? 147  SER A C   1 
ATOM   1022 O O   . SER A 1 147 ? 23.286  26.670  35.758  1.00 44.11 ? 147  SER A O   1 
ATOM   1023 C CB  . SER A 1 147 ? 22.896  29.560  34.565  1.00 44.08 ? 147  SER A CB  1 
ATOM   1024 O OG  . SER A 1 147 ? 21.894  29.918  33.630  1.00 50.47 ? 147  SER A OG  1 
ATOM   1025 N N   . GLN A 1 148 ? 22.238  26.338  33.785  1.00 39.39 ? 148  GLN A N   1 
ATOM   1026 C CA  . GLN A 1 148 ? 21.477  25.127  34.204  1.00 36.67 ? 148  GLN A CA  1 
ATOM   1027 C C   . GLN A 1 148 ? 22.196  23.859  33.742  1.00 35.58 ? 148  GLN A C   1 
ATOM   1028 O O   . GLN A 1 148 ? 21.799  22.756  34.194  1.00 37.21 ? 148  GLN A O   1 
ATOM   1029 C CB  . GLN A 1 148 ? 20.050  25.217  33.656  1.00 33.44 ? 148  GLN A CB  1 
ATOM   1030 C CG  . GLN A 1 148 ? 19.348  26.504  34.076  1.00 34.40 ? 148  GLN A CG  1 
ATOM   1031 C CD  . GLN A 1 148 ? 19.358  26.688  35.569  1.00 34.00 ? 148  GLN A CD  1 
ATOM   1032 O OE1 . GLN A 1 148 ? 19.414  25.725  36.330  1.00 35.63 ? 148  GLN A OE1 1 
ATOM   1033 N NE2 . GLN A 1 148 ? 19.274  27.934  35.999  1.00 36.42 ? 148  GLN A NE2 1 
ATOM   1034 N N   . LYS A 1 149 ? 23.176  24.016  32.852  1.00 35.79 ? 149  LYS A N   1 
ATOM   1035 C CA  . LYS A 1 149 ? 23.957  22.920  32.221  1.00 40.01 ? 149  LYS A CA  1 
ATOM   1036 C C   . LYS A 1 149 ? 24.299  21.858  33.263  1.00 37.17 ? 149  LYS A C   1 
ATOM   1037 O O   . LYS A 1 149 ? 24.035  20.667  33.008  1.00 32.73 ? 149  LYS A O   1 
ATOM   1038 C CB  . LYS A 1 149 ? 25.256  23.476  31.625  1.00 46.80 ? 149  LYS A CB  1 
ATOM   1039 C CG  . LYS A 1 149 ? 25.442  23.295  30.127  1.00 51.43 ? 149  LYS A CG  1 
ATOM   1040 C CD  . LYS A 1 149 ? 26.144  22.006  29.746  1.00 57.46 ? 149  LYS A CD  1 
ATOM   1041 C CE  . LYS A 1 149 ? 27.523  21.855  30.359  1.00 59.49 ? 149  LYS A CE  1 
ATOM   1042 N NZ  . LYS A 1 149 ? 28.382  23.025  30.065  1.00 62.31 ? 149  LYS A NZ  1 
ATOM   1043 N N   . GLU A 1 150 ? 24.894  22.288  34.375  1.00 37.78 ? 150  GLU A N   1 
ATOM   1044 C CA  . GLU A 1 150 ? 25.437  21.398  35.437  1.00 39.32 ? 150  GLU A CA  1 
ATOM   1045 C C   . GLU A 1 150 ? 24.295  20.589  36.069  1.00 33.51 ? 150  GLU A C   1 
ATOM   1046 O O   . GLU A 1 150 ? 24.364  19.350  36.018  1.00 33.89 ? 150  GLU A O   1 
ATOM   1047 C CB  . GLU A 1 150 ? 26.201  22.235  36.465  1.00 45.88 ? 150  GLU A CB  1 
ATOM   1048 C CG  . GLU A 1 150 ? 26.872  21.409  37.544  1.00 51.78 ? 150  GLU A CG  1 
ATOM   1049 C CD  . GLU A 1 150 ? 28.107  20.647  37.097  1.00 57.66 ? 150  GLU A CD  1 
ATOM   1050 O OE1 . GLU A 1 150 ? 29.214  21.047  37.513  1.00 64.17 ? 150  GLU A OE1 1 
ATOM   1051 O OE2 . GLU A 1 150 ? 27.964  19.650  36.349  1.00 62.05 ? 150  GLU A OE2 1 
ATOM   1052 N N   . LEU A 1 151 ? 23.278  21.252  36.630  1.00 32.18 ? 151  LEU A N   1 
ATOM   1053 C CA  . LEU A 1 151 ? 22.028  20.592  37.119  1.00 30.84 ? 151  LEU A CA  1 
ATOM   1054 C C   . LEU A 1 151 ? 21.473  19.642  36.047  1.00 29.32 ? 151  LEU A C   1 
ATOM   1055 O O   . LEU A 1 151 ? 21.138  18.505  36.377  1.00 27.78 ? 151  LEU A O   1 
ATOM   1056 C CB  . LEU A 1 151 ? 20.980  21.655  37.464  1.00 30.75 ? 151  LEU A CB  1 
ATOM   1057 C CG  . LEU A 1 151 ? 19.635  21.109  37.946  1.00 29.51 ? 151  LEU A CG  1 
ATOM   1058 C CD1 . LEU A 1 151 ? 19.840  20.301  39.229  1.00 29.90 ? 151  LEU A CD1 1 
ATOM   1059 C CD2 . LEU A 1 151 ? 18.623  22.229  38.161  1.00 28.47 ? 151  LEU A CD2 1 
ATOM   1060 N N   . LEU A 1 152 ? 21.361  20.109  34.804  1.00 32.20 ? 152  LEU A N   1 
ATOM   1061 C CA  . LEU A 1 152 ? 20.711  19.357  33.707  1.00 34.87 ? 152  LEU A CA  1 
ATOM   1062 C C   . LEU A 1 152 ? 21.478  18.065  33.415  1.00 34.79 ? 152  LEU A C   1 
ATOM   1063 O O   . LEU A 1 152 ? 20.879  17.161  32.833  1.00 33.71 ? 152  LEU A O   1 
ATOM   1064 C CB  . LEU A 1 152 ? 20.638  20.242  32.465  1.00 39.31 ? 152  LEU A CB  1 
ATOM   1065 C CG  . LEU A 1 152 ? 19.441  21.188  32.403  1.00 44.63 ? 152  LEU A CG  1 
ATOM   1066 C CD1 . LEU A 1 152 ? 19.600  22.163  31.251  1.00 46.05 ? 152  LEU A CD1 1 
ATOM   1067 C CD2 . LEU A 1 152 ? 18.134  20.414  32.270  1.00 48.33 ? 152  LEU A CD2 1 
ATOM   1068 N N   . SER A 1 153 ? 22.763  17.989  33.772  1.00 36.19 ? 153  SER A N   1 
ATOM   1069 C CA  . SER A 1 153 ? 23.627  16.816  33.491  1.00 35.38 ? 153  SER A CA  1 
ATOM   1070 C C   . SER A 1 153 ? 23.137  15.620  34.312  1.00 32.45 ? 153  SER A C   1 
ATOM   1071 O O   . SER A 1 153 ? 23.464  14.492  33.946  1.00 30.83 ? 153  SER A O   1 
ATOM   1072 C CB  . SER A 1 153 ? 25.090  17.125  33.749  1.00 36.26 ? 153  SER A CB  1 
ATOM   1073 O OG  . SER A 1 153 ? 25.322  17.358  35.131  1.00 36.82 ? 153  SER A OG  1 
ATOM   1074 N N   . SER A 1 154 ? 22.340  15.850  35.360  1.00 33.94 ? 154  SER A N   1 
ATOM   1075 C CA  . SER A 1 154 ? 21.706  14.757  36.140  1.00 34.57 ? 154  SER A CA  1 
ATOM   1076 C C   . SER A 1 154 ? 20.819  13.888  35.235  1.00 31.61 ? 154  SER A C   1 
ATOM   1077 O O   . SER A 1 154 ? 20.727  12.690  35.513  1.00 31.73 ? 154  SER A O   1 
ATOM   1078 C CB  . SER A 1 154 ? 20.949  15.279  37.339  1.00 36.94 ? 154  SER A CB  1 
ATOM   1079 O OG  . SER A 1 154 ? 20.048  16.305  36.973  1.00 38.58 ? 154  SER A OG  1 
ATOM   1080 N N   . ILE A 1 155 ? 20.208  14.426  34.178  1.00 28.74 ? 155  ILE A N   1 
ATOM   1081 C CA  . ILE A 1 155 ? 19.224  13.631  33.370  1.00 31.67 ? 155  ILE A CA  1 
ATOM   1082 C C   . ILE A 1 155 ? 19.884  13.102  32.098  1.00 29.48 ? 155  ILE A C   1 
ATOM   1083 O O   . ILE A 1 155 ? 19.186  12.516  31.285  1.00 29.94 ? 155  ILE A O   1 
ATOM   1084 C CB  . ILE A 1 155 ? 17.932  14.423  33.084  1.00 31.72 ? 155  ILE A CB  1 
ATOM   1085 C CG1 . ILE A 1 155 ? 18.168  15.625  32.162  1.00 31.60 ? 155  ILE A CG1 1 
ATOM   1086 C CG2 . ILE A 1 155 ? 17.296  14.828  34.408  1.00 34.70 ? 155  ILE A CG2 1 
ATOM   1087 C CD1 . ILE A 1 155 ? 16.897  16.320  31.710  1.00 31.73 ? 155  ILE A CD1 1 
ATOM   1088 N N   . GLY A 1 156 ? 21.196  13.278  31.970  1.00 32.26 ? 156  GLY A N   1 
ATOM   1089 C CA  . GLY A 1 156 ? 21.986  12.773  30.836  1.00 33.47 ? 156  GLY A CA  1 
ATOM   1090 C C   . GLY A 1 156 ? 22.626  13.929  30.111  1.00 33.53 ? 156  GLY A C   1 
ATOM   1091 O O   . GLY A 1 156 ? 22.819  14.982  30.747  1.00 36.86 ? 156  GLY A O   1 
ATOM   1092 N N   . THR A 1 157 ? 22.956  13.737  28.840  1.00 35.58 ? 157  THR A N   1 
ATOM   1093 C CA  . THR A 1 157 ? 23.598  14.773  28.005  1.00 39.51 ? 157  THR A CA  1 
ATOM   1094 C C   . THR A 1 157 ? 22.486  15.653  27.466  1.00 37.70 ? 157  THR A C   1 
ATOM   1095 O O   . THR A 1 157 ? 21.511  15.094  26.961  1.00 42.20 ? 157  THR A O   1 
ATOM   1096 C CB  . THR A 1 157 ? 24.423  14.164  26.871  1.00 44.49 ? 157  THR A CB  1 
ATOM   1097 O OG1 . THR A 1 157 ? 23.540  13.282  26.167  1.00 48.89 ? 157  THR A OG1 1 
ATOM   1098 C CG2 . THR A 1 157 ? 25.658  13.463  27.396  1.00 43.78 ? 157  THR A CG2 1 
ATOM   1099 N N   . THR A 1 158 ? 22.621  16.957  27.664  1.00 35.69 ? 158  THR A N   1 
ATOM   1100 C CA  . THR A 1 158 ? 21.777  18.006  27.056  1.00 36.78 ? 158  THR A CA  1 
ATOM   1101 C C   . THR A 1 158 ? 22.446  18.453  25.757  1.00 36.93 ? 158  THR A C   1 
ATOM   1102 O O   . THR A 1 158 ? 23.672  18.531  25.736  1.00 34.55 ? 158  THR A O   1 
ATOM   1103 C CB  . THR A 1 158 ? 21.558  19.154  28.042  1.00 35.64 ? 158  THR A CB  1 
ATOM   1104 O OG1 . THR A 1 158 ? 22.814  19.549  28.592  1.00 34.55 ? 158  THR A OG1 1 
ATOM   1105 C CG2 . THR A 1 158 ? 20.619  18.755  29.156  1.00 37.43 ? 158  THR A CG2 1 
ATOM   1106 N N   . ARG A 1 159 ? 21.654  18.630  24.701  1.00 38.87 ? 159  ARG A N   1 
ATOM   1107 C CA  . ARG A 1 159 ? 22.082  19.258  23.434  1.00 36.32 ? 159  ARG A CA  1 
ATOM   1108 C C   . ARG A 1 159 ? 21.313  20.572  23.294  1.00 34.64 ? 159  ARG A C   1 
ATOM   1109 O O   . ARG A 1 159 ? 20.095  20.526  23.067  1.00 32.23 ? 159  ARG A O   1 
ATOM   1110 C CB  . ARG A 1 159 ? 21.853  18.304  22.263  1.00 40.46 ? 159  ARG A CB  1 
ATOM   1111 C CG  . ARG A 1 159 ? 21.770  19.012  20.921  1.00 48.29 ? 159  ARG A CG  1 
ATOM   1112 C CD  . ARG A 1 159 ? 22.644  18.437  19.830  1.00 55.31 ? 159  ARG A CD  1 
ATOM   1113 N NE  . ARG A 1 159 ? 22.142  17.176  19.294  1.00 59.64 ? 159  ARG A NE  1 
ATOM   1114 C CZ  . ARG A 1 159 ? 22.117  16.848  18.000  1.00 62.26 ? 159  ARG A CZ  1 
ATOM   1115 N NH1 . ARG A 1 159 ? 22.540  17.701  17.078  1.00 59.66 ? 159  ARG A NH1 1 
ATOM   1116 N NH2 . ARG A 1 159 ? 21.651  15.663  17.631  1.00 61.93 ? 159  ARG A NH2 1 
ATOM   1117 N N   . HIS A 1 160 ? 22.009  21.703  23.425  1.00 35.18 ? 160  HIS A N   1 
ATOM   1118 C CA  . HIS A 1 160 ? 21.447  23.051  23.180  1.00 35.13 ? 160  HIS A CA  1 
ATOM   1119 C C   . HIS A 1 160 ? 21.314  23.274  21.677  1.00 30.97 ? 160  HIS A C   1 
ATOM   1120 O O   . HIS A 1 160 ? 22.329  23.529  21.040  1.00 34.96 ? 160  HIS A O   1 
ATOM   1121 C CB  . HIS A 1 160 ? 22.314  24.142  23.807  1.00 38.18 ? 160  HIS A CB  1 
ATOM   1122 C CG  . HIS A 1 160 ? 21.687  25.484  23.673  1.00 37.95 ? 160  HIS A CG  1 
ATOM   1123 N ND1 . HIS A 1 160 ? 22.175  26.439  22.818  1.00 45.88 ? 160  HIS A ND1 1 
ATOM   1124 C CD2 . HIS A 1 160 ? 20.589  26.011  24.250  1.00 38.15 ? 160  HIS A CD2 1 
ATOM   1125 C CE1 . HIS A 1 160 ? 21.427  27.520  22.902  1.00 46.14 ? 160  HIS A CE1 1 
ATOM   1126 N NE2 . HIS A 1 160 ? 20.457  27.286  23.790  1.00 42.36 ? 160  HIS A NE2 1 
ATOM   1127 N N   . VAL A 1 161 ? 20.108  23.187  21.138  1.00 30.77 ? 161  VAL A N   1 
ATOM   1128 C CA  . VAL A 1 161 ? 19.880  23.138  19.664  1.00 31.69 ? 161  VAL A CA  1 
ATOM   1129 C C   . VAL A 1 161 ? 19.625  24.555  19.119  1.00 32.84 ? 161  VAL A C   1 
ATOM   1130 O O   . VAL A 1 161 ? 19.690  24.722  17.900  1.00 37.36 ? 161  VAL A O   1 
ATOM   1131 C CB  . VAL A 1 161 ? 18.747  22.158  19.298  1.00 31.32 ? 161  VAL A CB  1 
ATOM   1132 C CG1 . VAL A 1 161 ? 19.120  20.751  19.706  1.00 33.54 ? 161  VAL A CG1 1 
ATOM   1133 C CG2 . VAL A 1 161 ? 17.396  22.529  19.894  1.00 32.45 ? 161  VAL A CG2 1 
ATOM   1134 N N   . SER A 1 162 ? 19.333  25.541  19.966  1.00 30.50 ? 162  SER A N   1 
ATOM   1135 C CA  . SER A 1 162 ? 18.992  26.904  19.507  1.00 31.44 ? 162  SER A CA  1 
ATOM   1136 C C   . SER A 1 162 ? 18.725  27.844  20.678  1.00 32.06 ? 162  SER A C   1 
ATOM   1137 O O   . SER A 1 162 ? 18.346  27.356  21.763  1.00 29.56 ? 162  SER A O   1 
ATOM   1138 C CB  . SER A 1 162 ? 17.818  26.869  18.599  1.00 33.73 ? 162  SER A CB  1 
ATOM   1139 O OG  . SER A 1 162 ? 17.283  28.165  18.469  1.00 33.01 ? 162  SER A OG  1 
ATOM   1140 N N   . ASP A 1 163 ? 18.880  29.152  20.436  1.00 30.53 ? 163  ASP A N   1 
ATOM   1141 C CA  . ASP A 1 163 ? 18.565  30.213  21.431  1.00 30.70 ? 163  ASP A CA  1 
ATOM   1142 C C   . ASP A 1 163 ? 17.060  30.461  21.425  1.00 29.53 ? 163  ASP A C   1 
ATOM   1143 O O   . ASP A 1 163 ? 16.564  31.099  22.366  1.00 29.12 ? 163  ASP A O   1 
ATOM   1144 C CB  . ASP A 1 163 ? 19.337  31.509  21.169  1.00 29.58 ? 163  ASP A CB  1 
ATOM   1145 C CG  . ASP A 1 163 ? 20.650  31.594  21.928  1.00 31.32 ? 163  ASP A CG  1 
ATOM   1146 O OD1 . ASP A 1 163 ? 21.525  30.697  21.715  1.00 31.00 ? 163  ASP A OD1 1 
ATOM   1147 O OD2 . ASP A 1 163 ? 20.789  32.542  22.745  1.00 32.56 ? 163  ASP A OD2 1 
ATOM   1148 N N   . ASP A 1 164 ? 16.380  30.017  20.371  1.00 29.45 ? 164  ASP A N   1 
ATOM   1149 C CA  . ASP A 1 164 ? 14.910  30.168  20.203  1.00 30.65 ? 164  ASP A CA  1 
ATOM   1150 C C   . ASP A 1 164 ? 14.185  29.132  21.079  1.00 31.40 ? 164  ASP A C   1 
ATOM   1151 O O   . ASP A 1 164 ? 14.350  27.919  20.845  1.00 30.13 ? 164  ASP A O   1 
ATOM   1152 C CB  . ASP A 1 164 ? 14.534  30.007  18.735  1.00 32.67 ? 164  ASP A CB  1 
ATOM   1153 C CG  . ASP A 1 164 ? 13.059  30.191  18.436  1.00 34.67 ? 164  ASP A CG  1 
ATOM   1154 O OD1 . ASP A 1 164 ? 12.263  30.299  19.379  1.00 39.35 ? 164  ASP A OD1 1 
ATOM   1155 O OD2 . ASP A 1 164 ? 12.723  30.212  17.261  1.00 41.82 ? 164  ASP A OD2 1 
ATOM   1156 N N   . ILE A 1 165 ? 13.375  29.624  22.018  1.00 33.29 ? 165  ILE A N   1 
ATOM   1157 C CA  . ILE A 1 165 ? 12.621  28.856  23.049  1.00 33.42 ? 165  ILE A CA  1 
ATOM   1158 C C   . ILE A 1 165 ? 11.781  27.768  22.374  1.00 28.78 ? 165  ILE A C   1 
ATOM   1159 O O   . ILE A 1 165 ? 11.690  26.683  22.935  1.00 28.97 ? 165  ILE A O   1 
ATOM   1160 C CB  . ILE A 1 165 ? 11.752  29.819  23.883  1.00 36.03 ? 165  ILE A CB  1 
ATOM   1161 C CG1 . ILE A 1 165 ? 12.614  30.665  24.825  1.00 39.04 ? 165  ILE A CG1 1 
ATOM   1162 C CG2 . ILE A 1 165 ? 10.673  29.051  24.632  1.00 38.27 ? 165  ILE A CG2 1 
ATOM   1163 C CD1 . ILE A 1 165 ? 11.982  31.990  25.233  1.00 40.11 ? 165  ILE A CD1 1 
ATOM   1164 N N   . ALA A 1 166 ? 11.189  28.061  21.219  1.00 26.58 ? 166  ALA A N   1 
ATOM   1165 C CA  . ALA A 1 166 ? 10.259  27.171  20.486  1.00 25.51 ? 166  ALA A CA  1 
ATOM   1166 C C   . ALA A 1 166 ? 10.968  25.983  19.816  1.00 28.34 ? 166  ALA A C   1 
ATOM   1167 O O   . ALA A 1 166 ? 10.241  25.056  19.405  1.00 29.43 ? 166  ALA A O   1 
ATOM   1168 C CB  . ALA A 1 166 ? 9.515   27.993  19.468  1.00 26.83 ? 166  ALA A CB  1 
ATOM   1169 N N   . LYS A 1 167 ? 12.304  25.979  19.669  1.00 29.24 ? 167  LYS A N   1 
ATOM   1170 C CA  . LYS A 1 167 ? 12.992  25.025  18.743  1.00 29.78 ? 167  LYS A CA  1 
ATOM   1171 C C   . LYS A 1 167 ? 13.011  23.594  19.296  1.00 27.31 ? 167  LYS A C   1 
ATOM   1172 O O   . LYS A 1 167 ? 12.854  22.676  18.484  1.00 26.47 ? 167  LYS A O   1 
ATOM   1173 C CB  . LYS A 1 167 ? 14.454  25.386  18.448  1.00 34.95 ? 167  LYS A CB  1 
ATOM   1174 C CG  . LYS A 1 167 ? 14.690  26.447  17.374  1.00 40.03 ? 167  LYS A CG  1 
ATOM   1175 C CD  . LYS A 1 167 ? 13.953  26.238  16.069  1.00 43.16 ? 167  LYS A CD  1 
ATOM   1176 C CE  . LYS A 1 167 ? 12.646  27.000  15.984  1.00 43.31 ? 167  LYS A CE  1 
ATOM   1177 N NZ  . LYS A 1 167 ? 12.262  27.248  14.575  1.00 45.83 ? 167  LYS A NZ  1 
ATOM   1178 N N   . ALA A 1 168 ? 13.306  23.377  20.582  1.00 25.15 ? 168  ALA A N   1 
ATOM   1179 C CA  . ALA A 1 168 ? 13.377  22.005  21.139  1.00 25.00 ? 168  ALA A CA  1 
ATOM   1180 C C   . ALA A 1 168 ? 12.033  21.311  20.889  1.00 24.47 ? 168  ALA A C   1 
ATOM   1181 O O   . ALA A 1 168 ? 12.060  20.146  20.497  1.00 23.62 ? 168  ALA A O   1 
ATOM   1182 C CB  . ALA A 1 168 ? 13.732  21.998  22.599  1.00 24.28 ? 168  ALA A CB  1 
ATOM   1183 N N   . SER A 1 169 ? 10.914  22.029  21.038  1.00 23.09 ? 169  SER A N   1 
ATOM   1184 C CA  . SER A 1 169 ? 9.551   21.493  20.785  1.00 23.68 ? 169  SER A CA  1 
ATOM   1185 C C   . SER A 1 169 ? 9.318   21.242  19.291  1.00 24.52 ? 169  SER A C   1 
ATOM   1186 O O   . SER A 1 169 ? 8.705   20.210  18.947  1.00 23.89 ? 169  SER A O   1 
ATOM   1187 C CB  . SER A 1 169 ? 8.494   22.388  21.359  1.00 23.29 ? 169  SER A CB  1 
ATOM   1188 O OG  . SER A 1 169 ? 8.364   22.189  22.758  1.00 22.37 ? 169  SER A OG  1 
ATOM   1189 N N   . LEU A 1 170 ? 9.741   22.154  18.420  1.00 26.12 ? 170  LEU A N   1 
ATOM   1190 C CA  . LEU A 1 170 ? 9.653   21.937  16.946  1.00 27.62 ? 170  LEU A CA  1 
ATOM   1191 C C   . LEU A 1 170 ? 10.377  20.630  16.586  1.00 24.99 ? 170  LEU A C   1 
ATOM   1192 O O   . LEU A 1 170 ? 9.820   19.839  15.831  1.00 22.12 ? 170  LEU A O   1 
ATOM   1193 C CB  . LEU A 1 170 ? 10.291  23.123  16.206  1.00 28.61 ? 170  LEU A CB  1 
ATOM   1194 C CG  . LEU A 1 170 ? 10.365  22.969  14.691  1.00 29.19 ? 170  LEU A CG  1 
ATOM   1195 C CD1 . LEU A 1 170 ? 9.027   23.311  14.046  1.00 28.85 ? 170  LEU A CD1 1 
ATOM   1196 C CD2 . LEU A 1 170 ? 11.488  23.821  14.116  1.00 32.06 ? 170  LEU A CD2 1 
ATOM   1197 N N   . LEU A 1 171 ? 11.605  20.449  17.073  1.00 24.24 ? 171  LEU A N   1 
ATOM   1198 C CA  . LEU A 1 171 ? 12.420  19.253  16.744  1.00 26.37 ? 171  LEU A CA  1 
ATOM   1199 C C   . LEU A 1 171 ? 11.797  18.026  17.421  1.00 25.40 ? 171  LEU A C   1 
ATOM   1200 O O   . LEU A 1 171 ? 11.745  16.954  16.782  1.00 24.49 ? 171  LEU A O   1 
ATOM   1201 C CB  . LEU A 1 171 ? 13.863  19.470  17.206  1.00 26.40 ? 171  LEU A CB  1 
ATOM   1202 C CG  . LEU A 1 171 ? 14.622  20.607  16.522  1.00 28.20 ? 171  LEU A CG  1 
ATOM   1203 C CD1 . LEU A 1 171 ? 16.007  20.732  17.114  1.00 28.16 ? 171  LEU A CD1 1 
ATOM   1204 C CD2 . LEU A 1 171 ? 14.716  20.386  15.030  1.00 30.41 ? 171  LEU A CD2 1 
ATOM   1205 N N   . ASP A 1 172 ? 11.339  18.195  18.667  1.00 24.44 ? 172  ASP A N   1 
ATOM   1206 C CA  . ASP A 1 172 ? 10.551  17.179  19.419  1.00 26.03 ? 172  ASP A CA  1 
ATOM   1207 C C   . ASP A 1 172 ? 9.417   16.666  18.517  1.00 23.31 ? 172  ASP A C   1 
ATOM   1208 O O   . ASP A 1 172 ? 9.358   15.469  18.293  1.00 21.12 ? 172  ASP A O   1 
ATOM   1209 C CB  . ASP A 1 172 ? 9.988   17.745  20.728  1.00 24.54 ? 172  ASP A CB  1 
ATOM   1210 C CG  . ASP A 1 172 ? 9.456   16.698  21.698  1.00 26.71 ? 172  ASP A CG  1 
ATOM   1211 O OD1 . ASP A 1 172 ? 9.930   15.511  21.628  1.00 23.96 ? 172  ASP A OD1 1 
ATOM   1212 O OD2 . ASP A 1 172 ? 8.585   17.079  22.547  1.00 24.05 ? 172  ASP A OD2 1 
ATOM   1213 N N   . ASN A 1 173 ? 8.548   17.553  18.027  1.00 22.97 ? 173  ASN A N   1 
ATOM   1214 C CA  . ASN A 1 173 ? 7.378   17.180  17.187  1.00 23.20 ? 173  ASN A CA  1 
ATOM   1215 C C   . ASN A 1 173 ? 7.863   16.469  15.918  1.00 23.74 ? 173  ASN A C   1 
ATOM   1216 O O   . ASN A 1 173 ? 7.305   15.423  15.591  1.00 21.85 ? 173  ASN A O   1 
ATOM   1217 C CB  . ASN A 1 173 ? 6.474   18.382  16.912  1.00 24.31 ? 173  ASN A CB  1 
ATOM   1218 C CG  . ASN A 1 173 ? 5.556   18.666  18.080  1.00 21.77 ? 173  ASN A CG  1 
ATOM   1219 O OD1 . ASN A 1 173 ? 4.436   18.191  18.087  1.00 21.47 ? 173  ASN A OD1 1 
ATOM   1220 N ND2 . ASN A 1 173 ? 6.051   19.324  19.115  1.00 23.14 ? 173  ASN A ND2 1 
ATOM   1221 N N   . ALA A 1 174 ? 8.917   16.973  15.271  1.00 24.76 ? 174  ALA A N   1 
ATOM   1222 C CA  . ALA A 1 174 ? 9.498   16.341  14.062  1.00 25.10 ? 174  ALA A CA  1 
ATOM   1223 C C   . ALA A 1 174 ? 9.976   14.912  14.394  1.00 23.43 ? 174  ALA A C   1 
ATOM   1224 O O   . ALA A 1 174 ? 9.659   13.970  13.640  1.00 23.11 ? 174  ALA A O   1 
ATOM   1225 C CB  . ALA A 1 174 ? 10.610  17.205  13.510  1.00 25.74 ? 174  ALA A CB  1 
ATOM   1226 N N   . LEU A 1 175 ? 10.706  14.736  15.490  1.00 21.22 ? 175  LEU A N   1 
ATOM   1227 C CA  . LEU A 1 175 ? 11.303  13.418  15.839  1.00 20.65 ? 175  LEU A CA  1 
ATOM   1228 C C   . LEU A 1 175 ? 10.196  12.451  16.266  1.00 21.31 ? 175  LEU A C   1 
ATOM   1229 O O   . LEU A 1 175 ? 10.285  11.273  15.919  1.00 22.77 ? 175  LEU A O   1 
ATOM   1230 C CB  . LEU A 1 175 ? 12.323  13.597  16.958  1.00 20.63 ? 175  LEU A CB  1 
ATOM   1231 C CG  . LEU A 1 175 ? 13.672  14.218  16.580  1.00 22.08 ? 175  LEU A CG  1 
ATOM   1232 C CD1 . LEU A 1 175 ? 14.479  14.446  17.838  1.00 24.02 ? 175  LEU A CD1 1 
ATOM   1233 C CD2 . LEU A 1 175 ? 14.452  13.334  15.597  1.00 22.79 ? 175  LEU A CD2 1 
ATOM   1234 N N   . LEU A 1 176 ? 9.204   12.926  17.021  1.00 20.71 ? 176  LEU A N   1 
ATOM   1235 C CA  . LEU A 1 176 ? 8.051   12.100  17.470  1.00 20.40 ? 176  LEU A CA  1 
ATOM   1236 C C   . LEU A 1 176 ? 7.182   11.716  16.270  1.00 20.49 ? 176  LEU A C   1 
ATOM   1237 O O   . LEU A 1 176 ? 6.556   10.641  16.333  1.00 21.18 ? 176  LEU A O   1 
ATOM   1238 C CB  . LEU A 1 176 ? 7.233   12.879  18.493  1.00 21.37 ? 176  LEU A CB  1 
ATOM   1239 C CG  . LEU A 1 176 ? 7.882   13.018  19.857  1.00 22.38 ? 176  LEU A CG  1 
ATOM   1240 C CD1 . LEU A 1 176 ? 6.939   13.733  20.799  1.00 23.03 ? 176  LEU A CD1 1 
ATOM   1241 C CD2 . LEU A 1 176 ? 8.272   11.660  20.406  1.00 22.84 ? 176  LEU A CD2 1 
ATOM   1242 N N   . SER A 1 177 ? 7.151   12.532  15.209  1.00 19.98 ? 177  SER A N   1 
ATOM   1243 C CA  . SER A 1 177 ? 6.523   12.151  13.914  1.00 22.17 ? 177  SER A CA  1 
ATOM   1244 C C   . SER A 1 177 ? 7.165   10.869  13.374  1.00 21.70 ? 177  SER A C   1 
ATOM   1245 O O   . SER A 1 177 ? 6.420   9.965   12.953  1.00 21.20 ? 177  SER A O   1 
ATOM   1246 C CB  . SER A 1 177 ? 6.641   13.259  12.907  1.00 22.72 ? 177  SER A CB  1 
ATOM   1247 O OG  . SER A 1 177 ? 5.963   14.406  13.377  1.00 25.46 ? 177  SER A OG  1 
ATOM   1248 N N   . ILE A 1 178 ? 8.503   10.810  13.382  1.00 21.11 ? 178  ILE A N   1 
ATOM   1249 C CA  . ILE A 1 178 ? 9.274   9.642   12.874  1.00 21.92 ? 178  ILE A CA  1 
ATOM   1250 C C   . ILE A 1 178 ? 8.944   8.452   13.776  1.00 22.67 ? 178  ILE A C   1 
ATOM   1251 O O   . ILE A 1 178 ? 8.608   7.377   13.264  1.00 21.86 ? 178  ILE A O   1 
ATOM   1252 C CB  . ILE A 1 178 ? 10.773  9.964   12.852  1.00 23.02 ? 178  ILE A CB  1 
ATOM   1253 C CG1 . ILE A 1 178 ? 11.067  11.197  12.000  1.00 22.42 ? 178  ILE A CG1 1 
ATOM   1254 C CG2 . ILE A 1 178 ? 11.591  8.759   12.407  1.00 24.12 ? 178  ILE A CG2 1 
ATOM   1255 C CD1 . ILE A 1 178 ? 12.447  11.787  12.265  1.00 22.97 ? 178  ILE A CD1 1 
ATOM   1256 N N   . MET A 1 179 ? 9.021   8.665   15.089  1.00 24.39 ? 179  MET A N   1 
ATOM   1257 C CA  . MET A 1 179 ? 8.729   7.618   16.093  1.00 26.13 ? 179  MET A CA  1 
ATOM   1258 C C   . MET A 1 179 ? 7.301   7.098   15.891  1.00 23.34 ? 179  MET A C   1 
ATOM   1259 O O   . MET A 1 179 ? 7.145   5.893   15.847  1.00 24.17 ? 179  MET A O   1 
ATOM   1260 C CB  . MET A 1 179 ? 8.885   8.132   17.523  1.00 29.22 ? 179  MET A CB  1 
ATOM   1261 C CG  . MET A 1 179 ? 8.966   6.992   18.507  1.00 35.93 ? 179  MET A CG  1 
ATOM   1262 S SD  . MET A 1 179 ? 9.105   7.545   20.205  1.00 46.17 ? 179  MET A SD  1 
ATOM   1263 C CE  . MET A 1 179 ? 10.637  8.476   20.120  1.00 45.74 ? 179  MET A CE  1 
ATOM   1264 N N   . GLY A 1 180 ? 6.320   7.985   15.758  1.00 21.05 ? 180  GLY A N   1 
ATOM   1265 C CA  . GLY A 1 180 ? 4.926   7.615   15.476  1.00 21.89 ? 180  GLY A CA  1 
ATOM   1266 C C   . GLY A 1 180 ? 4.809   6.735   14.249  1.00 21.54 ? 180  GLY A C   1 
ATOM   1267 O O   . GLY A 1 180 ? 4.138   5.692   14.333  1.00 21.90 ? 180  GLY A O   1 
ATOM   1268 N N   . GLY A 1 181 ? 5.454   7.132   13.158  1.00 21.74 ? 181  GLY A N   1 
ATOM   1269 C CA  . GLY A 1 181 ? 5.489   6.375   11.891  1.00 21.82 ? 181  GLY A CA  1 
ATOM   1270 C C   . GLY A 1 181 ? 6.120   4.998   12.056  1.00 20.85 ? 181  GLY A C   1 
ATOM   1271 O O   . GLY A 1 181 ? 5.534   4.006   11.595  1.00 18.92 ? 181  GLY A O   1 
ATOM   1272 N N   . VAL A 1 182 ? 7.295   4.948   12.689  1.00 22.79 ? 182  VAL A N   1 
ATOM   1273 C CA  . VAL A 1 182 ? 8.056   3.693   12.983  1.00 21.02 ? 182  VAL A CA  1 
ATOM   1274 C C   . VAL A 1 182 ? 7.160   2.715   13.746  1.00 19.81 ? 182  VAL A C   1 
ATOM   1275 O O   . VAL A 1 182 ? 7.021   1.550   13.297  1.00 20.63 ? 182  VAL A O   1 
ATOM   1276 C CB  . VAL A 1 182 ? 9.344   4.025   13.759  1.00 22.39 ? 182  VAL A CB  1 
ATOM   1277 C CG1 . VAL A 1 182 ? 9.997   2.787   14.350  1.00 24.14 ? 182  VAL A CG1 1 
ATOM   1278 C CG2 . VAL A 1 182 ? 10.316  4.775   12.871  1.00 23.66 ? 182  VAL A CG2 1 
ATOM   1279 N N   . PHE A 1 183 ? 6.560   3.156   14.857  1.00 21.01 ? 183  PHE A N   1 
ATOM   1280 C CA  . PHE A 1 183 ? 5.693   2.317   15.733  1.00 21.93 ? 183  PHE A CA  1 
ATOM   1281 C C   . PHE A 1 183 ? 4.442   1.864   14.969  1.00 21.94 ? 183  PHE A C   1 
ATOM   1282 O O   . PHE A 1 183 ? 4.017   0.694   15.136  1.00 21.59 ? 183  PHE A O   1 
ATOM   1283 C CB  . PHE A 1 183 ? 5.311   3.087   16.999  1.00 24.81 ? 183  PHE A CB  1 
ATOM   1284 C CG  . PHE A 1 183 ? 6.412   3.274   18.014  1.00 25.46 ? 183  PHE A CG  1 
ATOM   1285 C CD1 . PHE A 1 183 ? 7.562   2.504   17.982  1.00 28.70 ? 183  PHE A CD1 1 
ATOM   1286 C CD2 . PHE A 1 183 ? 6.260   4.196   19.037  1.00 27.56 ? 183  PHE A CD2 1 
ATOM   1287 C CE1 . PHE A 1 183 ? 8.558   2.674   18.936  1.00 31.76 ? 183  PHE A CE1 1 
ATOM   1288 C CE2 . PHE A 1 183 ? 7.247   4.362   19.995  1.00 31.75 ? 183  PHE A CE2 1 
ATOM   1289 C CZ  . PHE A 1 183 ? 8.399   3.598   19.943  1.00 31.21 ? 183  PHE A CZ  1 
ATOM   1290 N N   . GLU A 1 184 ? 3.858   2.751   14.154  1.00 21.53 ? 184  GLU A N   1 
ATOM   1291 C CA  . GLU A 1 184 ? 2.637   2.434   13.372  1.00 22.75 ? 184  GLU A CA  1 
ATOM   1292 C C   . GLU A 1 184 ? 2.975   1.245   12.469  1.00 22.59 ? 184  GLU A C   1 
ATOM   1293 O O   . GLU A 1 184 ? 2.215   0.267   12.497  1.00 20.39 ? 184  GLU A O   1 
ATOM   1294 C CB  . GLU A 1 184 ? 2.180   3.635   12.545  1.00 22.17 ? 184  GLU A CB  1 
ATOM   1295 C CG  . GLU A 1 184 ? 0.849   3.413   11.849  1.00 23.95 ? 184  GLU A CG  1 
ATOM   1296 C CD  . GLU A 1 184 ? 0.379   4.581   10.989  1.00 26.39 ? 184  GLU A CD  1 
ATOM   1297 O OE1 . GLU A 1 184 ? -0.757  4.532   10.469  1.00 27.41 ? 184  GLU A OE1 1 
ATOM   1298 O OE2 . GLU A 1 184 ? 1.142   5.563   10.870  1.00 31.31 ? 184  GLU A OE2 1 
ATOM   1299 N N   . GLY A 1 185 ? 4.099   1.344   11.738  1.00 22.54 ? 185  GLY A N   1 
ATOM   1300 C CA  . GLY A 1 185 ? 4.567   0.304   10.798  1.00 22.75 ? 185  GLY A CA  1 
ATOM   1301 C C   . GLY A 1 185 ? 4.895   -0.972  11.547  1.00 23.52 ? 185  GLY A C   1 
ATOM   1302 O O   . GLY A 1 185 ? 4.541   -2.061  11.068  1.00 23.57 ? 185  GLY A O   1 
ATOM   1303 N N   . TRP A 1 186 ? 5.562   -0.829  12.692  1.00 24.82 ? 186  TRP A N   1 
ATOM   1304 C CA  . TRP A 1 186 ? 6.108   -1.960  13.488  1.00 24.90 ? 186  TRP A CA  1 
ATOM   1305 C C   . TRP A 1 186 ? 4.931   -2.754  14.040  1.00 23.29 ? 186  TRP A C   1 
ATOM   1306 O O   . TRP A 1 186 ? 4.901   -3.971  13.828  1.00 24.03 ? 186  TRP A O   1 
ATOM   1307 C CB  . TRP A 1 186 ? 7.018   -1.454  14.606  1.00 27.01 ? 186  TRP A CB  1 
ATOM   1308 C CG  . TRP A 1 186 ? 7.699   -2.537  15.386  1.00 29.15 ? 186  TRP A CG  1 
ATOM   1309 C CD1 . TRP A 1 186 ? 7.581   -2.789  16.723  1.00 30.16 ? 186  TRP A CD1 1 
ATOM   1310 C CD2 . TRP A 1 186 ? 8.626   -3.507  14.878  1.00 29.84 ? 186  TRP A CD2 1 
ATOM   1311 N NE1 . TRP A 1 186 ? 8.410   -3.814  17.092  1.00 29.79 ? 186  TRP A NE1 1 
ATOM   1312 C CE2 . TRP A 1 186 ? 9.058   -4.280  15.982  1.00 31.73 ? 186  TRP A CE2 1 
ATOM   1313 C CE3 . TRP A 1 186 ? 9.177   -3.754  13.618  1.00 30.26 ? 186  TRP A CE3 1 
ATOM   1314 C CZ2 . TRP A 1 186 ? 9.980   -5.313  15.847  1.00 32.61 ? 186  TRP A CZ2 1 
ATOM   1315 C CZ3 . TRP A 1 186 ? 10.097  -4.769  13.489  1.00 33.29 ? 186  TRP A CZ3 1 
ATOM   1316 C CH2 . TRP A 1 186 ? 10.494  -5.531  14.590  1.00 33.97 ? 186  TRP A CH2 1 
ATOM   1317 N N   . VAL A 1 187 ? 3.965   -2.062  14.640  1.00 23.29 ? 187  VAL A N   1 
ATOM   1318 C CA  . VAL A 1 187 ? 2.703   -2.670  15.151  1.00 23.04 ? 187  VAL A CA  1 
ATOM   1319 C C   . VAL A 1 187 ? 1.962   -3.375  14.000  1.00 23.54 ? 187  VAL A C   1 
ATOM   1320 O O   . VAL A 1 187 ? 1.464   -4.500  14.208  1.00 25.12 ? 187  VAL A O   1 
ATOM   1321 C CB  . VAL A 1 187 ? 1.825   -1.597  15.814  1.00 24.66 ? 187  VAL A CB  1 
ATOM   1322 C CG1 . VAL A 1 187 ? 0.394   -2.077  16.001  1.00 24.34 ? 187  VAL A CG1 1 
ATOM   1323 C CG2 . VAL A 1 187 ? 2.437   -1.136  17.131  1.00 24.80 ? 187  VAL A CG2 1 
ATOM   1324 N N   . GLN A 1 188 ? 1.862   -2.752  12.827  1.00 21.90 ? 188  GLN A N   1 
ATOM   1325 C CA  . GLN A 1 188 ? 1.228   -3.415  11.653  1.00 23.54 ? 188  GLN A CA  1 
ATOM   1326 C C   . GLN A 1 188 ? 2.027   -4.672  11.280  1.00 22.63 ? 188  GLN A C   1 
ATOM   1327 O O   . GLN A 1 188 ? 1.414   -5.740  11.117  1.00 24.96 ? 188  GLN A O   1 
ATOM   1328 C CB  . GLN A 1 188 ? 1.159   -2.481  10.452  1.00 23.62 ? 188  GLN A CB  1 
ATOM   1329 C CG  . GLN A 1 188 ? 0.555   -3.158  9.237   1.00 23.91 ? 188  GLN A CG  1 
ATOM   1330 C CD  . GLN A 1 188 ? -0.937  -3.279  9.380   1.00 25.29 ? 188  GLN A CD  1 
ATOM   1331 O OE1 . GLN A 1 188 ? -1.632  -2.282  9.383   1.00 32.98 ? 188  GLN A OE1 1 
ATOM   1332 N NE2 . GLN A 1 188 ? -1.433  -4.492  9.536   1.00 24.17 ? 188  GLN A NE2 1 
ATOM   1333 N N   . ALA A 1 189 ? 3.356   -4.562  11.196  1.00 21.21 ? 189  ALA A N   1 
ATOM   1334 C CA  . ALA A 1 189 ? 4.252   -5.705  10.882  1.00 22.57 ? 189  ALA A CA  1 
ATOM   1335 C C   . ALA A 1 189 ? 4.015   -6.857  11.869  1.00 22.20 ? 189  ALA A C   1 
ATOM   1336 O O   . ALA A 1 189 ? 3.819   -8.006  11.388  1.00 19.76 ? 189  ALA A O   1 
ATOM   1337 C CB  . ALA A 1 189 ? 5.687   -5.266  10.890  1.00 23.75 ? 189  ALA A CB  1 
ATOM   1338 N N   . LEU A 1 190 ? 3.993   -6.569  13.178  1.00 20.36 ? 190  LEU A N   1 
ATOM   1339 C CA  . LEU A 1 190 ? 3.889   -7.612  14.234  1.00 21.31 ? 190  LEU A CA  1 
ATOM   1340 C C   . LEU A 1 190 ? 2.496   -8.287  14.224  1.00 22.42 ? 190  LEU A C   1 
ATOM   1341 O O   . LEU A 1 190 ? 2.431   -9.507  14.519  1.00 23.29 ? 190  LEU A O   1 
ATOM   1342 C CB  . LEU A 1 190 ? 4.222   -6.993  15.593  1.00 21.16 ? 190  LEU A CB  1 
ATOM   1343 C CG  . LEU A 1 190 ? 5.680   -6.554  15.785  1.00 22.10 ? 190  LEU A CG  1 
ATOM   1344 C CD1 . LEU A 1 190 ? 5.887   -6.009  17.173  1.00 22.12 ? 190  LEU A CD1 1 
ATOM   1345 C CD2 . LEU A 1 190 ? 6.641   -7.704  15.528  1.00 22.60 ? 190  LEU A CD2 1 
ATOM   1346 N N   . ALA A 1 191 ? 1.429   -7.556  13.890  1.00 22.52 ? 191  ALA A N   1 
ATOM   1347 C CA  . ALA A 1 191 ? 0.042   -8.075  13.853  1.00 23.45 ? 191  ALA A CA  1 
ATOM   1348 C C   . ALA A 1 191 ? -0.045  -9.080  12.707  1.00 24.16 ? 191  ALA A C   1 
ATOM   1349 O O   . ALA A 1 191 ? -0.529  -10.206 12.932  1.00 27.57 ? 191  ALA A O   1 
ATOM   1350 C CB  . ALA A 1 191 ? -0.948  -6.946  13.704  1.00 22.64 ? 191  ALA A CB  1 
ATOM   1351 N N   . ILE A 1 192 ? 0.497   -8.717  11.542  1.00 22.66 ? 192  ILE A N   1 
ATOM   1352 C CA  . ILE A 1 192 ? 0.510   -9.627  10.361  1.00 23.36 ? 192  ILE A CA  1 
ATOM   1353 C C   . ILE A 1 192 ? 1.296   -10.892 10.720  1.00 24.16 ? 192  ILE A C   1 
ATOM   1354 O O   . ILE A 1 192 ? 0.690   -11.967 10.615  1.00 21.84 ? 192  ILE A O   1 
ATOM   1355 C CB  . ILE A 1 192 ? 1.025   -8.939  9.083   1.00 22.52 ? 192  ILE A CB  1 
ATOM   1356 C CG1 . ILE A 1 192 ? 0.017   -7.883  8.606   1.00 22.41 ? 192  ILE A CG1 1 
ATOM   1357 C CG2 . ILE A 1 192 ? 1.316   -9.962  8.001   1.00 22.57 ? 192  ILE A CG2 1 
ATOM   1358 C CD1 . ILE A 1 192 ? 0.582   -6.829  7.676   1.00 22.02 ? 192  ILE A CD1 1 
ATOM   1359 N N   . VAL A 1 193 ? 2.585   -10.788 11.088  1.00 23.61 ? 193  VAL A N   1 
ATOM   1360 C CA  . VAL A 1 193 ? 3.431   -12.004 11.263  1.00 25.00 ? 193  VAL A CA  1 
ATOM   1361 C C   . VAL A 1 193 ? 2.818   -12.838 12.403  1.00 24.73 ? 193  VAL A C   1 
ATOM   1362 O O   . VAL A 1 193 ? 2.679   -14.065 12.240  1.00 25.75 ? 193  VAL A O   1 
ATOM   1363 C CB  . VAL A 1 193 ? 4.931   -11.685 11.458  1.00 26.49 ? 193  VAL A CB  1 
ATOM   1364 C CG1 . VAL A 1 193 ? 5.488   -10.829 10.316  1.00 27.20 ? 193  VAL A CG1 1 
ATOM   1365 C CG2 . VAL A 1 193 ? 5.238   -11.041 12.796  1.00 25.28 ? 193  VAL A CG2 1 
ATOM   1366 N N   . GLY A 1 194 ? 2.392   -12.183 13.481  1.00 24.13 ? 194  GLY A N   1 
ATOM   1367 C CA  . GLY A 1 194 ? 1.743   -12.814 14.646  1.00 25.14 ? 194  GLY A CA  1 
ATOM   1368 C C   . GLY A 1 194 ? 0.521   -13.634 14.263  1.00 26.26 ? 194  GLY A C   1 
ATOM   1369 O O   . GLY A 1 194 ? 0.473   -14.837 14.617  1.00 23.89 ? 194  GLY A O   1 
ATOM   1370 N N   . LYS A 1 195 ? -0.438  -13.016 13.572  1.00 26.70 ? 195  LYS A N   1 
ATOM   1371 C CA  . LYS A 1 195 ? -1.707  -13.688 13.193  1.00 29.53 ? 195  LYS A CA  1 
ATOM   1372 C C   . LYS A 1 195 ? -1.367  -14.876 12.298  1.00 30.32 ? 195  LYS A C   1 
ATOM   1373 O O   . LYS A 1 195 ? -1.999  -15.918 12.480  1.00 32.36 ? 195  LYS A O   1 
ATOM   1374 C CB  . LYS A 1 195 ? -2.698  -12.732 12.525  1.00 30.17 ? 195  LYS A CB  1 
ATOM   1375 C CG  . LYS A 1 195 ? -4.095  -12.756 13.126  1.00 34.00 ? 195  LYS A CG  1 
ATOM   1376 C CD  . LYS A 1 195 ? -4.829  -14.058 12.981  1.00 36.34 ? 195  LYS A CD  1 
ATOM   1377 C CE  . LYS A 1 195 ? -6.158  -14.055 13.696  1.00 38.89 ? 195  LYS A CE  1 
ATOM   1378 N NZ  . LYS A 1 195 ? -7.034  -12.958 13.212  1.00 40.31 ? 195  LYS A NZ  1 
ATOM   1379 N N   . ALA A 1 196 ? -0.370  -14.752 11.419  1.00 30.48 ? 196  ALA A N   1 
ATOM   1380 C CA  . ALA A 1 196 ? -0.019  -15.811 10.441  1.00 31.81 ? 196  ALA A CA  1 
ATOM   1381 C C   . ALA A 1 196 ? 0.771   -16.930 11.140  1.00 35.53 ? 196  ALA A C   1 
ATOM   1382 O O   . ALA A 1 196 ? 1.156   -17.904 10.455  1.00 33.80 ? 196  ALA A O   1 
ATOM   1383 C CB  . ALA A 1 196 ? 0.765   -15.209 9.297   1.00 31.93 ? 196  ALA A CB  1 
ATOM   1384 N N   . GLY A 1 197 ? 1.046   -16.772 12.440  1.00 35.08 ? 197  GLY A N   1 
ATOM   1385 C CA  . GLY A 1 197 ? 1.574   -17.842 13.307  1.00 34.51 ? 197  GLY A CA  1 
ATOM   1386 C C   . GLY A 1 197 ? 3.089   -17.802 13.403  1.00 33.59 ? 197  GLY A C   1 
ATOM   1387 O O   . GLY A 1 197 ? 3.670   -18.798 13.849  1.00 32.00 ? 197  GLY A O   1 
ATOM   1388 N N   . GLU A 1 198 ? 3.719   -16.691 12.998  1.00 33.22 ? 198  GLU A N   1 
ATOM   1389 C CA  . GLU A 1 198 ? 5.179   -16.482 13.171  1.00 29.83 ? 198  GLU A CA  1 
ATOM   1390 C C   . GLU A 1 198 ? 5.472   -15.996 14.587  1.00 27.87 ? 198  GLU A C   1 
ATOM   1391 O O   . GLU A 1 198 ? 4.610   -15.333 15.237  1.00 28.84 ? 198  GLU A O   1 
ATOM   1392 C CB  . GLU A 1 198 ? 5.755   -15.451 12.197  1.00 31.01 ? 198  GLU A CB  1 
ATOM   1393 C CG  . GLU A 1 198 ? 5.535   -15.788 10.738  1.00 31.38 ? 198  GLU A CG  1 
ATOM   1394 C CD  . GLU A 1 198 ? 6.285   -16.997 10.214  1.00 31.70 ? 198  GLU A CD  1 
ATOM   1395 O OE1 . GLU A 1 198 ? 5.670   -17.798 9.508   1.00 31.74 ? 198  GLU A OE1 1 
ATOM   1396 O OE2 . GLU A 1 198 ? 7.499   -17.092 10.449  1.00 38.69 ? 198  GLU A OE2 1 
ATOM   1397 N N   . ASP A 1 199 ? 6.699   -16.247 15.000  1.00 26.73 ? 199  ASP A N   1 
ATOM   1398 C CA  . ASP A 1 199 ? 7.282   -15.742 16.257  1.00 27.80 ? 199  ASP A CA  1 
ATOM   1399 C C   . ASP A 1 199 ? 7.766   -14.309 16.020  1.00 28.24 ? 199  ASP A C   1 
ATOM   1400 O O   . ASP A 1 199 ? 8.535   -14.111 15.080  1.00 25.59 ? 199  ASP A O   1 
ATOM   1401 C CB  . ASP A 1 199 ? 8.418   -16.648 16.704  1.00 30.77 ? 199  ASP A CB  1 
ATOM   1402 C CG  . ASP A 1 199 ? 8.972   -16.236 18.041  1.00 31.10 ? 199  ASP A CG  1 
ATOM   1403 O OD1 . ASP A 1 199 ? 9.781   -15.295 18.062  1.00 33.16 ? 199  ASP A OD1 1 
ATOM   1404 O OD2 . ASP A 1 199 ? 8.552   -16.836 19.029  1.00 33.07 ? 199  ASP A OD2 1 
ATOM   1405 N N   . GLU A 1 200 ? 7.303   -13.364 16.843  1.00 24.94 ? 200  GLU A N   1 
ATOM   1406 C CA  . GLU A 1 200 ? 7.560   -11.914 16.685  1.00 25.62 ? 200  GLU A CA  1 
ATOM   1407 C C   . GLU A 1 200 ? 9.037   -11.630 16.977  1.00 24.07 ? 200  GLU A C   1 
ATOM   1408 O O   . GLU A 1 200 ? 9.602   -10.727 16.338  1.00 23.38 ? 200  GLU A O   1 
ATOM   1409 C CB  . GLU A 1 200 ? 6.645   -11.130 17.621  1.00 25.39 ? 200  GLU A CB  1 
ATOM   1410 C CG  . GLU A 1 200 ? 5.176   -11.256 17.277  1.00 26.69 ? 200  GLU A CG  1 
ATOM   1411 C CD  . GLU A 1 200 ? 4.408   -12.362 17.980  1.00 26.71 ? 200  GLU A CD  1 
ATOM   1412 O OE1 . GLU A 1 200 ? 3.183   -12.266 18.005  1.00 28.44 ? 200  GLU A OE1 1 
ATOM   1413 O OE2 . GLU A 1 200 ? 5.035   -13.319 18.482  1.00 27.64 ? 200  GLU A OE2 1 
ATOM   1414 N N   . VAL A 1 201 ? 9.653   -12.380 17.893  1.00 26.05 ? 201  VAL A N   1 
ATOM   1415 C CA  . VAL A 1 201 ? 11.090  -12.179 18.248  1.00 27.30 ? 201  VAL A CA  1 
ATOM   1416 C C   . VAL A 1 201 ? 11.959  -12.618 17.054  1.00 27.45 ? 201  VAL A C   1 
ATOM   1417 O O   . VAL A 1 201 ? 12.926  -11.891 16.719  1.00 29.37 ? 201  VAL A O   1 
ATOM   1418 C CB  . VAL A 1 201 ? 11.484  -12.886 19.562  1.00 28.03 ? 201  VAL A CB  1 
ATOM   1419 C CG1 . VAL A 1 201 ? 12.997  -12.911 19.741  1.00 29.27 ? 201  VAL A CG1 1 
ATOM   1420 C CG2 . VAL A 1 201 ? 10.835  -12.231 20.770  1.00 28.18 ? 201  VAL A CG2 1 
ATOM   1421 N N   . ASP A 1 202 ? 11.652  -13.755 16.429  1.00 29.02 ? 202  ASP A N   1 
ATOM   1422 C CA  . ASP A 1 202 ? 12.382  -14.249 15.228  1.00 29.66 ? 202  ASP A CA  1 
ATOM   1423 C C   . ASP A 1 202 ? 12.182  -13.278 14.056  1.00 29.18 ? 202  ASP A C   1 
ATOM   1424 O O   . ASP A 1 202 ? 13.174  -13.010 13.332  1.00 26.93 ? 202  ASP A O   1 
ATOM   1425 C CB  . ASP A 1 202 ? 11.942  -15.657 14.829  1.00 31.74 ? 202  ASP A CB  1 
ATOM   1426 C CG  . ASP A 1 202 ? 12.356  -16.713 15.846  1.00 34.40 ? 202  ASP A CG  1 
ATOM   1427 O OD1 . ASP A 1 202 ? 13.203  -16.394 16.720  1.00 32.25 ? 202  ASP A OD1 1 
ATOM   1428 O OD2 . ASP A 1 202 ? 11.831  -17.851 15.747  1.00 32.88 ? 202  ASP A OD2 1 
ATOM   1429 N N   . PHE A 1 203 ? 10.962  -12.767 13.873  1.00 25.66 ? 203  PHE A N   1 
ATOM   1430 C CA  . PHE A 1 203 ? 10.651  -11.763 12.824  1.00 25.79 ? 203  PHE A CA  1 
ATOM   1431 C C   . PHE A 1 203 ? 11.484  -10.497 13.065  1.00 23.57 ? 203  PHE A C   1 
ATOM   1432 O O   . PHE A 1 203 ? 12.060  -9.936  12.113  1.00 25.53 ? 203  PHE A O   1 
ATOM   1433 C CB  . PHE A 1 203 ? 9.160   -11.403 12.765  1.00 24.46 ? 203  PHE A CB  1 
ATOM   1434 C CG  . PHE A 1 203 ? 8.912   -10.291 11.776  1.00 25.20 ? 203  PHE A CG  1 
ATOM   1435 C CD1 . PHE A 1 203 ? 9.137   -10.498 10.421  1.00 25.56 ? 203  PHE A CD1 1 
ATOM   1436 C CD2 . PHE A 1 203 ? 8.606   -9.007  12.204  1.00 25.16 ? 203  PHE A CD2 1 
ATOM   1437 C CE1 . PHE A 1 203 ? 8.972   -9.473  9.497   1.00 25.02 ? 203  PHE A CE1 1 
ATOM   1438 C CE2 . PHE A 1 203 ? 8.443   -7.985  11.285  1.00 25.26 ? 203  PHE A CE2 1 
ATOM   1439 C CZ  . PHE A 1 203 ? 8.642   -8.215  9.933   1.00 25.16 ? 203  PHE A CZ  1 
ATOM   1440 N N   . ALA A 1 204 ? 11.524  -10.023 14.302  1.00 24.48 ? 204  ALA A N   1 
ATOM   1441 C CA  . ALA A 1 204 ? 12.307  -8.823  14.670  1.00 26.21 ? 204  ALA A CA  1 
ATOM   1442 C C   . ALA A 1 204 ? 13.794  -9.057  14.357  1.00 26.20 ? 204  ALA A C   1 
ATOM   1443 O O   . ALA A 1 204 ? 14.412  -8.133  13.826  1.00 25.26 ? 204  ALA A O   1 
ATOM   1444 C CB  . ALA A 1 204 ? 12.059  -8.446  16.109  1.00 26.48 ? 204  ALA A CB  1 
ATOM   1445 N N   . ALA A 1 205 ? 14.353  -10.244 14.617  1.00 27.17 ? 205  ALA A N   1 
ATOM   1446 C CA  . ALA A 1 205 ? 15.771  -10.538 14.282  1.00 29.37 ? 205  ALA A CA  1 
ATOM   1447 C C   . ALA A 1 205 ? 15.960  -10.386 12.767  1.00 30.05 ? 205  ALA A C   1 
ATOM   1448 O O   . ALA A 1 205 ? 16.962  -9.766  12.313  1.00 27.33 ? 205  ALA A O   1 
ATOM   1449 C CB  . ALA A 1 205 ? 16.183  -11.918 14.744  1.00 30.12 ? 205  ALA A CB  1 
ATOM   1450 N N   . LEU A 1 206 ? 15.016  -10.913 11.993  1.00 30.51 ? 206  LEU A N   1 
ATOM   1451 C CA  . LEU A 1 206 ? 15.096  -10.870 10.514  1.00 30.53 ? 206  LEU A CA  1 
ATOM   1452 C C   . LEU A 1 206 ? 14.950  -9.413  10.037  1.00 27.40 ? 206  LEU A C   1 
ATOM   1453 O O   . LEU A 1 206 ? 15.696  -9.017  9.113   1.00 29.44 ? 206  LEU A O   1 
ATOM   1454 C CB  . LEU A 1 206 ? 14.042  -11.824 9.938   1.00 34.11 ? 206  LEU A CB  1 
ATOM   1455 C CG  . LEU A 1 206 ? 13.980  -11.877 8.409   1.00 35.72 ? 206  LEU A CG  1 
ATOM   1456 C CD1 . LEU A 1 206 ? 13.598  -13.272 7.909   1.00 36.04 ? 206  LEU A CD1 1 
ATOM   1457 C CD2 . LEU A 1 206 ? 13.029  -10.824 7.863   1.00 32.77 ? 206  LEU A CD2 1 
ATOM   1458 N N   . ALA A 1 207 ? 14.092  -8.618  10.677  1.00 25.43 ? 207  ALA A N   1 
ATOM   1459 C CA  . ALA A 1 207 ? 13.725  -7.238  10.259  1.00 25.07 ? 207  ALA A CA  1 
ATOM   1460 C C   . ALA A 1 207 ? 14.856  -6.220  10.517  1.00 29.05 ? 207  ALA A C   1 
ATOM   1461 O O   . ALA A 1 207 ? 14.991  -5.227  9.730   1.00 25.19 ? 207  ALA A O   1 
ATOM   1462 C CB  . ALA A 1 207 ? 12.489  -6.831  11.006  1.00 23.53 ? 207  ALA A CB  1 
ATOM   1463 N N   . SER A 1 208 ? 15.615  -6.397  11.605  1.00 30.07 ? 208  SER A N   1 
ATOM   1464 C CA  . SER A 1 208 ? 16.527  -5.353  12.148  1.00 32.58 ? 208  SER A CA  1 
ATOM   1465 C C   . SER A 1 208 ? 17.478  -4.866  11.061  1.00 32.00 ? 208  SER A C   1 
ATOM   1466 O O   . SER A 1 208 ? 17.579  -3.666  10.856  1.00 31.06 ? 208  SER A O   1 
ATOM   1467 C CB  . SER A 1 208 ? 17.260  -5.821  13.384  1.00 35.83 ? 208  SER A CB  1 
ATOM   1468 O OG  . SER A 1 208 ? 16.404  -5.744  14.524  1.00 37.14 ? 208  SER A OG  1 
ATOM   1469 N N   . PRO A 1 209 ? 18.169  -5.755  10.307  1.00 32.27 ? 209  PRO A N   1 
ATOM   1470 C CA  . PRO A 1 209 ? 19.028  -5.321  9.206   1.00 32.90 ? 209  PRO A CA  1 
ATOM   1471 C C   . PRO A 1 209 ? 18.279  -4.492  8.151   1.00 31.44 ? 209  PRO A C   1 
ATOM   1472 O O   . PRO A 1 209 ? 18.820  -3.498  7.703   1.00 32.38 ? 209  PRO A O   1 
ATOM   1473 C CB  . PRO A 1 209 ? 19.564  -6.637  8.611   1.00 33.49 ? 209  PRO A CB  1 
ATOM   1474 C CG  . PRO A 1 209 ? 19.483  -7.616  9.751   1.00 33.17 ? 209  PRO A CG  1 
ATOM   1475 C CD  . PRO A 1 209 ? 18.221  -7.213  10.490  1.00 34.70 ? 209  PRO A CD  1 
ATOM   1476 N N   . PHE A 1 210 ? 17.053  -4.890  7.799   1.00 30.51 ? 210  PHE A N   1 
ATOM   1477 C CA  . PHE A 1 210 ? 16.196  -4.153  6.831   1.00 29.38 ? 210  PHE A CA  1 
ATOM   1478 C C   . PHE A 1 210 ? 15.797  -2.794  7.410   1.00 28.58 ? 210  PHE A C   1 
ATOM   1479 O O   . PHE A 1 210 ? 15.840  -1.797  6.675   1.00 26.14 ? 210  PHE A O   1 
ATOM   1480 C CB  . PHE A 1 210 ? 14.989  -4.998  6.414   1.00 30.41 ? 210  PHE A CB  1 
ATOM   1481 C CG  . PHE A 1 210 ? 15.383  -6.261  5.694   1.00 28.95 ? 210  PHE A CG  1 
ATOM   1482 C CD1 . PHE A 1 210 ? 15.821  -6.216  4.381   1.00 29.40 ? 210  PHE A CD1 1 
ATOM   1483 C CD2 . PHE A 1 210 ? 15.358  -7.487  6.342   1.00 30.49 ? 210  PHE A CD2 1 
ATOM   1484 C CE1 . PHE A 1 210 ? 16.207  -7.376  3.722   1.00 32.70 ? 210  PHE A CE1 1 
ATOM   1485 C CE2 . PHE A 1 210 ? 15.752  -8.646  5.691   1.00 29.03 ? 210  PHE A CE2 1 
ATOM   1486 C CZ  . PHE A 1 210 ? 16.170  -8.591  4.381   1.00 33.31 ? 210  PHE A CZ  1 
ATOM   1487 N N   . VAL A 1 211 ? 15.477  -2.725  8.697   1.00 30.01 ? 211  VAL A N   1 
ATOM   1488 C CA  . VAL A 1 211 ? 15.062  -1.441  9.343   1.00 31.85 ? 211  VAL A CA  1 
ATOM   1489 C C   . VAL A 1 211 ? 16.256  -0.482  9.355   1.00 33.93 ? 211  VAL A C   1 
ATOM   1490 O O   . VAL A 1 211 ? 16.046  0.729   9.164   1.00 31.92 ? 211  VAL A O   1 
ATOM   1491 C CB  . VAL A 1 211 ? 14.484  -1.656  10.755  1.00 33.25 ? 211  VAL A CB  1 
ATOM   1492 C CG1 . VAL A 1 211 ? 14.233  -0.332  11.470  1.00 32.24 ? 211  VAL A CG1 1 
ATOM   1493 C CG2 . VAL A 1 211 ? 13.213  -2.494  10.697  1.00 33.70 ? 211  VAL A CG2 1 
ATOM   1494 N N   . LYS A 1 212 ? 17.470  -1.003  9.543   1.00 41.32 ? 212  LYS A N   1 
ATOM   1495 C CA  . LYS A 1 212 ? 18.719  -0.190  9.516   1.00 44.75 ? 212  LYS A CA  1 
ATOM   1496 C C   . LYS A 1 212 ? 18.921  0.397   8.116   1.00 41.54 ? 212  LYS A C   1 
ATOM   1497 O O   . LYS A 1 212 ? 19.298  1.569   8.033   1.00 41.39 ? 212  LYS A O   1 
ATOM   1498 C CB  . LYS A 1 212 ? 19.930  -1.011  9.966   1.00 51.65 ? 212  LYS A CB  1 
ATOM   1499 C CG  . LYS A 1 212 ? 20.391  -0.708  11.385  1.00 59.10 ? 212  LYS A CG  1 
ATOM   1500 C CD  . LYS A 1 212 ? 19.273  -0.698  12.426  1.00 61.38 ? 212  LYS A CD  1 
ATOM   1501 C CE  . LYS A 1 212 ? 19.768  -0.926  13.845  1.00 62.02 ? 212  LYS A CE  1 
ATOM   1502 N NZ  . LYS A 1 212 ? 20.256  0.327   14.472  1.00 64.52 ? 212  LYS A NZ  1 
ATOM   1503 N N   . SER A 1 213 ? 18.647  -0.371  7.060   1.00 40.65 ? 213  SER A N   1 
ATOM   1504 C CA  . SER A 1 213 ? 18.740  0.115   5.659   1.00 40.48 ? 213  SER A CA  1 
ATOM   1505 C C   . SER A 1 213 ? 17.763  1.272   5.454   1.00 37.17 ? 213  SER A C   1 
ATOM   1506 O O   . SER A 1 213 ? 18.181  2.305   4.918   1.00 40.64 ? 213  SER A O   1 
ATOM   1507 C CB  . SER A 1 213 ? 18.520  -0.982  4.674   1.00 39.78 ? 213  SER A CB  1 
ATOM   1508 O OG  . SER A 1 213 ? 19.571  -1.920  4.795   1.00 44.75 ? 213  SER A OG  1 
ATOM   1509 N N   . MET A 1 214 ? 16.523  1.125   5.903   1.00 36.18 ? 214  MET A N   1 
ATOM   1510 C CA  . MET A 1 214 ? 15.517  2.210   5.788   1.00 35.04 ? 214  MET A CA  1 
ATOM   1511 C C   . MET A 1 214 ? 16.118  3.451   6.467   1.00 33.31 ? 214  MET A C   1 
ATOM   1512 O O   . MET A 1 214 ? 16.166  4.495   5.829   1.00 30.64 ? 214  MET A O   1 
ATOM   1513 C CB  . MET A 1 214 ? 14.171  1.798   6.398   1.00 35.98 ? 214  MET A CB  1 
ATOM   1514 C CG  . MET A 1 214 ? 13.595  0.517   5.762   1.00 39.10 ? 214  MET A CG  1 
ATOM   1515 S SD  . MET A 1 214 ? 12.065  -0.163  6.537   1.00 41.01 ? 214  MET A SD  1 
ATOM   1516 C CE  . MET A 1 214 ? 12.075  -1.859  5.940   1.00 41.36 ? 214  MET A CE  1 
ATOM   1517 N N   . ALA A 1 215 ? 16.663  3.325   7.681   1.00 34.20 ? 215  ALA A N   1 
ATOM   1518 C CA  . ALA A 1 215 ? 17.245  4.463   8.432   1.00 33.01 ? 215  ALA A CA  1 
ATOM   1519 C C   . ALA A 1 215 ? 18.322  5.144   7.575   1.00 35.76 ? 215  ALA A C   1 
ATOM   1520 O O   . ALA A 1 215 ? 18.308  6.383   7.522   1.00 33.57 ? 215  ALA A O   1 
ATOM   1521 C CB  . ALA A 1 215 ? 17.792  3.997   9.754   1.00 33.63 ? 215  ALA A CB  1 
ATOM   1522 N N   . ASP A 1 216 ? 19.176  4.367   6.889   1.00 35.34 ? 216  ASP A N   1 
ATOM   1523 C CA  . ASP A 1 216 ? 20.295  4.889   6.050   1.00 39.41 ? 216  ASP A CA  1 
ATOM   1524 C C   . ASP A 1 216 ? 19.783  5.608   4.789   1.00 37.52 ? 216  ASP A C   1 
ATOM   1525 O O   . ASP A 1 216 ? 20.504  6.498   4.328   1.00 40.64 ? 216  ASP A O   1 
ATOM   1526 C CB  . ASP A 1 216 ? 21.277  3.782   5.649   1.00 41.00 ? 216  ASP A CB  1 
ATOM   1527 C CG  . ASP A 1 216 ? 22.120  3.216   6.789   1.00 43.89 ? 216  ASP A CG  1 
ATOM   1528 O OD1 . ASP A 1 216 ? 22.261  3.893   7.837   1.00 43.81 ? 216  ASP A OD1 1 
ATOM   1529 O OD2 . ASP A 1 216 ? 22.659  2.106   6.610   1.00 47.98 ? 216  ASP A OD2 1 
ATOM   1530 N N   . TRP A 1 217 ? 18.608  5.257   4.239   1.00 37.07 ? 217  TRP A N   1 
ATOM   1531 C CA  . TRP A 1 217 ? 18.016  5.942   3.047   1.00 34.49 ? 217  TRP A CA  1 
ATOM   1532 C C   . TRP A 1 217 ? 17.435  7.316   3.429   1.00 33.44 ? 217  TRP A C   1 
ATOM   1533 O O   . TRP A 1 217 ? 17.060  8.072   2.517   1.00 33.32 ? 217  TRP A O   1 
ATOM   1534 C CB  . TRP A 1 217 ? 16.923  5.093   2.370   1.00 36.07 ? 217  TRP A CB  1 
ATOM   1535 C CG  . TRP A 1 217 ? 17.307  3.687   2.023   1.00 37.47 ? 217  TRP A CG  1 
ATOM   1536 C CD1 . TRP A 1 217 ? 18.564  3.206   1.783   1.00 37.51 ? 217  TRP A CD1 1 
ATOM   1537 C CD2 . TRP A 1 217 ? 16.410  2.572   1.844   1.00 35.75 ? 217  TRP A CD2 1 
ATOM   1538 N NE1 . TRP A 1 217 ? 18.515  1.866   1.498   1.00 39.43 ? 217  TRP A NE1 1 
ATOM   1539 C CE2 . TRP A 1 217 ? 17.206  1.448   1.522   1.00 38.00 ? 217  TRP A CE2 1 
ATOM   1540 C CE3 . TRP A 1 217 ? 15.022  2.404   1.941   1.00 36.13 ? 217  TRP A CE3 1 
ATOM   1541 C CZ2 . TRP A 1 217 ? 16.655  0.182   1.286   1.00 37.68 ? 217  TRP A CZ2 1 
ATOM   1542 C CZ3 . TRP A 1 217 ? 14.481  1.156   1.697   1.00 37.80 ? 217  TRP A CZ3 1 
ATOM   1543 C CH2 . TRP A 1 217 ? 15.287  0.058   1.383   1.00 35.86 ? 217  TRP A CH2 1 
ATOM   1544 N N   . LEU A 1 218 ? 17.279  7.630   4.714   1.00 31.47 ? 218  LEU A N   1 
ATOM   1545 C CA  . LEU A 1 218 ? 16.468  8.810   5.125   1.00 31.87 ? 218  LEU A CA  1 
ATOM   1546 C C   . LEU A 1 218 ? 17.217  10.092  4.782   1.00 29.44 ? 218  LEU A C   1 
ATOM   1547 O O   . LEU A 1 218 ? 16.638  10.988  4.175   1.00 27.93 ? 218  LEU A O   1 
ATOM   1548 C CB  . LEU A 1 218 ? 16.096  8.703   6.606   1.00 30.90 ? 218  LEU A CB  1 
ATOM   1549 C CG  . LEU A 1 218 ? 15.227  7.493   6.951   1.00 31.83 ? 218  LEU A CG  1 
ATOM   1550 C CD1 . LEU A 1 218 ? 14.960  7.425   8.447   1.00 35.06 ? 218  LEU A CD1 1 
ATOM   1551 C CD2 . LEU A 1 218 ? 13.912  7.521   6.178   1.00 32.49 ? 218  LEU A CD2 1 
ATOM   1552 N N   . PRO A 1 219 ? 18.517  10.223  5.114   1.00 32.14 ? 219  PRO A N   1 
ATOM   1553 C CA  . PRO A 1 219 ? 19.289  11.399  4.696   1.00 34.54 ? 219  PRO A CA  1 
ATOM   1554 C C   . PRO A 1 219 ? 19.257  11.673  3.185   1.00 32.88 ? 219  PRO A C   1 
ATOM   1555 O O   . PRO A 1 219 ? 19.120  12.816  2.824   1.00 36.07 ? 219  PRO A O   1 
ATOM   1556 C CB  . PRO A 1 219 ? 20.723  11.071  5.141   1.00 34.61 ? 219  PRO A CB  1 
ATOM   1557 C CG  . PRO A 1 219 ? 20.523  10.126  6.311   1.00 35.59 ? 219  PRO A CG  1 
ATOM   1558 C CD  . PRO A 1 219 ? 19.312  9.297   5.935   1.00 33.26 ? 219  PRO A CD  1 
ATOM   1559 N N   . ARG A 1 220 ? 19.377  10.639  2.346   1.00 34.42 ? 220  ARG A N   1 
ATOM   1560 C CA  . ARG A 1 220 ? 19.321  10.784  0.861   1.00 34.93 ? 220  ARG A CA  1 
ATOM   1561 C C   . ARG A 1 220 ? 17.970  11.433  0.543   1.00 31.60 ? 220  ARG A C   1 
ATOM   1562 O O   . ARG A 1 220 ? 17.957  12.409  -0.225  1.00 30.65 ? 220  ARG A O   1 
ATOM   1563 C CB  . ARG A 1 220 ? 19.507  9.455   0.107   1.00 39.74 ? 220  ARG A CB  1 
ATOM   1564 C CG  . ARG A 1 220 ? 20.664  8.580   0.591   1.00 50.00 ? 220  ARG A CG  1 
ATOM   1565 C CD  . ARG A 1 220 ? 21.151  7.494   -0.386  1.00 56.41 ? 220  ARG A CD  1 
ATOM   1566 N NE  . ARG A 1 220 ? 20.271  6.324   -0.476  1.00 62.03 ? 220  ARG A NE  1 
ATOM   1567 C CZ  . ARG A 1 220 ? 20.436  5.269   -1.291  1.00 71.55 ? 220  ARG A CZ  1 
ATOM   1568 N NH1 . ARG A 1 220 ? 19.551  4.283   -1.278  1.00 71.46 ? 220  ARG A NH1 1 
ATOM   1569 N NH2 . ARG A 1 220 ? 21.466  5.200   -2.122  1.00 74.84 ? 220  ARG A NH2 1 
ATOM   1570 N N   . ILE A 1 221 ? 16.883  10.949  1.168   1.00 27.85 ? 221  ILE A N   1 
ATOM   1571 C CA  . ILE A 1 221 ? 15.507  11.466  0.937   1.00 25.55 ? 221  ILE A CA  1 
ATOM   1572 C C   . ILE A 1 221 ? 15.457  12.927  1.393   1.00 23.16 ? 221  ILE A C   1 
ATOM   1573 O O   . ILE A 1 221 ? 14.842  13.709  0.709   1.00 23.38 ? 221  ILE A O   1 
ATOM   1574 C CB  . ILE A 1 221 ? 14.409  10.604  1.606   1.00 26.20 ? 221  ILE A CB  1 
ATOM   1575 C CG1 . ILE A 1 221 ? 14.334  9.188   1.031   1.00 27.29 ? 221  ILE A CG1 1 
ATOM   1576 C CG2 . ILE A 1 221 ? 13.059  11.281  1.486   1.00 24.38 ? 221  ILE A CG2 1 
ATOM   1577 C CD1 . ILE A 1 221 ? 13.523  8.226   1.874   1.00 28.12 ? 221  ILE A CD1 1 
ATOM   1578 N N   . ALA A 1 222 ? 16.079  13.299  2.508   1.00 24.55 ? 222  ALA A N   1 
ATOM   1579 C CA  . ALA A 1 222 ? 16.016  14.688  3.018   1.00 24.99 ? 222  ALA A CA  1 
ATOM   1580 C C   . ALA A 1 222 ? 16.702  15.613  2.003   1.00 26.33 ? 222  ALA A C   1 
ATOM   1581 O O   . ALA A 1 222 ? 16.210  16.731  1.779   1.00 25.89 ? 222  ALA A O   1 
ATOM   1582 C CB  . ALA A 1 222 ? 16.638  14.773  4.393   1.00 24.65 ? 222  ALA A CB  1 
ATOM   1583 N N   . GLY A 1 223 ? 17.792  15.149  1.384   1.00 31.16 ? 223  GLY A N   1 
ATOM   1584 C CA  . GLY A 1 223 ? 18.488  15.875  0.299   1.00 32.47 ? 223  GLY A CA  1 
ATOM   1585 C C   . GLY A 1 223 ? 17.567  16.070  -0.892  1.00 33.77 ? 223  GLY A C   1 
ATOM   1586 O O   . GLY A 1 223 ? 17.416  17.212  -1.368  1.00 36.17 ? 223  GLY A O   1 
ATOM   1587 N N   . HIS A 1 224 ? 16.932  14.994  -1.343  1.00 33.29 ? 224  HIS A N   1 
ATOM   1588 C CA  . HIS A 1 224 ? 15.921  15.026  -2.428  1.00 35.25 ? 224  HIS A CA  1 
ATOM   1589 C C   . HIS A 1 224 ? 14.871  16.081  -2.098  1.00 35.64 ? 224  HIS A C   1 
ATOM   1590 O O   . HIS A 1 224 ? 14.525  16.864  -2.990  1.00 35.69 ? 224  HIS A O   1 
ATOM   1591 C CB  . HIS A 1 224 ? 15.302  13.641  -2.635  1.00 37.10 ? 224  HIS A CB  1 
ATOM   1592 C CG  . HIS A 1 224 ? 16.293  12.640  -3.109  1.00 40.87 ? 224  HIS A CG  1 
ATOM   1593 N ND1 . HIS A 1 224 ? 16.163  11.290  -2.844  1.00 45.14 ? 224  HIS A ND1 1 
ATOM   1594 C CD2 . HIS A 1 224 ? 17.448  12.798  -3.794  1.00 41.64 ? 224  HIS A CD2 1 
ATOM   1595 C CE1 . HIS A 1 224 ? 17.194  10.655  -3.362  1.00 45.36 ? 224  HIS A CE1 1 
ATOM   1596 N NE2 . HIS A 1 224 ? 17.991  11.560  -3.957  1.00 43.47 ? 224  HIS A NE2 1 
ATOM   1597 N N   . VAL A 1 225 ? 14.388  16.101  -0.855  1.00 33.30 ? 225  VAL A N   1 
ATOM   1598 C CA  . VAL A 1 225 ? 13.319  17.053  -0.437  1.00 31.44 ? 225  VAL A CA  1 
ATOM   1599 C C   . VAL A 1 225 ? 13.867  18.479  -0.575  1.00 30.53 ? 225  VAL A C   1 
ATOM   1600 O O   . VAL A 1 225 ? 13.192  19.304  -1.219  1.00 25.65 ? 225  VAL A O   1 
ATOM   1601 C CB  . VAL A 1 225 ? 12.786  16.757  0.984   1.00 29.23 ? 225  VAL A CB  1 
ATOM   1602 C CG1 . VAL A 1 225 ? 11.854  17.862  1.492   1.00 26.88 ? 225  VAL A CG1 1 
ATOM   1603 C CG2 . VAL A 1 225 ? 12.079  15.417  1.008   1.00 27.39 ? 225  VAL A CG2 1 
ATOM   1604 N N   . ARG A 1 226 ? 15.055  18.745  -0.029  1.00 33.97 ? 226  ARG A N   1 
ATOM   1605 C CA  . ARG A 1 226 ? 15.635  20.109  -0.017  1.00 34.95 ? 226  ARG A CA  1 
ATOM   1606 C C   . ARG A 1 226 ? 15.804  20.609  -1.452  1.00 35.49 ? 226  ARG A C   1 
ATOM   1607 O O   . ARG A 1 226 ? 15.471  21.777  -1.698  1.00 33.13 ? 226  ARG A O   1 
ATOM   1608 C CB  . ARG A 1 226 ? 16.995  20.168  0.672   1.00 34.64 ? 226  ARG A CB  1 
ATOM   1609 C CG  . ARG A 1 226 ? 17.528  21.591  0.709   1.00 35.37 ? 226  ARG A CG  1 
ATOM   1610 C CD  . ARG A 1 226 ? 18.728  21.762  1.583   1.00 35.98 ? 226  ARG A CD  1 
ATOM   1611 N NE  . ARG A 1 226 ? 19.847  21.087  0.963   1.00 38.94 ? 226  ARG A NE  1 
ATOM   1612 C CZ  . ARG A 1 226 ? 21.020  20.918  1.533   1.00 42.28 ? 226  ARG A CZ  1 
ATOM   1613 N NH1 . ARG A 1 226 ? 21.213  21.389  2.754   1.00 42.90 ? 226  ARG A NH1 1 
ATOM   1614 N NH2 . ARG A 1 226 ? 21.994  20.288  0.883   1.00 43.95 ? 226  ARG A NH2 1 
ATOM   1615 N N   . GLU A 1 227 ? 16.289  19.740  -2.343  1.00 37.50 ? 227  GLU A N   1 
ATOM   1616 C CA  . GLU A 1 227 ? 16.664  20.065  -3.748  1.00 37.92 ? 227  GLU A CA  1 
ATOM   1617 C C   . GLU A 1 227 ? 15.458  19.863  -4.677  1.00 36.96 ? 227  GLU A C   1 
ATOM   1618 O O   . GLU A 1 227 ? 15.624  19.993  -5.889  1.00 39.59 ? 227  GLU A O   1 
ATOM   1619 C CB  . GLU A 1 227 ? 17.835  19.184  -4.199  1.00 41.50 ? 227  GLU A CB  1 
ATOM   1620 C CG  . GLU A 1 227 ? 19.022  19.182  -3.248  1.00 44.89 ? 227  GLU A CG  1 
ATOM   1621 C CD  . GLU A 1 227 ? 19.565  20.561  -2.925  1.00 48.06 ? 227  GLU A CD  1 
ATOM   1622 O OE1 . GLU A 1 227 ? 20.093  20.734  -1.824  1.00 50.88 ? 227  GLU A OE1 1 
ATOM   1623 O OE2 . GLU A 1 227 ? 19.458  21.457  -3.782  1.00 53.43 ? 227  GLU A OE2 1 
ATOM   1624 N N   . LYS A 1 228 ? 14.288  19.540  -4.136  1.00 36.57 ? 228  LYS A N   1 
ATOM   1625 C CA  . LYS A 1 228 ? 13.081  19.209  -4.932  1.00 39.83 ? 228  LYS A CA  1 
ATOM   1626 C C   . LYS A 1 228 ? 13.445  18.251  -6.084  1.00 36.40 ? 228  LYS A C   1 
ATOM   1627 O O   . LYS A 1 228 ? 12.999  18.482  -7.208  1.00 33.44 ? 228  LYS A O   1 
ATOM   1628 C CB  . LYS A 1 228 ? 12.444  20.511  -5.424  1.00 42.85 ? 228  LYS A CB  1 
ATOM   1629 C CG  . LYS A 1 228 ? 12.168  21.526  -4.321  1.00 45.07 ? 228  LYS A CG  1 
ATOM   1630 C CD  . LYS A 1 228 ? 11.162  22.606  -4.706  1.00 45.21 ? 228  LYS A CD  1 
ATOM   1631 C CE  . LYS A 1 228 ? 10.938  23.617  -3.598  1.00 45.68 ? 228  LYS A CE  1 
ATOM   1632 N NZ  . LYS A 1 228 ? 12.228  24.097  -3.046  1.00 45.99 ? 228  LYS A NZ  1 
ATOM   1633 N N   . GLN A 1 229 ? 14.230  17.211  -5.807  1.00 33.43 ? 229  GLN A N   1 
ATOM   1634 C CA  . GLN A 1 229 ? 14.597  16.161  -6.792  1.00 33.98 ? 229  GLN A CA  1 
ATOM   1635 C C   . GLN A 1 229 ? 13.727  14.950  -6.466  1.00 32.46 ? 229  GLN A C   1 
ATOM   1636 O O   . GLN A 1 229 ? 14.001  14.274  -5.437  1.00 28.27 ? 229  GLN A O   1 
ATOM   1637 C CB  . GLN A 1 229 ? 16.092  15.846  -6.720  1.00 32.50 ? 229  GLN A CB  1 
ATOM   1638 C CG  . GLN A 1 229 ? 16.982  17.059  -6.971  1.00 33.15 ? 229  GLN A CG  1 
ATOM   1639 C CD  . GLN A 1 229 ? 16.935  17.472  -8.421  1.00 33.71 ? 229  GLN A CD  1 
ATOM   1640 O OE1 . GLN A 1 229 ? 17.477  16.795  -9.293  1.00 34.10 ? 229  GLN A OE1 1 
ATOM   1641 N NE2 . GLN A 1 229 ? 16.249  18.568  -8.693  1.00 30.47 ? 229  GLN A NE2 1 
ATOM   1642 N N   . TYR A 1 230 ? 12.717  14.725  -7.306  1.00 30.71 ? 230  TYR A N   1 
ATOM   1643 C CA  . TYR A 1 230 ? 11.601  13.780  -7.083  1.00 31.59 ? 230  TYR A CA  1 
ATOM   1644 C C   . TYR A 1 230 ? 11.689  12.546  -7.990  1.00 33.66 ? 230  TYR A C   1 
ATOM   1645 O O   . TYR A 1 230 ? 10.771  11.705  -7.873  1.00 34.40 ? 230  TYR A O   1 
ATOM   1646 C CB  . TYR A 1 230 ? 10.303  14.540  -7.315  1.00 32.55 ? 230  TYR A CB  1 
ATOM   1647 C CG  . TYR A 1 230 ? 10.178  15.772  -6.456  1.00 37.27 ? 230  TYR A CG  1 
ATOM   1648 C CD1 . TYR A 1 230 ? 10.525  15.743  -5.111  1.00 38.33 ? 230  TYR A CD1 1 
ATOM   1649 C CD2 . TYR A 1 230 ? 9.712   16.972  -6.974  1.00 37.06 ? 230  TYR A CD2 1 
ATOM   1650 C CE1 . TYR A 1 230 ? 10.406  16.869  -4.312  1.00 38.55 ? 230  TYR A CE1 1 
ATOM   1651 C CE2 . TYR A 1 230 ? 9.567   18.101  -6.182  1.00 37.29 ? 230  TYR A CE2 1 
ATOM   1652 C CZ  . TYR A 1 230 ? 9.909   18.046  -4.844  1.00 35.93 ? 230  TYR A CZ  1 
ATOM   1653 O OH  . TYR A 1 230 ? 9.812   19.154  -4.067  1.00 35.13 ? 230  TYR A OH  1 
ATOM   1654 N N   . VAL A 1 231 ? 12.705  12.418  -8.864  1.00 36.63 ? 231  VAL A N   1 
ATOM   1655 C CA  . VAL A 1 231 ? 12.773  11.257  -9.812  1.00 37.46 ? 231  VAL A CA  1 
ATOM   1656 C C   . VAL A 1 231 ? 13.807  10.245  -9.296  1.00 34.82 ? 231  VAL A C   1 
ATOM   1657 O O   . VAL A 1 231 ? 14.963  10.624  -9.018  1.00 34.65 ? 231  VAL A O   1 
ATOM   1658 C CB  . VAL A 1 231 ? 12.977  11.636  -11.302 1.00 39.07 ? 231  VAL A CB  1 
ATOM   1659 C CG1 . VAL A 1 231 ? 12.790  13.113  -11.587 1.00 37.90 ? 231  VAL A CG1 1 
ATOM   1660 C CG2 . VAL A 1 231 ? 14.292  11.150  -11.894 1.00 38.61 ? 231  VAL A CG2 1 
ATOM   1661 N N   . GLY A 1 232 ? 13.372  8.988   -9.175  1.00 31.58 ? 232  GLY A N   1 
ATOM   1662 C CA  . GLY A 1 232 ? 14.199  7.819   -8.821  1.00 26.05 ? 232  GLY A CA  1 
ATOM   1663 C C   . GLY A 1 232 ? 13.569  6.570   -9.405  1.00 24.85 ? 232  GLY A C   1 
ATOM   1664 O O   . GLY A 1 232 ? 12.772  6.689   -10.339 1.00 27.48 ? 232  GLY A O   1 
ATOM   1665 N N   . GLY A 1 233 ? 13.847  5.415   -8.832  1.00 25.10 ? 233  GLY A N   1 
ATOM   1666 C CA  . GLY A 1 233 ? 13.396  4.114   -9.356  1.00 25.94 ? 233  GLY A CA  1 
ATOM   1667 C C   . GLY A 1 233 ? 12.301  3.486   -8.508  1.00 25.57 ? 233  GLY A C   1 
ATOM   1668 O O   . GLY A 1 233 ? 12.046  2.289   -8.689  1.00 24.60 ? 233  GLY A O   1 
ATOM   1669 N N   . SER A 1 234 ? 11.664  4.260   -7.625  1.00 26.18 ? 234  SER A N   1 
ATOM   1670 C CA  . SER A 1 234 ? 10.684  3.761   -6.628  1.00 25.84 ? 234  SER A CA  1 
ATOM   1671 C C   . SER A 1 234 ? 9.485   4.694   -6.590  1.00 27.83 ? 234  SER A C   1 
ATOM   1672 O O   . SER A 1 234 ? 9.183   5.277   -5.546  1.00 29.77 ? 234  SER A O   1 
ATOM   1673 C CB  . SER A 1 234 ? 11.322  3.613   -5.272  1.00 25.16 ? 234  SER A CB  1 
ATOM   1674 O OG  . SER A 1 234 ? 12.435  2.739   -5.342  1.00 23.76 ? 234  SER A OG  1 
ATOM   1675 N N   . PRO A 1 235 ? 8.741   4.812   -7.711  1.00 27.28 ? 235  PRO A N   1 
ATOM   1676 C CA  . PRO A 1 235 ? 7.644   5.765   -7.802  1.00 28.70 ? 235  PRO A CA  1 
ATOM   1677 C C   . PRO A 1 235 ? 6.499   5.476   -6.824  1.00 29.64 ? 235  PRO A C   1 
ATOM   1678 O O   . PRO A 1 235 ? 6.332   4.364   -6.374  1.00 30.60 ? 235  PRO A O   1 
ATOM   1679 C CB  . PRO A 1 235 ? 7.160   5.633   -9.255  1.00 29.67 ? 235  PRO A CB  1 
ATOM   1680 C CG  . PRO A 1 235 ? 7.568   4.223   -9.652  1.00 29.12 ? 235  PRO A CG  1 
ATOM   1681 C CD  . PRO A 1 235 ? 8.887   4.014   -8.937  1.00 28.39 ? 235  PRO A CD  1 
ATOM   1682 N N   . LEU A 1 236 ? 5.722   6.526   -6.569  1.00 33.42 ? 236  LEU A N   1 
ATOM   1683 C CA  . LEU A 1 236 ? 4.543   6.573   -5.671  1.00 30.19 ? 236  LEU A CA  1 
ATOM   1684 C C   . LEU A 1 236 ? 3.482   5.592   -6.169  1.00 28.63 ? 236  LEU A C   1 
ATOM   1685 O O   . LEU A 1 236 ? 2.844   4.975   -5.322  1.00 26.44 ? 236  LEU A O   1 
ATOM   1686 C CB  . LEU A 1 236 ? 4.024   8.019   -5.632  1.00 30.51 ? 236  LEU A CB  1 
ATOM   1687 C CG  . LEU A 1 236 ? 4.265   8.839   -4.360  1.00 30.77 ? 236  LEU A CG  1 
ATOM   1688 C CD1 . LEU A 1 236 ? 5.417   8.311   -3.509  1.00 32.37 ? 236  LEU A CD1 1 
ATOM   1689 C CD2 . LEU A 1 236 ? 4.461   10.311  -4.692  1.00 28.91 ? 236  LEU A CD2 1 
ATOM   1690 N N   . THR A 1 237 ? 3.325   5.414   -7.483  1.00 27.82 ? 237  THR A N   1 
ATOM   1691 C CA  . THR A 1 237 ? 2.335   4.453   -8.065  1.00 27.34 ? 237  THR A CA  1 
ATOM   1692 C C   . THR A 1 237 ? 2.633   3.042   -7.549  1.00 25.91 ? 237  THR A C   1 
ATOM   1693 O O   . THR A 1 237 ? 1.703   2.389   -7.037  1.00 24.82 ? 237  THR A O   1 
ATOM   1694 C CB  . THR A 1 237 ? 2.344   4.451   -9.603  1.00 25.82 ? 237  THR A CB  1 
ATOM   1695 O OG1 . THR A 1 237 ? 3.694   4.377   -10.064 1.00 25.96 ? 237  THR A OG1 1 
ATOM   1696 C CG2 . THR A 1 237 ? 1.733   5.698   -10.202 1.00 26.28 ? 237  THR A CG2 1 
ATOM   1697 N N   . MET A 1 238 ? 3.897   2.620   -7.662  1.00 25.15 ? 238  MET A N   1 
ATOM   1698 C CA  . MET A 1 238 ? 4.397   1.276   -7.277  1.00 25.42 ? 238  MET A CA  1 
ATOM   1699 C C   . MET A 1 238 ? 4.248   1.111   -5.751  1.00 26.73 ? 238  MET A C   1 
ATOM   1700 O O   . MET A 1 238 ? 3.712   0.070   -5.309  1.00 24.67 ? 238  MET A O   1 
ATOM   1701 C CB  . MET A 1 238 ? 5.863   1.164   -7.706  1.00 24.92 ? 238  MET A CB  1 
ATOM   1702 C CG  . MET A 1 238 ? 6.512   -0.178  -7.394  1.00 24.86 ? 238  MET A CG  1 
ATOM   1703 S SD  . MET A 1 238 ? 7.089   -0.291  -5.694  1.00 22.30 ? 238  MET A SD  1 
ATOM   1704 C CE  . MET A 1 238 ? 8.176   1.133   -5.598  1.00 23.35 ? 238  MET A CE  1 
ATOM   1705 N N   . GLN A 1 239 ? 4.671   2.121   -4.977  1.00 27.27 ? 239  GLN A N   1 
ATOM   1706 C CA  . GLN A 1 239 ? 4.656   2.090   -3.488  1.00 29.46 ? 239  GLN A CA  1 
ATOM   1707 C C   . GLN A 1 239 ? 3.202   1.982   -3.030  1.00 29.12 ? 239  GLN A C   1 
ATOM   1708 O O   . GLN A 1 239 ? 2.944   1.187   -2.096  1.00 27.85 ? 239  GLN A O   1 
ATOM   1709 C CB  . GLN A 1 239 ? 5.315   3.327   -2.871  1.00 30.16 ? 239  GLN A CB  1 
ATOM   1710 C CG  . GLN A 1 239 ? 6.800   3.416   -3.183  1.00 32.96 ? 239  GLN A CG  1 
ATOM   1711 C CD  . GLN A 1 239 ? 7.626   4.133   -2.146  1.00 33.43 ? 239  GLN A CD  1 
ATOM   1712 O OE1 . GLN A 1 239 ? 7.286   4.169   -0.976  1.00 36.37 ? 239  GLN A OE1 1 
ATOM   1713 N NE2 . GLN A 1 239 ? 8.746   4.693   -2.571  1.00 37.20 ? 239  GLN A NE2 1 
ATOM   1714 N N   . LEU A 1 240 ? 2.301   2.744   -3.664  1.00 26.69 ? 240  LEU A N   1 
ATOM   1715 C CA  . LEU A 1 240 ? 0.854   2.726   -3.310  1.00 27.98 ? 240  LEU A CA  1 
ATOM   1716 C C   . LEU A 1 240 ? 0.322   1.321   -3.566  1.00 26.16 ? 240  LEU A C   1 
ATOM   1717 O O   . LEU A 1 240 ? -0.341  0.783   -2.680  1.00 26.47 ? 240  LEU A O   1 
ATOM   1718 C CB  . LEU A 1 240 ? 0.053   3.775   -4.086  1.00 28.89 ? 240  LEU A CB  1 
ATOM   1719 C CG  . LEU A 1 240 ? -1.442  3.825   -3.741  1.00 28.96 ? 240  LEU A CG  1 
ATOM   1720 C CD1 . LEU A 1 240 ? -1.647  4.030   -2.258  1.00 30.80 ? 240  LEU A CD1 1 
ATOM   1721 C CD2 . LEU A 1 240 ? -2.160  4.910   -4.518  1.00 29.70 ? 240  LEU A CD2 1 
ATOM   1722 N N   . GLU A 1 241 ? 0.679   0.713   -4.693  1.00 26.67 ? 241  GLU A N   1 
ATOM   1723 C CA  . GLU A 1 241 ? 0.256   -0.678  -5.022  1.00 27.69 ? 241  GLU A CA  1 
ATOM   1724 C C   . GLU A 1 241 ? 0.693   -1.622  -3.885  1.00 28.25 ? 241  GLU A C   1 
ATOM   1725 O O   . GLU A 1 241 ? -0.103  -2.520  -3.499  1.00 26.53 ? 241  GLU A O   1 
ATOM   1726 C CB  . GLU A 1 241 ? 0.839   -1.093  -6.376  1.00 29.76 ? 241  GLU A CB  1 
ATOM   1727 C CG  . GLU A 1 241 ? 0.215   -2.344  -6.953  1.00 33.78 ? 241  GLU A CG  1 
ATOM   1728 C CD  . GLU A 1 241 ? -1.124  -2.114  -7.637  1.00 33.84 ? 241  GLU A CD  1 
ATOM   1729 O OE1 . GLU A 1 241 ? -1.428  -0.961  -7.941  1.00 38.00 ? 241  GLU A OE1 1 
ATOM   1730 O OE2 . GLU A 1 241 ? -1.832  -3.096  -7.884  1.00 39.28 ? 241  GLU A OE2 1 
ATOM   1731 N N   . ALA A 1 242 ? 1.895   -1.430  -3.334  1.00 26.64 ? 242  ALA A N   1 
ATOM   1732 C CA  . ALA A 1 242 ? 2.443   -2.318  -2.275  1.00 27.19 ? 242  ALA A CA  1 
ATOM   1733 C C   . ALA A 1 242 ? 1.653   -2.123  -0.964  1.00 25.04 ? 242  ALA A C   1 
ATOM   1734 O O   . ALA A 1 242 ? 1.297   -3.135  -0.357  1.00 22.80 ? 242  ALA A O   1 
ATOM   1735 C CB  . ALA A 1 242 ? 3.932   -2.098  -2.110  1.00 26.04 ? 242  ALA A CB  1 
ATOM   1736 N N   . LEU A 1 243 ? 1.368   -0.878  -0.569  1.00 27.00 ? 243  LEU A N   1 
ATOM   1737 C CA  . LEU A 1 243 ? 0.490   -0.529  0.598   1.00 27.59 ? 243  LEU A CA  1 
ATOM   1738 C C   . LEU A 1 243 ? -0.894  -1.164  0.417   1.00 25.00 ? 243  LEU A C   1 
ATOM   1739 O O   . LEU A 1 243 ? -1.410  -1.713  1.396   1.00 22.81 ? 243  LEU A O   1 
ATOM   1740 C CB  . LEU A 1 243 ? 0.360   0.994   0.729   1.00 26.80 ? 243  LEU A CB  1 
ATOM   1741 C CG  . LEU A 1 243 ? 1.307   1.705   1.704   1.00 31.05 ? 243  LEU A CG  1 
ATOM   1742 C CD1 . LEU A 1 243 ? 2.613   0.961   1.936   1.00 30.54 ? 243  LEU A CD1 1 
ATOM   1743 C CD2 . LEU A 1 243 ? 1.585   3.117   1.227   1.00 29.24 ? 243  LEU A CD2 1 
ATOM   1744 N N   . GLU A 1 244 ? -1.499  -1.101  -0.772  1.00 25.47 ? 244  GLU A N   1 
ATOM   1745 C CA  . GLU A 1 244 ? -2.812  -1.773  -0.982  1.00 28.19 ? 244  GLU A CA  1 
ATOM   1746 C C   . GLU A 1 244 ? -2.662  -3.266  -0.674  1.00 27.48 ? 244  GLU A C   1 
ATOM   1747 O O   . GLU A 1 244 ? -3.587  -3.850  -0.077  1.00 28.80 ? 244  GLU A O   1 
ATOM   1748 C CB  . GLU A 1 244 ? -3.383  -1.580  -2.391  1.00 33.50 ? 244  GLU A CB  1 
ATOM   1749 C CG  . GLU A 1 244 ? -3.695  -0.134  -2.758  1.00 38.26 ? 244  GLU A CG  1 
ATOM   1750 C CD  . GLU A 1 244 ? -4.787  0.574   -1.963  1.00 43.78 ? 244  GLU A CD  1 
ATOM   1751 O OE1 . GLU A 1 244 ? -5.112  1.734   -2.332  1.00 46.72 ? 244  GLU A OE1 1 
ATOM   1752 O OE2 . GLU A 1 244 ? -5.314  -0.017  -0.982  1.00 43.70 ? 244  GLU A OE2 1 
ATOM   1753 N N   . ASN A 1 245 ? -1.550  -3.890  -1.059  1.00 27.07 ? 245  ASN A N   1 
ATOM   1754 C CA  . ASN A 1 245 ? -1.346  -5.340  -0.807  1.00 26.83 ? 245  ASN A CA  1 
ATOM   1755 C C   . ASN A 1 245 ? -1.172  -5.605  0.698   1.00 24.46 ? 245  ASN A C   1 
ATOM   1756 O O   . ASN A 1 245 ? -1.575  -6.705  1.132   1.00 22.57 ? 245  ASN A O   1 
ATOM   1757 C CB  . ASN A 1 245 ? -0.176  -5.901  -1.621  1.00 28.31 ? 245  ASN A CB  1 
ATOM   1758 C CG  . ASN A 1 245 ? -0.476  -6.003  -3.103  1.00 28.52 ? 245  ASN A CG  1 
ATOM   1759 O OD1 . ASN A 1 245 ? 0.407   -5.803  -3.938  1.00 30.66 ? 245  ASN A OD1 1 
ATOM   1760 N ND2 . ASN A 1 245 ? -1.696  -6.366  -3.440  1.00 24.60 ? 245  ASN A ND2 1 
ATOM   1761 N N   . ILE A 1 246 ? -0.567  -4.676  1.460   1.00 23.97 ? 246  ILE A N   1 
ATOM   1762 C CA  . ILE A 1 246 ? -0.513  -4.768  2.950   1.00 24.54 ? 246  ILE A CA  1 
ATOM   1763 C C   . ILE A 1 246 ? -1.963  -4.826  3.461   1.00 26.25 ? 246  ILE A C   1 
ATOM   1764 O O   . ILE A 1 246 ? -2.263  -5.773  4.214   1.00 26.91 ? 246  ILE A O   1 
ATOM   1765 C CB  . ILE A 1 246 ? 0.305   -3.631  3.599   1.00 24.56 ? 246  ILE A CB  1 
ATOM   1766 C CG1 . ILE A 1 246 ? 1.795   -3.714  3.242   1.00 24.12 ? 246  ILE A CG1 1 
ATOM   1767 C CG2 . ILE A 1 246 ? 0.091   -3.603  5.112   1.00 24.62 ? 246  ILE A CG2 1 
ATOM   1768 C CD1 . ILE A 1 246 ? 2.602   -2.472  3.608   1.00 23.10 ? 246  ILE A CD1 1 
ATOM   1769 N N   . SER A 1 247 ? -2.854  -3.914  3.039   1.00 28.48 ? 247  SER A N   1 
ATOM   1770 C CA  . SER A 1 247 ? -4.313  -3.973  3.371   1.00 29.62 ? 247  SER A CA  1 
ATOM   1771 C C   . SER A 1 247 ? -4.875  -5.367  3.056   1.00 27.71 ? 247  SER A C   1 
ATOM   1772 O O   . SER A 1 247 ? -5.492  -5.982  3.942   1.00 26.12 ? 247  SER A O   1 
ATOM   1773 C CB  . SER A 1 247 ? -5.164  -2.924  2.673   1.00 30.88 ? 247  SER A CB  1 
ATOM   1774 O OG  . SER A 1 247 ? -4.809  -1.615  3.056   1.00 35.30 ? 247  SER A OG  1 
ATOM   1775 N N   . GLU A 1 248 ? -4.696  -5.860  1.839   1.00 28.79 ? 248  GLU A N   1 
ATOM   1776 C CA  . GLU A 1 248 ? -5.311  -7.157  1.437   1.00 28.62 ? 248  GLU A CA  1 
ATOM   1777 C C   . GLU A 1 248 ? -4.691  -8.284  2.260   1.00 27.24 ? 248  GLU A C   1 
ATOM   1778 O O   . GLU A 1 248 ? -5.443  -9.153  2.713   1.00 25.28 ? 248  GLU A O   1 
ATOM   1779 C CB  . GLU A 1 248 ? -5.168  -7.411  -0.064  1.00 32.71 ? 248  GLU A CB  1 
ATOM   1780 C CG  . GLU A 1 248 ? -5.752  -8.741  -0.507  1.00 36.73 ? 248  GLU A CG  1 
ATOM   1781 C CD  . GLU A 1 248 ? -7.249  -8.861  -0.272  1.00 43.03 ? 248  GLU A CD  1 
ATOM   1782 O OE1 . GLU A 1 248 ? -7.779  -9.998  -0.352  1.00 47.91 ? 248  GLU A OE1 1 
ATOM   1783 O OE2 . GLU A 1 248 ? -7.886  -7.810  -0.011  1.00 48.44 ? 248  GLU A OE2 1 
ATOM   1784 N N   . THR A 1 249 ? -3.372  -8.259  2.488   1.00 26.29 ? 249  THR A N   1 
ATOM   1785 C CA  . THR A 1 249 ? -2.657  -9.309  3.268   1.00 25.48 ? 249  THR A CA  1 
ATOM   1786 C C   . THR A 1 249 ? -3.278  -9.361  4.667   1.00 23.26 ? 249  THR A C   1 
ATOM   1787 O O   . THR A 1 249 ? -3.570  -10.466 5.182   1.00 22.97 ? 249  THR A O   1 
ATOM   1788 C CB  . THR A 1 249 ? -1.141  -9.045  3.284   1.00 25.81 ? 249  THR A CB  1 
ATOM   1789 O OG1 . THR A 1 249 ? -0.624  -9.265  1.970   1.00 23.97 ? 249  THR A OG1 1 
ATOM   1790 C CG2 . THR A 1 249 ? -0.399  -9.946  4.247   1.00 26.06 ? 249  THR A CG2 1 
ATOM   1791 N N   . SER A 1 250 ? -3.477  -8.189  5.248   1.00 23.05 ? 250  SER A N   1 
ATOM   1792 C CA  . SER A 1 250 ? -4.062  -8.002  6.594   1.00 25.35 ? 250  SER A CA  1 
ATOM   1793 C C   . SER A 1 250 ? -5.503  -8.537  6.593   1.00 26.86 ? 250  SER A C   1 
ATOM   1794 O O   . SER A 1 250 ? -5.834  -9.315  7.502   1.00 24.33 ? 250  SER A O   1 
ATOM   1795 C CB  . SER A 1 250 ? -3.960  -6.565  7.013   1.00 24.76 ? 250  SER A CB  1 
ATOM   1796 O OG  . SER A 1 250 ? -2.597  -6.173  7.062   1.00 25.83 ? 250  SER A OG  1 
ATOM   1797 N N   . ARG A 1 251 ? -6.291  -8.205  5.569   1.00 29.07 ? 251  ARG A N   1 
ATOM   1798 C CA  . ARG A 1 251 ? -7.703  -8.663  5.436   1.00 33.15 ? 251  ARG A CA  1 
ATOM   1799 C C   . ARG A 1 251 ? -7.722  -10.187 5.405   1.00 34.35 ? 251  ARG A C   1 
ATOM   1800 O O   . ARG A 1 251 ? -8.425  -10.764 6.245   1.00 35.48 ? 251  ARG A O   1 
ATOM   1801 C CB  . ARG A 1 251 ? -8.372  -8.107  4.175   1.00 35.01 ? 251  ARG A CB  1 
ATOM   1802 C CG  . ARG A 1 251 ? -9.887  -8.264  4.175   1.00 38.54 ? 251  ARG A CG  1 
ATOM   1803 C CD  . ARG A 1 251 ? -10.533 -7.972  2.835   1.00 39.26 ? 251  ARG A CD  1 
ATOM   1804 N NE  . ARG A 1 251 ? -10.077 -8.927  1.836   1.00 41.47 ? 251  ARG A NE  1 
ATOM   1805 C CZ  . ARG A 1 251 ? -10.489 -10.184 1.739   1.00 42.06 ? 251  ARG A CZ  1 
ATOM   1806 N NH1 . ARG A 1 251 ? -11.397 -10.661 2.580   1.00 42.48 ? 251  ARG A NH1 1 
ATOM   1807 N NH2 . ARG A 1 251 ? -9.989  -10.963 0.792   1.00 42.10 ? 251  ARG A NH2 1 
ATOM   1808 N N   . GLU A 1 252 ? -6.952  -10.789 4.488   1.00 38.30 ? 252  GLU A N   1 
ATOM   1809 C CA  . GLU A 1 252 ? -6.794  -12.257 4.295   1.00 36.17 ? 252  GLU A CA  1 
ATOM   1810 C C   . GLU A 1 252 ? -6.627  -12.942 5.660   1.00 35.76 ? 252  GLU A C   1 
ATOM   1811 O O   . GLU A 1 252 ? -7.148  -14.058 5.829   1.00 36.00 ? 252  GLU A O   1 
ATOM   1812 C CB  . GLU A 1 252 ? -5.572  -12.576 3.414   1.00 39.35 ? 252  GLU A CB  1 
ATOM   1813 C CG  . GLU A 1 252 ? -5.766  -12.359 1.920   1.00 39.95 ? 252  GLU A CG  1 
ATOM   1814 C CD  . GLU A 1 252 ? -4.529  -12.457 1.022   1.00 41.02 ? 252  GLU A CD  1 
ATOM   1815 O OE1 . GLU A 1 252 ? -4.655  -12.042 -0.157  1.00 44.27 ? 252  GLU A OE1 1 
ATOM   1816 O OE2 . GLU A 1 252 ? -3.453  -12.982 1.457   1.00 30.63 ? 252  GLU A OE2 1 
ATOM   1817 N N   . LEU A 1 253 ? -5.887  -12.316 6.585   1.00 32.80 ? 253  LEU A N   1 
ATOM   1818 C CA  . LEU A 1 253 ? -5.551  -12.899 7.910   1.00 30.09 ? 253  LEU A CA  1 
ATOM   1819 C C   . LEU A 1 253 ? -6.612  -12.510 8.945   1.00 29.36 ? 253  LEU A C   1 
ATOM   1820 O O   . LEU A 1 253 ? -6.618  -13.111 10.012  1.00 33.23 ? 253  LEU A O   1 
ATOM   1821 C CB  . LEU A 1 253 ? -4.156  -12.427 8.333   1.00 29.45 ? 253  LEU A CB  1 
ATOM   1822 C CG  . LEU A 1 253 ? -2.993  -13.112 7.608   1.00 30.71 ? 253  LEU A CG  1 
ATOM   1823 C CD1 . LEU A 1 253 ? -1.725  -12.254 7.627   1.00 30.89 ? 253  LEU A CD1 1 
ATOM   1824 C CD2 . LEU A 1 253 ? -2.703  -14.471 8.213   1.00 31.12 ? 253  LEU A CD2 1 
ATOM   1825 N N   . GLY A 1 254 ? -7.480  -11.547 8.643   1.00 29.58 ? 254  GLY A N   1 
ATOM   1826 C CA  . GLY A 1 254 ? -8.483  -11.037 9.597   1.00 29.37 ? 254  GLY A CA  1 
ATOM   1827 C C   . GLY A 1 254 ? -7.859  -10.037 10.551  1.00 32.12 ? 254  GLY A C   1 
ATOM   1828 O O   . GLY A 1 254 ? -8.383  -9.890  11.680  1.00 35.91 ? 254  GLY A O   1 
ATOM   1829 N N   . VAL A 1 255 ? -6.767  -9.382  10.143  1.00 29.75 ? 255  VAL A N   1 
ATOM   1830 C CA  . VAL A 1 255 ? -6.105  -8.354  10.997  1.00 28.97 ? 255  VAL A CA  1 
ATOM   1831 C C   . VAL A 1 255 ? -6.380  -6.978  10.392  1.00 26.65 ? 255  VAL A C   1 
ATOM   1832 O O   . VAL A 1 255 ? -6.529  -6.869  9.149   1.00 28.11 ? 255  VAL A O   1 
ATOM   1833 C CB  . VAL A 1 255 ? -4.602  -8.626  11.266  1.00 31.48 ? 255  VAL A CB  1 
ATOM   1834 C CG1 . VAL A 1 255 ? -4.158  -10.022 10.868  1.00 30.51 ? 255  VAL A CG1 1 
ATOM   1835 C CG2 . VAL A 1 255 ? -3.676  -7.587  10.666  1.00 31.57 ? 255  VAL A CG2 1 
ATOM   1836 N N   . GLY A 1 256 ? -6.437  -5.976  11.268  1.00 25.18 ? 256  GLY A N   1 
ATOM   1837 C CA  . GLY A 1 256 ? -6.628  -4.558  10.932  1.00 25.20 ? 256  GLY A CA  1 
ATOM   1838 C C   . GLY A 1 256 ? -5.406  -3.908  10.302  1.00 26.82 ? 256  GLY A C   1 
ATOM   1839 O O   . GLY A 1 256 ? -4.273  -4.452  10.358  1.00 27.79 ? 256  GLY A O   1 
ATOM   1840 N N   . VAL A 1 257 ? -5.641  -2.710  9.796   1.00 24.82 ? 257  VAL A N   1 
ATOM   1841 C CA  . VAL A 1 257 ? -4.836  -2.031  8.758   1.00 26.39 ? 257  VAL A CA  1 
ATOM   1842 C C   . VAL A 1 257 ? -4.641  -0.602  9.237   1.00 25.85 ? 257  VAL A C   1 
ATOM   1843 O O   . VAL A 1 257 ? -5.665  0.053   9.479   1.00 25.28 ? 257  VAL A O   1 
ATOM   1844 C CB  . VAL A 1 257 ? -5.603  -2.115  7.431   1.00 26.10 ? 257  VAL A CB  1 
ATOM   1845 C CG1 . VAL A 1 257 ? -4.987  -1.281  6.348   1.00 28.74 ? 257  VAL A CG1 1 
ATOM   1846 C CG2 . VAL A 1 257 ? -5.759  -3.558  6.990   1.00 26.88 ? 257  VAL A CG2 1 
ATOM   1847 N N   . LEU A 1 258 ? -3.384  -0.205  9.458   1.00 24.13 ? 258  LEU A N   1 
ATOM   1848 C CA  . LEU A 1 258 ? -2.943  1.176   9.795   1.00 24.72 ? 258  LEU A CA  1 
ATOM   1849 C C   . LEU A 1 258 ? -2.459  1.816   8.484   1.00 24.17 ? 258  LEU A C   1 
ATOM   1850 O O   . LEU A 1 258 ? -2.828  1.276   7.425   1.00 25.81 ? 258  LEU A O   1 
ATOM   1851 C CB  . LEU A 1 258 ? -1.842  1.088   10.869  1.00 27.29 ? 258  LEU A CB  1 
ATOM   1852 C CG  . LEU A 1 258 ? -2.251  1.226   12.336  1.00 29.99 ? 258  LEU A CG  1 
ATOM   1853 C CD1 . LEU A 1 258 ? -3.710  0.842   12.591  1.00 30.24 ? 258  LEU A CD1 1 
ATOM   1854 C CD2 . LEU A 1 258 ? -1.315  0.435   13.245  1.00 29.63 ? 258  LEU A CD2 1 
ATOM   1855 N N   . LEU A 1 259 ? -1.700  2.915   8.523   1.00 23.92 ? 259  LEU A N   1 
ATOM   1856 C CA  . LEU A 1 259 ? -1.050  3.537   7.336   1.00 26.05 ? 259  LEU A CA  1 
ATOM   1857 C C   . LEU A 1 259 ? -2.092  4.208   6.410   1.00 26.65 ? 259  LEU A C   1 
ATOM   1858 O O   . LEU A 1 259 ? -1.710  4.599   5.292   1.00 27.04 ? 259  LEU A O   1 
ATOM   1859 C CB  . LEU A 1 259 ? -0.279  2.451   6.577   1.00 26.97 ? 259  LEU A CB  1 
ATOM   1860 C CG  . LEU A 1 259 ? 1.205   2.268   6.895   1.00 29.90 ? 259  LEU A CG  1 
ATOM   1861 C CD1 . LEU A 1 259 ? 1.580   2.720   8.286   1.00 31.67 ? 259  LEU A CD1 1 
ATOM   1862 C CD2 . LEU A 1 259 ? 1.621   0.824   6.686   1.00 30.17 ? 259  LEU A CD2 1 
ATOM   1863 N N   . GLY A 1 260 ? -3.345  4.360   6.841   1.00 27.24 ? 260  GLY A N   1 
ATOM   1864 C CA  . GLY A 1 260 ? -4.424  4.966   6.034   1.00 27.23 ? 260  GLY A CA  1 
ATOM   1865 C C   . GLY A 1 260 ? -4.057  6.344   5.507   1.00 27.71 ? 260  GLY A C   1 
ATOM   1866 O O   . GLY A 1 260 ? -4.348  6.618   4.320   1.00 29.05 ? 260  GLY A O   1 
ATOM   1867 N N   . SER A 1 261 ? -3.444  7.195   6.338   1.00 27.02 ? 261  SER A N   1 
ATOM   1868 C CA  . SER A 1 261 ? -3.019  8.576   5.969   1.00 27.45 ? 261  SER A CA  1 
ATOM   1869 C C   . SER A 1 261 ? -2.016  8.502   4.820   1.00 29.33 ? 261  SER A C   1 
ATOM   1870 O O   . SER A 1 261 ? -2.093  9.345   3.893   1.00 29.52 ? 261  SER A O   1 
ATOM   1871 C CB  . SER A 1 261 ? -2.402  9.311   7.132   1.00 26.95 ? 261  SER A CB  1 
ATOM   1872 O OG  . SER A 1 261 ? -3.363  9.627   8.128   1.00 24.58 ? 261  SER A OG  1 
ATOM   1873 N N   . MET A 1 262 ? -1.080  7.552   4.909   1.00 27.36 ? 262  MET A N   1 
ATOM   1874 C CA  . MET A 1 262 ? -0.064  7.308   3.853   1.00 29.24 ? 262  MET A CA  1 
ATOM   1875 C C   . MET A 1 262 ? -0.781  6.906   2.565   1.00 27.89 ? 262  MET A C   1 
ATOM   1876 O O   . MET A 1 262 ? -0.435  7.421   1.504   1.00 26.61 ? 262  MET A O   1 
ATOM   1877 C CB  . MET A 1 262 ? 0.919   6.198   4.245   1.00 28.26 ? 262  MET A CB  1 
ATOM   1878 C CG  . MET A 1 262 ? 2.166   6.247   3.438   1.00 29.07 ? 262  MET A CG  1 
ATOM   1879 S SD  . MET A 1 262 ? 3.024   7.839   3.536   1.00 30.77 ? 262  MET A SD  1 
ATOM   1880 C CE  . MET A 1 262 ? 4.687   7.286   3.163   1.00 32.18 ? 262  MET A CE  1 
ATOM   1881 N N   . ARG A 1 263 ? -1.722  5.980   2.670   1.00 28.26 ? 263  ARG A N   1 
ATOM   1882 C CA  . ARG A 1 263 ? -2.520  5.526   1.507   1.00 30.89 ? 263  ARG A CA  1 
ATOM   1883 C C   . ARG A 1 263 ? -3.242  6.738   0.904   1.00 31.41 ? 263  ARG A C   1 
ATOM   1884 O O   . ARG A 1 263 ? -3.091  6.951   -0.309  1.00 29.70 ? 263  ARG A O   1 
ATOM   1885 C CB  . ARG A 1 263 ? -3.479  4.413   1.911   1.00 31.65 ? 263  ARG A CB  1 
ATOM   1886 C CG  . ARG A 1 263 ? -2.996  3.027   1.515   1.00 34.91 ? 263  ARG A CG  1 
ATOM   1887 C CD  . ARG A 1 263 ? -4.023  1.948   1.801   1.00 37.47 ? 263  ARG A CD  1 
ATOM   1888 N NE  . ARG A 1 263 ? -3.722  1.487   3.130   1.00 45.60 ? 263  ARG A NE  1 
ATOM   1889 C CZ  . ARG A 1 263 ? -4.452  1.671   4.218   1.00 43.45 ? 263  ARG A CZ  1 
ATOM   1890 N NH1 . ARG A 1 263 ? -5.638  2.253   4.180   1.00 42.81 ? 263  ARG A NH1 1 
ATOM   1891 N NH2 . ARG A 1 263 ? -3.978  1.220   5.360   1.00 45.22 ? 263  ARG A NH2 1 
ATOM   1892 N N   . GLU A 1 264 ? -3.930  7.522   1.740   1.00 30.91 ? 264  GLU A N   1 
ATOM   1893 C CA  . GLU A 1 264 ? -4.733  8.699   1.315   1.00 31.19 ? 264  GLU A CA  1 
ATOM   1894 C C   . GLU A 1 264 ? -3.845  9.725   0.605   1.00 30.06 ? 264  GLU A C   1 
ATOM   1895 O O   . GLU A 1 264 ? -4.255  10.185  -0.488  1.00 30.19 ? 264  GLU A O   1 
ATOM   1896 C CB  . GLU A 1 264 ? -5.484  9.320   2.499   1.00 32.76 ? 264  GLU A CB  1 
ATOM   1897 C CG  . GLU A 1 264 ? -6.699  8.519   2.941   1.00 36.78 ? 264  GLU A CG  1 
ATOM   1898 C CD  . GLU A 1 264 ? -7.629  8.073   1.826   1.00 40.55 ? 264  GLU A CD  1 
ATOM   1899 O OE1 . GLU A 1 264 ? -7.874  8.868   0.914   1.00 40.57 ? 264  GLU A OE1 1 
ATOM   1900 O OE2 . GLU A 1 264 ? -8.091  6.925   1.869   1.00 51.05 ? 264  GLU A OE2 1 
ATOM   1901 N N   . VAL A 1 265 ? -2.690  10.089  1.175   1.00 28.02 ? 265  VAL A N   1 
ATOM   1902 C CA  . VAL A 1 265 ? -1.849  11.181  0.608   1.00 28.95 ? 265  VAL A CA  1 
ATOM   1903 C C   . VAL A 1 265 ? -1.224  10.702  -0.706  1.00 32.12 ? 265  VAL A C   1 
ATOM   1904 O O   . VAL A 1 265 ? -1.021  11.546  -1.609  1.00 31.12 ? 265  VAL A O   1 
ATOM   1905 C CB  . VAL A 1 265 ? -0.786  11.705  1.593   1.00 31.45 ? 265  VAL A CB  1 
ATOM   1906 C CG1 . VAL A 1 265 ? 0.288   10.670  1.898   1.00 31.15 ? 265  VAL A CG1 1 
ATOM   1907 C CG2 . VAL A 1 265 ? -0.164  13.012  1.110   1.00 30.00 ? 265  VAL A CG2 1 
ATOM   1908 N N   . MET A 1 266 ? -0.875  9.417   -0.790  1.00 31.57 ? 266  MET A N   1 
ATOM   1909 C CA  . MET A 1 266 ? -0.312  8.807   -2.019  1.00 31.14 ? 266  MET A CA  1 
ATOM   1910 C C   . MET A 1 266 ? -1.439  8.711   -3.067  1.00 29.33 ? 266  MET A C   1 
ATOM   1911 O O   . MET A 1 266 ? -1.123  8.931   -4.217  1.00 28.10 ? 266  MET A O   1 
ATOM   1912 C CB  . MET A 1 266 ? 0.280   7.410   -1.771  1.00 30.95 ? 266  MET A CB  1 
ATOM   1913 C CG  . MET A 1 266 ? 1.643   7.382   -1.081  1.00 33.70 ? 266  MET A CG  1 
ATOM   1914 S SD  . MET A 1 266 ? 2.475   5.756   -1.306  1.00 35.74 ? 266  MET A SD  1 
ATOM   1915 C CE  . MET A 1 266 ? 3.861   5.957   -0.187  1.00 35.14 ? 266  MET A CE  1 
ATOM   1916 N N   . SER A 1 267 ? -2.676  8.340   -2.702  1.00 29.45 ? 267  SER A N   1 
ATOM   1917 C CA  . SER A 1 267 ? -3.816  8.220   -3.663  1.00 33.26 ? 267  SER A CA  1 
ATOM   1918 C C   . SER A 1 267 ? -4.023  9.565   -4.365  1.00 34.66 ? 267  SER A C   1 
ATOM   1919 O O   . SER A 1 267 ? -4.077  9.608   -5.599  1.00 34.20 ? 267  SER A O   1 
ATOM   1920 C CB  . SER A 1 267 ? -5.103  7.798   -3.014  1.00 36.40 ? 267  SER A CB  1 
ATOM   1921 O OG  . SER A 1 267 ? -5.068  6.454   -2.584  1.00 43.15 ? 267  SER A OG  1 
ATOM   1922 N N   . GLU A 1 268 ? -4.102  10.636  -3.580  1.00 37.05 ? 268  GLU A N   1 
ATOM   1923 C CA  . GLU A 1 268 ? -4.271  12.015  -4.086  1.00 38.52 ? 268  GLU A CA  1 
ATOM   1924 C C   . GLU A 1 268 ? -3.028  12.422  -4.884  1.00 38.29 ? 268  GLU A C   1 
ATOM   1925 O O   . GLU A 1 268 ? -3.187  13.011  -5.973  1.00 39.55 ? 268  GLU A O   1 
ATOM   1926 C CB  . GLU A 1 268 ? -4.567  12.981  -2.938  1.00 40.66 ? 268  GLU A CB  1 
ATOM   1927 C CG  . GLU A 1 268 ? -5.003  14.362  -3.412  1.00 42.46 ? 268  GLU A CG  1 
ATOM   1928 C CD  . GLU A 1 268 ? -6.322  14.393  -4.173  1.00 44.35 ? 268  GLU A CD  1 
ATOM   1929 O OE1 . GLU A 1 268 ? -7.209  13.536  -3.885  1.00 39.97 ? 268  GLU A OE1 1 
ATOM   1930 O OE2 . GLU A 1 268 ? -6.465  15.285  -5.049  1.00 55.66 ? 268  GLU A OE2 1 
ATOM   1931 N N   . ALA A 1 269 ? -1.826  12.134  -4.395  1.00 35.91 ? 269  ALA A N   1 
ATOM   1932 C CA  . ALA A 1 269 ? -0.582  12.406  -5.157  1.00 36.06 ? 269  ALA A CA  1 
ATOM   1933 C C   . ALA A 1 269 ? -0.711  11.873  -6.603  1.00 36.07 ? 269  ALA A C   1 
ATOM   1934 O O   . ALA A 1 269 ? -0.394  12.626  -7.566  1.00 36.09 ? 269  ALA A O   1 
ATOM   1935 C CB  . ALA A 1 269 ? 0.605   11.817  -4.443  1.00 37.62 ? 269  ALA A CB  1 
ATOM   1936 N N   . VAL A 1 270 ? -1.147  10.624  -6.775  1.00 32.34 ? 270  VAL A N   1 
ATOM   1937 C CA  . VAL A 1 270 ? -1.367  10.023  -8.124  1.00 36.93 ? 270  VAL A CA  1 
ATOM   1938 C C   . VAL A 1 270 ? -2.346  10.916  -8.903  1.00 37.58 ? 270  VAL A C   1 
ATOM   1939 O O   . VAL A 1 270 ? -1.961  11.370  -10.011 1.00 37.22 ? 270  VAL A O   1 
ATOM   1940 C CB  . VAL A 1 270 ? -1.852  8.568   -8.039  1.00 35.11 ? 270  VAL A CB  1 
ATOM   1941 C CG1 . VAL A 1 270 ? -2.384  8.063   -9.378  1.00 35.72 ? 270  VAL A CG1 1 
ATOM   1942 C CG2 . VAL A 1 270 ? -0.749  7.655   -7.513  1.00 37.18 ? 270  VAL A CG2 1 
ATOM   1943 N N   . LYS A 1 271 ? -3.515  11.209  -8.321  1.00 40.23 ? 271  LYS A N   1 
ATOM   1944 C CA  . LYS A 1 271 ? -4.565  12.107  -8.894  1.00 44.75 ? 271  LYS A CA  1 
ATOM   1945 C C   . LYS A 1 271 ? -3.941  13.372  -9.522  1.00 45.48 ? 271  LYS A C   1 
ATOM   1946 O O   . LYS A 1 271 ? -4.342  13.720  -10.657 1.00 44.85 ? 271  LYS A O   1 
ATOM   1947 C CB  . LYS A 1 271 ? -5.586  12.490  -7.816  1.00 49.69 ? 271  LYS A CB  1 
ATOM   1948 C CG  . LYS A 1 271 ? -6.955  11.825  -7.912  1.00 53.62 ? 271  LYS A CG  1 
ATOM   1949 C CD  . LYS A 1 271 ? -7.203  10.709  -6.916  1.00 57.03 ? 271  LYS A CD  1 
ATOM   1950 C CE  . LYS A 1 271 ? -8.588  10.773  -6.301  1.00 58.47 ? 271  LYS A CE  1 
ATOM   1951 N NZ  . LYS A 1 271 ? -8.929  9.526   -5.572  1.00 57.99 ? 271  LYS A NZ  1 
ATOM   1952 N N   . LYS A 1 272 ? -2.985  14.019  -8.839  1.00 42.22 ? 272  LYS A N   1 
ATOM   1953 C CA  . LYS A 1 272 ? -2.337  15.295  -9.255  1.00 44.28 ? 272  LYS A CA  1 
ATOM   1954 C C   . LYS A 1 272 ? -1.138  15.045  -10.177 1.00 45.63 ? 272  LYS A C   1 
ATOM   1955 O O   . LYS A 1 272 ? -0.308  15.979  -10.345 1.00 42.65 ? 272  LYS A O   1 
ATOM   1956 C CB  . LYS A 1 272 ? -1.809  16.063  -8.038  1.00 46.71 ? 272  LYS A CB  1 
ATOM   1957 C CG  . LYS A 1 272 ? -2.837  16.406  -6.974  1.00 48.39 ? 272  LYS A CG  1 
ATOM   1958 C CD  . LYS A 1 272 ? -2.215  16.990  -5.722  1.00 49.70 ? 272  LYS A CD  1 
ATOM   1959 C CE  . LYS A 1 272 ? -3.230  17.639  -4.799  1.00 53.62 ? 272  LYS A CE  1 
ATOM   1960 N NZ  . LYS A 1 272 ? -3.242  19.114  -4.939  1.00 54.06 ? 272  LYS A NZ  1 
ATOM   1961 N N   . GLY A 1 273 ? -1.009  13.834  -10.726 1.00 47.24 ? 273  GLY A N   1 
ATOM   1962 C CA  . GLY A 1 273 ? 0.023   13.508  -11.726 1.00 43.65 ? 273  GLY A CA  1 
ATOM   1963 C C   . GLY A 1 273 ? 1.410   13.482  -11.119 1.00 44.11 ? 273  GLY A C   1 
ATOM   1964 O O   . GLY A 1 273 ? 2.380   13.737  -11.872 1.00 43.15 ? 273  GLY A O   1 
ATOM   1965 N N   . LYS A 1 274 ? 1.516   13.190  -9.813  1.00 39.41 ? 274  LYS A N   1 
ATOM   1966 C CA  . LYS A 1 274 ? 2.819   13.093  -9.103  1.00 38.59 ? 274  LYS A CA  1 
ATOM   1967 C C   . LYS A 1 274 ? 3.139   11.611  -8.870  1.00 34.30 ? 274  LYS A C   1 
ATOM   1968 O O   . LYS A 1 274 ? 4.162   11.335  -8.214  1.00 32.37 ? 274  LYS A O   1 
ATOM   1969 C CB  . LYS A 1 274 ? 2.786   13.881  -7.789  1.00 42.91 ? 274  LYS A CB  1 
ATOM   1970 C CG  . LYS A 1 274 ? 2.736   15.399  -7.915  1.00 42.35 ? 274  LYS A CG  1 
ATOM   1971 C CD  . LYS A 1 274 ? 2.365   16.119  -6.623  1.00 42.50 ? 274  LYS A CD  1 
ATOM   1972 C CE  . LYS A 1 274 ? 3.241   15.739  -5.440  1.00 44.89 ? 274  LYS A CE  1 
ATOM   1973 N NZ  . LYS A 1 274 ? 4.610   16.315  -5.501  1.00 43.57 ? 274  LYS A NZ  1 
ATOM   1974 N N   . GLY A 1 275 ? 2.311   10.718  -9.434  1.00 29.74 ? 275  GLY A N   1 
ATOM   1975 C CA  . GLY A 1 275 ? 2.416   9.247   -9.354  1.00 31.09 ? 275  GLY A CA  1 
ATOM   1976 C C   . GLY A 1 275 ? 3.819   8.723   -9.650  1.00 30.76 ? 275  GLY A C   1 
ATOM   1977 O O   . GLY A 1 275 ? 4.165   7.683   -9.098  1.00 32.11 ? 275  GLY A O   1 
ATOM   1978 N N   . GLY A 1 276 ? 4.582   9.402   -10.506 1.00 27.43 ? 276  GLY A N   1 
ATOM   1979 C CA  . GLY A 1 276 ? 5.914   8.966   -10.964 1.00 28.59 ? 276  GLY A CA  1 
ATOM   1980 C C   . GLY A 1 276 ? 7.021   9.488   -10.070 1.00 27.45 ? 276  GLY A C   1 
ATOM   1981 O O   . GLY A 1 276 ? 8.151   9.082   -10.277 1.00 31.60 ? 276  GLY A O   1 
ATOM   1982 N N   . GLU A 1 277 ? 6.695   10.309  -9.072  1.00 28.08 ? 277  GLU A N   1 
ATOM   1983 C CA  . GLU A 1 277 ? 7.697   10.915  -8.166  1.00 31.27 ? 277  GLU A CA  1 
ATOM   1984 C C   . GLU A 1 277 ? 8.053   9.929   -7.056  1.00 29.16 ? 277  GLU A C   1 
ATOM   1985 O O   . GLU A 1 277 ? 7.294   8.963   -6.823  1.00 30.07 ? 277  GLU A O   1 
ATOM   1986 C CB  . GLU A 1 277 ? 7.184   12.216  -7.551  1.00 35.00 ? 277  GLU A CB  1 
ATOM   1987 C CG  . GLU A 1 277 ? 6.970   13.313  -8.579  1.00 38.90 ? 277  GLU A CG  1 
ATOM   1988 C CD  . GLU A 1 277 ? 6.557   14.644  -7.976  1.00 44.31 ? 277  GLU A CD  1 
ATOM   1989 O OE1 . GLU A 1 277 ? 6.008   14.646  -6.849  1.00 44.53 ? 277  GLU A OE1 1 
ATOM   1990 O OE2 . GLU A 1 277 ? 6.816   15.670  -8.618  1.00 48.32 ? 277  GLU A OE2 1 
ATOM   1991 N N   . SER A 1 278 ? 9.179   10.205  -6.416  1.00 26.97 ? 278  SER A N   1 
ATOM   1992 C CA  . SER A 1 278 ? 9.683   9.499   -5.219  1.00 28.65 ? 278  SER A CA  1 
ATOM   1993 C C   . SER A 1 278 ? 8.883   9.943   -3.998  1.00 27.94 ? 278  SER A C   1 
ATOM   1994 O O   . SER A 1 278 ? 8.080   10.905  -4.077  1.00 24.34 ? 278  SER A O   1 
ATOM   1995 C CB  . SER A 1 278 ? 11.158  9.743   -5.007  1.00 30.54 ? 278  SER A CB  1 
ATOM   1996 O OG  . SER A 1 278 ? 11.408  11.068  -4.534  1.00 30.98 ? 278  SER A OG  1 
ATOM   1997 N N   . ILE A 1 279 ? 9.138   9.251   -2.900  1.00 28.24 ? 279  ILE A N   1 
ATOM   1998 C CA  . ILE A 1 279 ? 8.565   9.522   -1.556  1.00 27.61 ? 279  ILE A CA  1 
ATOM   1999 C C   . ILE A 1 279 ? 8.814   10.996  -1.178  1.00 25.23 ? 279  ILE A C   1 
ATOM   2000 O O   . ILE A 1 279 ? 7.975   11.557  -0.456  1.00 25.71 ? 279  ILE A O   1 
ATOM   2001 C CB  . ILE A 1 279 ? 9.158   8.487   -0.579  1.00 29.48 ? 279  ILE A CB  1 
ATOM   2002 C CG1 . ILE A 1 279 ? 8.326   8.374   0.696   1.00 33.28 ? 279  ILE A CG1 1 
ATOM   2003 C CG2 . ILE A 1 279 ? 10.636  8.739   -0.305  1.00 31.27 ? 279  ILE A CG2 1 
ATOM   2004 C CD1 . ILE A 1 279 ? 7.039   7.600   0.483   1.00 33.67 ? 279  ILE A CD1 1 
ATOM   2005 N N   . ALA A 1 280 ? 9.895   11.625  -1.672  1.00 27.32 ? 280  ALA A N   1 
ATOM   2006 C CA  . ALA A 1 280 ? 10.251  13.051  -1.411  1.00 28.62 ? 280  ALA A CA  1 
ATOM   2007 C C   . ALA A 1 280 ? 9.120   13.989  -1.867  1.00 29.88 ? 280  ALA A C   1 
ATOM   2008 O O   . ALA A 1 280 ? 9.018   15.092  -1.304  1.00 34.86 ? 280  ALA A O   1 
ATOM   2009 C CB  . ALA A 1 280 ? 11.557  13.409  -2.071  1.00 25.90 ? 280  ALA A CB  1 
ATOM   2010 N N   . GLY A 1 281 ? 8.291   13.541  -2.823  1.00 31.89 ? 281  GLY A N   1 
ATOM   2011 C CA  . GLY A 1 281 ? 7.205   14.318  -3.449  1.00 30.30 ? 281  GLY A CA  1 
ATOM   2012 C C   . GLY A 1 281 ? 6.013   14.449  -2.526  1.00 31.63 ? 281  GLY A C   1 
ATOM   2013 O O   . GLY A 1 281 ? 5.131   15.275  -2.801  1.00 28.04 ? 281  GLY A O   1 
ATOM   2014 N N   . LEU A 1 282 ? 5.956   13.634  -1.473  1.00 29.76 ? 282  LEU A N   1 
ATOM   2015 C CA  . LEU A 1 282 ? 4.842   13.695  -0.508  1.00 28.17 ? 282  LEU A CA  1 
ATOM   2016 C C   . LEU A 1 282 ? 5.010   14.935  0.372   1.00 27.50 ? 282  LEU A C   1 
ATOM   2017 O O   . LEU A 1 282 ? 4.003   15.371  0.943   1.00 27.13 ? 282  LEU A O   1 
ATOM   2018 C CB  . LEU A 1 282 ? 4.786   12.417  0.326   1.00 28.96 ? 282  LEU A CB  1 
ATOM   2019 C CG  . LEU A 1 282 ? 4.328   11.156  -0.399  1.00 29.00 ? 282  LEU A CG  1 
ATOM   2020 C CD1 . LEU A 1 282 ? 4.202   10.006  0.587   1.00 29.11 ? 282  LEU A CD1 1 
ATOM   2021 C CD2 . LEU A 1 282 ? 3.006   11.360  -1.130  1.00 29.30 ? 282  LEU A CD2 1 
ATOM   2022 N N   . VAL A 1 283 ? 6.209   15.511  0.449   1.00 27.58 ? 283  VAL A N   1 
ATOM   2023 C CA  . VAL A 1 283 ? 6.489   16.581  1.450   1.00 30.02 ? 283  VAL A CA  1 
ATOM   2024 C C   . VAL A 1 283 ? 5.770   17.854  0.998   1.00 35.48 ? 283  VAL A C   1 
ATOM   2025 O O   . VAL A 1 283 ? 4.989   18.401  1.776   1.00 35.77 ? 283  VAL A O   1 
ATOM   2026 C CB  . VAL A 1 283 ? 7.991   16.754  1.719   1.00 29.68 ? 283  VAL A CB  1 
ATOM   2027 C CG1 . VAL A 1 283 ? 8.286   18.026  2.496   1.00 29.53 ? 283  VAL A CG1 1 
ATOM   2028 C CG2 . VAL A 1 283 ? 8.555   15.541  2.451   1.00 28.55 ? 283  VAL A CG2 1 
ATOM   2029 N N   . PRO A 1 284 ? 5.912   18.309  -0.275  1.00 35.58 ? 284  PRO A N   1 
ATOM   2030 C CA  . PRO A 1 284 ? 5.079   19.392  -0.792  1.00 36.95 ? 284  PRO A CA  1 
ATOM   2031 C C   . PRO A 1 284 ? 3.561   19.145  -0.700  1.00 33.82 ? 284  PRO A C   1 
ATOM   2032 O O   . PRO A 1 284 ? 2.858   20.111  -0.580  1.00 32.14 ? 284  PRO A O   1 
ATOM   2033 C CB  . PRO A 1 284 ? 5.522   19.528  -2.260  1.00 37.27 ? 284  PRO A CB  1 
ATOM   2034 C CG  . PRO A 1 284 ? 6.919   18.980  -2.273  1.00 36.37 ? 284  PRO A CG  1 
ATOM   2035 C CD  . PRO A 1 284 ? 6.880   17.841  -1.279  1.00 35.89 ? 284  PRO A CD  1 
ATOM   2036 N N   . MET A 1 285 ? 3.077   17.897  -0.750  1.00 33.41 ? 285  MET A N   1 
ATOM   2037 C CA  . MET A 1 285 ? 1.635   17.609  -0.504  1.00 32.14 ? 285  MET A CA  1 
ATOM   2038 C C   . MET A 1 285 ? 1.268   18.128  0.891   1.00 33.32 ? 285  MET A C   1 
ATOM   2039 O O   . MET A 1 285 ? 0.100   18.502  1.114   1.00 30.73 ? 285  MET A O   1 
ATOM   2040 C CB  . MET A 1 285 ? 1.298   16.117  -0.513  1.00 35.98 ? 285  MET A CB  1 
ATOM   2041 C CG  . MET A 1 285 ? 1.602   15.377  -1.799  1.00 41.04 ? 285  MET A CG  1 
ATOM   2042 S SD  . MET A 1 285 ? 0.339   15.642  -3.033  1.00 46.07 ? 285  MET A SD  1 
ATOM   2043 C CE  . MET A 1 285 ? -1.140  15.095  -2.184  1.00 42.26 ? 285  MET A CE  1 
ATOM   2044 N N   . LEU A 1 286 ? 2.216   18.054  1.832   1.00 34.48 ? 286  LEU A N   1 
ATOM   2045 C CA  . LEU A 1 286 ? 1.967   18.397  3.259   1.00 35.34 ? 286  LEU A CA  1 
ATOM   2046 C C   . LEU A 1 286 ? 2.181   19.903  3.471   1.00 31.35 ? 286  LEU A C   1 
ATOM   2047 O O   . LEU A 1 286 ? 1.347   20.509  4.141   1.00 34.79 ? 286  LEU A O   1 
ATOM   2048 C CB  . LEU A 1 286 ? 2.852   17.524  4.161   1.00 32.90 ? 286  LEU A CB  1 
ATOM   2049 C CG  . LEU A 1 286 ? 2.160   16.352  4.862   1.00 33.38 ? 286  LEU A CG  1 
ATOM   2050 C CD1 . LEU A 1 286 ? 1.280   15.543  3.929   1.00 35.15 ? 286  LEU A CD1 1 
ATOM   2051 C CD2 . LEU A 1 286 ? 3.173   15.445  5.530   1.00 32.82 ? 286  LEU A CD2 1 
ATOM   2052 N N   . THR A 1 287 ? 3.210   20.504  2.884   1.00 34.75 ? 287  THR A N   1 
ATOM   2053 C CA  . THR A 1 287 ? 3.652   21.875  3.261   1.00 37.88 ? 287  THR A CA  1 
ATOM   2054 C C   . THR A 1 287 ? 2.720   22.923  2.643   1.00 41.38 ? 287  THR A C   1 
ATOM   2055 O O   . THR A 1 287 ? 2.770   24.090  3.096   1.00 42.45 ? 287  THR A O   1 
ATOM   2056 C CB  . THR A 1 287 ? 5.122   22.124  2.913   1.00 34.72 ? 287  THR A CB  1 
ATOM   2057 O OG1 . THR A 1 287 ? 5.316   21.903  1.522   1.00 33.66 ? 287  THR A OG1 1 
ATOM   2058 C CG2 . THR A 1 287 ? 6.066   21.231  3.684   1.00 37.09 ? 287  THR A CG2 1 
ATOM   2059 N N   . GLU A 1 288 ? 1.873   22.530  1.691   1.00 44.33 ? 288  GLU A N   1 
ATOM   2060 C CA  . GLU A 1 288 ? 1.072   23.500  0.909   1.00 46.33 ? 288  GLU A CA  1 
ATOM   2061 C C   . GLU A 1 288 ? -0.408  23.413  1.294   1.00 46.26 ? 288  GLU A C   1 
ATOM   2062 O O   . GLU A 1 288 ? -1.162  24.233  0.762   1.00 48.61 ? 288  GLU A O   1 
ATOM   2063 C CB  . GLU A 1 288 ? 1.337   23.305  -0.588  1.00 49.91 ? 288  GLU A CB  1 
ATOM   2064 C CG  . GLU A 1 288 ? 0.478   22.250  -1.267  1.00 49.98 ? 288  GLU A CG  1 
ATOM   2065 C CD  . GLU A 1 288 ? 0.877   21.952  -2.712  1.00 54.65 ? 288  GLU A CD  1 
ATOM   2066 O OE1 . GLU A 1 288 ? 0.037   21.369  -3.438  1.00 56.35 ? 288  GLU A OE1 1 
ATOM   2067 O OE2 . GLU A 1 288 ? 2.036   22.290  -3.118  1.00 50.91 ? 288  GLU A OE2 1 
ATOM   2068 N N   . LEU A 1 289 ? -0.821  22.516  2.203   1.00 43.30 ? 289  LEU A N   1 
ATOM   2069 C CA  . LEU A 1 289 ? -2.268  22.352  2.521   1.00 39.03 ? 289  LEU A CA  1 
ATOM   2070 C C   . LEU A 1 289 ? -2.480  21.885  3.963   1.00 41.89 ? 289  LEU A C   1 
ATOM   2071 O O   . LEU A 1 289 ? -2.033  20.774  4.328   1.00 39.95 ? 289  LEU A O   1 
ATOM   2072 C CB  . LEU A 1 289 ? -2.892  21.370  1.526   1.00 39.57 ? 289  LEU A CB  1 
ATOM   2073 C CG  . LEU A 1 289 ? -4.330  20.956  1.832   1.00 36.16 ? 289  LEU A CG  1 
ATOM   2074 C CD1 . LEU A 1 289 ? -5.237  22.169  1.960   1.00 38.74 ? 289  LEU A CD1 1 
ATOM   2075 C CD2 . LEU A 1 289 ? -4.855  20.020  0.756   1.00 36.85 ? 289  LEU A CD2 1 
ATOM   2076 N N   . ASP A 1 290 ? -3.198  22.693  4.741   1.00 39.06 ? 290  ASP A N   1 
ATOM   2077 C CA  . ASP A 1 290 ? -3.594  22.360  6.128   1.00 38.58 ? 290  ASP A CA  1 
ATOM   2078 C C   . ASP A 1 290 ? -4.701  21.297  6.070   1.00 37.48 ? 290  ASP A C   1 
ATOM   2079 O O   . ASP A 1 290 ? -5.854  21.663  5.875   1.00 32.87 ? 290  ASP A O   1 
ATOM   2080 C CB  . ASP A 1 290 ? -3.979  23.637  6.867   1.00 40.64 ? 290  ASP A CB  1 
ATOM   2081 C CG  . ASP A 1 290 ? -4.575  23.376  8.231   1.00 43.36 ? 290  ASP A CG  1 
ATOM   2082 O OD1 . ASP A 1 290 ? -4.572  22.201  8.655   1.00 42.39 ? 290  ASP A OD1 1 
ATOM   2083 O OD2 . ASP A 1 290 ? -5.054  24.342  8.843   1.00 49.39 ? 290  ASP A OD2 1 
ATOM   2084 N N   . LYS A 1 291 ? -4.359  20.019  6.259   1.00 38.79 ? 291  LYS A N   1 
ATOM   2085 C CA  . LYS A 1 291 ? -5.313  18.875  6.137   1.00 36.97 ? 291  LYS A CA  1 
ATOM   2086 C C   . LYS A 1 291 ? -4.832  17.670  6.966   1.00 36.78 ? 291  LYS A C   1 
ATOM   2087 O O   . LYS A 1 291 ? -3.607  17.445  7.053   1.00 34.65 ? 291  LYS A O   1 
ATOM   2088 C CB  . LYS A 1 291 ? -5.450  18.471  4.664   1.00 36.68 ? 291  LYS A CB  1 
ATOM   2089 C CG  . LYS A 1 291 ? -6.436  17.341  4.392   1.00 36.63 ? 291  LYS A CG  1 
ATOM   2090 C CD  . LYS A 1 291 ? -6.511  16.913  2.935   1.00 35.47 ? 291  LYS A CD  1 
ATOM   2091 C CE  . LYS A 1 291 ? -7.419  15.713  2.758   1.00 37.71 ? 291  LYS A CE  1 
ATOM   2092 N NZ  . LYS A 1 291 ? -7.784  15.502  1.340   1.00 38.68 ? 291  LYS A NZ  1 
ATOM   2093 N N   . LYS A 1 292 ? -5.779  16.919  7.531   1.00 35.90 ? 292  LYS A N   1 
ATOM   2094 C CA  . LYS A 1 292 ? -5.553  15.641  8.246   1.00 37.41 ? 292  LYS A CA  1 
ATOM   2095 C C   . LYS A 1 292 ? -5.910  14.497  7.290   1.00 35.91 ? 292  LYS A C   1 
ATOM   2096 O O   . LYS A 1 292 ? -7.100  14.306  7.033   1.00 37.06 ? 292  LYS A O   1 
ATOM   2097 C CB  . LYS A 1 292 ? -6.393  15.618  9.525   1.00 38.88 ? 292  LYS A CB  1 
ATOM   2098 C CG  . LYS A 1 292 ? -6.112  16.755  10.499  1.00 42.73 ? 292  LYS A CG  1 
ATOM   2099 C CD  . LYS A 1 292 ? -6.936  16.666  11.772  1.00 45.39 ? 292  LYS A CD  1 
ATOM   2100 C CE  . LYS A 1 292 ? -6.395  17.523  12.897  1.00 46.17 ? 292  LYS A CE  1 
ATOM   2101 N NZ  . LYS A 1 292 ? -7.216  17.393  14.123  1.00 50.51 ? 292  LYS A NZ  1 
ATOM   2102 N N   . TRP A 1 293 ? -4.907  13.813  6.738   1.00 32.81 ? 293  TRP A N   1 
ATOM   2103 C CA  . TRP A 1 293 ? -5.061  12.747  5.712   1.00 30.83 ? 293  TRP A CA  1 
ATOM   2104 C C   . TRP A 1 293 ? -5.512  11.435  6.361   1.00 31.92 ? 293  TRP A C   1 
ATOM   2105 O O   . TRP A 1 293 ? -5.170  11.378  7.551   1.00 31.18 ? 293  TRP A O   1 
ATOM   2106 C CB  . TRP A 1 293 ? -3.739  12.593  4.961   1.00 31.68 ? 293  TRP A CB  1 
ATOM   2107 C CG  . TRP A 1 293 ? -3.373  13.803  4.161   1.00 32.99 ? 293  TRP A CG  1 
ATOM   2108 C CD1 . TRP A 1 293 ? -2.651  14.885  4.570   1.00 33.10 ? 293  TRP A CD1 1 
ATOM   2109 C CD2 . TRP A 1 293 ? -3.717  14.047  2.787   1.00 32.30 ? 293  TRP A CD2 1 
ATOM   2110 N NE1 . TRP A 1 293 ? -2.499  15.771  3.537   1.00 32.78 ? 293  TRP A NE1 1 
ATOM   2111 C CE2 . TRP A 1 293 ? -3.156  15.290  2.436   1.00 31.39 ? 293  TRP A CE2 1 
ATOM   2112 C CE3 . TRP A 1 293 ? -4.426  13.325  1.820   1.00 34.29 ? 293  TRP A CE3 1 
ATOM   2113 C CZ2 . TRP A 1 293 ? -3.304  15.836  1.164   1.00 31.18 ? 293  TRP A CZ2 1 
ATOM   2114 C CZ3 . TRP A 1 293 ? -4.556  13.863  0.560   1.00 30.64 ? 293  TRP A CZ3 1 
ATOM   2115 C CH2 . TRP A 1 293 ? -4.005  15.098  0.242   1.00 30.40 ? 293  TRP A CH2 1 
ATOM   2116 N N   . PRO B 1 7   ? 23.840  -19.733 -20.489 1.00 48.71 ? 7    PRO B N   1 
ATOM   2117 C CA  . PRO B 1 7   ? 22.734  -19.825 -19.510 1.00 46.40 ? 7    PRO B CA  1 
ATOM   2118 C C   . PRO B 1 7   ? 21.583  -18.928 -19.989 1.00 43.71 ? 7    PRO B C   1 
ATOM   2119 O O   . PRO B 1 7   ? 21.716  -17.711 -19.949 1.00 44.54 ? 7    PRO B O   1 
ATOM   2120 C CB  . PRO B 1 7   ? 23.284  -19.352 -18.145 1.00 47.35 ? 7    PRO B CB  1 
ATOM   2121 C CG  . PRO B 1 7   ? 24.699  -18.875 -18.438 1.00 47.05 ? 7    PRO B CG  1 
ATOM   2122 C CD  . PRO B 1 7   ? 24.818  -18.781 -19.951 1.00 47.00 ? 7    PRO B CD  1 
ATOM   2123 N N   . HIS B 1 8   ? 20.505  -19.557 -20.454 1.00 42.81 ? 8    HIS B N   1 
ATOM   2124 C CA  . HIS B 1 8   ? 19.319  -18.912 -21.070 1.00 44.37 ? 8    HIS B CA  1 
ATOM   2125 C C   . HIS B 1 8   ? 18.303  -18.561 -19.973 1.00 44.41 ? 8    HIS B C   1 
ATOM   2126 O O   . HIS B 1 8   ? 17.816  -19.497 -19.296 1.00 47.89 ? 8    HIS B O   1 
ATOM   2127 C CB  . HIS B 1 8   ? 18.729  -19.829 -22.154 1.00 46.42 ? 8    HIS B CB  1 
ATOM   2128 C CG  . HIS B 1 8   ? 19.555  -19.886 -23.398 1.00 55.18 ? 8    HIS B CG  1 
ATOM   2129 N ND1 . HIS B 1 8   ? 20.949  -19.933 -23.372 1.00 55.76 ? 8    HIS B ND1 1 
ATOM   2130 C CD2 . HIS B 1 8   ? 19.198  -19.908 -24.703 1.00 54.80 ? 8    HIS B CD2 1 
ATOM   2131 C CE1 . HIS B 1 8   ? 21.407  -19.971 -24.608 1.00 55.59 ? 8    HIS B CE1 1 
ATOM   2132 N NE2 . HIS B 1 8   ? 20.353  -19.955 -25.441 1.00 53.46 ? 8    HIS B NE2 1 
ATOM   2133 N N   . VAL B 1 9   ? 18.015  -17.266 -19.795 1.00 39.96 ? 9    VAL B N   1 
ATOM   2134 C CA  . VAL B 1 9   ? 17.015  -16.730 -18.818 1.00 36.03 ? 9    VAL B CA  1 
ATOM   2135 C C   . VAL B 1 9   ? 16.015  -15.850 -19.582 1.00 34.16 ? 9    VAL B C   1 
ATOM   2136 O O   . VAL B 1 9   ? 16.441  -15.102 -20.490 1.00 31.77 ? 9    VAL B O   1 
ATOM   2137 C CB  . VAL B 1 9   ? 17.725  -15.969 -17.684 1.00 38.51 ? 9    VAL B CB  1 
ATOM   2138 C CG1 . VAL B 1 9   ? 16.749  -15.441 -16.640 1.00 41.15 ? 9    VAL B CG1 1 
ATOM   2139 C CG2 . VAL B 1 9   ? 18.799  -16.818 -17.026 1.00 42.22 ? 9    VAL B CG2 1 
ATOM   2140 N N   . SER B 1 10  ? 14.723  -15.974 -19.273 1.00 32.91 ? 10   SER B N   1 
ATOM   2141 C CA  . SER B 1 10  ? 13.649  -15.094 -19.795 1.00 30.33 ? 10   SER B CA  1 
ATOM   2142 C C   . SER B 1 10  ? 13.157  -14.166 -18.671 1.00 29.39 ? 10   SER B C   1 
ATOM   2143 O O   . SER B 1 10  ? 12.998  -14.636 -17.526 1.00 25.49 ? 10   SER B O   1 
ATOM   2144 C CB  . SER B 1 10  ? 12.553  -15.905 -20.410 1.00 32.49 ? 10   SER B CB  1 
ATOM   2145 O OG  . SER B 1 10  ? 12.849  -16.209 -21.779 1.00 35.93 ? 10   SER B OG  1 
ATOM   2146 N N   . LEU B 1 11  ? 12.944  -12.884 -18.974 1.00 27.10 ? 11   LEU B N   1 
ATOM   2147 C CA  . LEU B 1 11  ? 12.435  -11.874 -18.004 1.00 24.81 ? 11   LEU B CA  1 
ATOM   2148 C C   . LEU B 1 11  ? 11.134  -11.279 -18.541 1.00 23.37 ? 11   LEU B C   1 
ATOM   2149 O O   . LEU B 1 11  ? 11.101  -10.840 -19.699 1.00 24.33 ? 11   LEU B O   1 
ATOM   2150 C CB  . LEU B 1 11  ? 13.509  -10.803 -17.813 1.00 23.04 ? 11   LEU B CB  1 
ATOM   2151 C CG  . LEU B 1 11  ? 13.134  -9.617  -16.935 1.00 23.57 ? 11   LEU B CG  1 
ATOM   2152 C CD1 . LEU B 1 11  ? 12.913  -10.050 -15.493 1.00 23.76 ? 11   LEU B CD1 1 
ATOM   2153 C CD2 . LEU B 1 11  ? 14.223  -8.554  -17.002 1.00 23.33 ? 11   LEU B CD2 1 
ATOM   2154 N N   . ILE B 1 12  ? 10.115  -11.211 -17.703 1.00 23.22 ? 12   ILE B N   1 
ATOM   2155 C CA  . ILE B 1 12  ? 8.806   -10.593 -18.036 1.00 24.00 ? 12   ILE B CA  1 
ATOM   2156 C C   . ILE B 1 12  ? 8.690   -9.382  -17.125 1.00 22.64 ? 12   ILE B C   1 
ATOM   2157 O O   . ILE B 1 12  ? 8.632   -9.579  -15.915 1.00 22.56 ? 12   ILE B O   1 
ATOM   2158 C CB  . ILE B 1 12  ? 7.636   -11.576 -17.823 1.00 27.11 ? 12   ILE B CB  1 
ATOM   2159 C CG1 . ILE B 1 12  ? 7.727   -12.810 -18.729 1.00 29.77 ? 12   ILE B CG1 1 
ATOM   2160 C CG2 . ILE B 1 12  ? 6.299   -10.865 -17.977 1.00 25.41 ? 12   ILE B CG2 1 
ATOM   2161 C CD1 . ILE B 1 12  ? 7.111   -12.601 -20.093 1.00 32.28 ? 12   ILE B CD1 1 
ATOM   2162 N N   . GLY B 1 13  ? 8.694   -8.181  -17.684 1.00 22.16 ? 13   GLY B N   1 
ATOM   2163 C CA  . GLY B 1 13  ? 8.627   -6.943  -16.886 1.00 22.41 ? 13   GLY B CA  1 
ATOM   2164 C C   . GLY B 1 13  ? 9.918   -6.162  -16.973 1.00 21.81 ? 13   GLY B C   1 
ATOM   2165 O O   . GLY B 1 13  ? 10.946  -6.652  -16.460 1.00 21.23 ? 13   GLY B O   1 
ATOM   2166 N N   . LEU B 1 14  ? 9.871   -4.996  -17.610 1.00 21.94 ? 14   LEU B N   1 
ATOM   2167 C CA  . LEU B 1 14  ? 11.033  -4.082  -17.728 1.00 21.28 ? 14   LEU B CA  1 
ATOM   2168 C C   . LEU B 1 14  ? 10.696  -2.711  -17.141 1.00 21.24 ? 14   LEU B C   1 
ATOM   2169 O O   . LEU B 1 14  ? 11.162  -1.711  -17.680 1.00 19.66 ? 14   LEU B O   1 
ATOM   2170 C CB  . LEU B 1 14  ? 11.434  -3.977  -19.202 1.00 21.42 ? 14   LEU B CB  1 
ATOM   2171 C CG  . LEU B 1 14  ? 11.949  -5.258  -19.855 1.00 21.08 ? 14   LEU B CG  1 
ATOM   2172 C CD1 . LEU B 1 14  ? 12.175  -5.044  -21.351 1.00 22.26 ? 14   LEU B CD1 1 
ATOM   2173 C CD2 . LEU B 1 14  ? 13.254  -5.749  -19.215 1.00 20.57 ? 14   LEU B CD2 1 
ATOM   2174 N N   . GLY B 1 15  ? 9.967   -2.658  -16.029 1.00 20.66 ? 15   GLY B N   1 
ATOM   2175 C CA  . GLY B 1 15  ? 9.829   -1.411  -15.250 1.00 20.63 ? 15   GLY B CA  1 
ATOM   2176 C C   . GLY B 1 15  ? 11.114  -1.047  -14.529 1.00 20.02 ? 15   GLY B C   1 
ATOM   2177 O O   . GLY B 1 15  ? 12.157  -1.565  -14.887 1.00 18.87 ? 15   GLY B O   1 
ATOM   2178 N N   . ASN B 1 16  ? 11.037  -0.164  -13.543 1.00 20.72 ? 16   ASN B N   1 
ATOM   2179 C CA  . ASN B 1 16  ? 12.200  0.260   -12.717 1.00 23.14 ? 16   ASN B CA  1 
ATOM   2180 C C   . ASN B 1 16  ? 12.942  -0.969  -12.177 1.00 24.29 ? 16   ASN B C   1 
ATOM   2181 O O   . ASN B 1 16  ? 14.169  -1.063  -12.386 1.00 23.03 ? 16   ASN B O   1 
ATOM   2182 C CB  . ASN B 1 16  ? 11.771  1.167   -11.568 1.00 24.38 ? 16   ASN B CB  1 
ATOM   2183 C CG  . ASN B 1 16  ? 11.244  2.496   -12.067 1.00 24.49 ? 16   ASN B CG  1 
ATOM   2184 O OD1 . ASN B 1 16  ? 10.074  2.794   -11.903 1.00 27.00 ? 16   ASN B OD1 1 
ATOM   2185 N ND2 . ASN B 1 16  ? 12.099  3.289   -12.681 1.00 25.49 ? 16   ASN B ND2 1 
ATOM   2186 N N   . MET B 1 17  ? 12.232  -1.918  -11.568 1.00 22.30 ? 17   MET B N   1 
ATOM   2187 C CA  . MET B 1 17  ? 12.910  -3.096  -10.982 1.00 22.26 ? 17   MET B CA  1 
ATOM   2188 C C   . MET B 1 17  ? 13.265  -4.097  -12.089 1.00 21.66 ? 17   MET B C   1 
ATOM   2189 O O   . MET B 1 17  ? 14.386  -4.583  -12.099 1.00 21.43 ? 17   MET B O   1 
ATOM   2190 C CB  . MET B 1 17  ? 12.071  -3.750  -9.881  1.00 22.85 ? 17   MET B CB  1 
ATOM   2191 C CG  . MET B 1 17  ? 12.855  -4.847  -9.139  1.00 22.60 ? 17   MET B CG  1 
ATOM   2192 S SD  . MET B 1 17  ? 14.404  -4.224  -8.416  1.00 23.54 ? 17   MET B SD  1 
ATOM   2193 C CE  . MET B 1 17  ? 13.771  -3.220  -7.075  1.00 25.93 ? 17   MET B CE  1 
ATOM   2194 N N   . GLY B 1 18  ? 12.344  -4.391  -12.999 1.00 20.48 ? 18   GLY B N   1 
ATOM   2195 C CA  . GLY B 1 18  ? 12.583  -5.316  -14.112 1.00 20.98 ? 18   GLY B CA  1 
ATOM   2196 C C   . GLY B 1 18  ? 13.817  -4.942  -14.914 1.00 22.38 ? 18   GLY B C   1 
ATOM   2197 O O   . GLY B 1 18  ? 14.557  -5.844  -15.290 1.00 21.40 ? 18   GLY B O   1 
ATOM   2198 N N   . LEU B 1 19  ? 14.033  -3.659  -15.198 1.00 24.17 ? 19   LEU B N   1 
ATOM   2199 C CA  . LEU B 1 19  ? 15.208  -3.208  -15.993 1.00 25.70 ? 19   LEU B CA  1 
ATOM   2200 C C   . LEU B 1 19  ? 16.496  -3.420  -15.173 1.00 26.29 ? 19   LEU B C   1 
ATOM   2201 O O   . LEU B 1 19  ? 17.499  -3.870  -15.759 1.00 25.42 ? 19   LEU B O   1 
ATOM   2202 C CB  . LEU B 1 19  ? 15.016  -1.747  -16.413 1.00 27.48 ? 19   LEU B CB  1 
ATOM   2203 C CG  . LEU B 1 19  ? 15.948  -1.296  -17.543 1.00 33.10 ? 19   LEU B CG  1 
ATOM   2204 C CD1 . LEU B 1 19  ? 15.614  -2.019  -18.850 1.00 32.00 ? 19   LEU B CD1 1 
ATOM   2205 C CD2 . LEU B 1 19  ? 15.913  0.225   -17.712 1.00 32.38 ? 19   LEU B CD2 1 
ATOM   2206 N N   . ALA B 1 20  ? 16.470  -3.154  -13.860 1.00 24.96 ? 20   ALA B N   1 
ATOM   2207 C CA  . ALA B 1 20  ? 17.595  -3.431  -12.937 1.00 25.62 ? 20   ALA B CA  1 
ATOM   2208 C C   . ALA B 1 20  ? 17.929  -4.929  -12.932 1.00 26.53 ? 20   ALA B C   1 
ATOM   2209 O O   . ALA B 1 20  ? 19.124  -5.283  -12.964 1.00 28.21 ? 20   ALA B O   1 
ATOM   2210 C CB  . ALA B 1 20  ? 17.257  -2.949  -11.565 1.00 26.58 ? 20   ALA B CB  1 
ATOM   2211 N N   . ILE B 1 21  ? 16.918  -5.797  -12.877 1.00 28.34 ? 21   ILE B N   1 
ATOM   2212 C CA  . ILE B 1 21  ? 17.107  -7.277  -12.901 1.00 26.82 ? 21   ILE B CA  1 
ATOM   2213 C C   . ILE B 1 21  ? 17.803  -7.638  -14.211 1.00 26.60 ? 21   ILE B C   1 
ATOM   2214 O O   . ILE B 1 21  ? 18.774  -8.417  -14.176 1.00 27.76 ? 21   ILE B O   1 
ATOM   2215 C CB  . ILE B 1 21  ? 15.759  -8.003  -12.754 1.00 25.27 ? 21   ILE B CB  1 
ATOM   2216 C CG1 . ILE B 1 21  ? 15.193  -7.823  -11.346 1.00 24.45 ? 21   ILE B CG1 1 
ATOM   2217 C CG2 . ILE B 1 21  ? 15.898  -9.459  -13.147 1.00 26.15 ? 21   ILE B CG2 1 
ATOM   2218 C CD1 . ILE B 1 21  ? 13.783  -8.269  -11.196 1.00 24.30 ? 21   ILE B CD1 1 
ATOM   2219 N N   . ALA B 1 22  ? 17.305  -7.094  -15.315 1.00 24.68 ? 22   ALA B N   1 
ATOM   2220 C CA  . ALA B 1 22  ? 17.822  -7.360  -16.666 1.00 27.54 ? 22   ALA B CA  1 
ATOM   2221 C C   . ALA B 1 22  ? 19.323  -7.044  -16.671 1.00 28.26 ? 22   ALA B C   1 
ATOM   2222 O O   . ALA B 1 22  ? 20.098  -7.867  -17.166 1.00 30.33 ? 22   ALA B O   1 
ATOM   2223 C CB  . ALA B 1 22  ? 17.058  -6.543  -17.678 1.00 27.73 ? 22   ALA B CB  1 
ATOM   2224 N N   . ASN B 1 23  ? 19.706  -5.898  -16.118 1.00 29.52 ? 23   ASN B N   1 
ATOM   2225 C CA  . ASN B 1 23  ? 21.107  -5.410  -16.110 1.00 32.68 ? 23   ASN B CA  1 
ATOM   2226 C C   . ASN B 1 23  ? 21.970  -6.285  -15.195 1.00 34.31 ? 23   ASN B C   1 
ATOM   2227 O O   . ASN B 1 23  ? 23.111  -6.576  -15.589 1.00 38.32 ? 23   ASN B O   1 
ATOM   2228 C CB  . ASN B 1 23  ? 21.172  -3.914  -15.819 1.00 33.40 ? 23   ASN B CB  1 
ATOM   2229 C CG  . ASN B 1 23  ? 20.892  -3.138  -17.083 1.00 32.90 ? 23   ASN B CG  1 
ATOM   2230 O OD1 . ASN B 1 23  ? 21.458  -3.464  -18.122 1.00 33.55 ? 23   ASN B OD1 1 
ATOM   2231 N ND2 . ASN B 1 23  ? 19.985  -2.175  -17.022 1.00 31.08 ? 23   ASN B ND2 1 
ATOM   2232 N N   . CYS B 1 24  ? 21.451  -6.746  -14.059 1.00 32.59 ? 24   CYS B N   1 
ATOM   2233 C CA  . CYS B 1 24  ? 22.148  -7.751  -13.216 1.00 31.30 ? 24   CYS B CA  1 
ATOM   2234 C C   . CYS B 1 24  ? 22.370  -9.051  -14.004 1.00 31.21 ? 24   CYS B C   1 
ATOM   2235 O O   . CYS B 1 24  ? 23.474  -9.610  -13.934 1.00 32.60 ? 24   CYS B O   1 
ATOM   2236 C CB  . CYS B 1 24  ? 21.370  -8.026  -11.942 1.00 29.82 ? 24   CYS B CB  1 
ATOM   2237 S SG  . CYS B 1 24  ? 21.361  -6.608  -10.828 1.00 27.87 ? 24   CYS B SG  1 
ATOM   2238 N N   . LEU B 1 25  ? 21.365  -9.523  -14.733 1.00 32.29 ? 25   LEU B N   1 
ATOM   2239 C CA  . LEU B 1 25  ? 21.417  -10.849 -15.396 1.00 35.00 ? 25   LEU B CA  1 
ATOM   2240 C C   . LEU B 1 25  ? 22.395  -10.795 -16.576 1.00 39.61 ? 25   LEU B C   1 
ATOM   2241 O O   . LEU B 1 25  ? 23.041  -11.824 -16.846 1.00 44.98 ? 25   LEU B O   1 
ATOM   2242 C CB  . LEU B 1 25  ? 20.011  -11.265 -15.834 1.00 32.71 ? 25   LEU B CB  1 
ATOM   2243 C CG  . LEU B 1 25  ? 19.049  -11.609 -14.699 1.00 31.42 ? 25   LEU B CG  1 
ATOM   2244 C CD1 . LEU B 1 25  ? 17.653  -11.852 -15.244 1.00 28.48 ? 25   LEU B CD1 1 
ATOM   2245 C CD2 . LEU B 1 25  ? 19.535  -12.813 -13.910 1.00 32.19 ? 25   LEU B CD2 1 
ATOM   2246 N N   . ILE B 1 26  ? 22.467  -9.657  -17.263 1.00 42.66 ? 26   ILE B N   1 
ATOM   2247 C CA  . ILE B 1 26  ? 23.425  -9.407  -18.376 1.00 45.59 ? 26   ILE B CA  1 
ATOM   2248 C C   . ILE B 1 26  ? 24.834  -9.421  -17.772 1.00 49.41 ? 26   ILE B C   1 
ATOM   2249 O O   . ILE B 1 26  ? 25.628  -10.274 -18.188 1.00 51.45 ? 26   ILE B O   1 
ATOM   2250 C CB  . ILE B 1 26  ? 23.098  -8.094  -19.116 1.00 43.97 ? 26   ILE B CB  1 
ATOM   2251 C CG1 . ILE B 1 26  ? 21.777  -8.191  -19.885 1.00 42.63 ? 26   ILE B CG1 1 
ATOM   2252 C CG2 . ILE B 1 26  ? 24.244  -7.678  -20.031 1.00 43.95 ? 26   ILE B CG2 1 
ATOM   2253 C CD1 . ILE B 1 26  ? 21.212  -6.858  -20.265 1.00 42.41 ? 26   ILE B CD1 1 
ATOM   2254 N N   . LYS B 1 27  ? 25.082  -8.557  -16.783 1.00 50.70 ? 27   LYS B N   1 
ATOM   2255 C CA  . LYS B 1 27  ? 26.372  -8.401  -16.057 1.00 54.69 ? 27   LYS B CA  1 
ATOM   2256 C C   . LYS B 1 27  ? 26.927  -9.767  -15.616 1.00 57.10 ? 27   LYS B C   1 
ATOM   2257 O O   . LYS B 1 27  ? 28.159  -9.880  -15.556 1.00 59.13 ? 27   LYS B O   1 
ATOM   2258 C CB  . LYS B 1 27  ? 26.180  -7.449  -14.872 1.00 56.91 ? 27   LYS B CB  1 
ATOM   2259 C CG  . LYS B 1 27  ? 27.079  -7.690  -13.665 1.00 62.25 ? 27   LYS B CG  1 
ATOM   2260 C CD  . LYS B 1 27  ? 28.530  -7.304  -13.866 1.00 64.60 ? 27   LYS B CD  1 
ATOM   2261 C CE  . LYS B 1 27  ? 28.821  -5.858  -13.517 1.00 67.90 ? 27   LYS B CE  1 
ATOM   2262 N NZ  . LYS B 1 27  ? 28.629  -5.581  -12.071 1.00 69.34 ? 27   LYS B NZ  1 
ATOM   2263 N N   . SER B 1 28  ? 26.064  -10.753 -15.317 1.00 55.60 ? 28   SER B N   1 
ATOM   2264 C CA  . SER B 1 28  ? 26.434  -12.123 -14.861 1.00 50.57 ? 28   SER B CA  1 
ATOM   2265 C C   . SER B 1 28  ? 26.384  -13.145 -16.011 1.00 48.66 ? 28   SER B C   1 
ATOM   2266 O O   . SER B 1 28  ? 26.366  -14.354 -15.716 1.00 46.53 ? 28   SER B O   1 
ATOM   2267 C CB  . SER B 1 28  ? 25.544  -12.564 -13.736 1.00 50.25 ? 28   SER B CB  1 
ATOM   2268 O OG  . SER B 1 28  ? 24.386  -13.208 -14.256 1.00 56.19 ? 28   SER B OG  1 
ATOM   2269 N N   . GLY B 1 29  ? 26.308  -12.692 -17.265 1.00 49.20 ? 29   GLY B N   1 
ATOM   2270 C CA  . GLY B 1 29  ? 26.550  -13.518 -18.465 1.00 51.09 ? 29   GLY B CA  1 
ATOM   2271 C C   . GLY B 1 29  ? 25.411  -14.462 -18.809 1.00 52.67 ? 29   GLY B C   1 
ATOM   2272 O O   . GLY B 1 29  ? 25.696  -15.531 -19.368 1.00 61.32 ? 29   GLY B O   1 
ATOM   2273 N N   . CYS B 1 30  ? 24.164  -14.085 -18.540 1.00 49.29 ? 30   CYS B N   1 
ATOM   2274 C CA  . CYS B 1 30  ? 22.958  -14.805 -19.027 1.00 51.20 ? 30   CYS B CA  1 
ATOM   2275 C C   . CYS B 1 30  ? 22.770  -14.525 -20.526 1.00 47.56 ? 30   CYS B C   1 
ATOM   2276 O O   . CYS B 1 30  ? 23.299  -13.511 -21.000 1.00 48.60 ? 30   CYS B O   1 
ATOM   2277 C CB  . CYS B 1 30  ? 21.722  -14.406 -18.224 1.00 56.48 ? 30   CYS B CB  1 
ATOM   2278 S SG  . CYS B 1 30  ? 21.863  -14.803 -16.455 1.00 62.33 ? 30   CYS B SG  1 
ATOM   2279 N N   . LYS B 1 31  ? 22.086  -15.431 -21.233 1.00 44.44 ? 31   LYS B N   1 
ATOM   2280 C CA  . LYS B 1 31  ? 21.473  -15.210 -22.566 1.00 44.65 ? 31   LYS B CA  1 
ATOM   2281 C C   . LYS B 1 31  ? 20.013  -14.771 -22.376 1.00 37.91 ? 31   LYS B C   1 
ATOM   2282 O O   . LYS B 1 31  ? 19.098  -15.632 -22.319 1.00 32.19 ? 31   LYS B O   1 
ATOM   2283 C CB  . LYS B 1 31  ? 21.530  -16.478 -23.421 1.00 49.92 ? 31   LYS B CB  1 
ATOM   2284 C CG  . LYS B 1 31  ? 20.970  -16.316 -24.828 1.00 53.51 ? 31   LYS B CG  1 
ATOM   2285 C CD  . LYS B 1 31  ? 22.011  -15.827 -25.810 1.00 59.14 ? 31   LYS B CD  1 
ATOM   2286 C CE  . LYS B 1 31  ? 21.421  -15.102 -27.000 1.00 58.94 ? 31   LYS B CE  1 
ATOM   2287 N NZ  . LYS B 1 31  ? 22.243  -15.310 -28.211 1.00 62.56 ? 31   LYS B NZ  1 
ATOM   2288 N N   . LEU B 1 32  ? 19.796  -13.461 -22.301 1.00 34.78 ? 32   LEU B N   1 
ATOM   2289 C CA  . LEU B 1 32  ? 18.513  -12.887 -21.824 1.00 29.37 ? 32   LEU B CA  1 
ATOM   2290 C C   . LEU B 1 32  ? 17.551  -12.691 -22.991 1.00 27.98 ? 32   LEU B C   1 
ATOM   2291 O O   . LEU B 1 32  ? 17.955  -12.044 -23.993 1.00 25.74 ? 32   LEU B O   1 
ATOM   2292 C CB  . LEU B 1 32  ? 18.791  -11.556 -21.131 1.00 30.80 ? 32   LEU B CB  1 
ATOM   2293 C CG  . LEU B 1 32  ? 17.575  -10.954 -20.436 1.00 28.77 ? 32   LEU B CG  1 
ATOM   2294 C CD1 . LEU B 1 32  ? 17.075  -11.916 -19.363 1.00 28.92 ? 32   LEU B CD1 1 
ATOM   2295 C CD2 . LEU B 1 32  ? 17.914  -9.581  -19.870 1.00 26.56 ? 32   LEU B CD2 1 
ATOM   2296 N N   . THR B 1 33  ? 16.338  -13.231 -22.843 1.00 24.58 ? 33   THR B N   1 
ATOM   2297 C CA  . THR B 1 33  ? 15.141  -12.884 -23.636 1.00 27.54 ? 33   THR B CA  1 
ATOM   2298 C C   . THR B 1 33  ? 14.221  -12.064 -22.730 1.00 28.53 ? 33   THR B C   1 
ATOM   2299 O O   . THR B 1 33  ? 14.054  -12.461 -21.579 1.00 28.93 ? 33   THR B O   1 
ATOM   2300 C CB  . THR B 1 33  ? 14.458  -14.145 -24.179 1.00 28.49 ? 33   THR B CB  1 
ATOM   2301 O OG1 . THR B 1 33  ? 15.494  -14.947 -24.755 1.00 32.56 ? 33   THR B OG1 1 
ATOM   2302 C CG2 . THR B 1 33  ? 13.374  -13.848 -25.189 1.00 27.46 ? 33   THR B CG2 1 
ATOM   2303 N N   . VAL B 1 34  ? 13.639  -10.974 -23.230 1.00 27.72 ? 34   VAL B N   1 
ATOM   2304 C CA  . VAL B 1 34  ? 12.787  -10.088 -22.397 1.00 25.43 ? 34   VAL B CA  1 
ATOM   2305 C C   . VAL B 1 34  ? 11.436  -9.909  -23.082 1.00 26.20 ? 34   VAL B C   1 
ATOM   2306 O O   . VAL B 1 34  ? 11.341  -10.003 -24.334 1.00 26.15 ? 34   VAL B O   1 
ATOM   2307 C CB  . VAL B 1 34  ? 13.460  -8.739  -22.119 1.00 24.62 ? 34   VAL B CB  1 
ATOM   2308 C CG1 . VAL B 1 34  ? 14.760  -8.921  -21.348 1.00 24.36 ? 34   VAL B CG1 1 
ATOM   2309 C CG2 . VAL B 1 34  ? 13.690  -7.933  -23.389 1.00 25.34 ? 34   VAL B CG2 1 
ATOM   2310 N N   . TRP B 1 35  ? 10.431  -9.620  -22.277 1.00 24.13 ? 35   TRP B N   1 
ATOM   2311 C CA  . TRP B 1 35  ? 9.149   -9.087  -22.784 1.00 23.95 ? 35   TRP B CA  1 
ATOM   2312 C C   . TRP B 1 35  ? 8.665   -8.027  -21.809 1.00 23.38 ? 35   TRP B C   1 
ATOM   2313 O O   . TRP B 1 35  ? 8.869   -8.183  -20.588 1.00 21.99 ? 35   TRP B O   1 
ATOM   2314 C CB  . TRP B 1 35  ? 8.128   -10.196 -23.016 1.00 24.55 ? 35   TRP B CB  1 
ATOM   2315 C CG  . TRP B 1 35  ? 6.841   -9.655  -23.545 1.00 26.57 ? 35   TRP B CG  1 
ATOM   2316 C CD1 . TRP B 1 35  ? 6.475   -9.526  -24.851 1.00 29.18 ? 35   TRP B CD1 1 
ATOM   2317 C CD2 . TRP B 1 35  ? 5.765   -9.101  -22.775 1.00 28.33 ? 35   TRP B CD2 1 
ATOM   2318 N NE1 . TRP B 1 35  ? 5.234   -8.958  -24.942 1.00 29.79 ? 35   TRP B NE1 1 
ATOM   2319 C CE2 . TRP B 1 35  ? 4.773   -8.690  -23.685 1.00 28.00 ? 35   TRP B CE2 1 
ATOM   2320 C CE3 . TRP B 1 35  ? 5.540   -8.945  -21.409 1.00 27.69 ? 35   TRP B CE3 1 
ATOM   2321 C CZ2 . TRP B 1 35  ? 3.586   -8.094  -23.279 1.00 30.14 ? 35   TRP B CZ2 1 
ATOM   2322 C CZ3 . TRP B 1 35  ? 4.360   -8.366  -21.004 1.00 32.87 ? 35   TRP B CZ3 1 
ATOM   2323 C CH2 . TRP B 1 35  ? 3.401   -7.941  -21.926 1.00 30.84 ? 35   TRP B CH2 1 
ATOM   2324 N N   . ASN B 1 36  ? 8.125   -6.950  -22.355 1.00 20.97 ? 36   ASN B N   1 
ATOM   2325 C CA  . ASN B 1 36  ? 7.448   -5.887  -21.580 1.00 22.56 ? 36   ASN B CA  1 
ATOM   2326 C C   . ASN B 1 36  ? 6.288   -5.388  -22.451 1.00 21.41 ? 36   ASN B C   1 
ATOM   2327 O O   . ASN B 1 36  ? 6.441   -5.380  -23.672 1.00 21.42 ? 36   ASN B O   1 
ATOM   2328 C CB  . ASN B 1 36  ? 8.428   -4.776  -21.184 1.00 21.47 ? 36   ASN B CB  1 
ATOM   2329 C CG  . ASN B 1 36  ? 7.837   -3.812  -20.180 1.00 21.44 ? 36   ASN B CG  1 
ATOM   2330 O OD1 . ASN B 1 36  ? 7.425   -4.240  -19.109 1.00 20.16 ? 36   ASN B OD1 1 
ATOM   2331 N ND2 . ASN B 1 36  ? 7.782   -2.524  -20.513 1.00 19.94 ? 36   ASN B ND2 1 
ATOM   2332 N N   . ARG B 1 37  ? 5.179   -5.000  -21.845 1.00 24.12 ? 37   ARG B N   1 
ATOM   2333 C CA  . ARG B 1 37  ? 4.065   -4.328  -22.558 1.00 25.53 ? 37   ARG B CA  1 
ATOM   2334 C C   . ARG B 1 37  ? 4.633   -3.206  -23.436 1.00 28.29 ? 37   ARG B C   1 
ATOM   2335 O O   . ARG B 1 37  ? 4.377   -3.251  -24.644 1.00 29.44 ? 37   ARG B O   1 
ATOM   2336 C CB  . ARG B 1 37  ? 3.066   -3.767  -21.553 1.00 26.71 ? 37   ARG B CB  1 
ATOM   2337 C CG  . ARG B 1 37  ? 1.995   -2.873  -22.163 1.00 27.22 ? 37   ARG B CG  1 
ATOM   2338 C CD  . ARG B 1 37  ? 1.029   -2.456  -21.087 1.00 28.23 ? 37   ARG B CD  1 
ATOM   2339 N NE  . ARG B 1 37  ? 1.663   -1.567  -20.123 1.00 28.94 ? 37   ARG B NE  1 
ATOM   2340 C CZ  . ARG B 1 37  ? 1.022   -0.990  -19.122 1.00 30.59 ? 37   ARG B CZ  1 
ATOM   2341 N NH1 . ARG B 1 37  ? 1.672   -0.192  -18.292 1.00 31.00 ? 37   ARG B NH1 1 
ATOM   2342 N NH2 . ARG B 1 37  ? -0.266  -1.244  -18.938 1.00 33.55 ? 37   ARG B NH2 1 
ATOM   2343 N N   . SER B 1 38  ? 5.344   -2.230  -22.850 1.00 27.25 ? 38   SER B N   1 
ATOM   2344 C CA  . SER B 1 38  ? 6.103   -1.190  -23.597 1.00 28.43 ? 38   SER B CA  1 
ATOM   2345 C C   . SER B 1 38  ? 7.476   -1.746  -23.997 1.00 26.78 ? 38   SER B C   1 
ATOM   2346 O O   . SER B 1 38  ? 8.409   -1.732  -23.147 1.00 25.91 ? 38   SER B O   1 
ATOM   2347 C CB  . SER B 1 38  ? 6.225   0.100   -22.821 1.00 28.61 ? 38   SER B CB  1 
ATOM   2348 O OG  . SER B 1 38  ? 5.020   0.411   -22.144 1.00 29.86 ? 38   SER B OG  1 
ATOM   2349 N N   . ALA B 1 39  ? 7.602   -2.200  -25.248 1.00 28.49 ? 39   ALA B N   1 
ATOM   2350 C CA  . ALA B 1 39  ? 8.805   -2.870  -25.805 1.00 29.23 ? 39   ALA B CA  1 
ATOM   2351 C C   . ALA B 1 39  ? 9.997   -1.911  -25.779 1.00 30.09 ? 39   ALA B C   1 
ATOM   2352 O O   . ALA B 1 39  ? 11.131  -2.377  -25.563 1.00 38.43 ? 39   ALA B O   1 
ATOM   2353 C CB  . ALA B 1 39  ? 8.529   -3.383  -27.202 1.00 29.85 ? 39   ALA B CB  1 
ATOM   2354 N N   . SER B 1 40  ? 9.738   -0.616  -25.909 1.00 29.69 ? 40   SER B N   1 
ATOM   2355 C CA  . SER B 1 40  ? 10.762  0.457   -26.018 1.00 31.59 ? 40   SER B CA  1 
ATOM   2356 C C   . SER B 1 40  ? 11.677  0.422   -24.794 1.00 28.80 ? 40   SER B C   1 
ATOM   2357 O O   . SER B 1 40  ? 12.840  0.796   -24.922 1.00 32.16 ? 40   SER B O   1 
ATOM   2358 C CB  . SER B 1 40  ? 10.109  1.817   -26.179 1.00 30.62 ? 40   SER B CB  1 
ATOM   2359 O OG  . SER B 1 40  ? 9.414   2.183   -24.992 1.00 34.63 ? 40   SER B OG  1 
ATOM   2360 N N   . LYS B 1 41  ? 11.168  -0.055  -23.664 1.00 26.28 ? 41   LYS B N   1 
ATOM   2361 C CA  . LYS B 1 41  ? 11.918  -0.162  -22.391 1.00 27.00 ? 41   LYS B CA  1 
ATOM   2362 C C   . LYS B 1 41  ? 13.043  -1.201  -22.520 1.00 27.59 ? 41   LYS B C   1 
ATOM   2363 O O   . LYS B 1 41  ? 13.885  -1.254  -21.607 1.00 31.38 ? 41   LYS B O   1 
ATOM   2364 C CB  . LYS B 1 41  ? 10.945  -0.519  -21.263 1.00 28.18 ? 41   LYS B CB  1 
ATOM   2365 C CG  . LYS B 1 41  ? 9.724   0.387   -21.126 1.00 28.81 ? 41   LYS B CG  1 
ATOM   2366 C CD  . LYS B 1 41  ? 9.868   1.471   -20.108 1.00 31.35 ? 41   LYS B CD  1 
ATOM   2367 C CE  . LYS B 1 41  ? 8.547   2.007   -19.589 1.00 31.77 ? 41   LYS B CE  1 
ATOM   2368 N NZ  . LYS B 1 41  ? 8.115   1.294   -18.361 1.00 33.08 ? 41   LYS B NZ  1 
ATOM   2369 N N   . ALA B 1 42  ? 13.068  -2.009  -23.590 1.00 28.10 ? 42   ALA B N   1 
ATOM   2370 C CA  . ALA B 1 42  ? 14.170  -2.967  -23.874 1.00 30.22 ? 42   ALA B CA  1 
ATOM   2371 C C   . ALA B 1 42  ? 15.302  -2.302  -24.679 1.00 29.68 ? 42   ALA B C   1 
ATOM   2372 O O   . ALA B 1 42  ? 16.318  -2.976  -24.920 1.00 30.06 ? 42   ALA B O   1 
ATOM   2373 C CB  . ALA B 1 42  ? 13.644  -4.202  -24.583 1.00 30.25 ? 42   ALA B CB  1 
ATOM   2374 N N   . ALA B 1 43  ? 15.169  -1.031  -25.055 1.00 28.36 ? 43   ALA B N   1 
ATOM   2375 C CA  . ALA B 1 43  ? 16.120  -0.321  -25.946 1.00 28.76 ? 43   ALA B CA  1 
ATOM   2376 C C   . ALA B 1 43  ? 17.540  -0.325  -25.355 1.00 28.94 ? 43   ALA B C   1 
ATOM   2377 O O   . ALA B 1 43  ? 18.495  -0.558  -26.117 1.00 27.13 ? 43   ALA B O   1 
ATOM   2378 C CB  . ALA B 1 43  ? 15.628  1.079   -26.208 1.00 27.41 ? 43   ALA B CB  1 
ATOM   2379 N N   . SER B 1 44  ? 17.699  -0.074  -24.054 1.00 30.77 ? 44   SER B N   1 
ATOM   2380 C CA  . SER B 1 44  ? 19.031  -0.035  -23.382 1.00 32.85 ? 44   SER B CA  1 
ATOM   2381 C C   . SER B 1 44  ? 19.645  -1.444  -23.304 1.00 33.52 ? 44   SER B C   1 
ATOM   2382 O O   . SER B 1 44  ? 20.837  -1.549  -22.978 1.00 34.98 ? 44   SER B O   1 
ATOM   2383 C CB  . SER B 1 44  ? 18.938  0.562   -22.012 1.00 31.32 ? 44   SER B CB  1 
ATOM   2384 O OG  . SER B 1 44  ? 18.226  -0.319  -21.154 1.00 30.12 ? 44   SER B OG  1 
ATOM   2385 N N   . LEU B 1 45  ? 18.864  -2.488  -23.585 1.00 32.46 ? 45   LEU B N   1 
ATOM   2386 C CA  . LEU B 1 45  ? 19.307  -3.898  -23.456 1.00 33.75 ? 45   LEU B CA  1 
ATOM   2387 C C   . LEU B 1 45  ? 19.751  -4.457  -24.805 1.00 34.67 ? 45   LEU B C   1 
ATOM   2388 O O   . LEU B 1 45  ? 20.519  -5.417  -24.768 1.00 31.26 ? 45   LEU B O   1 
ATOM   2389 C CB  . LEU B 1 45  ? 18.164  -4.730  -22.873 1.00 32.67 ? 45   LEU B CB  1 
ATOM   2390 C CG  . LEU B 1 45  ? 17.593  -4.184  -21.569 1.00 31.44 ? 45   LEU B CG  1 
ATOM   2391 C CD1 . LEU B 1 45  ? 16.386  -5.003  -21.150 1.00 30.42 ? 45   LEU B CD1 1 
ATOM   2392 C CD2 . LEU B 1 45  ? 18.672  -4.157  -20.484 1.00 31.12 ? 45   LEU B CD2 1 
ATOM   2393 N N   . VAL B 1 46  ? 19.275  -3.907  -25.930 1.00 34.31 ? 46   VAL B N   1 
ATOM   2394 C CA  . VAL B 1 46  ? 19.556  -4.479  -27.278 1.00 38.43 ? 46   VAL B CA  1 
ATOM   2395 C C   . VAL B 1 46  ? 21.059  -4.331  -27.599 1.00 38.70 ? 46   VAL B C   1 
ATOM   2396 O O   . VAL B 1 46  ? 21.659  -5.333  -27.997 1.00 36.65 ? 46   VAL B O   1 
ATOM   2397 C CB  . VAL B 1 46  ? 18.609  -3.899  -28.346 1.00 39.13 ? 46   VAL B CB  1 
ATOM   2398 C CG1 . VAL B 1 46  ? 18.994  -4.331  -29.756 1.00 40.04 ? 46   VAL B CG1 1 
ATOM   2399 C CG2 . VAL B 1 46  ? 17.166  -4.287  -28.049 1.00 38.39 ? 46   VAL B CG2 1 
ATOM   2400 N N   . ALA B 1 47  ? 21.683  -3.185  -27.330 1.00 44.34 ? 47   ALA B N   1 
ATOM   2401 C CA  . ALA B 1 47  ? 23.157  -3.011  -27.407 1.00 49.21 ? 47   ALA B CA  1 
ATOM   2402 C C   . ALA B 1 47  ? 23.853  -4.202  -26.736 1.00 51.87 ? 47   ALA B C   1 
ATOM   2403 O O   . ALA B 1 47  ? 24.798  -4.781  -27.323 1.00 53.21 ? 47   ALA B O   1 
ATOM   2404 C CB  . ALA B 1 47  ? 23.570  -1.724  -26.738 1.00 53.16 ? 47   ALA B CB  1 
ATOM   2405 N N   . GLN B 1 48  ? 23.379  -4.572  -25.547 1.00 48.37 ? 48   GLN B N   1 
ATOM   2406 C CA  . GLN B 1 48  ? 24.048  -5.550  -24.659 1.00 45.45 ? 48   GLN B CA  1 
ATOM   2407 C C   . GLN B 1 48  ? 23.761  -6.970  -25.159 1.00 42.00 ? 48   GLN B C   1 
ATOM   2408 O O   . GLN B 1 48  ? 24.212  -7.921  -24.511 1.00 47.05 ? 48   GLN B O   1 
ATOM   2409 C CB  . GLN B 1 48  ? 23.594  -5.308  -23.219 1.00 50.00 ? 48   GLN B CB  1 
ATOM   2410 C CG  . GLN B 1 48  ? 23.501  -3.827  -22.846 1.00 49.75 ? 48   GLN B CG  1 
ATOM   2411 C CD  . GLN B 1 48  ? 23.345  -3.625  -21.359 1.00 47.60 ? 48   GLN B CD  1 
ATOM   2412 O OE1 . GLN B 1 48  ? 24.076  -4.210  -20.562 1.00 48.50 ? 48   GLN B OE1 1 
ATOM   2413 N NE2 . GLN B 1 48  ? 22.378  -2.807  -20.974 1.00 40.74 ? 48   GLN B NE2 1 
ATOM   2414 N N   . GLY B 1 49  ? 23.021  -7.115  -26.256 1.00 39.09 ? 49   GLY B N   1 
ATOM   2415 C CA  . GLY B 1 49  ? 22.811  -8.406  -26.936 1.00 39.09 ? 49   GLY B CA  1 
ATOM   2416 C C   . GLY B 1 49  ? 21.567  -9.148  -26.470 1.00 38.65 ? 49   GLY B C   1 
ATOM   2417 O O   . GLY B 1 49  ? 21.495  -10.361 -26.730 1.00 40.56 ? 49   GLY B O   1 
ATOM   2418 N N   . VAL B 1 50  ? 20.590  -8.486  -25.839 1.00 40.30 ? 50   VAL B N   1 
ATOM   2419 C CA  . VAL B 1 50  ? 19.354  -9.191  -25.364 1.00 38.56 ? 50   VAL B CA  1 
ATOM   2420 C C   . VAL B 1 50  ? 18.376  -9.289  -26.529 1.00 35.29 ? 50   VAL B C   1 
ATOM   2421 O O   . VAL B 1 50  ? 18.355  -8.352  -27.367 1.00 34.76 ? 50   VAL B O   1 
ATOM   2422 C CB  . VAL B 1 50  ? 18.693  -8.571  -24.114 1.00 41.63 ? 50   VAL B CB  1 
ATOM   2423 C CG1 . VAL B 1 50  ? 19.711  -7.895  -23.205 1.00 40.52 ? 50   VAL B CG1 1 
ATOM   2424 C CG2 . VAL B 1 50  ? 17.540  -7.640  -24.443 1.00 44.27 ? 50   VAL B CG2 1 
ATOM   2425 N N   . THR B 1 51  ? 17.631  -10.399 -26.564 1.00 33.00 ? 51   THR B N   1 
ATOM   2426 C CA  . THR B 1 51  ? 16.520  -10.698 -27.511 1.00 32.40 ? 51   THR B CA  1 
ATOM   2427 C C   . THR B 1 51  ? 15.200  -10.222 -26.905 1.00 30.57 ? 51   THR B C   1 
ATOM   2428 O O   . THR B 1 51  ? 14.922  -10.544 -25.732 1.00 30.50 ? 51   THR B O   1 
ATOM   2429 C CB  . THR B 1 51  ? 16.461  -12.199 -27.829 1.00 33.06 ? 51   THR B CB  1 
ATOM   2430 O OG1 . THR B 1 51  ? 17.773  -12.584 -28.228 1.00 30.65 ? 51   THR B OG1 1 
ATOM   2431 C CG2 . THR B 1 51  ? 15.456  -12.565 -28.898 1.00 34.38 ? 51   THR B CG2 1 
ATOM   2432 N N   . VAL B 1 52  ? 14.418  -9.483  -27.687 1.00 29.83 ? 52   VAL B N   1 
ATOM   2433 C CA  . VAL B 1 52  ? 13.058  -9.013  -27.335 1.00 29.58 ? 52   VAL B CA  1 
ATOM   2434 C C   . VAL B 1 52  ? 12.067  -9.979  -27.979 1.00 31.95 ? 52   VAL B C   1 
ATOM   2435 O O   . VAL B 1 52  ? 12.117  -10.134 -29.202 1.00 29.93 ? 52   VAL B O   1 
ATOM   2436 C CB  . VAL B 1 52  ? 12.830  -7.574  -27.822 1.00 30.65 ? 52   VAL B CB  1 
ATOM   2437 C CG1 . VAL B 1 52  ? 11.495  -7.050  -27.339 1.00 32.21 ? 52   VAL B CG1 1 
ATOM   2438 C CG2 . VAL B 1 52  ? 13.971  -6.650  -27.402 1.00 30.17 ? 52   VAL B CG2 1 
ATOM   2439 N N   . ALA B 1 53  ? 11.224  -10.634 -27.181 1.00 32.27 ? 53   ALA B N   1 
ATOM   2440 C CA  . ALA B 1 53  ? 10.184  -11.567 -27.673 1.00 30.98 ? 53   ALA B CA  1 
ATOM   2441 C C   . ALA B 1 53  ? 8.946   -10.737 -28.007 1.00 27.03 ? 53   ALA B C   1 
ATOM   2442 O O   . ALA B 1 53  ? 8.781   -9.676  -27.432 1.00 26.37 ? 53   ALA B O   1 
ATOM   2443 C CB  . ALA B 1 53  ? 9.903   -12.632 -26.632 1.00 33.12 ? 53   ALA B CB  1 
ATOM   2444 N N   . ALA B 1 54  ? 8.103   -11.199 -28.911 1.00 28.07 ? 54   ALA B N   1 
ATOM   2445 C CA  . ALA B 1 54  ? 6.919   -10.442 -29.361 1.00 27.64 ? 54   ALA B CA  1 
ATOM   2446 C C   . ALA B 1 54  ? 5.813   -10.540 -28.301 1.00 26.74 ? 54   ALA B C   1 
ATOM   2447 O O   . ALA B 1 54  ? 5.001   -9.618  -28.188 1.00 29.45 ? 54   ALA B O   1 
ATOM   2448 C CB  . ALA B 1 54  ? 6.495   -10.980 -30.704 1.00 30.21 ? 54   ALA B CB  1 
ATOM   2449 N N   . THR B 1 55  ? 5.772   -11.634 -27.548 1.00 28.11 ? 55   THR B N   1 
ATOM   2450 C CA  . THR B 1 55  ? 4.640   -11.982 -26.650 1.00 29.02 ? 55   THR B CA  1 
ATOM   2451 C C   . THR B 1 55  ? 5.156   -12.658 -25.386 1.00 27.55 ? 55   THR B C   1 
ATOM   2452 O O   . THR B 1 55  ? 6.220   -13.267 -25.378 1.00 28.35 ? 55   THR B O   1 
ATOM   2453 C CB  . THR B 1 55  ? 3.661   -12.958 -27.318 1.00 29.62 ? 55   THR B CB  1 
ATOM   2454 O OG1 . THR B 1 55  ? 4.370   -14.191 -27.471 1.00 31.09 ? 55   THR B OG1 1 
ATOM   2455 C CG2 . THR B 1 55  ? 3.120   -12.456 -28.638 1.00 31.43 ? 55   THR B CG2 1 
ATOM   2456 N N   . PRO B 1 56  ? 4.392   -12.626 -24.282 1.00 28.71 ? 56   PRO B N   1 
ATOM   2457 C CA  . PRO B 1 56  ? 4.758   -13.404 -23.102 1.00 29.79 ? 56   PRO B CA  1 
ATOM   2458 C C   . PRO B 1 56  ? 5.022   -14.860 -23.503 1.00 28.51 ? 56   PRO B C   1 
ATOM   2459 O O   . PRO B 1 56  ? 6.097   -15.371 -23.203 1.00 32.23 ? 56   PRO B O   1 
ATOM   2460 C CB  . PRO B 1 56  ? 3.545   -13.191 -22.184 1.00 29.27 ? 56   PRO B CB  1 
ATOM   2461 C CG  . PRO B 1 56  ? 3.068   -11.825 -22.588 1.00 30.12 ? 56   PRO B CG  1 
ATOM   2462 C CD  . PRO B 1 56  ? 3.173   -11.830 -24.096 1.00 28.86 ? 56   PRO B CD  1 
ATOM   2463 N N   . ALA B 1 57  ? 4.069   -15.485 -24.193 1.00 31.32 ? 57   ALA B N   1 
ATOM   2464 C CA  . ALA B 1 57  ? 4.178   -16.889 -24.659 1.00 32.98 ? 57   ALA B CA  1 
ATOM   2465 C C   . ALA B 1 57  ? 5.548   -17.109 -25.314 1.00 33.55 ? 57   ALA B C   1 
ATOM   2466 O O   . ALA B 1 57  ? 6.283   -18.032 -24.906 1.00 33.79 ? 57   ALA B O   1 
ATOM   2467 C CB  . ALA B 1 57  ? 3.038   -17.220 -25.598 1.00 35.10 ? 57   ALA B CB  1 
ATOM   2468 N N   . GLU B 1 58  ? 5.933   -16.277 -26.283 1.00 36.96 ? 58   GLU B N   1 
ATOM   2469 C CA  . GLU B 1 58  ? 7.203   -16.497 -27.034 1.00 34.99 ? 58   GLU B CA  1 
ATOM   2470 C C   . GLU B 1 58  ? 8.406   -16.201 -26.141 1.00 32.98 ? 58   GLU B C   1 
ATOM   2471 O O   . GLU B 1 58  ? 9.466   -16.821 -26.344 1.00 34.67 ? 58   GLU B O   1 
ATOM   2472 C CB  . GLU B 1 58  ? 7.258   -15.629 -28.284 1.00 40.47 ? 58   GLU B CB  1 
ATOM   2473 C CG  . GLU B 1 58  ? 6.215   -16.004 -29.306 1.00 42.78 ? 58   GLU B CG  1 
ATOM   2474 C CD  . GLU B 1 58  ? 6.250   -15.069 -30.494 1.00 43.96 ? 58   GLU B CD  1 
ATOM   2475 O OE1 . GLU B 1 58  ? 7.352   -14.873 -31.052 1.00 40.31 ? 58   GLU B OE1 1 
ATOM   2476 O OE2 . GLU B 1 58  ? 5.191   -14.517 -30.826 1.00 48.00 ? 58   GLU B OE2 1 
ATOM   2477 N N   . CYS B 1 59  ? 8.280   -15.263 -25.204 1.00 30.79 ? 59   CYS B N   1 
ATOM   2478 C CA  . CYS B 1 59  ? 9.357   -14.997 -24.221 1.00 27.63 ? 59   CYS B CA  1 
ATOM   2479 C C   . CYS B 1 59  ? 9.570   -16.238 -23.336 1.00 29.60 ? 59   CYS B C   1 
ATOM   2480 O O   . CYS B 1 59  ? 10.743  -16.662 -23.154 1.00 26.47 ? 59   CYS B O   1 
ATOM   2481 C CB  . CYS B 1 59  ? 9.043   -13.788 -23.356 1.00 27.72 ? 59   CYS B CB  1 
ATOM   2482 S SG  . CYS B 1 59  ? 10.443  -13.390 -22.285 1.00 29.00 ? 59   CYS B SG  1 
ATOM   2483 N N   . VAL B 1 60  ? 8.485   -16.803 -22.802 1.00 32.13 ? 60   VAL B N   1 
ATOM   2484 C CA  . VAL B 1 60  ? 8.527   -18.006 -21.903 1.00 35.26 ? 60   VAL B CA  1 
ATOM   2485 C C   . VAL B 1 60  ? 9.076   -19.188 -22.718 1.00 36.74 ? 60   VAL B C   1 
ATOM   2486 O O   . VAL B 1 60  ? 10.040  -19.834 -22.276 1.00 38.66 ? 60   VAL B O   1 
ATOM   2487 C CB  . VAL B 1 60  ? 7.137   -18.288 -21.292 1.00 36.46 ? 60   VAL B CB  1 
ATOM   2488 C CG1 . VAL B 1 60  ? 7.047   -19.671 -20.665 1.00 38.28 ? 60   VAL B CG1 1 
ATOM   2489 C CG2 . VAL B 1 60  ? 6.726   -17.226 -20.281 1.00 35.04 ? 60   VAL B CG2 1 
ATOM   2490 N N   . ALA B 1 61  ? 8.530   -19.387 -23.919 1.00 40.13 ? 61   ALA B N   1 
ATOM   2491 C CA  . ALA B 1 61  ? 8.997   -20.358 -24.934 1.00 44.05 ? 61   ALA B CA  1 
ATOM   2492 C C   . ALA B 1 61  ? 10.522  -20.311 -25.111 1.00 43.77 ? 61   ALA B C   1 
ATOM   2493 O O   . ALA B 1 61  ? 11.071  -21.353 -25.480 1.00 53.16 ? 61   ALA B O   1 
ATOM   2494 C CB  . ALA B 1 61  ? 8.292   -20.106 -26.252 1.00 43.52 ? 61   ALA B CB  1 
ATOM   2495 N N   . SER B 1 62  ? 11.191  -19.178 -24.871 1.00 41.34 ? 62   SER B N   1 
ATOM   2496 C CA  . SER B 1 62  ? 12.605  -18.946 -25.279 1.00 40.00 ? 62   SER B CA  1 
ATOM   2497 C C   . SER B 1 62  ? 13.645  -19.497 -24.289 1.00 39.88 ? 62   SER B C   1 
ATOM   2498 O O   . SER B 1 62  ? 14.835  -19.546 -24.689 1.00 34.68 ? 62   SER B O   1 
ATOM   2499 C CB  . SER B 1 62  ? 12.867  -17.464 -25.522 1.00 42.08 ? 62   SER B CB  1 
ATOM   2500 O OG  . SER B 1 62  ? 11.891  -16.911 -26.397 1.00 42.77 ? 62   SER B OG  1 
ATOM   2501 N N   . SER B 1 63  ? 13.289  -19.806 -23.033 1.00 38.68 ? 63   SER B N   1 
ATOM   2502 C CA  . SER B 1 63  ? 14.287  -20.096 -21.958 1.00 37.76 ? 63   SER B CA  1 
ATOM   2503 C C   . SER B 1 63  ? 13.746  -21.121 -20.970 1.00 36.03 ? 63   SER B C   1 
ATOM   2504 O O   . SER B 1 63  ? 12.543  -21.165 -20.737 1.00 39.38 ? 63   SER B O   1 
ATOM   2505 C CB  . SER B 1 63  ? 14.681  -18.852 -21.208 1.00 36.32 ? 63   SER B CB  1 
ATOM   2506 O OG  . SER B 1 63  ? 15.244  -17.867 -22.053 1.00 42.52 ? 63   SER B OG  1 
ATOM   2507 N N   . PRO B 1 64  ? 14.626  -21.917 -20.314 1.00 38.76 ? 64   PRO B N   1 
ATOM   2508 C CA  . PRO B 1 64  ? 14.211  -22.853 -19.261 1.00 41.52 ? 64   PRO B CA  1 
ATOM   2509 C C   . PRO B 1 64  ? 13.780  -22.167 -17.949 1.00 39.49 ? 64   PRO B C   1 
ATOM   2510 O O   . PRO B 1 64  ? 12.953  -22.720 -17.243 1.00 32.39 ? 64   PRO B O   1 
ATOM   2511 C CB  . PRO B 1 64  ? 15.500  -23.661 -19.004 1.00 40.82 ? 64   PRO B CB  1 
ATOM   2512 C CG  . PRO B 1 64  ? 16.600  -22.682 -19.300 1.00 42.22 ? 64   PRO B CG  1 
ATOM   2513 C CD  . PRO B 1 64  ? 16.085  -21.911 -20.497 1.00 39.44 ? 64   PRO B CD  1 
ATOM   2514 N N   . THR B 1 65  ? 14.396  -21.016 -17.639 1.00 35.95 ? 65   THR B N   1 
ATOM   2515 C CA  . THR B 1 65  ? 14.215  -20.241 -16.380 1.00 34.11 ? 65   THR B CA  1 
ATOM   2516 C C   . THR B 1 65  ? 13.526  -18.909 -16.700 1.00 33.00 ? 65   THR B C   1 
ATOM   2517 O O   . THR B 1 65  ? 14.114  -18.116 -17.456 1.00 31.99 ? 65   THR B O   1 
ATOM   2518 C CB  . THR B 1 65  ? 15.564  -20.023 -15.686 1.00 37.70 ? 65   THR B CB  1 
ATOM   2519 O OG1 . THR B 1 65  ? 16.150  -21.315 -15.526 1.00 39.68 ? 65   THR B OG1 1 
ATOM   2520 C CG2 . THR B 1 65  ? 15.452  -19.328 -14.343 1.00 38.49 ? 65   THR B CG2 1 
ATOM   2521 N N   . ILE B 1 66  ? 12.322  -18.701 -16.163 1.00 30.53 ? 66   ILE B N   1 
ATOM   2522 C CA  . ILE B 1 66  ? 11.501  -17.467 -16.308 1.00 29.23 ? 66   ILE B CA  1 
ATOM   2523 C C   . ILE B 1 66  ? 11.583  -16.603 -15.028 1.00 29.49 ? 66   ILE B C   1 
ATOM   2524 O O   . ILE B 1 66  ? 11.170  -17.079 -13.945 1.00 29.44 ? 66   ILE B O   1 
ATOM   2525 C CB  . ILE B 1 66  ? 10.039  -17.826 -16.623 1.00 28.14 ? 66   ILE B CB  1 
ATOM   2526 C CG1 . ILE B 1 66  ? 9.901   -18.892 -17.722 1.00 32.90 ? 66   ILE B CG1 1 
ATOM   2527 C CG2 . ILE B 1 66  ? 9.258   -16.569 -16.957 1.00 27.90 ? 66   ILE B CG2 1 
ATOM   2528 C CD1 . ILE B 1 66  ? 10.690  -18.618 -18.982 1.00 31.57 ? 66   ILE B CD1 1 
ATOM   2529 N N   . VAL B 1 67  ? 12.017  -15.346 -15.153 1.00 24.60 ? 67   VAL B N   1 
ATOM   2530 C CA  . VAL B 1 67  ? 11.901  -14.304 -14.087 1.00 23.96 ? 67   VAL B CA  1 
ATOM   2531 C C   . VAL B 1 67  ? 10.711  -13.401 -14.419 1.00 22.43 ? 67   VAL B C   1 
ATOM   2532 O O   . VAL B 1 67  ? 10.585  -12.955 -15.575 1.00 21.19 ? 67   VAL B O   1 
ATOM   2533 C CB  . VAL B 1 67  ? 13.193  -13.485 -13.959 1.00 23.12 ? 67   VAL B CB  1 
ATOM   2534 C CG1 . VAL B 1 67  ? 13.220  -12.683 -12.674 1.00 21.83 ? 67   VAL B CG1 1 
ATOM   2535 C CG2 . VAL B 1 67  ? 14.411  -14.378 -14.092 1.00 24.48 ? 67   VAL B CG2 1 
ATOM   2536 N N   . ILE B 1 68  ? 9.831   -13.202 -13.451 1.00 22.73 ? 68   ILE B N   1 
ATOM   2537 C CA  . ILE B 1 68  ? 8.686   -12.262 -13.558 1.00 22.68 ? 68   ILE B CA  1 
ATOM   2538 C C   . ILE B 1 68  ? 8.890   -11.153 -12.528 1.00 21.30 ? 68   ILE B C   1 
ATOM   2539 O O   . ILE B 1 68  ? 9.032   -11.439 -11.325 1.00 19.39 ? 68   ILE B O   1 
ATOM   2540 C CB  . ILE B 1 68  ? 7.339   -12.972 -13.362 1.00 24.24 ? 68   ILE B CB  1 
ATOM   2541 C CG1 . ILE B 1 68  ? 7.240   -14.238 -14.221 1.00 25.77 ? 68   ILE B CG1 1 
ATOM   2542 C CG2 . ILE B 1 68  ? 6.214   -11.989 -13.642 1.00 25.31 ? 68   ILE B CG2 1 
ATOM   2543 C CD1 . ILE B 1 68  ? 6.040   -15.103 -13.883 1.00 26.64 ? 68   ILE B CD1 1 
ATOM   2544 N N   . CYS B 1 69  ? 8.871   -9.917  -12.994 1.00 22.88 ? 69   CYS B N   1 
ATOM   2545 C CA  . CYS B 1 69  ? 8.841   -8.736  -12.114 1.00 22.80 ? 69   CYS B CA  1 
ATOM   2546 C C   . CYS B 1 69  ? 7.882   -7.716  -12.717 1.00 23.70 ? 69   CYS B C   1 
ATOM   2547 O O   . CYS B 1 69  ? 8.363   -6.775  -13.402 1.00 21.43 ? 69   CYS B O   1 
ATOM   2548 C CB  . CYS B 1 69  ? 10.239  -8.170  -11.926 1.00 22.99 ? 69   CYS B CB  1 
ATOM   2549 S SG  . CYS B 1 69  ? 10.284  -6.893  -10.651 1.00 23.13 ? 69   CYS B SG  1 
ATOM   2550 N N   . LEU B 1 70  ? 6.585   -7.884  -12.418 1.00 22.48 ? 70   LEU B N   1 
ATOM   2551 C CA  . LEU B 1 70  ? 5.496   -7.012  -12.907 1.00 21.69 ? 70   LEU B CA  1 
ATOM   2552 C C   . LEU B 1 70  ? 4.938   -6.195  -11.742 1.00 23.44 ? 70   LEU B C   1 
ATOM   2553 O O   . LEU B 1 70  ? 5.375   -6.410  -10.576 1.00 22.02 ? 70   LEU B O   1 
ATOM   2554 C CB  . LEU B 1 70  ? 4.413   -7.889  -13.545 1.00 22.08 ? 70   LEU B CB  1 
ATOM   2555 C CG  . LEU B 1 70  ? 4.825   -8.549  -14.850 1.00 22.21 ? 70   LEU B CG  1 
ATOM   2556 C CD1 . LEU B 1 70  ? 3.886   -9.692  -15.215 1.00 23.62 ? 70   LEU B CD1 1 
ATOM   2557 C CD2 . LEU B 1 70  ? 4.902   -7.517  -15.960 1.00 22.66 ? 70   LEU B CD2 1 
ATOM   2558 N N   . LEU B 1 71  ? 4.029   -5.269  -12.046 1.00 23.36 ? 71   LEU B N   1 
ATOM   2559 C CA  . LEU B 1 71  ? 3.454   -4.347  -11.024 1.00 26.02 ? 71   LEU B CA  1 
ATOM   2560 C C   . LEU B 1 71  ? 2.772   -5.163  -9.916  1.00 25.28 ? 71   LEU B C   1 
ATOM   2561 O O   . LEU B 1 71  ? 3.004   -4.864  -8.735  1.00 23.40 ? 71   LEU B O   1 
ATOM   2562 C CB  . LEU B 1 71  ? 2.445   -3.391  -11.670 1.00 28.42 ? 71   LEU B CB  1 
ATOM   2563 C CG  . LEU B 1 71  ? 2.341   -1.967  -11.106 1.00 31.09 ? 71   LEU B CG  1 
ATOM   2564 C CD1 . LEU B 1 71  ? 0.897   -1.510  -11.154 1.00 30.81 ? 71   LEU B CD1 1 
ATOM   2565 C CD2 . LEU B 1 71  ? 2.913   -1.823  -9.692  1.00 30.24 ? 71   LEU B CD2 1 
ATOM   2566 N N   . SER B 1 72  ? 1.963   -6.162  -10.277 1.00 24.09 ? 72   SER B N   1 
ATOM   2567 C CA  . SER B 1 72  ? 0.995   -6.779  -9.338  1.00 25.73 ? 72   SER B CA  1 
ATOM   2568 C C   . SER B 1 72  ? 0.599   -8.174  -9.813  1.00 24.54 ? 72   SER B C   1 
ATOM   2569 O O   . SER B 1 72  ? 0.883   -8.527  -10.960 1.00 23.76 ? 72   SER B O   1 
ATOM   2570 C CB  . SER B 1 72  ? -0.227  -5.916  -9.246  1.00 24.72 ? 72   SER B CB  1 
ATOM   2571 O OG  . SER B 1 72  ? -0.884  -5.972  -10.495 1.00 24.78 ? 72   SER B OG  1 
ATOM   2572 N N   . TYR B 1 73  ? -0.075  -8.909  -8.940  1.00 27.55 ? 73   TYR B N   1 
ATOM   2573 C CA  . TYR B 1 73  ? -0.688  -10.229 -9.222  1.00 27.81 ? 73   TYR B CA  1 
ATOM   2574 C C   . TYR B 1 73  ? -1.612  -10.092 -10.435 1.00 28.41 ? 73   TYR B C   1 
ATOM   2575 O O   . TYR B 1 73  ? -1.509  -10.923 -11.357 1.00 27.21 ? 73   TYR B O   1 
ATOM   2576 C CB  . TYR B 1 73  ? -1.463  -10.730 -7.999  1.00 28.41 ? 73   TYR B CB  1 
ATOM   2577 C CG  . TYR B 1 73  ? -2.423  -11.833 -8.333  1.00 30.48 ? 73   TYR B CG  1 
ATOM   2578 C CD1 . TYR B 1 73  ? -1.972  -13.124 -8.548  1.00 31.17 ? 73   TYR B CD1 1 
ATOM   2579 C CD2 . TYR B 1 73  ? -3.772  -11.570 -8.532  1.00 32.14 ? 73   TYR B CD2 1 
ATOM   2580 C CE1 . TYR B 1 73  ? -2.845  -14.146 -8.881  1.00 32.54 ? 73   TYR B CE1 1 
ATOM   2581 C CE2 . TYR B 1 73  ? -4.657  -12.582 -8.877  1.00 32.42 ? 73   TYR B CE2 1 
ATOM   2582 C CZ  . TYR B 1 73  ? -4.191  -13.871 -9.059  1.00 33.19 ? 73   TYR B CZ  1 
ATOM   2583 O OH  . TYR B 1 73  ? -5.059  -14.875 -9.386  1.00 39.28 ? 73   TYR B OH  1 
ATOM   2584 N N   . ASP B 1 74  ? -2.491  -9.085  -10.399 1.00 29.93 ? 74   ASP B N   1 
ATOM   2585 C CA  . ASP B 1 74  ? -3.500  -8.811  -11.451 1.00 35.25 ? 74   ASP B CA  1 
ATOM   2586 C C   . ASP B 1 74  ? -2.779  -8.768  -12.793 1.00 31.76 ? 74   ASP B C   1 
ATOM   2587 O O   . ASP B 1 74  ? -3.124  -9.552  -13.684 1.00 28.77 ? 74   ASP B O   1 
ATOM   2588 C CB  . ASP B 1 74  ? -4.221  -7.483  -11.203 1.00 41.20 ? 74   ASP B CB  1 
ATOM   2589 C CG  . ASP B 1 74  ? -5.279  -7.142  -12.241 1.00 47.37 ? 74   ASP B CG  1 
ATOM   2590 O OD1 . ASP B 1 74  ? -5.866  -8.078  -12.835 1.00 53.10 ? 74   ASP B OD1 1 
ATOM   2591 O OD2 . ASP B 1 74  ? -5.498  -5.935  -12.464 1.00 60.70 ? 74   ASP B OD2 1 
ATOM   2592 N N   . VAL B 1 75  ? -1.768  -7.909  -12.891 1.00 29.89 ? 75   VAL B N   1 
ATOM   2593 C CA  . VAL B 1 75  ? -0.969  -7.743  -14.136 1.00 28.27 ? 75   VAL B CA  1 
ATOM   2594 C C   . VAL B 1 75  ? -0.287  -9.069  -14.493 1.00 25.55 ? 75   VAL B C   1 
ATOM   2595 O O   . VAL B 1 75  ? -0.244  -9.383  -15.687 1.00 28.10 ? 75   VAL B O   1 
ATOM   2596 C CB  . VAL B 1 75  ? 0.016   -6.576  -13.985 1.00 28.55 ? 75   VAL B CB  1 
ATOM   2597 C CG1 . VAL B 1 75  ? 1.018   -6.527  -15.132 1.00 30.28 ? 75   VAL B CG1 1 
ATOM   2598 C CG2 . VAL B 1 75  ? -0.741  -5.260  -13.867 1.00 28.92 ? 75   VAL B CG2 1 
ATOM   2599 N N   . THR B 1 76  ? 0.187   -9.833  -13.503 1.00 22.98 ? 76   THR B N   1 
ATOM   2600 C CA  . THR B 1 76  ? 0.846   -11.150 -13.707 1.00 24.73 ? 76   THR B CA  1 
ATOM   2601 C C   . THR B 1 76  ? -0.130  -12.142 -14.351 1.00 28.17 ? 76   THR B C   1 
ATOM   2602 O O   . THR B 1 76  ? 0.251   -12.792 -15.368 1.00 24.95 ? 76   THR B O   1 
ATOM   2603 C CB  . THR B 1 76  ? 1.412   -11.724 -12.405 1.00 23.49 ? 76   THR B CB  1 
ATOM   2604 O OG1 . THR B 1 76  ? 2.264   -10.740 -11.811 1.00 23.06 ? 76   THR B OG1 1 
ATOM   2605 C CG2 . THR B 1 76  ? 2.156   -13.017 -12.641 1.00 23.96 ? 76   THR B CG2 1 
ATOM   2606 N N   . GLN B 1 77  ? -1.338  -12.282 -13.798 1.00 32.27 ? 77   GLN B N   1 
ATOM   2607 C CA  . GLN B 1 77  ? -2.286  -13.318 -14.293 1.00 34.74 ? 77   GLN B CA  1 
ATOM   2608 C C   . GLN B 1 77  ? -2.770  -12.874 -15.687 1.00 36.58 ? 77   GLN B C   1 
ATOM   2609 O O   . GLN B 1 77  ? -2.770  -13.714 -16.608 1.00 37.24 ? 77   GLN B O   1 
ATOM   2610 C CB  . GLN B 1 77  ? -3.332  -13.639 -13.220 1.00 37.61 ? 77   GLN B CB  1 
ATOM   2611 C CG  . GLN B 1 77  ? -4.417  -12.598 -13.044 1.00 40.35 ? 77   GLN B CG  1 
ATOM   2612 C CD  . GLN B 1 77  ? -5.556  -12.768 -14.022 1.00 45.66 ? 77   GLN B CD  1 
ATOM   2613 O OE1 . GLN B 1 77  ? -6.212  -11.798 -14.404 1.00 49.50 ? 77   GLN B OE1 1 
ATOM   2614 N NE2 . GLN B 1 77  ? -5.800  -14.005 -14.434 1.00 42.57 ? 77   GLN B NE2 1 
ATOM   2615 N N   . GLN B 1 78  ? -3.075  -11.585 -15.844 1.00 35.79 ? 78   GLN B N   1 
ATOM   2616 C CA  . GLN B 1 78  ? -3.464  -10.908 -17.111 1.00 39.97 ? 78   GLN B CA  1 
ATOM   2617 C C   . GLN B 1 78  ? -2.365  -11.083 -18.181 1.00 40.64 ? 78   GLN B C   1 
ATOM   2618 O O   . GLN B 1 78  ? -2.728  -11.304 -19.359 1.00 40.36 ? 78   GLN B O   1 
ATOM   2619 C CB  . GLN B 1 78  ? -3.780  -9.459  -16.743 1.00 44.70 ? 78   GLN B CB  1 
ATOM   2620 C CG  . GLN B 1 78  ? -4.140  -8.537  -17.893 1.00 50.52 ? 78   GLN B CG  1 
ATOM   2621 C CD  . GLN B 1 78  ? -4.030  -7.113  -17.404 1.00 54.62 ? 78   GLN B CD  1 
ATOM   2622 O OE1 . GLN B 1 78  ? -4.487  -6.780  -16.311 1.00 60.06 ? 78   GLN B OE1 1 
ATOM   2623 N NE2 . GLN B 1 78  ? -3.383  -6.267  -18.191 1.00 59.74 ? 78   GLN B NE2 1 
ATOM   2624 N N   . THR B 1 79  ? -1.079  -11.050 -17.794 1.00 36.09 ? 79   THR B N   1 
ATOM   2625 C CA  . THR B 1 79  ? 0.091   -11.208 -18.704 1.00 32.76 ? 79   THR B CA  1 
ATOM   2626 C C   . THR B 1 79  ? 0.355   -12.684 -18.972 1.00 32.12 ? 79   THR B C   1 
ATOM   2627 O O   . THR B 1 79  ? 0.926   -12.983 -20.028 1.00 36.56 ? 79   THR B O   1 
ATOM   2628 C CB  . THR B 1 79  ? 1.365   -10.582 -18.119 1.00 30.30 ? 79   THR B CB  1 
ATOM   2629 O OG1 . THR B 1 79  ? 1.151   -9.178  -17.997 1.00 28.71 ? 79   THR B OG1 1 
ATOM   2630 C CG2 . THR B 1 79  ? 2.594   -10.843 -18.957 1.00 30.15 ? 79   THR B CG2 1 
ATOM   2631 N N   . LEU B 1 80  ? 0.009   -13.571 -18.042 1.00 34.11 ? 80   LEU B N   1 
ATOM   2632 C CA  . LEU B 1 80  ? 0.134   -15.037 -18.260 1.00 39.84 ? 80   LEU B CA  1 
ATOM   2633 C C   . LEU B 1 80  ? -1.145  -15.597 -18.913 1.00 43.47 ? 80   LEU B C   1 
ATOM   2634 O O   . LEU B 1 80  ? -1.217  -16.832 -19.063 1.00 46.09 ? 80   LEU B O   1 
ATOM   2635 C CB  . LEU B 1 80  ? 0.426   -15.725 -16.924 1.00 39.61 ? 80   LEU B CB  1 
ATOM   2636 C CG  . LEU B 1 80  ? 1.809   -15.459 -16.324 1.00 39.58 ? 80   LEU B CG  1 
ATOM   2637 C CD1 . LEU B 1 80  ? 1.885   -16.029 -14.920 1.00 38.70 ? 80   LEU B CD1 1 
ATOM   2638 C CD2 . LEU B 1 80  ? 2.915   -16.045 -17.190 1.00 39.36 ? 80   LEU B CD2 1 
ATOM   2639 N N   . ASP B 1 81  ? -2.087  -14.734 -19.315 1.00 48.46 ? 81   ASP B N   1 
ATOM   2640 C CA  . ASP B 1 81  ? -3.412  -15.108 -19.889 1.00 53.79 ? 81   ASP B CA  1 
ATOM   2641 C C   . ASP B 1 81  ? -3.247  -16.153 -20.999 1.00 52.68 ? 81   ASP B C   1 
ATOM   2642 O O   . ASP B 1 81  ? -3.995  -17.137 -20.972 1.00 48.54 ? 81   ASP B O   1 
ATOM   2643 C CB  . ASP B 1 81  ? -4.156  -13.902 -20.473 1.00 59.22 ? 81   ASP B CB  1 
ATOM   2644 C CG  . ASP B 1 81  ? -5.650  -13.905 -20.190 1.00 65.75 ? 81   ASP B CG  1 
ATOM   2645 O OD1 . ASP B 1 81  ? -6.187  -14.991 -19.864 1.00 61.94 ? 81   ASP B OD1 1 
ATOM   2646 O OD2 . ASP B 1 81  ? -6.263  -12.810 -20.270 1.00 66.58 ? 81   ASP B OD2 1 
ATOM   2647 N N   . GLU B 1 82  ? -2.327  -15.935 -21.948 1.00 50.79 ? 82   GLU B N   1 
ATOM   2648 C CA  . GLU B 1 82  ? -2.136  -16.821 -23.134 1.00 48.79 ? 82   GLU B CA  1 
ATOM   2649 C C   . GLU B 1 82  ? -0.812  -17.583 -23.051 1.00 41.29 ? 82   GLU B C   1 
ATOM   2650 O O   . GLU B 1 82  ? -0.404  -18.156 -24.091 1.00 38.16 ? 82   GLU B O   1 
ATOM   2651 C CB  . GLU B 1 82  ? -2.231  -16.019 -24.433 1.00 53.55 ? 82   GLU B CB  1 
ATOM   2652 C CG  . GLU B 1 82  ? -3.655  -15.899 -24.948 1.00 58.22 ? 82   GLU B CG  1 
ATOM   2653 C CD  . GLU B 1 82  ? -3.983  -14.565 -25.590 1.00 59.32 ? 82   GLU B CD  1 
ATOM   2654 O OE1 . GLU B 1 82  ? -5.137  -14.127 -25.457 1.00 61.02 ? 82   GLU B OE1 1 
ATOM   2655 O OE2 . GLU B 1 82  ? -3.083  -13.971 -26.216 1.00 64.92 ? 82   GLU B OE2 1 
ATOM   2656 N N   . VAL B 1 83  ? -0.180  -17.623 -21.873 1.00 36.23 ? 83   VAL B N   1 
ATOM   2657 C CA  . VAL B 1 83  ? 0.971   -18.534 -21.607 1.00 36.57 ? 83   VAL B CA  1 
ATOM   2658 C C   . VAL B 1 83  ? 0.413   -19.866 -21.075 1.00 40.32 ? 83   VAL B C   1 
ATOM   2659 O O   . VAL B 1 83  ? 0.218   -19.978 -19.858 1.00 43.13 ? 83   VAL B O   1 
ATOM   2660 C CB  . VAL B 1 83  ? 1.993   -17.913 -20.644 1.00 35.29 ? 83   VAL B CB  1 
ATOM   2661 C CG1 . VAL B 1 83  ? 3.206   -18.819 -20.493 1.00 35.62 ? 83   VAL B CG1 1 
ATOM   2662 C CG2 . VAL B 1 83  ? 2.420   -16.517 -21.085 1.00 35.34 ? 83   VAL B CG2 1 
ATOM   2663 N N   . ILE B 1 84  ? 0.186   -20.846 -21.956 1.00 43.83 ? 84   ILE B N   1 
ATOM   2664 C CA  . ILE B 1 84  ? -0.615  -22.075 -21.649 1.00 45.09 ? 84   ILE B CA  1 
ATOM   2665 C C   . ILE B 1 84  ? 0.305   -23.294 -21.551 1.00 42.75 ? 84   ILE B C   1 
ATOM   2666 O O   . ILE B 1 84  ? -0.216  -24.370 -21.178 1.00 42.41 ? 84   ILE B O   1 
ATOM   2667 C CB  . ILE B 1 84  ? -1.776  -22.303 -22.656 1.00 49.26 ? 84   ILE B CB  1 
ATOM   2668 C CG1 . ILE B 1 84  ? -1.335  -22.948 -23.979 1.00 51.94 ? 84   ILE B CG1 1 
ATOM   2669 C CG2 . ILE B 1 84  ? -2.594  -21.039 -22.879 1.00 46.47 ? 84   ILE B CG2 1 
ATOM   2670 C CD1 . ILE B 1 84  ? -0.215  -22.258 -24.721 1.00 51.85 ? 84   ILE B CD1 1 
ATOM   2671 N N   . ASP B 1 85  ? 1.606   -23.134 -21.833 1.00 42.41 ? 85   ASP B N   1 
ATOM   2672 C CA  . ASP B 1 85  ? 2.590   -24.245 -21.805 1.00 43.27 ? 85   ASP B CA  1 
ATOM   2673 C C   . ASP B 1 85  ? 3.851   -23.874 -21.007 1.00 42.39 ? 85   ASP B C   1 
ATOM   2674 O O   . ASP B 1 85  ? 4.803   -23.316 -21.589 1.00 40.40 ? 85   ASP B O   1 
ATOM   2675 C CB  . ASP B 1 85  ? 2.938   -24.675 -23.230 1.00 47.68 ? 85   ASP B CB  1 
ATOM   2676 C CG  . ASP B 1 85  ? 3.776   -25.937 -23.273 1.00 47.27 ? 85   ASP B CG  1 
ATOM   2677 O OD1 . ASP B 1 85  ? 3.959   -26.557 -22.203 1.00 46.75 ? 85   ASP B OD1 1 
ATOM   2678 O OD2 . ASP B 1 85  ? 4.245   -26.282 -24.371 1.00 51.92 ? 85   ASP B OD2 1 
ATOM   2679 N N   . LEU B 1 86  ? 3.908   -24.261 -19.730 1.00 42.58 ? 86   LEU B N   1 
ATOM   2680 C CA  . LEU B 1 86  ? 5.100   -24.023 -18.872 1.00 45.03 ? 86   LEU B CA  1 
ATOM   2681 C C   . LEU B 1 86  ? 5.879   -25.329 -18.721 1.00 42.84 ? 86   LEU B C   1 
ATOM   2682 O O   . LEU B 1 86  ? 6.735   -25.381 -17.823 1.00 41.27 ? 86   LEU B O   1 
ATOM   2683 C CB  . LEU B 1 86  ? 4.676   -23.466 -17.502 1.00 48.30 ? 86   LEU B CB  1 
ATOM   2684 C CG  . LEU B 1 86  ? 4.375   -21.966 -17.390 1.00 48.04 ? 86   LEU B CG  1 
ATOM   2685 C CD1 . LEU B 1 86  ? 5.345   -21.134 -18.207 1.00 47.29 ? 86   LEU B CD1 1 
ATOM   2686 C CD2 . LEU B 1 86  ? 2.939   -21.643 -17.781 1.00 49.69 ? 86   LEU B CD2 1 
ATOM   2687 N N   . SER B 1 87  ? 5.628   -26.339 -19.569 1.00 45.13 ? 87   SER B N   1 
ATOM   2688 C CA  . SER B 1 87  ? 6.370   -27.631 -19.535 1.00 43.58 ? 87   SER B CA  1 
ATOM   2689 C C   . SER B 1 87  ? 7.858   -27.309 -19.577 1.00 39.22 ? 87   SER B C   1 
ATOM   2690 O O   . SER B 1 87  ? 8.248   -26.554 -20.473 1.00 46.09 ? 87   SER B O   1 
ATOM   2691 C CB  . SER B 1 87  ? 6.005   -28.563 -20.670 1.00 46.56 ? 87   SER B CB  1 
ATOM   2692 O OG  . SER B 1 87  ? 4.610   -28.569 -20.900 1.00 45.68 ? 87   SER B OG  1 
ATOM   2693 N N   . GLY B 1 88  ? 8.632   -27.806 -18.615 1.00 37.74 ? 88   GLY B N   1 
ATOM   2694 C CA  . GLY B 1 88  ? 10.095  -27.604 -18.544 1.00 39.99 ? 88   GLY B CA  1 
ATOM   2695 C C   . GLY B 1 88  ? 10.510  -26.285 -17.892 1.00 41.26 ? 88   GLY B C   1 
ATOM   2696 O O   . GLY B 1 88  ? 11.716  -26.126 -17.635 1.00 43.79 ? 88   GLY B O   1 
ATOM   2697 N N   . LYS B 1 89  ? 9.573   -25.372 -17.607 1.00 42.62 ? 89   LYS B N   1 
ATOM   2698 C CA  . LYS B 1 89  ? 9.894   -23.995 -17.128 1.00 45.06 ? 89   LYS B CA  1 
ATOM   2699 C C   . LYS B 1 89  ? 9.985   -23.946 -15.593 1.00 42.41 ? 89   LYS B C   1 
ATOM   2700 O O   . LYS B 1 89  ? 9.021   -24.380 -14.923 1.00 40.04 ? 89   LYS B O   1 
ATOM   2701 C CB  . LYS B 1 89  ? 8.830   -23.004 -17.616 1.00 47.12 ? 89   LYS B CB  1 
ATOM   2702 C CG  . LYS B 1 89  ? 8.510   -23.054 -19.105 1.00 47.69 ? 89   LYS B CG  1 
ATOM   2703 C CD  . LYS B 1 89  ? 9.723   -23.044 -19.988 1.00 47.36 ? 89   LYS B CD  1 
ATOM   2704 C CE  . LYS B 1 89  ? 9.364   -23.079 -21.454 1.00 47.29 ? 89   LYS B CE  1 
ATOM   2705 N NZ  . LYS B 1 89  ? 10.581  -22.860 -22.264 1.00 47.69 ? 89   LYS B NZ  1 
ATOM   2706 N N   . THR B 1 90  ? 11.081  -23.388 -15.066 1.00 42.96 ? 90   THR B N   1 
ATOM   2707 C CA  . THR B 1 90  ? 11.240  -22.971 -13.644 1.00 43.31 ? 90   THR B CA  1 
ATOM   2708 C C   . THR B 1 90  ? 10.904  -21.476 -13.507 1.00 41.37 ? 90   THR B C   1 
ATOM   2709 O O   . THR B 1 90  ? 11.635  -20.638 -14.099 1.00 38.75 ? 90   THR B O   1 
ATOM   2710 C CB  . THR B 1 90  ? 12.648  -23.296 -13.124 1.00 46.27 ? 90   THR B CB  1 
ATOM   2711 O OG1 . THR B 1 90  ? 12.698  -24.703 -12.898 1.00 46.65 ? 90   THR B OG1 1 
ATOM   2712 C CG2 . THR B 1 90  ? 12.997  -22.583 -11.834 1.00 50.55 ? 90   THR B CG2 1 
ATOM   2713 N N   . ILE B 1 91  ? 9.857   -21.159 -12.737 1.00 34.89 ? 91   ILE B N   1 
ATOM   2714 C CA  . ILE B 1 91  ? 9.300   -19.785 -12.567 1.00 31.96 ? 91   ILE B CA  1 
ATOM   2715 C C   . ILE B 1 91  ? 9.855   -19.149 -11.288 1.00 31.38 ? 91   ILE B C   1 
ATOM   2716 O O   . ILE B 1 91  ? 9.639   -19.705 -10.199 1.00 32.33 ? 91   ILE B O   1 
ATOM   2717 C CB  . ILE B 1 91  ? 7.768   -19.818 -12.535 1.00 33.10 ? 91   ILE B CB  1 
ATOM   2718 C CG1 . ILE B 1 91  ? 7.188   -20.615 -13.706 1.00 34.32 ? 91   ILE B CG1 1 
ATOM   2719 C CG2 . ILE B 1 91  ? 7.218   -18.399 -12.474 1.00 33.03 ? 91   ILE B CG2 1 
ATOM   2720 C CD1 . ILE B 1 91  ? 7.725   -20.207 -15.064 1.00 34.53 ? 91   ILE B CD1 1 
ATOM   2721 N N   . ILE B 1 92  ? 10.550  -18.024 -11.433 1.00 28.39 ? 92   ILE B N   1 
ATOM   2722 C CA  . ILE B 1 92  ? 10.974  -17.131 -10.318 1.00 27.89 ? 92   ILE B CA  1 
ATOM   2723 C C   . ILE B 1 92  ? 10.092  -15.878 -10.407 1.00 26.93 ? 92   ILE B C   1 
ATOM   2724 O O   . ILE B 1 92  ? 10.244  -15.095 -11.368 1.00 27.09 ? 92   ILE B O   1 
ATOM   2725 C CB  . ILE B 1 92  ? 12.487  -16.836 -10.391 1.00 25.86 ? 92   ILE B CB  1 
ATOM   2726 C CG1 . ILE B 1 92  ? 13.305  -18.128 -10.531 1.00 25.45 ? 92   ILE B CG1 1 
ATOM   2727 C CG2 . ILE B 1 92  ? 12.968  -16.022 -9.190  1.00 25.87 ? 92   ILE B CG2 1 
ATOM   2728 C CD1 . ILE B 1 92  ? 14.711  -17.905 -10.949 1.00 24.54 ? 92   ILE B CD1 1 
ATOM   2729 N N   . ASN B 1 93  ? 9.154   -15.728 -9.475  1.00 24.73 ? 93   ASN B N   1 
ATOM   2730 C CA  . ASN B 1 93  ? 8.232   -14.572 -9.441  1.00 22.57 ? 93   ASN B CA  1 
ATOM   2731 C C   . ASN B 1 93  ? 8.713   -13.562 -8.386  1.00 21.04 ? 93   ASN B C   1 
ATOM   2732 O O   . ASN B 1 93  ? 8.608   -13.840 -7.161  1.00 20.49 ? 93   ASN B O   1 
ATOM   2733 C CB  . ASN B 1 93  ? 6.795   -15.016 -9.195  1.00 21.91 ? 93   ASN B CB  1 
ATOM   2734 C CG  . ASN B 1 93  ? 5.811   -13.912 -9.507  1.00 21.92 ? 93   ASN B CG  1 
ATOM   2735 O OD1 . ASN B 1 93  ? 6.208   -12.864 -10.000 1.00 21.70 ? 93   ASN B OD1 1 
ATOM   2736 N ND2 . ASN B 1 93  ? 4.534   -14.136 -9.256  1.00 23.46 ? 93   ASN B ND2 1 
ATOM   2737 N N   . LEU B 1 94  ? 9.193   -12.412 -8.845  1.00 21.30 ? 94   LEU B N   1 
ATOM   2738 C CA  . LEU B 1 94  ? 9.682   -11.304 -7.979  1.00 20.79 ? 94   LEU B CA  1 
ATOM   2739 C C   . LEU B 1 94  ? 8.650   -10.173 -7.969  1.00 20.04 ? 94   LEU B C   1 
ATOM   2740 O O   . LEU B 1 94  ? 9.001   -9.057  -7.609  1.00 19.30 ? 94   LEU B O   1 
ATOM   2741 C CB  . LEU B 1 94  ? 11.063  -10.864 -8.469  1.00 21.44 ? 94   LEU B CB  1 
ATOM   2742 C CG  . LEU B 1 94  ? 12.055  -12.016 -8.645  1.00 22.53 ? 94   LEU B CG  1 
ATOM   2743 C CD1 . LEU B 1 94  ? 13.405  -11.539 -9.185  1.00 23.76 ? 94   LEU B CD1 1 
ATOM   2744 C CD2 . LEU B 1 94  ? 12.241  -12.737 -7.322  1.00 22.44 ? 94   LEU B CD2 1 
ATOM   2745 N N   . THR B 1 95  ? 7.387   -10.501 -8.219  1.00 19.38 ? 95   THR B N   1 
ATOM   2746 C CA  . THR B 1 95  ? 6.263   -9.530  -8.215  1.00 20.46 ? 95   THR B CA  1 
ATOM   2747 C C   . THR B 1 95  ? 5.690   -9.433  -6.800  1.00 19.14 ? 95   THR B C   1 
ATOM   2748 O O   . THR B 1 95  ? 5.295   -10.456 -6.266  1.00 23.07 ? 95   THR B O   1 
ATOM   2749 C CB  . THR B 1 95  ? 5.204   -9.930  -9.247  1.00 19.71 ? 95   THR B CB  1 
ATOM   2750 O OG1 . THR B 1 95  ? 5.839   -10.004 -10.530 1.00 19.36 ? 95   THR B OG1 1 
ATOM   2751 C CG2 . THR B 1 95  ? 4.054   -8.953  -9.278  1.00 19.90 ? 95   THR B CG2 1 
ATOM   2752 N N   . ASN B 1 96  ? 5.707   -8.252  -6.201  1.00 20.13 ? 96   ASN B N   1 
ATOM   2753 C CA  . ASN B 1 96  ? 5.116   -7.989  -4.864  1.00 20.64 ? 96   ASN B CA  1 
ATOM   2754 C C   . ASN B 1 96  ? 3.633   -8.351  -4.894  1.00 21.64 ? 96   ASN B C   1 
ATOM   2755 O O   . ASN B 1 96  ? 2.959   -8.010  -5.873  1.00 21.43 ? 96   ASN B O   1 
ATOM   2756 C CB  . ASN B 1 96  ? 5.247   -6.529  -4.432  1.00 21.19 ? 96   ASN B CB  1 
ATOM   2757 C CG  . ASN B 1 96  ? 4.308   -6.174  -3.292  1.00 21.48 ? 96   ASN B CG  1 
ATOM   2758 O OD1 . ASN B 1 96  ? 4.639   -6.396  -2.125  1.00 21.05 ? 96   ASN B OD1 1 
ATOM   2759 N ND2 . ASN B 1 96  ? 3.155   -5.604  -3.620  1.00 17.22 ? 96   ASN B ND2 1 
ATOM   2760 N N   . GLY B 1 97  ? 3.161   -9.035  -3.855  1.00 20.98 ? 97   GLY B N   1 
ATOM   2761 C CA  . GLY B 1 97  ? 1.735   -9.368  -3.717  1.00 21.20 ? 97   GLY B CA  1 
ATOM   2762 C C   . GLY B 1 97  ? 1.459   -9.984  -2.369  1.00 21.14 ? 97   GLY B C   1 
ATOM   2763 O O   . GLY B 1 97  ? 2.368   -10.003 -1.497  1.00 21.63 ? 97   GLY B O   1 
ATOM   2764 N N   . THR B 1 98  ? 0.241   -10.455 -2.188  1.00 20.99 ? 98   THR B N   1 
ATOM   2765 C CA  . THR B 1 98  ? -0.265  -11.009 -0.907  1.00 20.30 ? 98   THR B CA  1 
ATOM   2766 C C   . THR B 1 98  ? 0.191   -12.448 -0.816  1.00 21.05 ? 98   THR B C   1 
ATOM   2767 O O   . THR B 1 98  ? 0.541   -13.021 -1.836  1.00 22.23 ? 98   THR B O   1 
ATOM   2768 C CB  . THR B 1 98  ? -1.793  -10.946 -0.845  1.00 20.73 ? 98   THR B CB  1 
ATOM   2769 O OG1 . THR B 1 98  ? -2.299  -11.794 -1.868  1.00 21.51 ? 98   THR B OG1 1 
ATOM   2770 C CG2 . THR B 1 98  ? -2.344  -9.558  -1.035  1.00 19.95 ? 98   THR B CG2 1 
ATOM   2771 N N   . PRO B 1 99  ? 0.209   -13.066 0.387   1.00 22.26 ? 99   PRO B N   1 
ATOM   2772 C CA  . PRO B 1 99  ? 0.475   -14.499 0.517   1.00 23.13 ? 99   PRO B CA  1 
ATOM   2773 C C   . PRO B 1 99  ? -0.383  -15.376 -0.391  1.00 24.42 ? 99   PRO B C   1 
ATOM   2774 O O   . PRO B 1 99  ? 0.150   -16.295 -0.968  1.00 25.92 ? 99   PRO B O   1 
ATOM   2775 C CB  . PRO B 1 99  ? 0.157   -14.783 1.997   1.00 22.58 ? 99   PRO B CB  1 
ATOM   2776 C CG  . PRO B 1 99  ? 0.505   -13.472 2.689   1.00 21.79 ? 99   PRO B CG  1 
ATOM   2777 C CD  . PRO B 1 99  ? 0.068   -12.409 1.696   1.00 21.30 ? 99   PRO B CD  1 
ATOM   2778 N N   . GLN B 1 100 ? -1.679  -15.070 -0.487  1.00 26.91 ? 100  GLN B N   1 
ATOM   2779 C CA  . GLN B 1 100 ? -2.660  -15.880 -1.261  1.00 28.82 ? 100  GLN B CA  1 
ATOM   2780 C C   . GLN B 1 100 ? -2.372  -15.709 -2.752  1.00 25.83 ? 100  GLN B C   1 
ATOM   2781 O O   . GLN B 1 100 ? -2.457  -16.686 -3.486  1.00 25.77 ? 100  GLN B O   1 
ATOM   2782 C CB  . GLN B 1 100 ? -4.107  -15.505 -0.878  1.00 30.85 ? 100  GLN B CB  1 
ATOM   2783 C CG  . GLN B 1 100 ? -4.650  -16.227 0.353   1.00 35.62 ? 100  GLN B CG  1 
ATOM   2784 C CD  . GLN B 1 100 ? -3.626  -17.015 1.147   1.00 42.80 ? 100  GLN B CD  1 
ATOM   2785 O OE1 . GLN B 1 100 ? -3.202  -16.590 2.223   1.00 55.65 ? 100  GLN B OE1 1 
ATOM   2786 N NE2 . GLN B 1 100 ? -3.226  -18.183 0.646   1.00 41.31 ? 100  GLN B NE2 1 
ATOM   2787 N N   . GLN B 1 101 ? -2.032  -14.509 -3.199  1.00 26.06 ? 101  GLN B N   1 
ATOM   2788 C CA  . GLN B 1 101 ? -1.635  -14.300 -4.621  1.00 24.46 ? 101  GLN B CA  1 
ATOM   2789 C C   . GLN B 1 101 ? -0.451  -15.198 -4.973  1.00 23.95 ? 101  GLN B C   1 
ATOM   2790 O O   . GLN B 1 101 ? -0.421  -15.680 -6.086  1.00 26.22 ? 101  GLN B O   1 
ATOM   2791 C CB  . GLN B 1 101 ? -1.309  -12.838 -4.875  1.00 26.18 ? 101  GLN B CB  1 
ATOM   2792 C CG  . GLN B 1 101 ? -2.550  -11.978 -4.791  1.00 27.28 ? 101  GLN B CG  1 
ATOM   2793 C CD  . GLN B 1 101 ? -2.303  -10.496 -4.872  1.00 27.02 ? 101  GLN B CD  1 
ATOM   2794 O OE1 . GLN B 1 101 ? -1.219  -9.999  -4.602  1.00 27.25 ? 101  GLN B OE1 1 
ATOM   2795 N NE2 . GLN B 1 101 ? -3.352  -9.769  -5.217  1.00 26.83 ? 101  GLN B NE2 1 
ATOM   2796 N N   . ALA B 1 102 ? 0.507   -15.409 -4.071  1.00 24.46 ? 102  ALA B N   1 
ATOM   2797 C CA  . ALA B 1 102 ? 1.711   -16.211 -4.387  1.00 25.38 ? 102  ALA B CA  1 
ATOM   2798 C C   . ALA B 1 102 ? 1.286   -17.670 -4.619  1.00 26.38 ? 102  ALA B C   1 
ATOM   2799 O O   . ALA B 1 102 ? 1.814   -18.334 -5.550  1.00 29.17 ? 102  ALA B O   1 
ATOM   2800 C CB  . ALA B 1 102 ? 2.722   -16.082 -3.292  1.00 23.41 ? 102  ALA B CB  1 
ATOM   2801 N N   . VAL B 1 103 ? 0.362   -18.145 -3.797  1.00 27.10 ? 103  VAL B N   1 
ATOM   2802 C CA  . VAL B 1 103 ? -0.234  -19.506 -3.895  1.00 29.59 ? 103  VAL B CA  1 
ATOM   2803 C C   . VAL B 1 103 ? -1.005  -19.599 -5.218  1.00 30.44 ? 103  VAL B C   1 
ATOM   2804 O O   . VAL B 1 103 ? -0.850  -20.616 -5.922  1.00 30.94 ? 103  VAL B O   1 
ATOM   2805 C CB  . VAL B 1 103 ? -1.149  -19.788 -2.693  1.00 31.27 ? 103  VAL B CB  1 
ATOM   2806 C CG1 . VAL B 1 103 ? -1.806  -21.171 -2.796  1.00 34.28 ? 103  VAL B CG1 1 
ATOM   2807 C CG2 . VAL B 1 103 ? -0.395  -19.633 -1.384  1.00 29.74 ? 103  VAL B CG2 1 
ATOM   2808 N N   . LYS B 1 104 ? -1.780  -18.567 -5.559  1.00 30.09 ? 104  LYS B N   1 
ATOM   2809 C CA  . LYS B 1 104 ? -2.570  -18.561 -6.814  1.00 33.00 ? 104  LYS B CA  1 
ATOM   2810 C C   . LYS B 1 104 ? -1.615  -18.713 -7.999  1.00 31.81 ? 104  LYS B C   1 
ATOM   2811 O O   . LYS B 1 104 ? -1.877  -19.592 -8.830  1.00 32.84 ? 104  LYS B O   1 
ATOM   2812 C CB  . LYS B 1 104 ? -3.490  -17.342 -6.888  1.00 32.77 ? 104  LYS B CB  1 
ATOM   2813 C CG  . LYS B 1 104 ? -4.779  -17.523 -6.101  1.00 37.19 ? 104  LYS B CG  1 
ATOM   2814 C CD  . LYS B 1 104 ? -5.780  -16.393 -6.252  1.00 42.34 ? 104  LYS B CD  1 
ATOM   2815 C CE  . LYS B 1 104 ? -5.334  -15.089 -5.620  1.00 44.34 ? 104  LYS B CE  1 
ATOM   2816 N NZ  . LYS B 1 104 ? -6.421  -14.074 -5.629  1.00 48.69 ? 104  LYS B NZ  1 
ATOM   2817 N N   . VAL B 1 105 ? -0.509  -17.961 -8.057  1.00 30.06 ? 105  VAL B N   1 
ATOM   2818 C CA  . VAL B 1 105 ? 0.369   -17.993 -9.267  1.00 27.03 ? 105  VAL B CA  1 
ATOM   2819 C C   . VAL B 1 105 ? 1.033   -19.373 -9.320  1.00 26.68 ? 105  VAL B C   1 
ATOM   2820 O O   . VAL B 1 105 ? 1.159   -19.917 -10.429 1.00 24.36 ? 105  VAL B O   1 
ATOM   2821 C CB  . VAL B 1 105 ? 1.409   -16.858 -9.317  1.00 26.66 ? 105  VAL B CB  1 
ATOM   2822 C CG1 . VAL B 1 105 ? 2.308   -16.993 -10.543 1.00 24.29 ? 105  VAL B CG1 1 
ATOM   2823 C CG2 . VAL B 1 105 ? 0.762   -15.480 -9.289  1.00 25.74 ? 105  VAL B CG2 1 
ATOM   2824 N N   . ALA B 1 106 ? 1.451   -19.908 -8.170  1.00 26.36 ? 106  ALA B N   1 
ATOM   2825 C CA  . ALA B 1 106 ? 2.084   -21.240 -8.070  1.00 26.74 ? 106  ALA B CA  1 
ATOM   2826 C C   . ALA B 1 106 ? 1.139   -22.304 -8.669  1.00 27.27 ? 106  ALA B C   1 
ATOM   2827 O O   . ALA B 1 106 ? 1.602   -23.105 -9.481  1.00 24.79 ? 106  ALA B O   1 
ATOM   2828 C CB  . ALA B 1 106 ? 2.438   -21.530 -6.641  1.00 25.12 ? 106  ALA B CB  1 
ATOM   2829 N N   . THR B 1 107 ? -0.139  -22.265 -8.291  1.00 30.66 ? 107  THR B N   1 
ATOM   2830 C CA  . THR B 1 107 ? -1.234  -23.149 -8.783  1.00 32.25 ? 107  THR B CA  1 
ATOM   2831 C C   . THR B 1 107 ? -1.415  -22.951 -10.289 1.00 33.57 ? 107  THR B C   1 
ATOM   2832 O O   . THR B 1 107 ? -1.387  -23.975 -11.030 1.00 29.47 ? 107  THR B O   1 
ATOM   2833 C CB  . THR B 1 107 ? -2.531  -22.858 -8.020  1.00 32.52 ? 107  THR B CB  1 
ATOM   2834 O OG1 . THR B 1 107 ? -2.247  -23.202 -6.669  1.00 31.67 ? 107  THR B OG1 1 
ATOM   2835 C CG2 . THR B 1 107 ? -3.740  -23.635 -8.498  1.00 34.47 ? 107  THR B CG2 1 
ATOM   2836 N N   . LEU B 1 108 ? -1.553  -21.685 -10.711 1.00 35.70 ? 108  LEU B N   1 
ATOM   2837 C CA  . LEU B 1 108 ? -1.794  -21.271 -12.122 1.00 38.00 ? 108  LEU B CA  1 
ATOM   2838 C C   . LEU B 1 108 ? -0.700  -21.873 -13.004 1.00 36.62 ? 108  LEU B C   1 
ATOM   2839 O O   . LEU B 1 108 ? -1.014  -22.399 -14.065 1.00 40.27 ? 108  LEU B O   1 
ATOM   2840 C CB  . LEU B 1 108 ? -1.816  -19.739 -12.208 1.00 42.27 ? 108  LEU B CB  1 
ATOM   2841 C CG  . LEU B 1 108 ? -2.340  -19.137 -13.508 1.00 44.20 ? 108  LEU B CG  1 
ATOM   2842 C CD1 . LEU B 1 108 ? -3.719  -19.686 -13.851 1.00 46.89 ? 108  LEU B CD1 1 
ATOM   2843 C CD2 . LEU B 1 108 ? -2.398  -17.624 -13.407 1.00 46.78 ? 108  LEU B CD2 1 
ATOM   2844 N N   . VAL B 1 109 ? 0.534   -21.846 -12.521 1.00 34.12 ? 109  VAL B N   1 
ATOM   2845 C CA  . VAL B 1 109 ? 1.764   -22.174 -13.290 1.00 33.15 ? 109  VAL B CA  1 
ATOM   2846 C C   . VAL B 1 109 ? 1.989   -23.698 -13.213 1.00 35.17 ? 109  VAL B C   1 
ATOM   2847 O O   . VAL B 1 109 ? 2.418   -24.303 -14.216 1.00 32.99 ? 109  VAL B O   1 
ATOM   2848 C CB  . VAL B 1 109 ? 2.906   -21.286 -12.751 1.00 31.73 ? 109  VAL B CB  1 
ATOM   2849 C CG1 . VAL B 1 109 ? 4.127   -22.037 -12.273 1.00 33.43 ? 109  VAL B CG1 1 
ATOM   2850 C CG2 . VAL B 1 109 ? 3.277   -20.185 -13.737 1.00 32.51 ? 109  VAL B CG2 1 
ATOM   2851 N N   . GLN B 1 110 ? 1.671   -24.320 -12.075 1.00 32.91 ? 110  GLN B N   1 
ATOM   2852 C CA  . GLN B 1 110 ? 1.620   -25.803 -11.952 1.00 31.66 ? 110  GLN B CA  1 
ATOM   2853 C C   . GLN B 1 110 ? 0.651   -26.379 -13.007 1.00 30.70 ? 110  GLN B C   1 
ATOM   2854 O O   . GLN B 1 110 ? 1.098   -27.266 -13.775 1.00 31.50 ? 110  GLN B O   1 
ATOM   2855 C CB  . GLN B 1 110 ? 1.220   -26.200 -10.532 1.00 29.32 ? 110  GLN B CB  1 
ATOM   2856 C CG  . GLN B 1 110 ? 1.276   -27.695 -10.318 1.00 29.97 ? 110  GLN B CG  1 
ATOM   2857 C CD  . GLN B 1 110 ? 0.873   -28.071 -8.918  1.00 29.55 ? 110  GLN B CD  1 
ATOM   2858 O OE1 . GLN B 1 110 ? 1.641   -28.691 -8.203  1.00 30.98 ? 110  GLN B OE1 1 
ATOM   2859 N NE2 . GLN B 1 110 ? -0.334  -27.702 -8.520  1.00 28.54 ? 110  GLN B NE2 1 
ATOM   2860 N N   . GLN B 1 111 ? -0.601  -25.886 -13.037 1.00 29.33 ? 111  GLN B N   1 
ATOM   2861 C CA  . GLN B 1 111 ? -1.721  -26.284 -13.943 1.00 32.18 ? 111  GLN B CA  1 
ATOM   2862 C C   . GLN B 1 111 ? -1.248  -26.342 -15.401 1.00 37.63 ? 111  GLN B C   1 
ATOM   2863 O O   . GLN B 1 111 ? -1.880  -27.061 -16.210 1.00 36.96 ? 111  GLN B O   1 
ATOM   2864 C CB  . GLN B 1 111 ? -2.903  -25.305 -13.866 1.00 33.33 ? 111  GLN B CB  1 
ATOM   2865 C CG  . GLN B 1 111 ? -3.846  -25.529 -12.685 1.00 36.37 ? 111  GLN B CG  1 
ATOM   2866 C CD  . GLN B 1 111 ? -4.721  -24.352 -12.278 1.00 43.13 ? 111  GLN B CD  1 
ATOM   2867 O OE1 . GLN B 1 111 ? -4.500  -23.186 -12.634 1.00 40.40 ? 111  GLN B OE1 1 
ATOM   2868 N NE2 . GLN B 1 111 ? -5.729  -24.645 -11.468 1.00 41.47 ? 111  GLN B NE2 1 
ATOM   2869 N N   . ARG B 1 112 ? -0.212  -25.572 -15.737 1.00 38.78 ? 112  ARG B N   1 
ATOM   2870 C CA  . ARG B 1 112 ? 0.223   -25.334 -17.129 1.00 37.29 ? 112  ARG B CA  1 
ATOM   2871 C C   . ARG B 1 112 ? 1.529   -26.079 -17.369 1.00 37.78 ? 112  ARG B C   1 
ATOM   2872 O O   . ARG B 1 112 ? 1.980   -26.045 -18.512 1.00 36.82 ? 112  ARG B O   1 
ATOM   2873 C CB  . ARG B 1 112 ? 0.309   -23.828 -17.380 1.00 40.62 ? 112  ARG B CB  1 
ATOM   2874 C CG  . ARG B 1 112 ? -1.054  -23.156 -17.311 1.00 40.29 ? 112  ARG B CG  1 
ATOM   2875 C CD  . ARG B 1 112 ? -1.000  -21.667 -17.528 1.00 41.33 ? 112  ARG B CD  1 
ATOM   2876 N NE  . ARG B 1 112 ? -2.290  -21.059 -17.275 1.00 41.25 ? 112  ARG B NE  1 
ATOM   2877 C CZ  . ARG B 1 112 ? -2.565  -19.772 -17.454 1.00 46.30 ? 112  ARG B CZ  1 
ATOM   2878 N NH1 . ARG B 1 112 ? -1.624  -18.948 -17.883 1.00 53.06 ? 112  ARG B NH1 1 
ATOM   2879 N NH2 . ARG B 1 112 ? -3.771  -19.300 -17.183 1.00 46.61 ? 112  ARG B NH2 1 
ATOM   2880 N N   . GLY B 1 113 ? 2.077   -26.751 -16.344 1.00 35.61 ? 113  GLY B N   1 
ATOM   2881 C CA  . GLY B 1 113 ? 3.133   -27.768 -16.500 1.00 32.67 ? 113  GLY B CA  1 
ATOM   2882 C C   . GLY B 1 113 ? 4.480   -27.337 -15.950 1.00 36.58 ? 113  GLY B C   1 
ATOM   2883 O O   . GLY B 1 113 ? 5.472   -28.070 -16.182 1.00 33.19 ? 113  GLY B O   1 
ATOM   2884 N N   . ALA B 1 114 ? 4.552   -26.205 -15.235 1.00 39.25 ? 114  ALA B N   1 
ATOM   2885 C CA  . ALA B 1 114 ? 5.833   -25.626 -14.757 1.00 40.02 ? 114  ALA B CA  1 
ATOM   2886 C C   . ALA B 1 114 ? 6.577   -26.689 -13.950 1.00 39.89 ? 114  ALA B C   1 
ATOM   2887 O O   . ALA B 1 114 ? 5.881   -27.432 -13.237 1.00 37.82 ? 114  ALA B O   1 
ATOM   2888 C CB  . ALA B 1 114 ? 5.559   -24.391 -13.941 1.00 41.92 ? 114  ALA B CB  1 
ATOM   2889 N N   . GLU B 1 115 ? 7.902   -26.812 -14.101 1.00 40.54 ? 115  GLU B N   1 
ATOM   2890 C CA  . GLU B 1 115 ? 8.706   -27.710 -13.234 1.00 43.63 ? 115  GLU B CA  1 
ATOM   2891 C C   . GLU B 1 115 ? 8.452   -27.256 -11.797 1.00 44.26 ? 115  GLU B C   1 
ATOM   2892 O O   . GLU B 1 115 ? 7.848   -28.029 -11.049 1.00 47.32 ? 115  GLU B O   1 
ATOM   2893 C CB  . GLU B 1 115 ? 10.208  -27.715 -13.539 1.00 47.71 ? 115  GLU B CB  1 
ATOM   2894 C CG  . GLU B 1 115 ? 11.032  -28.339 -12.404 1.00 55.97 ? 115  GLU B CG  1 
ATOM   2895 C CD  . GLU B 1 115 ? 12.333  -29.067 -12.743 1.00 63.03 ? 115  GLU B CD  1 
ATOM   2896 O OE1 . GLU B 1 115 ? 12.342  -29.857 -13.710 1.00 66.82 ? 115  GLU B OE1 1 
ATOM   2897 O OE2 . GLU B 1 115 ? 13.336  -28.877 -12.008 1.00 65.28 ? 115  GLU B OE2 1 
ATOM   2898 N N   . SER B 1 116 ? 8.839   -26.019 -11.465 1.00 41.27 ? 116  SER B N   1 
ATOM   2899 C CA  . SER B 1 116 ? 8.791   -25.472 -10.087 1.00 38.36 ? 116  SER B CA  1 
ATOM   2900 C C   . SER B 1 116 ? 8.532   -23.960 -10.088 1.00 36.20 ? 116  SER B C   1 
ATOM   2901 O O   . SER B 1 116 ? 8.506   -23.320 -11.154 1.00 32.30 ? 116  SER B O   1 
ATOM   2902 C CB  . SER B 1 116 ? 10.042  -25.843 -9.305  1.00 39.33 ? 116  SER B CB  1 
ATOM   2903 O OG  . SER B 1 116 ? 11.204  -25.198 -9.798  1.00 39.65 ? 116  SER B OG  1 
ATOM   2904 N N   . TYR B 1 117 ? 8.294   -23.426 -8.896  1.00 32.41 ? 117  TYR B N   1 
ATOM   2905 C CA  . TYR B 1 117 ? 7.895   -22.023 -8.672  1.00 32.06 ? 117  TYR B CA  1 
ATOM   2906 C C   . TYR B 1 117 ? 8.503   -21.575 -7.358  1.00 30.07 ? 117  TYR B C   1 
ATOM   2907 O O   . TYR B 1 117 ? 8.281   -22.248 -6.342  1.00 30.54 ? 117  TYR B O   1 
ATOM   2908 C CB  . TYR B 1 117 ? 6.377   -21.853 -8.621  1.00 30.07 ? 117  TYR B CB  1 
ATOM   2909 C CG  . TYR B 1 117 ? 5.930   -20.439 -8.346  1.00 28.06 ? 117  TYR B CG  1 
ATOM   2910 C CD1 . TYR B 1 117 ? 5.759   -19.990 -7.053  1.00 26.63 ? 117  TYR B CD1 1 
ATOM   2911 C CD2 . TYR B 1 117 ? 5.637   -19.559 -9.372  1.00 27.87 ? 117  TYR B CD2 1 
ATOM   2912 C CE1 . TYR B 1 117 ? 5.341   -18.700 -6.775  1.00 25.98 ? 117  TYR B CE1 1 
ATOM   2913 C CE2 . TYR B 1 117 ? 5.210   -18.263 -9.113  1.00 27.74 ? 117  TYR B CE2 1 
ATOM   2914 C CZ  . TYR B 1 117 ? 5.068   -17.830 -7.810  1.00 24.06 ? 117  TYR B CZ  1 
ATOM   2915 O OH  . TYR B 1 117 ? 4.632   -16.570 -7.545  1.00 23.72 ? 117  TYR B OH  1 
ATOM   2916 N N   . ILE B 1 118 ? 9.270   -20.497 -7.403  1.00 26.73 ? 118  ILE B N   1 
ATOM   2917 C CA  . ILE B 1 118 ? 9.721   -19.826 -6.159  1.00 26.05 ? 118  ILE B CA  1 
ATOM   2918 C C   . ILE B 1 118 ? 9.291   -18.372 -6.238  1.00 24.37 ? 118  ILE B C   1 
ATOM   2919 O O   . ILE B 1 118 ? 9.132   -17.839 -7.350  1.00 24.36 ? 118  ILE B O   1 
ATOM   2920 C CB  . ILE B 1 118 ? 11.223  -20.020 -5.933  1.00 26.60 ? 118  ILE B CB  1 
ATOM   2921 C CG1 . ILE B 1 118 ? 12.063  -19.489 -7.091  1.00 26.21 ? 118  ILE B CG1 1 
ATOM   2922 C CG2 . ILE B 1 118 ? 11.498  -21.484 -5.648  1.00 28.75 ? 118  ILE B CG2 1 
ATOM   2923 C CD1 . ILE B 1 118 ? 13.507  -19.386 -6.764  1.00 26.57 ? 118  ILE B CD1 1 
ATOM   2924 N N   . HIS B 1 119 ? 9.032   -17.801 -5.076  1.00 23.11 ? 119  HIS B N   1 
ATOM   2925 C CA  . HIS B 1 119 ? 8.644   -16.385 -4.921  1.00 20.77 ? 119  HIS B CA  1 
ATOM   2926 C C   . HIS B 1 119 ? 9.781   -15.685 -4.195  1.00 21.11 ? 119  HIS B C   1 
ATOM   2927 O O   . HIS B 1 119 ? 10.338  -16.258 -3.206  1.00 21.99 ? 119  HIS B O   1 
ATOM   2928 C CB  . HIS B 1 119 ? 7.313   -16.256 -4.175  1.00 20.48 ? 119  HIS B CB  1 
ATOM   2929 C CG  . HIS B 1 119 ? 6.606   -15.009 -4.561  1.00 19.53 ? 119  HIS B CG  1 
ATOM   2930 N ND1 . HIS B 1 119 ? 5.629   -15.004 -5.522  1.00 18.84 ? 119  HIS B ND1 1 
ATOM   2931 C CD2 . HIS B 1 119 ? 6.825   -13.721 -4.228  1.00 18.52 ? 119  HIS B CD2 1 
ATOM   2932 C CE1 . HIS B 1 119 ? 5.221   -13.766 -5.726  1.00 18.16 ? 119  HIS B CE1 1 
ATOM   2933 N NE2 . HIS B 1 119 ? 5.919   -12.960 -4.934  1.00 18.09 ? 119  HIS B NE2 1 
ATOM   2934 N N   . GLY B 1 120 ? 10.138  -14.526 -4.709  1.00 19.63 ? 120  GLY B N   1 
ATOM   2935 C CA  . GLY B 1 120 ? 11.127  -13.659 -4.072  1.00 20.25 ? 120  GLY B CA  1 
ATOM   2936 C C   . GLY B 1 120 ? 10.576  -12.269 -3.890  1.00 19.66 ? 120  GLY B C   1 
ATOM   2937 O O   . GLY B 1 120 ? 9.706   -11.851 -4.692  1.00 19.00 ? 120  GLY B O   1 
ATOM   2938 N N   . ALA B 1 121 ? 11.034  -11.607 -2.840  1.00 18.82 ? 121  ALA B N   1 
ATOM   2939 C CA  . ALA B 1 121 ? 10.696  -10.209 -2.518  1.00 19.72 ? 121  ALA B CA  1 
ATOM   2940 C C   . ALA B 1 121 ? 12.010  -9.452  -2.459  1.00 18.86 ? 121  ALA B C   1 
ATOM   2941 O O   . ALA B 1 121 ? 12.796  -9.758  -1.565  1.00 20.76 ? 121  ALA B O   1 
ATOM   2942 C CB  . ALA B 1 121 ? 9.968   -10.119 -1.203  1.00 20.04 ? 121  ALA B CB  1 
ATOM   2943 N N   . ILE B 1 122 ? 12.225  -8.536  -3.391  1.00 18.46 ? 122  ILE B N   1 
ATOM   2944 C CA  . ILE B 1 122 ? 13.409  -7.637  -3.406  1.00 20.09 ? 122  ILE B CA  1 
ATOM   2945 C C   . ILE B 1 122 ? 13.170  -6.531  -2.383  1.00 19.40 ? 122  ILE B C   1 
ATOM   2946 O O   . ILE B 1 122 ? 12.080  -5.945  -2.383  1.00 20.04 ? 122  ILE B O   1 
ATOM   2947 C CB  . ILE B 1 122 ? 13.618  -7.119  -4.828  1.00 21.59 ? 122  ILE B CB  1 
ATOM   2948 C CG1 . ILE B 1 122 ? 13.809  -8.297  -5.790  1.00 20.85 ? 122  ILE B CG1 1 
ATOM   2949 C CG2 . ILE B 1 122 ? 14.786  -6.140  -4.852  1.00 22.58 ? 122  ILE B CG2 1 
ATOM   2950 C CD1 . ILE B 1 122 ? 13.764  -7.910  -7.261  1.00 22.17 ? 122  ILE B CD1 1 
ATOM   2951 N N   . MET B 1 123 ? 14.108  -6.335  -1.465  1.00 20.94 ? 123  MET B N   1 
ATOM   2952 C CA  . MET B 1 123 ? 13.919  -5.430  -0.305  1.00 22.17 ? 123  MET B CA  1 
ATOM   2953 C C   . MET B 1 123 ? 14.797  -4.179  -0.479  1.00 22.15 ? 123  MET B C   1 
ATOM   2954 O O   . MET B 1 123 ? 14.988  -3.458  0.506   1.00 23.34 ? 123  MET B O   1 
ATOM   2955 C CB  . MET B 1 123 ? 14.207  -6.153  1.020   1.00 21.81 ? 123  MET B CB  1 
ATOM   2956 C CG  . MET B 1 123 ? 13.400  -7.430  1.271   1.00 21.78 ? 123  MET B CG  1 
ATOM   2957 S SD  . MET B 1 123 ? 11.629  -7.321  0.878   1.00 25.00 ? 123  MET B SD  1 
ATOM   2958 C CE  . MET B 1 123 ? 11.130  -5.937  1.909   1.00 23.06 ? 123  MET B CE  1 
ATOM   2959 N N   . VAL B 1 124 ? 15.166  -3.830  -1.716  1.00 24.72 ? 124  VAL B N   1 
ATOM   2960 C CA  . VAL B 1 124 ? 15.965  -2.597  -2.020  1.00 25.41 ? 124  VAL B CA  1 
ATOM   2961 C C   . VAL B 1 124 ? 15.425  -1.907  -3.273  1.00 26.74 ? 124  VAL B C   1 
ATOM   2962 O O   . VAL B 1 124 ? 14.695  -2.502  -4.065  1.00 28.65 ? 124  VAL B O   1 
ATOM   2963 C CB  . VAL B 1 124 ? 17.473  -2.899  -2.156  1.00 26.75 ? 124  VAL B CB  1 
ATOM   2964 C CG1 . VAL B 1 124 ? 18.013  -3.617  -0.920  1.00 28.07 ? 124  VAL B CG1 1 
ATOM   2965 C CG2 . VAL B 1 124 ? 17.812  -3.682  -3.412  1.00 26.40 ? 124  VAL B CG2 1 
ATOM   2966 N N   . PRO B 1 125 ? 15.753  -0.609  -3.470  1.00 27.12 ? 125  PRO B N   1 
ATOM   2967 C CA  . PRO B 1 125 ? 15.481  0.086   -4.722  1.00 27.49 ? 125  PRO B CA  1 
ATOM   2968 C C   . PRO B 1 125 ? 16.381  -0.412  -5.842  1.00 27.73 ? 125  PRO B C   1 
ATOM   2969 O O   . PRO B 1 125 ? 17.463  -0.924  -5.583  1.00 25.19 ? 125  PRO B O   1 
ATOM   2970 C CB  . PRO B 1 125 ? 15.789  1.558   -4.411  1.00 27.12 ? 125  PRO B CB  1 
ATOM   2971 C CG  . PRO B 1 125 ? 16.806  1.461   -3.318  1.00 27.36 ? 125  PRO B CG  1 
ATOM   2972 C CD  . PRO B 1 125 ? 16.343  0.295   -2.469  1.00 26.68 ? 125  PRO B CD  1 
ATOM   2973 N N   . PRO B 1 126 ? 15.954  -0.251  -7.113  1.00 27.61 ? 126  PRO B N   1 
ATOM   2974 C CA  . PRO B 1 126 ? 16.699  -0.774  -8.259  1.00 28.02 ? 126  PRO B CA  1 
ATOM   2975 C C   . PRO B 1 126 ? 18.204  -0.452  -8.226  1.00 28.14 ? 126  PRO B C   1 
ATOM   2976 O O   . PRO B 1 126 ? 19.002  -1.277  -8.644  1.00 28.80 ? 126  PRO B O   1 
ATOM   2977 C CB  . PRO B 1 126 ? 16.037  -0.070  -9.452  1.00 27.61 ? 126  PRO B CB  1 
ATOM   2978 C CG  . PRO B 1 126 ? 14.623  0.164   -8.987  1.00 28.10 ? 126  PRO B CG  1 
ATOM   2979 C CD  . PRO B 1 126 ? 14.733  0.455   -7.504  1.00 27.08 ? 126  PRO B CD  1 
ATOM   2980 N N   . ILE B 1 127 ? 18.570  0.736   -7.754  1.00 27.90 ? 127  ILE B N   1 
ATOM   2981 C CA  . ILE B 1 127 ? 19.981  1.198   -7.854  1.00 30.11 ? 127  ILE B CA  1 
ATOM   2982 C C   . ILE B 1 127 ? 20.853  0.274   -6.987  1.00 29.72 ? 127  ILE B C   1 
ATOM   2983 O O   . ILE B 1 127 ? 22.004  0.057   -7.360  1.00 30.91 ? 127  ILE B O   1 
ATOM   2984 C CB  . ILE B 1 127 ? 20.104  2.691   -7.496  1.00 31.16 ? 127  ILE B CB  1 
ATOM   2985 C CG1 . ILE B 1 127 ? 21.344  3.300   -8.165  1.00 34.65 ? 127  ILE B CG1 1 
ATOM   2986 C CG2 . ILE B 1 127 ? 20.017  2.902   -5.989  1.00 31.29 ? 127  ILE B CG2 1 
ATOM   2987 C CD1 . ILE B 1 127 ? 22.267  4.118   -7.281  1.00 37.44 ? 127  ILE B CD1 1 
ATOM   2988 N N   . LEU B 1 128 ? 20.308  -0.327  -5.923  1.00 28.62 ? 128  LEU B N   1 
ATOM   2989 C CA  . LEU B 1 128 ? 21.105  -1.177  -4.998  1.00 29.36 ? 128  LEU B CA  1 
ATOM   2990 C C   . LEU B 1 128 ? 21.034  -2.646  -5.413  1.00 31.39 ? 128  LEU B C   1 
ATOM   2991 O O   . LEU B 1 128 ? 21.749  -3.463  -4.805  1.00 32.03 ? 128  LEU B O   1 
ATOM   2992 C CB  . LEU B 1 128 ? 20.634  -0.955  -3.560  1.00 27.97 ? 128  LEU B CB  1 
ATOM   2993 C CG  . LEU B 1 128 ? 20.754  0.479   -3.062  1.00 28.11 ? 128  LEU B CG  1 
ATOM   2994 C CD1 . LEU B 1 128 ? 20.186  0.617   -1.662  1.00 28.49 ? 128  LEU B CD1 1 
ATOM   2995 C CD2 . LEU B 1 128 ? 22.206  0.948   -3.102  1.00 32.26 ? 128  LEU B CD2 1 
ATOM   2996 N N   . LEU B 1 129 ? 20.242  -2.982  -6.435  1.00 32.45 ? 129  LEU B N   1 
ATOM   2997 C CA  . LEU B 1 129 ? 20.105  -4.386  -6.893  1.00 29.92 ? 129  LEU B CA  1 
ATOM   2998 C C   . LEU B 1 129 ? 21.446  -4.822  -7.482  1.00 33.22 ? 129  LEU B C   1 
ATOM   2999 O O   . LEU B 1 129 ? 22.012  -4.036  -8.258  1.00 36.26 ? 129  LEU B O   1 
ATOM   3000 C CB  . LEU B 1 129 ? 18.982  -4.523  -7.925  1.00 28.60 ? 129  LEU B CB  1 
ATOM   3001 C CG  . LEU B 1 129 ? 18.563  -5.962  -8.197  1.00 24.95 ? 129  LEU B CG  1 
ATOM   3002 C CD1 . LEU B 1 129 ? 17.885  -6.536  -6.968  1.00 25.70 ? 129  LEU B CD1 1 
ATOM   3003 C CD2 . LEU B 1 129 ? 17.673  -6.055  -9.419  1.00 26.48 ? 129  LEU B CD2 1 
ATOM   3004 N N   . GLY B 1 130 ? 21.925  -6.010  -7.097  1.00 34.61 ? 130  GLY B N   1 
ATOM   3005 C CA  . GLY B 1 130 ? 23.220  -6.572  -7.532  1.00 35.93 ? 130  GLY B CA  1 
ATOM   3006 C C   . GLY B 1 130 ? 24.310  -6.457  -6.471  1.00 34.47 ? 130  GLY B C   1 
ATOM   3007 O O   . GLY B 1 130 ? 25.294  -7.193  -6.570  1.00 32.72 ? 130  GLY B O   1 
ATOM   3008 N N   . GLN B 1 131 ? 24.155  -5.574  -5.488  1.00 36.45 ? 131  GLN B N   1 
ATOM   3009 C CA  . GLN B 1 131 ? 25.080  -5.488  -4.325  1.00 40.00 ? 131  GLN B CA  1 
ATOM   3010 C C   . GLN B 1 131 ? 24.864  -6.705  -3.421  1.00 42.31 ? 131  GLN B C   1 
ATOM   3011 O O   . GLN B 1 131 ? 23.723  -7.071  -3.127  1.00 43.08 ? 131  GLN B O   1 
ATOM   3012 C CB  . GLN B 1 131 ? 24.870  -4.163  -3.594  1.00 39.47 ? 131  GLN B CB  1 
ATOM   3013 C CG  . GLN B 1 131 ? 25.174  -2.964  -4.474  1.00 43.27 ? 131  GLN B CG  1 
ATOM   3014 C CD  . GLN B 1 131 ? 25.532  -1.716  -3.706  1.00 46.84 ? 131  GLN B CD  1 
ATOM   3015 O OE1 . GLN B 1 131 ? 25.936  -0.717  -4.296  1.00 58.16 ? 131  GLN B OE1 1 
ATOM   3016 N NE2 . GLN B 1 131 ? 25.403  -1.755  -2.389  1.00 48.34 ? 131  GLN B NE2 1 
ATOM   3017 N N   . PRO B 1 132 ? 25.940  -7.402  -2.979  1.00 40.85 ? 132  PRO B N   1 
ATOM   3018 C CA  . PRO B 1 132 ? 25.796  -8.529  -2.060  1.00 38.39 ? 132  PRO B CA  1 
ATOM   3019 C C   . PRO B 1 132 ? 25.055  -8.161  -0.763  1.00 34.53 ? 132  PRO B C   1 
ATOM   3020 O O   . PRO B 1 132 ? 24.416  -9.022  -0.207  1.00 36.08 ? 132  PRO B O   1 
ATOM   3021 C CB  . PRO B 1 132 ? 27.246  -8.962  -1.793  1.00 43.57 ? 132  PRO B CB  1 
ATOM   3022 C CG  . PRO B 1 132 ? 28.006  -8.526  -3.036  1.00 42.84 ? 132  PRO B CG  1 
ATOM   3023 C CD  . PRO B 1 132 ? 27.339  -7.219  -3.414  1.00 45.37 ? 132  PRO B CD  1 
ATOM   3024 N N   . SER B 1 133 ? 25.127  -6.897  -0.349  1.00 32.63 ? 133  SER B N   1 
ATOM   3025 C CA  . SER B 1 133 ? 24.409  -6.335  0.822   1.00 34.45 ? 133  SER B CA  1 
ATOM   3026 C C   . SER B 1 133 ? 22.891  -6.294  0.581   1.00 32.10 ? 133  SER B C   1 
ATOM   3027 O O   . SER B 1 133 ? 22.168  -6.162  1.559   1.00 35.86 ? 133  SER B O   1 
ATOM   3028 C CB  . SER B 1 133 ? 24.924  -4.967  1.141   1.00 35.93 ? 133  SER B CB  1 
ATOM   3029 O OG  . SER B 1 133 ? 25.005  -4.180  -0.041  1.00 40.14 ? 133  SER B OG  1 
ATOM   3030 N N   . SER B 1 134 ? 22.429  -6.354  -0.670  1.00 31.63 ? 134  SER B N   1 
ATOM   3031 C CA  . SER B 1 134 ? 20.980  -6.341  -1.023  1.00 30.90 ? 134  SER B CA  1 
ATOM   3032 C C   . SER B 1 134 ? 20.373  -7.738  -0.871  1.00 28.75 ? 134  SER B C   1 
ATOM   3033 O O   . SER B 1 134 ? 20.713  -8.637  -1.679  1.00 28.99 ? 134  SER B O   1 
ATOM   3034 C CB  . SER B 1 134 ? 20.771  -5.793  -2.398  1.00 28.31 ? 134  SER B CB  1 
ATOM   3035 O OG  . SER B 1 134 ? 21.116  -4.415  -2.396  1.00 28.92 ? 134  SER B OG  1 
ATOM   3036 N N   . VAL B 1 135 ? 19.457  -7.882  0.090   1.00 32.20 ? 135  VAL B N   1 
ATOM   3037 C CA  . VAL B 1 135 ? 18.777  -9.172  0.414   1.00 32.94 ? 135  VAL B CA  1 
ATOM   3038 C C   . VAL B 1 135 ? 17.424  -9.257  -0.302  1.00 30.12 ? 135  VAL B C   1 
ATOM   3039 O O   . VAL B 1 135 ? 16.595  -8.336  -0.179  1.00 31.41 ? 135  VAL B O   1 
ATOM   3040 C CB  . VAL B 1 135 ? 18.622  -9.398  1.928   1.00 34.13 ? 135  VAL B CB  1 
ATOM   3041 C CG1 . VAL B 1 135 ? 17.891  -10.704 2.200   1.00 36.92 ? 135  VAL B CG1 1 
ATOM   3042 C CG2 . VAL B 1 135 ? 19.977  -9.394  2.625   1.00 33.50 ? 135  VAL B CG2 1 
ATOM   3043 N N   . THR B 1 136 ? 17.259  -10.331 -1.068  1.00 26.20 ? 136  THR B N   1 
ATOM   3044 C CA  . THR B 1 136 ? 15.984  -10.777 -1.658  1.00 25.70 ? 136  THR B CA  1 
ATOM   3045 C C   . THR B 1 136 ? 15.566  -12.031 -0.894  1.00 26.86 ? 136  THR B C   1 
ATOM   3046 O O   . THR B 1 136 ? 16.341  -13.027 -0.868  1.00 27.88 ? 136  THR B O   1 
ATOM   3047 C CB  . THR B 1 136 ? 16.106  -10.942 -3.182  1.00 26.10 ? 136  THR B CB  1 
ATOM   3048 O OG1 . THR B 1 136 ? 16.298  -9.641  -3.752  1.00 27.58 ? 136  THR B OG1 1 
ATOM   3049 C CG2 . THR B 1 136 ? 14.888  -11.573 -3.816  1.00 23.68 ? 136  THR B CG2 1 
ATOM   3050 N N   . LEU B 1 137 ? 14.388  -11.973 -0.280  1.00 26.07 ? 137  LEU B N   1 
ATOM   3051 C CA  . LEU B 1 137 ? 13.773  -13.100 0.458   1.00 26.14 ? 137  LEU B CA  1 
ATOM   3052 C C   . LEU B 1 137 ? 13.227  -14.053 -0.595  1.00 26.63 ? 137  LEU B C   1 
ATOM   3053 O O   . LEU B 1 137 ? 12.642  -13.567 -1.569  1.00 28.16 ? 137  LEU B O   1 
ATOM   3054 C CB  . LEU B 1 137 ? 12.674  -12.553 1.377   1.00 26.56 ? 137  LEU B CB  1 
ATOM   3055 C CG  . LEU B 1 137 ? 13.127  -11.479 2.368   1.00 26.68 ? 137  LEU B CG  1 
ATOM   3056 C CD1 . LEU B 1 137 ? 11.969  -11.038 3.250   1.00 27.21 ? 137  LEU B CD1 1 
ATOM   3057 C CD2 . LEU B 1 137 ? 14.277  -11.984 3.224   1.00 27.96 ? 137  LEU B CD2 1 
ATOM   3058 N N   . ILE B 1 138 ? 13.501  -15.343 -0.464  1.00 25.53 ? 138  ILE B N   1 
ATOM   3059 C CA  . ILE B 1 138 ? 12.994  -16.366 -1.415  1.00 25.94 ? 138  ILE B CA  1 
ATOM   3060 C C   . ILE B 1 138 ? 12.187  -17.363 -0.595  1.00 24.73 ? 138  ILE B C   1 
ATOM   3061 O O   . ILE B 1 138 ? 12.675  -17.797 0.453   1.00 24.11 ? 138  ILE B O   1 
ATOM   3062 C CB  . ILE B 1 138 ? 14.129  -17.069 -2.196  1.00 26.68 ? 138  ILE B CB  1 
ATOM   3063 C CG1 . ILE B 1 138 ? 15.009  -16.088 -2.973  1.00 27.54 ? 138  ILE B CG1 1 
ATOM   3064 C CG2 . ILE B 1 138 ? 13.542  -18.126 -3.119  1.00 26.64 ? 138  ILE B CG2 1 
ATOM   3065 C CD1 . ILE B 1 138 ? 14.268  -15.313 -4.031  1.00 28.80 ? 138  ILE B CD1 1 
ATOM   3066 N N   . SER B 1 139 ? 11.009  -17.737 -1.066  1.00 22.79 ? 139  SER B N   1 
ATOM   3067 C CA  . SER B 1 139 ? 10.289  -18.877 -0.469  1.00 23.84 ? 139  SER B CA  1 
ATOM   3068 C C   . SER B 1 139 ? 9.893   -19.825 -1.587  1.00 25.83 ? 139  SER B C   1 
ATOM   3069 O O   . SER B 1 139 ? 9.770   -19.377 -2.738  1.00 26.42 ? 139  SER B O   1 
ATOM   3070 C CB  . SER B 1 139 ? 9.115   -18.444 0.355   1.00 24.18 ? 139  SER B CB  1 
ATOM   3071 O OG  . SER B 1 139 ? 8.057   -17.959 -0.466  1.00 22.72 ? 139  SER B OG  1 
ATOM   3072 N N   . GLY B 1 140 ? 9.716   -21.089 -1.226  1.00 31.10 ? 140  GLY B N   1 
ATOM   3073 C CA  . GLY B 1 140 ? 9.433   -22.192 -2.156  1.00 32.64 ? 140  GLY B CA  1 
ATOM   3074 C C   . GLY B 1 140 ? 10.370  -23.363 -1.900  1.00 34.87 ? 140  GLY B C   1 
ATOM   3075 O O   . GLY B 1 140 ? 11.199  -23.296 -0.992  1.00 31.06 ? 140  GLY B O   1 
ATOM   3076 N N   . PRO B 1 141 ? 10.208  -24.465 -2.680  1.00 40.93 ? 141  PRO B N   1 
ATOM   3077 C CA  . PRO B 1 141 ? 11.013  -25.677 -2.530  1.00 38.89 ? 141  PRO B CA  1 
ATOM   3078 C C   . PRO B 1 141 ? 12.518  -25.403 -2.450  1.00 37.46 ? 141  PRO B C   1 
ATOM   3079 O O   . PRO B 1 141 ? 13.032  -24.685 -3.284  1.00 35.99 ? 141  PRO B O   1 
ATOM   3080 C CB  . PRO B 1 141 ? 10.664  -26.478 -3.792  1.00 41.71 ? 141  PRO B CB  1 
ATOM   3081 C CG  . PRO B 1 141 ? 9.226   -26.092 -4.082  1.00 42.51 ? 141  PRO B CG  1 
ATOM   3082 C CD  . PRO B 1 141 ? 9.140   -24.631 -3.685  1.00 42.62 ? 141  PRO B CD  1 
ATOM   3083 N N   . LYS B 1 142 ? 13.165  -25.965 -1.427  1.00 36.35 ? 142  LYS B N   1 
ATOM   3084 C CA  . LYS B 1 142 ? 14.618  -25.794 -1.156  1.00 38.85 ? 142  LYS B CA  1 
ATOM   3085 C C   . LYS B 1 142 ? 15.402  -26.146 -2.421  1.00 41.22 ? 142  LYS B C   1 
ATOM   3086 O O   . LYS B 1 142 ? 16.334  -25.388 -2.742  1.00 41.96 ? 142  LYS B O   1 
ATOM   3087 C CB  . LYS B 1 142 ? 15.068  -26.677 0.012   1.00 39.11 ? 142  LYS B CB  1 
ATOM   3088 C CG  . LYS B 1 142 ? 16.456  -26.374 0.552   1.00 41.68 ? 142  LYS B CG  1 
ATOM   3089 C CD  . LYS B 1 142 ? 16.484  -25.163 1.457   1.00 47.50 ? 142  LYS B CD  1 
ATOM   3090 C CE  . LYS B 1 142 ? 17.871  -24.614 1.733   1.00 51.70 ? 142  LYS B CE  1 
ATOM   3091 N NZ  . LYS B 1 142 ? 17.825  -23.506 2.721   1.00 54.92 ? 142  LYS B NZ  1 
ATOM   3092 N N   . THR B 1 143 ? 15.022  -27.240 -3.102  1.00 44.67 ? 143  THR B N   1 
ATOM   3093 C CA  . THR B 1 143 ? 15.730  -27.807 -4.288  1.00 50.47 ? 143  THR B CA  1 
ATOM   3094 C C   . THR B 1 143 ? 15.659  -26.787 -5.433  1.00 47.76 ? 143  THR B C   1 
ATOM   3095 O O   . THR B 1 143 ? 16.726  -26.456 -5.986  1.00 48.92 ? 143  THR B O   1 
ATOM   3096 C CB  . THR B 1 143 ? 15.176  -29.187 -4.693  1.00 54.69 ? 143  THR B CB  1 
ATOM   3097 O OG1 . THR B 1 143 ? 13.746  -29.135 -4.703  1.00 57.90 ? 143  THR B OG1 1 
ATOM   3098 C CG2 . THR B 1 143 ? 15.635  -30.308 -3.781  1.00 53.45 ? 143  THR B CG2 1 
ATOM   3099 N N   . ALA B 1 144 ? 14.451  -26.304 -5.744  1.00 47.20 ? 144  ALA B N   1 
ATOM   3100 C CA  . ALA B 1 144 ? 14.169  -25.234 -6.731  1.00 44.51 ? 144  ALA B CA  1 
ATOM   3101 C C   . ALA B 1 144 ? 15.011  -23.985 -6.415  1.00 44.71 ? 144  ALA B C   1 
ATOM   3102 O O   . ALA B 1 144 ? 15.581  -23.437 -7.350  1.00 49.22 ? 144  ALA B O   1 
ATOM   3103 C CB  . ALA B 1 144 ? 12.695  -24.932 -6.744  1.00 43.97 ? 144  ALA B CB  1 
ATOM   3104 N N   . TYR B 1 145 ? 15.107  -23.568 -5.147  1.00 42.61 ? 145  TYR B N   1 
ATOM   3105 C CA  . TYR B 1 145 ? 15.953  -22.434 -4.689  1.00 40.21 ? 145  TYR B CA  1 
ATOM   3106 C C   . TYR B 1 145 ? 17.438  -22.759 -4.903  1.00 45.91 ? 145  TYR B C   1 
ATOM   3107 O O   . TYR B 1 145 ? 18.204  -21.892 -5.412  1.00 41.59 ? 145  TYR B O   1 
ATOM   3108 C CB  . TYR B 1 145 ? 15.714  -22.131 -3.208  1.00 36.69 ? 145  TYR B CB  1 
ATOM   3109 C CG  . TYR B 1 145 ? 16.730  -21.192 -2.608  1.00 38.18 ? 145  TYR B CG  1 
ATOM   3110 C CD1 . TYR B 1 145 ? 16.673  -19.828 -2.849  1.00 39.57 ? 145  TYR B CD1 1 
ATOM   3111 C CD2 . TYR B 1 145 ? 17.765  -21.661 -1.818  1.00 37.71 ? 145  TYR B CD2 1 
ATOM   3112 C CE1 . TYR B 1 145 ? 17.600  -18.954 -2.307  1.00 40.27 ? 145  TYR B CE1 1 
ATOM   3113 C CE2 . TYR B 1 145 ? 18.707  -20.803 -1.277  1.00 38.37 ? 145  TYR B CE2 1 
ATOM   3114 C CZ  . TYR B 1 145 ? 18.630  -19.441 -1.520  1.00 40.48 ? 145  TYR B CZ  1 
ATOM   3115 O OH  . TYR B 1 145 ? 19.551  -18.585 -0.973  1.00 40.56 ? 145  TYR B OH  1 
ATOM   3116 N N   . GLU B 1 146 ? 17.850  -23.956 -4.468  1.00 49.28 ? 146  GLU B N   1 
ATOM   3117 C CA  . GLU B 1 146 ? 19.246  -24.466 -4.580  1.00 50.21 ? 146  GLU B CA  1 
ATOM   3118 C C   . GLU B 1 146 ? 19.685  -24.384 -6.047  1.00 45.61 ? 146  GLU B C   1 
ATOM   3119 O O   . GLU B 1 146 ? 20.815  -23.890 -6.301  1.00 41.93 ? 146  GLU B O   1 
ATOM   3120 C CB  . GLU B 1 146 ? 19.362  -25.908 -4.064  1.00 52.37 ? 146  GLU B CB  1 
ATOM   3121 C CG  . GLU B 1 146 ? 19.340  -26.053 -2.546  1.00 54.52 ? 146  GLU B CG  1 
ATOM   3122 C CD  . GLU B 1 146 ? 20.243  -25.099 -1.783  1.00 56.74 ? 146  GLU B CD  1 
ATOM   3123 O OE1 . GLU B 1 146 ? 21.376  -24.862 -2.233  1.00 62.31 ? 146  GLU B OE1 1 
ATOM   3124 O OE2 . GLU B 1 146 ? 19.798  -24.578 -0.751  1.00 62.76 ? 146  GLU B OE2 1 
ATOM   3125 N N   . SER B 1 147 ? 18.837  -24.853 -6.971  1.00 41.22 ? 147  SER B N   1 
ATOM   3126 C CA  . SER B 1 147 ? 19.120  -24.805 -8.431  1.00 48.82 ? 147  SER B CA  1 
ATOM   3127 C C   . SER B 1 147 ? 19.343  -23.348 -8.880  1.00 50.01 ? 147  SER B C   1 
ATOM   3128 O O   . SER B 1 147 ? 20.323  -23.105 -9.594  1.00 55.23 ? 147  SER B O   1 
ATOM   3129 C CB  . SER B 1 147 ? 18.059  -25.498 -9.253  1.00 48.69 ? 147  SER B CB  1 
ATOM   3130 O OG  . SER B 1 147 ? 16.769  -25.325 -8.698  1.00 52.46 ? 147  SER B OG  1 
ATOM   3131 N N   . GLN B 1 148 ? 18.511  -22.401 -8.435  1.00 48.61 ? 148  GLN B N   1 
ATOM   3132 C CA  . GLN B 1 148 ? 18.505  -21.009 -8.961  1.00 45.68 ? 148  GLN B CA  1 
ATOM   3133 C C   . GLN B 1 148 ? 19.451  -20.114 -8.164  1.00 41.89 ? 148  GLN B C   1 
ATOM   3134 O O   . GLN B 1 148 ? 19.704  -18.987 -8.613  1.00 41.48 ? 148  GLN B O   1 
ATOM   3135 C CB  . GLN B 1 148 ? 17.086  -20.445 -8.935  1.00 44.98 ? 148  GLN B CB  1 
ATOM   3136 C CG  . GLN B 1 148 ? 16.138  -21.197 -9.852  1.00 47.55 ? 148  GLN B CG  1 
ATOM   3137 C CD  . GLN B 1 148 ? 16.642  -21.307 -11.272 1.00 49.45 ? 148  GLN B CD  1 
ATOM   3138 O OE1 . GLN B 1 148 ? 17.546  -20.584 -11.703 1.00 48.20 ? 148  GLN B OE1 1 
ATOM   3139 N NE2 . GLN B 1 148 ? 16.032  -22.212 -12.023 1.00 49.01 ? 148  GLN B NE2 1 
ATOM   3140 N N   . LYS B 1 149 ? 19.950  -20.584 -7.027  1.00 42.43 ? 149  LYS B N   1 
ATOM   3141 C CA  . LYS B 1 149 ? 20.762  -19.753 -6.109  1.00 42.83 ? 149  LYS B CA  1 
ATOM   3142 C C   . LYS B 1 149 ? 21.866  -19.030 -6.892  1.00 42.78 ? 149  LYS B C   1 
ATOM   3143 O O   . LYS B 1 149 ? 22.134  -17.856 -6.569  1.00 40.66 ? 149  LYS B O   1 
ATOM   3144 C CB  . LYS B 1 149 ? 21.358  -20.606 -4.986  1.00 45.78 ? 149  LYS B CB  1 
ATOM   3145 C CG  . LYS B 1 149 ? 22.272  -19.820 -4.055  1.00 50.79 ? 149  LYS B CG  1 
ATOM   3146 C CD  . LYS B 1 149 ? 22.179  -20.190 -2.589  1.00 56.93 ? 149  LYS B CD  1 
ATOM   3147 C CE  . LYS B 1 149 ? 22.608  -19.041 -1.694  1.00 59.94 ? 149  LYS B CE  1 
ATOM   3148 N NZ  . LYS B 1 149 ? 22.723  -19.441 -0.270  1.00 60.43 ? 149  LYS B NZ  1 
ATOM   3149 N N   . GLU B 1 150 ? 22.512  -19.722 -7.845  1.00 48.85 ? 150  GLU B N   1 
ATOM   3150 C CA  . GLU B 1 150 ? 23.696  -19.214 -8.597  1.00 49.95 ? 150  GLU B CA  1 
ATOM   3151 C C   . GLU B 1 150 ? 23.260  -18.036 -9.476  1.00 44.69 ? 150  GLU B C   1 
ATOM   3152 O O   . GLU B 1 150 ? 23.855  -16.945 -9.339  1.00 45.38 ? 150  GLU B O   1 
ATOM   3153 C CB  . GLU B 1 150 ? 24.352  -20.333 -9.415  1.00 57.23 ? 150  GLU B CB  1 
ATOM   3154 C CG  . GLU B 1 150 ? 25.784  -20.028 -9.848  1.00 62.89 ? 150  GLU B CG  1 
ATOM   3155 C CD  . GLU B 1 150 ? 26.757  -19.689 -8.723  1.00 69.21 ? 150  GLU B CD  1 
ATOM   3156 O OE1 . GLU B 1 150 ? 27.779  -19.016 -8.996  1.00 70.41 ? 150  GLU B OE1 1 
ATOM   3157 O OE2 . GLU B 1 150 ? 26.497  -20.098 -7.570  1.00 77.41 ? 150  GLU B OE2 1 
ATOM   3158 N N   . LEU B 1 151 ? 22.239  -18.239 -10.311 1.00 41.93 ? 151  LEU B N   1 
ATOM   3159 C CA  . LEU B 1 151 ? 21.624  -17.181 -11.155 1.00 40.45 ? 151  LEU B CA  1 
ATOM   3160 C C   . LEU B 1 151 ? 21.277  -15.971 -10.287 1.00 40.37 ? 151  LEU B C   1 
ATOM   3161 O O   . LEU B 1 151 ? 21.667  -14.852 -10.644 1.00 41.48 ? 151  LEU B O   1 
ATOM   3162 C CB  . LEU B 1 151 ? 20.354  -17.741 -11.800 1.00 42.81 ? 151  LEU B CB  1 
ATOM   3163 C CG  . LEU B 1 151 ? 19.557  -16.735 -12.630 1.00 41.41 ? 151  LEU B CG  1 
ATOM   3164 C CD1 . LEU B 1 151 ? 20.432  -16.154 -13.731 1.00 42.59 ? 151  LEU B CD1 1 
ATOM   3165 C CD2 . LEU B 1 151 ? 18.317  -17.381 -13.214 1.00 40.50 ? 151  LEU B CD2 1 
ATOM   3166 N N   . LEU B 1 152 ? 20.581  -16.213 -9.172  1.00 39.22 ? 152  LEU B N   1 
ATOM   3167 C CA  . LEU B 1 152 ? 19.959  -15.166 -8.332  1.00 37.57 ? 152  LEU B CA  1 
ATOM   3168 C C   . LEU B 1 152 ? 21.037  -14.382 -7.586  1.00 37.87 ? 152  LEU B C   1 
ATOM   3169 O O   . LEU B 1 152 ? 20.714  -13.258 -7.115  1.00 36.01 ? 152  LEU B O   1 
ATOM   3170 C CB  . LEU B 1 152 ? 18.972  -15.816 -7.356  1.00 40.48 ? 152  LEU B CB  1 
ATOM   3171 C CG  . LEU B 1 152 ? 17.659  -16.296 -7.968  1.00 42.56 ? 152  LEU B CG  1 
ATOM   3172 C CD1 . LEU B 1 152 ? 16.755  -16.890 -6.901  1.00 43.65 ? 152  LEU B CD1 1 
ATOM   3173 C CD2 . LEU B 1 152 ? 16.953  -15.167 -8.700  1.00 42.18 ? 152  LEU B CD2 1 
ATOM   3174 N N   . SER B 1 153 ? 22.251  -14.947 -7.458  1.00 37.29 ? 153  SER B N   1 
ATOM   3175 C CA  . SER B 1 153 ? 23.423  -14.251 -6.865  1.00 36.42 ? 153  SER B CA  1 
ATOM   3176 C C   . SER B 1 153 ? 23.678  -12.947 -7.632  1.00 30.50 ? 153  SER B C   1 
ATOM   3177 O O   . SER B 1 153 ? 24.256  -12.062 -7.044  1.00 31.03 ? 153  SER B O   1 
ATOM   3178 C CB  . SER B 1 153 ? 24.664  -15.126 -6.819  1.00 35.59 ? 153  SER B CB  1 
ATOM   3179 O OG  . SER B 1 153 ? 24.988  -15.604 -8.114  1.00 33.81 ? 153  SER B OG  1 
ATOM   3180 N N   . SER B 1 154 ? 23.212  -12.824 -8.876  1.00 33.50 ? 154  SER B N   1 
ATOM   3181 C CA  . SER B 1 154 ? 23.366  -11.590 -9.696  1.00 35.68 ? 154  SER B CA  1 
ATOM   3182 C C   . SER B 1 154 ? 22.561  -10.415 -9.112  1.00 32.90 ? 154  SER B C   1 
ATOM   3183 O O   . SER B 1 154 ? 22.957  -9.273  -9.364  1.00 33.89 ? 154  SER B O   1 
ATOM   3184 C CB  . SER B 1 154 ? 23.039  -11.814 -11.158 1.00 40.34 ? 154  SER B CB  1 
ATOM   3185 O OG  . SER B 1 154 ? 21.794  -12.474 -11.335 1.00 47.98 ? 154  SER B OG  1 
ATOM   3186 N N   . ILE B 1 155 ? 21.479  -10.645 -8.364  1.00 31.66 ? 155  ILE B N   1 
ATOM   3187 C CA  . ILE B 1 155 ? 20.644  -9.511  -7.849  1.00 29.09 ? 155  ILE B CA  1 
ATOM   3188 C C   . ILE B 1 155 ? 21.060  -9.211  -6.407  1.00 28.35 ? 155  ILE B C   1 
ATOM   3189 O O   . ILE B 1 155 ? 20.484  -8.288  -5.812  1.00 25.74 ? 155  ILE B O   1 
ATOM   3190 C CB  . ILE B 1 155 ? 19.129  -9.765  -8.019  1.00 27.89 ? 155  ILE B CB  1 
ATOM   3191 C CG1 . ILE B 1 155 ? 18.587  -10.891 -7.136  1.00 28.95 ? 155  ILE B CG1 1 
ATOM   3192 C CG2 . ILE B 1 155 ? 18.799  -10.000 -9.485  1.00 29.46 ? 155  ILE B CG2 1 
ATOM   3193 C CD1 . ILE B 1 155 ? 17.069  -10.936 -7.068  1.00 29.76 ? 155  ILE B CD1 1 
ATOM   3194 N N   . GLY B 1 156 ? 22.060  -9.940  -5.896  1.00 30.00 ? 156  GLY B N   1 
ATOM   3195 C CA  . GLY B 1 156 ? 22.610  -9.760  -4.541  1.00 30.56 ? 156  GLY B CA  1 
ATOM   3196 C C   . GLY B 1 156 ? 22.556  -11.055 -3.753  1.00 31.45 ? 156  GLY B C   1 
ATOM   3197 O O   . GLY B 1 156 ? 22.705  -12.122 -4.364  1.00 36.90 ? 156  GLY B O   1 
ATOM   3198 N N   . THR B 1 157 ? 22.327  -10.969 -2.446  1.00 32.39 ? 157  THR B N   1 
ATOM   3199 C CA  . THR B 1 157 ? 22.257  -12.132 -1.519  1.00 34.75 ? 157  THR B CA  1 
ATOM   3200 C C   . THR B 1 157 ? 20.783  -12.534 -1.350  1.00 31.98 ? 157  THR B C   1 
ATOM   3201 O O   . THR B 1 157 ? 19.960  -11.718 -0.889  1.00 34.21 ? 157  THR B O   1 
ATOM   3202 C CB  . THR B 1 157 ? 23.001  -11.816 -0.209  1.00 37.16 ? 157  THR B CB  1 
ATOM   3203 O OG1 . THR B 1 157 ? 24.348  -11.442 -0.517  1.00 36.82 ? 157  THR B OG1 1 
ATOM   3204 C CG2 . THR B 1 157 ? 23.035  -12.978 0.756   1.00 38.05 ? 157  THR B CG2 1 
ATOM   3205 N N   . THR B 1 158 ? 20.451  -13.742 -1.762  1.00 32.06 ? 158  THR B N   1 
ATOM   3206 C CA  . THR B 1 158 ? 19.125  -14.361 -1.549  1.00 36.23 ? 158  THR B CA  1 
ATOM   3207 C C   . THR B 1 158 ? 19.144  -15.088 -0.214  1.00 37.74 ? 158  THR B C   1 
ATOM   3208 O O   . THR B 1 158 ? 20.201  -15.596 0.156   1.00 39.32 ? 158  THR B O   1 
ATOM   3209 C CB  . THR B 1 158 ? 18.778  -15.338 -2.666  1.00 37.36 ? 158  THR B CB  1 
ATOM   3210 O OG1 . THR B 1 158 ? 19.894  -16.224 -2.762  1.00 38.09 ? 158  THR B OG1 1 
ATOM   3211 C CG2 . THR B 1 158 ? 18.515  -14.638 -3.977  1.00 36.29 ? 158  THR B CG2 1 
ATOM   3212 N N   . ARG B 1 159 ? 17.998  -15.102 0.459   1.00 40.67 ? 159  ARG B N   1 
ATOM   3213 C CA  . ARG B 1 159 ? 17.777  -15.696 1.797   1.00 35.85 ? 159  ARG B CA  1 
ATOM   3214 C C   . ARG B 1 159 ? 16.503  -16.540 1.682   1.00 35.15 ? 159  ARG B C   1 
ATOM   3215 O O   . ARG B 1 159 ? 15.402  -15.959 1.487   1.00 29.36 ? 159  ARG B O   1 
ATOM   3216 C CB  . ARG B 1 159 ? 17.724  -14.554 2.817   1.00 41.84 ? 159  ARG B CB  1 
ATOM   3217 C CG  . ARG B 1 159 ? 16.985  -14.864 4.111   1.00 47.92 ? 159  ARG B CG  1 
ATOM   3218 C CD  . ARG B 1 159 ? 17.870  -15.511 5.147   1.00 51.97 ? 159  ARG B CD  1 
ATOM   3219 N NE  . ARG B 1 159 ? 17.240  -15.584 6.458   1.00 53.86 ? 159  ARG B NE  1 
ATOM   3220 C CZ  . ARG B 1 159 ? 17.196  -14.594 7.348   1.00 58.71 ? 159  ARG B CZ  1 
ATOM   3221 N NH1 . ARG B 1 159 ? 17.722  -13.408 7.078   1.00 59.33 ? 159  ARG B NH1 1 
ATOM   3222 N NH2 . ARG B 1 159 ? 16.607  -14.795 8.512   1.00 60.53 ? 159  ARG B NH2 1 
ATOM   3223 N N   . HIS B 1 160 ? 16.654  -17.863 1.736   1.00 31.15 ? 160  HIS B N   1 
ATOM   3224 C CA  . HIS B 1 160 ? 15.540  -18.826 1.638   1.00 32.04 ? 160  HIS B CA  1 
ATOM   3225 C C   . HIS B 1 160 ? 14.880  -18.861 3.018   1.00 32.99 ? 160  HIS B C   1 
ATOM   3226 O O   . HIS B 1 160 ? 15.552  -19.274 3.980   1.00 36.91 ? 160  HIS B O   1 
ATOM   3227 C CB  . HIS B 1 160 ? 16.027  -20.191 1.129   1.00 31.56 ? 160  HIS B CB  1 
ATOM   3228 C CG  . HIS B 1 160 ? 14.896  -21.134 0.927   1.00 30.57 ? 160  HIS B CG  1 
ATOM   3229 N ND1 . HIS B 1 160 ? 14.576  -22.098 1.845   1.00 32.34 ? 160  HIS B ND1 1 
ATOM   3230 C CD2 . HIS B 1 160 ? 13.950  -21.191 -0.030  1.00 31.93 ? 160  HIS B CD2 1 
ATOM   3231 C CE1 . HIS B 1 160 ? 13.505  -22.746 1.440   1.00 36.37 ? 160  HIS B CE1 1 
ATOM   3232 N NE2 . HIS B 1 160 ? 13.100  -22.208 0.289   1.00 33.05 ? 160  HIS B NE2 1 
ATOM   3233 N N   . VAL B 1 161 ? 13.658  -18.341 3.123   1.00 32.04 ? 161  VAL B N   1 
ATOM   3234 C CA  . VAL B 1 161 ? 13.003  -18.073 4.432   1.00 30.18 ? 161  VAL B CA  1 
ATOM   3235 C C   . VAL B 1 161 ? 12.118  -19.260 4.760   1.00 30.25 ? 161  VAL B C   1 
ATOM   3236 O O   . VAL B 1 161 ? 11.827  -19.433 5.944   1.00 27.97 ? 161  VAL B O   1 
ATOM   3237 C CB  . VAL B 1 161 ? 12.187  -16.771 4.463   1.00 28.94 ? 161  VAL B CB  1 
ATOM   3238 C CG1 . VAL B 1 161 ? 13.076  -15.546 4.317   1.00 28.25 ? 161  VAL B CG1 1 
ATOM   3239 C CG2 . VAL B 1 161 ? 11.043  -16.769 3.457   1.00 27.77 ? 161  VAL B CG2 1 
ATOM   3240 N N   . SER B 1 162 ? 11.652  -19.997 3.751   1.00 30.46 ? 162  SER B N   1 
ATOM   3241 C CA  . SER B 1 162 ? 10.689  -21.100 3.987   1.00 29.79 ? 162  SER B CA  1 
ATOM   3242 C C   . SER B 1 162 ? 10.435  -21.909 2.720   1.00 30.41 ? 162  SER B C   1 
ATOM   3243 O O   . SER B 1 162 ? 10.549  -21.346 1.621   1.00 30.57 ? 162  SER B O   1 
ATOM   3244 C CB  . SER B 1 162 ? 9.425   -20.544 4.542   1.00 29.23 ? 162  SER B CB  1 
ATOM   3245 O OG  . SER B 1 162 ? 8.441   -21.552 4.641   1.00 32.26 ? 162  SER B OG  1 
ATOM   3246 N N   . ASP B 1 163 ? 10.075  -23.181 2.906   1.00 30.35 ? 163  ASP B N   1 
ATOM   3247 C CA  . ASP B 1 163 ? 9.568   -24.111 1.863   1.00 32.79 ? 163  ASP B CA  1 
ATOM   3248 C C   . ASP B 1 163 ? 8.157   -23.672 1.442   1.00 29.52 ? 163  ASP B C   1 
ATOM   3249 O O   . ASP B 1 163 ? 7.722   -24.020 0.333   1.00 28.09 ? 163  ASP B O   1 
ATOM   3250 C CB  . ASP B 1 163 ? 9.560   -25.563 2.366   1.00 38.68 ? 163  ASP B CB  1 
ATOM   3251 C CG  . ASP B 1 163 ? 10.928  -26.219 2.528   1.00 46.92 ? 163  ASP B CG  1 
ATOM   3252 O OD1 . ASP B 1 163 ? 11.846  -25.884 1.747   1.00 49.63 ? 163  ASP B OD1 1 
ATOM   3253 O OD2 . ASP B 1 163 ? 11.069  -27.079 3.435   1.00 52.43 ? 163  ASP B OD2 1 
ATOM   3254 N N   . ASP B 1 164 ? 7.455   -22.929 2.291   1.00 29.74 ? 164  ASP B N   1 
ATOM   3255 C CA  . ASP B 1 164 ? 6.056   -22.505 2.034   1.00 28.94 ? 164  ASP B CA  1 
ATOM   3256 C C   . ASP B 1 164 ? 6.062   -21.331 1.044   1.00 32.16 ? 164  ASP B C   1 
ATOM   3257 O O   . ASP B 1 164 ? 6.692   -20.306 1.341   1.00 28.52 ? 164  ASP B O   1 
ATOM   3258 C CB  . ASP B 1 164 ? 5.364   -22.178 3.348   1.00 32.24 ? 164  ASP B CB  1 
ATOM   3259 C CG  . ASP B 1 164 ? 4.061   -21.423 3.201   1.00 36.08 ? 164  ASP B CG  1 
ATOM   3260 O OD1 . ASP B 1 164 ? 3.530   -21.334 2.067   1.00 36.72 ? 164  ASP B OD1 1 
ATOM   3261 O OD2 . ASP B 1 164 ? 3.610   -20.901 4.227   1.00 42.79 ? 164  ASP B OD2 1 
ATOM   3262 N N   . ILE B 1 165 ? 5.361   -21.464 -0.087  1.00 33.83 ? 165  ILE B N   1 
ATOM   3263 C CA  . ILE B 1 165 ? 5.498   -20.514 -1.230  1.00 35.54 ? 165  ILE B CA  1 
ATOM   3264 C C   . ILE B 1 165 ? 5.079   -19.102 -0.788  1.00 30.80 ? 165  ILE B C   1 
ATOM   3265 O O   . ILE B 1 165 ? 5.658   -18.149 -1.279  1.00 28.11 ? 165  ILE B O   1 
ATOM   3266 C CB  . ILE B 1 165 ? 4.745   -21.014 -2.485  1.00 38.19 ? 165  ILE B CB  1 
ATOM   3267 C CG1 . ILE B 1 165 ? 5.444   -20.533 -3.755  1.00 43.82 ? 165  ILE B CG1 1 
ATOM   3268 C CG2 . ILE B 1 165 ? 3.282   -20.618 -2.490  1.00 36.85 ? 165  ILE B CG2 1 
ATOM   3269 C CD1 . ILE B 1 165 ? 6.919   -20.883 -3.823  1.00 44.75 ? 165  ILE B CD1 1 
ATOM   3270 N N   . ALA B 1 166 ? 4.128   -18.997 0.140   1.00 28.57 ? 166  ALA B N   1 
ATOM   3271 C CA  . ALA B 1 166 ? 3.451   -17.745 0.565   1.00 26.08 ? 166  ALA B CA  1 
ATOM   3272 C C   . ALA B 1 166 ? 4.369   -16.884 1.458   1.00 25.89 ? 166  ALA B C   1 
ATOM   3273 O O   . ALA B 1 166 ? 4.085   -15.664 1.607   1.00 25.79 ? 166  ALA B O   1 
ATOM   3274 C CB  . ALA B 1 166 ? 2.162   -18.126 1.264   1.00 23.40 ? 166  ALA B CB  1 
ATOM   3275 N N   . LYS B 1 167 ? 5.460   -17.456 1.994   1.00 26.76 ? 167  LYS B N   1 
ATOM   3276 C CA  . LYS B 1 167 ? 6.248   -16.862 3.117   1.00 25.43 ? 167  LYS B CA  1 
ATOM   3277 C C   . LYS B 1 167 ? 6.965   -15.573 2.688   1.00 23.10 ? 167  LYS B C   1 
ATOM   3278 O O   . LYS B 1 167 ? 6.920   -14.599 3.450   1.00 20.57 ? 167  LYS B O   1 
ATOM   3279 C CB  . LYS B 1 167 ? 7.236   -17.876 3.697   1.00 28.49 ? 167  LYS B CB  1 
ATOM   3280 C CG  . LYS B 1 167 ? 7.625   -17.630 5.152   1.00 35.35 ? 167  LYS B CG  1 
ATOM   3281 C CD  . LYS B 1 167 ? 6.465   -17.663 6.159   1.00 40.85 ? 167  LYS B CD  1 
ATOM   3282 C CE  . LYS B 1 167 ? 5.627   -18.926 6.122   1.00 43.50 ? 167  LYS B CE  1 
ATOM   3283 N NZ  . LYS B 1 167 ? 4.533   -18.827 5.123   1.00 46.20 ? 167  LYS B NZ  1 
ATOM   3284 N N   . ALA B 1 168 ? 7.597   -15.535 1.520   1.00 22.81 ? 168  ALA B N   1 
ATOM   3285 C CA  . ALA B 1 168 ? 8.360   -14.345 1.061   1.00 22.02 ? 168  ALA B CA  1 
ATOM   3286 C C   . ALA B 1 168 ? 7.383   -13.173 1.005   1.00 19.76 ? 168  ALA B C   1 
ATOM   3287 O O   . ALA B 1 168 ? 7.715   -12.088 1.513   1.00 18.45 ? 168  ALA B O   1 
ATOM   3288 C CB  . ALA B 1 168 ? 9.042   -14.577 -0.272  1.00 21.38 ? 168  ALA B CB  1 
ATOM   3289 N N   . SER B 1 169 ? 6.194   -13.404 0.457   1.00 20.84 ? 169  SER B N   1 
ATOM   3290 C CA  . SER B 1 169 ? 5.153   -12.354 0.350   1.00 20.15 ? 169  SER B CA  1 
ATOM   3291 C C   . SER B 1 169 ? 4.608   -12.009 1.743   1.00 20.32 ? 169  SER B C   1 
ATOM   3292 O O   . SER B 1 169 ? 4.404   -10.804 2.003   1.00 21.13 ? 169  SER B O   1 
ATOM   3293 C CB  . SER B 1 169 ? 4.107   -12.712 -0.617  1.00 20.51 ? 169  SER B CB  1 
ATOM   3294 O OG  . SER B 1 169 ? 4.644   -12.756 -1.927  1.00 20.98 ? 169  SER B OG  1 
ATOM   3295 N N   . LEU B 1 170 ? 4.513   -12.963 2.669   1.00 21.52 ? 170  LEU B N   1 
ATOM   3296 C CA  . LEU B 1 170 ? 4.107   -12.606 4.061   1.00 23.63 ? 170  LEU B CA  1 
ATOM   3297 C C   . LEU B 1 170 ? 5.113   -11.621 4.661   1.00 21.69 ? 170  LEU B C   1 
ATOM   3298 O O   . LEU B 1 170 ? 4.689   -10.593 5.193   1.00 23.14 ? 170  LEU B O   1 
ATOM   3299 C CB  . LEU B 1 170 ? 4.021   -13.847 4.949   1.00 25.32 ? 170  LEU B CB  1 
ATOM   3300 C CG  . LEU B 1 170 ? 3.618   -13.531 6.386   1.00 24.89 ? 170  LEU B CG  1 
ATOM   3301 C CD1 . LEU B 1 170 ? 2.129   -13.236 6.443   1.00 26.91 ? 170  LEU B CD1 1 
ATOM   3302 C CD2 . LEU B 1 170 ? 4.002   -14.653 7.325   1.00 24.09 ? 170  LEU B CD2 1 
ATOM   3303 N N   . LEU B 1 171 ? 6.398   -11.967 4.628   1.00 22.27 ? 171  LEU B N   1 
ATOM   3304 C CA  . LEU B 1 171 ? 7.478   -11.189 5.279   1.00 22.48 ? 171  LEU B CA  1 
ATOM   3305 C C   . LEU B 1 171 ? 7.633   -9.854  4.533   1.00 23.05 ? 171  LEU B C   1 
ATOM   3306 O O   . LEU B 1 171 ? 7.832   -8.819  5.218   1.00 23.04 ? 171  LEU B O   1 
ATOM   3307 C CB  . LEU B 1 171 ? 8.766   -12.024 5.276   1.00 23.91 ? 171  LEU B CB  1 
ATOM   3308 C CG  . LEU B 1 171 ? 8.697   -13.357 6.027   1.00 25.16 ? 171  LEU B CG  1 
ATOM   3309 C CD1 . LEU B 1 171 ? 9.942   -14.189 5.767   1.00 27.39 ? 171  LEU B CD1 1 
ATOM   3310 C CD2 . LEU B 1 171 ? 8.504   -13.139 7.515   1.00 28.17 ? 171  LEU B CD2 1 
ATOM   3311 N N   . ASP B 1 172 ? 7.533   -9.881  3.194   1.00 22.56 ? 172  ASP B N   1 
ATOM   3312 C CA  . ASP B 1 172 ? 7.532   -8.671  2.321   1.00 23.74 ? 172  ASP B CA  1 
ATOM   3313 C C   . ASP B 1 172 ? 6.498   -7.650  2.818   1.00 23.07 ? 172  ASP B C   1 
ATOM   3314 O O   . ASP B 1 172 ? 6.887   -6.504  3.086   1.00 22.53 ? 172  ASP B O   1 
ATOM   3315 C CB  . ASP B 1 172 ? 7.219   -9.036  0.873   1.00 23.97 ? 172  ASP B CB  1 
ATOM   3316 C CG  . ASP B 1 172 ? 7.458   -7.920  -0.114  1.00 23.80 ? 172  ASP B CG  1 
ATOM   3317 O OD1 . ASP B 1 172 ? 8.241   -7.008  0.213   1.00 26.30 ? 172  ASP B OD1 1 
ATOM   3318 O OD2 . ASP B 1 172 ? 6.852   -7.974  -1.197  1.00 24.07 ? 172  ASP B OD2 1 
ATOM   3319 N N   . ASN B 1 173 ? 5.227   -8.047  2.932   1.00 23.79 ? 173  ASN B N   1 
ATOM   3320 C CA  . ASN B 1 173 ? 4.114   -7.187  3.436   1.00 22.93 ? 173  ASN B CA  1 
ATOM   3321 C C   . ASN B 1 173 ? 4.414   -6.676  4.854   1.00 21.77 ? 173  ASN B C   1 
ATOM   3322 O O   . ASN B 1 173 ? 4.203   -5.462  5.133   1.00 22.36 ? 173  ASN B O   1 
ATOM   3323 C CB  . ASN B 1 173 ? 2.781   -7.930  3.398   1.00 22.99 ? 173  ASN B CB  1 
ATOM   3324 C CG  . ASN B 1 173 ? 2.225   -7.964  1.999   1.00 24.26 ? 173  ASN B CG  1 
ATOM   3325 O OD1 . ASN B 1 173 ? 1.499   -7.045  1.607   1.00 25.57 ? 173  ASN B OD1 1 
ATOM   3326 N ND2 . ASN B 1 173 ? 2.630   -8.962  1.230   1.00 21.31 ? 173  ASN B ND2 1 
ATOM   3327 N N   . ALA B 1 174 ? 4.894   -7.550  5.728   1.00 22.58 ? 174  ALA B N   1 
ATOM   3328 C CA  . ALA B 1 174 ? 5.329   -7.179  7.101   1.00 22.69 ? 174  ALA B CA  1 
ATOM   3329 C C   . ALA B 1 174 ? 6.464   -6.145  7.040   1.00 21.09 ? 174  ALA B C   1 
ATOM   3330 O O   . ALA B 1 174 ? 6.324   -5.085  7.654   1.00 19.86 ? 174  ALA B O   1 
ATOM   3331 C CB  . ALA B 1 174 ? 5.718   -8.393  7.893   1.00 22.98 ? 174  ALA B CB  1 
ATOM   3332 N N   . LEU B 1 175 ? 7.533   -6.398  6.286   1.00 20.96 ? 175  LEU B N   1 
ATOM   3333 C CA  . LEU B 1 175 ? 8.649   -5.413  6.175   1.00 21.25 ? 175  LEU B CA  1 
ATOM   3334 C C   . LEU B 1 175 ? 8.164   -4.106  5.509   1.00 20.63 ? 175  LEU B C   1 
ATOM   3335 O O   . LEU B 1 175 ? 8.636   -3.009  5.915   1.00 20.13 ? 175  LEU B O   1 
ATOM   3336 C CB  . LEU B 1 175 ? 9.799   -6.048  5.393   1.00 21.68 ? 175  LEU B CB  1 
ATOM   3337 C CG  . LEU B 1 175 ? 10.541  -7.175  6.115   1.00 22.17 ? 175  LEU B CG  1 
ATOM   3338 C CD1 . LEU B 1 175 ? 11.516  -7.863  5.174   1.00 21.60 ? 175  LEU B CD1 1 
ATOM   3339 C CD2 . LEU B 1 175 ? 11.267  -6.655  7.353   1.00 22.14 ? 175  LEU B CD2 1 
ATOM   3340 N N   . LEU B 1 176 ? 7.286   -4.180  4.499   1.00 19.33 ? 176  LEU B N   1 
ATOM   3341 C CA  . LEU B 1 176 ? 6.873   -2.963  3.749   1.00 19.42 ? 176  LEU B CA  1 
ATOM   3342 C C   . LEU B 1 176 ? 5.948   -2.113  4.630   1.00 17.62 ? 176  LEU B C   1 
ATOM   3343 O O   . LEU B 1 176 ? 5.963   -0.899  4.448   1.00 18.60 ? 176  LEU B O   1 
ATOM   3344 C CB  . LEU B 1 176 ? 6.237   -3.324  2.403   1.00 19.35 ? 176  LEU B CB  1 
ATOM   3345 C CG  . LEU B 1 176 ? 7.190   -3.851  1.328   1.00 19.72 ? 176  LEU B CG  1 
ATOM   3346 C CD1 . LEU B 1 176 ? 6.427   -4.294  0.094   1.00 18.70 ? 176  LEU B CD1 1 
ATOM   3347 C CD2 . LEU B 1 176 ? 8.254   -2.839  0.931   1.00 20.58 ? 176  LEU B CD2 1 
ATOM   3348 N N   . SER B 1 177 ? 5.258   -2.712  5.591   1.00 17.97 ? 177  SER B N   1 
ATOM   3349 C CA  . SER B 1 177 ? 4.459   -2.004  6.628   1.00 19.92 ? 177  SER B CA  1 
ATOM   3350 C C   . SER B 1 177 ? 5.357   -1.070  7.440   1.00 21.14 ? 177  SER B C   1 
ATOM   3351 O O   . SER B 1 177 ? 4.987   0.122   7.646   1.00 20.64 ? 177  SER B O   1 
ATOM   3352 C CB  . SER B 1 177 ? 3.731   -2.968  7.522   1.00 20.30 ? 177  SER B CB  1 
ATOM   3353 O OG  . SER B 1 177 ? 2.801   -3.736  6.771   1.00 18.52 ? 177  SER B OG  1 
ATOM   3354 N N   . ILE B 1 178 ? 6.506   -1.590  7.871   1.00 21.94 ? 178  ILE B N   1 
ATOM   3355 C CA  . ILE B 1 178 ? 7.507   -0.813  8.647   1.00 20.78 ? 178  ILE B CA  1 
ATOM   3356 C C   . ILE B 1 178 ? 7.996   0.326   7.747   1.00 20.46 ? 178  ILE B C   1 
ATOM   3357 O O   . ILE B 1 178 ? 8.047   1.471   8.207   1.00 18.28 ? 178  ILE B O   1 
ATOM   3358 C CB  . ILE B 1 178 ? 8.661   -1.712  9.122   1.00 20.79 ? 178  ILE B CB  1 
ATOM   3359 C CG1 . ILE B 1 178 ? 8.188   -2.924  9.927   1.00 22.86 ? 178  ILE B CG1 1 
ATOM   3360 C CG2 . ILE B 1 178 ? 9.687   -0.905  9.887   1.00 21.70 ? 178  ILE B CG2 1 
ATOM   3361 C CD1 . ILE B 1 178 ? 9.298   -3.954  10.178  1.00 22.50 ? 178  ILE B CD1 1 
ATOM   3362 N N   . MET B 1 179 ? 8.426   -0.002  6.529   1.00 21.01 ? 179  MET B N   1 
ATOM   3363 C CA  . MET B 1 179 ? 8.965   0.992   5.576   1.00 22.64 ? 179  MET B CA  1 
ATOM   3364 C C   . MET B 1 179 ? 7.932   2.104   5.372   1.00 21.75 ? 179  MET B C   1 
ATOM   3365 O O   . MET B 1 179 ? 8.343   3.261   5.346   1.00 18.85 ? 179  MET B O   1 
ATOM   3366 C CB  . MET B 1 179 ? 9.280   0.378   4.214   1.00 25.11 ? 179  MET B CB  1 
ATOM   3367 C CG  . MET B 1 179 ? 10.038  1.318   3.317   1.00 29.50 ? 179  MET B CG  1 
ATOM   3368 S SD  . MET B 1 179 ? 10.449  0.583   1.740   1.00 37.01 ? 179  MET B SD  1 
ATOM   3369 C CE  . MET B 1 179 ? 11.358  -0.890  2.227   1.00 36.23 ? 179  MET B CE  1 
ATOM   3370 N N   . GLY B 1 180 ? 6.665   1.752   5.160   1.00 20.87 ? 180  GLY B N   1 
ATOM   3371 C CA  . GLY B 1 180 ? 5.609   2.756   4.918   1.00 24.85 ? 180  GLY B CA  1 
ATOM   3372 C C   . GLY B 1 180 ? 5.395   3.636   6.149   1.00 24.02 ? 180  GLY B C   1 
ATOM   3373 O O   . GLY B 1 180 ? 5.169   4.844   5.995   1.00 22.76 ? 180  GLY B O   1 
ATOM   3374 N N   . GLY B 1 181 ? 5.460   3.040   7.341   1.00 23.19 ? 181  GLY B N   1 
ATOM   3375 C CA  . GLY B 1 181 ? 5.389   3.800   8.598   1.00 23.36 ? 181  GLY B CA  1 
ATOM   3376 C C   . GLY B 1 181 ? 6.541   4.773   8.692   1.00 24.61 ? 181  GLY B C   1 
ATOM   3377 O O   . GLY B 1 181 ? 6.294   5.924   9.028   1.00 24.48 ? 181  GLY B O   1 
ATOM   3378 N N   . VAL B 1 182 ? 7.759   4.300   8.420   1.00 23.83 ? 182  VAL B N   1 
ATOM   3379 C CA  . VAL B 1 182 ? 9.022   5.068   8.563   1.00 25.73 ? 182  VAL B CA  1 
ATOM   3380 C C   . VAL B 1 182 ? 8.935   6.279   7.626   1.00 26.61 ? 182  VAL B C   1 
ATOM   3381 O O   . VAL B 1 182 ? 9.233   7.415   8.062   1.00 21.37 ? 182  VAL B O   1 
ATOM   3382 C CB  . VAL B 1 182 ? 10.254  4.188   8.271   1.00 26.76 ? 182  VAL B CB  1 
ATOM   3383 C CG1 . VAL B 1 182 ? 11.503  5.017   8.048   1.00 28.92 ? 182  VAL B CG1 1 
ATOM   3384 C CG2 . VAL B 1 182 ? 10.502  3.156   9.363   1.00 27.41 ? 182  VAL B CG2 1 
ATOM   3385 N N   . PHE B 1 183 ? 8.537   6.038   6.378   1.00 26.40 ? 183  PHE B N   1 
ATOM   3386 C CA  . PHE B 1 183 ? 8.391   7.091   5.342   1.00 25.84 ? 183  PHE B CA  1 
ATOM   3387 C C   . PHE B 1 183 ? 7.336   8.113   5.774   1.00 25.24 ? 183  PHE B C   1 
ATOM   3388 O O   . PHE B 1 183 ? 7.610   9.335   5.671   1.00 25.28 ? 183  PHE B O   1 
ATOM   3389 C CB  . PHE B 1 183 ? 8.016   6.457   4.005   1.00 26.35 ? 183  PHE B CB  1 
ATOM   3390 C CG  . PHE B 1 183 ? 9.161   5.792   3.292   1.00 28.91 ? 183  PHE B CG  1 
ATOM   3391 C CD1 . PHE B 1 183 ? 10.474  5.960   3.718   1.00 28.31 ? 183  PHE B CD1 1 
ATOM   3392 C CD2 . PHE B 1 183 ? 8.924   5.044   2.149   1.00 29.39 ? 183  PHE B CD2 1 
ATOM   3393 C CE1 . PHE B 1 183 ? 11.520  5.351   3.039   1.00 31.23 ? 183  PHE B CE1 1 
ATOM   3394 C CE2 . PHE B 1 183 ? 9.971   4.441   1.472   1.00 30.39 ? 183  PHE B CE2 1 
ATOM   3395 C CZ  . PHE B 1 183 ? 11.269  4.596   1.917   1.00 28.95 ? 183  PHE B CZ  1 
ATOM   3396 N N   . GLU B 1 184 ? 6.188   7.619   6.231   1.00 22.77 ? 184  GLU B N   1 
ATOM   3397 C CA  . GLU B 1 184 ? 5.072   8.461   6.709   1.00 28.98 ? 184  GLU B CA  1 
ATOM   3398 C C   . GLU B 1 184 ? 5.605   9.423   7.771   1.00 27.30 ? 184  GLU B C   1 
ATOM   3399 O O   . GLU B 1 184 ? 5.335   10.627  7.676   1.00 28.23 ? 184  GLU B O   1 
ATOM   3400 C CB  . GLU B 1 184 ? 3.953   7.612   7.298   1.00 28.66 ? 184  GLU B CB  1 
ATOM   3401 C CG  . GLU B 1 184 ? 2.716   8.424   7.635   1.00 32.33 ? 184  GLU B CG  1 
ATOM   3402 C CD  . GLU B 1 184 ? 1.632   7.580   8.277   1.00 33.01 ? 184  GLU B CD  1 
ATOM   3403 O OE1 . GLU B 1 184 ? 0.462   7.956   8.199   1.00 30.90 ? 184  GLU B OE1 1 
ATOM   3404 O OE2 . GLU B 1 184 ? 1.984   6.534   8.845   1.00 37.66 ? 184  GLU B OE2 1 
ATOM   3405 N N   . GLY B 1 185 ? 6.344   8.877   8.732   1.00 25.32 ? 185  GLY B N   1 
ATOM   3406 C CA  . GLY B 1 185 ? 6.938   9.647   9.829   1.00 24.86 ? 185  GLY B CA  1 
ATOM   3407 C C   . GLY B 1 185 ? 7.924   10.657  9.295   1.00 23.99 ? 185  GLY B C   1 
ATOM   3408 O O   . GLY B 1 185 ? 7.858   11.794  9.722   1.00 22.81 ? 185  GLY B O   1 
ATOM   3409 N N   . TRP B 1 186 ? 8.829   10.219  8.416   1.00 23.87 ? 186  TRP B N   1 
ATOM   3410 C CA  . TRP B 1 186 ? 9.935   11.030  7.857   1.00 24.00 ? 186  TRP B CA  1 
ATOM   3411 C C   . TRP B 1 186 ? 9.364   12.202  7.057   1.00 25.10 ? 186  TRP B C   1 
ATOM   3412 O O   . TRP B 1 186 ? 9.848   13.322  7.230   1.00 26.39 ? 186  TRP B O   1 
ATOM   3413 C CB  . TRP B 1 186 ? 10.809  10.157  6.975   1.00 25.47 ? 186  TRP B CB  1 
ATOM   3414 C CG  . TRP B 1 186 ? 12.116  10.770  6.585   1.00 25.99 ? 186  TRP B CG  1 
ATOM   3415 C CD1 . TRP B 1 186 ? 12.608  10.883  5.322   1.00 25.80 ? 186  TRP B CD1 1 
ATOM   3416 C CD2 . TRP B 1 186 ? 13.131  11.284  7.466   1.00 27.49 ? 186  TRP B CD2 1 
ATOM   3417 N NE1 . TRP B 1 186 ? 13.851  11.439  5.345   1.00 26.16 ? 186  TRP B NE1 1 
ATOM   3418 C CE2 . TRP B 1 186 ? 14.203  11.699  6.646   1.00 28.86 ? 186  TRP B CE2 1 
ATOM   3419 C CE3 . TRP B 1 186 ? 13.247  11.422  8.854   1.00 27.86 ? 186  TRP B CE3 1 
ATOM   3420 C CZ2 . TRP B 1 186 ? 15.382  12.225  7.174   1.00 28.52 ? 186  TRP B CZ2 1 
ATOM   3421 C CZ3 . TRP B 1 186 ? 14.400  11.969  9.374   1.00 29.55 ? 186  TRP B CZ3 1 
ATOM   3422 C CH2 . TRP B 1 186 ? 15.454  12.363  8.543   1.00 29.99 ? 186  TRP B CH2 1 
ATOM   3423 N N   . VAL B 1 187 ? 8.380   11.916  6.209   1.00 25.34 ? 187  VAL B N   1 
ATOM   3424 C CA  . VAL B 1 187 ? 7.684   12.920  5.362   1.00 26.78 ? 187  VAL B CA  1 
ATOM   3425 C C   . VAL B 1 187 ? 7.056   13.967  6.292   1.00 26.46 ? 187  VAL B C   1 
ATOM   3426 O O   . VAL B 1 187 ? 7.267   15.158  6.031   1.00 26.78 ? 187  VAL B O   1 
ATOM   3427 C CB  . VAL B 1 187 ? 6.636   12.238  4.462   1.00 28.27 ? 187  VAL B CB  1 
ATOM   3428 C CG1 . VAL B 1 187 ? 5.756   13.259  3.773   1.00 30.66 ? 187  VAL B CG1 1 
ATOM   3429 C CG2 . VAL B 1 187 ? 7.293   11.332  3.429   1.00 31.12 ? 187  VAL B CG2 1 
ATOM   3430 N N   . GLN B 1 188 ? 6.360   13.530  7.350   1.00 25.59 ? 188  GLN B N   1 
ATOM   3431 C CA  . GLN B 1 188 ? 5.729   14.437  8.346   1.00 25.98 ? 188  GLN B CA  1 
ATOM   3432 C C   . GLN B 1 188 ? 6.805   15.317  8.973   1.00 24.83 ? 188  GLN B C   1 
ATOM   3433 O O   . GLN B 1 188 ? 6.609   16.520  9.038   1.00 26.54 ? 188  GLN B O   1 
ATOM   3434 C CB  . GLN B 1 188 ? 4.991   13.671  9.442   1.00 25.79 ? 188  GLN B CB  1 
ATOM   3435 C CG  . GLN B 1 188 ? 4.236   14.585  10.397  1.00 26.63 ? 188  GLN B CG  1 
ATOM   3436 C CD  . GLN B 1 188 ? 3.084   15.272  9.694   1.00 30.15 ? 188  GLN B CD  1 
ATOM   3437 O OE1 . GLN B 1 188 ? 2.121   14.629  9.298   1.00 33.97 ? 188  GLN B OE1 1 
ATOM   3438 N NE2 . GLN B 1 188 ? 3.180   16.579  9.517   1.00 26.41 ? 188  GLN B NE2 1 
ATOM   3439 N N   . ALA B 1 189 ? 7.891   14.714  9.443   1.00 25.35 ? 189  ALA B N   1 
ATOM   3440 C CA  . ALA B 1 189 ? 9.024   15.408  10.089  1.00 26.02 ? 189  ALA B CA  1 
ATOM   3441 C C   . ALA B 1 189 ? 9.612   16.448  9.125   1.00 26.34 ? 189  ALA B C   1 
ATOM   3442 O O   . ALA B 1 189 ? 9.914   17.594  9.570   1.00 22.69 ? 189  ALA B O   1 
ATOM   3443 C CB  . ALA B 1 189 ? 10.062  14.397  10.514  1.00 25.52 ? 189  ALA B CB  1 
ATOM   3444 N N   . LEU B 1 190 ? 9.810   16.065  7.858   1.00 26.23 ? 190  LEU B N   1 
ATOM   3445 C CA  . LEU B 1 190 ? 10.506  16.949  6.875   1.00 26.61 ? 190  LEU B CA  1 
ATOM   3446 C C   . LEU B 1 190 ? 9.597   18.123  6.508   1.00 26.89 ? 190  LEU B C   1 
ATOM   3447 O O   . LEU B 1 190 ? 10.121  19.257  6.387   1.00 30.86 ? 190  LEU B O   1 
ATOM   3448 C CB  . LEU B 1 190 ? 10.917  16.138  5.643   1.00 27.11 ? 190  LEU B CB  1 
ATOM   3449 C CG  . LEU B 1 190 ? 12.080  15.175  5.853   1.00 27.66 ? 190  LEU B CG  1 
ATOM   3450 C CD1 . LEU B 1 190 ? 12.541  14.598  4.527   1.00 29.62 ? 190  LEU B CD1 1 
ATOM   3451 C CD2 . LEU B 1 190 ? 13.231  15.867  6.550   1.00 28.80 ? 190  LEU B CD2 1 
ATOM   3452 N N   . ALA B 1 191 ? 8.292   17.866  6.365   1.00 27.58 ? 191  ALA B N   1 
ATOM   3453 C CA  . ALA B 1 191 ? 7.277   18.897  6.068   1.00 29.24 ? 191  ALA B CA  1 
ATOM   3454 C C   . ALA B 1 191 ? 7.279   19.910  7.214   1.00 30.17 ? 191  ALA B C   1 
ATOM   3455 O O   . ALA B 1 191 ? 7.204   21.110  6.935   1.00 28.07 ? 191  ALA B O   1 
ATOM   3456 C CB  . ALA B 1 191 ? 5.915   18.271  5.872   1.00 26.70 ? 191  ALA B CB  1 
ATOM   3457 N N   . ILE B 1 192 ? 7.349   19.426  8.460   1.00 28.44 ? 192  ILE B N   1 
ATOM   3458 C CA  . ILE B 1 192 ? 7.250   20.294  9.661   1.00 27.53 ? 192  ILE B CA  1 
ATOM   3459 C C   . ILE B 1 192 ? 8.475   21.203  9.684   1.00 28.53 ? 192  ILE B C   1 
ATOM   3460 O O   . ILE B 1 192 ? 8.296   22.413  9.805   1.00 28.54 ? 192  ILE B O   1 
ATOM   3461 C CB  . ILE B 1 192 ? 7.092   19.477  10.958  1.00 28.31 ? 192  ILE B CB  1 
ATOM   3462 C CG1 . ILE B 1 192 ? 5.662   18.941  11.069  1.00 27.75 ? 192  ILE B CG1 1 
ATOM   3463 C CG2 . ILE B 1 192 ? 7.496   20.314  12.170  1.00 27.70 ? 192  ILE B CG2 1 
ATOM   3464 C CD1 . ILE B 1 192 ? 5.429   17.962  12.199  1.00 29.12 ? 192  ILE B CD1 1 
ATOM   3465 N N   . VAL B 1 193 ? 9.676   20.638  9.588   1.00 28.65 ? 193  VAL B N   1 
ATOM   3466 C CA  . VAL B 1 193 ? 10.929  21.397  9.868   1.00 29.72 ? 193  VAL B CA  1 
ATOM   3467 C C   . VAL B 1 193 ? 11.237  22.296  8.656   1.00 30.25 ? 193  VAL B C   1 
ATOM   3468 O O   . VAL B 1 193 ? 11.736  23.424  8.868   1.00 30.98 ? 193  VAL B O   1 
ATOM   3469 C CB  . VAL B 1 193 ? 12.092  20.451  10.224  1.00 30.12 ? 193  VAL B CB  1 
ATOM   3470 C CG1 . VAL B 1 193 ? 11.764  19.597  11.439  1.00 30.74 ? 193  VAL B CG1 1 
ATOM   3471 C CG2 . VAL B 1 193 ? 12.507  19.590  9.044   1.00 28.27 ? 193  VAL B CG2 1 
ATOM   3472 N N   . GLY B 1 194 ? 10.952  21.816  7.444   1.00 28.27 ? 194  GLY B N   1 
ATOM   3473 C CA  . GLY B 1 194 ? 11.039  22.612  6.202   1.00 31.41 ? 194  GLY B CA  1 
ATOM   3474 C C   . GLY B 1 194 ? 10.143  23.848  6.243   1.00 30.72 ? 194  GLY B C   1 
ATOM   3475 O O   . GLY B 1 194 ? 10.662  24.949  6.021   1.00 29.75 ? 194  GLY B O   1 
ATOM   3476 N N   . LYS B 1 195 ? 8.853   23.698  6.551   1.00 28.70 ? 195  LYS B N   1 
ATOM   3477 C CA  . LYS B 1 195 ? 7.925   24.861  6.631   1.00 30.83 ? 195  LYS B CA  1 
ATOM   3478 C C   . LYS B 1 195 ? 8.407   25.827  7.726   1.00 30.49 ? 195  LYS B C   1 
ATOM   3479 O O   . LYS B 1 195 ? 8.373   27.034  7.491   1.00 28.99 ? 195  LYS B O   1 
ATOM   3480 C CB  . LYS B 1 195 ? 6.479   24.420  6.844   1.00 29.96 ? 195  LYS B CB  1 
ATOM   3481 C CG  . LYS B 1 195 ? 5.447   25.526  6.638   1.00 33.61 ? 195  LYS B CG  1 
ATOM   3482 C CD  . LYS B 1 195 ? 5.387   26.073  5.215   1.00 34.80 ? 195  LYS B CD  1 
ATOM   3483 C CE  . LYS B 1 195 ? 4.226   27.021  4.989   1.00 35.09 ? 195  LYS B CE  1 
ATOM   3484 N NZ  . LYS B 1 195 ? 2.921   26.353  5.208   1.00 37.42 ? 195  LYS B NZ  1 
ATOM   3485 N N   . ALA B 1 196 ? 8.939   25.316  8.838   1.00 30.56 ? 196  ALA B N   1 
ATOM   3486 C CA  . ALA B 1 196 ? 9.461   26.131  9.961   1.00 33.31 ? 196  ALA B CA  1 
ATOM   3487 C C   . ALA B 1 196 ? 10.737  26.866  9.549   1.00 34.18 ? 196  ALA B C   1 
ATOM   3488 O O   . ALA B 1 196 ? 11.240  27.648  10.380  1.00 34.76 ? 196  ALA B O   1 
ATOM   3489 C CB  . ALA B 1 196 ? 9.722   25.262  11.173  1.00 34.44 ? 196  ALA B CB  1 
ATOM   3490 N N   . GLY B 1 197 ? 11.283  26.566  8.364   1.00 34.48 ? 197  GLY B N   1 
ATOM   3491 C CA  . GLY B 1 197 ? 12.473  27.237  7.806   1.00 36.20 ? 197  GLY B CA  1 
ATOM   3492 C C   . GLY B 1 197 ? 13.776  26.556  8.190   1.00 36.97 ? 197  GLY B C   1 
ATOM   3493 O O   . GLY B 1 197 ? 14.830  27.183  8.020   1.00 35.39 ? 197  GLY B O   1 
ATOM   3494 N N   . GLU B 1 198 ? 13.716  25.308  8.669   1.00 36.22 ? 198  GLU B N   1 
ATOM   3495 C CA  . GLU B 1 198 ? 14.910  24.486  8.996   1.00 34.68 ? 198  GLU B CA  1 
ATOM   3496 C C   . GLU B 1 198 ? 15.441  23.834  7.719   1.00 34.46 ? 198  GLU B C   1 
ATOM   3497 O O   . GLU B 1 198 ? 14.669  23.674  6.763   1.00 32.80 ? 198  GLU B O   1 
ATOM   3498 C CB  . GLU B 1 198 ? 14.569  23.384  10.004  1.00 35.34 ? 198  GLU B CB  1 
ATOM   3499 C CG  . GLU B 1 198 ? 14.171  23.910  11.363  1.00 35.55 ? 198  GLU B CG  1 
ATOM   3500 C CD  . GLU B 1 198 ? 15.253  24.752  12.016  1.00 36.54 ? 198  GLU B CD  1 
ATOM   3501 O OE1 . GLU B 1 198 ? 14.901  25.795  12.587  1.00 38.48 ? 198  GLU B OE1 1 
ATOM   3502 O OE2 . GLU B 1 198 ? 16.441  24.351  11.959  1.00 34.63 ? 198  GLU B OE2 1 
ATOM   3503 N N   . ASP B 1 199 ? 16.713  23.451  7.738   1.00 34.13 ? 199  ASP B N   1 
ATOM   3504 C CA  . ASP B 1 199 ? 17.384  22.691  6.655   1.00 35.68 ? 199  ASP B CA  1 
ATOM   3505 C C   . ASP B 1 199 ? 17.073  21.202  6.848   1.00 35.27 ? 199  ASP B C   1 
ATOM   3506 O O   . ASP B 1 199 ? 17.392  20.674  7.935   1.00 34.33 ? 199  ASP B O   1 
ATOM   3507 C CB  . ASP B 1 199 ? 18.897  22.909  6.665   1.00 34.39 ? 199  ASP B CB  1 
ATOM   3508 C CG  . ASP B 1 199 ? 19.572  22.313  5.438   1.00 36.81 ? 199  ASP B CG  1 
ATOM   3509 O OD1 . ASP B 1 199 ? 19.588  23.003  4.385   1.00 35.22 ? 199  ASP B OD1 1 
ATOM   3510 O OD2 . ASP B 1 199 ? 20.032  21.145  5.530   1.00 37.47 ? 199  ASP B OD2 1 
ATOM   3511 N N   . GLU B 1 200 ? 16.492  20.559  5.831   1.00 31.43 ? 200  GLU B N   1 
ATOM   3512 C CA  . GLU B 1 200 ? 16.099  19.125  5.875   1.00 32.01 ? 200  GLU B CA  1 
ATOM   3513 C C   . GLU B 1 200 ? 17.343  18.245  6.069   1.00 31.04 ? 200  GLU B C   1 
ATOM   3514 O O   . GLU B 1 200 ? 17.213  17.213  6.729   1.00 31.59 ? 200  GLU B O   1 
ATOM   3515 C CB  . GLU B 1 200 ? 15.342  18.728  4.610   1.00 28.71 ? 200  GLU B CB  1 
ATOM   3516 C CG  . GLU B 1 200 ? 13.995  19.423  4.463   1.00 29.39 ? 200  GLU B CG  1 
ATOM   3517 C CD  . GLU B 1 200 ? 14.034  20.765  3.736   1.00 28.29 ? 200  GLU B CD  1 
ATOM   3518 O OE1 . GLU B 1 200 ? 12.962  21.234  3.302   1.00 24.18 ? 200  GLU B OE1 1 
ATOM   3519 O OE2 . GLU B 1 200 ? 15.147  21.335  3.605   1.00 29.68 ? 200  GLU B OE2 1 
ATOM   3520 N N   . VAL B 1 201 ? 18.495  18.629  5.512   1.00 31.32 ? 201  VAL B N   1 
ATOM   3521 C CA  . VAL B 1 201 ? 19.734  17.788  5.531   1.00 32.83 ? 201  VAL B CA  1 
ATOM   3522 C C   . VAL B 1 201 ? 20.384  17.922  6.913   1.00 33.60 ? 201  VAL B C   1 
ATOM   3523 O O   . VAL B 1 201 ? 20.777  16.882  7.466   1.00 35.19 ? 201  VAL B O   1 
ATOM   3524 C CB  . VAL B 1 201 ? 20.695  18.120  4.365   1.00 32.51 ? 201  VAL B CB  1 
ATOM   3525 C CG1 . VAL B 1 201 ? 22.138  17.731  4.649   1.00 30.87 ? 201  VAL B CG1 1 
ATOM   3526 C CG2 . VAL B 1 201 ? 20.228  17.475  3.066   1.00 32.06 ? 201  VAL B CG2 1 
ATOM   3527 N N   . ASP B 1 202 ? 20.467  19.138  7.465   1.00 35.33 ? 202  ASP B N   1 
ATOM   3528 C CA  . ASP B 1 202 ? 20.975  19.352  8.848   1.00 34.85 ? 202  ASP B CA  1 
ATOM   3529 C C   . ASP B 1 202 ? 20.039  18.632  9.828   1.00 34.04 ? 202  ASP B C   1 
ATOM   3530 O O   . ASP B 1 202 ? 20.561  17.958  10.763  1.00 31.12 ? 202  ASP B O   1 
ATOM   3531 C CB  . ASP B 1 202 ? 21.128  20.834  9.183   1.00 36.60 ? 202  ASP B CB  1 
ATOM   3532 C CG  . ASP B 1 202 ? 22.099  21.561  8.265   1.00 38.79 ? 202  ASP B CG  1 
ATOM   3533 O OD1 . ASP B 1 202 ? 22.994  20.898  7.728   1.00 42.28 ? 202  ASP B OD1 1 
ATOM   3534 O OD2 . ASP B 1 202 ? 21.946  22.776  8.094   1.00 41.22 ? 202  ASP B OD2 1 
ATOM   3535 N N   . PHE B 1 203 ? 18.717  18.721  9.623   1.00 32.99 ? 203  PHE B N   1 
ATOM   3536 C CA  . PHE B 1 203 ? 17.731  18.007  10.484  1.00 31.12 ? 203  PHE B CA  1 
ATOM   3537 C C   . PHE B 1 203 ? 18.050  16.501  10.474  1.00 32.91 ? 203  PHE B C   1 
ATOM   3538 O O   . PHE B 1 203 ? 18.134  15.912  11.576  1.00 33.78 ? 203  PHE B O   1 
ATOM   3539 C CB  . PHE B 1 203 ? 16.283  18.275  10.069  1.00 32.26 ? 203  PHE B CB  1 
ATOM   3540 C CG  . PHE B 1 203 ? 15.305  17.362  10.763  1.00 28.86 ? 203  PHE B CG  1 
ATOM   3541 C CD1 . PHE B 1 203 ? 15.004  17.537  12.115  1.00 27.79 ? 203  PHE B CD1 1 
ATOM   3542 C CD2 . PHE B 1 203 ? 14.750  16.285  10.091  1.00 27.18 ? 203  PHE B CD2 1 
ATOM   3543 C CE1 . PHE B 1 203 ? 14.153  16.656  12.767  1.00 27.51 ? 203  PHE B CE1 1 
ATOM   3544 C CE2 . PHE B 1 203 ? 13.879  15.418  10.741  1.00 27.62 ? 203  PHE B CE2 1 
ATOM   3545 C CZ  . PHE B 1 203 ? 13.589  15.600  12.078  1.00 26.44 ? 203  PHE B CZ  1 
ATOM   3546 N N   . ALA B 1 204 ? 18.226  15.903  9.284   1.00 32.46 ? 204  ALA B N   1 
ATOM   3547 C CA  . ALA B 1 204 ? 18.514  14.460  9.085   1.00 34.55 ? 204  ALA B CA  1 
ATOM   3548 C C   . ALA B 1 204 ? 19.773  14.037  9.852   1.00 34.98 ? 204  ALA B C   1 
ATOM   3549 O O   . ALA B 1 204 ? 19.758  12.943  10.434  1.00 35.94 ? 204  ALA B O   1 
ATOM   3550 C CB  . ALA B 1 204 ? 18.637  14.139  7.621   1.00 35.21 ? 204  ALA B CB  1 
ATOM   3551 N N   . ALA B 1 205 ? 20.825  14.860  9.844   1.00 35.45 ? 205  ALA B N   1 
ATOM   3552 C CA  . ALA B 1 205 ? 22.076  14.627  10.610  1.00 35.89 ? 205  ALA B CA  1 
ATOM   3553 C C   . ALA B 1 205 ? 21.746  14.549  12.099  1.00 37.67 ? 205  ALA B C   1 
ATOM   3554 O O   . ALA B 1 205 ? 22.249  13.632  12.771  1.00 39.91 ? 205  ALA B O   1 
ATOM   3555 C CB  . ALA B 1 205 ? 23.087  15.727  10.360  1.00 33.37 ? 205  ALA B CB  1 
ATOM   3556 N N   . LEU B 1 206 ? 20.963  15.518  12.587  1.00 39.65 ? 206  LEU B N   1 
ATOM   3557 C CA  . LEU B 1 206 ? 20.518  15.610  14.002  1.00 38.13 ? 206  LEU B CA  1 
ATOM   3558 C C   . LEU B 1 206 ? 19.643  14.402  14.354  1.00 35.00 ? 206  LEU B C   1 
ATOM   3559 O O   . LEU B 1 206 ? 19.782  13.880  15.467  1.00 34.86 ? 206  LEU B O   1 
ATOM   3560 C CB  . LEU B 1 206 ? 19.747  16.917  14.195  1.00 40.01 ? 206  LEU B CB  1 
ATOM   3561 C CG  . LEU B 1 206 ? 19.281  17.207  15.623  1.00 41.70 ? 206  LEU B CG  1 
ATOM   3562 C CD1 . LEU B 1 206 ? 19.216  18.715  15.855  1.00 41.98 ? 206  LEU B CD1 1 
ATOM   3563 C CD2 . LEU B 1 206 ? 17.935  16.542  15.920  1.00 41.34 ? 206  LEU B CD2 1 
ATOM   3564 N N   . ALA B 1 207 ? 18.758  13.996  13.447  1.00 33.85 ? 207  ALA B N   1 
ATOM   3565 C CA  . ALA B 1 207 ? 17.764  12.920  13.663  1.00 32.92 ? 207  ALA B CA  1 
ATOM   3566 C C   . ALA B 1 207 ? 18.426  11.539  13.693  1.00 33.97 ? 207  ALA B C   1 
ATOM   3567 O O   . ALA B 1 207 ? 17.867  10.630  14.363  1.00 29.20 ? 207  ALA B O   1 
ATOM   3568 C CB  . ALA B 1 207 ? 16.722  12.970  12.577  1.00 35.13 ? 207  ALA B CB  1 
ATOM   3569 N N   . SER B 1 208 ? 19.535  11.363  12.961  1.00 36.55 ? 208  SER B N   1 
ATOM   3570 C CA  . SER B 1 208 ? 20.126  10.033  12.647  1.00 36.08 ? 208  SER B CA  1 
ATOM   3571 C C   . SER B 1 208 ? 20.306  9.237   13.928  1.00 34.10 ? 208  SER B C   1 
ATOM   3572 O O   . SER B 1 208 ? 19.759  8.147   14.036  1.00 34.98 ? 208  SER B O   1 
ATOM   3573 C CB  . SER B 1 208 ? 21.426  10.131  11.870  1.00 41.86 ? 208  SER B CB  1 
ATOM   3574 O OG  . SER B 1 208 ? 21.420  9.234   10.769  1.00 44.92 ? 208  SER B OG  1 
ATOM   3575 N N   . PRO B 1 209 ? 21.069  9.732   14.932  1.00 37.78 ? 209  PRO B N   1 
ATOM   3576 C CA  . PRO B 1 209 ? 21.255  8.983   16.174  1.00 39.27 ? 209  PRO B CA  1 
ATOM   3577 C C   . PRO B 1 209 ? 19.926  8.527   16.794  1.00 37.22 ? 209  PRO B C   1 
ATOM   3578 O O   . PRO B 1 209 ? 19.888  7.423   17.282  1.00 35.64 ? 209  PRO B O   1 
ATOM   3579 C CB  . PRO B 1 209 ? 21.962  9.956   17.135  1.00 40.95 ? 209  PRO B CB  1 
ATOM   3580 C CG  . PRO B 1 209 ? 22.577  11.020  16.236  1.00 42.11 ? 209  PRO B CG  1 
ATOM   3581 C CD  . PRO B 1 209 ? 21.798  11.013  14.937  1.00 38.81 ? 209  PRO B CD  1 
ATOM   3582 N N   . PHE B 1 210 ? 18.888  9.381   16.748  1.00 36.01 ? 210  PHE B N   1 
ATOM   3583 C CA  . PHE B 1 210 ? 17.564  9.153   17.396  1.00 34.44 ? 210  PHE B CA  1 
ATOM   3584 C C   . PHE B 1 210 ? 16.818  8.046   16.650  1.00 33.06 ? 210  PHE B C   1 
ATOM   3585 O O   . PHE B 1 210 ? 16.208  7.183   17.310  1.00 29.76 ? 210  PHE B O   1 
ATOM   3586 C CB  . PHE B 1 210 ? 16.745  10.445  17.464  1.00 33.94 ? 210  PHE B CB  1 
ATOM   3587 C CG  . PHE B 1 210 ? 17.382  11.522  18.306  1.00 32.25 ? 210  PHE B CG  1 
ATOM   3588 C CD1 . PHE B 1 210 ? 17.308  11.475  19.695  1.00 32.09 ? 210  PHE B CD1 1 
ATOM   3589 C CD2 . PHE B 1 210 ? 18.106  12.543  17.714  1.00 31.75 ? 210  PHE B CD2 1 
ATOM   3590 C CE1 . PHE B 1 210 ? 17.893  12.464  20.470  1.00 33.03 ? 210  PHE B CE1 1 
ATOM   3591 C CE2 . PHE B 1 210 ? 18.699  13.528  18.490  1.00 31.76 ? 210  PHE B CE2 1 
ATOM   3592 C CZ  . PHE B 1 210 ? 18.589  13.488  19.865  1.00 32.48 ? 210  PHE B CZ  1 
ATOM   3593 N N   . VAL B 1 211 ? 16.891  8.045   15.320  1.00 32.26 ? 211  VAL B N   1 
ATOM   3594 C CA  . VAL B 1 211 ? 16.185  7.026   14.492  1.00 33.89 ? 211  VAL B CA  1 
ATOM   3595 C C   . VAL B 1 211 ? 16.855  5.661   14.711  1.00 36.49 ? 211  VAL B C   1 
ATOM   3596 O O   . VAL B 1 211 ? 16.118  4.653   14.791  1.00 32.90 ? 211  VAL B O   1 
ATOM   3597 C CB  . VAL B 1 211 ? 16.155  7.394   13.004  1.00 33.71 ? 211  VAL B CB  1 
ATOM   3598 C CG1 . VAL B 1 211 ? 15.461  6.300   12.209  1.00 36.03 ? 211  VAL B CG1 1 
ATOM   3599 C CG2 . VAL B 1 211 ? 15.500  8.749   12.766  1.00 35.15 ? 211  VAL B CG2 1 
ATOM   3600 N N   . LYS B 1 212 ? 18.193  5.628   14.794  1.00 37.27 ? 212  LYS B N   1 
ATOM   3601 C CA  . LYS B 1 212 ? 18.962  4.377   15.063  1.00 43.24 ? 212  LYS B CA  1 
ATOM   3602 C C   . LYS B 1 212 ? 18.557  3.826   16.437  1.00 40.08 ? 212  LYS B C   1 
ATOM   3603 O O   . LYS B 1 212 ? 18.369  2.611   16.529  1.00 40.06 ? 212  LYS B O   1 
ATOM   3604 C CB  . LYS B 1 212 ? 20.481  4.588   14.968  1.00 43.72 ? 212  LYS B CB  1 
ATOM   3605 C CG  . LYS B 1 212 ? 21.026  4.914   13.577  1.00 48.32 ? 212  LYS B CG  1 
ATOM   3606 C CD  . LYS B 1 212 ? 20.221  4.317   12.419  1.00 53.59 ? 212  LYS B CD  1 
ATOM   3607 C CE  . LYS B 1 212 ? 20.995  4.174   11.119  1.00 57.50 ? 212  LYS B CE  1 
ATOM   3608 N NZ  . LYS B 1 212 ? 21.246  2.748   10.774  1.00 61.25 ? 212  LYS B NZ  1 
ATOM   3609 N N   . SER B 1 213 ? 18.410  4.688   17.446  1.00 38.11 ? 213  SER B N   1 
ATOM   3610 C CA  . SER B 1 213 ? 17.870  4.341   18.790  1.00 42.69 ? 213  SER B CA  1 
ATOM   3611 C C   . SER B 1 213 ? 16.466  3.724   18.698  1.00 39.56 ? 213  SER B C   1 
ATOM   3612 O O   . SER B 1 213 ? 16.246  2.698   19.335  1.00 38.96 ? 213  SER B O   1 
ATOM   3613 C CB  . SER B 1 213 ? 17.877  5.537   19.698  1.00 42.14 ? 213  SER B CB  1 
ATOM   3614 O OG  . SER B 1 213 ? 19.204  5.828   20.087  1.00 45.07 ? 213  SER B OG  1 
ATOM   3615 N N   . MET B 1 214 ? 15.542  4.316   17.940  1.00 40.09 ? 214  MET B N   1 
ATOM   3616 C CA  . MET B 1 214 ? 14.177  3.742   17.740  1.00 40.61 ? 214  MET B CA  1 
ATOM   3617 C C   . MET B 1 214 ? 14.329  2.335   17.150  1.00 36.47 ? 214  MET B C   1 
ATOM   3618 O O   . MET B 1 214 ? 13.690  1.413   17.663  1.00 35.21 ? 214  MET B O   1 
ATOM   3619 C CB  . MET B 1 214 ? 13.297  4.581   16.801  1.00 40.43 ? 214  MET B CB  1 
ATOM   3620 C CG  . MET B 1 214 ? 12.911  5.956   17.342  1.00 41.12 ? 214  MET B CG  1 
ATOM   3621 S SD  . MET B 1 214 ? 12.381  7.111   16.020  1.00 40.39 ? 214  MET B SD  1 
ATOM   3622 C CE  . MET B 1 214 ? 12.692  8.695   16.808  1.00 37.80 ? 214  MET B CE  1 
ATOM   3623 N N   . ALA B 1 215 ? 15.141  2.186   16.105  1.00 35.96 ? 215  ALA B N   1 
ATOM   3624 C CA  . ALA B 1 215 ? 15.424  0.883   15.457  1.00 37.38 ? 215  ALA B CA  1 
ATOM   3625 C C   . ALA B 1 215 ? 15.752  -0.161  16.531  1.00 36.01 ? 215  ALA B C   1 
ATOM   3626 O O   . ALA B 1 215 ? 15.168  -1.259  16.458  1.00 33.05 ? 215  ALA B O   1 
ATOM   3627 C CB  . ALA B 1 215 ? 16.547  1.022   14.455  1.00 38.51 ? 215  ALA B CB  1 
ATOM   3628 N N   . ASP B 1 216 ? 16.624  0.192   17.490  1.00 35.89 ? 216  ASP B N   1 
ATOM   3629 C CA  . ASP B 1 216 ? 17.124  -0.691  18.588  1.00 37.76 ? 216  ASP B CA  1 
ATOM   3630 C C   . ASP B 1 216 ? 15.985  -1.076  19.538  1.00 34.36 ? 216  ASP B C   1 
ATOM   3631 O O   . ASP B 1 216 ? 16.039  -2.181  20.082  1.00 31.44 ? 216  ASP B O   1 
ATOM   3632 C CB  . ASP B 1 216 ? 18.187  -0.025  19.481  1.00 40.66 ? 216  ASP B CB  1 
ATOM   3633 C CG  . ASP B 1 216 ? 19.538  0.277   18.846  1.00 43.46 ? 216  ASP B CG  1 
ATOM   3634 O OD1 . ASP B 1 216 ? 19.867  -0.347  17.800  1.00 42.44 ? 216  ASP B OD1 1 
ATOM   3635 O OD2 . ASP B 1 216 ? 20.258  1.147   19.412  1.00 45.55 ? 216  ASP B OD2 1 
ATOM   3636 N N   . TRP B 1 217 ? 15.006  -0.193  19.757  1.00 36.15 ? 217  TRP B N   1 
ATOM   3637 C CA  . TRP B 1 217 ? 13.877  -0.452  20.694  1.00 37.63 ? 217  TRP B CA  1 
ATOM   3638 C C   . TRP B 1 217 ? 12.950  -1.550  20.146  1.00 33.38 ? 217  TRP B C   1 
ATOM   3639 O O   . TRP B 1 217 ? 12.277  -2.170  20.955  1.00 34.40 ? 217  TRP B O   1 
ATOM   3640 C CB  . TRP B 1 217 ? 13.085  0.823   21.008  1.00 40.09 ? 217  TRP B CB  1 
ATOM   3641 C CG  . TRP B 1 217 ? 13.854  1.909   21.697  1.00 45.23 ? 217  TRP B CG  1 
ATOM   3642 C CD1 . TRP B 1 217 ? 14.991  1.795   22.449  1.00 48.94 ? 217  TRP B CD1 1 
ATOM   3643 C CD2 . TRP B 1 217 ? 13.506  3.309   21.714  1.00 47.44 ? 217  TRP B CD2 1 
ATOM   3644 N NE1 . TRP B 1 217 ? 15.390  3.026   22.909  1.00 50.15 ? 217  TRP B NE1 1 
ATOM   3645 C CE2 . TRP B 1 217 ? 14.497  3.975   22.474  1.00 50.40 ? 217  TRP B CE2 1 
ATOM   3646 C CE3 . TRP B 1 217 ? 12.460  4.057   21.155  1.00 49.66 ? 217  TRP B CE3 1 
ATOM   3647 C CZ2 . TRP B 1 217 ? 14.466  5.354   22.685  1.00 51.89 ? 217  TRP B CZ2 1 
ATOM   3648 C CZ3 . TRP B 1 217 ? 12.432  5.421   21.362  1.00 52.40 ? 217  TRP B CZ3 1 
ATOM   3649 C CH2 . TRP B 1 217 ? 13.419  6.057   22.123  1.00 53.48 ? 217  TRP B CH2 1 
ATOM   3650 N N   . LEU B 1 218 ? 12.923  -1.796  18.833  1.00 34.60 ? 218  LEU B N   1 
ATOM   3651 C CA  . LEU B 1 218 ? 11.860  -2.615  18.169  1.00 32.56 ? 218  LEU B CA  1 
ATOM   3652 C C   . LEU B 1 218 ? 11.918  -4.079  18.610  1.00 32.55 ? 218  LEU B C   1 
ATOM   3653 O O   . LEU B 1 218 ? 10.873  -4.662  18.867  1.00 34.38 ? 218  LEU B O   1 
ATOM   3654 C CB  . LEU B 1 218 ? 11.952  -2.489  16.642  1.00 30.99 ? 218  LEU B CB  1 
ATOM   3655 C CG  . LEU B 1 218 ? 11.852  -1.069  16.079  1.00 31.53 ? 218  LEU B CG  1 
ATOM   3656 C CD1 . LEU B 1 218 ? 11.684  -1.105  14.567  1.00 33.97 ? 218  LEU B CD1 1 
ATOM   3657 C CD2 . LEU B 1 218 ? 10.710  -0.281  16.719  1.00 30.75 ? 218  LEU B CD2 1 
ATOM   3658 N N   . PRO B 1 219 ? 13.092  -4.754  18.698  1.00 36.38 ? 219  PRO B N   1 
ATOM   3659 C CA  . PRO B 1 219 ? 13.140  -6.137  19.189  1.00 32.86 ? 219  PRO B CA  1 
ATOM   3660 C C   . PRO B 1 219 ? 12.573  -6.349  20.606  1.00 30.58 ? 219  PRO B C   1 
ATOM   3661 O O   . PRO B 1 219 ? 11.871  -7.335  20.837  1.00 29.80 ? 219  PRO B O   1 
ATOM   3662 C CB  . PRO B 1 219 ? 14.631  -6.493  19.120  1.00 35.57 ? 219  PRO B CB  1 
ATOM   3663 C CG  . PRO B 1 219 ? 15.173  -5.582  18.037  1.00 35.93 ? 219  PRO B CG  1 
ATOM   3664 C CD  . PRO B 1 219 ? 14.409  -4.284  18.231  1.00 37.89 ? 219  PRO B CD  1 
ATOM   3665 N N   . ARG B 1 220 ? 12.821  -5.412  21.512  1.00 29.18 ? 220  ARG B N   1 
ATOM   3666 C CA  . ARG B 1 220 ? 12.201  -5.427  22.854  1.00 31.71 ? 220  ARG B CA  1 
ATOM   3667 C C   . ARG B 1 220 ? 10.668  -5.404  22.696  1.00 32.51 ? 220  ARG B C   1 
ATOM   3668 O O   . ARG B 1 220 ? 9.979   -6.270  23.302  1.00 30.99 ? 220  ARG B O   1 
ATOM   3669 C CB  . ARG B 1 220 ? 12.684  -4.233  23.675  1.00 38.36 ? 220  ARG B CB  1 
ATOM   3670 C CG  . ARG B 1 220 ? 12.503  -4.415  25.175  1.00 44.20 ? 220  ARG B CG  1 
ATOM   3671 C CD  . ARG B 1 220 ? 12.509  -3.088  25.913  1.00 51.98 ? 220  ARG B CD  1 
ATOM   3672 N NE  . ARG B 1 220 ? 13.306  -2.109  25.188  1.00 56.94 ? 220  ARG B NE  1 
ATOM   3673 C CZ  . ARG B 1 220 ? 14.633  -2.097  25.133  1.00 60.47 ? 220  ARG B CZ  1 
ATOM   3674 N NH1 . ARG B 1 220 ? 15.345  -3.006  25.783  1.00 68.44 ? 220  ARG B NH1 1 
ATOM   3675 N NH2 . ARG B 1 220 ? 15.244  -1.167  24.423  1.00 63.84 ? 220  ARG B NH2 1 
ATOM   3676 N N   . ILE B 1 221 ? 10.126  -4.479  21.895  1.00 28.33 ? 221  ILE B N   1 
ATOM   3677 C CA  . ILE B 1 221 ? 8.649   -4.366  21.730  1.00 25.52 ? 221  ILE B CA  1 
ATOM   3678 C C   . ILE B 1 221 ? 8.100   -5.702  21.202  1.00 25.02 ? 221  ILE B C   1 
ATOM   3679 O O   . ILE B 1 221 ? 7.031   -6.108  21.664  1.00 24.41 ? 221  ILE B O   1 
ATOM   3680 C CB  . ILE B 1 221 ? 8.264   -3.168  20.850  1.00 25.91 ? 221  ILE B CB  1 
ATOM   3681 C CG1 . ILE B 1 221 ? 8.647   -1.844  21.520  1.00 26.58 ? 221  ILE B CG1 1 
ATOM   3682 C CG2 . ILE B 1 221 ? 6.781   -3.210  20.491  1.00 25.84 ? 221  ILE B CG2 1 
ATOM   3683 C CD1 . ILE B 1 221 ? 8.773   -0.694  20.554  1.00 27.86 ? 221  ILE B CD1 1 
ATOM   3684 N N   . ALA B 1 222 ? 8.792   -6.360  20.272  1.00 24.74 ? 222  ALA B N   1 
ATOM   3685 C CA  . ALA B 1 222 ? 8.416   -7.693  19.729  1.00 24.83 ? 222  ALA B CA  1 
ATOM   3686 C C   . ALA B 1 222 ? 8.285   -8.732  20.848  1.00 27.36 ? 222  ALA B C   1 
ATOM   3687 O O   . ALA B 1 222 ? 7.337   -9.532  20.798  1.00 28.12 ? 222  ALA B O   1 
ATOM   3688 C CB  . ALA B 1 222 ? 9.424   -8.147  18.705  1.00 25.33 ? 222  ALA B CB  1 
ATOM   3689 N N   . GLY B 1 223 ? 9.232   -8.754  21.797  1.00 30.19 ? 223  GLY B N   1 
ATOM   3690 C CA  . GLY B 1 223 ? 9.159   -9.606  23.007  1.00 28.86 ? 223  GLY B CA  1 
ATOM   3691 C C   . GLY B 1 223 ? 7.936   -9.270  23.840  1.00 27.90 ? 223  GLY B C   1 
ATOM   3692 O O   . GLY B 1 223 ? 7.175   -10.192 24.186  1.00 30.17 ? 223  GLY B O   1 
ATOM   3693 N N   . HIS B 1 224 ? 7.699   -7.985  24.104  1.00 27.97 ? 224  HIS B N   1 
ATOM   3694 C CA  . HIS B 1 224 ? 6.470   -7.519  24.809  1.00 29.38 ? 224  HIS B CA  1 
ATOM   3695 C C   . HIS B 1 224 ? 5.231   -8.074  24.107  1.00 28.32 ? 224  HIS B C   1 
ATOM   3696 O O   . HIS B 1 224 ? 4.343   -8.601  24.798  1.00 26.50 ? 224  HIS B O   1 
ATOM   3697 C CB  . HIS B 1 224 ? 6.422   -5.991  24.919  1.00 30.49 ? 224  HIS B CB  1 
ATOM   3698 C CG  . HIS B 1 224 ? 7.561   -5.450  25.709  1.00 30.65 ? 224  HIS B CG  1 
ATOM   3699 N ND1 . HIS B 1 224 ? 7.965   -4.133  25.615  1.00 33.10 ? 224  HIS B ND1 1 
ATOM   3700 C CD2 . HIS B 1 224 ? 8.383   -6.051  26.597  1.00 32.30 ? 224  HIS B CD2 1 
ATOM   3701 C CE1 . HIS B 1 224 ? 8.995   -3.942  26.421  1.00 33.66 ? 224  HIS B CE1 1 
ATOM   3702 N NE2 . HIS B 1 224 ? 9.268   -5.109  27.037  1.00 31.71 ? 224  HIS B NE2 1 
ATOM   3703 N N   . VAL B 1 225 ? 5.158   -7.956  22.784  1.00 27.44 ? 225  VAL B N   1 
ATOM   3704 C CA  . VAL B 1 225 ? 3.992   -8.483  22.023  1.00 26.84 ? 225  VAL B CA  1 
ATOM   3705 C C   . VAL B 1 225 ? 3.932   -9.995  22.230  1.00 28.10 ? 225  VAL B C   1 
ATOM   3706 O O   . VAL B 1 225 ? 2.825   -10.465 22.587  1.00 26.15 ? 225  VAL B O   1 
ATOM   3707 C CB  . VAL B 1 225 ? 4.030   -8.102  20.533  1.00 27.90 ? 225  VAL B CB  1 
ATOM   3708 C CG1 . VAL B 1 225 ? 2.982   -8.859  19.723  1.00 26.62 ? 225  VAL B CG1 1 
ATOM   3709 C CG2 . VAL B 1 225 ? 3.882   -6.599  20.370  1.00 26.26 ? 225  VAL B CG2 1 
ATOM   3710 N N   . ARG B 1 226 ? 5.046   -10.734 22.065  1.00 29.88 ? 226  ARG B N   1 
ATOM   3711 C CA  . ARG B 1 226 ? 4.978   -12.224 22.199  1.00 32.84 ? 226  ARG B CA  1 
ATOM   3712 C C   . ARG B 1 226 ? 4.562   -12.583 23.640  1.00 32.75 ? 226  ARG B C   1 
ATOM   3713 O O   . ARG B 1 226 ? 3.635   -13.399 23.791  1.00 30.57 ? 226  ARG B O   1 
ATOM   3714 C CB  . ARG B 1 226 ? 6.270   -12.944 21.784  1.00 34.59 ? 226  ARG B CB  1 
ATOM   3715 C CG  . ARG B 1 226 ? 6.090   -14.455 21.651  1.00 35.00 ? 226  ARG B CG  1 
ATOM   3716 C CD  . ARG B 1 226 ? 7.361   -15.270 21.485  1.00 39.04 ? 226  ARG B CD  1 
ATOM   3717 N NE  . ARG B 1 226 ? 8.350   -14.923 22.498  1.00 42.13 ? 226  ARG B NE  1 
ATOM   3718 C CZ  . ARG B 1 226 ? 9.657   -15.148 22.419  1.00 41.92 ? 226  ARG B CZ  1 
ATOM   3719 N NH1 . ARG B 1 226 ? 10.187  -15.765 21.372  1.00 43.33 ? 226  ARG B NH1 1 
ATOM   3720 N NH2 . ARG B 1 226 ? 10.434  -14.755 23.413  1.00 45.37 ? 226  ARG B NH2 1 
ATOM   3721 N N   . GLU B 1 227 ? 5.195   -11.964 24.648  1.00 34.38 ? 227  GLU B N   1 
ATOM   3722 C CA  . GLU B 1 227 ? 4.937   -12.223 26.095  1.00 36.45 ? 227  GLU B CA  1 
ATOM   3723 C C   . GLU B 1 227 ? 3.652   -11.526 26.591  1.00 36.22 ? 227  GLU B C   1 
ATOM   3724 O O   . GLU B 1 227 ? 3.328   -11.699 27.780  1.00 38.72 ? 227  GLU B O   1 
ATOM   3725 C CB  . GLU B 1 227 ? 6.126   -11.760 26.956  1.00 38.80 ? 227  GLU B CB  1 
ATOM   3726 C CG  . GLU B 1 227 ? 7.475   -12.368 26.595  1.00 40.63 ? 227  GLU B CG  1 
ATOM   3727 C CD  . GLU B 1 227 ? 7.437   -13.818 26.151  1.00 43.22 ? 227  GLU B CD  1 
ATOM   3728 O OE1 . GLU B 1 227 ? 8.250   -14.188 25.299  1.00 48.09 ? 227  GLU B OE1 1 
ATOM   3729 O OE2 . GLU B 1 227 ? 6.585   -14.563 26.652  1.00 43.48 ? 227  GLU B OE2 1 
ATOM   3730 N N   . LYS B 1 228 ? 2.961   -10.741 25.762  1.00 34.51 ? 228  LYS B N   1 
ATOM   3731 C CA  . LYS B 1 228 ? 1.735   -9.992  26.154  1.00 33.70 ? 228  LYS B CA  1 
ATOM   3732 C C   . LYS B 1 228 ? 2.011   -9.093  27.373  1.00 31.57 ? 228  LYS B C   1 
ATOM   3733 O O   . LYS B 1 228 ? 1.096   -8.911  28.195  1.00 33.54 ? 228  LYS B O   1 
ATOM   3734 C CB  . LYS B 1 228 ? 0.611   -11.007 26.403  1.00 36.96 ? 228  LYS B CB  1 
ATOM   3735 C CG  . LYS B 1 228 ? -0.412  -11.111 25.281  1.00 40.60 ? 228  LYS B CG  1 
ATOM   3736 C CD  . LYS B 1 228 ? -0.978  -12.483 25.082  1.00 41.68 ? 228  LYS B CD  1 
ATOM   3737 C CE  . LYS B 1 228 ? -0.022  -13.414 24.367  1.00 46.17 ? 228  LYS B CE  1 
ATOM   3738 N NZ  . LYS B 1 228 ? -0.758  -14.318 23.454  1.00 45.32 ? 228  LYS B NZ  1 
ATOM   3739 N N   . GLN B 1 229 ? 3.224   -8.546  27.479  1.00 29.28 ? 229  GLN B N   1 
ATOM   3740 C CA  . GLN B 1 229 ? 3.687   -7.615  28.542  1.00 29.26 ? 229  GLN B CA  1 
ATOM   3741 C C   . GLN B 1 229 ? 3.446   -6.168  28.085  1.00 29.79 ? 229  GLN B C   1 
ATOM   3742 O O   . GLN B 1 229 ? 4.215   -5.689  27.241  1.00 30.50 ? 229  GLN B O   1 
ATOM   3743 C CB  . GLN B 1 229 ? 5.173   -7.871  28.836  1.00 28.73 ? 229  GLN B CB  1 
ATOM   3744 C CG  . GLN B 1 229 ? 5.454   -9.280  29.363  1.00 27.43 ? 229  GLN B CG  1 
ATOM   3745 C CD  . GLN B 1 229 ? 4.609   -9.550  30.587  1.00 28.47 ? 229  GLN B CD  1 
ATOM   3746 O OE1 . GLN B 1 229 ? 3.631   -10.310 30.557  1.00 28.05 ? 229  GLN B OE1 1 
ATOM   3747 N NE2 . GLN B 1 229 ? 4.948   -8.862  31.659  1.00 24.91 ? 229  GLN B NE2 1 
ATOM   3748 N N   . TYR B 1 230 ? 2.423   -5.492  28.619  1.00 27.72 ? 230  TYR B N   1 
ATOM   3749 C CA  . TYR B 1 230 ? 1.979   -4.159  28.132  1.00 28.23 ? 230  TYR B CA  1 
ATOM   3750 C C   . TYR B 1 230 ? 2.261   -3.061  29.159  1.00 28.38 ? 230  TYR B C   1 
ATOM   3751 O O   . TYR B 1 230 ? 1.749   -1.944  28.977  1.00 26.27 ? 230  TYR B O   1 
ATOM   3752 C CB  . TYR B 1 230 ? 0.495   -4.189  27.772  1.00 27.27 ? 230  TYR B CB  1 
ATOM   3753 C CG  . TYR B 1 230 ? 0.121   -5.306  26.838  1.00 29.36 ? 230  TYR B CG  1 
ATOM   3754 C CD1 . TYR B 1 230 ? 0.744   -5.453  25.610  1.00 29.64 ? 230  TYR B CD1 1 
ATOM   3755 C CD2 . TYR B 1 230 ? -0.849  -6.234  27.185  1.00 32.69 ? 230  TYR B CD2 1 
ATOM   3756 C CE1 . TYR B 1 230 ? 0.381   -6.463  24.732  1.00 28.99 ? 230  TYR B CE1 1 
ATOM   3757 C CE2 . TYR B 1 230 ? -1.214  -7.261  26.327  1.00 31.45 ? 230  TYR B CE2 1 
ATOM   3758 C CZ  . TYR B 1 230 ? -0.601  -7.372  25.090  1.00 31.62 ? 230  TYR B CZ  1 
ATOM   3759 O OH  . TYR B 1 230 ? -0.943  -8.397  24.255  1.00 30.33 ? 230  TYR B OH  1 
ATOM   3760 N N   . VAL B 1 231 ? 3.047   -3.341  30.200  1.00 27.89 ? 231  VAL B N   1 
ATOM   3761 C CA  . VAL B 1 231 ? 3.289   -2.331  31.270  1.00 29.81 ? 231  VAL B CA  1 
ATOM   3762 C C   . VAL B 1 231 ? 4.697   -1.758  31.082  1.00 29.62 ? 231  VAL B C   1 
ATOM   3763 O O   . VAL B 1 231 ? 5.643   -2.537  31.014  1.00 28.31 ? 231  VAL B O   1 
ATOM   3764 C CB  . VAL B 1 231 ? 3.064   -2.897  32.686  1.00 29.64 ? 231  VAL B CB  1 
ATOM   3765 C CG1 . VAL B 1 231 ? 3.363   -1.851  33.764  1.00 30.37 ? 231  VAL B CG1 1 
ATOM   3766 C CG2 . VAL B 1 231 ? 1.643   -3.416  32.820  1.00 29.19 ? 231  VAL B CG2 1 
ATOM   3767 N N   . GLY B 1 232 ? 4.806   -0.431  30.976  1.00 28.31 ? 232  GLY B N   1 
ATOM   3768 C CA  . GLY B 1 232 ? 6.100   0.270   30.928  1.00 26.59 ? 232  GLY B CA  1 
ATOM   3769 C C   . GLY B 1 232 ? 5.933   1.689   31.410  1.00 26.44 ? 232  GLY B C   1 
ATOM   3770 O O   . GLY B 1 232 ? 4.929   1.968   32.094  1.00 28.87 ? 232  GLY B O   1 
ATOM   3771 N N   . GLY B 1 233 ? 6.841   2.576   31.019  1.00 24.35 ? 233  GLY B N   1 
ATOM   3772 C CA  . GLY B 1 233 ? 6.845   3.974   31.488  1.00 25.67 ? 233  GLY B CA  1 
ATOM   3773 C C   . GLY B 1 233 ? 6.443   4.959   30.402  1.00 24.24 ? 233  GLY B C   1 
ATOM   3774 O O   . GLY B 1 233 ? 6.708   6.146   30.627  1.00 23.50 ? 233  GLY B O   1 
ATOM   3775 N N   . SER B 1 234 ? 5.812   4.482   29.306  1.00 22.25 ? 234  SER B N   1 
ATOM   3776 C CA  . SER B 1 234 ? 5.468   5.259   28.090  1.00 22.26 ? 234  SER B CA  1 
ATOM   3777 C C   . SER B 1 234 ? 4.064   4.906   27.603  1.00 22.38 ? 234  SER B C   1 
ATOM   3778 O O   . SER B 1 234 ? 3.897   4.352   26.514  1.00 21.45 ? 234  SER B O   1 
ATOM   3779 C CB  . SER B 1 234 ? 6.499   5.025   27.024  1.00 22.82 ? 234  SER B CB  1 
ATOM   3780 O OG  . SER B 1 234 ? 7.774   5.373   27.519  1.00 23.88 ? 234  SER B OG  1 
ATOM   3781 N N   . PRO B 1 235 ? 3.029   5.211   28.411  1.00 22.57 ? 235  PRO B N   1 
ATOM   3782 C CA  . PRO B 1 235 ? 1.670   4.756   28.123  1.00 23.46 ? 235  PRO B CA  1 
ATOM   3783 C C   . PRO B 1 235 ? 1.080   5.436   26.874  1.00 23.88 ? 235  PRO B C   1 
ATOM   3784 O O   . PRO B 1 235 ? 1.492   6.545   26.529  1.00 22.57 ? 235  PRO B O   1 
ATOM   3785 C CB  . PRO B 1 235 ? 0.889   5.093   29.400  1.00 22.89 ? 235  PRO B CB  1 
ATOM   3786 C CG  . PRO B 1 235 ? 1.667   6.203   30.064  1.00 24.89 ? 235  PRO B CG  1 
ATOM   3787 C CD  . PRO B 1 235 ? 3.110   6.054   29.612  1.00 23.22 ? 235  PRO B CD  1 
ATOM   3788 N N   . LEU B 1 236 ? 0.104   4.769   26.245  1.00 24.67 ? 236  LEU B N   1 
ATOM   3789 C CA  . LEU B 1 236 ? -0.606  5.257   25.025  1.00 24.01 ? 236  LEU B CA  1 
ATOM   3790 C C   . LEU B 1 236 ? -1.259  6.622   25.276  1.00 23.72 ? 236  LEU B C   1 
ATOM   3791 O O   . LEU B 1 236 ? -1.285  7.416   24.318  1.00 24.36 ? 236  LEU B O   1 
ATOM   3792 C CB  . LEU B 1 236 ? -1.664  4.247   24.570  1.00 23.89 ? 236  LEU B CB  1 
ATOM   3793 C CG  . LEU B 1 236 ? -1.135  2.896   24.115  1.00 23.03 ? 236  LEU B CG  1 
ATOM   3794 C CD1 . LEU B 1 236 ? -2.281  1.950   23.785  1.00 22.54 ? 236  LEU B CD1 1 
ATOM   3795 C CD2 . LEU B 1 236 ? -0.198  3.069   22.913  1.00 25.11 ? 236  LEU B CD2 1 
ATOM   3796 N N   . THR B 1 237 ? -1.836  6.875   26.455  1.00 23.89 ? 237  THR B N   1 
ATOM   3797 C CA  . THR B 1 237 ? -2.476  8.189   26.756  1.00 24.48 ? 237  THR B CA  1 
ATOM   3798 C C   . THR B 1 237 ? -1.429  9.287   26.549  1.00 25.01 ? 237  THR B C   1 
ATOM   3799 O O   . THR B 1 237 ? -1.719  10.298  25.866  1.00 21.48 ? 237  THR B O   1 
ATOM   3800 C CB  . THR B 1 237 ? -3.009  8.268   28.189  1.00 25.57 ? 237  THR B CB  1 
ATOM   3801 O OG1 . THR B 1 237 ? -1.913  7.863   29.016  1.00 26.25 ? 237  THR B OG1 1 
ATOM   3802 C CG2 . THR B 1 237 ? -4.229  7.405   28.407  1.00 24.61 ? 237  THR B CG2 1 
ATOM   3803 N N   . MET B 1 238 ? -0.219  9.063   27.067  1.00 26.42 ? 238  MET B N   1 
ATOM   3804 C CA  . MET B 1 238 ? 0.903   10.030  26.943  1.00 25.55 ? 238  MET B CA  1 
ATOM   3805 C C   . MET B 1 238 ? 1.311   10.149  25.466  1.00 26.54 ? 238  MET B C   1 
ATOM   3806 O O   . MET B 1 238 ? 1.441   11.295  24.958  1.00 26.70 ? 238  MET B O   1 
ATOM   3807 C CB  . MET B 1 238 ? 2.078   9.590   27.823  1.00 27.33 ? 238  MET B CB  1 
ATOM   3808 C CG  . MET B 1 238 ? 3.270   10.545  27.816  1.00 27.10 ? 238  MET B CG  1 
ATOM   3809 S SD  . MET B 1 238 ? 4.338   10.279  26.375  1.00 28.78 ? 238  MET B SD  1 
ATOM   3810 C CE  . MET B 1 238 ? 4.966   8.640   26.733  1.00 29.09 ? 238  MET B CE  1 
ATOM   3811 N N   . GLN B 1 239 ? 1.489   9.032   24.768  1.00 25.38 ? 239  GLN B N   1 
ATOM   3812 C CA  . GLN B 1 239 ? 1.872   9.034   23.333  1.00 25.82 ? 239  GLN B CA  1 
ATOM   3813 C C   . GLN B 1 239 ? 0.796   9.725   22.476  1.00 25.68 ? 239  GLN B C   1 
ATOM   3814 O O   . GLN B 1 239 ? 1.178   10.548  21.613  1.00 22.54 ? 239  GLN B O   1 
ATOM   3815 C CB  . GLN B 1 239 ? 2.166   7.611   22.880  1.00 28.25 ? 239  GLN B CB  1 
ATOM   3816 C CG  . GLN B 1 239 ? 3.388   7.058   23.588  1.00 31.03 ? 239  GLN B CG  1 
ATOM   3817 C CD  . GLN B 1 239 ? 3.920   5.785   22.992  1.00 34.16 ? 239  GLN B CD  1 
ATOM   3818 O OE1 . GLN B 1 239 ? 4.188   4.822   23.712  1.00 37.20 ? 239  GLN B OE1 1 
ATOM   3819 N NE2 . GLN B 1 239 ? 4.123   5.802   21.682  1.00 35.71 ? 239  GLN B NE2 1 
ATOM   3820 N N   . LEU B 1 240 ? -0.491  9.416   22.689  1.00 24.84 ? 240  LEU B N   1 
ATOM   3821 C CA  . LEU B 1 240 ? -1.619  10.049  21.950  1.00 24.86 ? 240  LEU B CA  1 
ATOM   3822 C C   . LEU B 1 240 ? -1.533  11.573  22.107  1.00 25.35 ? 240  LEU B C   1 
ATOM   3823 O O   . LEU B 1 240 ? -1.610  12.288  21.084  1.00 25.77 ? 240  LEU B O   1 
ATOM   3824 C CB  . LEU B 1 240 ? -2.942  9.519   22.502  1.00 24.90 ? 240  LEU B CB  1 
ATOM   3825 C CG  . LEU B 1 240 ? -4.203  10.018  21.807  1.00 23.97 ? 240  LEU B CG  1 
ATOM   3826 C CD1 . LEU B 1 240 ? -4.112  9.825   20.296  1.00 23.09 ? 240  LEU B CD1 1 
ATOM   3827 C CD2 . LEU B 1 240 ? -5.420  9.299   22.362  1.00 23.63 ? 240  LEU B CD2 1 
ATOM   3828 N N   . GLU B 1 241 ? -1.346  12.043  23.342  1.00 24.43 ? 241  GLU B N   1 
ATOM   3829 C CA  . GLU B 1 241 ? -1.211  13.484  23.655  1.00 27.57 ? 241  GLU B CA  1 
ATOM   3830 C C   . GLU B 1 241 ? -0.123  14.089  22.753  1.00 25.05 ? 241  GLU B C   1 
ATOM   3831 O O   . GLU B 1 241 ? -0.403  15.109  22.132  1.00 26.97 ? 241  GLU B O   1 
ATOM   3832 C CB  . GLU B 1 241 ? -0.915  13.700  25.137  1.00 30.74 ? 241  GLU B CB  1 
ATOM   3833 C CG  . GLU B 1 241 ? -1.182  15.119  25.572  1.00 34.96 ? 241  GLU B CG  1 
ATOM   3834 C CD  . GLU B 1 241 ? -2.647  15.517  25.610  1.00 35.61 ? 241  GLU B CD  1 
ATOM   3835 O OE1 . GLU B 1 241 ? -3.426  14.828  26.277  1.00 39.48 ? 241  GLU B OE1 1 
ATOM   3836 O OE2 . GLU B 1 241 ? -2.989  16.547  25.005  1.00 38.41 ? 241  GLU B OE2 1 
ATOM   3837 N N   . ALA B 1 242 ? 1.035   13.443  22.635  1.00 22.12 ? 242  ALA B N   1 
ATOM   3838 C CA  . ALA B 1 242 ? 2.167   13.875  21.789  1.00 23.22 ? 242  ALA B CA  1 
ATOM   3839 C C   . ALA B 1 242 ? 1.781   13.854  20.294  1.00 22.92 ? 242  ALA B C   1 
ATOM   3840 O O   . ALA B 1 242 ? 2.141   14.802  19.581  1.00 22.15 ? 242  ALA B O   1 
ATOM   3841 C CB  . ALA B 1 242 ? 3.366   13.003  22.075  1.00 23.63 ? 242  ALA B CB  1 
ATOM   3842 N N   . LEU B 1 243 ? 1.070   12.823  19.829  1.00 23.57 ? 243  LEU B N   1 
ATOM   3843 C CA  . LEU B 1 243 ? 0.609   12.722  18.414  1.00 24.94 ? 243  LEU B CA  1 
ATOM   3844 C C   . LEU B 1 243 ? -0.302  13.915  18.131  1.00 24.42 ? 243  LEU B C   1 
ATOM   3845 O O   . LEU B 1 243 ? -0.131  14.540  17.070  1.00 24.79 ? 243  LEU B O   1 
ATOM   3846 C CB  . LEU B 1 243 ? -0.123  11.396  18.178  1.00 26.20 ? 243  LEU B CB  1 
ATOM   3847 C CG  . LEU B 1 243 ? 0.585   10.329  17.330  1.00 30.09 ? 243  LEU B CG  1 
ATOM   3848 C CD1 . LEU B 1 243 ? 2.103   10.456  17.344  1.00 28.68 ? 243  LEU B CD1 1 
ATOM   3849 C CD2 . LEU B 1 243 ? 0.169   8.931   17.773  1.00 30.06 ? 243  LEU B CD2 1 
ATOM   3850 N N   . GLU B 1 244 ? -1.180  14.253  19.082  1.00 25.10 ? 244  GLU B N   1 
ATOM   3851 C CA  . GLU B 1 244 ? -2.141  15.387  18.945  1.00 25.27 ? 244  GLU B CA  1 
ATOM   3852 C C   . GLU B 1 244 ? -1.348  16.688  18.822  1.00 23.39 ? 244  GLU B C   1 
ATOM   3853 O O   . GLU B 1 244 ? -1.758  17.566  18.048  1.00 22.68 ? 244  GLU B O   1 
ATOM   3854 C CB  . GLU B 1 244 ? -3.112  15.462  20.123  1.00 27.21 ? 244  GLU B CB  1 
ATOM   3855 C CG  . GLU B 1 244 ? -3.973  14.231  20.307  1.00 31.26 ? 244  GLU B CG  1 
ATOM   3856 C CD  . GLU B 1 244 ? -5.135  14.100  19.339  1.00 39.35 ? 244  GLU B CD  1 
ATOM   3857 O OE1 . GLU B 1 244 ? -6.019  13.255  19.620  1.00 43.36 ? 244  GLU B OE1 1 
ATOM   3858 O OE2 . GLU B 1 244 ? -5.160  14.839  18.305  1.00 39.67 ? 244  GLU B OE2 1 
ATOM   3859 N N   . ASN B 1 245 ? -0.246  16.805  19.562  1.00 21.64 ? 245  ASN B N   1 
ATOM   3860 C CA  . ASN B 1 245 ? 0.633   18.001  19.521  1.00 22.87 ? 245  ASN B CA  1 
ATOM   3861 C C   . ASN B 1 245 ? 1.336   18.101  18.155  1.00 22.71 ? 245  ASN B C   1 
ATOM   3862 O O   . ASN B 1 245 ? 1.626   19.220  17.715  1.00 23.23 ? 245  ASN B O   1 
ATOM   3863 C CB  . ASN B 1 245 ? 1.592   18.006  20.718  1.00 24.41 ? 245  ASN B CB  1 
ATOM   3864 C CG  . ASN B 1 245 ? 0.922   18.360  22.037  1.00 23.32 ? 245  ASN B CG  1 
ATOM   3865 O OD1 . ASN B 1 245 ? -0.122  18.995  22.063  1.00 22.59 ? 245  ASN B OD1 1 
ATOM   3866 N ND2 . ASN B 1 245 ? 1.516   17.964  23.148  1.00 24.13 ? 245  ASN B ND2 1 
ATOM   3867 N N   . ILE B 1 246 ? 1.635   16.980  17.498  1.00 23.21 ? 246  ILE B N   1 
ATOM   3868 C CA  . ILE B 1 246 ? 2.156   16.974  16.101  1.00 23.88 ? 246  ILE B CA  1 
ATOM   3869 C C   . ILE B 1 246 ? 1.091   17.577  15.167  1.00 24.19 ? 246  ILE B C   1 
ATOM   3870 O O   . ILE B 1 246 ? 1.449   18.354  14.269  1.00 23.88 ? 246  ILE B O   1 
ATOM   3871 C CB  . ILE B 1 246 ? 2.594   15.555  15.682  1.00 22.66 ? 246  ILE B CB  1 
ATOM   3872 C CG1 . ILE B 1 246 ? 3.776   15.093  16.540  1.00 22.98 ? 246  ILE B CG1 1 
ATOM   3873 C CG2 . ILE B 1 246 ? 2.900   15.470  14.191  1.00 22.80 ? 246  ILE B CG2 1 
ATOM   3874 C CD1 . ILE B 1 246 ? 4.156   13.625  16.363  1.00 24.09 ? 246  ILE B CD1 1 
ATOM   3875 N N   . SER B 1 247 ? -0.181  17.249  15.347  1.00 26.79 ? 247  SER B N   1 
ATOM   3876 C CA  . SER B 1 247 ? -1.282  17.879  14.557  1.00 29.52 ? 247  SER B CA  1 
ATOM   3877 C C   . SER B 1 247 ? -1.331  19.392  14.783  1.00 27.44 ? 247  SER B C   1 
ATOM   3878 O O   . SER B 1 247 ? -1.402  20.114  13.778  1.00 27.27 ? 247  SER B O   1 
ATOM   3879 C CB  . SER B 1 247 ? -2.593  17.271  14.871  1.00 28.96 ? 247  SER B CB  1 
ATOM   3880 O OG  . SER B 1 247 ? -2.467  15.879  14.719  1.00 32.57 ? 247  SER B OG  1 
ATOM   3881 N N   . GLU B 1 248 ? -1.284  19.846  16.038  1.00 26.65 ? 248  GLU B N   1 
ATOM   3882 C CA  . GLU B 1 248 ? -1.346  21.292  16.379  1.00 26.62 ? 248  GLU B CA  1 
ATOM   3883 C C   . GLU B 1 248 ? -0.112  22.043  15.871  1.00 25.81 ? 248  GLU B C   1 
ATOM   3884 O O   . GLU B 1 248 ? -0.286  23.166  15.342  1.00 23.82 ? 248  GLU B O   1 
ATOM   3885 C CB  . GLU B 1 248 ? -1.525  21.489  17.883  1.00 27.90 ? 248  GLU B CB  1 
ATOM   3886 C CG  . GLU B 1 248 ? -1.787  22.940  18.290  1.00 29.27 ? 248  GLU B CG  1 
ATOM   3887 C CD  . GLU B 1 248 ? -3.034  23.626  17.748  1.00 31.85 ? 248  GLU B CD  1 
ATOM   3888 O OE1 . GLU B 1 248 ? -3.837  22.969  17.038  1.00 36.19 ? 248  GLU B OE1 1 
ATOM   3889 O OE2 . GLU B 1 248 ? -3.204  24.845  18.029  1.00 33.70 ? 248  GLU B OE2 1 
ATOM   3890 N N   . THR B 1 249 ? 1.086   21.490  16.092  1.00 26.24 ? 249  THR B N   1 
ATOM   3891 C CA  . THR B 1 249 ? 2.388   21.956  15.529  1.00 25.79 ? 249  THR B CA  1 
ATOM   3892 C C   . THR B 1 249 ? 2.229   22.162  14.018  1.00 25.72 ? 249  THR B C   1 
ATOM   3893 O O   . THR B 1 249 ? 2.669   23.194  13.483  1.00 26.27 ? 249  THR B O   1 
ATOM   3894 C CB  . THR B 1 249 ? 3.494   20.942  15.865  1.00 27.34 ? 249  THR B CB  1 
ATOM   3895 O OG1 . THR B 1 249 ? 3.692   20.916  17.283  1.00 25.85 ? 249  THR B OG1 1 
ATOM   3896 C CG2 . THR B 1 249 ? 4.808   21.232  15.183  1.00 26.40 ? 249  THR B CG2 1 
ATOM   3897 N N   . SER B 1 250 ? 1.592   21.205  13.355  1.00 26.00 ? 250  SER B N   1 
ATOM   3898 C CA  . SER B 1 250 ? 1.393   21.197  11.890  1.00 26.32 ? 250  SER B CA  1 
ATOM   3899 C C   . SER B 1 250 ? 0.410   22.317  11.517  1.00 26.00 ? 250  SER B C   1 
ATOM   3900 O O   . SER B 1 250 ? 0.749   23.145  10.663  1.00 24.95 ? 250  SER B O   1 
ATOM   3901 C CB  . SER B 1 250 ? 0.932   19.831  11.440  1.00 28.01 ? 250  SER B CB  1 
ATOM   3902 O OG  . SER B 1 250 ? 1.958   18.852  11.616  1.00 26.40 ? 250  SER B OG  1 
ATOM   3903 N N   . ARG B 1 251 ? -0.741  22.374  12.176  1.00 27.01 ? 251  ARG B N   1 
ATOM   3904 C CA  . ARG B 1 251 ? -1.736  23.468  12.002  1.00 31.23 ? 251  ARG B CA  1 
ATOM   3905 C C   . ARG B 1 251 ? -1.038  24.828  12.180  1.00 30.44 ? 251  ARG B C   1 
ATOM   3906 O O   . ARG B 1 251 ? -1.234  25.686  11.322  1.00 31.56 ? 251  ARG B O   1 
ATOM   3907 C CB  . ARG B 1 251 ? -2.931  23.268  12.942  1.00 33.65 ? 251  ARG B CB  1 
ATOM   3908 C CG  . ARG B 1 251 ? -4.175  24.053  12.545  1.00 35.25 ? 251  ARG B CG  1 
ATOM   3909 C CD  . ARG B 1 251 ? -5.329  23.879  13.513  1.00 33.52 ? 251  ARG B CD  1 
ATOM   3910 N NE  . ARG B 1 251 ? -5.057  24.373  14.860  1.00 36.69 ? 251  ARG B NE  1 
ATOM   3911 C CZ  . ARG B 1 251 ? -5.230  25.637  15.280  1.00 39.46 ? 251  ARG B CZ  1 
ATOM   3912 N NH1 . ARG B 1 251 ? -5.630  26.589  14.446  1.00 37.84 ? 251  ARG B NH1 1 
ATOM   3913 N NH2 . ARG B 1 251 ? -4.984  25.952  16.543  1.00 40.33 ? 251  ARG B NH2 1 
ATOM   3914 N N   . GLU B 1 252 ? -0.215  25.011  13.219  1.00 28.97 ? 252  GLU B N   1 
ATOM   3915 C CA  . GLU B 1 252 ? 0.479   26.300  13.502  1.00 29.41 ? 252  GLU B CA  1 
ATOM   3916 C C   . GLU B 1 252 ? 1.283   26.732  12.264  1.00 28.59 ? 252  GLU B C   1 
ATOM   3917 O O   . GLU B 1 252 ? 1.488   27.957  12.046  1.00 25.51 ? 252  GLU B O   1 
ATOM   3918 C CB  . GLU B 1 252 ? 1.422   26.189  14.710  1.00 28.59 ? 252  GLU B CB  1 
ATOM   3919 C CG  . GLU B 1 252 ? 0.722   26.123  16.060  1.00 28.79 ? 252  GLU B CG  1 
ATOM   3920 C CD  . GLU B 1 252 ? 1.651   25.875  17.248  1.00 29.19 ? 252  GLU B CD  1 
ATOM   3921 O OE1 . GLU B 1 252 ? 1.110   25.670  18.355  1.00 26.21 ? 252  GLU B OE1 1 
ATOM   3922 O OE2 . GLU B 1 252 ? 2.915   25.918  17.068  1.00 23.43 ? 252  GLU B OE2 1 
ATOM   3923 N N   . LEU B 1 253 ? 1.767   25.750  11.509  1.00 28.98 ? 253  LEU B N   1 
ATOM   3924 C CA  . LEU B 1 253 ? 2.708   25.939  10.383  1.00 28.12 ? 253  LEU B CA  1 
ATOM   3925 C C   . LEU B 1 253 ? 1.941   25.935  9.059   1.00 29.10 ? 253  LEU B C   1 
ATOM   3926 O O   . LEU B 1 253 ? 2.565   26.229  8.036   1.00 33.28 ? 253  LEU B O   1 
ATOM   3927 C CB  . LEU B 1 253 ? 3.764   24.824  10.445  1.00 29.06 ? 253  LEU B CB  1 
ATOM   3928 C CG  . LEU B 1 253 ? 4.879   25.023  11.474  1.00 27.28 ? 253  LEU B CG  1 
ATOM   3929 C CD1 . LEU B 1 253 ? 5.735   23.772  11.647  1.00 27.00 ? 253  LEU B CD1 1 
ATOM   3930 C CD2 . LEU B 1 253 ? 5.731   26.217  11.133  1.00 27.65 ? 253  LEU B CD2 1 
ATOM   3931 N N   . GLY B 1 254 ? 0.632   25.669  9.085   1.00 32.65 ? 254  GLY B N   1 
ATOM   3932 C CA  . GLY B 1 254 ? -0.205  25.491  7.883   1.00 34.52 ? 254  GLY B CA  1 
ATOM   3933 C C   . GLY B 1 254 ? 0.248   24.284  7.091   1.00 38.10 ? 254  GLY B C   1 
ATOM   3934 O O   . GLY B 1 254 ? 0.236   24.349  5.842   1.00 39.91 ? 254  GLY B O   1 
ATOM   3935 N N   . VAL B 1 255 ? 0.626   23.213  7.797   1.00 35.47 ? 255  VAL B N   1 
ATOM   3936 C CA  . VAL B 1 255 ? 1.219   21.971  7.215   1.00 34.27 ? 255  VAL B CA  1 
ATOM   3937 C C   . VAL B 1 255 ? 0.236   20.827  7.462   1.00 31.01 ? 255  VAL B C   1 
ATOM   3938 O O   . VAL B 1 255 ? -0.268  20.758  8.582   1.00 34.13 ? 255  VAL B O   1 
ATOM   3939 C CB  . VAL B 1 255 ? 2.597   21.694  7.849   1.00 36.29 ? 255  VAL B CB  1 
ATOM   3940 C CG1 . VAL B 1 255 ? 3.078   20.272  7.604   1.00 37.39 ? 255  VAL B CG1 1 
ATOM   3941 C CG2 . VAL B 1 255 ? 3.628   22.700  7.377   1.00 36.41 ? 255  VAL B CG2 1 
ATOM   3942 N N   . GLY B 1 256 ? -0.034  19.989  6.457   1.00 28.24 ? 256  GLY B N   1 
ATOM   3943 C CA  . GLY B 1 256 ? -0.910  18.806  6.596   1.00 30.20 ? 256  GLY B CA  1 
ATOM   3944 C C   . GLY B 1 256 ? -0.350  17.794  7.587   1.00 28.97 ? 256  GLY B C   1 
ATOM   3945 O O   . GLY B 1 256 ? 0.836   17.908  7.949   1.00 27.70 ? 256  GLY B O   1 
ATOM   3946 N N   . VAL B 1 257 ? -1.156  16.816  7.999   1.00 30.16 ? 257  VAL B N   1 
ATOM   3947 C CA  . VAL B 1 257 ? -0.736  15.820  9.024   1.00 28.86 ? 257  VAL B CA  1 
ATOM   3948 C C   . VAL B 1 257 ? -1.152  14.416  8.578   1.00 27.69 ? 257  VAL B C   1 
ATOM   3949 O O   . VAL B 1 257 ? -2.309  14.209  8.148   1.00 24.84 ? 257  VAL B O   1 
ATOM   3950 C CB  . VAL B 1 257 ? -1.245  16.197  10.434  1.00 31.24 ? 257  VAL B CB  1 
ATOM   3951 C CG1 . VAL B 1 257 ? -1.567  17.685  10.543  1.00 33.69 ? 257  VAL B CG1 1 
ATOM   3952 C CG2 . VAL B 1 257 ? -2.444  15.393  10.890  1.00 31.68 ? 257  VAL B CG2 1 
ATOM   3953 N N   . LEU B 1 258 ? -0.214  13.474  8.679   1.00 26.42 ? 258  LEU B N   1 
ATOM   3954 C CA  . LEU B 1 258 ? -0.467  12.031  8.449   1.00 26.19 ? 258  LEU B CA  1 
ATOM   3955 C C   . LEU B 1 258 ? -0.659  11.412  9.830   1.00 26.38 ? 258  LEU B C   1 
ATOM   3956 O O   . LEU B 1 258 ? -1.095  12.151  10.727  1.00 26.38 ? 258  LEU B O   1 
ATOM   3957 C CB  . LEU B 1 258 ? 0.713   11.436  7.666   1.00 27.29 ? 258  LEU B CB  1 
ATOM   3958 C CG  . LEU B 1 258 ? 1.126   12.180  6.393   1.00 27.13 ? 258  LEU B CG  1 
ATOM   3959 C CD1 . LEU B 1 258 ? 2.401   11.603  5.801   1.00 28.09 ? 258  LEU B CD1 1 
ATOM   3960 C CD2 . LEU B 1 258 ? 0.021   12.150  5.351   1.00 26.03 ? 258  LEU B CD2 1 
ATOM   3961 N N   . LEU B 1 259 ? -0.342  10.125  9.993   1.00 28.64 ? 259  LEU B N   1 
ATOM   3962 C CA  . LEU B 1 259 ? -0.390  9.359   11.267  1.00 28.83 ? 259  LEU B CA  1 
ATOM   3963 C C   . LEU B 1 259 ? -1.821  9.274   11.807  1.00 28.56 ? 259  LEU B C   1 
ATOM   3964 O O   . LEU B 1 259 ? -1.975  8.903   12.980  1.00 30.76 ? 259  LEU B O   1 
ATOM   3965 C CB  . LEU B 1 259 ? 0.551   10.026  12.272  1.00 28.82 ? 259  LEU B CB  1 
ATOM   3966 C CG  . LEU B 1 259 ? 2.027   9.990   11.887  1.00 28.75 ? 259  LEU B CG  1 
ATOM   3967 C CD1 . LEU B 1 259 ? 2.853   10.796  12.862  1.00 28.02 ? 259  LEU B CD1 1 
ATOM   3968 C CD2 . LEU B 1 259 ? 2.526   8.553   11.811  1.00 27.82 ? 259  LEU B CD2 1 
ATOM   3969 N N   . GLY B 1 260 ? -2.820  9.515   10.954  1.00 29.42 ? 260  GLY B N   1 
ATOM   3970 C CA  . GLY B 1 260 ? -4.263  9.412   11.254  1.00 26.54 ? 260  GLY B CA  1 
ATOM   3971 C C   . GLY B 1 260 ? -4.688  8.075   11.835  1.00 27.20 ? 260  GLY B C   1 
ATOM   3972 O O   . GLY B 1 260 ? -5.405  8.091   12.849  1.00 25.99 ? 260  GLY B O   1 
ATOM   3973 N N   . SER B 1 261 ? -4.320  6.949   11.211  1.00 28.13 ? 261  SER B N   1 
ATOM   3974 C CA  . SER B 1 261 ? -4.647  5.574   11.676  1.00 26.63 ? 261  SER B CA  1 
ATOM   3975 C C   . SER B 1 261 ? -4.007  5.324   13.048  1.00 28.72 ? 261  SER B C   1 
ATOM   3976 O O   . SER B 1 261 ? -4.607  4.568   13.861  1.00 27.81 ? 261  SER B O   1 
ATOM   3977 C CB  . SER B 1 261 ? -4.178  4.503   10.700  1.00 28.00 ? 261  SER B CB  1 
ATOM   3978 O OG  . SER B 1 261 ? -4.472  4.863   9.355   1.00 28.71 ? 261  SER B OG  1 
ATOM   3979 N N   . MET B 1 262 ? -2.832  5.914   13.284  1.00 27.18 ? 262  MET B N   1 
ATOM   3980 C CA  . MET B 1 262 ? -2.092  5.793   14.566  1.00 26.17 ? 262  MET B CA  1 
ATOM   3981 C C   . MET B 1 262 ? -2.860  6.560   15.648  1.00 25.55 ? 262  MET B C   1 
ATOM   3982 O O   . MET B 1 262 ? -3.086  5.979   16.710  1.00 23.29 ? 262  MET B O   1 
ATOM   3983 C CB  . MET B 1 262 ? -0.657  6.330   14.434  1.00 25.08 ? 262  MET B CB  1 
ATOM   3984 C CG  . MET B 1 262 ? 0.259   5.889   15.529  1.00 25.02 ? 262  MET B CG  1 
ATOM   3985 S SD  . MET B 1 262 ? 0.168   4.101   15.813  1.00 27.14 ? 262  MET B SD  1 
ATOM   3986 C CE  . MET B 1 262 ? 1.736   3.853   16.649  1.00 27.80 ? 262  MET B CE  1 
ATOM   3987 N N   . ARG B 1 263 ? -3.254  7.818   15.400  1.00 27.22 ? 263  ARG B N   1 
ATOM   3988 C CA  . ARG B 1 263 ? -4.118  8.555   16.371  1.00 27.91 ? 263  ARG B CA  1 
ATOM   3989 C C   . ARG B 1 263 ? -5.400  7.749   16.612  1.00 27.46 ? 263  ARG B C   1 
ATOM   3990 O O   . ARG B 1 263 ? -5.774  7.563   17.796  1.00 29.10 ? 263  ARG B O   1 
ATOM   3991 C CB  . ARG B 1 263 ? -4.419  9.990   15.925  1.00 29.15 ? 263  ARG B CB  1 
ATOM   3992 C CG  . ARG B 1 263 ? -3.220  10.925  16.032  1.00 29.94 ? 263  ARG B CG  1 
ATOM   3993 C CD  . ARG B 1 263 ? -3.607  12.374  15.824  1.00 29.04 ? 263  ARG B CD  1 
ATOM   3994 N NE  . ARG B 1 263 ? -4.417  12.526  14.627  1.00 29.62 ? 263  ARG B NE  1 
ATOM   3995 C CZ  . ARG B 1 263 ? -3.955  12.572  13.372  1.00 29.98 ? 263  ARG B CZ  1 
ATOM   3996 N NH1 . ARG B 1 263 ? -4.815  12.661  12.368  1.00 28.87 ? 263  ARG B NH1 1 
ATOM   3997 N NH2 . ARG B 1 263 ? -2.657  12.490  13.113  1.00 27.63 ? 263  ARG B NH2 1 
ATOM   3998 N N   . GLU B 1 264 ? -6.043  7.247   15.556  1.00 27.52 ? 264  GLU B N   1 
ATOM   3999 C CA  . GLU B 1 264 ? -7.360  6.569   15.684  1.00 28.56 ? 264  GLU B CA  1 
ATOM   4000 C C   . GLU B 1 264 ? -7.243  5.330   16.564  1.00 27.86 ? 264  GLU B C   1 
ATOM   4001 O O   . GLU B 1 264 ? -8.105  5.165   17.452  1.00 28.79 ? 264  GLU B O   1 
ATOM   4002 C CB  . GLU B 1 264 ? -7.940  6.161   14.331  1.00 31.24 ? 264  GLU B CB  1 
ATOM   4003 C CG  . GLU B 1 264 ? -8.380  7.349   13.505  1.00 36.10 ? 264  GLU B CG  1 
ATOM   4004 C CD  . GLU B 1 264 ? -9.428  8.202   14.202  1.00 43.55 ? 264  GLU B CD  1 
ATOM   4005 O OE1 . GLU B 1 264 ? -10.448 7.633   14.651  1.00 43.26 ? 264  GLU B OE1 1 
ATOM   4006 O OE2 . GLU B 1 264 ? -9.201  9.422   14.320  1.00 52.72 ? 264  GLU B OE2 1 
ATOM   4007 N N   . VAL B 1 265 ? -6.279  4.444   16.298  1.00 25.36 ? 265  VAL B N   1 
ATOM   4008 C CA  . VAL B 1 265 ? -6.196  3.155   17.049  1.00 26.00 ? 265  VAL B CA  1 
ATOM   4009 C C   . VAL B 1 265 ? -5.839  3.419   18.518  1.00 24.92 ? 265  VAL B C   1 
ATOM   4010 O O   . VAL B 1 265 ? -6.378  2.701   19.387  1.00 25.24 ? 265  VAL B O   1 
ATOM   4011 C CB  . VAL B 1 265 ? -5.215  2.158   16.414  1.00 26.41 ? 265  VAL B CB  1 
ATOM   4012 C CG1 . VAL B 1 265 ? -3.760  2.643   16.508  1.00 25.81 ? 265  VAL B CG1 1 
ATOM   4013 C CG2 . VAL B 1 265 ? -5.386  0.788   17.045  1.00 25.84 ? 265  VAL B CG2 1 
ATOM   4014 N N   . MET B 1 266 ? -4.964  4.390   18.788  1.00 26.04 ? 266  MET B N   1 
ATOM   4015 C CA  . MET B 1 266 ? -4.603  4.798   20.171  1.00 28.71 ? 266  MET B CA  1 
ATOM   4016 C C   . MET B 1 266 ? -5.859  5.351   20.876  1.00 29.13 ? 266  MET B C   1 
ATOM   4017 O O   . MET B 1 266 ? -6.062  5.016   22.046  1.00 28.28 ? 266  MET B O   1 
ATOM   4018 C CB  . MET B 1 266 ? -3.509  5.868   20.196  1.00 27.27 ? 266  MET B CB  1 
ATOM   4019 C CG  . MET B 1 266 ? -2.124  5.334   19.982  1.00 31.85 ? 266  MET B CG  1 
ATOM   4020 S SD  . MET B 1 266 ? -0.841  6.604   20.291  1.00 31.34 ? 266  MET B SD  1 
ATOM   4021 C CE  . MET B 1 266 ? 0.533   5.815   19.457  1.00 35.25 ? 266  MET B CE  1 
ATOM   4022 N N   . SER B 1 267 ? -6.652  6.197   20.212  1.00 29.19 ? 267  SER B N   1 
ATOM   4023 C CA  . SER B 1 267 ? -7.970  6.667   20.749  1.00 30.45 ? 267  SER B CA  1 
ATOM   4024 C C   . SER B 1 267 ? -8.836  5.484   21.173  1.00 28.88 ? 267  SER B C   1 
ATOM   4025 O O   . SER B 1 267 ? -9.278  5.451   22.327  1.00 31.30 ? 267  SER B O   1 
ATOM   4026 C CB  . SER B 1 267 ? -8.707  7.497   19.775  1.00 27.67 ? 267  SER B CB  1 
ATOM   4027 O OG  . SER B 1 267 ? -8.115  8.751   19.726  1.00 27.74 ? 267  SER B OG  1 
ATOM   4028 N N   . GLU B 1 268 ? -9.050  4.512   20.296  1.00 29.42 ? 268  GLU B N   1 
ATOM   4029 C CA  . GLU B 1 268 ? -9.888  3.345   20.669  1.00 30.82 ? 268  GLU B CA  1 
ATOM   4030 C C   . GLU B 1 268 ? -9.227  2.589   21.832  1.00 34.92 ? 268  GLU B C   1 
ATOM   4031 O O   . GLU B 1 268 ? -9.956  2.178   22.771  1.00 34.35 ? 268  GLU B O   1 
ATOM   4032 C CB  . GLU B 1 268 ? -10.158 2.453   19.465  1.00 33.75 ? 268  GLU B CB  1 
ATOM   4033 C CG  . GLU B 1 268 ? -11.182 1.363   19.741  1.00 37.96 ? 268  GLU B CG  1 
ATOM   4034 C CD  . GLU B 1 268 ? -12.594 1.818   20.096  1.00 41.44 ? 268  GLU B CD  1 
ATOM   4035 O OE1 . GLU B 1 268 ? -13.377 0.970   20.593  1.00 46.28 ? 268  GLU B OE1 1 
ATOM   4036 O OE2 . GLU B 1 268 ? -12.904 3.007   19.898  1.00 37.92 ? 268  GLU B OE2 1 
ATOM   4037 N N   . ALA B 1 269 ? -7.906  2.396   21.803  1.00 32.51 ? 269  ALA B N   1 
ATOM   4038 C CA  . ALA B 1 269 ? -7.176  1.761   22.921  1.00 30.34 ? 269  ALA B CA  1 
ATOM   4039 C C   . ALA B 1 269 ? -7.549  2.465   24.240  1.00 28.05 ? 269  ALA B C   1 
ATOM   4040 O O   . ALA B 1 269 ? -7.955  1.782   25.193  1.00 26.50 ? 269  ALA B O   1 
ATOM   4041 C CB  . ALA B 1 269 ? -5.687  1.779   22.655  1.00 30.20 ? 269  ALA B CB  1 
ATOM   4042 N N   . VAL B 1 270 ? -7.411  3.784   24.305  1.00 30.19 ? 270  VAL B N   1 
ATOM   4043 C CA  . VAL B 1 270 ? -7.802  4.601   25.499  1.00 34.30 ? 270  VAL B CA  1 
ATOM   4044 C C   . VAL B 1 270 ? -9.263  4.289   25.883  1.00 39.11 ? 270  VAL B C   1 
ATOM   4045 O O   . VAL B 1 270 ? -9.502  3.883   27.049  1.00 39.66 ? 270  VAL B O   1 
ATOM   4046 C CB  . VAL B 1 270 ? -7.534  6.101   25.261  1.00 33.35 ? 270  VAL B CB  1 
ATOM   4047 C CG1 . VAL B 1 270 ? -8.109  6.987   26.358  1.00 34.39 ? 270  VAL B CG1 1 
ATOM   4048 C CG2 . VAL B 1 270 ? -6.040  6.366   25.119  1.00 34.80 ? 270  VAL B CG2 1 
ATOM   4049 N N   . LYS B 1 271 ? -10.209 4.381   24.945  1.00 41.12 ? 271  LYS B N   1 
ATOM   4050 C CA  . LYS B 1 271 ? -11.630 4.005   25.189  1.00 43.57 ? 271  LYS B CA  1 
ATOM   4051 C C   . LYS B 1 271 ? -11.718 2.615   25.849  1.00 43.98 ? 271  LYS B C   1 
ATOM   4052 O O   . LYS B 1 271 ? -12.459 2.461   26.825  1.00 45.09 ? 271  LYS B O   1 
ATOM   4053 C CB  . LYS B 1 271 ? -12.424 4.002   23.877  1.00 47.70 ? 271  LYS B CB  1 
ATOM   4054 C CG  . LYS B 1 271 ? -13.906 4.325   24.013  1.00 52.41 ? 271  LYS B CG  1 
ATOM   4055 C CD  . LYS B 1 271 ? -14.794 3.588   23.022  1.00 56.99 ? 271  LYS B CD  1 
ATOM   4056 C CE  . LYS B 1 271 ? -15.884 4.446   22.415  1.00 56.62 ? 271  LYS B CE  1 
ATOM   4057 N NZ  . LYS B 1 271 ? -16.229 3.967   21.056  1.00 60.71 ? 271  LYS B NZ  1 
ATOM   4058 N N   . LYS B 1 272 ? -11.019 1.608   25.335  1.00 42.32 ? 272  LYS B N   1 
ATOM   4059 C CA  . LYS B 1 272 ? -11.173 0.212   25.812  1.00 43.87 ? 272  LYS B CA  1 
ATOM   4060 C C   . LYS B 1 272 ? -10.422 0.009   27.133  1.00 42.00 ? 272  LYS B C   1 
ATOM   4061 O O   . LYS B 1 272 ? -10.326 -1.146  27.553  1.00 41.03 ? 272  LYS B O   1 
ATOM   4062 C CB  . LYS B 1 272 ? -10.667 -0.779  24.758  1.00 50.14 ? 272  LYS B CB  1 
ATOM   4063 C CG  . LYS B 1 272 ? -11.500 -0.871  23.486  1.00 54.51 ? 272  LYS B CG  1 
ATOM   4064 C CD  . LYS B 1 272 ? -11.092 -2.053  22.616  1.00 58.79 ? 272  LYS B CD  1 
ATOM   4065 C CE  . LYS B 1 272 ? -11.329 -1.833  21.136  1.00 61.31 ? 272  LYS B CE  1 
ATOM   4066 N NZ  . LYS B 1 272 ? -11.532 -3.109  20.411  1.00 60.67 ? 272  LYS B NZ  1 
ATOM   4067 N N   . GLY B 1 273 ? -9.892  1.072   27.749  1.00 41.35 ? 273  GLY B N   1 
ATOM   4068 C CA  . GLY B 1 273 ? -9.197  1.014   29.053  1.00 40.79 ? 273  GLY B CA  1 
ATOM   4069 C C   . GLY B 1 273 ? -7.751  0.565   28.910  1.00 39.98 ? 273  GLY B C   1 
ATOM   4070 O O   . GLY B 1 273 ? -7.214  -0.073  29.847  1.00 37.67 ? 273  GLY B O   1 
ATOM   4071 N N   . LYS B 1 274 ? -7.128  0.837   27.765  1.00 36.40 ? 274  LYS B N   1 
ATOM   4072 C CA  . LYS B 1 274 ? -5.763  0.330   27.492  1.00 38.28 ? 274  LYS B CA  1 
ATOM   4073 C C   . LYS B 1 274 ? -4.811  1.524   27.426  1.00 34.63 ? 274  LYS B C   1 
ATOM   4074 O O   . LYS B 1 274 ? -3.693  1.329   26.955  1.00 39.71 ? 274  LYS B O   1 
ATOM   4075 C CB  . LYS B 1 274 ? -5.780  -0.542  26.229  1.00 40.53 ? 274  LYS B CB  1 
ATOM   4076 C CG  . LYS B 1 274 ? -6.382  -1.930  26.421  1.00 39.81 ? 274  LYS B CG  1 
ATOM   4077 C CD  . LYS B 1 274 ? -6.774  -2.639  25.122  1.00 41.10 ? 274  LYS B CD  1 
ATOM   4078 C CE  . LYS B 1 274 ? -5.654  -2.786  24.102  1.00 42.50 ? 274  LYS B CE  1 
ATOM   4079 N NZ  . LYS B 1 274 ? -4.600  -3.754  24.508  1.00 40.72 ? 274  LYS B NZ  1 
ATOM   4080 N N   . GLY B 1 275 ? -5.260  2.700   27.885  1.00 29.99 ? 275  GLY B N   1 
ATOM   4081 C CA  . GLY B 1 275 ? -4.493  3.958   27.916  1.00 28.39 ? 275  GLY B CA  1 
ATOM   4082 C C   . GLY B 1 275 ? -3.187  3.789   28.661  1.00 27.80 ? 275  GLY B C   1 
ATOM   4083 O O   . GLY B 1 275 ? -2.200  4.412   28.255  1.00 28.25 ? 275  GLY B O   1 
ATOM   4084 N N   . GLY B 1 276 ? -3.175  2.956   29.709  1.00 27.56 ? 276  GLY B N   1 
ATOM   4085 C CA  . GLY B 1 276 ? -1.989  2.699   30.551  1.00 27.02 ? 276  GLY B CA  1 
ATOM   4086 C C   . GLY B 1 276 ? -0.999  1.776   29.867  1.00 26.58 ? 276  GLY B C   1 
ATOM   4087 O O   . GLY B 1 276 ? 0.113   1.658   30.340  1.00 25.14 ? 276  GLY B O   1 
ATOM   4088 N N   . GLU B 1 277 ? -1.393  1.132   28.773  1.00 28.60 ? 277  GLU B N   1 
ATOM   4089 C CA  . GLU B 1 277 ? -0.537  0.116   28.111  1.00 28.33 ? 277  GLU B CA  1 
ATOM   4090 C C   . GLU B 1 277 ? 0.528   0.782   27.224  1.00 24.99 ? 277  GLU B C   1 
ATOM   4091 O O   . GLU B 1 277 ? 0.434   1.981   26.908  1.00 25.80 ? 277  GLU B O   1 
ATOM   4092 C CB  . GLU B 1 277 ? -1.414  -0.859  27.337  1.00 29.39 ? 277  GLU B CB  1 
ATOM   4093 C CG  . GLU B 1 277 ? -2.340  -1.663  28.225  1.00 30.81 ? 277  GLU B CG  1 
ATOM   4094 C CD  . GLU B 1 277 ? -2.985  -2.823  27.490  1.00 35.76 ? 277  GLU B CD  1 
ATOM   4095 O OE1 . GLU B 1 277 ? -3.650  -3.631  28.140  1.00 42.33 ? 277  GLU B OE1 1 
ATOM   4096 O OE2 . GLU B 1 277 ? -2.820  -2.906  26.253  1.00 33.24 ? 277  GLU B OE2 1 
ATOM   4097 N N   . SER B 1 278 ? 1.545   0.001   26.884  1.00 26.14 ? 278  SER B N   1 
ATOM   4098 C CA  . SER B 1 278 ? 2.668   0.356   25.993  1.00 23.94 ? 278  SER B CA  1 
ATOM   4099 C C   . SER B 1 278 ? 2.213   0.239   24.542  1.00 24.62 ? 278  SER B C   1 
ATOM   4100 O O   . SER B 1 278 ? 1.065   -0.197  24.288  1.00 23.74 ? 278  SER B O   1 
ATOM   4101 C CB  . SER B 1 278 ? 3.836   -0.537  26.259  1.00 25.57 ? 278  SER B CB  1 
ATOM   4102 O OG  . SER B 1 278 ? 3.573   -1.837  25.741  1.00 25.39 ? 278  SER B OG  1 
ATOM   4103 N N   . ILE B 1 279 ? 3.089   0.633   23.616  1.00 27.09 ? 279  ILE B N   1 
ATOM   4104 C CA  . ILE B 1 279 ? 2.861   0.490   22.147  1.00 29.09 ? 279  ILE B CA  1 
ATOM   4105 C C   . ILE B 1 279 ? 2.517   -0.974  21.813  1.00 24.97 ? 279  ILE B C   1 
ATOM   4106 O O   . ILE B 1 279 ? 1.692   -1.185  20.917  1.00 25.02 ? 279  ILE B O   1 
ATOM   4107 C CB  . ILE B 1 279 ? 4.096   1.012   21.379  1.00 34.00 ? 279  ILE B CB  1 
ATOM   4108 C CG1 . ILE B 1 279 ? 3.710   1.452   19.970  1.00 37.39 ? 279  ILE B CG1 1 
ATOM   4109 C CG2 . ILE B 1 279 ? 5.219   -0.003  21.381  1.00 35.22 ? 279  ILE B CG2 1 
ATOM   4110 C CD1 . ILE B 1 279 ? 2.917   2.743   19.965  1.00 39.18 ? 279  ILE B CD1 1 
ATOM   4111 N N   . ALA B 1 280 ? 3.098   -1.959  22.513  1.00 23.62 ? 280  ALA B N   1 
ATOM   4112 C CA  . ALA B 1 280 ? 2.829   -3.402  22.298  1.00 23.71 ? 280  ALA B CA  1 
ATOM   4113 C C   . ALA B 1 280 ? 1.342   -3.698  22.476  1.00 24.52 ? 280  ALA B C   1 
ATOM   4114 O O   . ALA B 1 280 ? 0.872   -4.666  21.866  1.00 25.00 ? 280  ALA B O   1 
ATOM   4115 C CB  . ALA B 1 280 ? 3.627   -4.272  23.234  1.00 25.48 ? 280  ALA B CB  1 
ATOM   4116 N N   . GLY B 1 281 ? 0.636   -2.905  23.291  1.00 25.54 ? 281  GLY B N   1 
ATOM   4117 C CA  . GLY B 1 281 ? -0.810  -3.079  23.520  1.00 25.78 ? 281  GLY B CA  1 
ATOM   4118 C C   . GLY B 1 281 ? -1.645  -2.737  22.295  1.00 25.98 ? 281  GLY B C   1 
ATOM   4119 O O   . GLY B 1 281 ? -2.842  -3.024  22.300  1.00 26.65 ? 281  GLY B O   1 
ATOM   4120 N N   . LEU B 1 282 ? -1.066  -2.127  21.273  1.00 25.60 ? 282  LEU B N   1 
ATOM   4121 C CA  . LEU B 1 282 ? -1.787  -1.866  20.000  1.00 26.01 ? 282  LEU B CA  1 
ATOM   4122 C C   . LEU B 1 282 ? -1.874  -3.139  19.163  1.00 26.47 ? 282  LEU B C   1 
ATOM   4123 O O   . LEU B 1 282 ? -2.744  -3.182  18.284  1.00 25.43 ? 282  LEU B O   1 
ATOM   4124 C CB  . LEU B 1 282 ? -1.053  -0.788  19.204  1.00 27.09 ? 282  LEU B CB  1 
ATOM   4125 C CG  . LEU B 1 282 ? -1.089  0.615   19.800  1.00 26.55 ? 282  LEU B CG  1 
ATOM   4126 C CD1 . LEU B 1 282 ? -0.421  1.589   18.852  1.00 25.81 ? 282  LEU B CD1 1 
ATOM   4127 C CD2 . LEU B 1 282 ? -2.525  1.036   20.099  1.00 27.94 ? 282  LEU B CD2 1 
ATOM   4128 N N   . VAL B 1 283 ? -0.973  -4.111  19.334  1.00 24.48 ? 283  VAL B N   1 
ATOM   4129 C CA  . VAL B 1 283 ? -0.950  -5.242  18.363  1.00 26.99 ? 283  VAL B CA  1 
ATOM   4130 C C   . VAL B 1 283 ? -2.257  -6.037  18.481  1.00 27.81 ? 283  VAL B C   1 
ATOM   4131 O O   . VAL B 1 283 ? -2.850  -6.394  17.458  1.00 25.78 ? 283  VAL B O   1 
ATOM   4132 C CB  . VAL B 1 283 ? 0.321   -6.101  18.480  1.00 27.05 ? 283  VAL B CB  1 
ATOM   4133 C CG1 . VAL B 1 283 ? 0.193   -7.400  17.712  1.00 28.68 ? 283  VAL B CG1 1 
ATOM   4134 C CG2 . VAL B 1 283 ? 1.532   -5.324  18.004  1.00 27.84 ? 283  VAL B CG2 1 
ATOM   4135 N N   . PRO B 1 284 ? -2.767  -6.341  19.700  1.00 28.45 ? 284  PRO B N   1 
ATOM   4136 C CA  . PRO B 1 284 ? -4.052  -7.027  19.822  1.00 30.17 ? 284  PRO B CA  1 
ATOM   4137 C C   . PRO B 1 284 ? -5.248  -6.222  19.270  1.00 29.18 ? 284  PRO B C   1 
ATOM   4138 O O   . PRO B 1 284 ? -6.130  -6.835  18.732  1.00 32.99 ? 284  PRO B O   1 
ATOM   4139 C CB  . PRO B 1 284 ? -4.197  -7.327  21.323  1.00 31.77 ? 284  PRO B CB  1 
ATOM   4140 C CG  . PRO B 1 284 ? -2.822  -7.104  21.910  1.00 30.07 ? 284  PRO B CG  1 
ATOM   4141 C CD  . PRO B 1 284 ? -2.134  -6.109  21.007  1.00 28.41 ? 284  PRO B CD  1 
ATOM   4142 N N   . MET B 1 285 ? -5.222  -4.887  19.303  1.00 30.26 ? 285  MET B N   1 
ATOM   4143 C CA  . MET B 1 285 ? -6.242  -4.035  18.618  1.00 29.96 ? 285  MET B CA  1 
ATOM   4144 C C   . MET B 1 285 ? -6.391  -4.463  17.145  1.00 31.34 ? 285  MET B C   1 
ATOM   4145 O O   . MET B 1 285 ? -7.484  -4.281  16.589  1.00 31.89 ? 285  MET B O   1 
ATOM   4146 C CB  . MET B 1 285 ? -5.866  -2.549  18.634  1.00 34.46 ? 285  MET B CB  1 
ATOM   4147 C CG  . MET B 1 285 ? -5.550  -1.949  20.004  1.00 35.55 ? 285  MET B CG  1 
ATOM   4148 S SD  . MET B 1 285 ? -7.028  -1.624  20.940  1.00 39.69 ? 285  MET B SD  1 
ATOM   4149 C CE  . MET B 1 285 ? -7.767  -0.308  19.982  1.00 41.45 ? 285  MET B CE  1 
ATOM   4150 N N   . LEU B 1 286 ? -5.308  -4.932  16.499  1.00 33.42 ? 286  LEU B N   1 
ATOM   4151 C CA  . LEU B 1 286 ? -5.263  -5.229  15.039  1.00 32.26 ? 286  LEU B CA  1 
ATOM   4152 C C   . LEU B 1 286 ? -5.587  -6.710  14.798  1.00 31.88 ? 286  LEU B C   1 
ATOM   4153 O O   . LEU B 1 286 ? -6.301  -7.010  13.816  1.00 29.84 ? 286  LEU B O   1 
ATOM   4154 C CB  . LEU B 1 286 ? -3.885  -4.864  14.472  1.00 31.50 ? 286  LEU B CB  1 
ATOM   4155 C CG  . LEU B 1 286 ? -3.738  -3.458  13.894  1.00 32.81 ? 286  LEU B CG  1 
ATOM   4156 C CD1 . LEU B 1 286 ? -4.319  -2.404  14.811  1.00 36.03 ? 286  LEU B CD1 1 
ATOM   4157 C CD2 . LEU B 1 286 ? -2.285  -3.138  13.591  1.00 30.66 ? 286  LEU B CD2 1 
ATOM   4158 N N   . THR B 1 287 ? -5.075  -7.614  15.633  1.00 33.28 ? 287  THR B N   1 
ATOM   4159 C CA  . THR B 1 287 ? -5.206  -9.084  15.409  1.00 34.90 ? 287  THR B CA  1 
ATOM   4160 C C   . THR B 1 287 ? -6.664  -9.507  15.631  1.00 38.68 ? 287  THR B C   1 
ATOM   4161 O O   . THR B 1 287 ? -7.073  -10.522 15.023  1.00 41.84 ? 287  THR B O   1 
ATOM   4162 C CB  . THR B 1 287 ? -4.238  -9.896  16.276  1.00 32.11 ? 287  THR B CB  1 
ATOM   4163 O OG1 . THR B 1 287 ? -4.515  -9.639  17.649  1.00 33.43 ? 287  THR B OG1 1 
ATOM   4164 C CG2 . THR B 1 287 ? -2.790  -9.579  15.982  1.00 33.24 ? 287  THR B CG2 1 
ATOM   4165 N N   . GLU B 1 288 ? -7.412  -8.748  16.440  1.00 41.72 ? 288  GLU B N   1 
ATOM   4166 C CA  . GLU B 1 288 ? -8.795  -9.095  16.878  1.00 46.55 ? 288  GLU B CA  1 
ATOM   4167 C C   . GLU B 1 288 ? -9.811  -8.785  15.768  1.00 44.81 ? 288  GLU B C   1 
ATOM   4168 O O   . GLU B 1 288 ? -10.719 -9.580  15.578  1.00 45.97 ? 288  GLU B O   1 
ATOM   4169 C CB  . GLU B 1 288 ? -9.110  -8.383  18.191  1.00 48.70 ? 288  GLU B CB  1 
ATOM   4170 C CG  . GLU B 1 288 ? -8.414  -9.054  19.364  1.00 52.70 ? 288  GLU B CG  1 
ATOM   4171 C CD  . GLU B 1 288 ? -8.569  -8.396  20.727  1.00 55.04 ? 288  GLU B CD  1 
ATOM   4172 O OE1 . GLU B 1 288 ? -7.695  -8.641  21.601  1.00 48.06 ? 288  GLU B OE1 1 
ATOM   4173 O OE2 . GLU B 1 288 ? -9.557  -7.651  20.916  1.00 50.69 ? 288  GLU B OE2 1 
ATOM   4174 N N   . LEU B 1 289 ? -9.595  -7.728  14.991  1.00 43.42 ? 289  LEU B N   1 
ATOM   4175 C CA  . LEU B 1 289 ? -10.634 -7.121  14.132  1.00 42.13 ? 289  LEU B CA  1 
ATOM   4176 C C   . LEU B 1 289 ? -10.067 -6.746  12.761  1.00 42.91 ? 289  LEU B C   1 
ATOM   4177 O O   . LEU B 1 289 ? -9.089  -5.952  12.710  1.00 40.42 ? 289  LEU B O   1 
ATOM   4178 C CB  . LEU B 1 289 ? -11.145 -5.879  14.859  1.00 42.20 ? 289  LEU B CB  1 
ATOM   4179 C CG  . LEU B 1 289 ? -12.199 -5.068  14.113  1.00 42.41 ? 289  LEU B CG  1 
ATOM   4180 C CD1 . LEU B 1 289 ? -13.518 -5.844  13.989  1.00 38.93 ? 289  LEU B CD1 1 
ATOM   4181 C CD2 . LEU B 1 289 ? -12.409 -3.744  14.820  1.00 42.66 ? 289  LEU B CD2 1 
ATOM   4182 N N   . ASP B 1 290 ? -10.701 -7.260  11.702  1.00 41.48 ? 290  ASP B N   1 
ATOM   4183 C CA  . ASP B 1 290 ? -10.646 -6.704  10.327  1.00 43.62 ? 290  ASP B CA  1 
ATOM   4184 C C   . ASP B 1 290 ? -11.248 -5.291  10.348  1.00 41.93 ? 290  ASP B C   1 
ATOM   4185 O O   . ASP B 1 290 ? -12.477 -5.177  10.332  1.00 44.10 ? 290  ASP B O   1 
ATOM   4186 C CB  . ASP B 1 290 ? -11.387 -7.616  9.339   1.00 45.47 ? 290  ASP B CB  1 
ATOM   4187 C CG  . ASP B 1 290 ? -11.390 -7.091  7.913   1.00 45.66 ? 290  ASP B CG  1 
ATOM   4188 O OD1 . ASP B 1 290 ? -10.828 -6.008  7.687   1.00 45.23 ? 290  ASP B OD1 1 
ATOM   4189 O OD2 . ASP B 1 290 ? -11.940 -7.775  7.040   1.00 51.27 ? 290  ASP B OD2 1 
ATOM   4190 N N   . LYS B 1 291 ? -10.410 -4.254  10.383  1.00 42.79 ? 291  LYS B N   1 
ATOM   4191 C CA  . LYS B 1 291 ? -10.856 -2.837  10.333  1.00 40.28 ? 291  LYS B CA  1 
ATOM   4192 C C   . LYS B 1 291 ? -9.722  -1.949  9.811   1.00 42.48 ? 291  LYS B C   1 
ATOM   4193 O O   . LYS B 1 291 ? -8.555  -2.150  10.221  1.00 39.00 ? 291  LYS B O   1 
ATOM   4194 C CB  . LYS B 1 291 ? -11.314 -2.377  11.717  1.00 40.05 ? 291  LYS B CB  1 
ATOM   4195 C CG  . LYS B 1 291 ? -11.633 -0.892  11.813  1.00 44.98 ? 291  LYS B CG  1 
ATOM   4196 C CD  . LYS B 1 291 ? -11.901 -0.408  13.222  1.00 45.45 ? 291  LYS B CD  1 
ATOM   4197 C CE  . LYS B 1 291 ? -11.844 1.101   13.336  1.00 46.21 ? 291  LYS B CE  1 
ATOM   4198 N NZ  . LYS B 1 291 ? -12.453 1.559   14.607  1.00 46.72 ? 291  LYS B NZ  1 
ATOM   4199 N N   . LYS B 1 292 ? -10.069 -0.970  8.978   1.00 41.10 ? 292  LYS B N   1 
ATOM   4200 C CA  . LYS B 1 292 ? -9.146  0.085   8.494   1.00 42.84 ? 292  LYS B CA  1 
ATOM   4201 C C   . LYS B 1 292 ? -9.311  1.305   9.405   1.00 43.17 ? 292  LYS B C   1 
ATOM   4202 O O   . LYS B 1 292 ? -10.453 1.749   9.591   1.00 50.35 ? 292  LYS B O   1 
ATOM   4203 C CB  . LYS B 1 292 ? -9.421  0.356   7.013   1.00 42.39 ? 292  LYS B CB  1 
ATOM   4204 C CG  . LYS B 1 292 ? -9.401  -0.899  6.144   1.00 46.72 ? 292  LYS B CG  1 
ATOM   4205 C CD  . LYS B 1 292 ? -8.801  -0.686  4.776   1.00 50.05 ? 292  LYS B CD  1 
ATOM   4206 C CE  . LYS B 1 292 ? -9.464  0.439   4.005   1.00 53.44 ? 292  LYS B CE  1 
ATOM   4207 N NZ  . LYS B 1 292 ? -8.935  0.527   2.623   1.00 56.99 ? 292  LYS B NZ  1 
ATOM   4208 N N   . TRP B 1 293 ? -8.206  1.821   9.937   1.00 35.87 ? 293  TRP B N   1 
ATOM   4209 C CA  . TRP B 1 293 ? -8.160  2.760   11.085  1.00 34.46 ? 293  TRP B CA  1 
ATOM   4210 C C   . TRP B 1 293 ? -7.873  4.182   10.596  1.00 31.87 ? 293  TRP B C   1 
ATOM   4211 O O   . TRP B 1 293 ? -7.175  4.184   9.571   1.00 33.79 ? 293  TRP B O   1 
ATOM   4212 C CB  . TRP B 1 293 ? -7.088  2.274   12.068  1.00 33.43 ? 293  TRP B CB  1 
ATOM   4213 C CG  . TRP B 1 293 ? -7.468  1.048   12.839  1.00 32.30 ? 293  TRP B CG  1 
ATOM   4214 C CD1 . TRP B 1 293 ? -7.213  -0.255  12.512  1.00 34.82 ? 293  TRP B CD1 1 
ATOM   4215 C CD2 . TRP B 1 293 ? -8.174  1.006   14.088  1.00 31.87 ? 293  TRP B CD2 1 
ATOM   4216 N NE1 . TRP B 1 293 ? -7.727  -1.101  13.460  1.00 32.60 ? 293  TRP B NE1 1 
ATOM   4217 C CE2 . TRP B 1 293 ? -8.311  -0.354  14.443  1.00 30.15 ? 293  TRP B CE2 1 
ATOM   4218 C CE3 . TRP B 1 293 ? -8.705  1.985   14.934  1.00 32.35 ? 293  TRP B CE3 1 
ATOM   4219 C CZ2 . TRP B 1 293 ? -8.943  -0.756  15.612  1.00 30.36 ? 293  TRP B CZ2 1 
ATOM   4220 C CZ3 . TRP B 1 293 ? -9.342  1.583   16.083  1.00 31.88 ? 293  TRP B CZ3 1 
ATOM   4221 C CH2 . TRP B 1 293 ? -9.459  0.232   16.417  1.00 30.82 ? 293  TRP B CH2 1 
HETATM 4222 C C1  . PEG C 2 .   ? 9.192   8.869   23.736  1.00 56.23 ? 2901 PEG A C1  1 
HETATM 4223 O O1  . PEG C 2 .   ? 10.022  9.995   23.497  1.00 55.96 ? 2901 PEG A O1  1 
HETATM 4224 C C2  . PEG C 2 .   ? 9.975   7.583   23.756  1.00 55.66 ? 2901 PEG A C2  1 
HETATM 4225 O O2  . PEG C 2 .   ? 9.268   6.600   24.513  1.00 55.56 ? 2901 PEG A O2  1 
HETATM 4226 C C3  . PEG C 2 .   ? 8.641   5.572   23.740  1.00 53.02 ? 2901 PEG A C3  1 
HETATM 4227 C C4  . PEG C 2 .   ? 9.145   4.215   24.179  1.00 54.69 ? 2901 PEG A C4  1 
HETATM 4228 O O4  . PEG C 2 .   ? 8.228   3.162   23.907  1.00 52.97 ? 2901 PEG A O4  1 
HETATM 4229 P PA  . NAP D 3 .   ? 2.191   10.586  32.764  1.00 25.79 ? 2902 NAP A PA  1 
HETATM 4230 O O1A . NAP D 3 .   ? 0.829   10.548  32.161  1.00 24.25 ? 2902 NAP A O1A 1 
HETATM 4231 O O2A . NAP D 3 .   ? 2.809   9.366   33.395  1.00 25.47 ? 2902 NAP A O2A 1 
HETATM 4232 O O5B . NAP D 3 .   ? 2.177   11.752  33.812  1.00 24.89 ? 2902 NAP A O5B 1 
HETATM 4233 C C5B . NAP D 3 .   ? 1.517   12.955  33.452  1.00 25.68 ? 2902 NAP A C5B 1 
HETATM 4234 C C4B . NAP D 3 .   ? 1.662   14.048  34.498  1.00 25.98 ? 2902 NAP A C4B 1 
HETATM 4235 O O4B . NAP D 3 .   ? 0.674   15.054  34.152  1.00 26.00 ? 2902 NAP A O4B 1 
HETATM 4236 C C3B . NAP D 3 .   ? 1.369   13.564  35.920  1.00 24.38 ? 2902 NAP A C3B 1 
HETATM 4237 O O3B . NAP D 3 .   ? 2.152   14.298  36.847  1.00 22.31 ? 2902 NAP A O3B 1 
HETATM 4238 C C2B . NAP D 3 .   ? -0.113  13.894  36.071  1.00 25.10 ? 2902 NAP A C2B 1 
HETATM 4239 O O2B . NAP D 3 .   ? -0.615  13.936  37.415  1.00 25.15 ? 2902 NAP A O2B 1 
HETATM 4240 C C1B . NAP D 3 .   ? -0.128  15.221  35.337  1.00 25.32 ? 2902 NAP A C1B 1 
HETATM 4241 N N9A . NAP D 3 .   ? -1.473  15.583  34.959  1.00 25.39 ? 2902 NAP A N9A 1 
HETATM 4242 C C8A . NAP D 3 .   ? -2.212  15.054  33.963  1.00 26.52 ? 2902 NAP A C8A 1 
HETATM 4243 N N7A . NAP D 3 .   ? -3.435  15.634  33.887  1.00 24.57 ? 2902 NAP A N7A 1 
HETATM 4244 C C5A . NAP D 3 .   ? -3.441  16.557  34.848  1.00 25.84 ? 2902 NAP A C5A 1 
HETATM 4245 C C6A . NAP D 3 .   ? -4.420  17.541  35.296  1.00 25.51 ? 2902 NAP A C6A 1 
HETATM 4246 N N6A . NAP D 3 .   ? -5.579  17.577  34.649  1.00 26.11 ? 2902 NAP A N6A 1 
HETATM 4247 N N1A . NAP D 3 .   ? -4.083  18.365  36.291  1.00 25.11 ? 2902 NAP A N1A 1 
HETATM 4248 C C2A . NAP D 3 .   ? -2.884  18.265  36.908  1.00 26.53 ? 2902 NAP A C2A 1 
HETATM 4249 N N3A . NAP D 3 .   ? -1.919  17.378  36.547  1.00 27.26 ? 2902 NAP A N3A 1 
HETATM 4250 C C4A . NAP D 3 .   ? -2.161  16.525  35.549  1.00 25.52 ? 2902 NAP A C4A 1 
HETATM 4251 O O3  . NAP D 3 .   ? 3.142   11.116  31.567  1.00 25.86 ? 2902 NAP A O3  1 
HETATM 4252 P PN  . NAP D 3 .   ? 4.755   11.279  31.662  1.00 20.81 ? 2902 NAP A PN  1 
HETATM 4253 O O1N . NAP D 3 .   ? 5.334   10.123  30.896  1.00 22.34 ? 2902 NAP A O1N 1 
HETATM 4254 O O2N . NAP D 3 .   ? 5.267   11.683  33.031  1.00 20.05 ? 2902 NAP A O2N 1 
HETATM 4255 O O5D . NAP D 3 .   ? 5.035   12.469  30.628  1.00 21.98 ? 2902 NAP A O5D 1 
HETATM 4256 C C5D . NAP D 3 .   ? 5.146   13.851  31.033  1.00 22.49 ? 2902 NAP A C5D 1 
HETATM 4257 C C4D . NAP D 3 .   ? 5.739   14.624  29.864  1.00 21.14 ? 2902 NAP A C4D 1 
HETATM 4258 O O4D . NAP D 3 .   ? 7.004   14.021  29.559  1.00 23.13 ? 2902 NAP A O4D 1 
HETATM 4259 C C3D . NAP D 3 .   ? 4.863   14.486  28.628  1.00 21.55 ? 2902 NAP A C3D 1 
HETATM 4260 O O3D . NAP D 3 .   ? 4.628   15.711  27.925  1.00 19.51 ? 2902 NAP A O3D 1 
HETATM 4261 C C2D . NAP D 3 .   ? 5.644   13.515  27.783  1.00 21.88 ? 2902 NAP A C2D 1 
HETATM 4262 O O2D . NAP D 3 .   ? 5.413   13.628  26.391  1.00 21.13 ? 2902 NAP A O2D 1 
HETATM 4263 C C1D . NAP D 3 .   ? 7.098   13.741  28.155  1.00 22.97 ? 2902 NAP A C1D 1 
HETATM 4264 N N1N . NAP D 3 .   ? 7.909   12.550  27.824  1.00 23.92 ? 2902 NAP A N1N 1 
HETATM 4265 C C2N . NAP D 3 .   ? 7.555   11.340  28.319  1.00 23.40 ? 2902 NAP A C2N 1 
HETATM 4266 C C3N . NAP D 3 .   ? 8.270   10.207  28.013  1.00 22.44 ? 2902 NAP A C3N 1 
HETATM 4267 C C7N . NAP D 3 .   ? 7.867   8.885   28.566  1.00 21.91 ? 2902 NAP A C7N 1 
HETATM 4268 O O7N . NAP D 3 .   ? 7.205   8.746   29.619  1.00 21.95 ? 2902 NAP A O7N 1 
HETATM 4269 N N7N . NAP D 3 .   ? 8.259   7.862   27.850  1.00 20.15 ? 2902 NAP A N7N 1 
HETATM 4270 C C4N . NAP D 3 .   ? 9.370   10.321  27.168  1.00 23.99 ? 2902 NAP A C4N 1 
HETATM 4271 C C5N . NAP D 3 .   ? 9.732   11.559  26.673  1.00 23.95 ? 2902 NAP A C5N 1 
HETATM 4272 C C6N . NAP D 3 .   ? 8.981   12.677  27.018  1.00 24.34 ? 2902 NAP A C6N 1 
HETATM 4273 P P2B . NAP D 3 .   ? -1.141  12.573  38.221  1.00 26.15 ? 2902 NAP A P2B 1 
HETATM 4274 O O1X . NAP D 3 .   ? 0.046   11.784  38.691  1.00 24.11 ? 2902 NAP A O1X 1 
HETATM 4275 O O2X . NAP D 3 .   ? -1.879  13.182  39.366  1.00 22.09 ? 2902 NAP A O2X 1 
HETATM 4276 O O3X . NAP D 3 .   ? -1.888  11.762  37.223  1.00 22.61 ? 2902 NAP A O3X 1 
HETATM 4277 C C1  . PEG E 2 .   ? 10.975  -1.138  -1.600  1.00 47.77 ? 3601 PEG B C1  1 
HETATM 4278 O O1  . PEG E 2 .   ? 9.817   -0.575  -2.219  1.00 43.81 ? 3601 PEG B O1  1 
HETATM 4279 C C2  . PEG E 2 .   ? 12.117  -0.156  -1.441  1.00 47.65 ? 3601 PEG B C2  1 
HETATM 4280 O O2  . PEG E 2 .   ? 11.721  1.150   -1.858  1.00 49.83 ? 3601 PEG B O2  1 
HETATM 4281 C C3  . PEG E 2 .   ? 12.732  2.141   -1.677  1.00 47.51 ? 3601 PEG B C3  1 
HETATM 4282 C C4  . PEG E 2 .   ? 12.114  3.504   -1.650  1.00 48.87 ? 3601 PEG B C4  1 
HETATM 4283 O O4  . PEG E 2 .   ? 13.079  4.539   -1.627  1.00 50.44 ? 3601 PEG B O4  1 
HETATM 4284 P PA  . NAP F 3 .   ? 7.095   -0.126  -12.448 1.00 26.35 ? 3602 NAP B PA  1 
HETATM 4285 O O1A . NAP F 3 .   ? 5.753   0.422   -12.184 1.00 28.27 ? 3602 NAP B O1A 1 
HETATM 4286 O O2A . NAP F 3 .   ? 8.367   0.656   -12.715 1.00 24.70 ? 3602 NAP B O2A 1 
HETATM 4287 O O5B . NAP F 3 .   ? 6.853   -1.221  -13.560 1.00 26.82 ? 3602 NAP B O5B 1 
HETATM 4288 C C5B . NAP F 3 .   ? 5.643   -1.975  -13.608 1.00 26.70 ? 3602 NAP B C5B 1 
HETATM 4289 C C4B . NAP F 3 .   ? 5.783   -3.074  -14.663 1.00 25.05 ? 3602 NAP B C4B 1 
HETATM 4290 O O4B . NAP F 3 .   ? 4.528   -3.758  -14.827 1.00 25.31 ? 3602 NAP B O4B 1 
HETATM 4291 C C3B . NAP F 3 .   ? 6.144   -2.521  -16.025 1.00 24.85 ? 3602 NAP B C3B 1 
HETATM 4292 O O3B . NAP F 3 .   ? 6.866   -3.484  -16.780 1.00 22.19 ? 3602 NAP B O3B 1 
HETATM 4293 C C2B . NAP F 3 .   ? 4.773   -2.298  -16.637 1.00 25.46 ? 3602 NAP B C2B 1 
HETATM 4294 O O2B . NAP F 3 .   ? 4.744   -2.279  -18.060 1.00 24.33 ? 3602 NAP B O2B 1 
HETATM 4295 C C1B . NAP F 3 .   ? 4.059   -3.504  -16.134 1.00 25.58 ? 3602 NAP B C1B 1 
HETATM 4296 N N9A . NAP F 3 .   ? 2.632   -3.260  -16.145 1.00 28.15 ? 3602 NAP B N9A 1 
HETATM 4297 C C8A . NAP F 3 .   ? 1.936   -2.383  -15.371 1.00 26.76 ? 3602 NAP B C8A 1 
HETATM 4298 N N7A . NAP F 3 .   ? 0.625   -2.494  -15.688 1.00 26.82 ? 3602 NAP B N7A 1 
HETATM 4299 C C5A . NAP F 3 .   ? 0.510   -3.426  -16.676 1.00 27.89 ? 3602 NAP B C5A 1 
HETATM 4300 C C6A . NAP F 3 .   ? -0.585  -4.003  -17.463 1.00 29.78 ? 3602 NAP B C6A 1 
HETATM 4301 N N6A . NAP F 3 .   ? -1.814  -3.567  -17.187 1.00 31.85 ? 3602 NAP B N6A 1 
HETATM 4302 N N1A . NAP F 3 .   ? -0.319  -4.952  -18.382 1.00 29.78 ? 3602 NAP B N1A 1 
HETATM 4303 C C2A . NAP F 3 .   ? 0.961   -5.381  -18.622 1.00 29.56 ? 3602 NAP B C2A 1 
HETATM 4304 N N3A . NAP F 3 .   ? 2.014   -4.872  -17.935 1.00 28.09 ? 3602 NAP B N3A 1 
HETATM 4305 C C4A . NAP F 3 .   ? 1.831   -3.929  -16.987 1.00 26.33 ? 3602 NAP B C4A 1 
HETATM 4306 O O3  . NAP F 3 .   ? 7.283   -0.927  -11.066 1.00 25.55 ? 3602 NAP B O3  1 
HETATM 4307 P PN  . NAP F 3 .   ? 8.649   -1.658  -10.707 1.00 20.88 ? 3602 NAP B PN  1 
HETATM 4308 O O1N . NAP F 3 .   ? 9.325   -0.666  -9.834  1.00 23.38 ? 3602 NAP B O1N 1 
HETATM 4309 O O2N . NAP F 3 .   ? 9.262   -2.365  -11.901 1.00 21.92 ? 3602 NAP B O2N 1 
HETATM 4310 O O5D . NAP F 3 .   ? 8.079   -2.777  -9.704  1.00 20.49 ? 3602 NAP B O5D 1 
HETATM 4311 C C5D . NAP F 3 .   ? 8.039   -4.147  -10.090 1.00 20.00 ? 3602 NAP B C5D 1 
HETATM 4312 C C4D . NAP F 3 .   ? 7.710   -5.023  -8.919  1.00 19.47 ? 3602 NAP B C4D 1 
HETATM 4313 O O4D . NAP F 3 .   ? 8.877   -5.052  -8.089  1.00 20.86 ? 3602 NAP B O4D 1 
HETATM 4314 C C3D . NAP F 3 .   ? 6.564   -4.483  -8.081  1.00 20.82 ? 3602 NAP B C3D 1 
HETATM 4315 O O3D . NAP F 3 .   ? 5.726   -5.552  -7.630  1.00 20.76 ? 3602 NAP B O3D 1 
HETATM 4316 C C2D . NAP F 3 .   ? 7.307   -3.838  -6.927  1.00 20.41 ? 3602 NAP B C2D 1 
HETATM 4317 O O2D . NAP F 3 .   ? 6.580   -3.828  -5.745  1.00 22.66 ? 3602 NAP B O2D 1 
HETATM 4318 C C1D . NAP F 3 .   ? 8.571   -4.642  -6.764  1.00 20.09 ? 3602 NAP B C1D 1 
HETATM 4319 N N1N . NAP F 3 .   ? 9.656   -3.825  -6.175  1.00 22.02 ? 3602 NAP B N1N 1 
HETATM 4320 C C2N . NAP F 3 .   ? 9.931   -2.587  -6.606  1.00 20.90 ? 3602 NAP B C2N 1 
HETATM 4321 C C3N . NAP F 3 .   ? 10.914  -1.831  -5.965  1.00 24.08 ? 3602 NAP B C3N 1 
HETATM 4322 C C7N . NAP F 3 .   ? 11.249  -0.436  -6.392  1.00 24.33 ? 3602 NAP B C7N 1 
HETATM 4323 O O7N . NAP F 3 .   ? 11.900  0.240   -5.626  1.00 25.07 ? 3602 NAP B O7N 1 
HETATM 4324 N N7N . NAP F 3 .   ? 10.878  0.007   -7.596  1.00 24.01 ? 3602 NAP B N7N 1 
HETATM 4325 C C4N . NAP F 3 .   ? 11.620  -2.372  -4.895  1.00 23.32 ? 3602 NAP B C4N 1 
HETATM 4326 C C5N . NAP F 3 .   ? 11.319  -3.663  -4.496  1.00 22.27 ? 3602 NAP B C5N 1 
HETATM 4327 C C6N . NAP F 3 .   ? 10.341  -4.369  -5.143  1.00 21.04 ? 3602 NAP B C6N 1 
HETATM 4328 P P2B . NAP F 3 .   ? 5.132   -0.911  -18.847 1.00 24.64 ? 3602 NAP B P2B 1 
HETATM 4329 O O1X . NAP F 3 .   ? 4.591   -1.252  -20.207 1.00 24.37 ? 3602 NAP B O1X 1 
HETATM 4330 O O2X . NAP F 3 .   ? 4.425   0.223   -18.132 1.00 24.48 ? 3602 NAP B O2X 1 
HETATM 4331 O O3X . NAP F 3 .   ? 6.641   -0.713  -18.785 1.00 23.26 ? 3602 NAP B O3X 1 
HETATM 4332 O O   . HOH G 4 .   ? 6.841   7.277   44.392  1.00 33.60 ? 3001 HOH A O   1 
HETATM 4333 O O   . HOH G 4 .   ? 3.720   23.639  50.971  1.00 45.94 ? 3002 HOH A O   1 
HETATM 4334 O O   . HOH G 4 .   ? -0.519  2.531   -7.623  1.00 26.52 ? 3003 HOH A O   1 
HETATM 4335 O O   . HOH G 4 .   ? -6.884  10.301  -0.609  1.00 32.34 ? 3004 HOH A O   1 
HETATM 4336 O O   . HOH G 4 .   ? 19.636  15.234  46.694  1.00 43.10 ? 3005 HOH A O   1 
HETATM 4337 O O   . HOH G 4 .   ? 4.710   5.808   -11.662 1.00 32.35 ? 3006 HOH A O   1 
HETATM 4338 O O   . HOH G 4 .   ? 13.155  32.351  43.948  1.00 40.54 ? 3007 HOH A O   1 
HETATM 4339 O O   . HOH G 4 .   ? -7.944  -5.501  0.747   1.00 43.03 ? 3008 HOH A O   1 
HETATM 4340 O O   . HOH G 4 .   ? 0.838   32.558  28.189  1.00 31.32 ? 3009 HOH A O   1 
HETATM 4341 O O   . HOH G 4 .   ? 10.354  -18.728 14.014  1.00 36.50 ? 3010 HOH A O   1 
HETATM 4342 O O   . HOH G 4 .   ? -7.678  22.482  25.023  1.00 37.96 ? 3011 HOH A O   1 
HETATM 4343 O O   . HOH G 4 .   ? 24.086  19.288  30.987  1.00 29.72 ? 3012 HOH A O   1 
HETATM 4344 O O   . HOH G 4 .   ? 6.067   17.996  -8.414  1.00 34.33 ? 3013 HOH A O   1 
HETATM 4345 O O   . HOH G 4 .   ? 10.772  19.151  -1.628  1.00 34.38 ? 3014 HOH A O   1 
HETATM 4346 O O   . HOH G 4 .   ? -4.704  26.321  28.379  1.00 42.93 ? 3015 HOH A O   1 
HETATM 4347 O O   . HOH G 4 .   ? 2.984   13.397  25.953  1.00 21.88 ? 3016 HOH A O   1 
HETATM 4348 O O   . HOH G 4 .   ? 14.301  32.404  28.260  1.00 31.54 ? 3017 HOH A O   1 
HETATM 4349 O O   . HOH G 4 .   ? 9.147   6.590   36.303  1.00 23.50 ? 3018 HOH A O   1 
HETATM 4350 O O   . HOH G 4 .   ? 5.542   13.484  34.746  1.00 15.53 ? 3019 HOH A O   1 
HETATM 4351 O O   . HOH G 4 .   ? -1.385  27.299  40.469  1.00 41.40 ? 3020 HOH A O   1 
HETATM 4352 O O   . HOH G 4 .   ? 13.907  11.787  -5.032  1.00 34.07 ? 3021 HOH A O   1 
HETATM 4353 O O   . HOH G 4 .   ? 10.240  8.677   -8.916  1.00 38.05 ? 3022 HOH A O   1 
HETATM 4354 O O   . HOH G 4 .   ? 1.278   -13.668 18.909  1.00 34.84 ? 3023 HOH A O   1 
HETATM 4355 O O   . HOH G 4 .   ? 19.238  -9.401  13.370  1.00 37.10 ? 3024 HOH A O   1 
HETATM 4356 O O   . HOH G 4 .   ? 19.065  13.603  28.854  1.00 36.32 ? 3025 HOH A O   1 
HETATM 4357 O O   . HOH G 4 .   ? 9.282   18.916  25.844  1.00 18.72 ? 3026 HOH A O   1 
HETATM 4358 O O   . HOH G 4 .   ? -3.620  9.934   37.682  1.00 37.66 ? 3027 HOH A O   1 
HETATM 4359 O O   . HOH G 4 .   ? 0.071   10.565  -11.355 1.00 33.88 ? 3028 HOH A O   1 
HETATM 4360 O O   . HOH G 4 .   ? 10.264  31.778  20.024  1.00 38.51 ? 3029 HOH A O   1 
HETATM 4361 O O   . HOH G 4 .   ? 14.777  -14.819 12.452  1.00 36.61 ? 3030 HOH A O   1 
HETATM 4362 O O   . HOH G 4 .   ? 2.382   -16.244 16.177  1.00 30.83 ? 3031 HOH A O   1 
HETATM 4363 O O   . HOH G 4 .   ? -5.155  15.189  31.989  1.00 32.17 ? 3032 HOH A O   1 
HETATM 4364 O O   . HOH G 4 .   ? 21.305  25.198  38.045  1.00 34.63 ? 3033 HOH A O   1 
HETATM 4365 O O   . HOH G 4 .   ? 10.517  24.365  22.721  1.00 21.22 ? 3034 HOH A O   1 
HETATM 4366 O O   . HOH G 4 .   ? 20.529  6.836   26.066  1.00 47.08 ? 3035 HOH A O   1 
HETATM 4367 O O   . HOH G 4 .   ? 22.099  5.443   34.917  1.00 39.08 ? 3036 HOH A O   1 
HETATM 4368 O O   . HOH G 4 .   ? -5.377  7.908   -7.110  1.00 40.55 ? 3037 HOH A O   1 
HETATM 4369 O O   . HOH G 4 .   ? 23.188  24.316  36.913  1.00 33.62 ? 3038 HOH A O   1 
HETATM 4370 O O   . HOH G 4 .   ? -3.873  17.751  27.825  1.00 38.65 ? 3039 HOH A O   1 
HETATM 4371 O O   . HOH G 4 .   ? 18.658  25.864  41.890  1.00 25.67 ? 3040 HOH A O   1 
HETATM 4372 O O   . HOH G 4 .   ? 5.013   30.783  44.828  1.00 37.77 ? 3041 HOH A O   1 
HETATM 4373 O O   . HOH G 4 .   ? -1.592  18.418  3.237   1.00 30.72 ? 3042 HOH A O   1 
HETATM 4374 O O   . HOH G 4 .   ? 7.808   4.491   34.793  1.00 32.15 ? 3043 HOH A O   1 
HETATM 4375 O O   . HOH G 4 .   ? 9.790   13.739  23.590  1.00 26.52 ? 3044 HOH A O   1 
HETATM 4376 O O   . HOH G 4 .   ? 14.377  4.516   -5.681  1.00 45.14 ? 3045 HOH A O   1 
HETATM 4377 O O   . HOH G 4 .   ? -0.694  28.199  47.408  1.00 32.64 ? 3046 HOH A O   1 
HETATM 4378 O O   . HOH G 4 .   ? 15.544  16.596  48.767  1.00 32.37 ? 3047 HOH A O   1 
HETATM 4379 O O   . HOH G 4 .   ? 8.259   19.594  23.334  1.00 20.89 ? 3048 HOH A O   1 
HETATM 4380 O O   . HOH G 4 .   ? -1.551  28.813  20.136  1.00 33.93 ? 3049 HOH A O   1 
HETATM 4381 O O   . HOH G 4 .   ? 2.770   -5.325  -0.015  1.00 16.91 ? 3050 HOH A O   1 
HETATM 4382 O O   . HOH G 4 .   ? -2.979  21.557  38.241  1.00 31.10 ? 3051 HOH A O   1 
HETATM 4383 O O   . HOH G 4 .   ? 15.995  7.030   34.910  1.00 21.13 ? 3052 HOH A O   1 
HETATM 4384 O O   . HOH G 4 .   ? 21.467  12.102  38.373  1.00 37.21 ? 3053 HOH A O   1 
HETATM 4385 O O   . HOH G 4 .   ? 3.633   -15.576 18.864  1.00 37.62 ? 3054 HOH A O   1 
HETATM 4386 O O   . HOH G 4 .   ? 10.587  22.950  50.433  1.00 45.66 ? 3055 HOH A O   1 
HETATM 4387 O O   . HOH G 4 .   ? 1.647   -10.295 16.994  1.00 21.70 ? 3056 HOH A O   1 
HETATM 4388 O O   . HOH G 4 .   ? 13.805  22.578  47.148  1.00 32.99 ? 3057 HOH A O   1 
HETATM 4389 O O   . HOH G 4 .   ? 8.855   15.834  24.924  1.00 26.64 ? 3058 HOH A O   1 
HETATM 4390 O O   . HOH G 4 .   ? 8.643   -17.176 12.891  1.00 43.15 ? 3059 HOH A O   1 
HETATM 4391 O O   . HOH G 4 .   ? 1.170   37.482  38.751  1.00 39.16 ? 3060 HOH A O   1 
HETATM 4392 O O   . HOH G 4 .   ? 4.845   22.246  26.423  1.00 25.20 ? 3061 HOH A O   1 
HETATM 4393 O O   . HOH G 4 .   ? -4.189  24.993  3.728   1.00 42.76 ? 3062 HOH A O   1 
HETATM 4394 O O   . HOH G 4 .   ? -2.062  25.232  22.359  1.00 37.49 ? 3063 HOH A O   1 
HETATM 4395 O O   . HOH G 4 .   ? 1.375   8.518   35.524  1.00 32.10 ? 3064 HOH A O   1 
HETATM 4396 O O   . HOH G 4 .   ? 14.739  -10.237 17.864  1.00 38.79 ? 3065 HOH A O   1 
HETATM 4397 O O   . HOH G 4 .   ? -2.477  -12.993 3.985   1.00 34.39 ? 3066 HOH A O   1 
HETATM 4398 O O   . HOH G 4 .   ? 0.382   6.635   43.446  1.00 33.72 ? 3067 HOH A O   1 
HETATM 4399 O O   . HOH G 4 .   ? 1.906   15.950  25.464  1.00 16.54 ? 3068 HOH A O   1 
HETATM 4400 O O   . HOH G 4 .   ? 11.640  7.711   -12.584 1.00 32.48 ? 3069 HOH A O   1 
HETATM 4401 O O   . HOH G 4 .   ? -5.242  12.770  42.051  1.00 37.48 ? 3070 HOH A O   1 
HETATM 4402 O O   . HOH G 4 .   ? 2.431   7.721   37.852  1.00 33.73 ? 3071 HOH A O   1 
HETATM 4403 O O   . HOH G 4 .   ? 10.365  6.975   50.416  1.00 38.19 ? 3072 HOH A O   1 
HETATM 4404 O O   . HOH G 4 .   ? 4.538   16.230  19.980  1.00 18.11 ? 3073 HOH A O   1 
HETATM 4405 O O   . HOH G 4 .   ? 6.042   23.085  23.883  1.00 19.30 ? 3074 HOH A O   1 
HETATM 4406 O O   . HOH G 4 .   ? 4.293   34.280  19.624  1.00 45.11 ? 3075 HOH A O   1 
HETATM 4407 O O   . HOH G 4 .   ? 2.372   18.699  51.228  1.00 35.56 ? 3076 HOH A O   1 
HETATM 4408 O O   . HOH G 4 .   ? 13.695  6.698   38.524  1.00 34.21 ? 3077 HOH A O   1 
HETATM 4409 O O   . HOH G 4 .   ? 4.736   11.826  -11.848 1.00 35.90 ? 3078 HOH A O   1 
HETATM 4410 O O   . HOH G 4 .   ? 26.555  20.723  48.786  1.00 50.06 ? 3079 HOH A O   1 
HETATM 4411 O O   . HOH G 4 .   ? -3.181  34.312  38.389  1.00 47.57 ? 3080 HOH A O   1 
HETATM 4412 O O   . HOH G 4 .   ? -1.854  6.746   9.185   1.00 23.52 ? 3081 HOH A O   1 
HETATM 4413 O O   . HOH G 4 .   ? -1.997  -17.454 14.809  1.00 39.24 ? 3082 HOH A O   1 
HETATM 4414 O O   . HOH G 4 .   ? 1.251   20.173  25.149  1.00 18.08 ? 3083 HOH A O   1 
HETATM 4415 O O   . HOH G 4 .   ? 25.822  25.139  34.901  1.00 37.53 ? 3084 HOH A O   1 
HETATM 4416 O O   . HOH G 4 .   ? 17.589  9.052   43.419  1.00 40.27 ? 3085 HOH A O   1 
HETATM 4417 O O   . HOH G 4 .   ? -4.708  17.523  43.946  1.00 44.97 ? 3086 HOH A O   1 
HETATM 4418 O O   . HOH G 4 .   ? 18.155  29.413  39.134  1.00 41.29 ? 3087 HOH A O   1 
HETATM 4419 O O   . HOH G 4 .   ? 5.564   33.012  17.934  1.00 43.85 ? 3088 HOH A O   1 
HETATM 4420 O O   . HOH G 4 .   ? 13.145  10.259  -2.438  1.00 31.23 ? 3089 HOH A O   1 
HETATM 4421 O O   . HOH G 4 .   ? 22.745  1.223   13.429  1.00 45.77 ? 3090 HOH A O   1 
HETATM 4422 O O   . HOH G 4 .   ? -1.560  17.107  45.519  1.00 36.18 ? 3091 HOH A O   1 
HETATM 4423 O O   . HOH G 4 .   ? 4.110   23.168  29.096  1.00 21.61 ? 3092 HOH A O   1 
HETATM 4424 O O   . HOH G 4 .   ? 20.348  29.849  18.095  1.00 39.34 ? 3093 HOH A O   1 
HETATM 4425 O O   . HOH G 4 .   ? -1.705  18.698  -1.084  1.00 32.03 ? 3094 HOH A O   1 
HETATM 4426 O O   . HOH G 4 .   ? -7.485  4.623   3.458   1.00 38.78 ? 3095 HOH A O   1 
HETATM 4427 O O   . HOH G 4 .   ? 4.629   8.112   38.639  1.00 25.87 ? 3096 HOH A O   1 
HETATM 4428 O O   . HOH G 4 .   ? 3.156   32.510  43.676  1.00 37.96 ? 3097 HOH A O   1 
HETATM 4429 O O   . HOH G 4 .   ? 22.251  14.442  20.162  1.00 46.98 ? 3098 HOH A O   1 
HETATM 4430 O O   . HOH G 4 .   ? 18.666  8.438   47.551  1.00 41.74 ? 3099 HOH A O   1 
HETATM 4431 O O   . HOH G 4 .   ? 0.516   16.931  38.413  1.00 28.81 ? 3100 HOH A O   1 
HETATM 4432 O O   . HOH G 4 .   ? 10.271  15.877  27.232  1.00 24.56 ? 3101 HOH A O   1 
HETATM 4433 O O   . HOH G 4 .   ? -2.519  10.528  45.468  1.00 35.07 ? 3102 HOH A O   1 
HETATM 4434 O O   . HOH G 4 .   ? -7.623  16.867  37.815  1.00 37.92 ? 3103 HOH A O   1 
HETATM 4435 O O   . HOH G 4 .   ? -0.669  27.073  43.503  1.00 35.38 ? 3104 HOH A O   1 
HETATM 4436 O O   . HOH G 4 .   ? 10.665  6.806   -3.324  1.00 20.81 ? 3105 HOH A O   1 
HETATM 4437 O O   . HOH G 4 .   ? 11.366  7.118   -7.120  1.00 28.19 ? 3106 HOH A O   1 
HETATM 4438 O O   . HOH G 4 .   ? -6.035  2.118   7.446   1.00 27.28 ? 3107 HOH A O   1 
HETATM 4439 O O   . HOH G 4 .   ? -2.148  7.802   37.495  1.00 33.11 ? 3108 HOH A O   1 
HETATM 4440 O O   . HOH G 4 .   ? 7.225   12.471  24.403  1.00 37.74 ? 3109 HOH A O   1 
HETATM 4441 O O   . HOH G 4 .   ? 20.885  4.589   26.814  1.00 41.08 ? 3110 HOH A O   1 
HETATM 4442 O O   . HOH G 4 .   ? 24.900  21.703  23.941  1.00 33.37 ? 3111 HOH A O   1 
HETATM 4443 O O   . HOH G 4 .   ? 10.808  3.639   31.144  1.00 22.35 ? 3112 HOH A O   1 
HETATM 4444 O O   . HOH G 4 .   ? 15.277  13.820  -9.191  1.00 44.37 ? 3113 HOH A O   1 
HETATM 4445 O O   . HOH G 4 .   ? 15.658  8.045   37.080  1.00 20.98 ? 3114 HOH A O   1 
HETATM 4446 O O   . HOH G 4 .   ? -6.250  -2.825  -0.957  1.00 46.27 ? 3115 HOH A O   1 
HETATM 4447 O O   . HOH G 4 .   ? 5.765   -17.831 18.958  1.00 42.05 ? 3116 HOH A O   1 
HETATM 4448 O O   . HOH G 4 .   ? -2.352  21.087  25.703  1.00 25.89 ? 3117 HOH A O   1 
HETATM 4449 O O   . HOH G 4 .   ? 12.643  16.143  -9.940  1.00 27.40 ? 3118 HOH A O   1 
HETATM 4450 O O   . HOH G 4 .   ? 14.754  24.080  0.082   1.00 45.08 ? 3119 HOH A O   1 
HETATM 4451 O O   . HOH G 4 .   ? -3.416  14.072  46.130  1.00 33.69 ? 3120 HOH A O   1 
HETATM 4452 O O   . HOH G 4 .   ? -10.099 -11.785 13.336  1.00 46.93 ? 3121 HOH A O   1 
HETATM 4453 O O   . HOH G 4 .   ? -8.672  17.924  7.469   1.00 40.92 ? 3122 HOH A O   1 
HETATM 4454 O O   . HOH G 4 .   ? 19.126  28.176  16.018  1.00 45.34 ? 3123 HOH A O   1 
HETATM 4455 O O   . HOH G 4 .   ? 25.539  6.099   29.164  1.00 43.77 ? 3124 HOH A O   1 
HETATM 4456 O O   . HOH G 4 .   ? 6.886   4.480   47.962  1.00 40.43 ? 3125 HOH A O   1 
HETATM 4457 O O   . HOH G 4 .   ? 9.640   -15.019 11.448  1.00 43.26 ? 3126 HOH A O   1 
HETATM 4458 O O   . HOH G 4 .   ? 1.346   13.330  -14.814 1.00 40.05 ? 3127 HOH A O   1 
HETATM 4459 O O   . HOH G 4 .   ? 1.478   18.683  -4.225  1.00 47.62 ? 3128 HOH A O   1 
HETATM 4460 O O   . HOH G 4 .   ? 7.446   0.314   25.049  1.00 39.28 ? 3129 HOH A O   1 
HETATM 4461 O O   . HOH G 4 .   ? 1.868   17.095  46.112  1.00 48.10 ? 3130 HOH A O   1 
HETATM 4462 O O   . HOH G 4 .   ? 12.237  4.228   47.539  1.00 46.16 ? 3131 HOH A O   1 
HETATM 4463 O O   . HOH G 4 .   ? -2.080  11.957  32.507  1.00 30.78 ? 3132 HOH A O   1 
HETATM 4464 O O   . HOH G 4 .   ? 5.159   8.985   18.847  1.00 34.34 ? 3133 HOH A O   1 
HETATM 4465 O O   . HOH G 4 .   ? 20.509  9.354   37.481  1.00 39.82 ? 3134 HOH A O   1 
HETATM 4466 O O   . HOH G 4 .   ? -7.971  -3.945  4.824   1.00 39.11 ? 3135 HOH A O   1 
HETATM 4467 O O   . HOH G 4 .   ? -3.787  17.783  -1.891  1.00 39.73 ? 3136 HOH A O   1 
HETATM 4468 O O   . HOH G 4 .   ? 6.257   19.335  -5.788  1.00 37.10 ? 3137 HOH A O   1 
HETATM 4469 O O   . HOH G 4 .   ? 0.429   27.212  1.831   1.00 39.12 ? 3138 HOH A O   1 
HETATM 4470 O O   . HOH G 4 .   ? -6.428  18.902  30.485  1.00 36.35 ? 3139 HOH A O   1 
HETATM 4471 O O   . HOH G 4 .   ? 20.467  3.854   38.208  1.00 44.85 ? 3140 HOH A O   1 
HETATM 4472 O O   . HOH G 4 .   ? 20.344  15.154  -2.618  1.00 31.61 ? 3141 HOH A O   1 
HETATM 4473 O O   . HOH G 4 .   ? 17.953  7.952   38.696  1.00 38.13 ? 3142 HOH A O   1 
HETATM 4474 O O   . HOH G 4 .   ? -2.510  -13.179 16.597  1.00 35.70 ? 3143 HOH A O   1 
HETATM 4475 O O   . HOH G 4 .   ? -6.982  7.995   7.088   1.00 34.36 ? 3144 HOH A O   1 
HETATM 4476 O O   . HOH G 4 .   ? -4.358  19.233  39.895  1.00 41.81 ? 3145 HOH A O   1 
HETATM 4477 O O   . HOH G 4 .   ? -3.240  21.108  20.803  1.00 46.10 ? 3146 HOH A O   1 
HETATM 4478 O O   . HOH G 4 .   ? 16.925  3.763   -10.285 1.00 26.76 ? 3147 HOH A O   1 
HETATM 4479 O O   . HOH G 4 .   ? -0.485  -10.990 17.799  1.00 36.62 ? 3148 HOH A O   1 
HETATM 4480 O O   . HOH G 4 .   ? 6.893   12.098  -12.528 1.00 41.25 ? 3149 HOH A O   1 
HETATM 4481 O O   . HOH G 4 .   ? 11.232  34.540  30.869  1.00 30.28 ? 3150 HOH A O   1 
HETATM 4482 O O   . HOH G 4 .   ? -7.772  11.800  3.590   1.00 44.56 ? 3151 HOH A O   1 
HETATM 4483 O O   . HOH G 4 .   ? 22.825  -2.263  12.633  1.00 47.61 ? 3152 HOH A O   1 
HETATM 4484 O O   . HOH G 4 .   ? 10.904  33.190  22.015  1.00 37.73 ? 3153 HOH A O   1 
HETATM 4485 O O   . HOH G 4 .   ? -2.438  -18.255 8.339   1.00 43.34 ? 3154 HOH A O   1 
HETATM 4486 O O   . HOH G 4 .   ? 7.254   22.700  -2.174  1.00 44.60 ? 3155 HOH A O   1 
HETATM 4487 O O   . HOH G 4 .   ? 20.329  27.469  42.909  1.00 37.54 ? 3156 HOH A O   1 
HETATM 4488 O O   . HOH G 4 .   ? -3.350  23.055  40.484  1.00 38.64 ? 3157 HOH A O   1 
HETATM 4489 O O   . HOH G 4 .   ? 4.156   32.282  46.819  1.00 42.31 ? 3158 HOH A O   1 
HETATM 4490 O O   . HOH G 4 .   ? -0.620  -19.405 15.651  1.00 45.15 ? 3159 HOH A O   1 
HETATM 4491 O O   . HOH G 4 .   ? -10.746 12.174  -1.454  1.00 43.49 ? 3160 HOH A O   1 
HETATM 4492 O O   . HOH G 4 .   ? 5.558   10.255  22.832  1.00 33.93 ? 3161 HOH A O   1 
HETATM 4493 O O   . HOH G 4 .   ? 9.278   21.632  -8.298  1.00 43.47 ? 3162 HOH A O   1 
HETATM 4494 O O   . HOH G 4 .   ? 8.215   37.270  22.885  1.00 39.65 ? 3163 HOH A O   1 
HETATM 4495 O O   . HOH H 4 .   ? 4.334   -13.169 -32.369 1.00 42.99 ? 3701 HOH B O   1 
HETATM 4496 O O   . HOH H 4 .   ? 3.624   -23.989 -9.211  1.00 30.65 ? 3702 HOH B O   1 
HETATM 4497 O O   . HOH H 4 .   ? 24.743  -11.635 -21.027 1.00 43.22 ? 3703 HOH B O   1 
HETATM 4498 O O   . HOH H 4 .   ? 3.814   -28.596 -24.674 1.00 33.07 ? 3704 HOH B O   1 
HETATM 4499 O O   . HOH H 4 .   ? -7.004  12.722  21.735  1.00 36.17 ? 3705 HOH B O   1 
HETATM 4500 O O   . HOH H 4 .   ? 5.099   -3.205  26.982  1.00 28.74 ? 3706 HOH B O   1 
HETATM 4501 O O   . HOH H 4 .   ? 3.937   2.319   -19.199 1.00 34.82 ? 3707 HOH B O   1 
HETATM 4502 O O   . HOH H 4 .   ? 17.030  -16.399 -23.298 1.00 26.56 ? 3708 HOH B O   1 
HETATM 4503 O O   . HOH H 4 .   ? -4.622  -5.793  27.664  1.00 34.78 ? 3709 HOH B O   1 
HETATM 4504 O O   . HOH H 4 .   ? -2.186  18.744  24.324  1.00 33.18 ? 3710 HOH B O   1 
HETATM 4505 O O   . HOH H 4 .   ? 9.404   -4.100  -13.610 1.00 17.68 ? 3711 HOH B O   1 
HETATM 4506 O O   . HOH H 4 .   ? -7.761  3.756   28.764  1.00 34.14 ? 3712 HOH B O   1 
HETATM 4507 O O   . HOH H 4 .   ? 10.089  -27.763 5.596   1.00 42.26 ? 3713 HOH B O   1 
HETATM 4508 O O   . HOH H 4 .   ? -12.834 -0.189  16.314  1.00 35.69 ? 3714 HOH B O   1 
HETATM 4509 O O   . HOH H 4 .   ? 16.056  0.437   -22.275 1.00 51.25 ? 3715 HOH B O   1 
HETATM 4510 O O   . HOH H 4 .   ? -12.220 5.380   19.728  1.00 39.96 ? 3716 HOH B O   1 
HETATM 4511 O O   . HOH H 4 .   ? 6.281   -22.377 -23.342 1.00 29.09 ? 3717 HOH B O   1 
HETATM 4512 O O   . HOH H 4 .   ? 5.213   -5.240  -25.936 1.00 29.24 ? 3718 HOH B O   1 
HETATM 4513 O O   . HOH H 4 .   ? -5.142  15.383  15.849  1.00 43.21 ? 3719 HOH B O   1 
HETATM 4514 O O   . HOH H 4 .   ? 21.231  -2.399  -10.008 1.00 25.93 ? 3720 HOH B O   1 
HETATM 4515 O O   . HOH H 4 .   ? -4.017  -28.402 -16.056 1.00 38.52 ? 3721 HOH B O   1 
HETATM 4516 O O   . HOH H 4 .   ? 19.204  -13.245 -26.249 1.00 33.84 ? 3722 HOH B O   1 
HETATM 4517 O O   . HOH H 4 .   ? -8.415  -3.883  14.015  1.00 28.70 ? 3723 HOH B O   1 
HETATM 4518 O O   . HOH H 4 .   ? 10.781  20.019  3.772   1.00 32.33 ? 3724 HOH B O   1 
HETATM 4519 O O   . HOH H 4 .   ? 14.949  23.773  2.903   1.00 42.60 ? 3725 HOH B O   1 
HETATM 4520 O O   . HOH H 4 .   ? 9.306   -13.370 -30.383 1.00 38.83 ? 3726 HOH B O   1 
HETATM 4521 O O   . HOH H 4 .   ? 4.550   -2.300  -6.016  1.00 35.75 ? 3727 HOH B O   1 
HETATM 4522 O O   . HOH H 4 .   ? -4.684  16.872  23.119  1.00 42.19 ? 3728 HOH B O   1 
HETATM 4523 O O   . HOH H 4 .   ? 18.583  -20.510 -17.073 1.00 39.92 ? 3729 HOH B O   1 
HETATM 4524 O O   . HOH H 4 .   ? 21.782  -16.216 -4.503  1.00 37.61 ? 3730 HOH B O   1 
HETATM 4525 O O   . HOH H 4 .   ? 8.295   -21.734 7.203   1.00 37.67 ? 3731 HOH B O   1 
HETATM 4526 O O   . HOH H 4 .   ? 7.191   -7.581  31.978  1.00 34.44 ? 3732 HOH B O   1 
HETATM 4527 O O   . HOH H 4 .   ? 24.258  12.010  12.429  1.00 37.97 ? 3733 HOH B O   1 
HETATM 4528 O O   . HOH H 4 .   ? 3.601   -25.592 -26.803 1.00 49.71 ? 3734 HOH B O   1 
HETATM 4529 O O   . HOH H 4 .   ? 7.667   -10.264 -4.290  1.00 19.46 ? 3735 HOH B O   1 
HETATM 4530 O O   . HOH H 4 .   ? 5.559   -15.535 -1.293  1.00 20.76 ? 3736 HOH B O   1 
HETATM 4531 O O   . HOH H 4 .   ? 13.475  25.173  4.981   1.00 37.64 ? 3737 HOH B O   1 
HETATM 4532 O O   . HOH H 4 .   ? 26.229  -8.052  -22.847 1.00 39.22 ? 3738 HOH B O   1 
HETATM 4533 O O   . HOH H 4 .   ? 2.419   29.595  10.226  1.00 28.31 ? 3739 HOH B O   1 
HETATM 4534 O O   . HOH H 4 .   ? -9.786  -3.926  17.788  1.00 35.63 ? 3740 HOH B O   1 
HETATM 4535 O O   . HOH H 4 .   ? 16.203  -23.870 -14.940 1.00 39.52 ? 3741 HOH B O   1 
HETATM 4536 O O   . HOH H 4 .   ? 22.461  -22.650 -7.925  1.00 43.73 ? 3742 HOH B O   1 
HETATM 4537 O O   . HOH H 4 .   ? 19.160  -9.263  -3.701  1.00 29.21 ? 3743 HOH B O   1 
HETATM 4538 O O   . HOH H 4 .   ? 22.420  2.044   18.219  1.00 46.27 ? 3744 HOH B O   1 
HETATM 4539 O O   . HOH H 4 .   ? 9.465   -5.577  -1.619  1.00 22.40 ? 3745 HOH B O   1 
HETATM 4540 O O   . HOH H 4 .   ? 5.469   -20.340 -23.919 1.00 43.04 ? 3746 HOH B O   1 
HETATM 4541 O O   . HOH H 4 .   ? 1.230   -6.676  30.655  1.00 24.12 ? 3747 HOH B O   1 
HETATM 4542 O O   . HOH H 4 .   ? 15.869  0.578   -13.565 1.00 24.99 ? 3748 HOH B O   1 
HETATM 4543 O O   . HOH H 4 .   ? -4.192  11.129  25.439  1.00 35.65 ? 3749 HOH B O   1 
HETATM 4544 O O   . HOH H 4 .   ? 0.536   -8.899  22.117  1.00 28.58 ? 3750 HOH B O   1 
HETATM 4545 O O   . HOH H 4 .   ? 12.181  0.710   -17.344 1.00 40.00 ? 3751 HOH B O   1 
HETATM 4546 O O   . HOH H 4 .   ? -1.338  26.453  19.007  1.00 29.75 ? 3752 HOH B O   1 
HETATM 4547 O O   . HOH H 4 .   ? 5.501   1.388   -16.007 1.00 31.10 ? 3753 HOH B O   1 
HETATM 4548 O O   . HOH H 4 .   ? -8.241  -5.418  7.653   1.00 30.79 ? 3754 HOH B O   1 
HETATM 4549 O O   . HOH H 4 .   ? 18.774  0.566   -28.508 1.00 30.63 ? 3755 HOH B O   1 
HETATM 4550 O O   . HOH H 4 .   ? 22.517  -2.987  -0.646  1.00 37.39 ? 3756 HOH B O   1 
HETATM 4551 O O   . HOH H 4 .   ? 19.089  -12.244 5.118   1.00 44.33 ? 3757 HOH B O   1 
HETATM 4552 O O   . HOH H 4 .   ? -11.266 -1.809  18.105  1.00 39.29 ? 3758 HOH B O   1 
HETATM 4553 O O   . HOH H 4 .   ? -4.853  0.892   30.608  1.00 31.82 ? 3759 HOH B O   1 
HETATM 4554 O O   . HOH H 4 .   ? -6.457  23.459  17.107  1.00 43.46 ? 3760 HOH B O   1 
HETATM 4555 O O   . HOH H 4 .   ? 7.873   1.801   -15.075 1.00 27.31 ? 3761 HOH B O   1 
HETATM 4556 O O   . HOH H 4 .   ? 27.709  -16.360 -8.731  1.00 43.12 ? 3762 HOH B O   1 
HETATM 4557 O O   . HOH H 4 .   ? 2.718   1.159   29.828  1.00 30.28 ? 3763 HOH B O   1 
HETATM 4558 O O   . HOH H 4 .   ? 10.126  -8.082  -5.037  1.00 18.50 ? 3764 HOH B O   1 
HETATM 4559 O O   . HOH H 4 .   ? -2.127  6.388   31.275  1.00 43.38 ? 3765 HOH B O   1 
HETATM 4560 O O   . HOH H 4 .   ? 5.638   -10.276 -2.371  1.00 20.19 ? 3766 HOH B O   1 
HETATM 4561 O O   . HOH H 4 .   ? -3.962  12.711  9.687   1.00 36.73 ? 3767 HOH B O   1 
HETATM 4562 O O   . HOH H 4 .   ? 22.670  -16.715 0.068   1.00 45.92 ? 3768 HOH B O   1 
HETATM 4563 O O   . HOH H 4 .   ? 27.415  -4.787  -1.149  1.00 39.84 ? 3769 HOH B O   1 
HETATM 4564 O O   . HOH H 4 .   ? -4.670  20.564  16.063  1.00 41.58 ? 3770 HOH B O   1 
HETATM 4565 O O   . HOH H 4 .   ? 20.960  -3.342  -12.415 1.00 31.00 ? 3771 HOH B O   1 
HETATM 4566 O O   . HOH H 4 .   ? 8.420   -6.257  -25.335 1.00 31.19 ? 3772 HOH B O   1 
HETATM 4567 O O   . HOH H 4 .   ? 21.545  -11.728 -23.495 1.00 33.49 ? 3773 HOH B O   1 
HETATM 4568 O O   . HOH H 4 .   ? -3.563  19.561  12.193  1.00 39.50 ? 3774 HOH B O   1 
HETATM 4569 O O   . HOH H 4 .   ? 14.285  -24.727 -15.926 1.00 43.57 ? 3775 HOH B O   1 
HETATM 4570 O O   . HOH H 4 .   ? 8.232   -7.108  -3.414  1.00 26.44 ? 3776 HOH B O   1 
HETATM 4571 O O   . HOH H 4 .   ? 14.146  3.014   -23.943 1.00 44.46 ? 3777 HOH B O   1 
HETATM 4572 O O   . HOH H 4 .   ? 24.729  -5.126  -17.295 1.00 40.73 ? 3778 HOH B O   1 
HETATM 4573 O O   . HOH H 4 .   ? 4.966   -5.534  -19.031 1.00 20.69 ? 3779 HOH B O   1 
HETATM 4574 O O   . HOH H 4 .   ? 2.581   -4.268  -6.000  1.00 19.96 ? 3780 HOH B O   1 
HETATM 4575 O O   . HOH H 4 .   ? 6.355   -30.351 -11.456 1.00 34.93 ? 3781 HOH B O   1 
HETATM 4576 O O   . HOH H 4 .   ? -12.645 3.126   10.636  1.00 45.69 ? 3782 HOH B O   1 
HETATM 4577 O O   . HOH H 4 .   ? 2.776   -14.936 21.606  1.00 46.98 ? 3783 HOH B O   1 
HETATM 4578 O O   . HOH H 4 .   ? 10.602  -17.896 7.947   1.00 37.58 ? 3784 HOH B O   1 
HETATM 4579 O O   . HOH H 4 .   ? 6.693   -26.121 -22.996 1.00 40.45 ? 3785 HOH B O   1 
HETATM 4580 O O   . HOH H 4 .   ? -1.760  0.640   -17.473 1.00 38.29 ? 3786 HOH B O   1 
HETATM 4581 O O   . HOH H 4 .   ? -0.544  -13.830 -22.529 1.00 36.79 ? 3787 HOH B O   1 
HETATM 4582 O O   . HOH H 4 .   ? 2.345   -4.932  -25.648 1.00 39.60 ? 3788 HOH B O   1 
HETATM 4583 O O   . HOH H 4 .   ? 14.810  -16.688 7.392   1.00 41.30 ? 3789 HOH B O   1 
HETATM 4584 O O   . HOH H 4 .   ? 24.786  -3.584  -7.930  1.00 45.24 ? 3790 HOH B O   1 
HETATM 4585 O O   . HOH H 4 .   ? 2.584   -12.596 -3.861  1.00 18.08 ? 3791 HOH B O   1 
HETATM 4586 O O   . HOH H 4 .   ? 4.210   -23.967 -0.738  1.00 31.13 ? 3792 HOH B O   1 
HETATM 4587 O O   . HOH H 4 .   ? -2.124  -15.476 4.610   1.00 35.60 ? 3793 HOH B O   1 
HETATM 4588 O O   . HOH H 4 .   ? 0.607   1.768   -16.522 1.00 40.12 ? 3794 HOH B O   1 
HETATM 4589 O O   . HOH H 4 .   ? 23.229  0.700   10.804  1.00 44.35 ? 3795 HOH B O   1 
HETATM 4590 O O   . HOH H 4 .   ? 2.359   -12.035 -9.267  1.00 26.72 ? 3796 HOH B O   1 
HETATM 4591 O O   . HOH H 4 .   ? -4.641  -19.905 -9.480  1.00 31.84 ? 3797 HOH B O   1 
HETATM 4592 O O   . HOH H 4 .   ? 4.604   24.802  15.032  1.00 25.46 ? 3798 HOH B O   1 
HETATM 4593 O O   . HOH H 4 .   ? -11.647 4.111   15.663  1.00 46.35 ? 3799 HOH B O   1 
HETATM 4594 O O   . HOH H 4 .   ? 14.972  3.140   -12.431 1.00 33.11 ? 3800 HOH B O   1 
HETATM 4595 O O   . HOH H 4 .   ? 0.063   -7.933  -6.184  1.00 24.63 ? 3801 HOH B O   1 
HETATM 4596 O O   . HOH H 4 .   ? -4.268  -22.541 -15.453 1.00 39.98 ? 3802 HOH B O   1 
HETATM 4597 O O   . HOH H 4 .   ? -7.754  -14.048 -10.112 1.00 43.06 ? 3803 HOH B O   1 
HETATM 4598 O O   . HOH H 4 .   ? 2.591   -11.470 -6.686  1.00 26.84 ? 3804 HOH B O   1 
HETATM 4599 O O   . HOH H 4 .   ? 4.861   -5.427  31.143  1.00 35.69 ? 3805 HOH B O   1 
HETATM 4600 O O   . HOH H 4 .   ? 19.374  -18.838 2.201   1.00 48.35 ? 3806 HOH B O   1 
HETATM 4601 O O   . HOH H 4 .   ? 19.156  -5.697  2.020   1.00 31.03 ? 3807 HOH B O   1 
HETATM 4602 O O   . HOH H 4 .   ? 7.071   0.931   -26.230 1.00 36.10 ? 3808 HOH B O   1 
HETATM 4603 O O   . HOH H 4 .   ? -6.086  -9.225  -10.145 1.00 50.63 ? 3809 HOH B O   1 
HETATM 4604 O O   . HOH H 4 .   ? 21.960  14.384  6.474   1.00 36.71 ? 3810 HOH B O   1 
HETATM 4605 O O   . HOH H 4 .   ? -5.962  -11.106 -5.482  1.00 33.84 ? 3811 HOH B O   1 
HETATM 4606 O O   . HOH H 4 .   ? 8.110   -2.166  29.437  1.00 45.70 ? 3812 HOH B O   1 
HETATM 4607 O O   . HOH H 4 .   ? 4.733   1.877   28.416  1.00 21.83 ? 3813 HOH B O   1 
HETATM 4608 O O   . HOH H 4 .   ? 5.348   2.274   24.676  1.00 23.23 ? 3814 HOH B O   1 
HETATM 4609 O O   . HOH H 4 .   ? 17.502  -13.214 10.866  1.00 36.78 ? 3815 HOH B O   1 
HETATM 4610 O O   . HOH H 4 .   ? 2.398   -21.013 -23.948 1.00 39.26 ? 3816 HOH B O   1 
HETATM 4611 O O   . HOH H 4 .   ? 16.591  2.974   -7.738  1.00 28.59 ? 3817 HOH B O   1 
HETATM 4612 O O   . HOH H 4 .   ? 6.208   -1.976  24.320  1.00 36.40 ? 3818 HOH B O   1 
HETATM 4613 O O   . HOH H 4 .   ? -3.115  -7.527  -7.893  1.00 23.31 ? 3819 HOH B O   1 
HETATM 4614 O O   . HOH H 4 .   ? -4.621  -6.761  24.891  1.00 42.50 ? 3820 HOH B O   1 
HETATM 4615 O O   . HOH H 4 .   ? 3.616   7.251   19.061  1.00 35.88 ? 3821 HOH B O   1 
HETATM 4616 O O   . HOH H 4 .   ? 6.022   1.003   2.072   1.00 34.27 ? 3822 HOH B O   1 
HETATM 4617 O O   . HOH H 4 .   ? -6.358  15.582  25.932  1.00 43.85 ? 3823 HOH B O   1 
HETATM 4618 O O   . HOH H 4 .   ? 14.156  -23.159 -23.110 1.00 32.62 ? 3824 HOH B O   1 
HETATM 4619 O O   . HOH H 4 .   ? 5.018   -26.277 -10.497 1.00 42.74 ? 3825 HOH B O   1 
HETATM 4620 O O   . HOH H 4 .   ? 18.430  3.640   23.187  1.00 40.09 ? 3826 HOH B O   1 
HETATM 4621 O O   . HOH H 4 .   ? 1.187   -14.447 -24.792 1.00 39.97 ? 3827 HOH B O   1 
HETATM 4622 O O   . HOH H 4 .   ? -6.124  -16.891 -13.204 1.00 45.10 ? 3828 HOH B O   1 
HETATM 4623 O O   . HOH H 4 .   ? 7.893   -25.908 -6.955  1.00 40.74 ? 3829 HOH B O   1 
HETATM 4624 O O   . HOH H 4 .   ? -2.156  -2.683  -21.048 1.00 35.68 ? 3830 HOH B O   1 
HETATM 4625 O O   . HOH H 4 .   ? -7.262  7.359   9.381   1.00 35.30 ? 3831 HOH B O   1 
HETATM 4626 O O   . HOH H 4 .   ? -8.416  27.381  15.855  1.00 38.55 ? 3832 HOH B O   1 
HETATM 4627 O O   . HOH H 4 .   ? 4.234   9.924   20.643  1.00 37.84 ? 3833 HOH B O   1 
HETATM 4628 O O   . HOH H 4 .   ? 1.495   -15.594 -28.156 1.00 47.87 ? 3834 HOH B O   1 
HETATM 4629 O O   . HOH H 4 .   ? 3.026   -6.943  -26.386 1.00 37.50 ? 3835 HOH B O   1 
HETATM 4630 O O   . HOH H 4 .   ? 8.158   -23.766 -24.360 1.00 43.01 ? 3836 HOH B O   1 
HETATM 4631 O O   . HOH H 4 .   ? 21.178  -15.027 3.300   1.00 45.16 ? 3837 HOH B O   1 
HETATM 4632 O O   . HOH H 4 .   ? 20.407  -1.237  -13.837 1.00 27.17 ? 3838 HOH B O   1 
HETATM 4633 O O   . HOH H 4 .   ? 15.155  -0.572  28.085  1.00 41.23 ? 3839 HOH B O   1 
HETATM 4634 O O   . HOH H 4 .   ? 18.672  3.026   -24.898 1.00 33.59 ? 3840 HOH B O   1 
HETATM 4635 O O   . HOH H 4 .   ? 1.014   2.397   -20.401 1.00 43.73 ? 3841 HOH B O   1 
HETATM 4636 O O   . HOH H 4 .   ? 14.696  -15.830 -28.038 1.00 42.14 ? 3842 HOH B O   1 
HETATM 4637 O O   . HOH H 4 .   ? 24.292  14.281  15.474  1.00 48.17 ? 3843 HOH B O   1 
HETATM 4638 O O   . HOH H 4 .   ? -4.484  5.400   31.818  1.00 39.04 ? 3844 HOH B O   1 
HETATM 4639 O O   . HOH H 4 .   ? 6.487   -30.347 -23.277 1.00 48.60 ? 3845 HOH B O   1 
HETATM 4640 O O   . HOH H 4 .   ? 6.537   -13.160 -34.014 1.00 44.33 ? 3846 HOH B O   1 
HETATM 4641 O O   . HOH H 4 .   ? 1.457   -17.140 4.768   1.00 44.66 ? 3847 HOH B O   1 
HETATM 4642 O O   . HOH H 4 .   ? 18.662  -4.352  19.156  1.00 45.46 ? 3848 HOH B O   1 
HETATM 4643 O O   . HOH H 4 .   ? 10.355  -9.510  25.965  1.00 39.40 ? 3849 HOH B O   1 
HETATM 4644 O O   . HOH H 4 .   ? 13.008  -10.268 22.557  1.00 41.16 ? 3850 HOH B O   1 
HETATM 4645 O O   . HOH H 4 .   ? -4.599  -23.362 -3.955  1.00 44.97 ? 3851 HOH B O   1 
HETATM 4646 O O   . HOH H 4 .   ? 13.971  1.906   -15.445 1.00 38.38 ? 3852 HOH B O   1 
HETATM 4647 O O   . HOH H 4 .   ? -0.509  -20.030 2.242   1.00 41.79 ? 3853 HOH B O   1 
HETATM 4648 O O   . HOH H 4 .   ? 23.801  -23.255 -19.517 1.00 33.89 ? 3854 HOH B O   1 
HETATM 4649 O O   . HOH H 4 .   ? -12.129 -1.288  2.210   1.00 44.70 ? 3855 HOH B O   1 
HETATM 4650 O O   . HOH H 4 .   ? 17.427  -29.081 -0.952  1.00 39.11 ? 3856 HOH B O   1 
HETATM 4651 O O   . HOH H 4 .   ? -11.985 2.045   30.690  1.00 41.81 ? 3857 HOH B O   1 
HETATM 4652 O O   . HOH H 4 .   ? 9.723   2.932   33.417  1.00 26.56 ? 3858 HOH B O   1 
HETATM 4653 O O   . HOH H 4 .   ? -9.014  9.162   23.372  1.00 41.22 ? 3859 HOH B O   1 
HETATM 4654 O O   . HOH H 4 .   ? 9.295   22.126  2.716   1.00 41.45 ? 3860 HOH B O   1 
HETATM 4655 O O   . HOH H 4 .   ? 1.195   -25.315 -5.934  1.00 44.15 ? 3861 HOH B O   1 
HETATM 4656 O O   . HOH H 4 .   ? 8.480   -9.156  27.721  1.00 43.73 ? 3862 HOH B O   1 
HETATM 4657 O O   . HOH H 4 .   ? -11.800 -12.319 18.383  1.00 42.82 ? 3863 HOH B O   1 
HETATM 4658 O O   . HOH H 4 .   ? 8.634   4.945   -15.090 1.00 40.33 ? 3864 HOH B O   1 
HETATM 4659 O O   . HOH H 4 .   ? 2.505   -11.618 -32.061 1.00 44.72 ? 3865 HOH B O   1 
HETATM 4660 O O   . HOH H 4 .   ? -0.278  -9.786  -22.485 1.00 38.95 ? 3866 HOH B O   1 
HETATM 4661 O O   . HOH H 4 .   ? -13.195 7.105   21.189  1.00 34.16 ? 3867 HOH B O   1 
HETATM 4662 O O   . HOH H 4 .   ? -3.080  -0.747  32.345  1.00 35.49 ? 3868 HOH B O   1 
HETATM 4663 O O   . HOH H 4 .   ? 7.377   29.822  4.249   1.00 38.71 ? 3869 HOH B O   1 
HETATM 4664 O O   . HOH H 4 .   ? 9.795   -0.735  31.146  1.00 36.07 ? 3870 HOH B O   1 
HETATM 4665 O O   . HOH H 4 .   ? 20.818  -12.897 3.747   1.00 44.17 ? 3871 HOH B O   1 
HETATM 4666 O O   . HOH H 4 .   ? 27.602  -2.226  -30.449 1.00 47.01 ? 3872 HOH B O   1 
HETATM 4667 O O   . HOH H 4 .   ? 7.596   -28.865 -3.907  1.00 43.66 ? 3873 HOH B O   1 
# 
