data_9B2F
# 
_entry.id   9B2F 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9B2F         pdb_00009b2f 10.2210/pdb9b2f/pdb 
WWPDB D_1000282202 ?            ?                   
# 
_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       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B2F 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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_database_related.content_type   unspecified 
_pdbx_database_related.db_id          9B2G 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'same protein in complex with NADH' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              sveta@lsu.edu 
_pdbx_contact_author.name_first         Svetlana 
_pdbx_contact_author.name_last          Pakhomova 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6729-2560 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Pakhomova, S.'    1 ? 
'Belyaeva, O.V.'   2 ? 
'Boeglin, W.E.'    3 ? 
'Kedishvili, N.Y.' 4 ? 
'Brash, A.R.'      5 ? 
'Newcomer, M.E.'   6 ? 
'Popov, K.M.'      7 ? 
# 
_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                     
;The large substrate binding pocket of dehydrogenase reductase 9 underlies its ability to oxidize diverse pro-inflammatory and pro-resolving oxylipins.
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Pakhomova, S.'    1 ? 
primary 'Belyaeva, O.V.'   2 ? 
primary 'Boeglin, W.E.'    3 ? 
primary 'Kedishvili, N.Y.' 4 ? 
primary 'Brash, A.R.'      5 ? 
primary 'Newcomer, M.E.'   6 ? 
primary 'Popov, K.M.'      7 ? 
# 
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 'Dehydrogenase/reductase SDR family member 9' 35289.121 1   1.1.1.209,1.1.1.53,1.1.1.105 ? ? ? 
2 non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE             663.425   1   ?                            ? ? ? 
3 non-polymer syn 'MALONATE ION'                                102.046   1   ?                            ? ? ? 
4 water       nat water                                         18.015    143 ?                            ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'3-alpha hydroxysteroid dehydrogenase,3-alpha-HSD,Retinol dehydrogenase,Short-chain dehydrogenase/reductase retSDR8' 
# 
_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       
;MLFWLLALLFLCAFLWNYKGQLKIADIADKYVFITGCDTGFGNLAARTFDKKGFRVIAACLTESGSAALKAKTSERLHTV
LLDVTDPENVKKTAQWVKSHVGEKGLWGLINNAGVLGVLAPTDWLTVDDYREPIEVNLFGLINVTLNMLPLVKKARGRVI
NVSSIGGRLAFGGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTELADPIKTTEKKLAIWKHLSPDIKQQYGE
GYIEKSLHRLKSNTSSVNLDLSLVVGCMDHALTSLFPKTRYIAGKDAKTFWIPLSHMPAVLQDFLLLKQKVELANPKAV
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MLFWLLALLFLCAFLWNYKGQLKIADIADKYVFITGCDTGFGNLAARTFDKKGFRVIAACLTESGSAALKAKTSERLHTV
LLDVTDPENVKKTAQWVKSHVGEKGLWGLINNAGVLGVLAPTDWLTVDDYREPIEVNLFGLINVTLNMLPLVKKARGRVI
NVSSIGGRLAFGGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTELADPIKTTEKKLAIWKHLSPDIKQQYGE
GYIEKSLHRLKSNTSSVNLDLSLVVGCMDHALTSLFPKTRYIAGKDAKTFWIPLSHMPAVLQDFLLLKQKVELANPKAV
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE NAD 
3 'MALONATE ION'                    MLI 
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   LEU n 
1 3   PHE n 
1 4   TRP n 
1 5   LEU n 
1 6   LEU n 
1 7   ALA n 
1 8   LEU n 
1 9   LEU n 
1 10  PHE n 
1 11  LEU n 
1 12  CYS n 
1 13  ALA n 
1 14  PHE n 
1 15  LEU n 
1 16  TRP n 
1 17  ASN n 
1 18  TYR n 
1 19  LYS n 
1 20  GLY n 
1 21  GLN n 
1 22  LEU n 
1 23  LYS n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  ILE n 
1 28  ALA n 
1 29  ASP n 
1 30  LYS n 
1 31  TYR n 
1 32  VAL n 
1 33  PHE n 
1 34  ILE n 
1 35  THR n 
1 36  GLY n 
1 37  CYS n 
1 38  ASP n 
1 39  THR n 
1 40  GLY n 
1 41  PHE n 
1 42  GLY n 
1 43  ASN n 
1 44  LEU n 
1 45  ALA n 
1 46  ALA n 
1 47  ARG n 
1 48  THR n 
1 49  PHE n 
1 50  ASP n 
1 51  LYS n 
1 52  LYS n 
1 53  GLY n 
1 54  PHE n 
1 55  ARG n 
1 56  VAL n 
1 57  ILE n 
1 58  ALA n 
1 59  ALA n 
1 60  CYS n 
1 61  LEU n 
1 62  THR n 
1 63  GLU n 
1 64  SER n 
1 65  GLY n 
1 66  SER n 
1 67  ALA n 
1 68  ALA n 
1 69  LEU n 
1 70  LYS n 
1 71  ALA n 
1 72  LYS n 
1 73  THR n 
1 74  SER n 
1 75  GLU n 
1 76  ARG n 
1 77  LEU n 
1 78  HIS n 
1 79  THR n 
1 80  VAL n 
1 81  LEU n 
1 82  LEU n 
1 83  ASP n 
1 84  VAL n 
1 85  THR n 
1 86  ASP n 
1 87  PRO n 
1 88  GLU n 
1 89  ASN n 
1 90  VAL n 
1 91  LYS n 
1 92  LYS n 
1 93  THR n 
1 94  ALA n 
1 95  GLN n 
1 96  TRP n 
1 97  VAL n 
1 98  LYS n 
1 99  SER n 
1 100 HIS n 
1 101 VAL n 
1 102 GLY n 
1 103 GLU n 
1 104 LYS n 
1 105 GLY n 
1 106 LEU n 
1 107 TRP n 
1 108 GLY n 
1 109 LEU n 
1 110 ILE n 
1 111 ASN n 
1 112 ASN n 
1 113 ALA n 
1 114 GLY n 
1 115 VAL n 
1 116 LEU n 
1 117 GLY n 
1 118 VAL n 
1 119 LEU n 
1 120 ALA n 
1 121 PRO n 
1 122 THR n 
1 123 ASP n 
1 124 TRP n 
1 125 LEU n 
1 126 THR n 
1 127 VAL n 
1 128 ASP n 
1 129 ASP n 
1 130 TYR n 
1 131 ARG n 
1 132 GLU n 
1 133 PRO n 
1 134 ILE n 
1 135 GLU n 
1 136 VAL n 
1 137 ASN n 
1 138 LEU n 
1 139 PHE n 
1 140 GLY n 
1 141 LEU n 
1 142 ILE n 
1 143 ASN n 
1 144 VAL n 
1 145 THR n 
1 146 LEU n 
1 147 ASN n 
1 148 MET n 
1 149 LEU n 
1 150 PRO n 
1 151 LEU n 
1 152 VAL n 
1 153 LYS n 
1 154 LYS n 
1 155 ALA n 
1 156 ARG n 
1 157 GLY n 
1 158 ARG n 
1 159 VAL n 
1 160 ILE n 
1 161 ASN n 
1 162 VAL n 
1 163 SER n 
1 164 SER n 
1 165 ILE n 
1 166 GLY n 
1 167 GLY n 
1 168 ARG n 
1 169 LEU n 
1 170 ALA n 
1 171 PHE n 
1 172 GLY n 
1 173 GLY n 
1 174 GLY n 
1 175 GLY n 
1 176 TYR n 
1 177 THR n 
1 178 PRO n 
1 179 SER n 
1 180 LYS n 
1 181 TYR n 
1 182 ALA n 
1 183 VAL n 
1 184 GLU n 
1 185 GLY n 
1 186 PHE n 
1 187 ASN n 
1 188 ASP n 
1 189 SER n 
1 190 LEU n 
1 191 ARG n 
1 192 ARG n 
1 193 ASP n 
1 194 MET n 
1 195 LYS n 
1 196 ALA n 
1 197 PHE n 
1 198 GLY n 
1 199 VAL n 
1 200 HIS n 
1 201 VAL n 
1 202 SER n 
1 203 CYS n 
1 204 ILE n 
1 205 GLU n 
1 206 PRO n 
1 207 GLY n 
1 208 LEU n 
1 209 PHE n 
1 210 LYS n 
1 211 THR n 
1 212 GLU n 
1 213 LEU n 
1 214 ALA n 
1 215 ASP n 
1 216 PRO n 
1 217 ILE n 
1 218 LYS n 
1 219 THR n 
1 220 THR n 
1 221 GLU n 
1 222 LYS n 
1 223 LYS n 
1 224 LEU n 
1 225 ALA n 
1 226 ILE n 
1 227 TRP n 
1 228 LYS n 
1 229 HIS n 
1 230 LEU n 
1 231 SER n 
1 232 PRO n 
1 233 ASP n 
1 234 ILE n 
1 235 LYS n 
1 236 GLN n 
1 237 GLN n 
1 238 TYR n 
1 239 GLY n 
1 240 GLU n 
1 241 GLY n 
1 242 TYR n 
1 243 ILE n 
1 244 GLU n 
1 245 LYS n 
1 246 SER n 
1 247 LEU n 
1 248 HIS n 
1 249 ARG n 
1 250 LEU n 
1 251 LYS n 
1 252 SER n 
1 253 ASN n 
1 254 THR n 
1 255 SER n 
1 256 SER n 
1 257 VAL n 
1 258 ASN n 
1 259 LEU n 
1 260 ASP n 
1 261 LEU n 
1 262 SER n 
1 263 LEU n 
1 264 VAL n 
1 265 VAL n 
1 266 GLY n 
1 267 CYS n 
1 268 MET n 
1 269 ASP n 
1 270 HIS n 
1 271 ALA n 
1 272 LEU n 
1 273 THR n 
1 274 SER n 
1 275 LEU n 
1 276 PHE n 
1 277 PRO n 
1 278 LYS n 
1 279 THR n 
1 280 ARG n 
1 281 TYR n 
1 282 ILE n 
1 283 ALA n 
1 284 GLY n 
1 285 LYS n 
1 286 ASP n 
1 287 ALA n 
1 288 LYS n 
1 289 THR n 
1 290 PHE n 
1 291 TRP n 
1 292 ILE n 
1 293 PRO n 
1 294 LEU n 
1 295 SER n 
1 296 HIS n 
1 297 MET n 
1 298 PRO n 
1 299 ALA n 
1 300 VAL n 
1 301 LEU n 
1 302 GLN n 
1 303 ASP n 
1 304 PHE n 
1 305 LEU n 
1 306 LEU n 
1 307 LEU n 
1 308 LYS n 
1 309 GLN n 
1 310 LYS n 
1 311 VAL n 
1 312 GLU n 
1 313 LEU n 
1 314 ALA n 
1 315 ASN n 
1 316 PRO n 
1 317 LYS n 
1 318 ALA n 
1 319 VAL 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                   319 
_entity_src_gen.gene_src_common_name               'house mouse' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Dhrs9 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pet19b 
_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 
MLI non-polymer         . 'MALONATE ION'                    ? 'C3 H2 O4 -2'       102.046 
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE ? 'C21 H27 N7 O14 P2' 663.425 
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   LEU 2   2   ?   ?   ?   A . n 
A 1 3   PHE 3   3   ?   ?   ?   A . n 
A 1 4   TRP 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   ALA 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  PHE 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  CYS 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  PHE 14  14  ?   ?   ?   A . n 
A 1 15  LEU 15  15  ?   ?   ?   A . n 
A 1 16  TRP 16  16  ?   ?   ?   A . n 
A 1 17  ASN 17  17  ?   ?   ?   A . n 
A 1 18  TYR 18  18  ?   ?   ?   A . n 
A 1 19  LYS 19  19  ?   ?   ?   A . n 
A 1 20  GLY 20  20  ?   ?   ?   A . n 
A 1 21  GLN 21  21  21  GLN GLN A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  ILE 24  24  24  ILE ILE A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  ILE 27  27  27  ILE ILE A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  CYS 37  37  37  CYS CYS A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  ARG 47  47  47  ARG ARG A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  GLY 53  53  53  GLY GLY A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  SER 64  64  64  SER SER A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  THR 73  73  73  THR THR A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  GLN 95  95  95  GLN GLN A . n 
A 1 96  TRP 96  96  96  TRP TRP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  LYS 98  98  98  LYS LYS A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLU 103 103 103 GLU GLU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLY 105 105 105 GLY GLY A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 TRP 107 107 107 TRP TRP A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 ASP 123 123 123 ASP ASP A . n 
A 1 124 TRP 124 124 124 TRP TRP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 VAL 136 136 136 VAL VAL A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 ASN 143 143 143 ASN ASN A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 ASN 147 147 147 ASN ASN A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 LYS 154 154 154 LYS LYS A . n 
A 1 155 ALA 155 155 155 ALA ALA A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 ILE 160 160 160 ILE ILE A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 SER 163 163 163 SER SER A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 PHE 171 171 171 PHE PHE A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 TYR 176 176 176 TYR TYR A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 SER 179 179 179 SER SER A . n 
A 1 180 LYS 180 180 180 LYS LYS A . n 
A 1 181 TYR 181 181 181 TYR TYR A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 VAL 183 183 183 VAL VAL 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 PHE 186 186 186 PHE PHE A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 SER 189 189 189 SER SER A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 ASP 193 193 193 ASP ASP A . n 
A 1 194 MET 194 194 194 MET MET 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 PHE 197 197 197 PHE PHE A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 HIS 200 200 200 HIS HIS A . n 
A 1 201 VAL 201 201 201 VAL VAL A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 CYS 203 203 203 CYS CYS A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 GLY 207 207 207 GLY GLY A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 LYS 210 210 210 LYS LYS A . n 
A 1 211 THR 211 211 211 THR THR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 THR 219 219 219 THR THR A . n 
A 1 220 THR 220 220 220 THR THR A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 LYS 223 223 223 LYS LYS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 TRP 227 227 227 TRP TRP A . n 
A 1 228 LYS 228 228 228 LYS LYS A . n 
A 1 229 HIS 229 229 229 HIS HIS A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 PRO 232 232 232 PRO PRO A . n 
A 1 233 ASP 233 233 233 ASP ASP A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 GLN 236 236 236 GLN GLN A . n 
A 1 237 GLN 237 237 237 GLN GLN A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 GLY 241 241 241 GLY GLY A . n 
A 1 242 TYR 242 242 242 TYR TYR A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 CYS 267 267 267 CYS CYS A . n 
A 1 268 MET 268 268 268 MET MET A . n 
A 1 269 ASP 269 269 269 ASP ASP A . n 
A 1 270 HIS 270 270 270 HIS HIS A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 THR 273 273 273 THR THR A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 LYS 278 278 278 LYS LYS A . n 
A 1 279 THR 279 279 279 THR THR A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 ALA 283 283 283 ALA ALA A . n 
A 1 284 GLY 284 284 284 GLY GLY A . n 
A 1 285 LYS 285 285 285 LYS LYS A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 LYS 288 288 288 LYS LYS A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 PHE 290 290 290 PHE PHE A . n 
A 1 291 TRP 291 291 291 TRP TRP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 HIS 296 296 296 HIS HIS A . n 
A 1 297 MET 297 297 297 MET MET A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 LEU 301 301 301 LEU LEU A . n 
A 1 302 GLN 302 302 302 GLN GLN A . n 
A 1 303 ASP 303 303 303 ASP ASP A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 LEU 307 307 307 LEU LEU A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 GLN 309 309 309 GLN GLN A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 GLU 312 312 312 GLU GLU A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 ASN 315 315 315 ASN ASN A . n 
A 1 316 PRO 316 316 316 PRO PRO A . n 
A 1 317 LYS 317 317 317 LYS LYS A . n 
A 1 318 ALA 318 318 318 ALA ALA A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAD 
_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 
B 2 NAD 1   401 401 NAD NAD A . 
C 3 MLI 1   402 402 MLI MLI A . 
D 4 HOH 1   501 135 HOH HOH A . 
D 4 HOH 2   502 82  HOH HOH A . 
D 4 HOH 3   503 76  HOH HOH A . 
D 4 HOH 4   504 118 HOH HOH A . 
D 4 HOH 5   505 119 HOH HOH A . 
D 4 HOH 6   506 81  HOH HOH A . 
D 4 HOH 7   507 130 HOH HOH A . 
D 4 HOH 8   508 112 HOH HOH A . 
D 4 HOH 9   509 95  HOH HOH A . 
D 4 HOH 10  510 75  HOH HOH A . 
D 4 HOH 11  511 41  HOH HOH A . 
D 4 HOH 12  512 20  HOH HOH A . 
D 4 HOH 13  513 34  HOH HOH A . 
D 4 HOH 14  514 116 HOH HOH A . 
D 4 HOH 15  515 47  HOH HOH A . 
D 4 HOH 16  516 123 HOH HOH A . 
D 4 HOH 17  517 55  HOH HOH A . 
D 4 HOH 18  518 127 HOH HOH A . 
D 4 HOH 19  519 8   HOH HOH A . 
D 4 HOH 20  520 54  HOH HOH A . 
D 4 HOH 21  521 72  HOH HOH A . 
D 4 HOH 22  522 84  HOH HOH A . 
D 4 HOH 23  523 94  HOH HOH A . 
D 4 HOH 24  524 108 HOH HOH A . 
D 4 HOH 25  525 28  HOH HOH A . 
D 4 HOH 26  526 62  HOH HOH A . 
D 4 HOH 27  527 103 HOH HOH A . 
D 4 HOH 28  528 86  HOH HOH A . 
D 4 HOH 29  529 78  HOH HOH A . 
D 4 HOH 30  530 2   HOH HOH A . 
D 4 HOH 31  531 51  HOH HOH A . 
D 4 HOH 32  532 70  HOH HOH A . 
D 4 HOH 33  533 36  HOH HOH A . 
D 4 HOH 34  534 9   HOH HOH A . 
D 4 HOH 35  535 139 HOH HOH A . 
D 4 HOH 36  536 50  HOH HOH A . 
D 4 HOH 37  537 137 HOH HOH A . 
D 4 HOH 38  538 15  HOH HOH A . 
D 4 HOH 39  539 40  HOH HOH A . 
D 4 HOH 40  540 89  HOH HOH A . 
D 4 HOH 41  541 32  HOH HOH A . 
D 4 HOH 42  542 68  HOH HOH A . 
D 4 HOH 43  543 39  HOH HOH A . 
D 4 HOH 44  544 16  HOH HOH A . 
D 4 HOH 45  545 71  HOH HOH A . 
D 4 HOH 46  546 80  HOH HOH A . 
D 4 HOH 47  547 7   HOH HOH A . 
D 4 HOH 48  548 5   HOH HOH A . 
D 4 HOH 49  549 92  HOH HOH A . 
D 4 HOH 50  550 6   HOH HOH A . 
D 4 HOH 51  551 126 HOH HOH A . 
D 4 HOH 52  552 31  HOH HOH A . 
D 4 HOH 53  553 107 HOH HOH A . 
D 4 HOH 54  554 69  HOH HOH A . 
D 4 HOH 55  555 43  HOH HOH A . 
D 4 HOH 56  556 129 HOH HOH A . 
D 4 HOH 57  557 140 HOH HOH A . 
D 4 HOH 58  558 30  HOH HOH A . 
D 4 HOH 59  559 14  HOH HOH A . 
D 4 HOH 60  560 21  HOH HOH A . 
D 4 HOH 61  561 48  HOH HOH A . 
D 4 HOH 62  562 87  HOH HOH A . 
D 4 HOH 63  563 22  HOH HOH A . 
D 4 HOH 64  564 109 HOH HOH A . 
D 4 HOH 65  565 13  HOH HOH A . 
D 4 HOH 66  566 59  HOH HOH A . 
D 4 HOH 67  567 24  HOH HOH A . 
D 4 HOH 68  568 83  HOH HOH A . 
D 4 HOH 69  569 19  HOH HOH A . 
D 4 HOH 70  570 38  HOH HOH A . 
D 4 HOH 71  571 66  HOH HOH A . 
D 4 HOH 72  572 85  HOH HOH A . 
D 4 HOH 73  573 142 HOH HOH A . 
D 4 HOH 74  574 49  HOH HOH A . 
D 4 HOH 75  575 44  HOH HOH A . 
D 4 HOH 76  576 63  HOH HOH A . 
D 4 HOH 77  577 61  HOH HOH A . 
D 4 HOH 78  578 17  HOH HOH A . 
D 4 HOH 79  579 113 HOH HOH A . 
D 4 HOH 80  580 132 HOH HOH A . 
D 4 HOH 81  581 35  HOH HOH A . 
D 4 HOH 82  582 10  HOH HOH A . 
D 4 HOH 83  583 3   HOH HOH A . 
D 4 HOH 84  584 96  HOH HOH A . 
D 4 HOH 85  585 27  HOH HOH A . 
D 4 HOH 86  586 56  HOH HOH A . 
D 4 HOH 87  587 23  HOH HOH A . 
D 4 HOH 88  588 42  HOH HOH A . 
D 4 HOH 89  589 143 HOH HOH A . 
D 4 HOH 90  590 104 HOH HOH A . 
D 4 HOH 91  591 106 HOH HOH A . 
D 4 HOH 92  592 33  HOH HOH A . 
D 4 HOH 93  593 74  HOH HOH A . 
D 4 HOH 94  594 52  HOH HOH A . 
D 4 HOH 95  595 18  HOH HOH A . 
D 4 HOH 96  596 115 HOH HOH A . 
D 4 HOH 97  597 4   HOH HOH A . 
D 4 HOH 98  598 90  HOH HOH A . 
D 4 HOH 99  599 26  HOH HOH A . 
D 4 HOH 100 600 46  HOH HOH A . 
D 4 HOH 101 601 122 HOH HOH A . 
D 4 HOH 102 602 57  HOH HOH A . 
D 4 HOH 103 603 11  HOH HOH A . 
D 4 HOH 104 604 114 HOH HOH A . 
D 4 HOH 105 605 93  HOH HOH A . 
D 4 HOH 106 606 97  HOH HOH A . 
D 4 HOH 107 607 29  HOH HOH A . 
D 4 HOH 108 608 58  HOH HOH A . 
D 4 HOH 109 609 134 HOH HOH A . 
D 4 HOH 110 610 105 HOH HOH A . 
D 4 HOH 111 611 128 HOH HOH A . 
D 4 HOH 112 612 25  HOH HOH A . 
D 4 HOH 113 613 37  HOH HOH A . 
D 4 HOH 114 614 100 HOH HOH A . 
D 4 HOH 115 615 64  HOH HOH A . 
D 4 HOH 116 616 121 HOH HOH A . 
D 4 HOH 117 617 67  HOH HOH A . 
D 4 HOH 118 618 101 HOH HOH A . 
D 4 HOH 119 619 79  HOH HOH A . 
D 4 HOH 120 620 53  HOH HOH A . 
D 4 HOH 121 621 60  HOH HOH A . 
D 4 HOH 122 622 12  HOH HOH A . 
D 4 HOH 123 623 110 HOH HOH A . 
D 4 HOH 124 624 141 HOH HOH A . 
D 4 HOH 125 625 117 HOH HOH A . 
D 4 HOH 126 626 65  HOH HOH A . 
D 4 HOH 127 627 111 HOH HOH A . 
D 4 HOH 128 628 1   HOH HOH A . 
D 4 HOH 129 629 124 HOH HOH A . 
D 4 HOH 130 630 77  HOH HOH A . 
D 4 HOH 131 631 131 HOH HOH A . 
D 4 HOH 132 632 99  HOH HOH A . 
D 4 HOH 133 633 120 HOH HOH A . 
D 4 HOH 134 634 45  HOH HOH A . 
D 4 HOH 135 635 138 HOH HOH A . 
D 4 HOH 136 636 88  HOH HOH A . 
D 4 HOH 137 637 102 HOH HOH A . 
D 4 HOH 138 638 98  HOH HOH A . 
D 4 HOH 139 639 133 HOH HOH A . 
D 4 HOH 140 640 73  HOH HOH A . 
D 4 HOH 141 641 136 HOH HOH A . 
D 4 HOH 142 642 91  HOH HOH A . 
D 4 HOH 143 643 125 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLN 21  ? CG  ? A GLN 21  CG  
2  1 Y 1 A GLN 21  ? CD  ? A GLN 21  CD  
3  1 Y 1 A GLN 21  ? OE1 ? A GLN 21  OE1 
4  1 Y 1 A GLN 21  ? NE2 ? A GLN 21  NE2 
5  1 Y 1 A LEU 22  ? CG  ? A LEU 22  CG  
6  1 Y 1 A LEU 22  ? CD1 ? A LEU 22  CD1 
7  1 Y 1 A LEU 22  ? CD2 ? A LEU 22  CD2 
8  1 Y 1 A THR 254 ? OG1 ? A THR 254 OG1 
9  1 Y 1 A THR 254 ? CG2 ? A THR 254 CG2 
10 1 Y 1 A LYS 310 ? CG  ? A LYS 310 CG  
11 1 Y 1 A LYS 310 ? CD  ? A LYS 310 CD  
12 1 Y 1 A LYS 310 ? CE  ? A LYS 310 CE  
13 1 Y 1 A LYS 310 ? NZ  ? A LYS 310 NZ  
# 
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  ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B2F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     74.384 
_cell.length_a_esd                 ? 
_cell.length_b                     103.045 
_cell.length_b_esd                 ? 
_cell.length_c                     103.082 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9B2F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B2F 
_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             2.80 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.05 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '15% Jeffamine SD-2001, 0.1 M Na citrate pH 5.0, 0.1 M Na malonate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-09 
_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                    'cryogenically cooled single crystal SI(220)' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9791 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B2F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.66 
_reflns.d_resolution_low                               72.88 
_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                                     46581 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.5 
_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                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.66 
_reflns_shell.d_res_low                                     1.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6403 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.482 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.764 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -2.535 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            4.690 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            -2.155 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               42.658 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.977 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_refine.details                                  'Hydrogens have been added in their 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                                 9B2F 
_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                            1.662 
_refine.ls_d_res_low                             50.005 
_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                     46568 
_refine.ls_number_reflns_R_free                  968 
_refine.ls_number_reflns_R_work                  45600 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.227 
_refine.ls_percent_reflns_R_free                 2.079 
_refine.ls_R_factor_all                          0.167 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1931 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1661 
_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                      0.195 
_refine.ls_wR_factor_R_work                      0.168 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'BABINET MODEL PLUS 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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.075 
_refine.pdbx_overall_ESU_R_Free                  0.076 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                             2.947 
_refine.overall_SU_ML                            0.085 
_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                    0.9263 
_refine.pdbx_average_fsc_free                    0.9226 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.662 
_refine_hist.d_res_low                        50.005 
_refine_hist.number_atoms_solvent             143 
_refine_hist.number_atoms_total               2493 
_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        2299 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         51 
_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' ? 0.001  0.016  2371 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.825  1.824  3345 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 0.600  1.765  5480 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 6.515  5.000  313  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 10.722 5.000  12   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.010  5.000  1    ? r_dihedral_angle_other_2_deg   ? ? 
'X-RAY DIFFRACTION' ? 15.436 10.000 425  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.267 10.000 94   ? r_dihedral_angle_6_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  386  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2824 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  531  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.231  0.200  452  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.185  0.200  1997 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.182  0.200  1184 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.082  0.200  1367 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.157  0.200  112  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  1    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.125  0.200  11   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.112  0.200  75   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.107  0.200  32   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.728  4.170  1211 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.724  4.169  1211 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 4.879  7.472  1516 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 4.897  7.472  1517 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.254  4.752  1244 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.235  4.747  1241 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 8.078  8.409  1821 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 8.075  8.410  1822 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 9.636  41.832 2710 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 9.632  40.114 2673 ? r_lrange_other                 ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.662 1.705  . . 78 3034 90.0202 . . . . 0.359 . . . . . . . . . . . 0.372 
'X-RAY DIFFRACTION' 7.356 50.005 . . 11 597  99.8358 . . . . 0.168 . . . . . . . . . . . 0.186 
# 
_struct.entry_id                     9B2F 
_struct.title                        
'Crystal structure of short chain dehydrogenase reductase 9 (short chain dehydrogenase reductase 9C4) in complex with NAD+' 
_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        9B2F 
_struct_keywords.text            'short-chain dehydrogenase reductase, oxylipins, polyunsaturated fatty acids, 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 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DHRS9_MOUSE 
_struct_ref.pdbx_db_accession          Q58NB6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MLFWLLALLFLCAFLWNYKGQLKIADIADKYVFITGCDTGFGNLAARTFDKKGFRVIAACLTESGSAALKAKTSERLHTV
LLDVTDPENVKKTAQWVKSHVGEKGLWGLINNAGVLGVLAPTDWLTVDDYREPIEVNLFGLINVTLNMLPLVKKARGRVI
NVSSIGGRLAFGGGGYTPSKYAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTELADPIKTTEKKLAIWKHLSPDIKQQYGE
GYIEKSLHRLKSNTSSVNLDLSLVVGCMDHALTSLFPKTRYIAGKDAKTFWIPLSHMPAVLQDFLLLKQKVELANPKAV
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9B2F 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 319 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q58NB6 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  319 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       319 
# 
_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)' 7330  ? 
1 MORE         -36   ? 
1 'SSA (A^2)'  25090 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 74.3840000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 ASP A 26  ? ASP A 29  ? ASP A 26  ASP A 29  5 ? 4  
HELX_P HELX_P2  AA2 THR A 39  ? GLY A 53  ? THR A 39  GLY A 53  1 ? 15 
HELX_P HELX_P3  AA3 THR A 62  ? THR A 73  ? THR A 62  THR A 73  1 ? 12 
HELX_P HELX_P4  AA4 ASP A 86  ? GLY A 102 ? ASP A 86  GLY A 102 1 ? 17 
HELX_P HELX_P5  AA5 GLU A 103 ? GLY A 105 ? GLU A 103 GLY A 105 5 ? 3  
HELX_P HELX_P6  AA6 PRO A 121 ? THR A 126 ? PRO A 121 THR A 126 5 ? 6  
HELX_P HELX_P7  AA7 VAL A 127 ? LEU A 138 ? VAL A 127 LEU A 138 1 ? 12 
HELX_P HELX_P8  AA8 LEU A 138 ? ARG A 156 ? LEU A 138 ARG A 156 1 ? 19 
HELX_P HELX_P9  AA9 SER A 164 ? ARG A 168 ? SER A 164 ARG A 168 5 ? 5  
HELX_P HELX_P10 AB1 GLY A 175 ? LYS A 195 ? GLY A 175 LYS A 195 1 ? 21 
HELX_P HELX_P11 AB2 ALA A 196 ? GLY A 198 ? ALA A 196 GLY A 198 5 ? 3  
HELX_P HELX_P12 AB3 ASP A 215 ? HIS A 229 ? ASP A 215 HIS A 229 1 ? 15 
HELX_P HELX_P13 AB4 SER A 231 ? GLY A 239 ? SER A 231 GLY A 239 1 ? 9  
HELX_P HELX_P14 AB5 GLY A 241 ? LYS A 251 ? GLY A 241 LYS A 251 1 ? 11 
HELX_P HELX_P15 AB6 ASN A 253 ? VAL A 257 ? ASN A 253 VAL A 257 5 ? 5  
HELX_P HELX_P16 AB7 LEU A 261 ? SER A 274 ? LEU A 261 SER A 274 1 ? 14 
HELX_P HELX_P17 AB8 GLY A 284 ? PHE A 290 ? GLY A 284 PHE A 290 1 ? 7  
HELX_P HELX_P18 AB9 PHE A 290 ? HIS A 296 ? PHE A 290 HIS A 296 1 ? 7  
HELX_P HELX_P19 AC1 PRO A 298 ? LYS A 308 ? PRO A 298 LYS A 308 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   7 
_struct_sheet.details          ? 
# 
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 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 78  ? LEU A 81  ? HIS A 78  LEU A 81  
AA1 2 ARG A 55  ? CYS A 60  ? ARG A 55  CYS A 60  
AA1 3 TYR A 31  ? ILE A 34  ? TYR A 31  ILE A 34  
AA1 4 GLY A 108 ? ASN A 111 ? GLY A 108 ASN A 111 
AA1 5 ARG A 158 ? VAL A 162 ? ARG A 158 VAL A 162 
AA1 6 HIS A 200 ? PRO A 206 ? HIS A 200 PRO A 206 
AA1 7 ARG A 280 ? ALA A 283 ? ARG A 280 ALA A 283 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O HIS A 78  ? O HIS A 78  N ALA A 58  ? N ALA A 58  
AA1 2 3 O ALA A 59  ? O ALA A 59  N ILE A 34  ? N ILE A 34  
AA1 3 4 N PHE A 33  ? N PHE A 33  O GLY A 108 ? O GLY A 108 
AA1 4 5 N LEU A 109 ? N LEU A 109 O ILE A 160 ? O ILE A 160 
AA1 5 6 N ASN A 161 ? N ASN A 161 O ILE A 204 ? O ILE A 204 
AA1 6 7 N GLU A 205 ? N GLU A 205 O TYR A 281 ? O TYR A 281 
# 
_pdbx_entry_details.entry_id                   9B2F 
_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_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              100 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              100 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             HIS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              100 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                122.54 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            12.14 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LEU A 138 ? ? -104.81 -67.49  
2 1 SER A 163 ? ? -96.92  -129.70 
3 1 THR A 211 ? ? -137.40 -159.47 
4 1 ASN A 253 ? ? -147.46 39.47   
5 1 PHE A 290 ? ? -129.45 -58.48  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLN 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    21 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   LEU 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    22 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            145.75 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     156 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.121 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    MLI 
_pdbx_struct_special_symmetry.auth_seq_id     402 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   C 
_pdbx_struct_special_symmetry.label_comp_id   MLI 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 LEU 2  ? A LEU 2  
3  1 Y 1 A PHE 3  ? A PHE 3  
4  1 Y 1 A TRP 4  ? A TRP 4  
5  1 Y 1 A LEU 5  ? A LEU 5  
6  1 Y 1 A LEU 6  ? A LEU 6  
7  1 Y 1 A ALA 7  ? A ALA 7  
8  1 Y 1 A LEU 8  ? A LEU 8  
9  1 Y 1 A LEU 9  ? A LEU 9  
10 1 Y 1 A PHE 10 ? A PHE 10 
11 1 Y 1 A LEU 11 ? A LEU 11 
12 1 Y 1 A CYS 12 ? A CYS 12 
13 1 Y 1 A ALA 13 ? A ALA 13 
14 1 Y 1 A PHE 14 ? A PHE 14 
15 1 Y 1 A LEU 15 ? A LEU 15 
16 1 Y 1 A TRP 16 ? A TRP 16 
17 1 Y 1 A ASN 17 ? A ASN 17 
18 1 Y 1 A TYR 18 ? A TYR 18 
19 1 Y 1 A LYS 19 ? A LYS 19 
20 1 Y 1 A GLY 20 ? A GLY 20 
# 
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 
MLI C1   C N N 250 
MLI C2   C N N 251 
MLI C3   C N N 252 
MLI O6   O N N 253 
MLI O7   O N N 254 
MLI O8   O N N 255 
MLI O9   O N N 256 
MLI H11  H N N 257 
MLI H12  H N N 258 
NAD PA   P N S 259 
NAD O1A  O N N 260 
NAD O2A  O N N 261 
NAD O5B  O N N 262 
NAD C5B  C N N 263 
NAD C4B  C N R 264 
NAD O4B  O N N 265 
NAD C3B  C N S 266 
NAD O3B  O N N 267 
NAD C2B  C N R 268 
NAD O2B  O N N 269 
NAD C1B  C N R 270 
NAD N9A  N Y N 271 
NAD C8A  C Y N 272 
NAD N7A  N Y N 273 
NAD C5A  C Y N 274 
NAD C6A  C Y N 275 
NAD N6A  N N N 276 
NAD N1A  N Y N 277 
NAD C2A  C Y N 278 
NAD N3A  N Y N 279 
NAD C4A  C Y N 280 
NAD O3   O N N 281 
NAD PN   P N N 282 
NAD O1N  O N N 283 
NAD O2N  O N N 284 
NAD O5D  O N N 285 
NAD C5D  C N N 286 
NAD C4D  C N R 287 
NAD O4D  O N N 288 
NAD C3D  C N S 289 
NAD O3D  O N N 290 
NAD C2D  C N R 291 
NAD O2D  O N N 292 
NAD C1D  C N R 293 
NAD N1N  N Y N 294 
NAD C2N  C Y N 295 
NAD C3N  C Y N 296 
NAD C7N  C N N 297 
NAD O7N  O N N 298 
NAD N7N  N N N 299 
NAD C4N  C Y N 300 
NAD C5N  C Y N 301 
NAD C6N  C Y N 302 
NAD HOA2 H N N 303 
NAD H51A H N N 304 
NAD H52A H N N 305 
NAD H4B  H N N 306 
NAD H3B  H N N 307 
NAD HO3A H N N 308 
NAD H2B  H N N 309 
NAD HO2A H N N 310 
NAD H1B  H N N 311 
NAD H8A  H N N 312 
NAD H61A H N N 313 
NAD H62A H N N 314 
NAD H2A  H N N 315 
NAD H51N H N N 316 
NAD H52N H N N 317 
NAD H4D  H N N 318 
NAD H3D  H N N 319 
NAD HO3N H N N 320 
NAD H2D  H N N 321 
NAD HO2N H N N 322 
NAD H1D  H N N 323 
NAD H2N  H N N 324 
NAD H71N H N N 325 
NAD H72N H N N 326 
NAD H4N  H N N 327 
NAD H5N  H N N 328 
NAD H6N  H N N 329 
PHE N    N N N 330 
PHE CA   C N S 331 
PHE C    C N N 332 
PHE O    O N N 333 
PHE CB   C N N 334 
PHE CG   C Y N 335 
PHE CD1  C Y N 336 
PHE CD2  C Y N 337 
PHE CE1  C Y N 338 
PHE CE2  C Y N 339 
PHE CZ   C Y N 340 
PHE OXT  O N N 341 
PHE H    H N N 342 
PHE H2   H N N 343 
PHE HA   H N N 344 
PHE HB2  H N N 345 
PHE HB3  H N N 346 
PHE HD1  H N N 347 
PHE HD2  H N N 348 
PHE HE1  H N N 349 
PHE HE2  H N N 350 
PHE HZ   H N N 351 
PHE HXT  H N N 352 
PRO N    N N N 353 
PRO CA   C N S 354 
PRO C    C N N 355 
PRO O    O N N 356 
PRO CB   C N N 357 
PRO CG   C N N 358 
PRO CD   C N N 359 
PRO OXT  O N N 360 
PRO H    H N N 361 
PRO HA   H N N 362 
PRO HB2  H N N 363 
PRO HB3  H N N 364 
PRO HG2  H N N 365 
PRO HG3  H N N 366 
PRO HD2  H N N 367 
PRO HD3  H N N 368 
PRO HXT  H N N 369 
SER N    N N N 370 
SER CA   C N S 371 
SER C    C N N 372 
SER O    O N N 373 
SER CB   C N N 374 
SER OG   O N N 375 
SER OXT  O N N 376 
SER H    H N N 377 
SER H2   H N N 378 
SER HA   H N N 379 
SER HB2  H N N 380 
SER HB3  H N N 381 
SER HG   H N N 382 
SER HXT  H N N 383 
THR N    N N N 384 
THR CA   C N S 385 
THR C    C N N 386 
THR O    O N N 387 
THR CB   C N R 388 
THR OG1  O N N 389 
THR CG2  C N N 390 
THR OXT  O N N 391 
THR H    H N N 392 
THR H2   H N N 393 
THR HA   H N N 394 
THR HB   H N N 395 
THR HG1  H N N 396 
THR HG21 H N N 397 
THR HG22 H N N 398 
THR HG23 H N N 399 
THR HXT  H N N 400 
TRP N    N N N 401 
TRP CA   C N S 402 
TRP C    C N N 403 
TRP O    O N N 404 
TRP CB   C N N 405 
TRP CG   C Y N 406 
TRP CD1  C Y N 407 
TRP CD2  C Y N 408 
TRP NE1  N Y N 409 
TRP CE2  C Y N 410 
TRP CE3  C Y N 411 
TRP CZ2  C Y N 412 
TRP CZ3  C Y N 413 
TRP CH2  C Y N 414 
TRP OXT  O N N 415 
TRP H    H N N 416 
TRP H2   H N N 417 
TRP HA   H N N 418 
TRP HB2  H N N 419 
TRP HB3  H N N 420 
TRP HD1  H N N 421 
TRP HE1  H N N 422 
TRP HE3  H N N 423 
TRP HZ2  H N N 424 
TRP HZ3  H N N 425 
TRP HH2  H N N 426 
TRP HXT  H N N 427 
TYR N    N N N 428 
TYR CA   C N S 429 
TYR C    C N N 430 
TYR O    O N N 431 
TYR CB   C N N 432 
TYR CG   C Y N 433 
TYR CD1  C Y N 434 
TYR CD2  C Y N 435 
TYR CE1  C Y N 436 
TYR CE2  C Y N 437 
TYR CZ   C Y N 438 
TYR OH   O N N 439 
TYR OXT  O N N 440 
TYR H    H N N 441 
TYR H2   H N N 442 
TYR HA   H N N 443 
TYR HB2  H N N 444 
TYR HB3  H N N 445 
TYR HD1  H N N 446 
TYR HD2  H N N 447 
TYR HE1  H N N 448 
TYR HE2  H N N 449 
TYR HH   H N N 450 
TYR HXT  H N N 451 
VAL N    N N N 452 
VAL CA   C N S 453 
VAL C    C N N 454 
VAL O    O N N 455 
VAL CB   C N N 456 
VAL CG1  C N N 457 
VAL CG2  C N N 458 
VAL OXT  O N N 459 
VAL H    H N N 460 
VAL H2   H N N 461 
VAL HA   H N N 462 
VAL HB   H N N 463 
VAL HG11 H N N 464 
VAL HG12 H N N 465 
VAL HG13 H N N 466 
VAL HG21 H N N 467 
VAL HG22 H N N 468 
VAL HG23 H N N 469 
VAL HXT  H N N 470 
# 
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 
MLI C1  C2   sing N N 237 
MLI C1  C3   sing N N 238 
MLI C1  H11  sing N N 239 
MLI C1  H12  sing N N 240 
MLI C2  O6   doub N N 241 
MLI C2  O7   sing N N 242 
MLI C3  O8   doub N N 243 
MLI C3  O9   sing N N 244 
NAD PA  O1A  doub N N 245 
NAD PA  O2A  sing N N 246 
NAD PA  O5B  sing N N 247 
NAD PA  O3   sing N N 248 
NAD O2A HOA2 sing N N 249 
NAD O5B C5B  sing N N 250 
NAD C5B C4B  sing N N 251 
NAD C5B H51A sing N N 252 
NAD C5B H52A sing N N 253 
NAD C4B O4B  sing N N 254 
NAD C4B C3B  sing N N 255 
NAD C4B H4B  sing N N 256 
NAD O4B C1B  sing N N 257 
NAD C3B O3B  sing N N 258 
NAD C3B C2B  sing N N 259 
NAD C3B H3B  sing N N 260 
NAD O3B HO3A sing N N 261 
NAD C2B O2B  sing N N 262 
NAD C2B C1B  sing N N 263 
NAD C2B H2B  sing N N 264 
NAD O2B HO2A sing N N 265 
NAD C1B N9A  sing N N 266 
NAD C1B H1B  sing N N 267 
NAD N9A C8A  sing Y N 268 
NAD N9A C4A  sing Y N 269 
NAD C8A N7A  doub Y N 270 
NAD C8A H8A  sing N N 271 
NAD N7A C5A  sing Y N 272 
NAD C5A C6A  sing Y N 273 
NAD C5A C4A  doub Y N 274 
NAD C6A N6A  sing N N 275 
NAD C6A N1A  doub Y N 276 
NAD N6A H61A sing N N 277 
NAD N6A H62A sing N N 278 
NAD N1A C2A  sing Y N 279 
NAD C2A N3A  doub Y N 280 
NAD C2A H2A  sing N N 281 
NAD N3A C4A  sing Y N 282 
NAD O3  PN   sing N N 283 
NAD PN  O1N  doub N N 284 
NAD PN  O2N  sing N N 285 
NAD PN  O5D  sing N N 286 
NAD O5D C5D  sing N N 287 
NAD C5D C4D  sing N N 288 
NAD C5D H51N sing N N 289 
NAD C5D H52N sing N N 290 
NAD C4D O4D  sing N N 291 
NAD C4D C3D  sing N N 292 
NAD C4D H4D  sing N N 293 
NAD O4D C1D  sing N N 294 
NAD C3D O3D  sing N N 295 
NAD C3D C2D  sing N N 296 
NAD C3D H3D  sing N N 297 
NAD O3D HO3N sing N N 298 
NAD C2D O2D  sing N N 299 
NAD C2D C1D  sing N N 300 
NAD C2D H2D  sing N N 301 
NAD O2D HO2N sing N N 302 
NAD C1D N1N  sing N N 303 
NAD C1D H1D  sing N N 304 
NAD N1N C2N  sing Y N 305 
NAD N1N C6N  doub Y N 306 
NAD C2N C3N  doub Y N 307 
NAD C2N H2N  sing N N 308 
NAD C3N C7N  sing N N 309 
NAD C3N C4N  sing Y N 310 
NAD C7N O7N  doub N N 311 
NAD C7N N7N  sing N N 312 
NAD N7N H71N sing N N 313 
NAD N7N H72N sing N N 314 
NAD C4N C5N  doub Y N 315 
NAD C4N H4N  sing N N 316 
NAD C5N C6N  sing Y N 317 
NAD C5N H5N  sing N N 318 
NAD C6N H6N  sing N N 319 
PHE N   CA   sing N N 320 
PHE N   H    sing N N 321 
PHE N   H2   sing N N 322 
PHE CA  C    sing N N 323 
PHE CA  CB   sing N N 324 
PHE CA  HA   sing N N 325 
PHE C   O    doub N N 326 
PHE C   OXT  sing N N 327 
PHE CB  CG   sing N N 328 
PHE CB  HB2  sing N N 329 
PHE CB  HB3  sing N N 330 
PHE CG  CD1  doub Y N 331 
PHE CG  CD2  sing Y N 332 
PHE CD1 CE1  sing Y N 333 
PHE CD1 HD1  sing N N 334 
PHE CD2 CE2  doub Y N 335 
PHE CD2 HD2  sing N N 336 
PHE CE1 CZ   doub Y N 337 
PHE CE1 HE1  sing N N 338 
PHE CE2 CZ   sing Y N 339 
PHE CE2 HE2  sing N N 340 
PHE CZ  HZ   sing N N 341 
PHE OXT HXT  sing N N 342 
PRO N   CA   sing N N 343 
PRO N   CD   sing N N 344 
PRO N   H    sing N N 345 
PRO CA  C    sing N N 346 
PRO CA  CB   sing N N 347 
PRO CA  HA   sing N N 348 
PRO C   O    doub N N 349 
PRO C   OXT  sing N N 350 
PRO CB  CG   sing N N 351 
PRO CB  HB2  sing N N 352 
PRO CB  HB3  sing N N 353 
PRO CG  CD   sing N N 354 
PRO CG  HG2  sing N N 355 
PRO CG  HG3  sing N N 356 
PRO CD  HD2  sing N N 357 
PRO CD  HD3  sing N N 358 
PRO OXT HXT  sing N N 359 
SER N   CA   sing N N 360 
SER N   H    sing N N 361 
SER N   H2   sing N N 362 
SER CA  C    sing N N 363 
SER CA  CB   sing N N 364 
SER CA  HA   sing N N 365 
SER C   O    doub N N 366 
SER C   OXT  sing N N 367 
SER CB  OG   sing N N 368 
SER CB  HB2  sing N N 369 
SER CB  HB3  sing N N 370 
SER OG  HG   sing N N 371 
SER OXT HXT  sing N N 372 
THR N   CA   sing N N 373 
THR N   H    sing N N 374 
THR N   H2   sing N N 375 
THR CA  C    sing N N 376 
THR CA  CB   sing N N 377 
THR CA  HA   sing N N 378 
THR C   O    doub N N 379 
THR C   OXT  sing N N 380 
THR CB  OG1  sing N N 381 
THR CB  CG2  sing N N 382 
THR CB  HB   sing N N 383 
THR OG1 HG1  sing N N 384 
THR CG2 HG21 sing N N 385 
THR CG2 HG22 sing N N 386 
THR CG2 HG23 sing N N 387 
THR OXT HXT  sing N N 388 
TRP N   CA   sing N N 389 
TRP N   H    sing N N 390 
TRP N   H2   sing N N 391 
TRP CA  C    sing N N 392 
TRP CA  CB   sing N N 393 
TRP CA  HA   sing N N 394 
TRP C   O    doub N N 395 
TRP C   OXT  sing N N 396 
TRP CB  CG   sing N N 397 
TRP CB  HB2  sing N N 398 
TRP CB  HB3  sing N N 399 
TRP CG  CD1  doub Y N 400 
TRP CG  CD2  sing Y N 401 
TRP CD1 NE1  sing Y N 402 
TRP CD1 HD1  sing N N 403 
TRP CD2 CE2  doub Y N 404 
TRP CD2 CE3  sing Y N 405 
TRP NE1 CE2  sing Y N 406 
TRP NE1 HE1  sing N N 407 
TRP CE2 CZ2  sing Y N 408 
TRP CE3 CZ3  doub Y N 409 
TRP CE3 HE3  sing N N 410 
TRP CZ2 CH2  doub Y N 411 
TRP CZ2 HZ2  sing N N 412 
TRP CZ3 CH2  sing Y N 413 
TRP CZ3 HZ3  sing N N 414 
TRP CH2 HH2  sing N N 415 
TRP OXT HXT  sing N N 416 
TYR N   CA   sing N N 417 
TYR N   H    sing N N 418 
TYR N   H2   sing N N 419 
TYR CA  C    sing N N 420 
TYR CA  CB   sing N N 421 
TYR CA  HA   sing N N 422 
TYR C   O    doub N N 423 
TYR C   OXT  sing N N 424 
TYR CB  CG   sing N N 425 
TYR CB  HB2  sing N N 426 
TYR CB  HB3  sing N N 427 
TYR CG  CD1  doub Y N 428 
TYR CG  CD2  sing Y N 429 
TYR CD1 CE1  sing Y N 430 
TYR CD1 HD1  sing N N 431 
TYR CD2 CE2  doub Y N 432 
TYR CD2 HD2  sing N N 433 
TYR CE1 CZ   doub Y N 434 
TYR CE1 HE1  sing N N 435 
TYR CE2 CZ   sing Y N 436 
TYR CE2 HE2  sing N N 437 
TYR CZ  OH   sing N N 438 
TYR OH  HH   sing N N 439 
TYR OXT HXT  sing N N 440 
VAL N   CA   sing N N 441 
VAL N   H    sing N N 442 
VAL N   H2   sing N N 443 
VAL CA  C    sing N N 444 
VAL CA  CB   sing N N 445 
VAL CA  HA   sing N N 446 
VAL C   O    doub N N 447 
VAL C   OXT  sing N N 448 
VAL CB  CG1  sing N N 449 
VAL CB  CG2  sing N N 450 
VAL CB  HB   sing N N 451 
VAL CG1 HG11 sing N N 452 
VAL CG1 HG12 sing N N 453 
VAL CG1 HG13 sing N N 454 
VAL CG2 HG21 sing N N 455 
VAL CG2 HG22 sing N N 456 
VAL CG2 HG23 sing N N 457 
VAL OXT HXT  sing N N 458 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)' 'United States' 
AR076924 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)'                        'United States' 
GM134548 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6FFB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B2F 
_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]   0.013444 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009704 
_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]   0.009701 
_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   . GLN A 1 21  ? 27.178 50.636 27.090  1.000 101.820 0 21  GLN A N   1 
ATOM   2    C CA  . GLN A 1 21  ? 26.923 49.172 27.093  1.000 98.119  0 21  GLN A CA  1 
ATOM   3    C C   . GLN A 1 21  ? 25.635 48.877 27.862  1.000 101.225 0 21  GLN A C   1 
ATOM   4    O O   . GLN A 1 21  ? 25.649 48.735 29.084  1.000 106.399 0 21  GLN A O   1 
ATOM   5    C CB  . GLN A 1 21  ? 28.139 48.437 27.664  1.000 90.771  0 21  GLN A CB  1 
ATOM   6    N N   . LEU A 1 22  ? 24.508 48.829 27.140  1.000 97.718  0 22  LEU A N   1 
ATOM   7    C CA  . LEU A 1 22  ? 23.450 47.906 27.504  1.000 89.650  0 22  LEU A CA  1 
ATOM   8    C C   . LEU A 1 22  ? 23.949 46.522 27.057  1.000 79.372  0 22  LEU A C   1 
ATOM   9    O O   . LEU A 1 22  ? 24.209 46.280 25.878  1.000 73.753  0 22  LEU A O   1 
ATOM   10   C CB  . LEU A 1 22  ? 22.094 48.308 26.917  1.000 77.429  0 22  LEU A CB  1 
ATOM   11   N N   . LYS A 1 23  ? 24.250 45.669 28.041  1.000 68.438  0 23  LYS A N   1 
ATOM   12   C CA  . LYS A 1 23  ? 24.611 44.279 27.819  1.000 63.672  0 23  LYS A CA  1 
ATOM   13   C C   . LYS A 1 23  ? 23.357 43.405 27.903  1.000 64.168  0 23  LYS A C   1 
ATOM   14   O O   . LYS A 1 23  ? 22.295 43.871 28.314  1.000 53.572  0 23  LYS A O   1 
ATOM   15   C CB  . LYS A 1 23  ? 25.716 43.949 28.828  1.000 65.937  0 23  LYS A CB  1 
ATOM   16   C CG  . LYS A 1 23  ? 27.096 44.515 28.459  1.000 75.068  0 23  LYS A CG  1 
ATOM   17   C CD  . LYS A 1 23  ? 28.142 44.448 29.573  1.000 88.781  0 23  LYS A CD  1 
ATOM   18   C CE  . LYS A 1 23  ? 29.591 44.491 29.136  1.000 89.980  0 23  LYS A CE  1 
ATOM   19   N NZ  . LYS A 1 23  ? 30.195 43.152 29.047  1.000 88.450  0 23  LYS A NZ  1 
ATOM   20   N N   . ILE A 1 24  ? 23.449 42.142 27.466  1.000 51.157  0 24  ILE A N   1 
ATOM   21   C CA  . ILE A 1 24  ? 22.346 41.215 27.661  1.000 55.684  0 24  ILE A CA  1 
ATOM   22   C C   . ILE A 1 24  ? 22.204 40.962 29.161  1.000 54.047  0 24  ILE A C   1 
ATOM   23   O O   . ILE A 1 24  ? 23.144 41.192 29.921  1.000 50.015  0 24  ILE A O   1 
ATOM   24   C CB  . ILE A 1 24  ? 22.560 39.885 26.921  1.000 48.462  0 24  ILE A CB  1 
ATOM   25   C CG1 . ILE A 1 24  ? 23.822 39.193 27.422  1.000 51.044  0 24  ILE A CG1 1 
ATOM   26   C CG2 . ILE A 1 24  ? 22.556 40.103 25.414  1.000 57.876  0 24  ILE A CG2 1 
ATOM   27   C CD1 . ILE A 1 24  ? 23.944 37.738 26.998  1.000 53.797  0 24  ILE A CD1 1 
ATOM   28   N N   . ALA A 1 25  ? 21.036 40.437 29.552  1.000 54.034  0 25  ALA A N   1 
ATOM   29   C CA  . ALA A 1 25  ? 20.806 39.975 30.915  1.000 53.240  0 25  ALA A CA  1 
ATOM   30   C C   . ALA A 1 25  ? 20.867 38.446 30.943  1.000 50.733  0 25  ALA A C   1 
ATOM   31   O O   . ALA A 1 25  ? 20.851 37.788 29.892  1.000 51.344  0 25  ALA A O   1 
ATOM   32   C CB  . ALA A 1 25  ? 19.458 40.470 31.386  1.000 57.219  0 25  ALA A CB  1 
ATOM   33   N N   . ASP A 1 26  ? 20.908 37.907 32.159  1.000 46.633  0 26  ASP A N   1 
ATOM   34   C CA  . ASP A 1 26  ? 20.855 36.470 32.426  1.000 46.411  0 26  ASP A CA  1 
ATOM   35   C C   . ASP A 1 26  ? 21.984 35.694 31.733  1.000 44.447  0 26  ASP A C   1 
ATOM   36   O O   . ASP A 1 26  ? 21.770 34.584 31.230  1.000 43.185  0 26  ASP A O   1 
ATOM   37   C CB  . ASP A 1 26  ? 19.486 35.902 32.103  1.000 49.126  0 26  ASP A CB  1 
ATOM   38   C CG  . ASP A 1 26  ? 18.354 36.606 32.847  1.000 64.711  0 26  ASP A CG  1 
ATOM   39   O OD1 . ASP A 1 26  ? 18.519 36.833 34.067  1.000 67.626  0 26  ASP A OD1 1 
ATOM   40   O OD2 . ASP A 1 26  ? 17.335 36.945 32.207  1.000 62.448  0 26  ASP A OD2 1 
ATOM   41   N N   . ILE A 1 27  ? 23.203 36.239 31.818  1.000 40.792  0 27  ILE A N   1 
ATOM   42   C CA  . ILE A 1 27  ? 24.394 35.542 31.367  1.000 44.589  0 27  ILE A CA  1 
ATOM   43   C C   . ILE A 1 27  ? 24.438 34.147 31.996  1.000 46.744  0 27  ILE A C   1 
ATOM   44   O O   . ILE A 1 27  ? 24.776 33.167 31.340  1.000 40.100  0 27  ILE A O   1 
ATOM   45   C CB  . ILE A 1 27  ? 25.636 36.396 31.668  1.000 49.934  0 27  ILE A CB  1 
ATOM   46   C CG1 . ILE A 1 27  ? 25.707 37.577 30.691  1.000 54.559  0 27  ILE A CG1 1 
ATOM   47   C CG2 . ILE A 1 27  ? 26.909 35.555 31.644  1.000 48.660  0 27  ILE A CG2 1 
ATOM   48   C CD1 . ILE A 1 27  ? 26.539 38.754 31.186  1.000 60.503  0 27  ILE A CD1 1 
ATOM   49   N N   . ALA A 1 28  ? 24.051 34.027 33.269  1.000 40.209  0 28  ALA A N   1 
ATOM   50   C CA  . ALA A 1 28  ? 24.225 32.782 33.990  1.000 39.420  0 28  ALA A CA  1 
ATOM   51   C C   . ALA A 1 28  ? 23.355 31.650 33.454  1.000 37.537  0 28  ALA A C   1 
ATOM   52   O O   . ALA A 1 28  ? 23.612 30.466 33.745  1.000 39.281  0 28  ALA A O   1 
ATOM   53   C CB  . ALA A 1 28  ? 23.972 33.042 35.484  1.000 47.219  0 28  ALA A CB  1 
ATOM   54   N N   . ASP A 1 29  ? 22.302 32.005 32.702  1.000 40.564  0 29  ASP A N   1 
ATOM   55   C CA  . ASP A 1 29  ? 21.379 31.045 32.125  1.000 40.349  0 29  ASP A CA  1 
ATOM   56   C C   . ASP A 1 29  ? 21.724 30.668 30.679  1.000 38.711  0 29  ASP A C   1 
ATOM   57   O O   . ASP A 1 29  ? 20.978 29.878 30.098  1.000 41.037  0 29  ASP A O   1 
ATOM   58   C CB  . ASP A 1 29  ? 19.950 31.589 32.088  1.000 46.824  0 29  ASP A CB  1 
ATOM   59   C CG  . ASP A 1 29  ? 19.284 31.913 33.429  1.000 60.959  0 29  ASP A CG  1 
ATOM   60   O OD1 . ASP A 1 29  ? 19.686 31.325 34.454  1.000 52.948  0 29  ASP A OD1 1 
ATOM   61   O OD2 . ASP A 1 29  ? 18.416 32.810 33.441  1.000 61.269  0 29  ASP A OD2 1 
ATOM   62   N N   . LYS A 1 30  ? 22.796 31.240 30.101  1.000 37.698  0 30  LYS A N   1 
ATOM   63   C CA  . LYS A 1 30  ? 23.146 31.060 28.687  1.000 34.959  0 30  LYS A CA  1 
ATOM   64   C C   . LYS A 1 30  ? 24.351 30.136 28.467  1.000 34.329  0 30  LYS A C   1 
ATOM   65   O O   . LYS A 1 30  ? 25.361 30.205 29.170  1.000 35.341  0 30  LYS A O   1 
ATOM   66   C CB  . LYS A 1 30  ? 23.406 32.460 28.119  1.000 37.223  0 30  LYS A CB  1 
ATOM   67   C CG  . LYS A 1 30  ? 22.154 33.281 27.995  1.000 36.076  0 30  LYS A CG  1 
ATOM   68   C CD  . LYS A 1 30  ? 22.370 34.705 27.503  1.000 41.044  0 30  LYS A CD  1 
ATOM   69   C CE  . LYS A 1 30  ? 21.073 35.277 26.972  1.000 47.966  0 30  LYS A CE  1 
ATOM   70   N NZ  . LYS A 1 30  ? 20.175 35.599 28.085  1.000 49.034  0 30  LYS A NZ  1 
ATOM   71   N N   . TYR A 1 31  ? 24.192 29.212 27.503  1.000 35.952  0 31  TYR A N   1 
ATOM   72   C CA  . TYR A 1 31  ? 25.225 28.289 27.083  1.000 31.789  0 31  TYR A CA  1 
ATOM   73   C C   . TYR A 1 31  ? 26.016 28.857 25.912  1.000 31.923  0 31  TYR A C   1 
ATOM   74   O O   . TYR A 1 31  ? 25.435 29.449 24.996  1.000 32.033  0 31  TYR A O   1 
ATOM   75   C CB  . TYR A 1 31  ? 24.596 26.989 26.637  1.000 35.571  0 31  TYR A CB  1 
ATOM   76   C CG  . TYR A 1 31  ? 24.070 26.158 27.791  1.000 36.097  0 31  TYR A CG  1 
ATOM   77   C CD1 . TYR A 1 31  ? 22.760 26.296 28.226  1.000 41.135  0 31  TYR A CD1 1 
ATOM   78   C CD2 . TYR A 1 31  ? 24.891 25.254 28.440  1.000 38.618  0 31  TYR A CD2 1 
ATOM   79   C CE1 . TYR A 1 31  ? 22.263 25.522 29.260  1.000 44.596  0 31  TYR A CE1 1 
ATOM   80   C CE2 . TYR A 1 31  ? 24.427 24.498 29.508  1.000 41.967  0 31  TYR A CE2 1 
ATOM   81   C CZ  . TYR A 1 31  ? 23.108 24.639 29.911  1.000 46.765  0 31  TYR A CZ  1 
ATOM   82   O OH  . TYR A 1 31  ? 22.639 23.919 30.946  1.000 47.082  0 31  TYR A OH  1 
ATOM   83   N N   . VAL A 1 32  ? 27.334 28.666 25.956  1.000 31.987  0 32  VAL A N   1 
ATOM   84   C CA  . VAL A 1 32  ? 28.210 29.036 24.859  1.000 32.363  0 32  VAL A CA  1 
ATOM   85   C C   . VAL A 1 32  ? 29.065 27.836 24.470  1.000 36.152  0 32  VAL A C   1 
ATOM   86   O O   . VAL A 1 32  ? 29.775 27.307 25.318  1.000 36.147  0 32  VAL A O   1 
ATOM   87   C CB  . VAL A 1 32  ? 29.084 30.213 25.263  1.000 36.093  0 32  VAL A CB  1 
ATOM   88   C CG1 . VAL A 1 32  ? 30.050 30.591 24.122  1.000 35.853  0 32  VAL A CG1 1 
ATOM   89   C CG2 . VAL A 1 32  ? 28.220 31.389 25.668  1.000 40.984  0 32  VAL A CG2 1 
ATOM   90   N N   . PHE A 1 33  ? 28.990 27.420 23.198  1.000 32.599  0 33  PHE A N   1 
ATOM   91   C CA  . PHE A 1 33  ? 29.750 26.290 22.672  1.000 30.705  0 33  PHE A CA  1 
ATOM   92   C C   . PHE A 1 33  ? 30.954 26.806 21.895  1.000 31.578  0 33  PHE A C   1 
ATOM   93   O O   . PHE A 1 33  ? 30.765 27.609 21.007  1.000 33.456  0 33  PHE A O   1 
ATOM   94   C CB  . PHE A 1 33  ? 28.856 25.496 21.743  1.000 31.305  0 33  PHE A CB  1 
ATOM   95   C CG  . PHE A 1 33  ? 29.477 24.204 21.250  1.000 32.191  0 33  PHE A CG  1 
ATOM   96   C CD1 . PHE A 1 33  ? 29.319 23.046 21.983  1.000 35.252  0 33  PHE A CD1 1 
ATOM   97   C CD2 . PHE A 1 33  ? 30.304 24.169 20.134  1.000 34.828  0 33  PHE A CD2 1 
ATOM   98   C CE1 . PHE A 1 33  ? 29.882 21.868 21.554  1.000 35.189  0 33  PHE A CE1 1 
ATOM   99   C CE2 . PHE A 1 33  ? 30.897 22.983 19.732  1.000 36.296  0 33  PHE A CE2 1 
ATOM   100  C CZ  . PHE A 1 33  ? 30.671 21.835 20.425  1.000 38.229  0 33  PHE A CZ  1 
ATOM   101  N N   . ILE A 1 34  ? 32.162 26.418 22.291  1.000 31.901  0 34  ILE A N   1 
ATOM   102  C CA  . ILE A 1 34  ? 33.416 26.881 21.699  1.000 32.249  0 34  ILE A CA  1 
ATOM   103  C C   . ILE A 1 34  ? 34.194 25.697 21.135  1.000 33.543  0 34  ILE A C   1 
ATOM   104  O O   . ILE A 1 34  ? 34.425 24.703 21.843  1.000 33.594  0 34  ILE A O   1 
ATOM   105  C CB  . ILE A 1 34  ? 34.248 27.638 22.752  1.000 33.260  0 34  ILE A CB  1 
ATOM   106  C CG1 . ILE A 1 34  ? 33.430 28.625 23.526  1.000 34.625  0 34  ILE A CG1 1 
ATOM   107  C CG2 . ILE A 1 34  ? 35.459 28.298 22.117  1.000 34.487  0 34  ILE A CG2 1 
ATOM   108  C CD1 . ILE A 1 34  ? 34.193 29.399 24.586  1.000 37.959  0 34  ILE A CD1 1 
ATOM   109  N N   . THR A 1 35  ? 34.608 25.785 19.856  1.000 32.974  0 35  THR A N   1 
ATOM   110  C CA  . THR A 1 35  ? 35.423 24.737 19.243  1.000 32.405  0 35  THR A CA  1 
ATOM   111  C C   . THR A 1 35  ? 36.906 25.069 19.416  1.000 36.710  0 35  THR A C   1 
ATOM   112  O O   . THR A 1 35  ? 37.296 26.229 19.425  1.000 34.697  0 35  THR A O   1 
ATOM   113  C CB  . THR A 1 35  ? 35.075 24.499 17.764  1.000 33.666  0 35  THR A CB  1 
ATOM   114  O OG1 . THR A 1 35  ? 35.396 25.696 17.031  1.000 31.456  0 35  THR A OG1 1 
ATOM   115  C CG2 . THR A 1 35  ? 33.637 24.069 17.582  1.000 34.229  0 35  THR A CG2 1 
ATOM   116  N N   . GLY A 1 36  ? 37.728 24.025 19.596  1.000 35.817  0 36  GLY A N   1 
ATOM   117  C CA  . GLY A 1 36  ? 39.179 24.178 19.673  1.000 38.406  0 36  GLY A CA  1 
ATOM   118  C C   . GLY A 1 36  ? 39.683 24.859 20.959  1.000 36.256  0 36  GLY A C   1 
ATOM   119  O O   . GLY A 1 36  ? 40.373 25.881 20.902  1.000 35.122  0 36  GLY A O   1 
ATOM   120  N N   . CYS A 1 37  ? 39.404 24.256 22.123  1.000 33.334  0 37  CYS A N   1 
ATOM   121  C CA  . CYS A 1 37  ? 39.712 24.895 23.391  1.000 31.640  0 37  CYS A CA  1 
ATOM   122  C C   . CYS A 1 37  ? 40.976 24.336 24.051  1.000 35.743  0 37  CYS A C   1 
ATOM   123  O O   . CYS A 1 37  ? 41.271 24.690 25.183  1.000 35.795  0 37  CYS A O   1 
ATOM   124  C CB  . CYS A 1 37  ? 38.537 24.844 24.355  1.000 37.353  0 37  CYS A CB  1 
ATOM   125  S SG  . CYS A 1 37  ? 37.047 25.697 23.785  1.000 36.507  0 37  CYS A SG  1 
ATOM   126  N N   . ASP A 1 38  ? 41.724 23.451 23.379  1.000 37.082  0 38  ASP A N   1 
ATOM   127  C CA  . ASP A 1 38  ? 42.943 22.908 23.964  1.000 38.549  0 38  ASP A CA  1 
ATOM   128  C C   . ASP A 1 38  ? 43.970 23.994 24.250  1.000 39.823  0 38  ASP A C   1 
ATOM   129  O O   . ASP A 1 38  ? 44.579 23.971 25.323  1.000 37.660  0 38  ASP A O   1 
ATOM   130  C CB  . ASP A 1 38  ? 43.564 21.860 23.070  1.000 36.581  0 38  ASP A CB  1 
ATOM   131  C CG  . ASP A 1 38  ? 42.559 20.845 22.561  1.000 39.403  0 38  ASP A CG  1 
ATOM   132  O OD1 . ASP A 1 38  ? 41.693 21.203 21.669  1.000 38.286  0 38  ASP A OD1 1 
ATOM   133  O OD2 . ASP A 1 38  ? 42.619 19.724 23.080  1.000 42.250  0 38  ASP A OD2 1 
ATOM   134  N N   . THR A 1 39  ? 44.186 24.889 23.257  1.000 34.813  0 39  THR A N   1 
ATOM   135  C CA  . THR A 1 39  ? 45.177 25.942 23.360  1.000 34.756  0 39  THR A CA  1 
ATOM   136  C C   . THR A 1 39  ? 44.614 27.223 22.742  1.000 35.388  0 39  THR A C   1 
ATOM   137  O O   . THR A 1 39  ? 43.487 27.251 22.254  1.000 34.829  0 39  THR A O   1 
ATOM   138  C CB  . THR A 1 39  ? 46.496 25.552 22.670  1.000 37.433  0 39  THR A CB  1 
ATOM   139  O OG1 . THR A 1 39  ? 46.261 25.321 21.279  1.000 35.551  0 39  THR A OG1 1 
ATOM   140  C CG2 . THR A 1 39  ? 47.130 24.302 23.269  1.000 42.364  0 39  THR A CG2 1 
ATOM   141  N N   . GLY A 1 40  ? 45.431 28.271 22.778  1.000 34.625  0 40  GLY A N   1 
ATOM   142  C CA  . GLY A 1 40  ? 45.204 29.502 22.033  1.000 33.174  0 40  GLY A CA  1 
ATOM   143  C C   . GLY A 1 40  ? 43.948 30.258 22.455  1.000 36.585  0 40  GLY A C   1 
ATOM   144  O O   . GLY A 1 40  ? 43.612 30.321 23.646  1.000 35.454  0 40  GLY A O   1 
ATOM   145  N N   . PHE A 1 41  ? 43.307 30.905 21.455  1.000 34.895  0 41  PHE A N   1 
ATOM   146  C CA  . PHE A 1 41  ? 42.174 31.790 21.686  1.000 32.904  0 41  PHE A CA  1 
ATOM   147  C C   . PHE A 1 41  ? 41.041 31.041 22.367  1.000 32.324  0 41  PHE A C   1 
ATOM   148  O O   . PHE A 1 41  ? 40.402 31.570 23.258  1.000 33.861  0 41  PHE A O   1 
ATOM   149  C CB  . PHE A 1 41  ? 41.574 32.439 20.436  1.000 34.118  0 41  PHE A CB  1 
ATOM   150  C CG  . PHE A 1 41  ? 42.542 33.276 19.617  1.000 34.988  0 41  PHE A CG  1 
ATOM   151  C CD1 . PHE A 1 41  ? 43.444 34.138 20.209  1.000 37.729  0 41  PHE A CD1 1 
ATOM   152  C CD2 . PHE A 1 41  ? 42.542 33.177 18.237  1.000 34.603  0 41  PHE A CD2 1 
ATOM   153  C CE1 . PHE A 1 41  ? 44.274 34.925 19.434  1.000 39.241  0 41  PHE A CE1 1 
ATOM   154  C CE2 . PHE A 1 41  ? 43.379 33.953 17.473  1.000 34.632  0 41  PHE A CE2 1 
ATOM   155  C CZ  . PHE A 1 41  ? 44.264 34.800 18.072  1.000 35.427  0 41  PHE A CZ  1 
ATOM   156  N N   . GLY A 1 42  ? 40.802 29.810 21.941  1.000 30.943  0 42  GLY A N   1 
ATOM   157  C CA  . GLY A 1 42  ? 39.660 29.057 22.413  1.000 32.398  0 42  GLY A CA  1 
ATOM   158  C C   . GLY A 1 42  ? 39.820 28.628 23.872  1.000 33.014  0 42  GLY A C   1 
ATOM   159  O O   . GLY A 1 42  ? 38.856 28.645 24.635  1.000 33.270  0 42  GLY A O   1 
ATOM   160  N N   . ASN A 1 43  ? 41.047 28.312 24.282  1.000 34.622  0 43  ASN A N   1 
ATOM   161  C CA  . ASN A 1 43  ? 41.342 28.010 25.689  1.000 33.770  0 43  ASN A CA  1 
ATOM   162  C C   . ASN A 1 43  ? 41.082 29.238 26.570  1.000 32.950  0 43  ASN A C   1 
ATOM   163  O O   . ASN A 1 43  ? 40.446 29.149 27.613  1.000 35.942  0 43  ASN A O   1 
ATOM   164  C CB  . ASN A 1 43  ? 42.778 27.524 25.797  1.000 35.251  0 43  ASN A CB  1 
ATOM   165  C CG  . ASN A 1 43  ? 43.142 27.091 27.199  1.000 34.980  0 43  ASN A CG  1 
ATOM   166  O OD1 . ASN A 1 43  ? 43.577 27.906 28.007  1.000 35.838  0 43  ASN A OD1 1 
ATOM   167  N ND2 . ASN A 1 43  ? 42.897 25.835 27.503  1.000 35.545  0 43  ASN A ND2 1 
ATOM   168  N N   . LEU A 1 44  ? 41.623 30.388 26.168  1.000 31.835  0 44  LEU A N   1 
ATOM   169  C CA  . LEU A 1 44  ? 41.424 31.610 26.911  1.000 30.454  0 44  LEU A CA  1 
ATOM   170  C C   . LEU A 1 44  ? 39.948 32.000 26.943  1.000 35.766  0 44  LEU A C   1 
ATOM   171  O O   . LEU A 1 44  ? 39.454 32.455 27.982  1.000 35.180  0 44  LEU A O   1 
ATOM   172  C CB  . LEU A 1 44  ? 42.291 32.730 26.361  1.000 30.835  0 44  LEU A CB  1 
ATOM   173  C CG  . LEU A 1 44  ? 42.115 34.073 27.071  1.000 36.918  0 44  LEU A CG  1 
ATOM   174  C CD1 . LEU A 1 44  ? 42.436 33.928 28.548  1.000 38.871  0 44  LEU A CD1 1 
ATOM   175  C CD2 . LEU A 1 44  ? 42.941 35.182 26.437  1.000 38.193  0 44  LEU A CD2 1 
ATOM   176  N N   . ALA A 1 45  ? 39.242 31.859 25.799  1.000 34.391  0 45  ALA A N   1 
ATOM   177  C CA  . ALA A 1 45  ? 37.812 32.139 25.733  1.000 32.704  0 45  ALA A CA  1 
ATOM   178  C C   . ALA A 1 45  ? 37.054 31.270 26.735  1.000 32.742  0 45  ALA A C   1 
ATOM   179  O O   . ALA A 1 45  ? 36.193 31.775 27.444  1.000 30.898  0 45  ALA A O   1 
ATOM   180  C CB  . ALA A 1 45  ? 37.250 31.935 24.300  1.000 32.225  0 45  ALA A CB  1 
ATOM   181  N N   . ALA A 1 46  ? 37.300 29.950 26.722  1.000 31.019  0 46  ALA A N   1 
ATOM   182  C CA  . ALA A 1 46  ? 36.593 29.074 27.633  1.000 32.990  0 46  ALA A CA  1 
ATOM   183  C C   . ALA A 1 46  ? 36.781 29.516 29.087  1.000 33.755  0 46  ALA A C   1 
ATOM   184  O O   . ALA A 1 46  ? 35.816 29.582 29.858  1.000 34.656  0 46  ALA A O   1 
ATOM   185  C CB  . ALA A 1 46  ? 37.039 27.638 27.428  1.000 31.353  0 46  ALA A CB  1 
ATOM   186  N N   . ARG A 1 47  ? 38.026 29.795 29.474  1.000 33.441  0 47  ARG A N   1 
ATOM   187  C CA  . ARG A 1 47  ? 38.345 30.216 30.839  1.000 35.506  0 47  ARG A CA  1 
ATOM   188  C C   . ARG A 1 47  ? 37.697 31.546 31.175  1.000 38.514  0 47  ARG A C   1 
ATOM   189  O O   . ARG A 1 47  ? 37.184 31.730 32.289  1.000 37.005  0 47  ARG A O   1 
ATOM   190  C CB  . ARG A 1 47  ? 39.870 30.315 31.046  1.000 34.134  0 47  ARG A CB  1 
ATOM   191  C CG  . ARG A 1 47  ? 40.525 28.940 31.172  1.000 37.235  0 47  ARG A CG  1 
ATOM   192  C CD  . ARG A 1 47  ? 42.027 28.986 31.540  1.000 43.146  0 47  ARG A CD  1 
ATOM   193  N NE  . ARG A 1 47  ? 42.796 29.262 30.326  1.000 49.902  0 47  ARG A NE  1 
ATOM   194  C CZ  . ARG A 1 47  ? 43.533 30.346 30.063  1.000 55.026  0 47  ARG A CZ  1 
ATOM   195  N NH1 . ARG A 1 47  ? 43.725 31.244 31.015  1.000 58.178  0 47  ARG A NH1 1 
ATOM   196  N NH2 . ARG A 1 47  ? 44.118 30.498 28.863  1.000 46.888  0 47  ARG A NH2 1 
ATOM   197  N N   . THR A 1 48  ? 37.728 32.484 30.220  1.000 34.136  0 48  THR A N   1 
ATOM   198  C CA  . THR A 1 48  ? 37.188 33.823 30.452  1.000 33.057  0 48  THR A CA  1 
ATOM   199  C C   . THR A 1 48  ? 35.670 33.760 30.627  1.000 35.555  0 48  THR A C   1 
ATOM   200  O O   . THR A 1 48  ? 35.102 34.425 31.499  1.000 36.927  0 48  THR A O   1 
ATOM   201  C CB  . THR A 1 48  ? 37.533 34.733 29.268  1.000 36.066  0 48  THR A CB  1 
ATOM   202  O OG1 . THR A 1 48  ? 38.952 34.733 29.190  1.000 38.099  0 48  THR A OG1 1 
ATOM   203  C CG2 . THR A 1 48  ? 36.995 36.157 29.422  1.000 41.200  0 48  THR A CG2 1 
ATOM   204  N N   . PHE A 1 49  ? 34.982 33.014 29.761  1.000 33.759  0 49  PHE A N   1 
ATOM   205  C CA  . PHE A 1 49  ? 33.521 33.017 29.795  1.000 33.482  0 49  PHE A CA  1 
ATOM   206  C C   . PHE A 1 49  ? 33.006 32.206 30.981  1.000 36.722  0 49  PHE A C   1 
ATOM   207  O O   . PHE A 1 49  ? 31.923 32.483 31.491  1.000 37.396  0 49  PHE A O   1 
ATOM   208  C CB  . PHE A 1 49  ? 32.935 32.569 28.454  1.000 36.660  0 49  PHE A CB  1 
ATOM   209  C CG  . PHE A 1 49  ? 33.278 33.570 27.359  1.000 38.524  0 49  PHE A CG  1 
ATOM   210  C CD1 . PHE A 1 49  ? 33.210 34.943 27.605  1.000 45.783  0 49  PHE A CD1 1 
ATOM   211  C CD2 . PHE A 1 49  ? 33.775 33.148 26.134  1.000 39.744  0 49  PHE A CD2 1 
ATOM   212  C CE1 . PHE A 1 49  ? 33.576 35.865 26.637  1.000 51.891  0 49  PHE A CE1 1 
ATOM   213  C CE2 . PHE A 1 49  ? 34.154 34.075 25.172  1.000 38.951  0 49  PHE A CE2 1 
ATOM   214  C CZ  . PHE A 1 49  ? 34.078 35.423 25.425  1.000 44.478  0 49  PHE A CZ  1 
ATOM   215  N N   . ASP A 1 50  ? 33.759 31.175 31.371  1.000 36.855  0 50  ASP A N   1 
ATOM   216  C CA  . ASP A 1 50  ? 33.471 30.446 32.602  1.000 41.398  0 50  ASP A CA  1 
ATOM   217  C C   . ASP A 1 50  ? 33.471 31.389 33.818  1.000 42.955  0 50  ASP A C   1 
ATOM   218  O O   . ASP A 1 50  ? 32.512 31.444 34.590  1.000 40.250  0 50  ASP A O   1 
ATOM   219  C CB  . ASP A 1 50  ? 34.443 29.293 32.789  1.000 39.352  0 50  ASP A CB  1 
ATOM   220  C CG  . ASP A 1 50  ? 34.215 28.501 34.078  1.000 44.257  0 50  ASP A CG  1 
ATOM   221  O OD1 . ASP A 1 50  ? 35.153 28.426 34.917  1.000 41.239  0 50  ASP A OD1 1 
ATOM   222  O OD2 . ASP A 1 50  ? 33.073 28.058 34.279  1.000 40.589  0 50  ASP A OD2 1 
ATOM   223  N N   . LYS A 1 51  ? 34.498 32.229 33.921  1.000 43.760  0 51  LYS A N   1 
ATOM   224  C CA  . LYS A 1 51  ? 34.634 33.133 35.056  1.000 47.185  0 51  LYS A CA  1 
ATOM   225  C C   . LYS A 1 51  ? 33.561 34.214 34.968  1.000 48.034  0 51  LYS A C   1 
ATOM   226  O O   . LYS A 1 51  ? 33.094 34.677 35.984  1.000 41.813  0 51  LYS A O   1 
ATOM   227  C CB  . LYS A 1 51  ? 36.081 33.618 35.197  1.000 55.513  0 51  LYS A CB  1 
ATOM   228  C CG  . LYS A 1 51  ? 36.293 35.115 35.397  1.000 73.598  0 51  LYS A CG  1 
ATOM   229  C CD  . LYS A 1 51  ? 36.324 35.851 34.052  1.000 101.692 0 51  LYS A CD  1 
ATOM   230  C CE  . LYS A 1 51  ? 35.842 37.278 34.051  1.000 112.199 0 51  LYS A CE  1 
ATOM   231  N NZ  . LYS A 1 51  ? 36.507 38.080 35.082  1.000 114.729 0 51  LYS A NZ  1 
ATOM   232  N N   . LYS A 1 52  ? 33.142 34.587 33.760  1.000 43.401  0 52  LYS A N   1 
ATOM   233  C CA  . LYS A 1 52  ? 32.125 35.602 33.561  1.000 46.200  0 52  LYS A CA  1 
ATOM   234  C C   . LYS A 1 52  ? 30.738 35.087 33.948  1.000 48.510  0 52  LYS A C   1 
ATOM   235  O O   . LYS A 1 52  ? 29.838 35.879 34.175  1.000 52.403  0 52  LYS A O   1 
ATOM   236  C CB  . LYS A 1 52  ? 32.121 36.009 32.086  1.000 52.656  0 52  LYS A CB  1 
ATOM   237  C CG  . LYS A 1 52  ? 31.870 37.461 31.829  1.000 65.382  0 52  LYS A CG  1 
ATOM   238  C CD  . LYS A 1 52  ? 31.176 37.621 30.485  1.000 76.998  0 52  LYS A CD  1 
ATOM   239  C CE  . LYS A 1 52  ? 30.500 38.938 30.306  1.000 80.615  0 52  LYS A CE  1 
ATOM   240  N NZ  . LYS A 1 52  ? 31.453 39.995 29.975  1.000 76.738  0 52  LYS A NZ  1 
ATOM   241  N N   . GLY A 1 53  ? 30.515 33.771 33.956  1.000 42.526  0 53  GLY A N   1 
ATOM   242  C CA  . GLY A 1 53  ? 29.242 33.251 34.431  1.000 44.053  0 53  GLY A CA  1 
ATOM   243  C C   . GLY A 1 53  ? 28.429 32.517 33.361  1.000 48.122  0 53  GLY A C   1 
ATOM   244  O O   . GLY A 1 53  ? 27.344 32.003 33.653  1.000 42.235  0 53  GLY A O   1 
ATOM   245  N N   . PHE A 1 54  ? 28.930 32.480 32.110  1.000 41.273  0 54  PHE A N   1 
ATOM   246  C CA  . PHE A 1 54  ? 28.290 31.671 31.097  1.000 35.875  0 54  PHE A CA  1 
ATOM   247  C C   . PHE A 1 54  ? 28.477 30.208 31.475  1.000 33.937  0 54  PHE A C   1 
ATOM   248  O O   . PHE A 1 54  ? 29.400 29.848 32.200  1.000 38.357  0 54  PHE A O   1 
ATOM   249  C CB  . PHE A 1 54  ? 28.873 31.891 29.696  1.000 36.609  0 54  PHE A CB  1 
ATOM   250  C CG  . PHE A 1 54  ? 28.440 33.156 29.005  1.000 37.575  0 54  PHE A CG  1 
ATOM   251  C CD1 . PHE A 1 54  ? 27.176 33.262 28.437  1.000 38.221  0 54  PHE A CD1 1 
ATOM   252  C CD2 . PHE A 1 54  ? 29.302 34.229 28.905  1.000 38.817  0 54  PHE A CD2 1 
ATOM   253  C CE1 . PHE A 1 54  ? 26.784 34.429 27.795  1.000 37.822  0 54  PHE A CE1 1 
ATOM   254  C CE2 . PHE A 1 54  ? 28.906 35.383 28.244  1.000 40.921  0 54  PHE A CE2 1 
ATOM   255  C CZ  . PHE A 1 54  ? 27.649 35.481 27.703  1.000 38.660  0 54  PHE A CZ  1 
ATOM   256  N N   . ARG A 1 55  ? 27.573 29.385 30.978  1.000 34.563  0 55  ARG A N   1 
ATOM   257  C CA  . ARG A 1 55  ? 27.724 27.940 30.940  1.000 32.172  0 55  ARG A CA  1 
ATOM   258  C C   . ARG A 1 55  ? 28.463 27.509 29.668  1.000 35.269  0 55  ARG A C   1 
ATOM   259  O O   . ARG A 1 55  ? 27.883 27.434 28.574  1.000 34.716  0 55  ARG A O   1 
ATOM   260  C CB  . ARG A 1 55  ? 26.327 27.339 31.008  1.000 37.494  0 55  ARG A CB  1 
ATOM   261  C CG  . ARG A 1 55  ? 25.503 27.810 32.206  1.000 39.070  0 55  ARG A CG  1 
ATOM   262  C CD  . ARG A 1 55  ? 24.124 27.216 32.205  1.000 41.674  0 55  ARG A CD  1 
ATOM   263  N NE  . ARG A 1 55  ? 23.239 27.874 33.177  1.000 45.953  0 55  ARG A NE  1 
ATOM   264  C CZ  . ARG A 1 55  ? 22.142 27.291 33.633  1.000 49.982  0 55  ARG A CZ  1 
ATOM   265  N NH1 . ARG A 1 55  ? 21.906 26.050 33.276  1.000 48.437  0 55  ARG A NH1 1 
ATOM   266  N NH2 . ARG A 1 55  ? 21.311 27.916 34.448  1.000 45.369  0 55  ARG A NH2 1 
ATOM   267  N N   . VAL A 1 56  ? 29.753 27.214 29.806  1.000 33.620  0 56  VAL A N   1 
ATOM   268  C CA  . VAL A 1 56  ? 30.612 26.965 28.667  1.000 32.370  0 56  VAL A CA  1 
ATOM   269  C C   . VAL A 1 56  ? 30.577 25.477 28.350  1.000 34.349  0 56  VAL A C   1 
ATOM   270  O O   . VAL A 1 56  ? 30.677 24.647 29.237  1.000 34.594  0 56  VAL A O   1 
ATOM   271  C CB  . VAL A 1 56  ? 32.043 27.459 28.908  1.000 34.407  0 56  VAL A CB  1 
ATOM   272  C CG1 . VAL A 1 56  ? 32.967 27.074 27.762  1.000 38.210  0 56  VAL A CG1 1 
ATOM   273  C CG2 . VAL A 1 56  ? 32.087 28.966 29.146  1.000 36.096  0 56  VAL A CG2 1 
ATOM   274  N N   . ILE A 1 57  ? 30.425 25.174 27.062  1.000 32.722  0 57  ILE A N   1 
ATOM   275  C CA  . ILE A 1 57  ? 30.628 23.844 26.520  1.000 30.217  0 57  ILE A CA  1 
ATOM   276  C C   . ILE A 1 57  ? 31.872 23.943 25.648  1.000 38.544  0 57  ILE A C   1 
ATOM   277  O O   . ILE A 1 57  ? 31.837 24.488 24.545  1.000 35.253  0 57  ILE A O   1 
ATOM   278  C CB  . ILE A 1 57  ? 29.399 23.319 25.767  1.000 32.807  0 57  ILE A CB  1 
ATOM   279  C CG1 . ILE A 1 57  ? 28.117 23.503 26.591  1.000 40.069  0 57  ILE A CG1 1 
ATOM   280  C CG2 . ILE A 1 57  ? 29.613 21.862 25.344  1.000 34.190  0 57  ILE A CG2 1 
ATOM   281  C CD1 . ILE A 1 57  ? 26.816 23.188 25.874  1.000 41.353  0 57  ILE A CD1 1 
ATOM   282  N N   . ALA A 1 58  ? 32.989 23.478 26.195  1.000 34.809  0 58  ALA A N   1 
ATOM   283  C CA  . ALA A 1 58  ? 34.301 23.622 25.578  1.000 34.179  0 58  ALA A CA  1 
ATOM   284  C C   . ALA A 1 58  ? 34.685 22.358 24.824  1.000 39.156  0 58  ALA A C   1 
ATOM   285  O O   . ALA A 1 58  ? 35.063 21.361 25.434  1.000 39.393  0 58  ALA A O   1 
ATOM   286  C CB  . ALA A 1 58  ? 35.308 23.926 26.666  1.000 35.213  0 58  ALA A CB  1 
ATOM   287  N N   . ALA A 1 59  ? 34.676 22.425 23.487  1.000 33.999  0 59  ALA A N   1 
ATOM   288  C CA  . ALA A 1 59  ? 35.067 21.295 22.673  1.000 37.329  0 59  ALA A CA  1 
ATOM   289  C C   . ALA A 1 59  ? 36.582 21.320 22.480  1.000 39.239  0 59  ALA A C   1 
ATOM   290  O O   . ALA A 1 59  ? 37.139 22.362 22.197  1.000 38.673  0 59  ALA A O   1 
ATOM   291  C CB  . ALA A 1 59  ? 34.339 21.281 21.345  1.000 38.429  0 59  ALA A CB  1 
ATOM   292  N N   . CYS A 1 60  ? 37.221 20.171 22.719  1.000 35.645  0 60  CYS A N   1 
ATOM   293  C CA  . CYS A 1 60  ? 38.664 20.016 22.704  1.000 36.329  0 60  CYS A CA  1 
ATOM   294  C C   . CYS A 1 60  ? 38.978 18.879 21.738  1.000 37.010  0 60  CYS A C   1 
ATOM   295  O O   . CYS A 1 60  ? 38.223 17.909 21.646  1.000 37.639  0 60  CYS A O   1 
ATOM   296  C CB  . CYS A 1 60  ? 39.206 19.678 24.094  1.000 38.062  0 60  CYS A CB  1 
ATOM   297  S SG  . CYS A 1 60  ? 39.022 21.027 25.299  1.000 41.520  0 60  CYS A SG  1 
ATOM   298  N N   . LEU A 1 61  ? 40.080 19.027 21.011  1.000 36.995  0 61  LEU A N   1 
ATOM   299  C CA  . LEU A 1 61  ? 40.574 18.000 20.128  1.000 35.555  0 61  LEU A CA  1 
ATOM   300  C C   . LEU A 1 61  ? 41.182 16.840 20.924  1.000 40.116  0 61  LEU A C   1 
ATOM   301  O O   . LEU A 1 61  ? 41.146 15.743 20.419  1.000 38.902  0 61  LEU A O   1 
ATOM   302  C CB  . LEU A 1 61  ? 41.609 18.621 19.194  1.000 36.668  0 61  LEU A CB  1 
ATOM   303  C CG  . LEU A 1 61  ? 42.264 17.676 18.183  1.000 39.632  0 61  LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 61  ? 41.249 17.069 17.268  1.000 42.015  0 61  LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 61  ? 43.405 18.323 17.378  1.000 44.955  0 61  LEU A CD2 1 
ATOM   306  N N   . THR A 1 62  ? 41.814 17.093 22.089  1.000 42.129  0 62  THR A N   1 
ATOM   307  C CA  . THR A 1 62  ? 42.605 16.070 22.785  1.000 43.154  0 62  THR A CA  1 
ATOM   308  C C   . THR A 1 62  ? 42.103 15.883 24.224  1.000 41.849  0 62  THR A C   1 
ATOM   309  O O   . THR A 1 62  ? 41.609 16.799 24.874  1.000 38.331  0 62  THR A O   1 
ATOM   310  C CB  . THR A 1 62  ? 44.105 16.401 22.784  1.000 43.532  0 62  THR A CB  1 
ATOM   311  O OG1 . THR A 1 62  ? 44.312 17.579 23.560  1.000 40.744  0 62  THR A OG1 1 
ATOM   312  C CG2 . THR A 1 62  ? 44.697 16.634 21.399  1.000 45.323  0 62  THR A CG2 1 
ATOM   313  N N   . GLU A 1 63  ? 42.250 14.660 24.730  1.000 42.455  0 63  GLU A N   1 
ATOM   314  C CA  . GLU A 1 63  ? 41.975 14.357 26.128  1.000 45.116  0 63  GLU A CA  1 
ATOM   315  C C   . GLU A 1 63  ? 42.830 15.194 27.088  1.000 41.225  0 63  GLU A C   1 
ATOM   316  O O   . GLU A 1 63  ? 42.304 15.695 28.092  1.000 43.497  0 63  GLU A O   1 
ATOM   317  C CB  . GLU A 1 63  ? 42.190 12.853 26.345  1.000 55.941  0 63  GLU A CB  1 
ATOM   318  C CG  . GLU A 1 63  ? 41.854 12.396 27.764  1.000 63.797  0 63  GLU A CG  1 
ATOM   319  C CD  . GLU A 1 63  ? 40.499 12.883 28.266  1.000 70.287  0 63  GLU A CD  1 
ATOM   320  O OE1 . GLU A 1 63  ? 39.460 12.774 27.544  1.000 71.849  0 63  GLU A OE1 1 
ATOM   321  O OE2 . GLU A 1 63  ? 40.528 13.419 29.398  1.000 63.927  0 63  GLU A OE2 1 
ATOM   322  N N   . SER A 1 64  ? 44.133 15.392 26.806  1.000 38.889  0 64  SER A N   1 
ATOM   323  C CA  . SER A 1 64  ? 44.933 16.108 27.776  1.000 43.285  0 64  SER A CA  1 
ATOM   324  C C   . SER A 1 64  ? 44.593 17.595 27.759  1.000 40.878  0 64  SER A C   1 
ATOM   325  O O   . SER A 1 64  ? 44.700 18.273 28.787  1.000 41.108  0 64  SER A O   1 
ATOM   326  C CB  . SER A 1 64  ? 46.409 15.860 27.597  1.000 52.187  0 64  SER A CB  1 
ATOM   327  O OG  . SER A 1 64  ? 46.843 16.290 26.326  1.000 56.574  0 64  SER A OG  1 
ATOM   328  N N   . GLY A 1 65  ? 44.183 18.114 26.592  1.000 37.694  0 65  GLY A N   1 
ATOM   329  C CA  . GLY A 1 65  ? 43.719 19.492 26.562  1.000 38.678  0 65  GLY A CA  1 
ATOM   330  C C   . GLY A 1 65  ? 42.439 19.639 27.378  1.000 34.834  0 65  GLY A C   1 
ATOM   331  O O   . GLY A 1 65  ? 42.281 20.611 28.110  1.000 38.017  0 65  GLY A O   1 
ATOM   332  N N   . SER A 1 66  ? 41.518 18.687 27.215  1.000 37.733  0 66  SER A N   1 
ATOM   333  C CA  . SER A 1 66  ? 40.262 18.665 27.957  1.000 40.874  0 66  SER A CA  1 
ATOM   334  C C   . SER A 1 66  ? 40.494 18.589 29.486  1.000 38.528  0 66  SER A C   1 
ATOM   335  O O   . SER A 1 66  ? 39.950 19.370 30.276  1.000 40.045  0 66  SER A O   1 
ATOM   336  C CB  . SER A 1 66  ? 39.464 17.498 27.461  1.000 45.085  0 66  SER A CB  1 
ATOM   337  O OG  . SER A 1 66  ? 38.304 17.330 28.247  1.000 49.449  0 66  SER A OG  1 
ATOM   338  N N   . ALA A 1 67  ? 41.365 17.676 29.927  1.000 40.156  0 67  ALA A N   1 
ATOM   339  C CA  . ALA A 1 67  ? 41.609 17.488 31.363  1.000 43.652  0 67  ALA A CA  1 
ATOM   340  C C   . ALA A 1 67  ? 42.248 18.731 32.001  1.000 37.738  0 67  ALA A C   1 
ATOM   341  O O   . ALA A 1 67  ? 41.864 19.157 33.090  1.000 37.579  0 67  ALA A O   1 
ATOM   342  C CB  . ALA A 1 67  ? 42.431 16.222 31.566  1.000 43.085  0 67  ALA A CB  1 
ATOM   343  N N   . ALA A 1 68  ? 43.191 19.377 31.304  1.000 35.278  0 68  ALA A N   1 
ATOM   344  C CA  . ALA A 1 68  ? 43.801 20.590 31.796  1.000 36.728  0 68  ALA A CA  1 
ATOM   345  C C   . ALA A 1 68  ? 42.774 21.700 31.929  1.000 40.054  0 68  ALA A C   1 
ATOM   346  O O   . ALA A 1 68  ? 42.803 22.435 32.891  1.000 38.720  0 68  ALA A O   1 
ATOM   347  C CB  . ALA A 1 68  ? 44.955 21.039 30.906  1.000 41.499  0 68  ALA A CB  1 
ATOM   348  N N   . LEU A 1 69  ? 41.926 21.900 30.908  1.000 37.798  0 69  LEU A N   1 
ATOM   349  C CA  . LEU A 1 69  ? 40.944 22.970 30.951  1.000 34.746  0 69  LEU A CA  1 
ATOM   350  C C   . LEU A 1 69  ? 39.930 22.731 32.077  1.000 32.903  0 69  LEU A C   1 
ATOM   351  O O   . LEU A 1 69  ? 39.530 23.654 32.793  1.000 34.187  0 69  LEU A O   1 
ATOM   352  C CB  . LEU A 1 69  ? 40.241 23.051 29.595  1.000 34.582  0 69  LEU A CB  1 
ATOM   353  C CG  . LEU A 1 69  ? 39.114 24.077 29.532  1.000 36.196  0 69  LEU A CG  1 
ATOM   354  C CD1 . LEU A 1 69  ? 39.597 25.466 29.852  1.000 37.624  0 69  LEU A CD1 1 
ATOM   355  C CD2 . LEU A 1 69  ? 38.504 24.022 28.147  1.000 37.757  0 69  LEU A CD2 1 
ATOM   356  N N   . LYS A 1 70  ? 39.476 21.494 32.211  1.000 34.381  0 70  LYS A N   1 
ATOM   357  C CA  . LYS A 1 70  ? 38.534 21.161 33.273  1.000 38.066  0 70  LYS A CA  1 
ATOM   358  C C   . LYS A 1 70  ? 39.149 21.443 34.660  1.000 37.976  0 70  LYS A C   1 
ATOM   359  O O   . LYS A 1 70  ? 38.511 22.026 35.529  1.000 37.124  0 70  LYS A O   1 
ATOM   360  C CB  . LYS A 1 70  ? 38.239 19.675 33.077  1.000 44.900  0 70  LYS A CB  1 
ATOM   361  C CG  . LYS A 1 70  ? 37.051 19.235 33.887  1.000 61.614  0 70  LYS A CG  1 
ATOM   362  C CD  . LYS A 1 70  ? 36.698 17.753 33.795  1.000 78.785  0 70  LYS A CD  1 
ATOM   363  C CE  . LYS A 1 70  ? 35.526 17.456 34.707  1.000 88.176  0 70  LYS A CE  1 
ATOM   364  N NZ  . LYS A 1 70  ? 35.198 16.032 34.806  1.000 85.756  0 70  LYS A NZ  1 
ATOM   365  N N   . ALA A 1 71  ? 40.447 21.114 34.835  1.000 33.055  0 71  ALA A N   1 
ATOM   366  C CA  . ALA A 1 71  ? 41.104 21.306 36.125  1.000 35.793  0 71  ALA A CA  1 
ATOM   367  C C   . ALA A 1 71  ? 41.196 22.791 36.474  1.000 38.760  0 71  ALA A C   1 
ATOM   368  O O   . ALA A 1 71  ? 41.285 23.147 37.635  1.000 40.481  0 71  ALA A O   1 
ATOM   369  C CB  . ALA A 1 71  ? 42.467 20.691 36.086  1.000 38.409  0 71  ALA A CB  1 
ATOM   370  N N   . LYS A 1 72  ? 41.202 23.672 35.469  1.000 37.968  0 72  LYS A N   1 
ATOM   371  C CA  . LYS A 1 72  ? 41.339 25.114 35.711  1.000 36.004  0 72  LYS A CA  1 
ATOM   372  C C   . LYS A 1 72  ? 40.012 25.851 35.827  1.000 36.490  0 72  LYS A C   1 
ATOM   373  O O   . LYS A 1 72  ? 40.010 27.063 36.051  1.000 39.074  0 72  LYS A O   1 
ATOM   374  C CB  . LYS A 1 72  ? 42.086 25.771 34.548  1.000 41.110  0 72  LYS A CB  1 
ATOM   375  C CG  . LYS A 1 72  ? 43.485 25.237 34.353  1.000 45.158  0 72  LYS A CG  1 
ATOM   376  C CD  . LYS A 1 72  ? 44.223 25.737 33.122  1.000 47.687  0 72  LYS A CD  1 
ATOM   377  C CE  . LYS A 1 72  ? 45.545 25.053 33.051  1.000 49.216  0 72  LYS A CE  1 
ATOM   378  N NZ  . LYS A 1 72  ? 46.282 25.374 31.838  1.000 47.994  0 72  LYS A NZ  1 
ATOM   379  N N   . THR A 1 73  ? 38.882 25.172 35.614  1.000 36.556  0 73  THR A N   1 
ATOM   380  C CA  . THR A 1 73  ? 37.630 25.903 35.507  1.000 38.699  0 73  THR A CA  1 
ATOM   381  C C   . THR A 1 73  ? 36.637 25.442 36.567  1.000 39.135  0 73  THR A C   1 
ATOM   382  O O   . THR A 1 73  ? 36.852 24.418 37.233  1.000 42.146  0 73  THR A O   1 
ATOM   383  C CB  . THR A 1 73  ? 37.097 25.752 34.083  1.000 34.292  0 73  THR A CB  1 
ATOM   384  O OG1 . THR A 1 73  ? 37.116 24.368 33.675  1.000 35.263  0 73  THR A OG1 1 
ATOM   385  C CG2 . THR A 1 73  ? 37.977 26.522 33.117  1.000 36.585  0 73  THR A CG2 1 
ATOM   386  N N   . SER A 1 74  ? 35.497 26.143 36.603  1.000 41.000  0 74  SER A N   1 
ATOM   387  C CA  . SER A 1 74  ? 34.403 25.845 37.528  1.000 42.575  0 74  SER A CA  1 
ATOM   388  C C   . SER A 1 74  ? 33.551 24.672 37.066  1.000 45.695  0 74  SER A C   1 
ATOM   389  O O   . SER A 1 74  ? 33.649 24.190 35.931  1.000 44.652  0 74  SER A O   1 
ATOM   390  C CB  . SER A 1 74  ? 33.497 27.039 37.743  1.000 45.442  0 74  SER A CB  1 
ATOM   391  O OG  . SER A 1 74  ? 32.531 27.156 36.691  1.000 44.684  0 74  SER A OG  1 
ATOM   392  N N   . GLU A 1 75  ? 32.649 24.261 37.973  1.000 46.614  0 75  GLU A N   1 
ATOM   393  C CA  . GLU A 1 75  ? 31.659 23.216 37.713  1.000 54.755  0 75  GLU A CA  1 
ATOM   394  C C   . GLU A 1 75  ? 30.630 23.601 36.647  1.000 45.849  0 75  GLU A C   1 
ATOM   395  O O   . GLU A 1 75  ? 29.901 22.747 36.151  1.000 48.638  0 75  GLU A O   1 
ATOM   396  C CB  . GLU A 1 75  ? 30.882 22.919 39.001  1.000 61.098  0 75  GLU A CB  1 
ATOM   397  C CG  . GLU A 1 75  ? 31.670 22.068 39.992  1.000 73.139  0 75  GLU A CG  1 
ATOM   398  C CD  . GLU A 1 75  ? 31.876 20.656 39.480  1.000 76.801  0 75  GLU A CD  1 
ATOM   399  O OE1 . GLU A 1 75  ? 30.925 20.096 38.902  1.000 80.308  0 75  GLU A OE1 1 
ATOM   400  O OE2 . GLU A 1 75  ? 32.979 20.117 39.665  1.000 87.100  0 75  GLU A OE2 1 
ATOM   401  N N   . ARG A 1 76  ? 30.485 24.892 36.333  1.000 44.511  0 76  ARG A N   1 
ATOM   402  C CA  . ARG A 1 76  ? 29.550 25.308 35.289  1.000 44.188  0 76  ARG A CA  1 
ATOM   403  C C   . ARG A 1 76  ? 30.043 24.911 33.885  1.000 47.427  0 76  ARG A C   1 
ATOM   404  O O   . ARG A 1 76  ? 29.264 24.977 32.934  1.000 43.110  0 76  ARG A O   1 
ATOM   405  C CB  . ARG A 1 76  ? 29.382 26.836 35.309  1.000 49.392  0 76  ARG A CB  1 
ATOM   406  C CG  . ARG A 1 76  ? 28.756 27.475 36.549  1.000 60.968  0 76  ARG A CG  1 
ATOM   407  C CD  . ARG A 1 76  ? 28.687 28.993 36.346  1.000 63.141  0 76  ARG A CD  1 
ATOM   408  N NE  . ARG A 1 76  ? 30.002 29.647 36.221  1.000 67.632  0 76  ARG A NE  1 
ATOM   409  C CZ  . ARG A 1 76  ? 30.760 29.955 37.284  1.000 73.199  0 76  ARG A CZ  1 
ATOM   410  N NH1 . ARG A 1 76  ? 30.342 29.627 38.490  1.000 76.768  0 76  ARG A NH1 1 
ATOM   411  N NH2 . ARG A 1 76  ? 31.911 30.604 37.191  1.000 64.697  0 76  ARG A NH2 1 
ATOM   412  N N   . LEU A 1 77  ? 31.356 24.627 33.707  1.000 38.516  0 77  LEU A N   1 
ATOM   413  C CA  . LEU A 1 77  ? 31.928 24.337 32.390  1.000 41.002  0 77  LEU A CA  1 
ATOM   414  C C   . LEU A 1 77  ? 31.879 22.831 32.117  1.000 44.662  0 77  LEU A C   1 
ATOM   415  O O   . LEU A 1 77  ? 32.152 22.063 33.019  1.000 39.174  0 77  LEU A O   1 
ATOM   416  C CB  . LEU A 1 77  ? 33.368 24.847 32.308  1.000 39.487  0 77  LEU A CB  1 
ATOM   417  C CG  . LEU A 1 77  ? 34.068 24.627 30.962  1.000 38.867  0 77  LEU A CG  1 
ATOM   418  C CD1 . LEU A 1 77  ? 34.990 25.776 30.670  1.000 42.046  0 77  LEU A CD1 1 
ATOM   419  C CD2 . LEU A 1 77  ? 34.830 23.301 30.945  1.000 35.856  0 77  LEU A CD2 1 
ATOM   420  N N   . HIS A 1 78  ? 31.486 22.409 30.907  1.000 36.065  0 78  HIS A N   1 
ATOM   421  C CA  A HIS A 1 78  ? 31.611 21.007 30.493  0.500 36.820  0 78  HIS A CA  1 
ATOM   422  C CA  B HIS A 1 78  ? 31.584 21.018 30.473  0.500 36.919  0 78  HIS A CA  1 
ATOM   423  C C   . HIS A 1 78  ? 32.588 20.959 29.329  1.000 42.123  0 78  HIS A C   1 
ATOM   424  O O   . HIS A 1 78  ? 32.576 21.852 28.485  1.000 39.343  0 78  HIS A O   1 
ATOM   425  C CB  A HIS A 1 78  ? 30.263 20.363 30.099  0.500 39.751  0 78  HIS A CB  1 
ATOM   426  C CB  B HIS A 1 78  ? 30.207 20.507 30.015  0.500 39.420  0 78  HIS A CB  1 
ATOM   427  C CG  A HIS A 1 78  ? 30.272 18.852 30.008  0.500 43.258  0 78  HIS A CG  1 
ATOM   428  C CG  B HIS A 1 78  ? 29.230 20.290 31.127  0.500 43.926  0 78  HIS A CG  1 
ATOM   429  N ND1 A HIS A 1 78  ? 30.230 18.131 28.828  0.500 46.504  0 78  HIS A ND1 1 
ATOM   430  N ND1 B HIS A 1 78  ? 28.659 21.312 31.862  0.500 51.102  0 78  HIS A ND1 1 
ATOM   431  C CD2 A HIS A 1 78  ? 30.267 17.924 30.986  0.500 46.207  0 78  HIS A CD2 1 
ATOM   432  C CD2 B HIS A 1 78  ? 28.773 19.149 31.667  0.500 44.332  0 78  HIS A CD2 1 
ATOM   433  C CE1 A HIS A 1 78  ? 30.247 16.822 29.092  0.500 45.326  0 78  HIS A CE1 1 
ATOM   434  C CE1 B HIS A 1 78  ? 27.870 20.796 32.798  0.500 47.337  0 78  HIS A CE1 1 
ATOM   435  N NE2 A HIS A 1 78  ? 30.285 16.675 30.396  0.500 44.607  0 78  HIS A NE2 1 
ATOM   436  N NE2 B HIS A 1 78  ? 27.912 19.487 32.682  0.500 43.927  0 78  HIS A NE2 1 
ATOM   437  N N   . THR A 1 79  ? 33.428 19.906 29.272  1.000 38.298  0 79  THR A N   1 
ATOM   438  C CA  . THR A 1 79  ? 34.275 19.679 28.105  1.000 39.591  0 79  THR A CA  1 
ATOM   439  C C   . THR A 1 79  ? 33.689 18.528 27.311  1.000 46.912  0 79  THR A C   1 
ATOM   440  O O   . THR A 1 79  ? 33.022 17.687 27.896  1.000 40.524  0 79  THR A O   1 
ATOM   441  C CB  . THR A 1 79  ? 35.748 19.372 28.406  1.000 42.208  0 79  THR A CB  1 
ATOM   442  O OG1 . THR A 1 79  ? 35.840 18.253 29.286  1.000 41.183  0 79  THR A OG1 1 
ATOM   443  C CG2 . THR A 1 79  ? 36.467 20.511 29.079  1.000 38.840  0 79  THR A CG2 1 
ATOM   444  N N   . VAL A 1 80  ? 33.902 18.563 25.976  1.000 39.352  0 80  VAL A N   1 
ATOM   445  C CA  A VAL A 1 80  ? 33.572 17.459 25.087  0.500 36.956  0 80  VAL A CA  1 
ATOM   446  C CA  B VAL A 1 80  ? 33.575 17.454 25.094  0.500 39.717  0 80  VAL A CA  1 
ATOM   447  C C   . VAL A 1 80  ? 34.746 17.292 24.131  1.000 37.305  0 80  VAL A C   1 
ATOM   448  O O   . VAL A 1 80  ? 35.381 18.263 23.779  1.000 41.309  0 80  VAL A O   1 
ATOM   449  C CB  A VAL A 1 80  ? 32.265 17.650 24.291  0.500 38.084  0 80  VAL A CB  1 
ATOM   450  C CB  B VAL A 1 80  ? 32.256 17.667 24.323  0.500 45.173  0 80  VAL A CB  1 
ATOM   451  C CG1 A VAL A 1 80  ? 31.028 17.497 25.161  0.500 44.127  0 80  VAL A CG1 1 
ATOM   452  C CG1 B VAL A 1 80  ? 31.750 16.383 23.673  0.500 45.409  0 80  VAL A CG1 1 
ATOM   453  C CG2 A VAL A 1 80  ? 32.239 18.973 23.525  0.500 32.336  0 80  VAL A CG2 1 
ATOM   454  C CG2 B VAL A 1 80  ? 31.169 18.278 25.197  0.500 51.491  0 80  VAL A CG2 1 
ATOM   455  N N   . LEU A 1 81  ? 34.990 16.065 23.689  1.000 37.060  0 81  LEU A N   1 
ATOM   456  C CA  . LEU A 1 81  ? 36.010 15.774 22.697  1.000 44.155  0 81  LEU A CA  1 
ATOM   457  C C   . LEU A 1 81  ? 35.348 15.910 21.330  1.000 42.544  0 81  LEU A C   1 
ATOM   458  O O   . LEU A 1 81  ? 34.329 15.296 21.060  1.000 40.485  0 81  LEU A O   1 
ATOM   459  C CB  . LEU A 1 81  ? 36.607 14.375 22.879  1.000 48.930  0 81  LEU A CB  1 
ATOM   460  C CG  . LEU A 1 81  ? 37.394 14.191 24.181  1.000 61.129  0 81  LEU A CG  1 
ATOM   461  C CD1 . LEU A 1 81  ? 37.727 12.715 24.442  1.000 61.696  0 81  LEU A CD1 1 
ATOM   462  C CD2 . LEU A 1 81  ? 38.642 15.076 24.138  1.000 60.004  0 81  LEU A CD2 1 
ATOM   463  N N   . LEU A 1 82  ? 35.937 16.748 20.484  1.000 42.512  0 82  LEU A N   1 
ATOM   464  C CA  . LEU A 1 82  ? 35.405 16.971 19.155  1.000 37.551  0 82  LEU A CA  1 
ATOM   465  C C   . LEU A 1 82  ? 36.561 17.222 18.204  1.000 38.023  0 82  LEU A C   1 
ATOM   466  O O   . LEU A 1 82  ? 37.330 18.167 18.420  1.000 36.968  0 82  LEU A O   1 
ATOM   467  C CB  . LEU A 1 82  ? 34.448 18.159 19.165  1.000 37.273  0 82  LEU A CB  1 
ATOM   468  C CG  . LEU A 1 82  ? 33.866 18.548 17.804  1.000 39.921  0 82  LEU A CG  1 
ATOM   469  C CD1 . LEU A 1 82  ? 33.055 17.393 17.220  1.000 42.360  0 82  LEU A CD1 1 
ATOM   470  C CD2 . LEU A 1 82  ? 33.052 19.813 17.950  1.000 41.402  0 82  LEU A CD2 1 
ATOM   471  N N   . ASP A 1 83  ? 36.594 16.403 17.139  1.000 35.265  0 83  ASP A N   1 
ATOM   472  C CA  . ASP A 1 83  ? 37.325 16.696 15.921  1.000 35.162  0 83  ASP A CA  1 
ATOM   473  C C   . ASP A 1 83  ? 36.299 17.198 14.897  1.000 36.925  0 83  ASP A C   1 
ATOM   474  O O   . ASP A 1 83  ? 35.401 16.463 14.493  1.000 34.928  0 83  ASP A O   1 
ATOM   475  C CB  . ASP A 1 83  ? 38.092 15.462 15.454  1.000 42.140  0 83  ASP A CB  1 
ATOM   476  C CG  . ASP A 1 83  ? 38.832 15.605 14.130  1.000 45.211  0 83  ASP A CG  1 
ATOM   477  O OD1 . ASP A 1 83  ? 38.663 16.644 13.420  1.000 42.753  0 83  ASP A OD1 1 
ATOM   478  O OD2 . ASP A 1 83  ? 39.624 14.719 13.841  1.000 47.080  0 83  ASP A OD2 1 
ATOM   479  N N   . VAL A 1 84  ? 36.437 18.469 14.447  1.000 36.702  0 84  VAL A N   1 
ATOM   480  C CA  . VAL A 1 84  ? 35.384 19.115 13.662  1.000 34.347  0 84  VAL A CA  1 
ATOM   481  C C   . VAL A 1 84  ? 35.338 18.522 12.245  1.000 34.602  0 84  VAL A C   1 
ATOM   482  O O   . VAL A 1 84  ? 34.372 18.755 11.529  1.000 38.073  0 84  VAL A O   1 
ATOM   483  C CB  . VAL A 1 84  ? 35.519 20.670 13.602  1.000 31.031  0 84  VAL A CB  1 
ATOM   484  C CG1 . VAL A 1 84  ? 35.444 21.302 14.968  1.000 31.526  0 84  VAL A CG1 1 
ATOM   485  C CG2 . VAL A 1 84  ? 36.789 21.161 12.914  1.000 34.422  0 84  VAL A CG2 1 
ATOM   486  N N   . THR A 1 85  ? 36.363 17.754 11.846  1.000 34.996  0 85  THR A N   1 
ATOM   487  C CA  . THR A 1 85  ? 36.395 17.084 10.548  1.000 34.804  0 85  THR A CA  1 
ATOM   488  C C   . THR A 1 85  ? 35.756 15.696 10.581  1.000 39.174  0 85  THR A C   1 
ATOM   489  O O   . THR A 1 85  ? 35.728 15.041 9.550   1.000 39.037  0 85  THR A O   1 
ATOM   490  C CB  . THR A 1 85  ? 37.820 16.965 10.000  1.000 37.960  0 85  THR A CB  1 
ATOM   491  O OG1 . THR A 1 85  ? 38.612 16.006 10.704  1.000 34.331  0 85  THR A OG1 1 
ATOM   492  C CG2 . THR A 1 85  ? 38.543 18.298 10.077  1.000 34.746  0 85  THR A CG2 1 
ATOM   493  N N   . ASP A 1 86  ? 35.227 15.262 11.722  1.000 38.409  0 86  ASP A N   1 
ATOM   494  C CA  . ASP A 1 86  ? 34.622 13.941 11.839  1.000 39.492  0 86  ASP A CA  1 
ATOM   495  C C   . ASP A 1 86  ? 33.109 14.132 11.924  1.000 36.734  0 86  ASP A C   1 
ATOM   496  O O   . ASP A 1 86  ? 32.601 14.555 12.958  1.000 38.287  0 86  ASP A O   1 
ATOM   497  C CB  . ASP A 1 86  ? 35.191 13.212 13.047  1.000 41.053  0 86  ASP A CB  1 
ATOM   498  C CG  . ASP A 1 86  ? 34.540 11.869 13.386  1.000 44.501  0 86  ASP A CG  1 
ATOM   499  O OD1 . ASP A 1 86  ? 33.448 11.554 12.859  1.000 45.093  0 86  ASP A OD1 1 
ATOM   500  O OD2 . ASP A 1 86  ? 35.126 11.178 14.214  1.000 49.667  0 86  ASP A OD2 1 
ATOM   501  N N   . PRO A 1 87  ? 32.346 13.954 10.822  1.000 37.245  0 87  PRO A N   1 
ATOM   502  C CA  . PRO A 1 87  ? 30.945 14.350 10.824  1.000 41.597  0 87  PRO A CA  1 
ATOM   503  C C   . PRO A 1 87  ? 30.084 13.588 11.836  1.000 39.525  0 87  PRO A C   1 
ATOM   504  O O   . PRO A 1 87  ? 29.136 14.160 12.381  1.000 39.448  0 87  PRO A O   1 
ATOM   505  C CB  . PRO A 1 87  ? 30.490 14.126 9.377   1.000 44.155  0 87  PRO A CB  1 
ATOM   506  C CG  . PRO A 1 87  ? 31.536 13.229 8.751   1.000 43.718  0 87  PRO A CG  1 
ATOM   507  C CD  . PRO A 1 87  ? 32.790 13.363 9.545   1.000 38.793  0 87  PRO A CD  1 
ATOM   508  N N   . GLU A 1 88  ? 30.425 12.312 12.086  1.000 42.212  0 88  GLU A N   1 
ATOM   509  C CA  . GLU A 1 88  ? 29.752 11.520 13.109  1.000 42.496  0 88  GLU A CA  1 
ATOM   510  C C   . GLU A 1 88  ? 29.954 12.101 14.509  1.000 37.876  0 88  GLU A C   1 
ATOM   511  O O   . GLU A 1 88  ? 29.011 12.142 15.276  1.000 39.882  0 88  GLU A O   1 
ATOM   512  C CB  . GLU A 1 88  ? 30.242 10.069 13.045  1.000 52.636  0 88  GLU A CB  1 
ATOM   513  C CG  . GLU A 1 88  ? 29.558 9.299  11.923  1.000 70.184  0 88  GLU A CG  1 
ATOM   514  C CD  . GLU A 1 88  ? 28.039 9.420  12.044  1.000 90.588  0 88  GLU A CD  1 
ATOM   515  O OE1 . GLU A 1 88  ? 27.493 9.001  13.093  1.000 92.681  0 88  GLU A OE1 1 
ATOM   516  O OE2 . GLU A 1 88  ? 27.401 9.994  11.131  1.000 96.817  0 88  GLU A OE2 1 
ATOM   517  N N   . ASN A 1 89  ? 31.176 12.538 14.847  1.000 36.835  0 89  ASN A N   1 
ATOM   518  C CA  . ASN A 1 89  ? 31.491 13.138 16.133  1.000 38.610  0 89  ASN A CA  1 
ATOM   519  C C   . ASN A 1 89  ? 30.738 14.477 16.222  1.000 37.648  0 89  ASN A C   1 
ATOM   520  O O   . ASN A 1 89  ? 30.187 14.830 17.263  1.000 38.116  0 89  ASN A O   1 
ATOM   521  C CB  . ASN A 1 89  ? 33.016 13.141 16.255  1.000 37.626  0 89  ASN A CB  1 
ATOM   522  C CG  . ASN A 1 89  ? 33.640 13.745 17.486  1.000 44.700  0 89  ASN A CG  1 
ATOM   523  O OD1 . ASN A 1 89  ? 34.849 14.023 17.454  1.000 44.493  0 89  ASN A OD1 1 
ATOM   524  N ND2 . ASN A 1 89  ? 32.900 13.890 18.580  1.000 44.536  0 89  ASN A ND2 1 
ATOM   525  N N   . VAL A 1 90  ? 30.664 15.211 15.112  1.000 34.943  0 90  VAL A N   1 
ATOM   526  C CA  . VAL A 1 90  ? 29.957 16.487 15.150  1.000 34.194  0 90  VAL A CA  1 
ATOM   527  C C   . VAL A 1 90  ? 28.479 16.254 15.483  1.000 34.844  0 90  VAL A C   1 
ATOM   528  O O   . VAL A 1 90  ? 27.888 16.972 16.276  1.000 35.621  0 90  VAL A O   1 
ATOM   529  C CB  . VAL A 1 90  ? 30.075 17.314 13.853  1.000 33.700  0 90  VAL A CB  1 
ATOM   530  C CG1 . VAL A 1 90  ? 29.194 18.563 13.954  1.000 38.214  0 90  VAL A CG1 1 
ATOM   531  C CG2 . VAL A 1 90  ? 31.529 17.701 13.577  1.000 37.937  0 90  VAL A CG2 1 
ATOM   532  N N   . LYS A 1 91  ? 27.845 15.340 14.768  1.000 38.829  0 91  LYS A N   1 
ATOM   533  C CA  . LYS A 1 91  ? 26.423 15.059 14.952  1.000 42.458  0 91  LYS A CA  1 
ATOM   534  C C   . LYS A 1 91  ? 26.120 14.558 16.370  1.000 40.563  0 91  LYS A C   1 
ATOM   535  O O   . LYS A 1 91  ? 25.172 15.003 17.013  1.000 40.767  0 91  LYS A O   1 
ATOM   536  C CB  . LYS A 1 91  ? 26.035 14.087 13.836  1.000 46.955  0 91  LYS A CB  1 
ATOM   537  C CG  . LYS A 1 91  ? 24.570 13.694 13.805  1.000 59.372  0 91  LYS A CG  1 
ATOM   538  C CD  . LYS A 1 91  ? 24.242 12.673 12.720  1.000 69.078  0 91  LYS A CD  1 
ATOM   539  C CE  . LYS A 1 91  ? 22.778 12.329 12.799  1.000 80.010  0 91  LYS A CE  1 
ATOM   540  N NZ  . LYS A 1 91  ? 22.415 11.252 11.880  1.000 86.741  0 91  LYS A NZ  1 
ATOM   541  N N   . LYS A 1 92  ? 26.953 13.660 16.881  1.000 40.553  0 92  LYS A N   1 
ATOM   542  C CA  . LYS A 1 92  ? 26.793 13.186 18.252  1.000 44.540  0 92  LYS A CA  1 
ATOM   543  C C   . LYS A 1 92  ? 26.942 14.312 19.267  1.000 44.087  0 92  LYS A C   1 
ATOM   544  O O   . LYS A 1 92  ? 26.181 14.395 20.220  1.000 39.978  0 92  LYS A O   1 
ATOM   545  C CB  . LYS A 1 92  ? 27.768 12.047 18.551  1.000 52.844  0 92  LYS A CB  1 
ATOM   546  C CG  . LYS A 1 92  ? 27.231 10.736 18.003  1.000 64.424  0 92  LYS A CG  1 
ATOM   547  C CD  . LYS A 1 92  ? 28.256 9.629  17.793  1.000 78.229  0 92  LYS A CD  1 
ATOM   548  C CE  . LYS A 1 92  ? 27.625 8.461  17.086  1.000 81.030  0 92  LYS A CE  1 
ATOM   549  N NZ  . LYS A 1 92  ? 28.623 7.799  16.242  1.000 93.167  0 92  LYS A NZ  1 
ATOM   550  N N   . THR A 1 93  ? 27.962 15.145 19.092  1.000 38.183  0 93  THR A N   1 
ATOM   551  C CA  . THR A 1 93  ? 28.150 16.274 19.973  1.000 39.934  0 93  THR A CA  1 
ATOM   552  C C   . THR A 1 93  ? 26.925 17.179 19.893  1.000 36.969  0 93  THR A C   1 
ATOM   553  O O   . THR A 1 93  ? 26.465 17.645 20.938  1.000 39.339  0 93  THR A O   1 
ATOM   554  C CB  . THR A 1 93  ? 29.448 17.024 19.689  1.000 40.818  0 93  THR A CB  1 
ATOM   555  O OG1 . THR A 1 93  ? 30.498 16.103 19.916  1.000 40.235  0 93  THR A OG1 1 
ATOM   556  C CG2 . THR A 1 93  ? 29.666 18.238 20.578  1.000 39.855  0 93  THR A CG2 1 
ATOM   557  N N   . ALA A 1 94  ? 26.411 17.476 18.690  1.000 38.931  0 94  ALA A N   1 
ATOM   558  C CA  . ALA A 1 94  ? 25.239 18.336 18.590  1.000 40.343  0 94  ALA A CA  1 
ATOM   559  C C   . ALA A 1 94  ? 24.036 17.716 19.306  1.000 38.815  0 94  ALA A C   1 
ATOM   560  O O   . ALA A 1 94  ? 23.255 18.455 19.894  1.000 32.445  0 94  ALA A O   1 
ATOM   561  C CB  . ALA A 1 94  ? 24.886 18.671 17.154  1.000 36.673  0 94  ALA A CB  1 
ATOM   562  N N   . GLN A 1 95  ? 23.849 16.386 19.227  1.000 39.858  0 95  GLN A N   1 
ATOM   563  C CA  A GLN A 1 95  ? 22.759 15.717 19.939  0.500 38.001  0 95  GLN A CA  1 
ATOM   564  C CA  B GLN A 1 95  ? 22.773 15.703 19.934  0.500 38.187  0 95  GLN A CA  1 
ATOM   565  C C   . GLN A 1 95  ? 22.936 15.887 21.443  1.000 39.129  0 95  GLN A C   1 
ATOM   566  O O   . GLN A 1 95  ? 21.957 16.121 22.156  1.000 39.015  0 95  GLN A O   1 
ATOM   567  C CB  A GLN A 1 95  ? 22.610 14.218 19.647  0.500 45.033  0 95  GLN A CB  1 
ATOM   568  C CB  B GLN A 1 95  ? 22.747 14.271 19.382  0.500 44.873  0 95  GLN A CB  1 
ATOM   569  C CG  A GLN A 1 95  ? 21.411 13.552 20.332  0.500 45.319  0 95  GLN A CG  1 
ATOM   570  C CG  B GLN A 1 95  ? 22.194 14.215 17.958  0.500 47.398  0 95  GLN A CG  1 
ATOM   571  C CD  A GLN A 1 95  ? 20.093 14.269 20.112  0.500 48.045  0 95  GLN A CD  1 
ATOM   572  C CD  B GLN A 1 95  ? 22.367 12.894 17.239  0.500 53.375  0 95  GLN A CD  1 
ATOM   573  O OE1 A GLN A 1 95  ? 19.589 14.384 18.988  0.500 51.170  0 95  GLN A OE1 1 
ATOM   574  O OE1 B GLN A 1 95  ? 22.956 11.929 17.746  0.500 55.120  0 95  GLN A OE1 1 
ATOM   575  N NE2 A GLN A 1 95  ? 19.523 14.784 21.191  0.500 46.344  0 95  GLN A NE2 1 
ATOM   576  N NE2 B GLN A 1 95  ? 21.840 12.850 16.021  0.500 47.659  0 95  GLN A NE2 1 
ATOM   577  N N   . TRP A 1 96  ? 24.176 15.778 21.935  1.000 39.025  0 96  TRP A N   1 
ATOM   578  C CA  . TRP A 1 96  ? 24.464 15.948 23.359  1.000 39.311  0 96  TRP A CA  1 
ATOM   579  C C   . TRP A 1 96  ? 24.133 17.378 23.814  1.000 44.922  0 96  TRP A C   1 
ATOM   580  O O   . TRP A 1 96  ? 23.472 17.606 24.843  1.000 37.715  0 96  TRP A O   1 
ATOM   581  C CB  . TRP A 1 96  ? 25.944 15.583 23.632  1.000 44.110  0 96  TRP A CB  1 
ATOM   582  C CG  . TRP A 1 96  ? 26.303 15.642 25.097  1.000 45.921  0 96  TRP A CG  1 
ATOM   583  C CD1 . TRP A 1 96  ? 26.212 14.599 25.977  1.000 54.170  0 96  TRP A CD1 1 
ATOM   584  C CD2 . TRP A 1 96  ? 26.623 16.805 25.887  1.000 43.430  0 96  TRP A CD2 1 
ATOM   585  N NE1 . TRP A 1 96  ? 26.495 15.018 27.245  1.000 54.143  0 96  TRP A NE1 1 
ATOM   586  C CE2 . TRP A 1 96  ? 26.735 16.365 27.229  1.000 52.677  0 96  TRP A CE2 1 
ATOM   587  C CE3 . TRP A 1 96  ? 26.838 18.157 25.608  1.000 42.582  0 96  TRP A CE3 1 
ATOM   588  C CZ2 . TRP A 1 96  ? 27.040 17.226 28.274  1.000 53.250  0 96  TRP A CZ2 1 
ATOM   589  C CZ3 . TRP A 1 96  ? 27.109 19.017 26.649  1.000 50.302  0 96  TRP A CZ3 1 
ATOM   590  C CH2 . TRP A 1 96  ? 27.206 18.556 27.966  1.000 57.458  0 96  TRP A CH2 1 
ATOM   591  N N   . VAL A 1 97  ? 24.533 18.382 23.007  1.000 37.015  0 97  VAL A N   1 
ATOM   592  C CA  . VAL A 1 97  ? 24.215 19.759 23.374  1.000 33.640  0 97  VAL A CA  1 
ATOM   593  C C   . VAL A 1 97  ? 22.710 19.947 23.404  1.000 32.855  0 97  VAL A C   1 
ATOM   594  O O   . VAL A 1 97  ? 22.163 20.596 24.305  1.000 36.117  0 97  VAL A O   1 
ATOM   595  C CB  . VAL A 1 97  ? 24.904 20.719 22.390  1.000 33.325  0 97  VAL A CB  1 
ATOM   596  C CG1 . VAL A 1 97  ? 24.513 22.176 22.640  1.000 35.512  0 97  VAL A CG1 1 
ATOM   597  C CG2 . VAL A 1 97  ? 26.404 20.546 22.485  1.000 39.371  0 97  VAL A CG2 1 
ATOM   598  N N   . LYS A 1 98  ? 22.039 19.423 22.387  1.000 34.101  0 98  LYS A N   1 
ATOM   599  C CA  . LYS A 1 98  ? 20.602 19.610 22.278  1.000 35.182  0 98  LYS A CA  1 
ATOM   600  C C   . LYS A 1 98  ? 19.853 19.119 23.526  1.000 36.166  0 98  LYS A C   1 
ATOM   601  O O   . LYS A 1 98  ? 19.008 19.837 24.061  1.000 37.906  0 98  LYS A O   1 
ATOM   602  C CB  . LYS A 1 98  ? 20.090 18.887 21.037  1.000 35.208  0 98  LYS A CB  1 
ATOM   603  C CG  . LYS A 1 98  ? 18.567 18.966 20.925  1.000 42.975  0 98  LYS A CG  1 
ATOM   604  C CD  . LYS A 1 98  ? 18.038 18.139 19.763  1.000 48.085  0 98  LYS A CD  1 
ATOM   605  C CE  . LYS A 1 98  ? 16.541 18.211 19.734  1.000 58.553  0 98  LYS A CE  1 
ATOM   606  N NZ  . LYS A 1 98  ? 16.077 17.746 18.428  1.000 67.104  0 98  LYS A NZ  1 
ATOM   607  N N   . SER A 1 99  ? 20.169 17.912 24.009  1.000 41.979  0 99  SER A N   1 
ATOM   608  C CA  A SER A 1 99  ? 19.507 17.360 25.186  0.500 40.527  0 99  SER A CA  1 
ATOM   609  C CA  B SER A 1 99  ? 19.483 17.374 25.176  0.500 43.022  0 99  SER A CA  1 
ATOM   610  C C   . SER A 1 99  ? 19.855 18.158 26.434  1.000 47.277  0 99  SER A C   1 
ATOM   611  O O   . SER A 1 99  ? 19.009 18.315 27.318  1.000 46.823  0 99  SER A O   1 
ATOM   612  C CB  A SER A 1 99  ? 19.859 15.917 25.396  0.500 40.302  0 99  SER A CB  1 
ATOM   613  C CB  B SER A 1 99  ? 19.738 15.895 25.349  0.500 45.545  0 99  SER A CB  1 
ATOM   614  O OG  A SER A 1 99  ? 19.658 15.193 24.198  0.500 37.840  0 99  SER A OG  1 
ATOM   615  O OG  B SER A 1 99  ? 21.120 15.631 25.535  0.500 50.731  0 99  SER A OG  1 
ATOM   616  N N   . HIS A 1 100 ? 21.100 18.664 26.510  1.000 41.434  0 100 HIS A N   1 
ATOM   617  C CA  A HIS A 1 100 ? 21.630 19.335 27.695  0.500 42.940  0 100 HIS A CA  1 
ATOM   618  C CA  B HIS A 1 100 ? 21.563 19.292 27.740  0.500 44.187  0 100 HIS A CA  1 
ATOM   619  C C   . HIS A 1 100 ? 21.026 20.732 27.861  1.000 47.372  0 100 HIS A C   1 
ATOM   620  O O   . HIS A 1 100 ? 20.669 21.145 28.976  1.000 41.121  0 100 HIS A O   1 
ATOM   621  C CB  A HIS A 1 100 ? 23.159 19.466 27.607  0.500 43.039  0 100 HIS A CB  1 
ATOM   622  C CB  B HIS A 1 100 ? 23.046 18.939 27.963  0.500 47.344  0 100 HIS A CB  1 
ATOM   623  C CG  A HIS A 1 100 ? 23.859 19.969 28.841  0.500 48.514  0 100 HIS A CG  1 
ATOM   624  C CG  B HIS A 1 100 ? 23.244 17.512 28.424  0.500 47.638  0 100 HIS A CG  1 
ATOM   625  N ND1 A HIS A 1 100 ? 23.646 19.515 30.129  0.500 52.894  0 100 HIS A ND1 1 
ATOM   626  N ND1 B HIS A 1 100 ? 23.236 16.422 27.571  0.500 47.775  0 100 HIS A ND1 1 
ATOM   627  C CD2 A HIS A 1 100 ? 24.841 20.877 28.935  0.500 50.987  0 100 HIS A CD2 1 
ATOM   628  C CD2 B HIS A 1 100 ? 23.399 17.005 29.663  0.500 44.364  0 100 HIS A CD2 1 
ATOM   629  C CE1 A HIS A 1 100 ? 24.446 20.171 30.962  0.500 49.386  0 100 HIS A CE1 1 
ATOM   630  C CE1 B HIS A 1 100 ? 23.392 15.310 28.280  0.500 50.954  0 100 HIS A CE1 1 
ATOM   631  N NE2 A HIS A 1 100 ? 25.198 20.987 30.256  0.500 47.940  0 100 HIS A NE2 1 
ATOM   632  N NE2 B HIS A 1 100 ? 23.489 15.640 29.550  0.500 44.733  0 100 HIS A NE2 1 
ATOM   633  N N   . VAL A 1 101 ? 20.909 21.487 26.739  1.000 36.997  0 101 VAL A N   1 
ATOM   634  C CA  . VAL A 1 101 ? 20.479 22.872 26.836  1.000 37.303  0 101 VAL A CA  1 
ATOM   635  C C   . VAL A 1 101 ? 18.947 22.971 26.813  1.000 36.959  0 101 VAL A C   1 
ATOM   636  O O   . VAL A 1 101 ? 18.389 23.964 27.272  1.000 38.514  0 101 VAL A O   1 
ATOM   637  C CB  . VAL A 1 101 ? 21.091 23.769 25.748  1.000 38.002  0 101 VAL A CB  1 
ATOM   638  C CG1 . VAL A 1 101 ? 22.614 23.709 25.747  1.000 38.478  0 101 VAL A CG1 1 
ATOM   639  C CG2 . VAL A 1 101 ? 20.555 23.432 24.374  1.000 35.946  0 101 VAL A CG2 1 
ATOM   640  N N   . GLY A 1 102 ? 18.294 21.950 26.283  1.000 39.317  0 102 GLY A N   1 
ATOM   641  C CA  . GLY A 1 102 ? 16.838 21.893 26.250  1.000 42.423  0 102 GLY A CA  1 
ATOM   642  C C   . GLY A 1 102 ? 16.262 23.118 25.568  1.000 45.965  0 102 GLY A C   1 
ATOM   643  O O   . GLY A 1 102 ? 16.769 23.577 24.542  1.000 41.961  0 102 GLY A O   1 
ATOM   644  N N   . GLU A 1 103 ? 15.223 23.662 26.190  1.000 37.900  0 103 GLU A N   1 
ATOM   645  C CA  . GLU A 1 103 ? 14.412 24.690 25.566  1.000 41.190  0 103 GLU A CA  1 
ATOM   646  C C   . GLU A 1 103 ? 15.102 26.063 25.703  1.000 45.108  0 103 GLU A C   1 
ATOM   647  O O   . GLU A 1 103 ? 14.669 27.022 25.079  1.000 38.666  0 103 GLU A O   1 
ATOM   648  C CB  . GLU A 1 103 ? 12.999 24.668 26.185  1.000 47.105  0 103 GLU A CB  1 
ATOM   649  C CG  . GLU A 1 103 ? 12.069 23.601 25.609  1.000 53.108  0 103 GLU A CG  1 
ATOM   650  C CD  . GLU A 1 103 ? 10.734 23.483 26.344  1.000 52.080  0 103 GLU A CD  1 
ATOM   651  O OE1 . GLU A 1 103 ? 10.789 23.106 27.560  1.000 46.490  0 103 GLU A OE1 1 
ATOM   652  O OE2 . GLU A 1 103 ? 9.665  23.753 25.695  1.000 45.788  0 103 GLU A OE2 1 
ATOM   653  N N   . LYS A 1 104 ? 16.215 26.169 26.446  1.000 37.994  0 104 LYS A N   1 
ATOM   654  C CA  . LYS A 1 104 ? 17.024 27.388 26.381  1.000 38.341  0 104 LYS A CA  1 
ATOM   655  C C   . LYS A 1 104 ? 17.688 27.610 25.005  1.000 35.990  0 104 LYS A C   1 
ATOM   656  O O   . LYS A 1 104 ? 17.999 28.749 24.641  1.000 40.384  0 104 LYS A O   1 
ATOM   657  C CB  . LYS A 1 104 ? 18.131 27.301 27.436  1.000 40.047  0 104 LYS A CB  1 
ATOM   658  C CG  . LYS A 1 104 ? 17.707 27.341 28.915  1.000 43.701  0 104 LYS A CG  1 
ATOM   659  C CD  . LYS A 1 104 ? 18.914 27.064 29.805  1.000 46.875  0 104 LYS A CD  1 
ATOM   660  C CE  . LYS A 1 104 ? 18.673 27.433 31.219  1.000 50.877  0 104 LYS A CE  1 
ATOM   661  N NZ  . LYS A 1 104 ? 17.758 26.418 31.737  1.000 53.466  0 104 LYS A NZ  1 
ATOM   662  N N   . GLY A 1 105 ? 17.947 26.515 24.281  1.000 34.725  0 105 GLY A N   1 
ATOM   663  C CA  . GLY A 1 105 ? 18.754 26.534 23.075  1.000 37.981  0 105 GLY A CA  1 
ATOM   664  C C   . GLY A 1 105 ? 20.195 26.903 23.419  1.000 36.519  0 105 GLY A C   1 
ATOM   665  O O   . GLY A 1 105 ? 20.599 26.847 24.586  1.000 36.496  0 105 GLY A O   1 
ATOM   666  N N   . LEU A 1 106 ? 20.948 27.311 22.391  1.000 34.520  0 106 LEU A N   1 
ATOM   667  C CA  . LEU A 1 106 ? 22.365 27.624 22.523  1.000 31.080  0 106 LEU A CA  1 
ATOM   668  C C   . LEU A 1 106 ? 22.589 29.097 22.195  1.000 32.692  0 106 LEU A C   1 
ATOM   669  O O   . LEU A 1 106 ? 22.461 29.510 21.041  1.000 34.575  0 106 LEU A O   1 
ATOM   670  C CB  . LEU A 1 106 ? 23.099 26.716 21.543  1.000 31.128  0 106 LEU A CB  1 
ATOM   671  C CG  . LEU A 1 106 ? 24.623 26.865 21.514  1.000 31.295  0 106 LEU A CG  1 
ATOM   672  C CD1 . LEU A 1 106 ? 25.264 26.479 22.824  1.000 32.111  0 106 LEU A CD1 1 
ATOM   673  C CD2 . LEU A 1 106 ? 25.248 26.068 20.388  1.000 31.505  0 106 LEU A CD2 1 
ATOM   674  N N   . TRP A 1 107 ? 22.908 29.879 23.220  1.000 30.341  0 107 TRP A N   1 
ATOM   675  C CA  . TRP A 1 107 ? 23.057 31.307 23.055  1.000 30.424  0 107 TRP A CA  1 
ATOM   676  C C   . TRP A 1 107 ? 24.220 31.641 22.116  1.000 33.746  0 107 TRP A C   1 
ATOM   677  O O   . TRP A 1 107 ? 24.113 32.559 21.302  1.000 34.382  0 107 TRP A O   1 
ATOM   678  C CB  . TRP A 1 107 ? 23.273 31.965 24.404  1.000 31.308  0 107 TRP A CB  1 
ATOM   679  C CG  . TRP A 1 107 ? 23.642 33.411 24.281  1.000 31.808  0 107 TRP A CG  1 
ATOM   680  C CD1 . TRP A 1 107 ? 24.833 34.010 24.517  1.000 32.817  0 107 TRP A CD1 1 
ATOM   681  C CD2 . TRP A 1 107 ? 22.745 34.443 23.838  1.000 32.794  0 107 TRP A CD2 1 
ATOM   682  N NE1 . TRP A 1 107 ? 24.745 35.358 24.258  1.000 32.412  0 107 TRP A NE1 1 
ATOM   683  C CE2 . TRP A 1 107 ? 23.476 35.642 23.850  1.000 32.116  0 107 TRP A CE2 1 
ATOM   684  C CE3 . TRP A 1 107 ? 21.398 34.449 23.451  1.000 35.493  0 107 TRP A CE3 1 
ATOM   685  C CZ2 . TRP A 1 107 ? 22.900 36.854 23.468  1.000 37.186  0 107 TRP A CZ2 1 
ATOM   686  C CZ3 . TRP A 1 107 ? 20.840 35.641 23.049  1.000 37.630  0 107 TRP A CZ3 1 
ATOM   687  C CH2 . TRP A 1 107 ? 21.583 36.816 23.071  1.000 37.959  0 107 TRP A CH2 1 
ATOM   688  N N   . GLY A 1 108 ? 25.367 31.002 22.328  1.000 33.059  0 108 GLY A N   1 
ATOM   689  C CA  . GLY A 1 108 ? 26.560 31.300 21.537  1.000 32.286  0 108 GLY A CA  1 
ATOM   690  C C   . GLY A 1 108 ? 27.204 30.071 20.917  1.000 32.122  0 108 GLY A C   1 
ATOM   691  O O   . GLY A 1 108 ? 27.403 29.034 21.572  1.000 29.930  0 108 GLY A O   1 
ATOM   692  N N   . LEU A 1 109 ? 27.651 30.246 19.666  1.000 31.637  0 109 LEU A N   1 
ATOM   693  C CA  . LEU A 1 109 ? 28.552 29.325 18.995  1.000 32.717  0 109 LEU A CA  1 
ATOM   694  C C   . LEU A 1 109 ? 29.776 30.109 18.533  1.000 30.958  0 109 LEU A C   1 
ATOM   695  O O   . LEU A 1 109 ? 29.612 31.062 17.781  1.000 32.791  0 109 LEU A O   1 
ATOM   696  C CB  . LEU A 1 109 ? 27.861 28.674 17.799  1.000 34.558  0 109 LEU A CB  1 
ATOM   697  C CG  . LEU A 1 109 ? 28.782 27.824 16.911  1.000 34.906  0 109 LEU A CG  1 
ATOM   698  C CD1 . LEU A 1 109 ? 29.357 26.636 17.688  1.000 37.288  0 109 LEU A CD1 1 
ATOM   699  C CD2 . LEU A 1 109 ? 27.995 27.375 15.691  1.000 36.688  0 109 LEU A CD2 1 
ATOM   700  N N   . ILE A 1 110 ? 30.956 29.734 19.035  1.000 31.015  0 110 ILE A N   1 
ATOM   701  C CA  . ILE A 1 110 ? 32.234 30.269 18.611  1.000 32.207  0 110 ILE A CA  1 
ATOM   702  C C   . ILE A 1 110 ? 32.982 29.223 17.792  1.000 35.895  0 110 ILE A C   1 
ATOM   703  O O   . ILE A 1 110 ? 33.510 28.243 18.346  1.000 32.270  0 110 ILE A O   1 
ATOM   704  C CB  . ILE A 1 110 ? 33.062 30.770 19.814  1.000 35.224  0 110 ILE A CB  1 
ATOM   705  C CG1 . ILE A 1 110 ? 32.243 31.758 20.671  1.000 34.153  0 110 ILE A CG1 1 
ATOM   706  C CG2 . ILE A 1 110 ? 34.394 31.371 19.323  1.000 31.324  0 110 ILE A CG2 1 
ATOM   707  C CD1 . ILE A 1 110 ? 32.995 32.311 21.869  1.000 33.991  0 110 ILE A CD1 1 
ATOM   708  N N   . ASN A 1 111 ? 33.060 29.476 16.474  1.000 33.346  0 111 ASN A N   1 
ATOM   709  C CA  . ASN A 1 111 ? 33.807 28.615 15.568  1.000 30.246  0 111 ASN A CA  1 
ATOM   710  C C   . ASN A 1 111 ? 35.257 29.073 15.516  1.000 34.574  0 111 ASN A C   1 
ATOM   711  O O   . ASN A 1 111 ? 35.636 29.956 14.719  1.000 33.263  0 111 ASN A O   1 
ATOM   712  C CB  . ASN A 1 111 ? 33.203 28.601 14.176  1.000 30.735  0 111 ASN A CB  1 
ATOM   713  C CG  . ASN A 1 111 ? 31.918 27.822 14.099  1.000 35.821  0 111 ASN A CG  1 
ATOM   714  O OD1 . ASN A 1 111 ? 31.898 26.617 14.376  1.000 35.608  0 111 ASN A OD1 1 
ATOM   715  N ND2 . ASN A 1 111 ? 30.869 28.461 13.596  1.000 31.776  0 111 ASN A ND2 1 
ATOM   716  N N   . ASN A 1 112 ? 36.060 28.450 16.378  1.000 32.207  0 112 ASN A N   1 
ATOM   717  C CA  . ASN A 1 112 ? 37.435 28.861 16.627  1.000 30.276  0 112 ASN A CA  1 
ATOM   718  C C   . ASN A 1 112 ? 38.448 27.849 16.114  1.000 30.783  0 112 ASN A C   1 
ATOM   719  O O   . ASN A 1 112 ? 39.558 28.210 15.736  1.000 32.398  0 112 ASN A O   1 
ATOM   720  C CB  . ASN A 1 112 ? 37.624 29.183 18.107  1.000 34.543  0 112 ASN A CB  1 
ATOM   721  C CG  . ASN A 1 112 ? 39.071 29.328 18.520  1.000 34.363  0 112 ASN A CG  1 
ATOM   722  O OD1 . ASN A 1 112 ? 39.683 30.389 18.343  1.000 31.245  0 112 ASN A OD1 1 
ATOM   723  N ND2 . ASN A 1 112 ? 39.626 28.268 19.079  1.000 34.329  0 112 ASN A ND2 1 
ATOM   724  N N   . ALA A 1 113 ? 38.120 26.564 16.132  1.000 33.341  0 113 ALA A N   1 
ATOM   725  C CA  . ALA A 1 113 ? 39.078 25.562 15.715  1.000 30.500  0 113 ALA A CA  1 
ATOM   726  C C   . ALA A 1 113 ? 39.636 25.870 14.331  1.000 31.789  0 113 ALA A C   1 
ATOM   727  O O   . ALA A 1 113 ? 38.878 26.162 13.386  1.000 32.121  0 113 ALA A O   1 
ATOM   728  C CB  . ALA A 1 113 ? 38.413 24.214 15.671  1.000 31.643  0 113 ALA A CB  1 
ATOM   729  N N   . GLY A 1 114 ? 40.951 25.730 14.201  1.000 30.975  0 114 GLY A N   1 
ATOM   730  C CA  . GLY A 1 114 ? 41.584 25.954 12.923  1.000 31.567  0 114 GLY A CA  1 
ATOM   731  C C   . GLY A 1 114 ? 43.040 25.544 12.968  1.000 31.286  0 114 GLY A C   1 
ATOM   732  O O   . GLY A 1 114 ? 43.611 25.383 14.061  1.000 32.262  0 114 GLY A O   1 
ATOM   733  N N   . VAL A 1 115 ? 43.570 25.293 11.756  1.000 31.057  0 115 VAL A N   1 
ATOM   734  C CA  . VAL A 1 115 ? 44.956 24.905 11.525  1.000 30.947  0 115 VAL A CA  1 
ATOM   735  C C   . VAL A 1 115 ? 45.546 25.690 10.363  1.000 32.670  0 115 VAL A C   1 
ATOM   736  O O   . VAL A 1 115 ? 44.841 26.117 9.474   1.000 33.240  0 115 VAL A O   1 
ATOM   737  C CB  . VAL A 1 115 ? 45.130 23.404 11.205  1.000 34.839  0 115 VAL A CB  1 
ATOM   738  C CG1 . VAL A 1 115 ? 44.621 22.545 12.351  1.000 37.453  0 115 VAL A CG1 1 
ATOM   739  C CG2 . VAL A 1 115 ? 44.496 23.022 9.874   1.000 33.024  0 115 VAL A CG2 1 
ATOM   740  N N   . LEU A 1 116 ? 46.879 25.809 10.371  1.000 31.708  0 116 LEU A N   1 
ATOM   741  C CA  . LEU A 1 116 ? 47.616 26.566 9.357   1.000 32.566  0 116 LEU A CA  1 
ATOM   742  C C   . LEU A 1 116 ? 47.813 25.761 8.072   1.000 34.112  0 116 LEU A C   1 
ATOM   743  O O   . LEU A 1 116 ? 47.735 26.315 6.990   1.000 32.193  0 116 LEU A O   1 
ATOM   744  C CB  . LEU A 1 116 ? 48.975 26.976 9.921   1.000 35.234  0 116 LEU A CB  1 
ATOM   745  C CG  . LEU A 1 116 ? 49.750 27.996 9.088   1.000 38.939  0 116 LEU A CG  1 
ATOM   746  C CD1 . LEU A 1 116 ? 49.041 29.329 9.103   1.000 41.143  0 116 LEU A CD1 1 
ATOM   747  C CD2 . LEU A 1 116 ? 51.189 28.067 9.655   1.000 45.758  0 116 LEU A CD2 1 
ATOM   748  N N   . GLY A 1 117 ? 48.026 24.442 8.201   1.000 33.751  0 117 GLY A N   1 
ATOM   749  C CA  . GLY A 1 117 ? 48.506 23.599 7.116   1.000 34.687  0 117 GLY A CA  1 
ATOM   750  C C   . GLY A 1 117 ? 49.893 24.037 6.641   1.000 37.307  0 117 GLY A C   1 
ATOM   751  O O   . GLY A 1 117 ? 50.585 24.816 7.290   1.000 39.326  0 117 GLY A O   1 
ATOM   752  N N   . VAL A 1 118 ? 50.281 23.556 5.466   1.000 37.610  0 118 VAL A N   1 
ATOM   753  C CA  . VAL A 1 118 ? 51.581 23.868 4.870   1.000 37.079  0 118 VAL A CA  1 
ATOM   754  C C   . VAL A 1 118 ? 51.504 25.246 4.215   1.000 37.211  0 118 VAL A C   1 
ATOM   755  O O   . VAL A 1 118 ? 50.582 25.508 3.426   1.000 35.823  0 118 VAL A O   1 
ATOM   756  C CB  . VAL A 1 118 ? 51.953 22.823 3.799   1.000 45.186  0 118 VAL A CB  1 
ATOM   757  C CG1 . VAL A 1 118 ? 53.335 23.127 3.213   1.000 50.189  0 118 VAL A CG1 1 
ATOM   758  C CG2 . VAL A 1 118 ? 51.837 21.400 4.329   1.000 53.603  0 118 VAL A CG2 1 
ATOM   759  N N   . LEU A 1 119 ? 52.474 26.089 4.552   1.000 35.186  0 119 LEU A N   1 
ATOM   760  C CA  . LEU A 1 119 ? 52.704 27.381 3.926   1.000 41.202  0 119 LEU A CA  1 
ATOM   761  C C   . LEU A 1 119 ? 53.987 27.264 3.106   1.000 43.184  0 119 LEU A C   1 
ATOM   762  O O   . LEU A 1 119 ? 55.056 27.044 3.672   1.000 42.603  0 119 LEU A O   1 
ATOM   763  C CB  . LEU A 1 119 ? 52.902 28.512 4.925   1.000 45.350  0 119 LEU A CB  1 
ATOM   764  C CG  . LEU A 1 119 ? 51.720 28.926 5.796   1.000 50.798  0 119 LEU A CG  1 
ATOM   765  C CD1 . LEU A 1 119 ? 52.237 30.068 6.680   1.000 53.405  0 119 LEU A CD1 1 
ATOM   766  C CD2 . LEU A 1 119 ? 50.560 29.391 4.944   1.000 53.003  0 119 LEU A CD2 1 
ATOM   767  N N   . ALA A 1 120 ? 53.888 27.469 1.787   1.000 38.303  0 120 ALA A N   1 
ATOM   768  C CA  . ALA A 1 120 ? 55.070 27.450 0.932   1.000 37.198  0 120 ALA A CA  1 
ATOM   769  C C   . ALA A 1 120 ? 54.706 28.098 -0.396  1.000 36.488  0 120 ALA A C   1 
ATOM   770  O O   . ALA A 1 120 ? 53.518 28.280 -0.678  1.000 34.749  0 120 ALA A O   1 
ATOM   771  C CB  . ALA A 1 120 ? 55.527 26.015 0.743   1.000 39.636  0 120 ALA A CB  1 
ATOM   772  N N   . PRO A 1 121 ? 55.689 28.469 -1.247  1.000 36.181  0 121 PRO A N   1 
ATOM   773  C CA  . PRO A 1 121 ? 55.390 28.999 -2.580  1.000 36.324  0 121 PRO A CA  1 
ATOM   774  C C   . PRO A 1 121 ? 54.472 28.041 -3.324  1.000 31.763  0 121 PRO A C   1 
ATOM   775  O O   . PRO A 1 121 ? 54.571 26.815 -3.181  1.000 33.739  0 121 PRO A O   1 
ATOM   776  C CB  . PRO A 1 121 ? 56.772 29.118 -3.217  1.000 37.355  0 121 PRO A CB  1 
ATOM   777  C CG  . PRO A 1 121 ? 57.679 29.374 -2.022  1.000 38.063  0 121 PRO A CG  1 
ATOM   778  C CD  . PRO A 1 121 ? 57.138 28.380 -0.997  1.000 37.297  0 121 PRO A CD  1 
ATOM   779  N N   . THR A 1 122 ? 53.523 28.629 -4.046  1.000 33.784  0 122 THR A N   1 
ATOM   780  C CA  . THR A 1 122 ? 52.466 27.903 -4.727  1.000 31.727  0 122 THR A CA  1 
ATOM   781  C C   . THR A 1 122 ? 53.067 26.822 -5.632  1.000 32.571  0 122 THR A C   1 
ATOM   782  O O   . THR A 1 122 ? 52.533 25.715 -5.670  1.000 32.129  0 122 THR A O   1 
ATOM   783  C CB  . THR A 1 122 ? 51.583 28.884 -5.499  1.000 35.322  0 122 THR A CB  1 
ATOM   784  O OG1 . THR A 1 122 ? 51.052 29.831 -4.567  1.000 34.277  0 122 THR A OG1 1 
ATOM   785  C CG2 . THR A 1 122 ? 50.484 28.160 -6.242  1.000 35.567  0 122 THR A CG2 1 
ATOM   786  N N   . ASP A 1 123 ? 54.191 27.119 -6.311  1.000 35.174  0 123 ASP A N   1 
ATOM   787  C CA  . ASP A 1 123 ? 54.765 26.184 -7.273  1.000 33.539  0 123 ASP A CA  1 
ATOM   788  C C   . ASP A 1 123 ? 55.481 25.011 -6.614  1.000 37.682  0 123 ASP A C   1 
ATOM   789  O O   . ASP A 1 123 ? 55.908 24.101 -7.321  1.000 38.930  0 123 ASP A O   1 
ATOM   790  C CB  . ASP A 1 123 ? 55.625 26.884 -8.305  1.000 35.887  0 123 ASP A CB  1 
ATOM   791  C CG  . ASP A 1 123 ? 56.727 27.805 -7.803  1.000 39.383  0 123 ASP A CG  1 
ATOM   792  O OD1 . ASP A 1 123 ? 56.760 28.162 -6.587  1.000 37.195  0 123 ASP A OD1 1 
ATOM   793  O OD2 . ASP A 1 123 ? 57.539 28.179 -8.653  1.000 37.676  0 123 ASP A OD2 1 
ATOM   794  N N   . TRP A 1 124 ? 55.555 24.978 -5.273  1.000 34.129  0 124 TRP A N   1 
ATOM   795  C CA  . TRP A 1 124 ? 56.087 23.819 -4.580  1.000 34.417  0 124 TRP A CA  1 
ATOM   796  C C   . TRP A 1 124 ? 55.008 22.799 -4.227  1.000 39.859  0 124 TRP A C   1 
ATOM   797  O O   . TRP A 1 124 ? 55.364 21.736 -3.720  1.000 39.725  0 124 TRP A O   1 
ATOM   798  C CB  . TRP A 1 124 ? 56.753 24.214 -3.256  1.000 32.670  0 124 TRP A CB  1 
ATOM   799  C CG  . TRP A 1 124 ? 57.951 25.105 -3.353  1.000 34.879  0 124 TRP A CG  1 
ATOM   800  C CD1 . TRP A 1 124 ? 58.374 25.897 -4.376  1.000 38.136  0 124 TRP A CD1 1 
ATOM   801  C CD2 . TRP A 1 124 ? 58.899 25.302 -2.288  1.000 37.146  0 124 TRP A CD2 1 
ATOM   802  N NE1 . TRP A 1 124 ? 59.492 26.590 -4.016  1.000 36.401  0 124 TRP A NE1 1 
ATOM   803  C CE2 . TRP A 1 124 ? 59.835 26.253 -2.736  1.000 36.074  0 124 TRP A CE2 1 
ATOM   804  C CE3 . TRP A 1 124 ? 59.031 24.767 -1.003  1.000 40.920  0 124 TRP A CE3 1 
ATOM   805  C CZ2 . TRP A 1 124 ? 60.905 26.685 -1.946  1.000 40.451  0 124 TRP A CZ2 1 
ATOM   806  C CZ3 . TRP A 1 124 ? 60.070 25.218 -0.211  1.000 46.161  0 124 TRP A CZ3 1 
ATOM   807  C CH2 . TRP A 1 124 ? 60.986 26.171 -0.672  1.000 43.908  0 124 TRP A CH2 1 
ATOM   808  N N   . LEU A 1 125 ? 53.716 23.152 -4.367  1.000 39.127  0 125 LEU A N   1 
ATOM   809  C CA  . LEU A 1 125 ? 52.624 22.429 -3.711  1.000 36.716  0 125 LEU A CA  1 
ATOM   810  C C   . LEU A 1 125 ? 51.898 21.489 -4.668  1.000 38.031  0 125 LEU A C   1 
ATOM   811  O O   . LEU A 1 125 ? 51.894 21.711 -5.875  1.000 36.955  0 125 LEU A O   1 
ATOM   812  C CB  . LEU A 1 125 ? 51.629 23.401 -3.079  1.000 37.520  0 125 LEU A CB  1 
ATOM   813  C CG  . LEU A 1 125 ? 52.233 24.323 -2.002  1.000 38.338  0 125 LEU A CG  1 
ATOM   814  C CD1 . LEU A 1 125 ? 51.226 25.229 -1.357  1.000 38.097  0 125 LEU A CD1 1 
ATOM   815  C CD2 . LEU A 1 125 ? 52.927 23.469 -0.939  1.000 40.254  0 125 LEU A CD2 1 
ATOM   816  N N   . THR A 1 126 ? 51.217 20.471 -4.107  1.000 35.391  0 126 THR A N   1 
ATOM   817  C CA  . THR A 1 126 ? 50.212 19.720 -4.848  1.000 37.305  0 126 THR A CA  1 
ATOM   818  C C   . THR A 1 126 ? 48.830 20.092 -4.307  1.000 35.953  0 126 THR A C   1 
ATOM   819  O O   . THR A 1 126 ? 48.727 20.712 -3.251  1.000 36.425  0 126 THR A O   1 
ATOM   820  C CB  . THR A 1 126 ? 50.451 18.213 -4.733  1.000 43.263  0 126 THR A CB  1 
ATOM   821  O OG1 . THR A 1 126 ? 50.086 17.918 -3.389  1.000 45.313  0 126 THR A OG1 1 
ATOM   822  C CG2 . THR A 1 126 ? 51.882 17.837 -5.089  1.000 50.925  0 126 THR A CG2 1 
ATOM   823  N N   . VAL A 1 127 ? 47.771 19.696 -5.026  1.000 35.421  0 127 VAL A N   1 
ATOM   824  C CA  . VAL A 1 127 ? 46.409 20.045 -4.634  1.000 34.664  0 127 VAL A CA  1 
ATOM   825  C C   . VAL A 1 127 ? 46.129 19.416 -3.274  1.000 38.278  0 127 VAL A C   1 
ATOM   826  O O   . VAL A 1 127 ? 45.427 20.001 -2.449  1.000 36.511  0 127 VAL A O   1 
ATOM   827  C CB  . VAL A 1 127 ? 45.344 19.689 -5.699  1.000 35.221  0 127 VAL A CB  1 
ATOM   828  C CG1 . VAL A 1 127 ? 45.198 18.189 -5.928  1.000 41.419  0 127 VAL A CG1 1 
ATOM   829  C CG2 . VAL A 1 127 ? 43.990 20.299 -5.362  1.000 37.099  0 127 VAL A CG2 1 
ATOM   830  N N   . ASP A 1 128 ? 46.729 18.249 -2.984  1.000 38.627  0 128 ASP A N   1 
ATOM   831  C CA  A ASP A 1 128 ? 46.497 17.560 -1.723  0.500 42.246  0 128 ASP A CA  1 
ATOM   832  C CA  B ASP A 1 128 ? 46.455 17.584 -1.715  0.500 41.700  0 128 ASP A CA  1 
ATOM   833  C C   . ASP A 1 128 ? 46.929 18.429 -0.530  1.000 38.766  0 128 ASP A C   1 
ATOM   834  O O   . ASP A 1 128 ? 46.346 18.364 0.550   1.000 39.915  0 128 ASP A O   1 
ATOM   835  C CB  A ASP A 1 128 ? 47.132 16.180 -1.826  0.500 48.408  0 128 ASP A CB  1 
ATOM   836  C CB  B ASP A 1 128 ? 47.053 16.190 -1.600  0.500 47.677  0 128 ASP A CB  1 
ATOM   837  C CG  A ASP A 1 128 ? 46.858 15.486 -3.158  0.500 50.694  0 128 ASP A CG  1 
ATOM   838  C CG  B ASP A 1 128 ? 46.396 15.335 -0.527  0.500 49.768  0 128 ASP A CG  1 
ATOM   839  O OD1 A ASP A 1 128 ? 47.561 15.797 -4.176  0.500 52.197  0 128 ASP A OD1 1 
ATOM   840  O OD1 B ASP A 1 128 ? 45.201 14.992 -0.710  0.500 52.038  0 128 ASP A OD1 1 
ATOM   841  O OD2 A ASP A 1 128 ? 45.886 14.711 -3.195  0.500 54.290  0 128 ASP A OD2 1 
ATOM   842  O OD2 B ASP A 1 128 ? 47.060 15.059 0.499   0.500 54.585  0 128 ASP A OD2 1 
ATOM   843  N N   . ASP A 1 129 ? 47.955 19.262 -0.723  1.000 38.971  0 129 ASP A N   1 
ATOM   844  C CA  . ASP A 1 129 ? 48.471 20.129 0.333   1.000 36.525  0 129 ASP A CA  1 
ATOM   845  C C   . ASP A 1 129 ? 47.465 21.204 0.759   1.000 36.428  0 129 ASP A C   1 
ATOM   846  O O   . ASP A 1 129 ? 47.612 21.788 1.826   1.000 36.618  0 129 ASP A O   1 
ATOM   847  C CB  . ASP A 1 129 ? 49.759 20.820 -0.083  1.000 36.511  0 129 ASP A CB  1 
ATOM   848  C CG  . ASP A 1 129 ? 50.940 19.882 -0.320  1.000 46.020  0 129 ASP A CG  1 
ATOM   849  O OD1 . ASP A 1 129 ? 51.064 18.908 0.441   1.000 46.842  0 129 ASP A OD1 1 
ATOM   850  O OD2 . ASP A 1 129 ? 51.717 20.117 -1.271  1.000 40.552  0 129 ASP A OD2 1 
ATOM   851  N N   . TYR A 1 130 ? 46.464 21.487 -0.068  1.000 31.369  0 130 TYR A N   1 
ATOM   852  C CA  . TYR A 1 130 ? 45.482 22.512 0.235   1.000 32.984  0 130 TYR A CA  1 
ATOM   853  C C   . TYR A 1 130 ? 44.335 21.938 1.057   1.000 32.186  0 130 TYR A C   1 
ATOM   854  O O   . TYR A 1 130 ? 43.602 22.687 1.688   1.000 31.918  0 130 TYR A O   1 
ATOM   855  C CB  . TYR A 1 130 ? 44.898 23.116 -1.053  1.000 30.703  0 130 TYR A CB  1 
ATOM   856  C CG  . TYR A 1 130 ? 45.872 24.004 -1.775  1.000 31.250  0 130 TYR A CG  1 
ATOM   857  C CD1 . TYR A 1 130 ? 46.934 23.454 -2.507  1.000 30.155  0 130 TYR A CD1 1 
ATOM   858  C CD2 . TYR A 1 130 ? 45.736 25.382 -1.768  1.000 32.599  0 130 TYR A CD2 1 
ATOM   859  C CE1 . TYR A 1 130 ? 47.845 24.249 -3.161  1.000 30.816  0 130 TYR A CE1 1 
ATOM   860  C CE2 . TYR A 1 130 ? 46.660 26.190 -2.404  1.000 30.550  0 130 TYR A CE2 1 
ATOM   861  C CZ  . TYR A 1 130 ? 47.710 25.631 -3.105  1.000 32.593  0 130 TYR A CZ  1 
ATOM   862  O OH  . TYR A 1 130 ? 48.611 26.408 -3.768  1.000 32.714  0 130 TYR A OH  1 
ATOM   863  N N   . ARG A 1 131 ? 44.176 20.601 1.089   1.000 32.367  0 131 ARG A N   1 
ATOM   864  C CA  . ARG A 1 131 ? 42.962 19.995 1.631   1.000 33.321  0 131 ARG A CA  1 
ATOM   865  C C   . ARG A 1 131 ? 42.808 20.156 3.138   1.000 33.549  0 131 ARG A C   1 
ATOM   866  O O   . ARG A 1 131 ? 41.692 20.384 3.606   1.000 32.598  0 131 ARG A O   1 
ATOM   867  C CB  . ARG A 1 131 ? 42.877 18.508 1.278   1.000 39.124  0 131 ARG A CB  1 
ATOM   868  C CG  . ARG A 1 131 ? 42.720 18.404 -0.238  1.000 41.331  0 131 ARG A CG  1 
ATOM   869  C CD  . ARG A 1 131 ? 41.745 17.390 -0.708  1.000 43.740  0 131 ARG A CD  1 
ATOM   870  N NE  . ARG A 1 131 ? 41.630 17.349 -2.164  1.000 40.397  0 131 ARG A NE  1 
ATOM   871  C CZ  . ARG A 1 131 ? 40.528 17.524 -2.871  1.000 38.313  0 131 ARG A CZ  1 
ATOM   872  N NH1 . ARG A 1 131 ? 39.430 17.971 -2.289  1.000 36.962  0 131 ARG A NH1 1 
ATOM   873  N NH2 . ARG A 1 131 ? 40.566 17.336 -4.184  1.000 39.151  0 131 ARG A NH2 1 
ATOM   874  N N   . GLU A 1 132 ? 43.898 20.034 3.899   1.000 35.846  0 132 GLU A N   1 
ATOM   875  C CA  . GLU A 1 132 ? 43.808 19.966 5.360   1.000 36.976  0 132 GLU A CA  1 
ATOM   876  C C   . GLU A 1 132 ? 43.283 21.283 5.944   1.000 33.606  0 132 GLU A C   1 
ATOM   877  O O   . GLU A 1 132 ? 42.300 21.293 6.715   1.000 33.124  0 132 GLU A O   1 
ATOM   878  C CB  . GLU A 1 132 ? 45.174 19.625 5.965   1.000 46.330  0 132 GLU A CB  1 
ATOM   879  C CG  . GLU A 1 132 ? 45.210 19.595 7.501   1.000 52.600  0 132 GLU A CG  1 
ATOM   880  C CD  . GLU A 1 132 ? 46.610 19.663 8.150   1.000 66.109  0 132 GLU A CD  1 
ATOM   881  O OE1 . GLU A 1 132 ? 47.672 19.758 7.452   1.000 60.881  0 132 GLU A OE1 1 
ATOM   882  O OE2 . GLU A 1 132 ? 46.644 19.629 9.409   1.000 63.022  0 132 GLU A OE2 1 
ATOM   883  N N   . PRO A 1 133 ? 43.914 22.447 5.663   1.000 32.606  0 133 PRO A N   1 
ATOM   884  C CA  . PRO A 1 133 ? 43.361 23.700 6.188   1.000 30.315  0 133 PRO A CA  1 
ATOM   885  C C   . PRO A 1 133 ? 41.910 23.938 5.768   1.000 31.360  0 133 PRO A C   1 
ATOM   886  O O   . PRO A 1 133 ? 41.080 24.395 6.573   1.000 33.225  0 133 PRO A O   1 
ATOM   887  C CB  . PRO A 1 133 ? 44.325 24.795 5.745   1.000 31.092  0 133 PRO A CB  1 
ATOM   888  C CG  . PRO A 1 133 ? 45.175 24.157 4.692   1.000 30.889  0 133 PRO A CG  1 
ATOM   889  C CD  . PRO A 1 133 ? 45.140 22.635 4.858   1.000 33.205  0 133 PRO A CD  1 
ATOM   890  N N   . ILE A 1 134 ? 41.570 23.624 4.518   1.000 30.292  0 134 ILE A N   1 
ATOM   891  C CA  . ILE A 1 134 ? 40.196 23.794 4.068   1.000 31.021  0 134 ILE A CA  1 
ATOM   892  C C   . ILE A 1 134 ? 39.250 22.867 4.835   1.000 31.540  0 134 ILE A C   1 
ATOM   893  O O   . ILE A 1 134 ? 38.119 23.236 5.187   1.000 31.086  0 134 ILE A O   1 
ATOM   894  C CB  . ILE A 1 134 ? 40.113 23.691 2.535   1.000 33.255  0 134 ILE A CB  1 
ATOM   895  C CG1 . ILE A 1 134 ? 40.880 24.871 1.928   1.000 34.059  0 134 ILE A CG1 1 
ATOM   896  C CG2 . ILE A 1 134 ? 38.658 23.681 2.074   1.000 35.189  0 134 ILE A CG2 1 
ATOM   897  C CD1 . ILE A 1 134 ? 41.294 24.750 0.479   1.000 35.079  0 134 ILE A CD1 1 
ATOM   898  N N   . GLU A 1 135 ? 39.688 21.640 5.123   1.000 31.429  0 135 GLU A N   1 
ATOM   899  C CA  . GLU A 1 135 ? 38.807 20.703 5.802   1.000 32.580  0 135 GLU A CA  1 
ATOM   900  C C   . GLU A 1 135 ? 38.474 21.122 7.242   1.000 29.601  0 135 GLU A C   1 
ATOM   901  O O   . GLU A 1 135 ? 37.336 20.982 7.688   1.000 31.883  0 135 GLU A O   1 
ATOM   902  C CB  . GLU A 1 135 ? 39.473 19.322 5.806   1.000 36.755  0 135 GLU A CB  1 
ATOM   903  C CG  . GLU A 1 135 ? 38.466 18.229 6.155   1.000 38.671  0 135 GLU A CG  1 
ATOM   904  C CD  . GLU A 1 135 ? 37.307 18.033 5.143   1.000 39.718  0 135 GLU A CD  1 
ATOM   905  O OE1 . GLU A 1 135 ? 37.449 18.452 3.964   1.000 37.936  0 135 GLU A OE1 1 
ATOM   906  O OE2 . GLU A 1 135 ? 36.215 17.511 5.535   1.000 42.596  0 135 GLU A OE2 1 
ATOM   907  N N   . VAL A 1 136 ? 39.461 21.622 7.985   1.000 31.352  0 136 VAL A N   1 
ATOM   908  C CA  . VAL A 1 136 ? 39.259 22.096 9.343   1.000 31.282  0 136 VAL A CA  1 
ATOM   909  C C   . VAL A 1 136 ? 38.581 23.458 9.388   1.000 29.960  0 136 VAL A C   1 
ATOM   910  O O   . VAL A 1 136 ? 37.545 23.631 10.035  1.000 31.207  0 136 VAL A O   1 
ATOM   911  C CB  . VAL A 1 136 ? 40.585 22.168 10.123  1.000 32.394  0 136 VAL A CB  1 
ATOM   912  C CG1 . VAL A 1 136 ? 40.335 22.668 11.544  1.000 34.089  0 136 VAL A CG1 1 
ATOM   913  C CG2 . VAL A 1 136 ? 41.225 20.789 10.194  1.000 35.590  0 136 VAL A CG2 1 
ATOM   914  N N   . ASN A 1 137 ? 39.189 24.414 8.686   1.000 30.296  0 137 ASN A N   1 
ATOM   915  C CA  . ASN A 1 137 ? 38.845 25.824 8.828   1.000 28.756  0 137 ASN A CA  1 
ATOM   916  C C   . ASN A 1 137 ? 37.536 26.184 8.129   1.000 31.072  0 137 ASN A C   1 
ATOM   917  O O   . ASN A 1 137 ? 36.861 27.115 8.560   1.000 30.308  0 137 ASN A O   1 
ATOM   918  C CB  . ASN A 1 137 ? 39.922 26.708 8.244   1.000 29.986  0 137 ASN A CB  1 
ATOM   919  C CG  . ASN A 1 137 ? 41.282 26.471 8.876   1.000 31.587  0 137 ASN A CG  1 
ATOM   920  O OD1 . ASN A 1 137 ? 41.393 25.794 9.898   1.000 32.737  0 137 ASN A OD1 1 
ATOM   921  N ND2 . ASN A 1 137 ? 42.326 27.058 8.313   1.000 31.447  0 137 ASN A ND2 1 
ATOM   922  N N   . LEU A 1 138 ? 37.223 25.524 7.009   1.000 30.196  0 138 LEU A N   1 
ATOM   923  C CA  . LEU A 1 138 ? 36.008 25.793 6.250   1.000 29.006  0 138 LEU A CA  1 
ATOM   924  C C   . LEU A 1 138 ? 34.977 24.691 6.473   1.000 29.319  0 138 LEU A C   1 
ATOM   925  O O   . LEU A 1 138 ? 33.913 24.928 7.024   1.000 29.120  0 138 LEU A O   1 
ATOM   926  C CB  . LEU A 1 138 ? 36.275 25.978 4.763   1.000 29.196  0 138 LEU A CB  1 
ATOM   927  C CG  . LEU A 1 138 ? 35.010 26.236 3.943   1.000 30.976  0 138 LEU A CG  1 
ATOM   928  C CD1 . LEU A 1 138 ? 34.419 27.579 4.369   1.000 33.550  0 138 LEU A CD1 1 
ATOM   929  C CD2 . LEU A 1 138 ? 35.303 26.162 2.466   1.000 34.045  0 138 LEU A CD2 1 
ATOM   930  N N   . PHE A 1 139 ? 35.251 23.480 5.994   1.000 31.417  0 139 PHE A N   1 
ATOM   931  C CA  . PHE A 1 139 ? 34.242 22.434 6.093   1.000 30.243  0 139 PHE A CA  1 
ATOM   932  C C   . PHE A 1 139 ? 33.868 22.113 7.543   1.000 31.230  0 139 PHE A C   1 
ATOM   933  O O   . PHE A 1 139 ? 32.692 21.907 7.842   1.000 32.644  0 139 PHE A O   1 
ATOM   934  C CB  . PHE A 1 139 ? 34.615 21.165 5.329   1.000 30.907  0 139 PHE A CB  1 
ATOM   935  C CG  . PHE A 1 139 ? 34.560 21.344 3.815   1.000 33.185  0 139 PHE A CG  1 
ATOM   936  C CD1 . PHE A 1 139 ? 33.361 21.550 3.171   1.000 35.947  0 139 PHE A CD1 1 
ATOM   937  C CD2 . PHE A 1 139 ? 35.716 21.310 3.050   1.000 33.112  0 139 PHE A CD2 1 
ATOM   938  C CE1 . PHE A 1 139 ? 33.288 21.706 1.802   1.000 34.951  0 139 PHE A CE1 1 
ATOM   939  C CE2 . PHE A 1 139 ? 35.641 21.430 1.662   1.000 34.344  0 139 PHE A CE2 1 
ATOM   940  C CZ  . PHE A 1 139 ? 34.424 21.668 1.055   1.000 38.157  0 139 PHE A CZ  1 
ATOM   941  N N   . GLY A 1 140 ? 34.853 22.002 8.442   1.000 30.909  0 140 GLY A N   1 
ATOM   942  C CA  . GLY A 1 140 ? 34.556 21.769 9.849   1.000 33.116  0 140 GLY A CA  1 
ATOM   943  C C   . GLY A 1 140 ? 33.731 22.891 10.470  1.000 34.215  0 140 GLY A C   1 
ATOM   944  O O   . GLY A 1 140 ? 32.758 22.633 11.157  1.000 33.426  0 140 GLY A O   1 
ATOM   945  N N   . LEU A 1 141 ? 34.085 24.150 10.188  1.000 28.861  0 141 LEU A N   1 
ATOM   946  C CA  . LEU A 1 141 ? 33.279 25.267 10.631  1.000 31.189  0 141 LEU A CA  1 
ATOM   947  C C   . LEU A 1 141 ? 31.839 25.219 10.118  1.000 31.472  0 141 LEU A C   1 
ATOM   948  O O   . LEU A 1 141 ? 30.900 25.453 10.886  1.000 32.180  0 141 LEU A O   1 
ATOM   949  C CB  . LEU A 1 141 ? 34.048 26.512 10.197  1.000 31.672  0 141 LEU A CB  1 
ATOM   950  C CG  . LEU A 1 141 ? 33.361 27.818 10.597  1.000 30.899  0 141 LEU A CG  1 
ATOM   951  C CD1 . LEU A 1 141 ? 34.424 28.881 10.823  1.000 32.385  0 141 LEU A CD1 1 
ATOM   952  C CD2 . LEU A 1 141 ? 32.367 28.246 9.561   1.000 33.575  0 141 LEU A CD2 1 
ATOM   953  N N   . ILE A 1 142 ? 31.665 24.902 8.826   1.000 30.565  0 142 ILE A N   1 
ATOM   954  C CA  . ILE A 1 142 ? 30.340 24.787 8.260   1.000 28.680  0 142 ILE A CA  1 
ATOM   955  C C   . ILE A 1 142 ? 29.562 23.670 8.948   1.000 33.528  0 142 ILE A C   1 
ATOM   956  O O   . ILE A 1 142 ? 28.403 23.860 9.327   1.000 32.220  0 142 ILE A O   1 
ATOM   957  C CB  . ILE A 1 142 ? 30.412 24.597 6.738   1.000 29.892  0 142 ILE A CB  1 
ATOM   958  C CG1 . ILE A 1 142 ? 30.959 25.880 6.059   1.000 30.434  0 142 ILE A CG1 1 
ATOM   959  C CG2 . ILE A 1 142 ? 29.057 24.224 6.166   1.000 31.833  0 142 ILE A CG2 1 
ATOM   960  C CD1 . ILE A 1 142 ? 31.204 25.713 4.580   1.000 31.615  0 142 ILE A CD1 1 
ATOM   961  N N   . ASN A 1 143 ? 30.183 22.505 9.113   1.000 33.259  0 143 ASN A N   1 
ATOM   962  C CA  . ASN A 1 143 ? 29.406 21.387 9.663   1.000 30.695  0 143 ASN A CA  1 
ATOM   963  C C   . ASN A 1 143 ? 29.008 21.611 11.112  1.000 29.703  0 143 ASN A C   1 
ATOM   964  O O   . ASN A 1 143 ? 27.876 21.314 11.511  1.000 31.561  0 143 ASN A O   1 
ATOM   965  C CB  . ASN A 1 143 ? 30.129 20.077 9.429   1.000 32.354  0 143 ASN A CB  1 
ATOM   966  C CG  . ASN A 1 143 ? 29.170 18.925 9.579   1.000 34.360  0 143 ASN A CG  1 
ATOM   967  O OD1 . ASN A 1 143 ? 27.990 19.013 9.188   1.000 37.004  0 143 ASN A OD1 1 
ATOM   968  N ND2 . ASN A 1 143 ? 29.691 17.862 10.144  1.000 35.794  0 143 ASN A ND2 1 
ATOM   969  N N   . VAL A 1 144 ? 29.925 22.144 11.917  1.000 31.189  0 144 VAL A N   1 
ATOM   970  C CA  . VAL A 1 144 ? 29.564 22.518 13.271  1.000 31.635  0 144 VAL A CA  1 
ATOM   971  C C   . VAL A 1 144 ? 28.410 23.518 13.229  1.000 34.603  0 144 VAL A C   1 
ATOM   972  O O   . VAL A 1 144 ? 27.423 23.360 13.967  1.000 32.188  0 144 VAL A O   1 
ATOM   973  C CB  . VAL A 1 144 ? 30.757 23.059 14.070  1.000 31.440  0 144 VAL A CB  1 
ATOM   974  C CG1 . VAL A 1 144 ? 30.311 23.610 15.422  1.000 33.109  0 144 VAL A CG1 1 
ATOM   975  C CG2 . VAL A 1 144 ? 31.812 21.972 14.198  1.000 32.261  0 144 VAL A CG2 1 
ATOM   976  N N   . THR A 1 145 ? 28.527 24.570 12.395  1.000 32.535  0 145 THR A N   1 
ATOM   977  C CA  . THR A 1 145 ? 27.486 25.592 12.349  1.000 31.530  0 145 THR A CA  1 
ATOM   978  C C   . THR A 1 145 ? 26.125 24.965 12.010  1.000 32.364  0 145 THR A C   1 
ATOM   979  O O   . THR A 1 145 ? 25.124 25.162 12.723  1.000 32.400  0 145 THR A O   1 
ATOM   980  C CB  . THR A 1 145 ? 27.843 26.677 11.325  1.000 30.433  0 145 THR A CB  1 
ATOM   981  O OG1 . THR A 1 145 ? 29.058 27.278 11.762  1.000 32.611  0 145 THR A OG1 1 
ATOM   982  C CG2 . THR A 1 145 ? 26.709 27.667 11.254  1.000 32.396  0 145 THR A CG2 1 
ATOM   983  N N   . LEU A 1 146 ? 26.097 24.168 10.937  1.000 29.931  0 146 LEU A N   1 
ATOM   984  C CA  . LEU A 1 146 ? 24.831 23.589 10.466  1.000 34.320  0 146 LEU A CA  1 
ATOM   985  C C   . LEU A 1 146 ? 24.206 22.650 11.532  1.000 34.236  0 146 LEU A C   1 
ATOM   986  O O   . LEU A 1 146 ? 22.995 22.658 11.739  1.000 33.740  0 146 LEU A O   1 
ATOM   987  C CB  . LEU A 1 146 ? 25.016 22.849 9.143   1.000 34.724  0 146 LEU A CB  1 
ATOM   988  C CG  . LEU A 1 146 ? 25.529 23.640 7.938   1.000 38.483  0 146 LEU A CG  1 
ATOM   989  C CD1 . LEU A 1 146 ? 25.672 22.668 6.806   1.000 43.043  0 146 LEU A CD1 1 
ATOM   990  C CD2 . LEU A 1 146 ? 24.582 24.741 7.598   1.000 42.054  0 146 LEU A CD2 1 
ATOM   991  N N   . ASN A 1 147 ? 25.026 21.885 12.248  1.000 36.075  0 147 ASN A N   1 
ATOM   992  C CA  . ASN A 1 147 ? 24.527 20.963 13.275  1.000 35.163  0 147 ASN A CA  1 
ATOM   993  C C   . ASN A 1 147 ? 24.030 21.695 14.519  1.000 35.594  0 147 ASN A C   1 
ATOM   994  O O   . ASN A 1 147 ? 23.056 21.273 15.137  1.000 35.777  0 147 ASN A O   1 
ATOM   995  C CB  . ASN A 1 147 ? 25.607 19.971 13.640  1.000 36.695  0 147 ASN A CB  1 
ATOM   996  C CG  . ASN A 1 147 ? 25.573 18.777 12.721  1.000 38.897  0 147 ASN A CG  1 
ATOM   997  O OD1 . ASN A 1 147 ? 24.869 17.796 12.985  1.000 39.672  0 147 ASN A OD1 1 
ATOM   998  N ND2 . ASN A 1 147 ? 26.403 18.808 11.699  1.000 37.801  0 147 ASN A ND2 1 
ATOM   999  N N   . MET A 1 148 ? 24.573 22.876 14.816  1.000 35.850  0 148 MET A N   1 
ATOM   1000 C CA  . MET A 1 148 ? 24.174 23.624 15.994  1.000 37.358  0 148 MET A CA  1 
ATOM   1001 C C   . MET A 1 148 ? 23.118 24.687 15.695  1.000 35.923  0 148 MET A C   1 
ATOM   1002 O O   . MET A 1 148 ? 22.481 25.244 16.609  1.000 32.403  0 148 MET A O   1 
ATOM   1003 C CB  . MET A 1 148 ? 25.376 24.320 16.628  1.000 33.320  0 148 MET A CB  1 
ATOM   1004 C CG  . MET A 1 148 ? 26.485 23.421 17.109  1.000 36.875  0 148 MET A CG  1 
ATOM   1005 S SD  . MET A 1 148 ? 25.906 22.323 18.432  1.000 40.220  0 148 MET A SD  1 
ATOM   1006 C CE  . MET A 1 148 ? 27.443 21.442 18.754  1.000 41.818  0 148 MET A CE  1 
ATOM   1007 N N   . LEU A 1 149 ? 22.917 24.993 14.419  1.000 35.586  0 149 LEU A N   1 
ATOM   1008 C CA  . LEU A 1 149 ? 22.096 26.133 14.054  1.000 36.434  0 149 LEU A CA  1 
ATOM   1009 C C   . LEU A 1 149 ? 20.658 26.042 14.591  1.000 34.353  0 149 LEU A C   1 
ATOM   1010 O O   . LEU A 1 149 ? 20.116 27.061 14.995  1.000 33.314  0 149 LEU A O   1 
ATOM   1011 C CB  . LEU A 1 149 ? 22.090 26.258 12.525  1.000 39.903  0 149 LEU A CB  1 
ATOM   1012 C CG  . LEU A 1 149 ? 21.741 27.641 11.971  1.000 41.031  0 149 LEU A CG  1 
ATOM   1013 C CD1 . LEU A 1 149 ? 22.507 28.740 12.674  1.000 40.688  0 149 LEU A CD1 1 
ATOM   1014 C CD2 . LEU A 1 149 ? 22.055 27.644 10.458  1.000 40.682  0 149 LEU A CD2 1 
ATOM   1015 N N   . PRO A 1 150 ? 19.960 24.881 14.600  1.000 31.164  0 150 PRO A N   1 
ATOM   1016 C CA  . PRO A 1 150 ? 18.625 24.830 15.190  1.000 33.003  0 150 PRO A CA  1 
ATOM   1017 C C   . PRO A 1 150 ? 18.640 25.301 16.649  1.000 36.030  0 150 PRO A C   1 
ATOM   1018 O O   . PRO A 1 150 ? 17.669 25.903 17.120  1.000 35.128  0 150 PRO A O   1 
ATOM   1019 C CB  . PRO A 1 150 ? 18.211 23.362 15.098  1.000 36.406  0 150 PRO A CB  1 
ATOM   1020 C CG  . PRO A 1 150 ? 19.083 22.776 14.014  1.000 37.546  0 150 PRO A CG  1 
ATOM   1021 C CD  . PRO A 1 150 ? 20.359 23.596 13.999  1.000 34.648  0 150 PRO A CD  1 
ATOM   1022 N N   . LEU A 1 151 ? 19.729 25.013 17.390  1.000 32.644  0 151 LEU A N   1 
ATOM   1023 C CA  . LEU A 1 151 ? 19.783 25.383 18.798  1.000 34.193  0 151 LEU A CA  1 
ATOM   1024 C C   . LEU A 1 151 ? 20.023 26.881 18.945  1.000 34.913  0 151 LEU A C   1 
ATOM   1025 O O   . LEU A 1 151 ? 19.495 27.532 19.855  1.000 33.583  0 151 LEU A O   1 
ATOM   1026 C CB  . LEU A 1 151 ? 20.862 24.549 19.474  1.000 34.702  0 151 LEU A CB  1 
ATOM   1027 C CG  . LEU A 1 151 ? 20.753 23.048 19.212  1.000 35.203  0 151 LEU A CG  1 
ATOM   1028 C CD1 . LEU A 1 151 ? 21.858 22.375 19.917  1.000 37.990  0 151 LEU A CD1 1 
ATOM   1029 C CD2 . LEU A 1 151 ? 19.441 22.480 19.634  1.000 41.631  0 151 LEU A CD2 1 
ATOM   1030 N N   . VAL A 1 152 ? 20.848 27.437 18.056  1.000 31.470  0 152 VAL A N   1 
ATOM   1031 C CA  . VAL A 1 152 ? 21.086 28.873 18.117  1.000 29.017  0 152 VAL A CA  1 
ATOM   1032 C C   . VAL A 1 152 ? 19.814 29.631 17.750  1.000 28.278  0 152 VAL A C   1 
ATOM   1033 O O   . VAL A 1 152 ? 19.554 30.701 18.297  1.000 34.635  0 152 VAL A O   1 
ATOM   1034 C CB  . VAL A 1 152 ? 22.295 29.287 17.254  1.000 32.013  0 152 VAL A CB  1 
ATOM   1035 C CG1 . VAL A 1 152 ? 22.505 30.785 17.282  1.000 31.819  0 152 VAL A CG1 1 
ATOM   1036 C CG2 . VAL A 1 152 ? 23.592 28.607 17.688  1.000 35.874  0 152 VAL A CG2 1 
ATOM   1037 N N   . LYS A 1 153 ? 19.111 29.181 16.722  1.000 29.526  0 153 LYS A N   1 
ATOM   1038 C CA  . LYS A 1 153 ? 17.830 29.780 16.358  1.000 32.919  0 153 LYS A CA  1 
ATOM   1039 C C   . LYS A 1 153 ? 16.879 29.765 17.559  1.000 34.758  0 153 LYS A C   1 
ATOM   1040 O O   . LYS A 1 153 ? 16.214 30.753 17.845  1.000 32.885  0 153 LYS A O   1 
ATOM   1041 C CB  . LYS A 1 153 ? 17.238 29.032 15.166  1.000 32.029  0 153 LYS A CB  1 
ATOM   1042 C CG  . LYS A 1 153 ? 17.906 29.338 13.822  1.000 35.972  0 153 LYS A CG  1 
ATOM   1043 C CD  . LYS A 1 153 ? 17.606 28.350 12.710  1.000 38.565  0 153 LYS A CD  1 
ATOM   1044 C CE  . LYS A 1 153 ? 16.197 28.459 12.233  1.000 36.673  0 153 LYS A CE  1 
ATOM   1045 N NZ  . LYS A 1 153 ? 15.948 27.482 11.182  1.000 35.792  0 153 LYS A NZ  1 
ATOM   1046 N N   . LYS A 1 154 ? 16.837 28.634 18.264  1.000 33.201  0 154 LYS A N   1 
ATOM   1047 C CA  . LYS A 1 154 ? 15.938 28.489 19.403  1.000 34.698  0 154 LYS A CA  1 
ATOM   1048 C C   . LYS A 1 154 ? 16.232 29.559 20.441  1.000 35.167  0 154 LYS A C   1 
ATOM   1049 O O   . LYS A 1 154 ? 15.301 30.092 21.038  1.000 35.938  0 154 LYS A O   1 
ATOM   1050 C CB  . LYS A 1 154 ? 16.042 27.104 20.040  1.000 37.771  0 154 LYS A CB  1 
ATOM   1051 C CG  . LYS A 1 154 ? 15.044 26.854 21.155  1.000 45.697  0 154 LYS A CG  1 
ATOM   1052 C CD  . LYS A 1 154 ? 15.169 25.441 21.710  1.000 46.751  0 154 LYS A CD  1 
ATOM   1053 C CE  . LYS A 1 154 ? 14.980 24.291 20.756  1.000 53.632  0 154 LYS A CE  1 
ATOM   1054 N NZ  . LYS A 1 154 ? 13.671 24.329 20.080  1.000 55.909  0 154 LYS A NZ  1 
ATOM   1055 N N   . ALA A 1 155 ? 17.521 29.878 20.659  1.000 34.195  0 155 ALA A N   1 
ATOM   1056 C CA  . ALA A 1 155 ? 17.920 30.869 21.630  1.000 33.616  0 155 ALA A CA  1 
ATOM   1057 C C   . ALA A 1 155 ? 17.855 32.286 21.087  1.000 37.528  0 155 ALA A C   1 
ATOM   1058 O O   . ALA A 1 155 ? 18.128 33.210 21.853  1.000 35.652  0 155 ALA A O   1 
ATOM   1059 C CB  . ALA A 1 155 ? 19.328 30.627 22.085  1.000 37.965  0 155 ALA A CB  1 
ATOM   1060 N N   . ARG A 1 156 ? 17.625 32.445 19.784  1.000 37.037  0 156 ARG A N   1 
ATOM   1061 C CA  . ARG A 1 156 ? 17.850 33.730 19.113  1.000 35.317  0 156 ARG A CA  1 
ATOM   1062 C C   . ARG A 1 156 ? 19.231 34.253 19.440  1.000 34.716  0 156 ARG A C   1 
ATOM   1063 O O   . ARG A 1 156 ? 19.436 35.433 19.782  1.000 34.721  0 156 ARG A O   1 
ATOM   1064 C CB  . ARG A 1 156 ? 16.849 34.816 19.514  1.000 43.962  0 156 ARG A CB  1 
ATOM   1065 C CG  . ARG A 1 156 ? 15.384 34.583 19.191  1.000 59.080  0 156 ARG A CG  1 
ATOM   1066 C CD  . ARG A 1 156 ? 14.715 35.940 19.425  1.000 73.688  0 156 ARG A CD  1 
ATOM   1067 N NE  . ARG A 1 156 ? 13.250 35.981 19.415  1.000 90.578  0 156 ARG A NE  1 
ATOM   1068 C CZ  . ARG A 1 156 ? 12.410 35.203 18.721  1.000 105.959 0 156 ARG A CZ  1 
ATOM   1069 N NH1 . ARG A 1 156 ? 12.707 33.946 18.418  1.000 94.984  0 156 ARG A NH1 1 
ATOM   1070 N NH2 . ARG A 1 156 ? 11.208 35.668 18.427  1.000 113.508 0 156 ARG A NH2 1 
ATOM   1071 N N   . GLY A 1 157 ? 20.196 33.350 19.321  1.000 32.770  0 157 GLY A N   1 
ATOM   1072 C CA  . GLY A 1 157 ? 21.561 33.600 19.751  1.000 33.583  0 157 GLY A CA  1 
ATOM   1073 C C   . GLY A 1 157 ? 22.515 34.133 18.676  1.000 35.046  0 157 GLY A C   1 
ATOM   1074 O O   . GLY A 1 157 ? 22.149 34.909 17.795  1.000 35.427  0 157 GLY A O   1 
ATOM   1075 N N   . ARG A 1 158 ? 23.791 33.781 18.857  1.000 33.423  0 158 ARG A N   1 
ATOM   1076 C CA  . ARG A 1 158 ? 24.925 34.436 18.235  1.000 35.108  0 158 ARG A CA  1 
ATOM   1077 C C   . ARG A 1 158 ? 25.888 33.385 17.695  1.000 37.091  0 158 ARG A C   1 
ATOM   1078 O O   . ARG A 1 158 ? 26.292 32.459 18.431  1.000 34.277  0 158 ARG A O   1 
ATOM   1079 C CB  . ARG A 1 158 ? 25.690 35.276 19.262  1.000 40.584  0 158 ARG A CB  1 
ATOM   1080 C CG  . ARG A 1 158 ? 24.874 36.197 20.156  1.000 44.199  0 158 ARG A CG  1 
ATOM   1081 C CD  . ARG A 1 158 ? 24.615 37.501 19.509  1.000 45.613  0 158 ARG A CD  1 
ATOM   1082 N NE  . ARG A 1 158 ? 23.711 38.304 20.341  1.000 39.720  0 158 ARG A NE  1 
ATOM   1083 C CZ  . ARG A 1 158 ? 24.005 39.377 21.060  1.000 40.419  0 158 ARG A CZ  1 
ATOM   1084 N NH1 . ARG A 1 158 ? 25.259 39.713 21.325  1.000 42.813  0 158 ARG A NH1 1 
ATOM   1085 N NH2 . ARG A 1 158 ? 23.016 40.070 21.624  1.000 41.630  0 158 ARG A NH2 1 
ATOM   1086 N N   . VAL A 1 159 ? 26.241 33.534 16.412  1.000 33.199  0 159 VAL A N   1 
ATOM   1087 C CA  . VAL A 1 159 ? 27.306 32.756 15.787  1.000 33.402  0 159 VAL A CA  1 
ATOM   1088 C C   . VAL A 1 159 ? 28.506 33.667 15.560  1.000 32.815  0 159 VAL A C   1 
ATOM   1089 O O   . VAL A 1 159 ? 28.391 34.701 14.897  1.000 32.792  0 159 VAL A O   1 
ATOM   1090 C CB  . VAL A 1 159 ? 26.873 32.073 14.478  1.000 34.091  0 159 VAL A CB  1 
ATOM   1091 C CG1 . VAL A 1 159 ? 27.996 31.228 13.868  1.000 32.400  0 159 VAL A CG1 1 
ATOM   1092 C CG2 . VAL A 1 159 ? 25.632 31.216 14.660  1.000 36.910  0 159 VAL A CG2 1 
ATOM   1093 N N   . ILE A 1 160 ? 29.648 33.268 16.134  1.000 29.486  0 160 ILE A N   1 
ATOM   1094 C CA  . ILE A 1 160 ? 30.904 33.978 16.033  1.000 30.512  0 160 ILE A CA  1 
ATOM   1095 C C   . ILE A 1 160 ? 31.922 33.126 15.269  1.000 33.504  0 160 ILE A C   1 
ATOM   1096 O O   . ILE A 1 160 ? 32.317 32.050 15.701  1.000 33.891  0 160 ILE A O   1 
ATOM   1097 C CB  . ILE A 1 160 ? 31.380 34.328 17.443  1.000 37.647  0 160 ILE A CB  1 
ATOM   1098 C CG1 . ILE A 1 160 ? 30.321 35.186 18.158  1.000 39.703  0 160 ILE A CG1 1 
ATOM   1099 C CG2 . ILE A 1 160 ? 32.757 34.970 17.384  1.000 38.144  0 160 ILE A CG2 1 
ATOM   1100 C CD1 . ILE A 1 160 ? 30.384 35.134 19.662  1.000 46.508  0 160 ILE A CD1 1 
ATOM   1101 N N   . ASN A 1 161 ? 32.357 33.629 14.121  1.000 30.835  0 161 ASN A N   1 
ATOM   1102 C CA  . ASN A 1 161 ? 33.292 32.930 13.245  1.000 31.330  0 161 ASN A CA  1 
ATOM   1103 C C   . ASN A 1 161 ? 34.650 33.590 13.316  1.000 34.443  0 161 ASN A C   1 
ATOM   1104 O O   . ASN A 1 161 ? 34.769 34.811 13.131  1.000 32.808  0 161 ASN A O   1 
ATOM   1105 C CB  . ASN A 1 161 ? 32.771 32.895 11.818  1.000 31.408  0 161 ASN A CB  1 
ATOM   1106 C CG  . ASN A 1 161 ? 31.491 32.100 11.719  1.000 34.056  0 161 ASN A CG  1 
ATOM   1107 O OD1 . ASN A 1 161 ? 31.411 30.987 12.251  1.000 33.797  0 161 ASN A OD1 1 
ATOM   1108 N ND2 . ASN A 1 161 ? 30.500 32.627 11.010  1.000 35.401  0 161 ASN A ND2 1 
ATOM   1109 N N   . VAL A 1 162 ? 35.685 32.786 13.593  1.000 29.616  0 162 VAL A N   1 
ATOM   1110 C CA  . VAL A 1 162 ? 37.045 33.319 13.624  1.000 31.103  0 162 VAL A CA  1 
ATOM   1111 C C   . VAL A 1 162 ? 37.670 33.187 12.228  1.000 33.393  0 162 VAL A C   1 
ATOM   1112 O O   . VAL A 1 162 ? 37.955 32.100 11.720  1.000 33.718  0 162 VAL A O   1 
ATOM   1113 C CB  . VAL A 1 162 ? 37.928 32.702 14.720  1.000 32.706  0 162 VAL A CB  1 
ATOM   1114 C CG1 . VAL A 1 162 ? 39.284 33.362 14.777  1.000 32.669  0 162 VAL A CG1 1 
ATOM   1115 C CG2 . VAL A 1 162 ? 37.287 32.787 16.088  1.000 34.060  0 162 VAL A CG2 1 
ATOM   1116 N N   . SER A 1 163 ? 37.851 34.335 11.576  1.000 30.170  0 163 SER A N   1 
ATOM   1117 C CA  . SER A 1 163 ? 38.445 34.398 10.260  1.000 32.094  0 163 SER A CA  1 
ATOM   1118 C C   . SER A 1 163 ? 39.919 34.727 10.501  1.000 34.243  0 163 SER A C   1 
ATOM   1119 O O   . SER A 1 163 ? 40.538 34.137 11.372  1.000 38.653  0 163 SER A O   1 
ATOM   1120 C CB  . SER A 1 163 ? 37.739 35.416 9.359   1.000 35.417  0 163 SER A CB  1 
ATOM   1121 O OG  . SER A 1 163 ? 38.347 35.490 8.080   1.000 36.833  0 163 SER A OG  1 
ATOM   1122 N N   . SER A 1 164 ? 40.425 35.738 9.802   1.000 31.870  0 164 SER A N   1 
ATOM   1123 C CA  . SER A 1 164 ? 41.807 36.147 9.842   1.000 32.792  0 164 SER A CA  1 
ATOM   1124 C C   . SER A 1 164 ? 41.953 37.374 8.937   1.000 35.717  0 164 SER A C   1 
ATOM   1125 O O   . SER A 1 164 ? 41.188 37.534 7.971   1.000 33.755  0 164 SER A O   1 
ATOM   1126 C CB  . SER A 1 164 ? 42.729 35.047 9.354   1.000 32.042  0 164 SER A CB  1 
ATOM   1127 O OG  . SER A 1 164 ? 44.081 35.493 9.287   1.000 34.403  0 164 SER A OG  1 
ATOM   1128 N N   . ILE A 1 165 ? 43.011 38.155 9.173   1.000 34.991  0 165 ILE A N   1 
ATOM   1129 C CA  . ILE A 1 165 ? 43.366 39.153 8.188   1.000 39.434  0 165 ILE A CA  1 
ATOM   1130 C C   . ILE A 1 165 ? 43.717 38.415 6.890   1.000 35.426  0 165 ILE A C   1 
ATOM   1131 O O   . ILE A 1 165 ? 43.526 38.984 5.835   1.000 32.901  0 165 ILE A O   1 
ATOM   1132 C CB  . ILE A 1 165 ? 44.473 40.130 8.651   1.000 47.531  0 165 ILE A CB  1 
ATOM   1133 C CG1 . ILE A 1 165 ? 45.746 39.412 9.067   1.000 59.699  0 165 ILE A CG1 1 
ATOM   1134 C CG2 . ILE A 1 165 ? 43.946 41.053 9.755   1.000 48.868  0 165 ILE A CG2 1 
ATOM   1135 C CD1 . ILE A 1 165 ? 46.929 40.341 9.324   1.000 70.264  0 165 ILE A CD1 1 
ATOM   1136 N N   . GLY A 1 166 ? 44.162 37.143 6.987   1.000 35.328  0 166 GLY A N   1 
ATOM   1137 C CA  . GLY A 1 166 ? 44.462 36.286 5.850   1.000 33.871  0 166 GLY A CA  1 
ATOM   1138 C C   . GLY A 1 166 ? 43.245 35.801 5.054   1.000 32.228  0 166 GLY A C   1 
ATOM   1139 O O   . GLY A 1 166 ? 43.412 35.124 4.033   1.000 32.470  0 166 GLY A O   1 
ATOM   1140 N N   . GLY A 1 167 ? 42.036 36.086 5.528   1.000 28.907  0 167 GLY A N   1 
ATOM   1141 C CA  . GLY A 1 167 ? 40.799 35.938 4.789   1.000 27.175  0 167 GLY A CA  1 
ATOM   1142 C C   . GLY A 1 167 ? 40.401 37.192 3.997   1.000 28.255  0 167 GLY A C   1 
ATOM   1143 O O   . GLY A 1 167 ? 39.368 37.172 3.316   1.000 30.340  0 167 GLY A O   1 
ATOM   1144 N N   . ARG A 1 168 ? 41.205 38.261 4.115   1.000 29.927  0 168 ARG A N   1 
ATOM   1145 C CA  . ARG A 1 168 ? 40.941 39.524 3.433   1.000 31.150  0 168 ARG A CA  1 
ATOM   1146 C C   . ARG A 1 168 ? 42.118 39.951 2.551   1.000 31.658  0 168 ARG A C   1 
ATOM   1147 O O   . ARG A 1 168 ? 41.929 40.634 1.547   1.000 32.539  0 168 ARG A O   1 
ATOM   1148 C CB  . ARG A 1 168 ? 40.731 40.617 4.493   1.000 33.455  0 168 ARG A CB  1 
ATOM   1149 C CG  . ARG A 1 168 ? 39.541 40.443 5.428   1.000 36.064  0 168 ARG A CG  1 
ATOM   1150 C CD  . ARG A 1 168 ? 38.221 40.458 4.688   1.000 40.852  0 168 ARG A CD  1 
ATOM   1151 N NE  . ARG A 1 168 ? 37.911 41.812 4.218   1.000 42.615  0 168 ARG A NE  1 
ATOM   1152 C CZ  . ARG A 1 168 ? 37.488 42.852 4.945   1.000 43.248  0 168 ARG A CZ  1 
ATOM   1153 N NH1 . ARG A 1 168 ? 37.159 42.727 6.219   1.000 43.011  0 168 ARG A NH1 1 
ATOM   1154 N NH2 . ARG A 1 168 ? 37.348 44.041 4.356   1.000 48.934  0 168 ARG A NH2 1 
ATOM   1155 N N   . LEU A 1 169 ? 43.316 39.536 2.914   1.000 31.041  0 169 LEU A N   1 
ATOM   1156 C CA  . LEU A 1 169 ? 44.532 39.761 2.148   1.000 33.288  0 169 LEU A CA  1 
ATOM   1157 C C   . LEU A 1 169 ? 45.322 38.456 2.135   1.000 36.176  0 169 LEU A C   1 
ATOM   1158 O O   . LEU A 1 169 ? 45.447 37.812 3.169   1.000 34.951  0 169 LEU A O   1 
ATOM   1159 C CB  . LEU A 1 169 ? 45.235 40.903 2.893   1.000 43.362  0 169 LEU A CB  1 
ATOM   1160 C CG  . LEU A 1 169 ? 46.292 41.625 2.065   1.000 51.298  0 169 LEU A CG  1 
ATOM   1161 C CD1 . LEU A 1 169 ? 46.324 43.114 2.283   1.000 58.809  0 169 LEU A CD1 1 
ATOM   1162 C CD2 . LEU A 1 169 ? 47.592 40.960 2.409   1.000 60.648  0 169 LEU A CD2 1 
ATOM   1163 N N   . ALA A 1 170 ? 45.773 38.007 0.958   1.000 33.432  0 170 ALA A N   1 
ATOM   1164 C CA  . ALA A 1 170 ? 46.424 36.705 0.856   1.000 35.367  0 170 ALA A CA  1 
ATOM   1165 C C   . ALA A 1 170 ? 47.884 36.760 1.329   1.000 35.635  0 170 ALA A C   1 
ATOM   1166 O O   . ALA A 1 170 ? 48.740 37.358 0.700   1.000 36.357  0 170 ALA A O   1 
ATOM   1167 C CB  . ALA A 1 170 ? 46.329 36.218 -0.576  1.000 35.992  0 170 ALA A CB  1 
ATOM   1168 N N   . PHE A 1 171 ? 48.245 36.003 2.350   1.000 42.375  0 171 PHE A N   1 
ATOM   1169 C CA  . PHE A 1 171 ? 49.599 36.162 2.868   1.000 47.984  0 171 PHE A CA  1 
ATOM   1170 C C   . PHE A 1 171 ? 50.637 35.256 2.187   1.000 58.901  0 171 PHE A C   1 
ATOM   1171 O O   . PHE A 1 171 ? 51.814 35.613 2.133   1.000 63.616  0 171 PHE A O   1 
ATOM   1172 C CB  . PHE A 1 171 ? 49.569 36.082 4.399   1.000 61.607  0 171 PHE A CB  1 
ATOM   1173 C CG  . PHE A 1 171 ? 49.300 37.473 4.960   1.000 60.805  0 171 PHE A CG  1 
ATOM   1174 C CD1 . PHE A 1 171 ? 50.322 38.427 5.003   1.000 63.639  0 171 PHE A CD1 1 
ATOM   1175 C CD2 . PHE A 1 171 ? 48.013 37.855 5.326   1.000 62.162  0 171 PHE A CD2 1 
ATOM   1176 C CE1 . PHE A 1 171 ? 50.083 39.701 5.489   1.000 65.180  0 171 PHE A CE1 1 
ATOM   1177 C CE2 . PHE A 1 171 ? 47.766 39.148 5.778   1.000 72.604  0 171 PHE A CE2 1 
ATOM   1178 C CZ  . PHE A 1 171 ? 48.807 40.067 5.867   1.000 73.629  0 171 PHE A CZ  1 
ATOM   1179 N N   . GLY A 1 172 ? 50.272 34.112 1.636   1.000 50.783  0 172 GLY A N   1 
ATOM   1180 C CA  . GLY A 1 172 ? 51.305 33.296 1.006   1.000 45.871  0 172 GLY A CA  1 
ATOM   1181 C C   . GLY A 1 172 ? 50.681 32.029 0.460   1.000 49.008  0 172 GLY A C   1 
ATOM   1182 O O   . GLY A 1 172 ? 49.488 31.814 0.650   1.000 46.926  0 172 GLY A O   1 
ATOM   1183 N N   . GLY A 1 173 ? 51.481 31.181 -0.197  1.000 43.217  0 173 GLY A N   1 
ATOM   1184 C CA  . GLY A 1 173 ? 50.911 30.018 -0.860  1.000 38.278  0 173 GLY A CA  1 
ATOM   1185 C C   . GLY A 1 173 ? 50.353 29.012 0.155   1.000 42.196  0 173 GLY A C   1 
ATOM   1186 O O   . GLY A 1 173 ? 50.743 29.017 1.308   1.000 43.723  0 173 GLY A O   1 
ATOM   1187 N N   . GLY A 1 174 ? 49.504 28.094 -0.308  1.000 34.844  0 174 GLY A N   1 
ATOM   1188 C CA  . GLY A 1 174 ? 48.931 27.081 0.550   1.000 36.622  0 174 GLY A CA  1 
ATOM   1189 C C   . GLY A 1 174 ? 47.456 27.334 0.801   1.000 38.818  0 174 GLY A C   1 
ATOM   1190 O O   . GLY A 1 174 ? 46.894 28.366 0.406   1.000 32.686  0 174 GLY A O   1 
ATOM   1191 N N   . GLY A 1 175 ? 46.856 26.354 1.472   1.000 31.148  0 175 GLY A N   1 
ATOM   1192 C CA  . GLY A 1 175 ? 45.429 26.284 1.698   1.000 31.706  0 175 GLY A CA  1 
ATOM   1193 C C   . GLY A 1 175 ? 44.866 27.239 2.752   1.000 30.934  0 175 GLY A C   1 
ATOM   1194 O O   . GLY A 1 175 ? 43.649 27.390 2.842   1.000 30.977  0 175 GLY A O   1 
ATOM   1195 N N   . TYR A 1 176 ? 45.698 27.813 3.615   1.000 30.434  0 176 TYR A N   1 
ATOM   1196 C CA  . TYR A 1 176 ? 45.154 28.612 4.690   1.000 32.100  0 176 TYR A CA  1 
ATOM   1197 C C   . TYR A 1 176 ? 44.406 29.832 4.134   1.000 28.616  0 176 TYR A C   1 
ATOM   1198 O O   . TYR A 1 176 ? 43.278 30.099 4.532   1.000 28.894  0 176 TYR A O   1 
ATOM   1199 C CB  . TYR A 1 176 ? 46.253 29.064 5.639   1.000 30.055  0 176 TYR A CB  1 
ATOM   1200 C CG  . TYR A 1 176 ? 45.769 29.817 6.863   1.000 29.085  0 176 TYR A CG  1 
ATOM   1201 C CD1 . TYR A 1 176 ? 45.224 29.142 7.937   1.000 31.989  0 176 TYR A CD1 1 
ATOM   1202 C CD2 . TYR A 1 176 ? 45.902 31.198 6.947   1.000 33.232  0 176 TYR A CD2 1 
ATOM   1203 C CE1 . TYR A 1 176 ? 44.831 29.794 9.089   1.000 30.927  0 176 TYR A CE1 1 
ATOM   1204 C CE2 . TYR A 1 176 ? 45.494 31.874 8.085   1.000 32.673  0 176 TYR A CE2 1 
ATOM   1205 C CZ  . TYR A 1 176 ? 44.981 31.171 9.157   1.000 32.560  0 176 TYR A CZ  1 
ATOM   1206 O OH  . TYR A 1 176 ? 44.612 31.805 10.293  1.000 35.284  0 176 TYR A OH  1 
ATOM   1207 N N   . THR A 1 177 ? 45.037 30.546 3.221   1.000 29.578  0 177 THR A N   1 
ATOM   1208 C CA  . THR A 1 177 ? 44.420 31.719 2.597   1.000 33.050  0 177 THR A CA  1 
ATOM   1209 C C   . THR A 1 177 ? 43.040 31.390 2.009   1.000 29.561  0 177 THR A C   1 
ATOM   1210 O O   . THR A 1 177 ? 42.015 31.981 2.377   1.000 28.264  0 177 THR A O   1 
ATOM   1211 C CB  . THR A 1 177 ? 45.341 32.257 1.496   1.000 37.606  0 177 THR A CB  1 
ATOM   1212 O OG1 . THR A 1 177 ? 46.484 32.825 2.120   1.000 43.706  0 177 THR A OG1 1 
ATOM   1213 C CG2 . THR A 1 177 ? 44.678 33.303 0.615   1.000 34.853  0 177 THR A CG2 1 
ATOM   1214 N N   . PRO A 1 178 ? 42.921 30.438 1.047   1.000 28.483  0 178 PRO A N   1 
ATOM   1215 C CA  . PRO A 1 178 ? 41.604 30.133 0.489   1.000 27.662  0 178 PRO A CA  1 
ATOM   1216 C C   . PRO A 1 178 ? 40.592 29.718 1.544   1.000 28.736  0 178 PRO A C   1 
ATOM   1217 O O   . PRO A 1 178 ? 39.429 30.097 1.427   1.000 30.168  0 178 PRO A O   1 
ATOM   1218 C CB  . PRO A 1 178 ? 41.829 29.063 -0.557  1.000 29.342  0 178 PRO A CB  1 
ATOM   1219 C CG  . PRO A 1 178 ? 43.262 28.728 -0.498  1.000 34.656  0 178 PRO A CG  1 
ATOM   1220 C CD  . PRO A 1 178 ? 44.007 29.799 0.275   1.000 30.986  0 178 PRO A CD  1 
ATOM   1221 N N   . SER A 1 179 ? 41.042 28.966 2.573   1.000 28.752  0 179 SER A N   1 
ATOM   1222 C CA  . SER A 1 179 ? 40.153 28.562 3.659   1.000 27.448  0 179 SER A CA  1 
ATOM   1223 C C   . SER A 1 179 ? 39.517 29.762 4.349   1.000 29.272  0 179 SER A C   1 
ATOM   1224 O O   . SER A 1 179 ? 38.299 29.736 4.618   1.000 30.419  0 179 SER A O   1 
ATOM   1225 C CB  . SER A 1 179 ? 40.810 27.632 4.685   1.000 30.976  0 179 SER A CB  1 
ATOM   1226 O OG  . SER A 1 179 ? 41.697 28.268 5.606   1.000 32.108  0 179 SER A OG  1 
ATOM   1227 N N   . LYS A 1 180 ? 40.336 30.790 4.632   1.000 29.000  0 180 LYS A N   1 
ATOM   1228 C CA  . LYS A 1 180 ? 39.821 31.919 5.399   1.000 30.395  0 180 LYS A CA  1 
ATOM   1229 C C   . LYS A 1 180 ? 38.970 32.848 4.540   1.000 29.530  0 180 LYS A C   1 
ATOM   1230 O O   . LYS A 1 180 ? 37.986 33.430 5.027   1.000 30.613  0 180 LYS A O   1 
ATOM   1231 C CB  . LYS A 1 180 ? 40.981 32.602 6.114   1.000 30.478  0 180 LYS A CB  1 
ATOM   1232 C CG  . LYS A 1 180 ? 41.545 31.728 7.232   1.000 32.352  0 180 LYS A CG  1 
ATOM   1233 C CD  . LYS A 1 180 ? 40.574 31.488 8.393   1.000 33.012  0 180 LYS A CD  1 
ATOM   1234 C CE  . LYS A 1 180 ? 41.248 30.843 9.576   1.000 36.863  0 180 LYS A CE  1 
ATOM   1235 N NZ  . LYS A 1 180 ? 40.303 30.593 10.673  1.000 33.966  0 180 LYS A NZ  1 
ATOM   1236 N N   . TYR A 1 181 ? 39.378 33.027 3.278   1.000 28.768  0 181 TYR A N   1 
ATOM   1237 C CA  . TYR A 1 181 ? 38.542 33.722 2.310   1.000 28.674  0 181 TYR A CA  1 
ATOM   1238 C C   . TYR A 1 181 ? 37.172 33.085 2.273   1.000 27.935  0 181 TYR A C   1 
ATOM   1239 O O   . TYR A 1 181 ? 36.145 33.761 2.315   1.000 28.204  0 181 TYR A O   1 
ATOM   1240 C CB  . TYR A 1 181 ? 39.193 33.807 0.923   1.000 29.274  0 181 TYR A CB  1 
ATOM   1241 C CG  . TYR A 1 181 ? 40.107 34.997 0.639   1.000 29.212  0 181 TYR A CG  1 
ATOM   1242 C CD1 . TYR A 1 181 ? 41.353 35.110 1.245   1.000 30.331  0 181 TYR A CD1 1 
ATOM   1243 C CD2 . TYR A 1 181 ? 39.743 35.968 -0.287  1.000 32.443  0 181 TYR A CD2 1 
ATOM   1244 C CE1 . TYR A 1 181 ? 42.183 36.183 0.965   1.000 32.405  0 181 TYR A CE1 1 
ATOM   1245 C CE2 . TYR A 1 181 ? 40.557 37.049 -0.582  1.000 31.085  0 181 TYR A CE2 1 
ATOM   1246 C CZ  . TYR A 1 181 ? 41.775 37.162 0.073   1.000 34.738  0 181 TYR A CZ  1 
ATOM   1247 O OH  . TYR A 1 181 ? 42.661 38.155 -0.208  1.000 32.204  0 181 TYR A OH  1 
ATOM   1248 N N   . ALA A 1 182 ? 37.141 31.753 2.187   1.000 27.837  0 182 ALA A N   1 
ATOM   1249 C CA  . ALA A 1 182 ? 35.890 31.040 2.092   1.000 26.678  0 182 ALA A CA  1 
ATOM   1250 C C   . ALA A 1 182 ? 35.031 31.252 3.337   1.000 27.528  0 182 ALA A C   1 
ATOM   1251 O O   . ALA A 1 182 ? 33.812 31.326 3.233   1.000 28.806  0 182 ALA A O   1 
ATOM   1252 C CB  . ALA A 1 182 ? 36.206 29.573 1.831   1.000 27.699  0 182 ALA A CB  1 
ATOM   1253 N N   . VAL A 1 183 ? 35.640 31.311 4.518   1.000 28.125  0 183 VAL A N   1 
ATOM   1254 C CA  . VAL A 1 183 ? 34.912 31.526 5.756   1.000 29.952  0 183 VAL A CA  1 
ATOM   1255 C C   . VAL A 1 183 ? 34.248 32.899 5.729   1.000 30.965  0 183 VAL A C   1 
ATOM   1256 O O   . VAL A 1 183 ? 33.119 33.054 6.177   1.000 30.879  0 183 VAL A O   1 
ATOM   1257 C CB  . VAL A 1 183 ? 35.891 31.435 6.951   1.000 31.876  0 183 VAL A CB  1 
ATOM   1258 C CG1 . VAL A 1 183 ? 35.284 32.052 8.205   1.000 33.047  0 183 VAL A CG1 1 
ATOM   1259 C CG2 . VAL A 1 183 ? 36.282 29.984 7.214   1.000 34.017  0 183 VAL A CG2 1 
ATOM   1260 N N   . GLU A 1 184 ? 34.943 33.895 5.209   1.000 28.555  0 184 GLU A N   1 
ATOM   1261 C CA  . GLU A 1 184 ? 34.317 35.233 5.094   1.000 31.370  0 184 GLU A CA  1 
ATOM   1262 C C   . GLU A 1 184 ? 33.033 35.196 4.258   1.000 32.297  0 184 GLU A C   1 
ATOM   1263 O O   . GLU A 1 184 ? 32.017 35.795 4.629   1.000 31.119  0 184 GLU A O   1 
ATOM   1264 C CB  . GLU A 1 184 ? 35.282 36.194 4.407   1.000 33.029  0 184 GLU A CB  1 
ATOM   1265 C CG  . GLU A 1 184 ? 36.513 36.528 5.238   1.000 32.429  0 184 GLU A CG  1 
ATOM   1266 C CD  . GLU A 1 184 ? 36.320 37.718 6.172   1.000 37.250  0 184 GLU A CD  1 
ATOM   1267 O OE1 . GLU A 1 184 ? 35.431 38.555 5.887   1.000 35.410  0 184 GLU A OE1 1 
ATOM   1268 O OE2 . GLU A 1 184 ? 37.083 37.823 7.153   1.000 36.088  0 184 GLU A OE2 1 
ATOM   1269 N N   . GLY A 1 185 ? 33.076 34.509 3.105   1.000 30.494  0 185 GLY A N   1 
ATOM   1270 C CA  . GLY A 1 185 ? 31.903 34.391 2.257   1.000 30.685  0 185 GLY A CA  1 
ATOM   1271 C C   . GLY A 1 185 ? 30.772 33.587 2.909   1.000 33.370  0 185 GLY A C   1 
ATOM   1272 O O   . GLY A 1 185 ? 29.618 33.997 2.861   1.000 33.257  0 185 GLY A O   1 
ATOM   1273 N N   . PHE A 1 186 ? 31.106 32.434 3.527   1.000 30.081  0 186 PHE A N   1 
ATOM   1274 C CA  . PHE A 1 186 ? 30.107 31.668 4.245   1.000 31.992  0 186 PHE A CA  1 
ATOM   1275 C C   . PHE A 1 186 ? 29.468 32.516 5.365   1.000 28.505  0 186 PHE A C   1 
ATOM   1276 O O   . PHE A 1 186 ? 28.253 32.515 5.585   1.000 29.783  0 186 PHE A O   1 
ATOM   1277 C CB  . PHE A 1 186 ? 30.750 30.374 4.762   1.000 31.123  0 186 PHE A CB  1 
ATOM   1278 C CG  . PHE A 1 186 ? 29.825 29.622 5.723   1.000 30.858  0 186 PHE A CG  1 
ATOM   1279 C CD1 . PHE A 1 186 ? 28.728 28.911 5.254   1.000 31.071  0 186 PHE A CD1 1 
ATOM   1280 C CD2 . PHE A 1 186 ? 30.043 29.643 7.092   1.000 32.139  0 186 PHE A CD2 1 
ATOM   1281 C CE1 . PHE A 1 186 ? 27.892 28.257 6.142   1.000 31.407  0 186 PHE A CE1 1 
ATOM   1282 C CE2 . PHE A 1 186 ? 29.161 29.023 7.979   1.000 30.914  0 186 PHE A CE2 1 
ATOM   1283 C CZ  . PHE A 1 186 ? 28.114 28.299 7.491   1.000 30.333  0 186 PHE A CZ  1 
ATOM   1284 N N   . ASN A 1 187 ? 30.304 33.169 6.142   1.000 32.532  0 187 ASN A N   1 
ATOM   1285 C CA  . ASN A 1 187 ? 29.845 34.037 7.220   1.000 32.575  0 187 ASN A CA  1 
ATOM   1286 C C   . ASN A 1 187 ? 28.719 34.947 6.719   1.000 33.341  0 187 ASN A C   1 
ATOM   1287 O O   . ASN A 1 187 ? 27.693 35.164 7.376   1.000 29.522  0 187 ASN A O   1 
ATOM   1288 C CB  . ASN A 1 187 ? 31.031 34.777 7.811   1.000 32.361  0 187 ASN A CB  1 
ATOM   1289 C CG  . ASN A 1 187 ? 30.630 35.748 8.894   1.000 30.891  0 187 ASN A CG  1 
ATOM   1290 O OD1 . ASN A 1 187 ? 30.638 35.395 10.070  1.000 32.522  0 187 ASN A OD1 1 
ATOM   1291 N ND2 . ASN A 1 187 ? 30.296 36.963 8.529   1.000 31.749  0 187 ASN A ND2 1 
ATOM   1292 N N   . ASP A 1 188 ? 28.974 35.593 5.592   1.000 30.787  0 188 ASP A N   1 
ATOM   1293 C CA  . ASP A 1 188 ? 28.029 36.598 5.103   1.000 35.127  0 188 ASP A CA  1 
ATOM   1294 C C   . ASP A 1 188 ? 26.743 35.962 4.596   1.000 30.212  0 188 ASP A C   1 
ATOM   1295 O O   . ASP A 1 188 ? 25.656 36.474 4.872   1.000 31.898  0 188 ASP A O   1 
ATOM   1296 C CB  . ASP A 1 188 ? 28.653 37.466 4.034   1.000 34.338  0 188 ASP A CB  1 
ATOM   1297 C CG  . ASP A 1 188 ? 29.740 38.443 4.472   1.000 36.123  0 188 ASP A CG  1 
ATOM   1298 O OD1 . ASP A 1 188 ? 30.086 38.495 5.669   1.000 34.979  0 188 ASP A OD1 1 
ATOM   1299 O OD2 . ASP A 1 188 ? 30.241 39.157 3.584   1.000 36.310  0 188 ASP A OD2 1 
ATOM   1300 N N   . SER A 1 189 ? 26.848 34.838 3.886   1.000 31.236  0 189 SER A N   1 
ATOM   1301 C CA  . SER A 1 189 ? 25.673 34.074 3.476   1.000 30.820  0 189 SER A CA  1 
ATOM   1302 C C   . SER A 1 189 ? 24.834 33.709 4.707   1.000 31.833  0 189 SER A C   1 
ATOM   1303 O O   . SER A 1 189 ? 23.607 33.879 4.703   1.000 31.881  0 189 SER A O   1 
ATOM   1304 C CB  . SER A 1 189 ? 26.041 32.794 2.781   1.000 34.023  0 189 SER A CB  1 
ATOM   1305 O OG  . SER A 1 189 ? 26.727 32.951 1.556   1.000 34.882  0 189 SER A OG  1 
ATOM   1306 N N   . LEU A 1 190 ? 25.501 33.173 5.741   1.000 31.762  0 190 LEU A N   1 
ATOM   1307 C CA  . LEU A 1 190 ? 24.828 32.766 6.980   1.000 31.586  0 190 LEU A CA  1 
ATOM   1308 C C   . LEU A 1 190 ? 24.162 33.969 7.645   1.000 34.268  0 190 LEU A C   1 
ATOM   1309 O O   . LEU A 1 190 ? 23.005 33.883 8.082   1.000 33.521  0 190 LEU A O   1 
ATOM   1310 C CB  . LEU A 1 190 ? 25.841 32.125 7.918   1.000 32.188  0 190 LEU A CB  1 
ATOM   1311 C CG  . LEU A 1 190 ? 25.345 31.708 9.315   1.000 33.499  0 190 LEU A CG  1 
ATOM   1312 C CD1 . LEU A 1 190 ? 24.383 30.540 9.203   1.000 37.150  0 190 LEU A CD1 1 
ATOM   1313 C CD2 . LEU A 1 190 ? 26.541 31.361 10.189  1.000 32.659  0 190 LEU A CD2 1 
ATOM   1314 N N   . ARG A 1 191 ? 24.901 35.082 7.762   1.000 32.011  0 191 ARG A N   1 
ATOM   1315 C CA  . ARG A 1 191 ? 24.320 36.253 8.400   1.000 29.234  0 191 ARG A CA  1 
ATOM   1316 C C   . ARG A 1 191 ? 22.990 36.652 7.748   1.000 31.448  0 191 ARG A C   1 
ATOM   1317 O O   . ARG A 1 191 ? 21.970 36.908 8.422   1.000 35.545  0 191 ARG A O   1 
ATOM   1318 C CB  . ARG A 1 191 ? 25.298 37.437 8.410   1.000 30.589  0 191 ARG A CB  1 
ATOM   1319 C CG  . ARG A 1 191 ? 24.779 38.638 9.198   1.000 32.131  0 191 ARG A CG  1 
ATOM   1320 C CD  . ARG A 1 191 ? 25.732 39.824 9.177   1.000 34.236  0 191 ARG A CD  1 
ATOM   1321 N NE  . ARG A 1 191 ? 25.937 40.314 7.807   1.000 33.657  0 191 ARG A NE  1 
ATOM   1322 C CZ  . ARG A 1 191 ? 27.016 40.204 7.021   1.000 34.124  0 191 ARG A CZ  1 
ATOM   1323 N NH1 . ARG A 1 191 ? 28.176 39.760 7.471   1.000 33.973  0 191 ARG A NH1 1 
ATOM   1324 N NH2 . ARG A 1 191 ? 26.942 40.587 5.764   1.000 36.245  0 191 ARG A NH2 1 
ATOM   1325 N N   . ARG A 1 192 ? 22.990 36.803 6.436   1.000 32.586  0 192 ARG A N   1 
ATOM   1326 C CA  . ARG A 1 192 ? 21.783 37.244 5.750   1.000 33.920  0 192 ARG A CA  1 
ATOM   1327 C C   . ARG A 1 192 ? 20.663 36.202 5.831   1.000 36.030  0 192 ARG A C   1 
ATOM   1328 O O   . ARG A 1 192 ? 19.486 36.547 5.927   1.000 36.491  0 192 ARG A O   1 
ATOM   1329 C CB  . ARG A 1 192 ? 22.113 37.676 4.311   1.000 34.997  0 192 ARG A CB  1 
ATOM   1330 C CG  . ARG A 1 192 ? 22.724 39.078 4.350   1.000 33.784  0 192 ARG A CG  1 
ATOM   1331 C CD  . ARG A 1 192 ? 22.912 39.692 2.984   1.000 34.579  0 192 ARG A CD  1 
ATOM   1332 N NE  . ARG A 1 192 ? 24.087 39.211 2.267   1.000 36.395  0 192 ARG A NE  1 
ATOM   1333 C CZ  . ARG A 1 192 ? 25.266 39.780 2.146   1.000 33.776  0 192 ARG A CZ  1 
ATOM   1334 N NH1 . ARG A 1 192 ? 25.573 40.882 2.779   1.000 35.419  0 192 ARG A NH1 1 
ATOM   1335 N NH2 . ARG A 1 192 ? 26.148 39.277 1.296   1.000 38.260  0 192 ARG A NH2 1 
ATOM   1336 N N   . ASP A 1 193 ? 21.007 34.922 5.815   1.000 33.591  0 193 ASP A N   1 
ATOM   1337 C CA  . ASP A 1 193 ? 20.018 33.870 6.009   1.000 33.166  0 193 ASP A CA  1 
ATOM   1338 C C   . ASP A 1 193 ? 19.399 33.939 7.404   1.000 36.391  0 193 ASP A C   1 
ATOM   1339 O O   . ASP A 1 193 ? 18.216 33.611 7.576   1.000 38.407  0 193 ASP A O   1 
ATOM   1340 C CB  . ASP A 1 193 ? 20.613 32.509 5.615   1.000 35.929  0 193 ASP A CB  1 
ATOM   1341 C CG  . ASP A 1 193 ? 20.731 32.258 4.105   1.000 42.825  0 193 ASP A CG  1 
ATOM   1342 O OD1 . ASP A 1 193 ? 20.074 33.000 3.338   1.000 41.467  0 193 ASP A OD1 1 
ATOM   1343 O OD2 . ASP A 1 193 ? 21.456 31.321 3.676   1.000 39.091  0 193 ASP A OD2 1 
ATOM   1344 N N   . MET A 1 194 ? 20.185 34.327 8.406   1.000 35.300  0 194 MET A N   1 
ATOM   1345 C CA  . MET A 1 194 ? 19.755 34.207 9.794   1.000 38.181  0 194 MET A CA  1 
ATOM   1346 C C   . MET A 1 194 ? 19.087 35.468 10.340  1.000 35.597  0 194 MET A C   1 
ATOM   1347 O O   . MET A 1 194 ? 18.480 35.409 11.407  1.000 35.445  0 194 MET A O   1 
ATOM   1348 C CB  . MET A 1 194 ? 20.951 33.891 10.686  1.000 35.476  0 194 MET A CB  1 
ATOM   1349 C CG  . MET A 1 194 ? 21.408 32.472 10.615  1.000 40.567  0 194 MET A CG  1 
ATOM   1350 S SD  . MET A 1 194 ? 20.114 31.266 11.016  1.000 41.506  0 194 MET A SD  1 
ATOM   1351 C CE  . MET A 1 194 ? 19.601 30.664 9.411   1.000 41.783  0 194 MET A CE  1 
ATOM   1352 N N   . LYS A 1 195 ? 19.144 36.579 9.594   1.000 36.952  0 195 LYS A N   1 
ATOM   1353 C CA  . LYS A 1 195 ? 18.521 37.834 10.006  1.000 36.851  0 195 LYS A CA  1 
ATOM   1354 C C   . LYS A 1 195 ? 17.032 37.635 10.356  1.000 38.405  0 195 LYS A C   1 
ATOM   1355 O O   . LYS A 1 195 ? 16.583 38.114 11.394  1.000 38.787  0 195 LYS A O   1 
ATOM   1356 C CB  . LYS A 1 195 ? 18.692 38.883 8.898   1.000 45.905  0 195 LYS A CB  1 
ATOM   1357 C CG  . LYS A 1 195 ? 18.822 40.330 9.401   1.000 60.621  0 195 LYS A CG  1 
ATOM   1358 C CD  . LYS A 1 195 ? 17.659 40.979 10.144  1.000 78.128  0 195 LYS A CD  1 
ATOM   1359 C CE  . LYS A 1 195 ? 16.620 41.637 9.256   1.000 95.185  0 195 LYS A CE  1 
ATOM   1360 N NZ  . LYS A 1 195 ? 15.786 40.689 8.506   1.000 97.689  0 195 LYS A NZ  1 
ATOM   1361 N N   . ALA A 1 196 ? 16.306 36.853 9.544   1.000 39.707  0 196 ALA A N   1 
ATOM   1362 C CA  . ALA A 1 196 ? 14.874 36.600 9.727   1.000 44.210  0 196 ALA A CA  1 
ATOM   1363 C C   . ALA A 1 196 ? 14.574 35.909 11.061  1.000 42.967  0 196 ALA A C   1 
ATOM   1364 O O   . ALA A 1 196 ? 13.473 36.024 11.607  1.000 40.216  0 196 ALA A O   1 
ATOM   1365 C CB  . ALA A 1 196 ? 14.362 35.771 8.570   1.000 45.821  0 196 ALA A CB  1 
ATOM   1366 N N   . PHE A 1 197 ? 15.556 35.196 11.611  1.000 36.556  0 197 PHE A N   1 
ATOM   1367 C CA  . PHE A 1 197 ? 15.359 34.498 12.867  1.000 35.768  0 197 PHE A CA  1 
ATOM   1368 C C   . PHE A 1 197 ? 15.905 35.261 14.057  1.000 36.340  0 197 PHE A C   1 
ATOM   1369 O O   . PHE A 1 197 ? 15.905 34.745 15.166  1.000 38.568  0 197 PHE A O   1 
ATOM   1370 C CB  . PHE A 1 197 ? 16.093 33.173 12.813  1.000 35.922  0 197 PHE A CB  1 
ATOM   1371 C CG  . PHE A 1 197 ? 15.472 32.245 11.801  1.000 35.928  0 197 PHE A CG  1 
ATOM   1372 C CD1 . PHE A 1 197 ? 14.225 31.674 12.042  1.000 34.999  0 197 PHE A CD1 1 
ATOM   1373 C CD2 . PHE A 1 197 ? 16.108 31.985 10.601  1.000 35.305  0 197 PHE A CD2 1 
ATOM   1374 C CE1 . PHE A 1 197 ? 13.654 30.836 11.115  1.000 36.843  0 197 PHE A CE1 1 
ATOM   1375 C CE2 . PHE A 1 197 ? 15.530 31.129 9.681   1.000 37.829  0 197 PHE A CE2 1 
ATOM   1376 C CZ  . PHE A 1 197 ? 14.310 30.558 9.939   1.000 37.704  0 197 PHE A CZ  1 
ATOM   1377 N N   . GLY A 1 198 ? 16.378 36.491 13.850  1.000 38.841  0 198 GLY A N   1 
ATOM   1378 C CA  . GLY A 1 198 ? 16.915 37.268 14.955  1.000 36.430  0 198 GLY A CA  1 
ATOM   1379 C C   . GLY A 1 198 ? 18.262 36.730 15.473  1.000 40.830  0 198 GLY A C   1 
ATOM   1380 O O   . GLY A 1 198 ? 18.698 37.116 16.554  1.000 38.980  0 198 GLY A O   1 
ATOM   1381 N N   . VAL A 1 199 ? 18.943 35.855 14.713  1.000 35.248  0 199 VAL A N   1 
ATOM   1382 C CA  . VAL A 1 199 ? 20.277 35.387 15.078  1.000 36.062  0 199 VAL A CA  1 
ATOM   1383 C C   . VAL A 1 199 ? 21.330 36.341 14.521  1.000 36.015  0 199 VAL A C   1 
ATOM   1384 O O   . VAL A 1 199 ? 21.288 36.617 13.332  1.000 40.925  0 199 VAL A O   1 
ATOM   1385 C CB  . VAL A 1 199 ? 20.456 33.972 14.494  1.000 32.936  0 199 VAL A CB  1 
ATOM   1386 C CG1 . VAL A 1 199 ? 21.900 33.482 14.534  1.000 37.555  0 199 VAL A CG1 1 
ATOM   1387 C CG2 . VAL A 1 199 ? 19.521 32.998 15.187  1.000 34.926  0 199 VAL A CG2 1 
ATOM   1388 N N   . HIS A 1 200 ? 22.305 36.749 15.350  1.000 33.803  0 200 HIS A N   1 
ATOM   1389 C CA  A HIS A 1 200 ? 23.371 37.639 14.941  0.500 34.452  0 200 HIS A CA  1 
ATOM   1390 C CA  B HIS A 1 200 ? 23.369 37.641 14.921  0.500 34.966  0 200 HIS A CA  1 
ATOM   1391 C C   . HIS A 1 200 ? 24.590 36.789 14.586  1.000 38.315  0 200 HIS A C   1 
ATOM   1392 O O   . HIS A 1 200 ? 24.835 35.728 15.206  1.000 35.699  0 200 HIS A O   1 
ATOM   1393 C CB  A HIS A 1 200 ? 23.579 38.725 16.004  0.500 38.182  0 200 HIS A CB  1 
ATOM   1394 C CB  B HIS A 1 200 ? 23.642 38.776 15.925  0.500 39.565  0 200 HIS A CB  1 
ATOM   1395 C CG  A HIS A 1 200 ? 22.417 39.660 16.105  0.500 39.668  0 200 HIS A CG  1 
ATOM   1396 C CG  B HIS A 1 200 ? 24.497 39.889 15.368  0.500 41.747  0 200 HIS A CG  1 
ATOM   1397 N ND1 A HIS A 1 200 ? 21.333 39.415 16.926  0.500 40.004  0 200 HIS A ND1 1 
ATOM   1398 N ND1 B HIS A 1 200 ? 23.991 41.041 14.791  0.500 46.291  0 200 HIS A ND1 1 
ATOM   1399 C CD2 A HIS A 1 200 ? 22.144 40.817 15.457  0.500 41.827  0 200 HIS A CD2 1 
ATOM   1400 C CD2 B HIS A 1 200 ? 25.840 40.021 15.309  0.500 40.227  0 200 HIS A CD2 1 
ATOM   1401 C CE1 A HIS A 1 200 ? 20.450 40.389 16.772  0.500 40.691  0 200 HIS A CE1 1 
ATOM   1402 C CE1 B HIS A 1 200 ? 24.994 41.819 14.374  0.500 37.377  0 200 HIS A CE1 1 
ATOM   1403 N NE2 A HIS A 1 200 ? 20.919 41.242 15.891  0.500 38.200  0 200 HIS A NE2 1 
ATOM   1404 N NE2 B HIS A 1 200 ? 26.124 41.207 14.673  0.500 43.423  0 200 HIS A NE2 1 
ATOM   1405 N N   . VAL A 1 201 ? 25.334 37.235 13.577  1.000 31.523  0 201 VAL A N   1 
ATOM   1406 C CA  . VAL A 1 201 ? 26.532 36.532 13.116  1.000 32.657  0 201 VAL A CA  1 
ATOM   1407 C C   . VAL A 1 201 ? 27.636 37.567 13.068  1.000 32.497  0 201 VAL A C   1 
ATOM   1408 O O   . VAL A 1 201 ? 27.464 38.604 12.415  1.000 32.249  0 201 VAL A O   1 
ATOM   1409 C CB  . VAL A 1 201 ? 26.336 35.874 11.736  1.000 33.108  0 201 VAL A CB  1 
ATOM   1410 C CG1 . VAL A 1 201 ? 27.616 35.218 11.231  1.000 33.849  0 201 VAL A CG1 1 
ATOM   1411 C CG2 . VAL A 1 201 ? 25.164 34.925 11.734  1.000 31.113  0 201 VAL A CG2 1 
ATOM   1412 N N   . SER A 1 202 ? 28.746 37.262 13.744  1.000 31.453  0 202 SER A N   1 
ATOM   1413 C CA  . SER A 1 202 ? 29.906 38.124 13.841  1.000 32.010  0 202 SER A CA  1 
ATOM   1414 C C   . SER A 1 202 ? 31.126 37.395 13.330  1.000 34.797  0 202 SER A C   1 
ATOM   1415 O O   . SER A 1 202 ? 31.351 36.227 13.617  1.000 32.749  0 202 SER A O   1 
ATOM   1416 C CB  . SER A 1 202 ? 30.182 38.584 15.262  1.000 34.671  0 202 SER A CB  1 
ATOM   1417 O OG  . SER A 1 202 ? 29.053 39.234 15.816  1.000 36.114  0 202 SER A OG  1 
ATOM   1418 N N   . CYS A 1 203 ? 31.910 38.117 12.551  1.000 30.933  0 203 CYS A N   1 
ATOM   1419 C CA  . CYS A 1 203 ? 33.163 37.604 12.049  1.000 31.394  0 203 CYS A CA  1 
ATOM   1420 C C   . CYS A 1 203 ? 34.331 38.319 12.734  1.000 37.835  0 203 CYS A C   1 
ATOM   1421 O O   . CYS A 1 203 ? 34.377 39.554 12.761  1.000 36.652  0 203 CYS A O   1 
ATOM   1422 C CB  . CYS A 1 203 ? 33.134 37.810 10.550  1.000 34.918  0 203 CYS A CB  1 
ATOM   1423 S SG  . CYS A 1 203 ? 34.650 37.212 9.750   1.000 40.918  0 203 CYS A SG  1 
ATOM   1424 N N   . ILE A 1 204 ? 35.274 37.567 13.316  1.000 30.880  0 204 ILE A N   1 
ATOM   1425 C CA  . ILE A 1 204 ? 36.440 38.175 13.960  1.000 31.922  0 204 ILE A CA  1 
ATOM   1426 C C   . ILE A 1 204 ? 37.684 37.977 13.093  1.000 36.577  0 204 ILE A C   1 
ATOM   1427 O O   . ILE A 1 204 ? 37.971 36.858 12.679  1.000 31.645  0 204 ILE A O   1 
ATOM   1428 C CB  . ILE A 1 204 ? 36.645 37.616 15.375  1.000 37.130  0 204 ILE A CB  1 
ATOM   1429 C CG1 . ILE A 1 204 ? 35.350 37.794 16.187  1.000 38.048  0 204 ILE A CG1 1 
ATOM   1430 C CG2 . ILE A 1 204 ? 37.877 38.252 16.049  1.000 38.499  0 204 ILE A CG2 1 
ATOM   1431 C CD1 . ILE A 1 204 ? 35.417 37.285 17.607  1.000 44.187  0 204 ILE A CD1 1 
ATOM   1432 N N   . GLU A 1 205 ? 38.403 39.078 12.793  1.000 31.848  0 205 GLU A N   1 
ATOM   1433 C CA  . GLU A 1 205 ? 39.587 39.011 11.931  1.000 35.051  0 205 GLU A CA  1 
ATOM   1434 C C   . GLU A 1 205 ? 40.811 39.413 12.761  1.000 37.735  0 205 GLU A C   1 
ATOM   1435 O O   . GLU A 1 205 ? 41.102 40.594 12.909  1.000 34.082  0 205 GLU A O   1 
ATOM   1436 C CB  . GLU A 1 205 ? 39.436 39.925 10.711  1.000 36.185  0 205 GLU A CB  1 
ATOM   1437 C CG  . GLU A 1 205 ? 38.322 39.453 9.774   1.000 39.212  0 205 GLU A CG  1 
ATOM   1438 C CD  . GLU A 1 205 ? 37.654 40.546 8.942   1.000 44.114  0 205 GLU A CD  1 
ATOM   1439 O OE1 . GLU A 1 205 ? 37.848 41.736 9.266   1.000 43.379  0 205 GLU A OE1 1 
ATOM   1440 O OE2 . GLU A 1 205 ? 37.004 40.214 7.923   1.000 39.827  0 205 GLU A OE2 1 
ATOM   1441 N N   . PRO A 1 206 ? 41.527 38.481 13.413  1.000 31.246  0 206 PRO A N   1 
ATOM   1442 C CA  . PRO A 1 206 ? 42.763 38.841 14.113  1.000 33.363  0 206 PRO A CA  1 
ATOM   1443 C C   . PRO A 1 206 ? 43.925 39.058 13.170  1.000 37.438  0 206 PRO A C   1 
ATOM   1444 O O   . PRO A 1 206 ? 44.017 38.372 12.140  1.000 35.734  0 206 PRO A O   1 
ATOM   1445 C CB  . PRO A 1 206 ? 42.988 37.625 15.013  1.000 32.530  0 206 PRO A CB  1 
ATOM   1446 C CG  . PRO A 1 206 ? 41.677 36.869 14.978  1.000 35.307  0 206 PRO A CG  1 
ATOM   1447 C CD  . PRO A 1 206 ? 41.187 37.050 13.586  1.000 32.048  0 206 PRO A CD  1 
ATOM   1448 N N   . GLY A 1 207 ? 44.818 39.988 13.549  1.000 35.606  0 207 GLY A N   1 
ATOM   1449 C CA  . GLY A 1 207 ? 46.170 39.963 13.032  1.000 34.817  0 207 GLY A CA  1 
ATOM   1450 C C   . GLY A 1 207 ? 46.965 38.820 13.663  1.000 42.467  0 207 GLY A C   1 
ATOM   1451 O O   . GLY A 1 207 ? 46.375 37.886 14.197  1.000 37.506  0 207 GLY A O   1 
ATOM   1452 N N   . LEU A 1 208 ? 48.300 38.932 13.695  1.000 40.994  0 208 LEU A N   1 
ATOM   1453 C CA  . LEU A 1 208 ? 49.150 37.837 14.166  1.000 42.564  0 208 LEU A CA  1 
ATOM   1454 C C   . LEU A 1 208 ? 49.233 37.796 15.685  1.000 39.736  0 208 LEU A C   1 
ATOM   1455 O O   . LEU A 1 208 ? 49.523 38.796 16.324  1.000 39.131  0 208 LEU A O   1 
ATOM   1456 C CB  . LEU A 1 208 ? 50.553 37.982 13.578  1.000 47.181  0 208 LEU A CB  1 
ATOM   1457 C CG  . LEU A 1 208 ? 50.620 37.937 12.050  1.000 58.593  0 208 LEU A CG  1 
ATOM   1458 C CD1 . LEU A 1 208 ? 52.047 38.134 11.518  1.000 59.802  0 208 LEU A CD1 1 
ATOM   1459 C CD2 . LEU A 1 208 ? 50.012 36.622 11.552  1.000 61.615  0 208 LEU A CD2 1 
ATOM   1460 N N   . PHE A 1 209 ? 49.027 36.609 16.273  1.000 35.500  0 209 PHE A N   1 
ATOM   1461 C CA  . PHE A 1 209 ? 49.016 36.433 17.714  1.000 32.906  0 209 PHE A CA  1 
ATOM   1462 C C   . PHE A 1 209 ? 49.797 35.174 18.051  1.000 39.063  0 209 PHE A C   1 
ATOM   1463 O O   . PHE A 1 209 ? 49.759 34.210 17.284  1.000 37.625  0 209 PHE A O   1 
ATOM   1464 C CB  . PHE A 1 209 ? 47.627 36.250 18.327  1.000 36.836  0 209 PHE A CB  1 
ATOM   1465 C CG  . PHE A 1 209 ? 46.883 37.556 18.445  1.000 35.543  0 209 PHE A CG  1 
ATOM   1466 C CD1 . PHE A 1 209 ? 46.218 38.086 17.354  1.000 34.482  0 209 PHE A CD1 1 
ATOM   1467 C CD2 . PHE A 1 209 ? 46.903 38.270 19.631  1.000 37.642  0 209 PHE A CD2 1 
ATOM   1468 C CE1 . PHE A 1 209 ? 45.628 39.334 17.428  1.000 35.885  0 209 PHE A CE1 1 
ATOM   1469 C CE2 . PHE A 1 209 ? 46.280 39.502 19.715  1.000 39.765  0 209 PHE A CE2 1 
ATOM   1470 C CZ  . PHE A 1 209 ? 45.625 40.024 18.621  1.000 41.338  0 209 PHE A CZ  1 
ATOM   1471 N N   . LYS A 1 210 ? 50.530 35.224 19.170  1.000 41.209  0 210 LYS A N   1 
ATOM   1472 C CA  . LYS A 1 210 ? 51.359 34.112 19.614  1.000 43.330  0 210 LYS A CA  1 
ATOM   1473 C C   . LYS A 1 210 ? 50.496 33.002 20.202  1.000 40.499  0 210 LYS A C   1 
ATOM   1474 O O   . LYS A 1 210 ? 50.009 33.130 21.319  1.000 40.421  0 210 LYS A O   1 
ATOM   1475 C CB  . LYS A 1 210 ? 52.326 34.587 20.716  1.000 57.026  0 210 LYS A CB  1 
ATOM   1476 C CG  . LYS A 1 210 ? 53.208 33.485 21.332  1.000 57.055  0 210 LYS A CG  1 
ATOM   1477 C CD  . LYS A 1 210 ? 54.185 32.887 20.329  1.000 57.010  0 210 LYS A CD  1 
ATOM   1478 C CE  . LYS A 1 210 ? 55.026 31.794 20.949  1.000 65.133  0 210 LYS A CE  1 
ATOM   1479 N NZ  . LYS A 1 210 ? 54.326 30.511 20.831  1.000 65.868  0 210 LYS A NZ  1 
ATOM   1480 N N   . THR A 1 211 ? 50.267 31.931 19.422  1.000 42.784  0 211 THR A N   1 
ATOM   1481 C CA  . THR A 1 211 ? 49.441 30.802 19.852  1.000 40.578  0 211 THR A CA  1 
ATOM   1482 C C   . THR A 1 211 ? 50.199 29.558 19.393  1.000 40.228  0 211 THR A C   1 
ATOM   1483 O O   . THR A 1 211 ? 51.363 29.657 19.044  1.000 43.361  0 211 THR A O   1 
ATOM   1484 C CB  . THR A 1 211 ? 48.028 30.867 19.241  1.000 37.215  0 211 THR A CB  1 
ATOM   1485 O OG1 . THR A 1 211 ? 48.254 30.783 17.837  1.000 35.086  0 211 THR A OG1 1 
ATOM   1486 C CG2 . THR A 1 211 ? 47.265 32.139 19.565  1.000 38.480  0 211 THR A CG2 1 
ATOM   1487 N N   . GLU A 1 212 ? 49.523 28.420 19.268  1.000 41.021  0 212 GLU A N   1 
ATOM   1488 C CA  . GLU A 1 212 ? 50.154 27.237 18.703  1.000 37.214  0 212 GLU A CA  1 
ATOM   1489 C C   . GLU A 1 212 ? 49.870 27.127 17.213  1.000 39.775  0 212 GLU A C   1 
ATOM   1490 O O   . GLU A 1 212 ? 50.244 26.138 16.622  1.000 37.587  0 212 GLU A O   1 
ATOM   1491 C CB  . GLU A 1 212 ? 49.661 25.985 19.447  1.000 39.379  0 212 GLU A CB  1 
ATOM   1492 C CG  . GLU A 1 212 ? 50.064 25.993 20.925  1.000 41.996  0 212 GLU A CG  1 
ATOM   1493 C CD  . GLU A 1 212 ? 51.571 26.212 21.150  1.000 52.059  0 212 GLU A CD  1 
ATOM   1494 O OE1 . GLU A 1 212 ? 52.292 25.366 20.583  1.000 50.570  0 212 GLU A OE1 1 
ATOM   1495 O OE2 . GLU A 1 212 ? 52.041 27.148 21.862  1.000 56.220  0 212 GLU A OE2 1 
ATOM   1496 N N   . LEU A 1 213 ? 49.213 28.117 16.599  1.000 35.656  0 213 LEU A N   1 
ATOM   1497 C CA  . LEU A 1 213 ? 48.822 27.975 15.209  1.000 34.968  0 213 LEU A CA  1 
ATOM   1498 C C   . LEU A 1 213 ? 50.058 27.884 14.296  1.000 40.206  0 213 LEU A C   1 
ATOM   1499 O O   . LEU A 1 213 ? 50.140 27.039 13.422  1.000 37.510  0 213 LEU A O   1 
ATOM   1500 C CB  . LEU A 1 213 ? 47.967 29.166 14.759  1.000 35.519  0 213 LEU A CB  1 
ATOM   1501 C CG  . LEU A 1 213 ? 47.493 29.080 13.299  1.000 38.471  0 213 LEU A CG  1 
ATOM   1502 C CD1 . LEU A 1 213 ? 46.310 28.151 13.153  1.000 40.578  0 213 LEU A CD1 1 
ATOM   1503 C CD2 . LEU A 1 213 ? 47.148 30.452 12.759  1.000 39.524  0 213 LEU A CD2 1 
ATOM   1504 N N   . ALA A 1 214 ? 50.931 28.871 14.428  1.000 37.297  0 214 ALA A N   1 
ATOM   1505 C CA  . ALA A 1 214 ? 52.047 29.118 13.543  1.000 47.834  0 214 ALA A CA  1 
ATOM   1506 C C   . ALA A 1 214 ? 53.290 29.140 14.416  1.000 50.153  0 214 ALA A C   1 
ATOM   1507 O O   . ALA A 1 214 ? 53.320 29.643 15.542  1.000 55.970  0 214 ALA A O   1 
ATOM   1508 C CB  . ALA A 1 214 ? 51.872 30.455 12.851  1.000 53.414  0 214 ALA A CB  1 
ATOM   1509 N N   . ASP A 1 215 ? 54.320 28.564 13.881  1.000 54.771  0 215 ASP A N   1 
ATOM   1510 C CA  . ASP A 1 215 ? 55.531 28.386 14.633  1.000 59.549  0 215 ASP A CA  1 
ATOM   1511 C C   . ASP A 1 215 ? 56.554 28.303 13.516  1.000 47.213  0 215 ASP A C   1 
ATOM   1512 O O   . ASP A 1 215 ? 56.479 27.369 12.719  1.000 49.800  0 215 ASP A O   1 
ATOM   1513 C CB  . ASP A 1 215 ? 55.286 27.214 15.577  1.000 64.684  0 215 ASP A CB  1 
ATOM   1514 C CG  . ASP A 1 215 ? 56.508 26.502 16.126  1.000 69.489  0 215 ASP A CG  1 
ATOM   1515 O OD1 . ASP A 1 215 ? 57.615 26.833 15.658  1.000 60.071  0 215 ASP A OD1 1 
ATOM   1516 O OD2 . ASP A 1 215 ? 56.313 25.606 16.991  1.000 73.863  0 215 ASP A OD2 1 
ATOM   1517 N N   . PRO A 1 216 ? 57.473 29.278 13.398  1.000 49.111  0 216 PRO A N   1 
ATOM   1518 C CA  . PRO A 1 216 ? 58.409 29.322 12.280  1.000 53.119  0 216 PRO A CA  1 
ATOM   1519 C C   . PRO A 1 216 ? 59.163 28.018 12.106  1.000 51.789  0 216 PRO A C   1 
ATOM   1520 O O   . PRO A 1 216 ? 59.418 27.614 10.975  1.000 48.818  0 216 PRO A O   1 
ATOM   1521 C CB  . PRO A 1 216 ? 59.348 30.462 12.657  1.000 57.640  0 216 PRO A CB  1 
ATOM   1522 C CG  . PRO A 1 216 ? 58.485 31.355 13.508  1.000 60.273  0 216 PRO A CG  1 
ATOM   1523 C CD  . PRO A 1 216 ? 57.677 30.391 14.337  1.000 56.691  0 216 PRO A CD  1 
ATOM   1524 N N   . ILE A 1 217 ? 59.514 27.366 13.229  1.000 53.411  0 217 ILE A N   1 
ATOM   1525 C CA  . ILE A 1 217 ? 60.282 26.130 13.149  1.000 50.627  0 217 ILE A CA  1 
ATOM   1526 C C   . ILE A 1 217 ? 59.425 25.050 12.524  1.000 45.757  0 217 ILE A C   1 
ATOM   1527 O O   . ILE A 1 217 ? 59.927 24.244 11.736  1.000 46.188  0 217 ILE A O   1 
ATOM   1528 C CB  . ILE A 1 217 ? 60.863 25.657 14.507  1.000 55.078  0 217 ILE A CB  1 
ATOM   1529 C CG1 . ILE A 1 217 ? 61.974 26.578 15.055  1.000 57.324  0 217 ILE A CG1 1 
ATOM   1530 C CG2 . ILE A 1 217 ? 61.355 24.209 14.411  1.000 53.228  0 217 ILE A CG2 1 
ATOM   1531 C CD1 . ILE A 1 217 ? 63.221 26.688 14.187  1.000 66.102  0 217 ILE A CD1 1 
ATOM   1532 N N   . LYS A 1 218 ? 58.145 24.972 12.914  1.000 43.119  0 218 LYS A N   1 
ATOM   1533 C CA  . LYS A 1 218 ? 57.289 23.924 12.363  1.000 49.094  0 218 LYS A CA  1 
ATOM   1534 C C   . LYS A 1 218 ? 57.031 24.196 10.864  1.000 40.307  0 218 LYS A C   1 
ATOM   1535 O O   . LYS A 1 218 ? 56.951 23.260 10.066  1.000 46.505  0 218 LYS A O   1 
ATOM   1536 C CB  . LYS A 1 218 ? 55.995 23.895 13.178  1.000 57.512  0 218 LYS A CB  1 
ATOM   1537 C CG  . LYS A 1 218 ? 55.306 22.571 13.460  1.000 68.389  0 218 LYS A CG  1 
ATOM   1538 C CD  . LYS A 1 218 ? 54.949 22.567 14.951  1.000 82.280  0 218 LYS A CD  1 
ATOM   1539 C CE  . LYS A 1 218 ? 53.523 22.292 15.296  1.000 88.171  0 218 LYS A CE  1 
ATOM   1540 N NZ  . LYS A 1 218 ? 53.089 21.022 14.715  1.000 99.010  0 218 LYS A NZ  1 
ATOM   1541 N N   . THR A 1 219 ? 56.855 25.479 10.516  1.000 42.619  0 219 THR A N   1 
ATOM   1542 C CA  . THR A 1 219 ? 56.642 25.895 9.133   1.000 47.553  0 219 THR A CA  1 
ATOM   1543 C C   . THR A 1 219 ? 57.870 25.502 8.301   1.000 52.757  0 219 THR A C   1 
ATOM   1544 O O   . THR A 1 219 ? 57.723 24.848 7.264   1.000 49.204  0 219 THR A O   1 
ATOM   1545 C CB  . THR A 1 219 ? 56.320 27.392 9.085   1.000 47.931  0 219 THR A CB  1 
ATOM   1546 O OG1 . THR A 1 219 ? 54.960 27.426 9.504   1.000 45.828  0 219 THR A OG1 1 
ATOM   1547 C CG2 . THR A 1 219 ? 56.369 27.989 7.686   1.000 52.462  0 219 THR A CG2 1 
ATOM   1548 N N   . THR A 1 220 ? 59.084 25.796 8.804   1.000 48.451  0 220 THR A N   1 
ATOM   1549 C CA  . THR A 1 220 ? 60.324 25.392 8.133   1.000 44.789  0 220 THR A CA  1 
ATOM   1550 C C   . THR A 1 220 ? 60.414 23.870 7.986   1.000 46.693  0 220 THR A C   1 
ATOM   1551 O O   . THR A 1 220 ? 60.787 23.366 6.922   1.000 45.881  0 220 THR A O   1 
ATOM   1552 C CB  . THR A 1 220 ? 61.533 25.955 8.878   1.000 47.342  0 220 THR A CB  1 
ATOM   1553 O OG1 . THR A 1 220 ? 61.409 27.372 8.834   1.000 45.052  0 220 THR A OG1 1 
ATOM   1554 C CG2 . THR A 1 220 ? 62.837 25.608 8.191   1.000 54.803  0 220 THR A CG2 1 
ATOM   1555 N N   . GLU A 1 221 ? 60.042 23.102 9.011   1.000 44.729  0 221 GLU A N   1 
ATOM   1556 C CA  . GLU A 1 221 ? 60.064 21.649 8.905   1.000 48.141  0 221 GLU A CA  1 
ATOM   1557 C C   . GLU A 1 221 ? 59.191 21.166 7.754   1.000 50.976  0 221 GLU A C   1 
ATOM   1558 O O   . GLU A 1 221 ? 59.570 20.234 7.036   1.000 48.157  0 221 GLU A O   1 
ATOM   1559 C CB  . GLU A 1 221 ? 59.557 20.888 10.137  1.000 63.780  0 221 GLU A CB  1 
ATOM   1560 C CG  . GLU A 1 221 ? 60.581 20.749 11.265  1.000 80.292  0 221 GLU A CG  1 
ATOM   1561 C CD  . GLU A 1 221 ? 59.969 20.549 12.661  1.000 102.075 0 221 GLU A CD  1 
ATOM   1562 O OE1 . GLU A 1 221 ? 60.344 21.320 13.584  1.000 113.815 0 221 GLU A OE1 1 
ATOM   1563 O OE2 . GLU A 1 221 ? 59.105 19.652 12.848  1.000 84.593  0 221 GLU A OE2 1 
ATOM   1564 N N   . LYS A 1 222 ? 57.992 21.745 7.600   1.000 44.526  0 222 LYS A N   1 
ATOM   1565 C CA  . LYS A 1 222 ? 57.136 21.290 6.513   1.000 46.710  0 222 LYS A CA  1 
ATOM   1566 C C   . LYS A 1 222 ? 57.770 21.602 5.148   1.000 45.185  0 222 LYS A C   1 
ATOM   1567 O O   . LYS A 1 222 ? 57.680 20.794 4.228   1.000 50.556  0 222 LYS A O   1 
ATOM   1568 C CB  . LYS A 1 222 ? 55.732 21.857 6.724   1.000 54.322  0 222 LYS A CB  1 
ATOM   1569 C CG  . LYS A 1 222 ? 55.038 21.241 7.936   1.000 53.573  0 222 LYS A CG  1 
ATOM   1570 C CD  . LYS A 1 222 ? 53.590 21.690 8.097   1.000 57.110  0 222 LYS A CD  1 
ATOM   1571 C CE  . LYS A 1 222 ? 53.151 21.593 9.519   1.000 61.241  0 222 LYS A CE  1 
ATOM   1572 N NZ  . LYS A 1 222 ? 52.036 22.527 9.668   1.000 72.552  0 222 LYS A NZ  1 
ATOM   1573 N N   . LYS A 1 223 ? 58.396 22.764 5.003   1.000 45.585  0 223 LYS A N   1 
ATOM   1574 C CA  . LYS A 1 223 ? 59.057 23.124 3.750   1.000 45.665  0 223 LYS A CA  1 
ATOM   1575 C C   . LYS A 1 223 ? 60.201 22.164 3.398   1.000 51.765  0 223 LYS A C   1 
ATOM   1576 O O   . LYS A 1 223 ? 60.354 21.781 2.234   1.000 48.999  0 223 LYS A O   1 
ATOM   1577 C CB  . LYS A 1 223 ? 59.535 24.568 3.828   1.000 44.816  0 223 LYS A CB  1 
ATOM   1578 C CG  . LYS A 1 223 ? 58.389 25.547 3.646   1.000 48.525  0 223 LYS A CG  1 
ATOM   1579 C CD  . LYS A 1 223 ? 58.516 26.877 4.352   1.000 54.898  0 223 LYS A CD  1 
ATOM   1580 C CE  . LYS A 1 223 ? 59.364 27.867 3.695   1.000 61.994  0 223 LYS A CE  1 
ATOM   1581 N NZ  . LYS A 1 223 ? 59.021 29.125 4.362   1.000 61.746  0 223 LYS A NZ  1 
ATOM   1582 N N   . LEU A 1 224 ? 60.981 21.737 4.403   1.000 51.127  0 224 LEU A N   1 
ATOM   1583 C CA  . LEU A 1 224 ? 62.074 20.797 4.187   1.000 48.791  0 224 LEU A CA  1 
ATOM   1584 C C   . LEU A 1 224 ? 61.548 19.446 3.730   1.000 48.095  0 224 LEU A C   1 
ATOM   1585 O O   . LEU A 1 224 ? 62.149 18.797 2.883   1.000 56.930  0 224 LEU A O   1 
ATOM   1586 C CB  . LEU A 1 224 ? 62.867 20.654 5.480   1.000 52.909  0 224 LEU A CB  1 
ATOM   1587 C CG  . LEU A 1 224 ? 63.579 21.924 5.937   1.000 58.305  0 224 LEU A CG  1 
ATOM   1588 C CD1 . LEU A 1 224 ? 64.052 21.692 7.373   1.000 66.818  0 224 LEU A CD1 1 
ATOM   1589 C CD2 . LEU A 1 224 ? 64.736 22.284 5.000   1.000 55.379  0 224 LEU A CD2 1 
ATOM   1590 N N   . ALA A 1 225 ? 60.429 19.001 4.285   1.000 50.951  0 225 ALA A N   1 
ATOM   1591 C CA  . ALA A 1 225 ? 59.813 17.758 3.837   1.000 55.175  0 225 ALA A CA  1 
ATOM   1592 C C   . ALA A 1 225 ? 59.458 17.844 2.349   1.000 56.077  0 225 ALA A C   1 
ATOM   1593 O O   . ALA A 1 225 ? 59.615 16.884 1.605   1.000 57.027  0 225 ALA A O   1 
ATOM   1594 C CB  . ALA A 1 225 ? 58.564 17.477 4.650   1.000 61.821  0 225 ALA A CB  1 
ATOM   1595 N N   . ILE A 1 226 ? 58.922 19.000 1.938   1.000 52.273  0 226 ILE A N   1 
ATOM   1596 C CA  . ILE A 1 226 ? 58.498 19.184 0.565   1.000 52.146  0 226 ILE A CA  1 
ATOM   1597 C C   . ILE A 1 226 ? 59.722 19.240 -0.346  1.000 47.459  0 226 ILE A C   1 
ATOM   1598 O O   . ILE A 1 226 ? 59.682 18.653 -1.416  1.000 49.458  0 226 ILE A O   1 
ATOM   1599 C CB  . ILE A 1 226 ? 57.620 20.432 0.434   1.000 49.112  0 226 ILE A CB  1 
ATOM   1600 C CG1 . ILE A 1 226 ? 56.274 20.200 1.106   1.000 53.308  0 226 ILE A CG1 1 
ATOM   1601 C CG2 . ILE A 1 226 ? 57.450 20.832 -1.033  1.000 46.179  0 226 ILE A CG2 1 
ATOM   1602 C CD1 . ILE A 1 226 ? 55.426 21.448 1.142   1.000 55.397  0 226 ILE A CD1 1 
ATOM   1603 N N   . TRP A 1 227 ? 60.742 20.000 0.058   1.000 50.262  0 227 TRP A N   1 
ATOM   1604 C CA  . TRP A 1 227 ? 61.971 20.185 -0.701  1.000 54.236  0 227 TRP A CA  1 
ATOM   1605 C C   . TRP A 1 227 ? 62.569 18.843 -1.121  1.000 57.846  0 227 TRP A C   1 
ATOM   1606 O O   . TRP A 1 227 ? 62.974 18.681 -2.271  1.000 55.272  0 227 TRP A O   1 
ATOM   1607 C CB  . TRP A 1 227 ? 62.966 21.017 0.120   1.000 53.509  0 227 TRP A CB  1 
ATOM   1608 C CG  . TRP A 1 227 ? 64.173 21.480 -0.648  1.000 51.807  0 227 TRP A CG  1 
ATOM   1609 C CD1 . TRP A 1 227 ? 65.369 20.822 -0.750  1.000 53.962  0 227 TRP A CD1 1 
ATOM   1610 C CD2 . TRP A 1 227 ? 64.302 22.685 -1.438  1.000 47.751  0 227 TRP A CD2 1 
ATOM   1611 N NE1 . TRP A 1 227 ? 66.226 21.534 -1.545  1.000 59.742  0 227 TRP A NE1 1 
ATOM   1612 C CE2 . TRP A 1 227 ? 65.604 22.678 -1.983  1.000 52.930  0 227 TRP A CE2 1 
ATOM   1613 C CE3 . TRP A 1 227 ? 63.469 23.759 -1.740  1.000 45.756  0 227 TRP A CE3 1 
ATOM   1614 C CZ2 . TRP A 1 227 ? 66.070 23.701 -2.802  1.000 50.413  0 227 TRP A CZ2 1 
ATOM   1615 C CZ3 . TRP A 1 227 ? 63.937 24.778 -2.535  1.000 48.739  0 227 TRP A CZ3 1 
ATOM   1616 C CH2 . TRP A 1 227 ? 65.220 24.743 -3.074  1.000 48.645  0 227 TRP A CH2 1 
ATOM   1617 N N   . LYS A 1 228 ? 62.540 17.858 -0.224  1.000 57.523  0 228 LYS A N   1 
ATOM   1618 C CA  . LYS A 1 228 ? 63.150 16.569 -0.513  1.000 68.537  0 228 LYS A CA  1 
ATOM   1619 C C   . LYS A 1 228 ? 62.633 15.991 -1.822  1.000 67.840  0 228 LYS A C   1 
ATOM   1620 O O   . LYS A 1 228 ? 63.393 15.351 -2.533  1.000 77.603  0 228 LYS A O   1 
ATOM   1621 C CB  . LYS A 1 228 ? 62.972 15.557 0.623   1.000 78.781  0 228 LYS A CB  1 
ATOM   1622 C CG  . LYS A 1 228 ? 64.220 15.378 1.510   1.000 94.503  0 228 LYS A CG  1 
ATOM   1623 C CD  . LYS A 1 228 ? 64.008 15.194 3.014   1.000 103.130 0 228 LYS A CD  1 
ATOM   1624 C CE  . LYS A 1 228 ? 62.679 14.618 3.413   1.000 109.920 0 228 LYS A CE  1 
ATOM   1625 N NZ  . LYS A 1 228 ? 62.258 13.485 2.581   1.000 118.783 0 228 LYS A NZ  1 
ATOM   1626 N N   . HIS A 1 229 ? 61.358 16.204 -2.151  1.000 65.684  0 229 HIS A N   1 
ATOM   1627 C CA  . HIS A 1 229 ? 60.772 15.550 -3.313  1.000 66.174  0 229 HIS A CA  1 
ATOM   1628 C C   . HIS A 1 229 ? 60.427 16.554 -4.433  1.000 58.348  0 229 HIS A C   1 
ATOM   1629 O O   . HIS A 1 229 ? 59.727 16.190 -5.373  1.000 57.619  0 229 HIS A O   1 
ATOM   1630 C CB  . HIS A 1 229 ? 59.660 14.595 -2.845  1.000 73.057  0 229 HIS A CB  1 
ATOM   1631 C CG  . HIS A 1 229 ? 58.453 15.238 -2.227  1.000 91.752  0 229 HIS A CG  1 
ATOM   1632 N ND1 . HIS A 1 229 ? 57.849 16.393 -2.698  1.000 97.688  0 229 HIS A ND1 1 
ATOM   1633 C CD2 . HIS A 1 229 ? 57.716 14.845 -1.173  1.000 96.970  0 229 HIS A CD2 1 
ATOM   1634 C CE1 . HIS A 1 229 ? 56.795 16.690 -1.944  1.000 89.316  0 229 HIS A CE1 1 
ATOM   1635 N NE2 . HIS A 1 229 ? 56.696 15.764 -1.010  1.000 94.914  0 229 HIS A NE2 1 
ATOM   1636 N N   . LEU A 1 230 ? 60.924 17.809 -4.374  1.000 57.382  0 230 LEU A N   1 
ATOM   1637 C CA  . LEU A 1 230 ? 60.684 18.796 -5.429  1.000 49.785  0 230 LEU A CA  1 
ATOM   1638 C C   . LEU A 1 230 ? 61.474 18.443 -6.681  1.000 51.976  0 230 LEU A C   1 
ATOM   1639 O O   . LEU A 1 230 ? 62.618 18.018 -6.574  1.000 52.190  0 230 LEU A O   1 
ATOM   1640 C CB  . LEU A 1 230 ? 61.082 20.224 -5.073  1.000 45.750  0 230 LEU A CB  1 
ATOM   1641 C CG  . LEU A 1 230 ? 60.133 20.978 -4.144  1.000 47.445  0 230 LEU A CG  1 
ATOM   1642 C CD1 . LEU A 1 230 ? 60.756 22.325 -3.816  1.000 45.714  0 230 LEU A CD1 1 
ATOM   1643 C CD2 . LEU A 1 230 ? 58.771 21.110 -4.783  1.000 46.502  0 230 LEU A CD2 1 
ATOM   1644 N N   . SER A 1 231 ? 60.920 18.810 -7.843  1.000 48.629  0 231 SER A N   1 
ATOM   1645 C CA  . SER A 1 231 ? 61.623 18.647 -9.114  1.000 52.568  0 231 SER A CA  1 
ATOM   1646 C C   . SER A 1 231 ? 62.965 19.387 -9.137  1.000 50.310  0 231 SER A C   1 
ATOM   1647 O O   . SER A 1 231 ? 63.144 20.447 -8.526  1.000 45.169  0 231 SER A O   1 
ATOM   1648 C CB  . SER A 1 231 ? 60.762 19.067 -10.279 1.000 52.685  0 231 SER A CB  1 
ATOM   1649 O OG  . SER A 1 231 ? 60.844 20.468 -10.511 1.000 62.518  0 231 SER A OG  1 
ATOM   1650 N N   . PRO A 1 232 ? 63.971 18.861 -9.869  1.000 50.358  0 232 PRO A N   1 
ATOM   1651 C CA  . PRO A 1 232 ? 65.248 19.561 -10.022 1.000 49.151  0 232 PRO A CA  1 
ATOM   1652 C C   . PRO A 1 232 ? 65.169 21.024 -10.461 1.000 44.567  0 232 PRO A C   1 
ATOM   1653 O O   . PRO A 1 232 ? 65.951 21.857 -10.005 1.000 45.524  0 232 PRO A O   1 
ATOM   1654 C CB  . PRO A 1 232 ? 65.960 18.692 -11.100 1.000 55.574  0 232 PRO A CB  1 
ATOM   1655 C CG  . PRO A 1 232 ? 65.449 17.305 -10.827 1.000 58.171  0 232 PRO A CG  1 
ATOM   1656 C CD  . PRO A 1 232 ? 63.975 17.520 -10.488 1.000 56.749  0 232 PRO A CD  1 
ATOM   1657 N N   . ASP A 1 233 ? 64.232 21.329 -11.358 1.000 44.096  0 233 ASP A N   1 
ATOM   1658 C CA  . ASP A 1 233 ? 64.112 22.667 -11.919 1.000 45.563  0 233 ASP A CA  1 
ATOM   1659 C C   . ASP A 1 233 ? 63.636 23.660 -10.864 1.000 38.360  0 233 ASP A C   1 
ATOM   1660 O O   . ASP A 1 233 ? 64.048 24.805 -10.885 1.000 39.200  0 233 ASP A O   1 
ATOM   1661 C CB  . ASP A 1 233 ? 63.191 22.713 -13.127 1.000 55.288  0 233 ASP A CB  1 
ATOM   1662 C CG  . ASP A 1 233 ? 62.167 21.594 -13.193 1.000 84.240  0 233 ASP A CG  1 
ATOM   1663 O OD1 . ASP A 1 233 ? 60.981 21.882 -12.874 1.000 101.042 0 233 ASP A OD1 1 
ATOM   1664 O OD2 . ASP A 1 233 ? 62.580 20.444 -13.549 1.000 90.447  0 233 ASP A OD2 1 
ATOM   1665 N N   . ILE A 1 234 ? 62.709 23.257 -10.011 1.000 38.767  0 234 ILE A N   1 
ATOM   1666 C CA  . ILE A 1 234 ? 62.243 24.137 -8.941  1.000 41.011  0 234 ILE A CA  1 
ATOM   1667 C C   . ILE A 1 234 ? 63.409 24.451 -8.003  1.000 40.013  0 234 ILE A C   1 
ATOM   1668 O O   . ILE A 1 234 ? 63.655 25.593 -7.622  1.000 35.683  0 234 ILE A O   1 
ATOM   1669 C CB  . ILE A 1 234 ? 61.072 23.505 -8.162  1.000 38.773  0 234 ILE A CB  1 
ATOM   1670 C CG1 . ILE A 1 234 ? 59.832 23.287 -9.021  1.000 47.612  0 234 ILE A CG1 1 
ATOM   1671 C CG2 . ILE A 1 234 ? 60.736 24.348 -6.929  1.000 45.254  0 234 ILE A CG2 1 
ATOM   1672 C CD1 . ILE A 1 234 ? 59.061 24.552 -9.311  1.000 55.307  0 234 ILE A CD1 1 
ATOM   1673 N N   . LYS A 1 235 ? 64.143 23.411 -7.648  1.000 39.506  0 235 LYS A N   1 
ATOM   1674 C CA  . LYS A 1 235 ? 65.248 23.582 -6.734  1.000 46.147  0 235 LYS A CA  1 
ATOM   1675 C C   . LYS A 1 235 ? 66.311 24.470 -7.351  1.000 44.863  0 235 LYS A C   1 
ATOM   1676 O O   . LYS A 1 235 ? 66.895 25.235 -6.608  1.000 40.085  0 235 LYS A O   1 
ATOM   1677 C CB  . LYS A 1 235 ? 65.846 22.246 -6.297  1.000 46.121  0 235 LYS A CB  1 
ATOM   1678 C CG  . LYS A 1 235 ? 64.893 21.446 -5.459  1.000 51.904  0 235 LYS A CG  1 
ATOM   1679 C CD  . LYS A 1 235 ? 65.573 20.356 -4.641  1.000 59.667  0 235 LYS A CD  1 
ATOM   1680 C CE  . LYS A 1 235 ? 65.785 19.110 -5.389  1.000 66.826  0 235 LYS A CE  1 
ATOM   1681 N NZ  . LYS A 1 235 ? 65.431 18.004 -4.489  1.000 76.194  0 235 LYS A NZ  1 
ATOM   1682 N N   . GLN A 1 236 ? 66.492 24.438 -8.687  1.000 41.941  0 236 GLN A N   1 
ATOM   1683 C CA  . GLN A 1 236 ? 67.481 25.296 -9.320  1.000 40.332  0 236 GLN A CA  1 
ATOM   1684 C C   . GLN A 1 236 ? 66.985 26.740 -9.309  1.000 38.335  0 236 GLN A C   1 
ATOM   1685 O O   . GLN A 1 236 ? 67.735 27.684 -9.113  1.000 39.363  0 236 GLN A O   1 
ATOM   1686 C CB  . GLN A 1 236 ? 67.724 24.812 -10.757 1.000 42.945  0 236 GLN A CB  1 
ATOM   1687 C CG  . GLN A 1 236 ? 68.576 25.746 -11.613 1.000 44.377  0 236 GLN A CG  1 
ATOM   1688 C CD  . GLN A 1 236 ? 70.053 25.678 -11.284 1.000 57.608  0 236 GLN A CD  1 
ATOM   1689 O OE1 . GLN A 1 236 ? 70.478 24.947 -10.386 1.000 67.787  0 236 GLN A OE1 1 
ATOM   1690 N NE2 . GLN A 1 236 ? 70.874 26.441 -11.990 1.000 60.203  0 236 GLN A NE2 1 
ATOM   1691 N N   . GLN A 1 237 ? 65.690 26.939 -9.568  1.000 38.770  0 237 GLN A N   1 
ATOM   1692 C CA  . GLN A 1 237 ? 65.146 28.289 -9.660  1.000 34.188  0 237 GLN A CA  1 
ATOM   1693 C C   . GLN A 1 237 ? 65.217 28.969 -8.289  1.000 33.264  0 237 GLN A C   1 
ATOM   1694 O O   . GLN A 1 237 ? 65.557 30.152 -8.186  1.000 37.719  0 237 GLN A O   1 
ATOM   1695 C CB  . GLN A 1 237 ? 63.671 28.238 -10.080 1.000 37.440  0 237 GLN A CB  1 
ATOM   1696 C CG  . GLN A 1 237 ? 63.380 27.836 -11.521 1.000 40.051  0 237 GLN A CG  1 
ATOM   1697 C CD  . GLN A 1 237 ? 62.017 27.194 -11.704 1.000 39.524  0 237 GLN A CD  1 
ATOM   1698 O OE1 . GLN A 1 237 ? 61.135 27.213 -10.838 1.000 38.125  0 237 GLN A OE1 1 
ATOM   1699 N NE2 . GLN A 1 237 ? 61.884 26.486 -12.811 1.000 43.486  0 237 GLN A NE2 1 
ATOM   1700 N N   . TYR A 1 238 ? 64.815 28.249 -7.238  1.000 35.227  0 238 TYR A N   1 
ATOM   1701 C CA  . TYR A 1 238 ? 64.776 28.877 -5.912  1.000 36.064  0 238 TYR A CA  1 
ATOM   1702 C C   . TYR A 1 238 ? 66.203 28.945 -5.323  1.000 43.332  0 238 TYR A C   1 
ATOM   1703 O O   . TYR A 1 238 ? 66.603 29.996 -4.837  1.000 39.370  0 238 TYR A O   1 
ATOM   1704 C CB  . TYR A 1 238 ? 63.780 28.145 -5.018  1.000 37.219  0 238 TYR A CB  1 
ATOM   1705 C CG  . TYR A 1 238 ? 62.337 28.573 -5.267  1.000 35.736  0 238 TYR A CG  1 
ATOM   1706 C CD1 . TYR A 1 238 ? 61.618 28.109 -6.359  1.000 37.925  0 238 TYR A CD1 1 
ATOM   1707 C CD2 . TYR A 1 238 ? 61.730 29.535 -4.460  1.000 37.235  0 238 TYR A CD2 1 
ATOM   1708 C CE1 . TYR A 1 238 ? 60.317 28.525 -6.604  1.000 37.739  0 238 TYR A CE1 1 
ATOM   1709 C CE2 . TYR A 1 238 ? 60.439 29.974 -4.716  1.000 35.529  0 238 TYR A CE2 1 
ATOM   1710 C CZ  . TYR A 1 238 ? 59.727 29.472 -5.780  1.000 38.696  0 238 TYR A CZ  1 
ATOM   1711 O OH  . TYR A 1 238 ? 58.452 29.896 -6.020  1.000 36.119  0 238 TYR A OH  1 
ATOM   1712 N N   . GLY A 1 239 ? 66.948 27.830 -5.382  1.000 41.433  0 239 GLY A N   1 
ATOM   1713 C CA  . GLY A 1 239 ? 68.362 27.771 -5.012  1.000 46.010  0 239 GLY A CA  1 
ATOM   1714 C C   . GLY A 1 239 ? 68.516 27.050 -3.677  1.000 51.966  0 239 GLY A C   1 
ATOM   1715 O O   . GLY A 1 239 ? 67.641 27.162 -2.822  1.000 48.162  0 239 GLY A O   1 
ATOM   1716 N N   . GLU A 1 240 ? 69.600 26.288 -3.488  1.000 47.316  0 240 GLU A N   1 
ATOM   1717 C CA  . GLU A 1 240 ? 69.798 25.614 -2.213  1.000 55.289  0 240 GLU A CA  1 
ATOM   1718 C C   . GLU A 1 240 ? 69.903 26.675 -1.108  1.000 46.270  0 240 GLU A C   1 
ATOM   1719 O O   . GLU A 1 240 ? 70.301 27.808 -1.341  1.000 57.264  0 240 GLU A O   1 
ATOM   1720 C CB  . GLU A 1 240 ? 70.955 24.614 -2.263  1.000 62.008  0 240 GLU A CB  1 
ATOM   1721 C CG  . GLU A 1 240 ? 70.595 23.295 -1.579  1.000 67.358  0 240 GLU A CG  1 
ATOM   1722 C CD  . GLU A 1 240 ? 69.793 22.337 -2.452  1.000 76.327  0 240 GLU A CD  1 
ATOM   1723 O OE1 . GLU A 1 240 ? 69.151 21.405 -1.916  1.000 72.434  0 240 GLU A OE1 1 
ATOM   1724 O OE2 . GLU A 1 240 ? 69.825 22.497 -3.694  1.000 74.039  0 240 GLU A OE2 1 
ATOM   1725 N N   . GLY A 1 241 ? 69.407 26.367 0.084   1.000 52.593  0 241 GLY A N   1 
ATOM   1726 C CA  . GLY A 1 241 ? 69.385 27.366 1.145   1.000 56.076  0 241 GLY A CA  1 
ATOM   1727 C C   . GLY A 1 241 ? 68.368 28.498 0.952   1.000 58.637  0 241 GLY A C   1 
ATOM   1728 O O   . GLY A 1 241 ? 68.418 29.510 1.660   1.000 50.890  0 241 GLY A O   1 
ATOM   1729 N N   . TYR A 1 242 ? 67.431 28.355 -0.003  1.000 52.179  0 242 TYR A N   1 
ATOM   1730 C CA  . TYR A 1 242 ? 66.287 29.252 -0.053  1.000 47.781  0 242 TYR A CA  1 
ATOM   1731 C C   . TYR A 1 242 ? 65.533 29.156 1.282   1.000 40.112  0 242 TYR A C   1 
ATOM   1732 O O   . TYR A 1 242 ? 65.078 30.163 1.788   1.000 42.783  0 242 TYR A O   1 
ATOM   1733 C CB  . TYR A 1 242 ? 65.304 28.913 -1.176  1.000 42.685  0 242 TYR A CB  1 
ATOM   1734 C CG  . TYR A 1 242 ? 64.214 29.948 -1.318  1.000 44.130  0 242 TYR A CG  1 
ATOM   1735 C CD1 . TYR A 1 242 ? 64.492 31.149 -1.929  1.000 46.826  0 242 TYR A CD1 1 
ATOM   1736 C CD2 . TYR A 1 242 ? 62.940 29.735 -0.804  1.000 46.627  0 242 TYR A CD2 1 
ATOM   1737 C CE1 . TYR A 1 242 ? 63.520 32.119 -2.047  1.000 52.882  0 242 TYR A CE1 1 
ATOM   1738 C CE2 . TYR A 1 242 ? 61.963 30.704 -0.901  1.000 47.581  0 242 TYR A CE2 1 
ATOM   1739 C CZ  . TYR A 1 242 ? 62.264 31.900 -1.517  1.000 51.014  0 242 TYR A CZ  1 
ATOM   1740 O OH  . TYR A 1 242 ? 61.345 32.889 -1.682  1.000 63.037  0 242 TYR A OH  1 
ATOM   1741 N N   . ILE A 1 243 ? 65.388 27.943 1.823   1.000 41.910  0 243 ILE A N   1 
ATOM   1742 C CA  . ILE A 1 243 ? 64.569 27.718 3.002   1.000 45.577  0 243 ILE A CA  1 
ATOM   1743 C C   . ILE A 1 243 ? 65.250 28.321 4.223   1.000 56.921  0 243 ILE A C   1 
ATOM   1744 O O   . ILE A 1 243 ? 64.576 28.892 5.072   1.000 53.869  0 243 ILE A O   1 
ATOM   1745 C CB  . ILE A 1 243 ? 64.285 26.230 3.212   1.000 50.953  0 243 ILE A CB  1 
ATOM   1746 C CG1 . ILE A 1 243 ? 63.316 25.706 2.146   1.000 46.786  0 243 ILE A CG1 1 
ATOM   1747 C CG2 . ILE A 1 243 ? 63.727 25.989 4.621   1.000 55.903  0 243 ILE A CG2 1 
ATOM   1748 C CD1 . ILE A 1 243 ? 63.068 24.213 2.237   1.000 43.374  0 243 ILE A CD1 1 
ATOM   1749 N N   . GLU A 1 244 ? 66.580 28.166 4.296   1.000 52.532  0 244 GLU A N   1 
ATOM   1750 C CA  . GLU A 1 244 ? 67.374 28.781 5.345   1.000 62.324  0 244 GLU A CA  1 
ATOM   1751 C C   . GLU A 1 244 ? 67.179 30.291 5.325   1.000 55.190  0 244 GLU A C   1 
ATOM   1752 O O   . GLU A 1 244 ? 66.896 30.872 6.361   1.000 56.155  0 244 GLU A O   1 
ATOM   1753 C CB  . GLU A 1 244 ? 68.861 28.446 5.209   1.000 72.499  0 244 GLU A CB  1 
ATOM   1754 C CG  . GLU A 1 244 ? 69.313 27.335 6.151   1.000 91.861  0 244 GLU A CG  1 
ATOM   1755 C CD  . GLU A 1 244 ? 69.451 27.770 7.606   1.000 108.200 0 244 GLU A CD  1 
ATOM   1756 O OE1 . GLU A 1 244 ? 70.252 28.700 7.854   1.000 107.493 0 244 GLU A OE1 1 
ATOM   1757 O OE2 . GLU A 1 244 ? 68.768 27.200 8.494   1.000 110.610 0 244 GLU A OE2 1 
ATOM   1758 N N   . LYS A 1 245 ? 67.316 30.935 4.158   1.000 57.901  0 245 LYS A N   1 
ATOM   1759 C CA  . LYS A 1 245 ? 67.128 32.380 4.069   1.000 57.769  0 245 LYS A CA  1 
ATOM   1760 C C   . LYS A 1 245 ? 65.674 32.788 4.336   1.000 70.100  0 245 LYS A C   1 
ATOM   1761 O O   . LYS A 1 245 ? 65.421 33.938 4.699   1.000 72.362  0 245 LYS A O   1 
ATOM   1762 C CB  . LYS A 1 245 ? 67.548 32.942 2.711   1.000 64.903  0 245 LYS A CB  1 
ATOM   1763 C CG  . LYS A 1 245 ? 68.994 32.679 2.359   1.000 71.277  0 245 LYS A CG  1 
ATOM   1764 C CD  . LYS A 1 245 ? 69.579 33.678 1.372   1.000 81.460  0 245 LYS A CD  1 
ATOM   1765 C CE  . LYS A 1 245 ? 69.400 33.265 -0.048  1.000 84.486  0 245 LYS A CE  1 
ATOM   1766 N NZ  . LYS A 1 245 ? 69.745 34.405 -0.898  1.000 84.266  0 245 LYS A NZ  1 
ATOM   1767 N N   . SER A 1 246 ? 64.726 31.853 4.148   1.000 73.929  0 246 SER A N   1 
ATOM   1768 C CA  . SER A 1 246 ? 63.315 32.083 4.450   1.000 87.405  0 246 SER A CA  1 
ATOM   1769 C C   . SER A 1 246 ? 63.080 32.175 5.956   1.000 91.734  0 246 SER A C   1 
ATOM   1770 O O   . SER A 1 246 ? 62.335 33.037 6.416   1.000 87.206  0 246 SER A O   1 
ATOM   1771 C CB  . SER A 1 246 ? 62.425 31.007 3.882   1.000 78.254  0 246 SER A CB  1 
ATOM   1772 O OG  . SER A 1 246 ? 62.212 31.227 2.500   1.000 89.084  0 246 SER A OG  1 
ATOM   1773 N N   . LEU A 1 247 ? 63.676 31.231 6.697   1.000 89.910  0 247 LEU A N   1 
ATOM   1774 C CA  . LEU A 1 247 ? 63.606 31.198 8.149   1.000 82.603  0 247 LEU A CA  1 
ATOM   1775 C C   . LEU A 1 247 ? 64.208 32.474 8.745   1.000 79.487  0 247 LEU A C   1 
ATOM   1776 O O   . LEU A 1 247 ? 63.807 32.893 9.821   1.000 75.111  0 247 LEU A O   1 
ATOM   1777 C CB  . LEU A 1 247 ? 64.314 29.929 8.626   1.000 76.570  0 247 LEU A CB  1 
ATOM   1778 C CG  . LEU A 1 247 ? 64.302 29.677 10.137  1.000 80.909  0 247 LEU A CG  1 
ATOM   1779 C CD1 . LEU A 1 247 ? 62.905 29.789 10.749  1.000 83.951  0 247 LEU A CD1 1 
ATOM   1780 C CD2 . LEU A 1 247 ? 64.904 28.317 10.435  1.000 82.399  0 247 LEU A CD2 1 
ATOM   1781 N N   . HIS A 1 248 ? 65.110 33.120 7.999   1.000 78.452  0 248 HIS A N   1 
ATOM   1782 C CA  . HIS A 1 248 ? 65.803 34.325 8.421   1.000 83.456  0 248 HIS A CA  1 
ATOM   1783 C C   . HIS A 1 248 ? 65.055 35.604 8.034   1.000 94.808  0 248 HIS A C   1 
ATOM   1784 O O   . HIS A 1 248 ? 65.650 36.683 8.031   1.000 104.621 0 248 HIS A O   1 
ATOM   1785 C CB  . HIS A 1 248 ? 67.174 34.332 7.751   1.000 83.453  0 248 HIS A CB  1 
ATOM   1786 C CG  . HIS A 1 248 ? 68.262 34.813 8.624   1.000 96.916  0 248 HIS A CG  1 
ATOM   1787 N ND1 . HIS A 1 248 ? 68.768 34.006 9.621   1.000 98.185  0 248 HIS A ND1 1 
ATOM   1788 C CD2 . HIS A 1 248 ? 68.941 35.962 8.670   1.000 99.871  0 248 HIS A CD2 1 
ATOM   1789 C CE1 . HIS A 1 248 ? 69.737 34.653 10.245  1.000 97.456  0 248 HIS A CE1 1 
ATOM   1790 N NE2 . HIS A 1 248 ? 69.859 35.843 9.683   1.000 101.661 0 248 HIS A NE2 1 
ATOM   1791 N N   . ARG A 1 249 ? 63.775 35.473 7.651   1.000 98.848  0 249 ARG A N   1 
ATOM   1792 C CA  . ARG A 1 249 ? 62.857 36.600 7.512   1.000 98.721  0 249 ARG A CA  1 
ATOM   1793 C C   . ARG A 1 249 ? 61.684 36.423 8.473   1.000 88.552  0 249 ARG A C   1 
ATOM   1794 O O   . ARG A 1 249 ? 61.279 37.381 9.130   1.000 97.935  0 249 ARG A O   1 
ATOM   1795 C CB  . ARG A 1 249 ? 62.304 36.777 6.089   1.000 105.649 0 249 ARG A CB  1 
ATOM   1796 C CG  . ARG A 1 249 ? 63.011 37.849 5.273   1.000 107.495 0 249 ARG A CG  1 
ATOM   1797 C CD  . ARG A 1 249 ? 64.514 37.601 5.173   1.000 110.249 0 249 ARG A CD  1 
ATOM   1798 N NE  . ARG A 1 249 ? 65.209 38.818 4.748   1.000 110.540 0 249 ARG A NE  1 
ATOM   1799 C CZ  . ARG A 1 249 ? 65.080 39.386 3.559   1.000 109.284 0 249 ARG A CZ  1 
ATOM   1800 N NH1 . ARG A 1 249 ? 65.570 40.590 3.345   1.000 111.845 0 249 ARG A NH1 1 
ATOM   1801 N NH2 . ARG A 1 249 ? 64.425 38.772 2.596   1.000 109.690 0 249 ARG A NH2 1 
ATOM   1802 N N   . LEU A 1 250 ? 61.142 35.198 8.525   1.000 79.779  0 250 LEU A N   1 
ATOM   1803 C CA  . LEU A 1 250 ? 60.173 34.792 9.533   1.000 91.463  0 250 LEU A CA  1 
ATOM   1804 C C   . LEU A 1 250 ? 60.646 35.213 10.928  1.000 106.208 0 250 LEU A C   1 
ATOM   1805 O O   . LEU A 1 250 ? 59.858 35.716 11.733  1.000 106.918 0 250 LEU A O   1 
ATOM   1806 C CB  . LEU A 1 250 ? 59.958 33.279 9.458   1.000 79.576  0 250 LEU A CB  1 
ATOM   1807 C CG  . LEU A 1 250 ? 59.175 32.750 8.251   1.000 83.906  0 250 LEU A CG  1 
ATOM   1808 C CD1 . LEU A 1 250 ? 59.085 31.223 8.319   1.000 82.308  0 250 LEU A CD1 1 
ATOM   1809 C CD2 . LEU A 1 250 ? 57.789 33.386 8.147   1.000 80.882  0 250 LEU A CD2 1 
ATOM   1810 N N   . LYS A 1 251 ? 61.938 34.982 11.203  1.000 106.901 0 251 LYS A N   1 
ATOM   1811 C CA  . LYS A 1 251 ? 62.577 35.435 12.427  1.000 104.469 0 251 LYS A CA  1 
ATOM   1812 C C   . LYS A 1 251 ? 62.780 36.950 12.387  1.000 109.097 0 251 LYS A C   1 
ATOM   1813 O O   . LYS A 1 251 ? 62.473 37.632 13.359  1.000 127.998 0 251 LYS A O   1 
ATOM   1814 C CB  . LYS A 1 251 ? 63.905 34.698 12.650  1.000 103.333 0 251 LYS A CB  1 
ATOM   1815 C CG  . LYS A 1 251 ? 63.806 33.297 13.263  1.000 98.684  0 251 LYS A CG  1 
ATOM   1816 C CD  . LYS A 1 251 ? 65.175 32.663 13.502  1.000 104.286 0 251 LYS A CD  1 
ATOM   1817 C CE  . LYS A 1 251 ? 65.307 31.799 14.734  1.000 109.902 0 251 LYS A CE  1 
ATOM   1818 N NZ  . LYS A 1 251 ? 64.772 30.441 14.609  1.000 115.116 0 251 LYS A NZ  1 
ATOM   1819 N N   . SER A 1 252 ? 63.264 37.477 11.257  1.000 109.753 0 252 SER A N   1 
ATOM   1820 C CA  . SER A 1 252 ? 63.782 38.836 11.199  1.000 114.501 0 252 SER A CA  1 
ATOM   1821 C C   . SER A 1 252 ? 62.685 39.903 11.303  1.000 129.088 0 252 SER A C   1 
ATOM   1822 O O   . SER A 1 252 ? 63.008 41.091 11.280  1.000 131.583 0 252 SER A O   1 
ATOM   1823 C CB  . SER A 1 252 ? 64.606 39.026 9.955   1.000 111.740 0 252 SER A CB  1 
ATOM   1824 O OG  . SER A 1 252 ? 65.485 40.130 10.109  1.000 107.100 0 252 SER A OG  1 
ATOM   1825 N N   . ASN A 1 253 ? 61.404 39.499 11.401  1.000 132.411 0 253 ASN A N   1 
ATOM   1826 C CA  . ASN A 1 253 ? 60.310 40.418 11.703  1.000 125.846 0 253 ASN A CA  1 
ATOM   1827 C C   . ASN A 1 253 ? 59.215 39.717 12.513  1.000 123.544 0 253 ASN A C   1 
ATOM   1828 O O   . ASN A 1 253 ? 58.035 39.979 12.298  1.000 116.489 0 253 ASN A O   1 
ATOM   1829 C CB  . ASN A 1 253 ? 59.692 41.027 10.444  1.000 119.909 0 253 ASN A CB  1 
ATOM   1830 C CG  . ASN A 1 253 ? 60.483 42.193 9.901   1.000 119.738 0 253 ASN A CG  1 
ATOM   1831 O OD1 . ASN A 1 253 ? 60.598 43.230 10.561  1.000 111.897 0 253 ASN A OD1 1 
ATOM   1832 N ND2 . ASN A 1 253 ? 61.017 42.056 8.697   1.000 118.621 0 253 ASN A ND2 1 
ATOM   1833 N N   . THR A 1 254 ? 59.603 38.854 13.466  1.000 120.915 0 254 THR A N   1 
ATOM   1834 C CA  . THR A 1 254 ? 58.649 38.191 14.348  1.000 107.752 0 254 THR A CA  1 
ATOM   1835 C C   . THR A 1 254 ? 58.417 39.048 15.594  1.000 105.647 0 254 THR A C   1 
ATOM   1836 O O   . THR A 1 254 ? 57.774 38.600 16.542  1.000 89.543  0 254 THR A O   1 
ATOM   1837 C CB  . THR A 1 254 ? 59.142 36.790 14.719  1.000 99.538  0 254 THR A CB  1 
ATOM   1838 N N   . SER A 1 255 ? 58.912 40.293 15.585  1.000 102.956 0 255 SER A N   1 
ATOM   1839 C CA  . SER A 1 255 ? 58.827 41.154 16.754  1.000 97.502  0 255 SER A CA  1 
ATOM   1840 C C   . SER A 1 255 ? 57.487 41.886 16.800  1.000 94.599  0 255 SER A C   1 
ATOM   1841 O O   . SER A 1 255 ? 57.205 42.575 17.772  1.000 91.643  0 255 SER A O   1 
ATOM   1842 C CB  . SER A 1 255 ? 59.971 42.138 16.797  1.000 94.379  0 255 SER A CB  1 
ATOM   1843 O OG  . SER A 1 255 ? 59.723 43.248 15.945  1.000 95.601  0 255 SER A OG  1 
ATOM   1844 N N   . SER A 1 256 ? 56.673 41.772 15.745  1.000 93.270  0 256 SER A N   1 
ATOM   1845 C CA  . SER A 1 256 ? 55.380 42.440 15.723  1.000 89.861  0 256 SER A CA  1 
ATOM   1846 C C   . SER A 1 256 ? 54.244 41.416 15.792  1.000 80.908  0 256 SER A C   1 
ATOM   1847 O O   . SER A 1 256 ? 53.181 41.621 15.218  1.000 79.265  0 256 SER A O   1 
ATOM   1848 C CB  . SER A 1 256 ? 55.276 43.332 14.505  1.000 95.583  0 256 SER A CB  1 
ATOM   1849 O OG  . SER A 1 256 ? 55.679 42.631 13.336  1.000 88.496  0 256 SER A OG  1 
ATOM   1850 N N   . VAL A 1 257 ? 54.479 40.294 16.475  1.000 70.794  0 257 VAL A N   1 
ATOM   1851 C CA  . VAL A 1 257 ? 53.426 39.339 16.775  1.000 62.885  0 257 VAL A CA  1 
ATOM   1852 C C   . VAL A 1 257 ? 52.858 39.709 18.151  1.000 59.983  0 257 VAL A C   1 
ATOM   1853 O O   . VAL A 1 257 ? 53.580 39.799 19.142  1.000 54.823  0 257 VAL A O   1 
ATOM   1854 C CB  . VAL A 1 257 ? 53.960 37.890 16.675  1.000 66.087  0 257 VAL A CB  1 
ATOM   1855 C CG1 . VAL A 1 257 ? 53.009 36.846 17.233  1.000 65.441  0 257 VAL A CG1 1 
ATOM   1856 C CG2 . VAL A 1 257 ? 54.330 37.509 15.238  1.000 69.713  0 257 VAL A CG2 1 
ATOM   1857 N N   . ASN A 1 258 ? 51.541 39.949 18.208  1.000 53.340  0 258 ASN A N   1 
ATOM   1858 C CA  . ASN A 1 258 ? 50.845 40.258 19.452  1.000 44.639  0 258 ASN A CA  1 
ATOM   1859 C C   . ASN A 1 258 ? 50.930 39.123 20.476  1.000 48.628  0 258 ASN A C   1 
ATOM   1860 O O   . ASN A 1 258 ? 50.680 37.958 20.154  1.000 46.385  0 258 ASN A O   1 
ATOM   1861 C CB  . ASN A 1 258 ? 49.369 40.469 19.168  1.000 49.524  0 258 ASN A CB  1 
ATOM   1862 C CG  . ASN A 1 258 ? 49.049 41.859 18.694  1.000 56.382  0 258 ASN A CG  1 
ATOM   1863 O OD1 . ASN A 1 258 ? 48.929 42.750 19.539  1.000 61.545  0 258 ASN A OD1 1 
ATOM   1864 N ND2 . ASN A 1 258 ? 48.865 42.034 17.387  1.000 58.367  0 258 ASN A ND2 1 
ATOM   1865 N N   . LEU A 1 259 ? 51.203 39.456 21.740  1.000 45.934  0 259 LEU A N   1 
ATOM   1866 C CA  . LEU A 1 259 ? 51.207 38.467 22.810  1.000 54.905  0 259 LEU A CA  1 
ATOM   1867 C C   . LEU A 1 259 ? 49.882 38.466 23.580  1.000 50.210  0 259 LEU A C   1 
ATOM   1868 O O   . LEU A 1 259 ? 49.593 37.537 24.319  1.000 50.066  0 259 LEU A O   1 
ATOM   1869 C CB  . LEU A 1 259 ? 52.360 38.720 23.776  1.000 62.692  0 259 LEU A CB  1 
ATOM   1870 C CG  . LEU A 1 259 ? 53.761 38.749 23.159  1.000 70.815  0 259 LEU A CG  1 
ATOM   1871 C CD1 . LEU A 1 259 ? 54.773 39.040 24.274  1.000 72.449  0 259 LEU A CD1 1 
ATOM   1872 C CD2 . LEU A 1 259 ? 54.081 37.445 22.429  1.000 66.450  0 259 LEU A CD2 1 
ATOM   1873 N N   . ASP A 1 260 ? 49.083 39.518 23.451  1.000 50.274  0 260 ASP A N   1 
ATOM   1874 C CA  . ASP A 1 260 ? 47.916 39.679 24.303  1.000 45.654  0 260 ASP A CA  1 
ATOM   1875 C C   . ASP A 1 260 ? 46.678 39.048 23.652  1.000 39.169  0 260 ASP A C   1 
ATOM   1876 O O   . ASP A 1 260 ? 45.935 39.756 22.983  1.000 40.335  0 260 ASP A O   1 
ATOM   1877 C CB  . ASP A 1 260 ? 47.683 41.151 24.604  1.000 49.232  0 260 ASP A CB  1 
ATOM   1878 C CG  . ASP A 1 260 ? 46.542 41.424 25.582  1.000 53.476  0 260 ASP A CG  1 
ATOM   1879 O OD1 . ASP A 1 260 ? 46.024 40.434 26.158  1.000 55.064  0 260 ASP A OD1 1 
ATOM   1880 O OD2 . ASP A 1 260 ? 46.122 42.614 25.703  1.000 51.968  0 260 ASP A OD2 1 
ATOM   1881 N N   . LEU A 1 261 ? 46.436 37.746 23.919  1.000 39.360  0 261 LEU A N   1 
ATOM   1882 C CA  . LEU A 1 261 ? 45.328 37.011 23.317  1.000 38.093  0 261 LEU A CA  1 
ATOM   1883 C C   . LEU A 1 261 ? 44.003 37.595 23.769  1.000 39.492  0 261 LEU A C   1 
ATOM   1884 O O   . LEU A 1 261 ? 42.988 37.427 23.102  1.000 41.008  0 261 LEU A O   1 
ATOM   1885 C CB  . LEU A 1 261 ? 45.365 35.525 23.652  1.000 40.153  0 261 LEU A CB  1 
ATOM   1886 C CG  . LEU A 1 261 ? 46.656 34.790 23.332  1.000 42.482  0 261 LEU A CG  1 
ATOM   1887 C CD1 . LEU A 1 261 ? 46.406 33.282 23.458  1.000 43.173  0 261 LEU A CD1 1 
ATOM   1888 C CD2 . LEU A 1 261 ? 47.287 35.157 22.008  1.000 48.970  0 261 LEU A CD2 1 
ATOM   1889 N N   . SER A 1 262 ? 43.988 38.321 24.892  1.000 35.277  0 262 SER A N   1 
ATOM   1890 C CA  . SER A 1 262 ? 42.742 38.877 25.366  1.000 38.662  0 262 SER A CA  1 
ATOM   1891 C C   . SER A 1 262 ? 42.212 39.945 24.407  1.000 39.699  0 262 SER A C   1 
ATOM   1892 O O   . SER A 1 262 ? 41.055 40.290 24.483  1.000 38.451  0 262 SER A O   1 
ATOM   1893 C CB  . SER A 1 262 ? 42.869 39.418 26.799  1.000 46.688  0 262 SER A CB  1 
ATOM   1894 O OG  . SER A 1 262 ? 43.527 40.671 26.765  1.000 46.314  0 262 SER A OG  1 
ATOM   1895 N N   . LEU A 1 263 ? 43.011 40.460 23.470  1.000 40.527  0 263 LEU A N   1 
ATOM   1896 C CA  . LEU A 1 263 ? 42.429 41.361 22.479  1.000 39.205  0 263 LEU A CA  1 
ATOM   1897 C C   . LEU A 1 263 ? 41.392 40.633 21.627  1.000 40.269  0 263 LEU A C   1 
ATOM   1898 O O   . LEU A 1 263 ? 40.397 41.194 21.236  1.000 41.102  0 263 LEU A O   1 
ATOM   1899 C CB  . LEU A 1 263 ? 43.536 41.922 21.604  1.000 43.872  0 263 LEU A CB  1 
ATOM   1900 C CG  . LEU A 1 263 ? 44.515 42.867 22.296  1.000 47.374  0 263 LEU A CG  1 
ATOM   1901 C CD1 . LEU A 1 263 ? 45.564 43.285 21.284  1.000 47.618  0 263 LEU A CD1 1 
ATOM   1902 C CD2 . LEU A 1 263 ? 43.774 44.070 22.880  1.000 52.250  0 263 LEU A CD2 1 
ATOM   1903 N N   . VAL A 1 264 ? 41.599 39.349 21.348  1.000 36.535  0 264 VAL A N   1 
ATOM   1904 C CA  . VAL A 1 264 ? 40.658 38.630 20.509  1.000 34.835  0 264 VAL A CA  1 
ATOM   1905 C C   . VAL A 1 264 ? 39.467 38.171 21.347  1.000 33.525  0 264 VAL A C   1 
ATOM   1906 O O   . VAL A 1 264 ? 38.322 38.254 20.924  1.000 33.282  0 264 VAL A O   1 
ATOM   1907 C CB  . VAL A 1 264 ? 41.417 37.457 19.853  1.000 34.396  0 264 VAL A CB  1 
ATOM   1908 C CG1 . VAL A 1 264 ? 40.451 36.446 19.218  1.000 36.575  0 264 VAL A CG1 1 
ATOM   1909 C CG2 . VAL A 1 264 ? 42.409 37.942 18.805  1.000 36.486  0 264 VAL A CG2 1 
ATOM   1910 N N   . VAL A 1 265 ? 39.744 37.657 22.547  1.000 35.119  0 265 VAL A N   1 
ATOM   1911 C CA  . VAL A 1 265 ? 38.696 37.196 23.434  1.000 36.295  0 265 VAL A CA  1 
ATOM   1912 C C   . VAL A 1 265 ? 37.773 38.338 23.823  1.000 36.240  0 265 VAL A C   1 
ATOM   1913 O O   . VAL A 1 265 ? 36.574 38.097 23.964  1.000 38.571  0 265 VAL A O   1 
ATOM   1914 C CB  . VAL A 1 265 ? 39.256 36.445 24.652  1.000 38.771  0 265 VAL A CB  1 
ATOM   1915 C CG1 . VAL A 1 265 ? 38.112 36.017 25.574  1.000 37.975  0 265 VAL A CG1 1 
ATOM   1916 C CG2 . VAL A 1 265 ? 40.018 35.219 24.157  1.000 37.860  0 265 VAL A CG2 1 
ATOM   1917 N N   . GLY A 1 266 ? 38.330 39.551 23.987  1.000 38.465  0 266 GLY A N   1 
ATOM   1918 C CA  . GLY A 1 266 ? 37.528 40.755 24.204  1.000 40.533  0 266 GLY A CA  1 
ATOM   1919 C C   . GLY A 1 266 ? 36.531 41.014 23.066  1.000 39.371  0 266 GLY A C   1 
ATOM   1920 O O   . GLY A 1 266 ? 35.397 41.438 23.301  1.000 38.104  0 266 GLY A O   1 
ATOM   1921 N N   . CYS A 1 267 ? 36.928 40.739 21.813  1.000 38.029  0 267 CYS A N   1 
ATOM   1922 C CA  . CYS A 1 267 ? 36.001 40.839 20.697  1.000 34.046  0 267 CYS A CA  1 
ATOM   1923 C C   . CYS A 1 267 ? 34.924 39.777 20.856  1.000 34.173  0 267 CYS A C   1 
ATOM   1924 O O   . CYS A 1 267 ? 33.748 40.043 20.635  1.000 36.558  0 267 CYS A O   1 
ATOM   1925 C CB  . CYS A 1 267 ? 36.709 40.680 19.343  1.000 36.356  0 267 CYS A CB  1 
ATOM   1926 S SG  . CYS A 1 267 ? 37.898 42.004 18.977  1.000 43.448  0 267 CYS A SG  1 
ATOM   1927 N N   . MET A 1 268 ? 35.322 38.522 21.154  1.000 33.844  0 268 MET A N   1 
ATOM   1928 C CA  . MET A 1 268 ? 34.315 37.493 21.327  1.000 34.804  0 268 MET A CA  1 
ATOM   1929 C C   . MET A 1 268 ? 33.308 37.886 22.423  1.000 34.120  0 268 MET A C   1 
ATOM   1930 O O   . MET A 1 268 ? 32.111 37.614 22.337  1.000 35.398  0 268 MET A O   1 
ATOM   1931 C CB  . MET A 1 268 ? 34.977 36.160 21.699  1.000 38.012  0 268 MET A CB  1 
ATOM   1932 C CG  . MET A 1 268 ? 35.862 35.569 20.614  1.000 40.023  0 268 MET A CG  1 
ATOM   1933 S SD  . MET A 1 268 ? 36.752 34.113 21.206  1.000 37.154  0 268 MET A SD  1 
ATOM   1934 C CE  . MET A 1 268 ? 37.622 33.522 19.745  1.000 37.479  0 268 MET A CE  1 
ATOM   1935 N N   . ASP A 1 269 ? 33.815 38.486 23.498  1.000 36.750  0 269 ASP A N   1 
ATOM   1936 C CA  . ASP A 1 269 ? 32.985 38.844 24.638  1.000 40.112  0 269 ASP A CA  1 
ATOM   1937 C C   . ASP A 1 269 ? 31.917 39.854 24.230  1.000 38.345  0 269 ASP A C   1 
ATOM   1938 O O   . ASP A 1 269 ? 30.734 39.711 24.555  1.000 37.939  0 269 ASP A O   1 
ATOM   1939 C CB  . ASP A 1 269 ? 33.829 39.457 25.745  1.000 48.765  0 269 ASP A CB  1 
ATOM   1940 C CG  . ASP A 1 269 ? 33.044 39.801 27.011  1.000 51.809  0 269 ASP A CG  1 
ATOM   1941 O OD1 . ASP A 1 269 ? 32.223 40.745 26.972  1.000 65.520  0 269 ASP A OD1 1 
ATOM   1942 O OD2 . ASP A 1 269 ? 33.221 39.087 28.000  1.000 63.770  0 269 ASP A OD2 1 
ATOM   1943 N N   . HIS A 1 270 ? 32.334 40.898 23.516  1.000 38.306  0 270 HIS A N   1 
ATOM   1944 C CA  . HIS A 1 270 ? 31.381 41.862 22.998  1.000 37.869  0 270 HIS A CA  1 
ATOM   1945 C C   . HIS A 1 270 ? 30.355 41.185 22.087  1.000 39.012  0 270 HIS A C   1 
ATOM   1946 O O   . HIS A 1 270 ? 29.152 41.442 22.187  1.000 37.437  0 270 HIS A O   1 
ATOM   1947 C CB  . HIS A 1 270 ? 32.143 42.995 22.308  1.000 37.131  0 270 HIS A CB  1 
ATOM   1948 C CG  . HIS A 1 270 ? 31.285 44.114 21.892  1.000 39.935  0 270 HIS A CG  1 
ATOM   1949 N ND1 . HIS A 1 270 ? 30.558 44.185 20.726  1.000 41.100  0 270 HIS A ND1 1 
ATOM   1950 C CD2 . HIS A 1 270 ? 31.024 45.261 22.582  1.000 48.152  0 270 HIS A CD2 1 
ATOM   1951 C CE1 . HIS A 1 270 ? 29.909 45.354 20.693  1.000 47.467  0 270 HIS A CE1 1 
ATOM   1952 N NE2 . HIS A 1 270 ? 30.155 46.005 21.829  1.000 41.446  0 270 HIS A NE2 1 
ATOM   1953 N N   . ALA A 1 271 ? 30.802 40.294 21.174  1.000 37.430  0 271 ALA A N   1 
ATOM   1954 C CA  . ALA A 1 271 ? 29.873 39.641 20.254  1.000 33.556  0 271 ALA A CA  1 
ATOM   1955 C C   . ALA A 1 271 ? 28.810 38.835 21.006  1.000 36.340  0 271 ALA A C   1 
ATOM   1956 O O   . ALA A 1 271 ? 27.707 38.634 20.510  1.000 35.803  0 271 ALA A O   1 
ATOM   1957 C CB  . ALA A 1 271 ? 30.645 38.736 19.317  1.000 37.387  0 271 ALA A CB  1 
ATOM   1958 N N   . LEU A 1 272 ? 29.181 38.284 22.163  1.000 35.787  0 272 LEU A N   1 
ATOM   1959 C CA  . LEU A 1 272 ? 28.298 37.422 22.946  1.000 37.739  0 272 LEU A CA  1 
ATOM   1960 C C   . LEU A 1 272 ? 27.410 38.213 23.905  1.000 40.386  0 272 LEU A C   1 
ATOM   1961 O O   . LEU A 1 272 ? 26.357 37.708 24.259  1.000 40.462  0 272 LEU A O   1 
ATOM   1962 C CB  . LEU A 1 272 ? 29.088 36.492 23.858  1.000 40.409  0 272 LEU A CB  1 
ATOM   1963 C CG  . LEU A 1 272 ? 29.655 35.203 23.282  1.000 44.931  0 272 LEU A CG  1 
ATOM   1964 C CD1 . LEU A 1 272 ? 30.339 34.563 24.499  1.000 46.028  0 272 LEU A CD1 1 
ATOM   1965 C CD2 . LEU A 1 272 ? 28.654 34.261 22.672  1.000 44.644  0 272 LEU A CD2 1 
ATOM   1966 N N   . THR A 1 273 ? 27.857 39.392 24.385  1.000 39.005  0 273 THR A N   1 
ATOM   1967 C CA  . THR A 1 273 ? 27.196 40.062 25.517  1.000 42.025  0 273 THR A CA  1 
ATOM   1968 C C   . THR A 1 273 ? 26.603 41.422 25.151  1.000 47.295  0 273 THR A C   1 
ATOM   1969 O O   . THR A 1 273 ? 25.727 41.904 25.857  1.000 44.792  0 273 THR A O   1 
ATOM   1970 C CB  . THR A 1 273 ? 28.123 40.223 26.731  1.000 44.974  0 273 THR A CB  1 
ATOM   1971 O OG1 . THR A 1 273 ? 29.222 41.093 26.473  1.000 49.410  0 273 THR A OG1 1 
ATOM   1972 C CG2 . THR A 1 273 ? 28.750 38.928 27.181  1.000 42.815  0 273 THR A CG2 1 
ATOM   1973 N N   . SER A 1 274 ? 27.057 42.062 24.073  1.000 43.086  0 274 SER A N   1 
ATOM   1974 C CA  . SER A 1 274 ? 26.466 43.333 23.666  1.000 44.760  0 274 SER A CA  1 
ATOM   1975 C C   . SER A 1 274 ? 25.046 43.128 23.144  1.000 46.936  0 274 SER A C   1 
ATOM   1976 O O   . SER A 1 274 ? 24.721 42.113 22.531  1.000 42.974  0 274 SER A O   1 
ATOM   1977 C CB  . SER A 1 274 ? 27.320 43.995 22.633  1.000 47.161  0 274 SER A CB  1 
ATOM   1978 O OG  . SER A 1 274 ? 26.793 45.243 22.234  1.000 49.553  0 274 SER A OG  1 
ATOM   1979 N N   . LEU A 1 275 ? 24.183 44.131 23.352  1.000 44.530  0 275 LEU A N   1 
ATOM   1980 C CA  . LEU A 1 275 ? 22.876 44.158 22.718  1.000 43.666  0 275 LEU A CA  1 
ATOM   1981 C C   . LEU A 1 275 ? 23.014 44.591 21.259  1.000 43.696  0 275 LEU A C   1 
ATOM   1982 O O   . LEU A 1 275 ? 22.063 44.439 20.494  1.000 46.999  0 275 LEU A O   1 
ATOM   1983 C CB  . LEU A 1 275 ? 21.883 45.089 23.428  1.000 54.067  0 275 LEU A CB  1 
ATOM   1984 C CG  . LEU A 1 275 ? 21.419 44.667 24.821  1.000 59.132  0 275 LEU A CG  1 
ATOM   1985 C CD1 . LEU A 1 275 ? 20.564 45.776 25.420  1.000 72.073  0 275 LEU A CD1 1 
ATOM   1986 C CD2 . LEU A 1 275 ? 20.657 43.352 24.765  1.000 62.581  0 275 LEU A CD2 1 
ATOM   1987 N N   . PHE A 1 276 ? 24.178 45.141 20.892  1.000 46.262  0 276 PHE A N   1 
ATOM   1988 C CA  . PHE A 1 276 ? 24.464 45.594 19.543  1.000 45.220  0 276 PHE A CA  1 
ATOM   1989 C C   . PHE A 1 276 ? 25.782 44.967 19.073  1.000 42.738  0 276 PHE A C   1 
ATOM   1990 O O   . PHE A 1 276 ? 26.781 45.646 18.890  1.000 41.235  0 276 PHE A O   1 
ATOM   1991 C CB  . PHE A 1 276 ? 24.481 47.134 19.628  1.000 55.198  0 276 PHE A CB  1 
ATOM   1992 C CG  . PHE A 1 276 ? 23.120 47.770 19.907  1.000 63.651  0 276 PHE A CG  1 
ATOM   1993 C CD1 . PHE A 1 276 ? 22.177 47.916 18.885  1.000 72.365  0 276 PHE A CD1 1 
ATOM   1994 C CD2 . PHE A 1 276 ? 22.781 48.217 21.185  1.000 68.749  0 276 PHE A CD2 1 
ATOM   1995 C CE1 . PHE A 1 276 ? 20.938 48.489 19.137  1.000 75.110  0 276 PHE A CE1 1 
ATOM   1996 C CE2 . PHE A 1 276 ? 21.535 48.775 21.431  1.000 70.241  0 276 PHE A CE2 1 
ATOM   1997 C CZ  . PHE A 1 276 ? 20.618 48.910 20.409  1.000 71.170  0 276 PHE A CZ  1 
ATOM   1998 N N   . PRO A 1 277 ? 25.864 43.630 18.905  1.000 37.483  0 277 PRO A N   1 
ATOM   1999 C CA  . PRO A 1 277 ? 27.118 43.027 18.467  1.000 42.338  0 277 PRO A CA  1 
ATOM   2000 C C   . PRO A 1 277 ? 27.466 43.520 17.060  1.000 38.048  0 277 PRO A C   1 
ATOM   2001 O O   . PRO A 1 277 ? 26.592 43.728 16.220  1.000 39.435  0 277 PRO A O   1 
ATOM   2002 C CB  . PRO A 1 277 ? 26.815 41.498 18.517  1.000 41.146  0 277 PRO A CB  1 
ATOM   2003 C CG  . PRO A 1 277 ? 25.299 41.429 18.352  1.000 43.604  0 277 PRO A CG  1 
ATOM   2004 C CD  . PRO A 1 277 ? 24.752 42.678 19.014  1.000 41.802  0 277 PRO A CD  1 
ATOM   2005 N N   . LYS A 1 278 ? 28.769 43.608 16.777  1.000 37.292  0 278 LYS A N   1 
ATOM   2006 C CA  . LYS A 1 278 ? 29.231 44.066 15.475  1.000 35.503  0 278 LYS A CA  1 
ATOM   2007 C C   . LYS A 1 278 ? 29.182 42.926 14.468  1.000 38.803  0 278 LYS A C   1 
ATOM   2008 O O   . LYS A 1 278 ? 29.287 41.759 14.839  1.000 37.025  0 278 LYS A O   1 
ATOM   2009 C CB  . LYS A 1 278 ? 30.645 44.619 15.606  1.000 39.495  0 278 LYS A CB  1 
ATOM   2010 C CG  . LYS A 1 278 ? 30.693 45.863 16.503  1.000 47.399  0 278 LYS A CG  1 
ATOM   2011 C CD  . LYS A 1 278 ? 32.109 46.341 16.741  1.000 55.522  0 278 LYS A CD  1 
ATOM   2012 C CE  . LYS A 1 278 ? 32.760 46.664 15.448  1.000 69.454  0 278 LYS A CE  1 
ATOM   2013 N NZ  . LYS A 1 278 ? 34.169 47.018 15.620  1.000 85.042  0 278 LYS A NZ  1 
ATOM   2014 N N   . THR A 1 279 ? 29.123 43.277 13.187  1.000 36.735  0 279 THR A N   1 
ATOM   2015 C CA  . THR A 1 279 ? 29.194 42.273 12.137  1.000 35.400  0 279 THR A CA  1 
ATOM   2016 C C   . THR A 1 279 ? 30.641 41.818 11.924  1.000 34.249  0 279 THR A C   1 
ATOM   2017 O O   . THR A 1 279 ? 30.871 40.658 11.551  1.000 33.327  0 279 THR A O   1 
ATOM   2018 C CB  . THR A 1 279 ? 28.512 42.805 10.868  1.000 37.045  0 279 THR A CB  1 
ATOM   2019 O OG1 . THR A 1 279 ? 29.070 44.051 10.465  1.000 35.805  0 279 THR A OG1 1 
ATOM   2020 C CG2 . THR A 1 279 ? 27.018 43.017 11.072  1.000 37.680  0 279 THR A CG2 1 
ATOM   2021 N N   . ARG A 1 280 ? 31.599 42.729 12.141  1.000 33.207  0 280 ARG A N   1 
ATOM   2022 C CA  . ARG A 1 280 ? 33.024 42.439 12.019  1.000 35.869  0 280 ARG A CA  1 
ATOM   2023 C C   . ARG A 1 280 ? 33.794 43.065 13.176  1.000 35.254  0 280 ARG A C   1 
ATOM   2024 O O   . ARG A 1 280 ? 33.594 44.225 13.526  1.000 36.071  0 280 ARG A O   1 
ATOM   2025 C CB  . ARG A 1 280 ? 33.662 42.828 10.669  1.000 35.223  0 280 ARG A CB  1 
ATOM   2026 C CG  . ARG A 1 280 ? 33.490 41.745 9.609   1.000 37.051  0 280 ARG A CG  1 
ATOM   2027 C CD  . ARG A 1 280 ? 34.178 41.965 8.269   1.000 38.172  0 280 ARG A CD  1 
ATOM   2028 N NE  . ARG A 1 280 ? 33.928 40.831 7.364   1.000 38.044  0 280 ARG A NE  1 
ATOM   2029 C CZ  . ARG A 1 280 ? 32.732 40.455 6.842   1.000 40.085  0 280 ARG A CZ  1 
ATOM   2030 N NH1 . ARG A 1 280 ? 31.656 41.212 7.009   1.000 40.481  0 280 ARG A NH1 1 
ATOM   2031 N NH2 . ARG A 1 280 ? 32.635 39.348 6.101   1.000 40.996  0 280 ARG A NH2 1 
ATOM   2032 N N   . TYR A 1 281 ? 34.703 42.291 13.746  1.000 33.126  0 281 TYR A N   1 
ATOM   2033 C CA  . TYR A 1 281 ? 35.662 42.767 14.736  1.000 34.111  0 281 TYR A CA  1 
ATOM   2034 C C   . TYR A 1 281 ? 37.062 42.578 14.170  1.000 37.372  0 281 TYR A C   1 
ATOM   2035 O O   . TYR A 1 281 ? 37.366 41.526 13.624  1.000 38.494  0 281 TYR A O   1 
ATOM   2036 C CB  . TYR A 1 281 ? 35.583 41.956 16.031  1.000 34.487  0 281 TYR A CB  1 
ATOM   2037 C CG  . TYR A 1 281 ? 34.277 42.110 16.779  1.000 34.167  0 281 TYR A CG  1 
ATOM   2038 C CD1 . TYR A 1 281 ? 33.152 41.389 16.413  1.000 32.751  0 281 TYR A CD1 1 
ATOM   2039 C CD2 . TYR A 1 281 ? 34.135 43.069 17.793  1.000 35.354  0 281 TYR A CD2 1 
ATOM   2040 C CE1 . TYR A 1 281 ? 31.959 41.514 17.105  1.000 36.173  0 281 TYR A CE1 1 
ATOM   2041 C CE2 . TYR A 1 281 ? 32.935 43.207 18.476  1.000 35.659  0 281 TYR A CE2 1 
ATOM   2042 C CZ  . TYR A 1 281 ? 31.833 42.469 18.098  1.000 35.044  0 281 TYR A CZ  1 
ATOM   2043 O OH  . TYR A 1 281 ? 30.650 42.562 18.755  1.000 36.146  0 281 TYR A OH  1 
ATOM   2044 N N   . ILE A 1 282 ? 37.922 43.589 14.316  1.000 32.396  0 282 ILE A N   1 
ATOM   2045 C CA  . ILE A 1 282 ? 39.317 43.455 13.943  1.000 33.207  0 282 ILE A CA  1 
ATOM   2046 C C   . ILE A 1 282 ? 40.168 43.522 15.203  1.000 38.619  0 282 ILE A C   1 
ATOM   2047 O O   . ILE A 1 282 ? 39.958 44.387 16.037  1.000 38.449  0 282 ILE A O   1 
ATOM   2048 C CB  . ILE A 1 282 ? 39.685 44.544 12.933  1.000 36.799  0 282 ILE A CB  1 
ATOM   2049 C CG1 . ILE A 1 282 ? 38.763 44.531 11.732  1.000 40.865  0 282 ILE A CG1 1 
ATOM   2050 C CG2 . ILE A 1 282 ? 41.154 44.427 12.520  1.000 41.552  0 282 ILE A CG2 1 
ATOM   2051 C CD1 . ILE A 1 282 ? 38.676 45.885 11.061  1.000 46.892  0 282 ILE A CD1 1 
ATOM   2052 N N   . ALA A 1 283 ? 41.124 42.603 15.368  1.000 36.867  0 283 ALA A N   1 
ATOM   2053 C CA  . ALA A 1 283 ? 41.918 42.547 16.589  1.000 35.752  0 283 ALA A CA  1 
ATOM   2054 C C   . ALA A 1 283 ? 43.391 42.631 16.230  1.000 36.886  0 283 ALA A C   1 
ATOM   2055 O O   . ALA A 1 283 ? 43.893 41.871 15.403  1.000 37.384  0 283 ALA A O   1 
ATOM   2056 C CB  . ALA A 1 283 ? 41.630 41.268 17.364  1.000 38.683  0 283 ALA A CB  1 
ATOM   2057 N N   . GLY A 1 284 ? 44.094 43.511 16.931  1.000 39.124  0 284 GLY A N   1 
ATOM   2058 C CA  . GLY A 1 284 ? 45.494 43.789 16.655  1.000 40.533  0 284 GLY A CA  1 
ATOM   2059 C C   . GLY A 1 284 ? 45.604 45.214 16.094  1.000 45.583  0 284 GLY A C   1 
ATOM   2060 O O   . GLY A 1 284 ? 44.800 45.634 15.249  1.000 45.632  0 284 GLY A O   1 
ATOM   2061 N N   . LYS A 1 285 ? 46.580 45.961 16.592  1.000 52.967  0 285 LYS A N   1 
ATOM   2062 C CA  . LYS A 1 285 ? 46.732 47.370 16.246  1.000 57.564  0 285 LYS A CA  1 
ATOM   2063 C C   . LYS A 1 285 ? 47.055 47.499 14.752  1.000 51.911  0 285 LYS A C   1 
ATOM   2064 O O   . LYS A 1 285 ? 46.357 48.239 14.047  1.000 50.365  0 285 LYS A O   1 
ATOM   2065 C CB  . LYS A 1 285 ? 47.773 48.007 17.173  1.000 66.525  0 285 LYS A CB  1 
ATOM   2066 C CG  . LYS A 1 285 ? 47.560 49.490 17.466  1.000 83.075  0 285 LYS A CG  1 
ATOM   2067 C CD  . LYS A 1 285 ? 47.746 50.398 16.260  1.000 88.256  0 285 LYS A CD  1 
ATOM   2068 C CE  . LYS A 1 285 ? 47.686 51.866 16.595  1.000 96.312  0 285 LYS A CE  1 
ATOM   2069 N NZ  . LYS A 1 285 ? 48.870 52.360 17.308  1.000 101.575 0 285 LYS A NZ  1 
ATOM   2070 N N   . ASP A 1 286 ? 48.032 46.706 14.255  1.000 41.806  0 286 ASP A N   1 
ATOM   2071 C CA  . ASP A 1 286 ? 48.397 46.769 12.843  1.000 46.193  0 286 ASP A CA  1 
ATOM   2072 C C   . ASP A 1 286 ? 47.240 46.297 11.942  1.000 45.860  0 286 ASP A C   1 
ATOM   2073 O O   . ASP A 1 286 ? 47.042 46.838 10.858  1.000 39.551  0 286 ASP A O   1 
ATOM   2074 C CB  . ASP A 1 286 ? 49.659 45.969 12.562  1.000 48.354  0 286 ASP A CB  1 
ATOM   2075 C CG  . ASP A 1 286 ? 50.966 46.585 13.064  1.000 58.837  0 286 ASP A CG  1 
ATOM   2076 O OD1 . ASP A 1 286 ? 50.952 47.747 13.543  1.000 54.384  0 286 ASP A OD1 1 
ATOM   2077 O OD2 . ASP A 1 286 ? 51.990 45.889 12.992  1.000 54.172  0 286 ASP A OD2 1 
ATOM   2078 N N   . ALA A 1 287 ? 46.503 45.271 12.382  1.000 42.971  0 287 ALA A N   1 
ATOM   2079 C CA  . ALA A 1 287 ? 45.313 44.812 11.668  1.000 45.992  0 287 ALA A CA  1 
ATOM   2080 C C   . ALA A 1 287 ? 44.349 45.959 11.364  1.000 42.445  0 287 ALA A C   1 
ATOM   2081 O O   . ALA A 1 287 ? 43.868 46.085 10.246  1.000 37.876  0 287 ALA A O   1 
ATOM   2082 C CB  . ALA A 1 287 ? 44.613 43.717 12.440  1.000 45.230  0 287 ALA A CB  1 
ATOM   2083 N N   . LYS A 1 288 ? 44.004 46.779 12.350  1.000 39.588  0 288 LYS A N   1 
ATOM   2084 C CA  . LYS A 1 288 ? 42.907 47.710 12.139  1.000 42.669  0 288 LYS A CA  1 
ATOM   2085 C C   . LYS A 1 288 ? 43.416 48.951 11.403  1.000 38.227  0 288 LYS A C   1 
ATOM   2086 O O   . LYS A 1 288 ? 42.678 49.565 10.637  1.000 39.696  0 288 LYS A O   1 
ATOM   2087 C CB  . LYS A 1 288 ? 42.257 48.323 13.384  1.000 57.186  0 288 LYS A CB  1 
ATOM   2088 C CG  . LYS A 1 288 ? 42.250 47.555 14.681  1.000 69.416  0 288 LYS A CG  1 
ATOM   2089 C CD  . LYS A 1 288 ? 42.201 48.536 15.852  1.000 73.957  0 288 LYS A CD  1 
ATOM   2090 C CE  . LYS A 1 288 ? 42.342 47.882 17.173  1.000 79.512  0 288 LYS A CE  1 
ATOM   2091 N NZ  . LYS A 1 288 ? 41.135 47.092 17.399  1.000 78.785  0 288 LYS A NZ  1 
ATOM   2092 N N   . THR A 1 289 ? 44.654 49.369 11.686  1.000 40.525  0 289 THR A N   1 
ATOM   2093 C CA  . THR A 1 289 ? 45.155 50.646 11.162  1.000 48.721  0 289 THR A CA  1 
ATOM   2094 C C   . THR A 1 289 ? 45.777 50.476 9.785   1.000 43.411  0 289 THR A C   1 
ATOM   2095 O O   . THR A 1 289 ? 45.865 51.446 9.036   1.000 38.549  0 289 THR A O   1 
ATOM   2096 C CB  . THR A 1 289 ? 46.184 51.290 12.101  1.000 48.775  0 289 THR A CB  1 
ATOM   2097 O OG1 . THR A 1 289 ? 47.259 50.364 12.208  1.000 49.959  0 289 THR A OG1 1 
ATOM   2098 C CG2 . THR A 1 289 ? 45.632 51.559 13.488  1.000 53.773  0 289 THR A CG2 1 
ATOM   2099 N N   . PHE A 1 290 ? 46.240 49.263 9.455   1.000 38.623  0 290 PHE A N   1 
ATOM   2100 C CA  . PHE A 1 290 ? 46.994 49.081 8.224   1.000 39.372  0 290 PHE A CA  1 
ATOM   2101 C C   . PHE A 1 290 ? 46.485 47.929 7.347   1.000 38.777  0 290 PHE A C   1 
ATOM   2102 O O   . PHE A 1 290 ? 46.213 48.133 6.157   1.000 35.591  0 290 PHE A O   1 
ATOM   2103 C CB  . PHE A 1 290 ? 48.439 48.881 8.686   1.000 38.796  0 290 PHE A CB  1 
ATOM   2104 C CG  . PHE A 1 290 ? 49.387 48.836 7.508   1.000 44.249  0 290 PHE A CG  1 
ATOM   2105 C CD1 . PHE A 1 290 ? 49.821 50.017 6.920   1.000 53.024  0 290 PHE A CD1 1 
ATOM   2106 C CD2 . PHE A 1 290 ? 49.806 47.630 6.962   1.000 45.713  0 290 PHE A CD2 1 
ATOM   2107 C CE1 . PHE A 1 290 ? 50.690 49.982 5.849   1.000 56.097  0 290 PHE A CE1 1 
ATOM   2108 C CE2 . PHE A 1 290 ? 50.667 47.604 5.877   1.000 47.999  0 290 PHE A CE2 1 
ATOM   2109 C CZ  . PHE A 1 290 ? 51.090 48.780 5.315   1.000 50.800  0 290 PHE A CZ  1 
ATOM   2110 N N   . TRP A 1 291 ? 46.462 46.699 7.894   1.000 34.281  0 291 TRP A N   1 
ATOM   2111 C CA  . TRP A 1 291 ? 46.187 45.518 7.067   1.000 34.974  0 291 TRP A CA  1 
ATOM   2112 C C   . TRP A 1 291 ? 44.785 45.493 6.467   1.000 33.107  0 291 TRP A C   1 
ATOM   2113 O O   . TRP A 1 291 ? 44.641 45.245 5.278   1.000 35.353  0 291 TRP A O   1 
ATOM   2114 C CB  . TRP A 1 291 ? 46.443 44.213 7.827   1.000 36.216  0 291 TRP A CB  1 
ATOM   2115 C CG  . TRP A 1 291 ? 47.890 44.051 8.167   1.000 43.405  0 291 TRP A CG  1 
ATOM   2116 C CD1 . TRP A 1 291 ? 48.441 43.982 9.405   1.000 44.536  0 291 TRP A CD1 1 
ATOM   2117 C CD2 . TRP A 1 291 ? 48.985 44.019 7.229   1.000 43.425  0 291 TRP A CD2 1 
ATOM   2118 N NE1 . TRP A 1 291 ? 49.801 43.911 9.295   1.000 43.598  0 291 TRP A NE1 1 
ATOM   2119 C CE2 . TRP A 1 291 ? 50.164 43.922 7.985   1.000 45.873  0 291 TRP A CE2 1 
ATOM   2120 C CE3 . TRP A 1 291 ? 49.077 44.101 5.840   1.000 49.908  0 291 TRP A CE3 1 
ATOM   2121 C CZ2 . TRP A 1 291 ? 51.428 43.879 7.403   1.000 56.013  0 291 TRP A CZ2 1 
ATOM   2122 C CZ3 . TRP A 1 291 ? 50.327 44.082 5.260   1.000 59.100  0 291 TRP A CZ3 1 
ATOM   2123 C CH2 . TRP A 1 291 ? 51.483 43.964 6.031   1.000 60.767  0 291 TRP A CH2 1 
ATOM   2124 N N   . ILE A 1 292 ? 43.742 45.725 7.270   1.000 33.638  0 292 ILE A N   1 
ATOM   2125 C CA  . ILE A 1 292 ? 42.395 45.638 6.733   1.000 34.839  0 292 ILE A CA  1 
ATOM   2126 C C   . ILE A 1 292 ? 42.194 46.788 5.747   1.000 35.645  0 292 ILE A C   1 
ATOM   2127 O O   . ILE A 1 292 ? 41.678 46.570 4.651   1.000 33.246  0 292 ILE A O   1 
ATOM   2128 C CB  . ILE A 1 292 ? 41.320 45.573 7.832   1.000 36.004  0 292 ILE A CB  1 
ATOM   2129 C CG1 . ILE A 1 292 ? 41.378 44.249 8.610   1.000 38.625  0 292 ILE A CG1 1 
ATOM   2130 C CG2 . ILE A 1 292 ? 39.931 45.856 7.251   1.000 39.892  0 292 ILE A CG2 1 
ATOM   2131 C CD1 . ILE A 1 292 ? 41.252 43.006 7.746   1.000 42.996  0 292 ILE A CD1 1 
ATOM   2132 N N   . PRO A 1 293 ? 42.629 48.045 6.043   1.000 37.225  0 293 PRO A N   1 
ATOM   2133 C CA  . PRO A 1 293 ? 42.616 49.073 4.991   1.000 35.179  0 293 PRO A CA  1 
ATOM   2134 C C   . PRO A 1 293 ? 43.304 48.667 3.672   1.000 31.182  0 293 PRO A C   1 
ATOM   2135 O O   . PRO A 1 293 ? 42.747 48.828 2.582   1.000 32.659  0 293 PRO A O   1 
ATOM   2136 C CB  . PRO A 1 293 ? 43.260 50.290 5.718   1.000 37.329  0 293 PRO A CB  1 
ATOM   2137 C CG  . PRO A 1 293 ? 42.858 50.076 7.162   1.000 37.359  0 293 PRO A CG  1 
ATOM   2138 C CD  . PRO A 1 293 ? 43.010 48.565 7.371   1.000 37.837  0 293 PRO A CD  1 
ATOM   2139 N N   . LEU A 1 294 ? 44.498 48.118 3.754   1.000 33.733  0 294 LEU A N   1 
ATOM   2140 C CA  . LEU A 1 294 ? 45.217 47.692 2.562   1.000 34.534  0 294 LEU A CA  1 
ATOM   2141 C C   . LEU A 1 294 ? 44.477 46.611 1.759   1.000 34.614  0 294 LEU A C   1 
ATOM   2142 O O   . LEU A 1 294 ? 44.628 46.533 0.541   1.000 34.552  0 294 LEU A O   1 
ATOM   2143 C CB  . LEU A 1 294 ? 46.575 47.187 2.995   1.000 31.094  0 294 LEU A CB  1 
ATOM   2144 C CG  . LEU A 1 294 ? 47.495 46.735 1.864   1.000 35.325  0 294 LEU A CG  1 
ATOM   2145 C CD1 . LEU A 1 294 ? 47.810 47.972 1.002   1.000 38.742  0 294 LEU A CD1 1 
ATOM   2146 C CD2 . LEU A 1 294 ? 48.754 46.075 2.355   1.000 36.131  0 294 LEU A CD2 1 
ATOM   2147 N N   . SER A 1 295 ? 43.718 45.743 2.452   1.000 34.117  0 295 SER A N   1 
ATOM   2148 C CA  . SER A 1 295 ? 42.931 44.682 1.817   1.000 32.417  0 295 SER A CA  1 
ATOM   2149 C C   . SER A 1 295 ? 41.929 45.267 0.824   1.000 33.862  0 295 SER A C   1 
ATOM   2150 O O   . SER A 1 295 ? 41.523 44.601 -0.130  1.000 33.302  0 295 SER A O   1 
ATOM   2151 C CB  . SER A 1 295 ? 42.217 43.788 2.878   1.000 32.891  0 295 SER A CB  1 
ATOM   2152 O OG  . SER A 1 295 ? 41.025 44.411 3.366   1.000 33.407  0 295 SER A OG  1 
ATOM   2153 N N   . HIS A 1 296 ? 41.590 46.559 0.968   1.000 33.553  0 296 HIS A N   1 
ATOM   2154 C CA  . HIS A 1 296 ? 40.688 47.196 0.024   1.000 33.445  0 296 HIS A CA  1 
ATOM   2155 C C   . HIS A 1 296 ? 41.420 47.710 -1.223  1.000 35.872  0 296 HIS A C   1 
ATOM   2156 O O   . HIS A 1 296 ? 40.790 48.087 -2.212  1.000 35.399  0 296 HIS A O   1 
ATOM   2157 C CB  . HIS A 1 296 ? 39.927 48.362 0.682   1.000 35.983  0 296 HIS A CB  1 
ATOM   2158 C CG  . HIS A 1 296 ? 38.947 47.968 1.752   1.000 37.778  0 296 HIS A CG  1 
ATOM   2159 N ND1 . HIS A 1 296 ? 37.653 47.569 1.465   1.000 39.680  0 296 HIS A ND1 1 
ATOM   2160 C CD2 . HIS A 1 296 ? 39.089 47.860 3.077   1.000 36.901  0 296 HIS A CD2 1 
ATOM   2161 C CE1 . HIS A 1 296 ? 37.025 47.278 2.606   1.000 39.237  0 296 HIS A CE1 1 
ATOM   2162 N NE2 . HIS A 1 296 ? 37.891 47.430 3.600   1.000 39.927  0 296 HIS A NE2 1 
ATOM   2163 N N   . MET A 1 297 ? 42.738 47.819 -1.160  1.000 35.188  0 297 MET A N   1 
ATOM   2164 C CA  A MET A 1 297 ? 43.503 48.414 -2.242  0.500 35.149  0 297 MET A CA  1 
ATOM   2165 C CA  B MET A 1 297 ? 43.518 48.411 -2.240  0.500 36.215  0 297 MET A CA  1 
ATOM   2166 C C   . MET A 1 297 ? 43.708 47.398 -3.360  1.000 40.343  0 297 MET A C   1 
ATOM   2167 O O   . MET A 1 297 ? 43.810 46.202 -3.102  1.000 36.737  0 297 MET A O   1 
ATOM   2168 C CB  A MET A 1 297 ? 44.871 48.854 -1.731  0.500 36.026  0 297 MET A CB  1 
ATOM   2169 C CB  B MET A 1 297 ? 44.946 48.771 -1.827  0.500 39.009  0 297 MET A CB  1 
ATOM   2170 C CG  A MET A 1 297 ? 44.787 49.836 -0.600  0.500 40.449  0 297 MET A CG  1 
ATOM   2171 C CG  B MET A 1 297 ? 45.118 50.096 -1.151  0.500 45.539  0 297 MET A CG  1 
ATOM   2172 S SD  A MET A 1 297 ? 44.169 51.402 -1.260  0.500 49.036  0 297 MET A SD  1 
ATOM   2173 S SD  B MET A 1 297 ? 44.227 51.429 -1.981  0.500 44.574  0 297 MET A SD  1 
ATOM   2174 C CE  A MET A 1 297 ? 45.363 51.488 -2.592  0.500 32.621  0 297 MET A CE  1 
ATOM   2175 C CE  B MET A 1 297 ? 42.673 51.476 -1.055  0.500 39.861  0 297 MET A CE  1 
ATOM   2176 N N   . PRO A 1 298 ? 43.845 47.856 -4.614  1.000 38.992  0 298 PRO A N   1 
ATOM   2177 C CA  . PRO A 1 298 ? 44.211 46.954 -5.713  1.000 42.225  0 298 PRO A CA  1 
ATOM   2178 C C   . PRO A 1 298 ? 45.609 46.353 -5.577  1.000 35.649  0 298 PRO A C   1 
ATOM   2179 O O   . PRO A 1 298 ? 46.452 46.794 -4.784  1.000 34.217  0 298 PRO A O   1 
ATOM   2180 C CB  . PRO A 1 298 ? 44.076 47.825 -6.961  1.000 45.028  0 298 PRO A CB  1 
ATOM   2181 C CG  . PRO A 1 298 ? 44.247 49.248 -6.447  1.000 45.393  0 298 PRO A CG  1 
ATOM   2182 C CD  . PRO A 1 298 ? 43.630 49.249 -5.053  1.000 42.495  0 298 PRO A CD  1 
ATOM   2183 N N   . ALA A 1 299 ? 45.856 45.335 -6.405  1.000 34.962  0 299 ALA A N   1 
ATOM   2184 C CA  . ALA A 1 299 ? 47.062 44.521 -6.320  1.000 37.246  0 299 ALA A CA  1 
ATOM   2185 C C   . ALA A 1 299 ? 48.338 45.342 -6.447  1.000 31.939  0 299 ALA A C   1 
ATOM   2186 O O   . ALA A 1 299 ? 49.294 45.067 -5.735  1.000 34.520  0 299 ALA A O   1 
ATOM   2187 C CB  . ALA A 1 299 ? 46.992 43.434 -7.381  1.000 38.637  0 299 ALA A CB  1 
ATOM   2188 N N   . VAL A 1 300 ? 48.326 46.406 -7.279  1.000 38.686  0 300 VAL A N   1 
ATOM   2189 C CA  . VAL A 1 300 ? 49.542 47.174 -7.532  1.000 39.729  0 300 VAL A CA  1 
ATOM   2190 C C   . VAL A 1 300 ? 50.141 47.712 -6.223  1.000 42.321  0 300 VAL A C   1 
ATOM   2191 O O   . VAL A 1 300 ? 51.352 47.658 -6.042  1.000 42.036  0 300 VAL A O   1 
ATOM   2192 C CB  . VAL A 1 300 ? 49.301 48.304 -8.550  1.000 46.376  0 300 VAL A CB  1 
ATOM   2193 C CG1 . VAL A 1 300 ? 48.316 49.352 -8.054  1.000 44.336  0 300 VAL A CG1 1 
ATOM   2194 C CG2 . VAL A 1 300 ? 50.615 48.984 -8.932  1.000 53.823  0 300 VAL A CG2 1 
ATOM   2195 N N   . LEU A 1 301 ? 49.298 48.145 -5.272  1.000 38.423  0 301 LEU A N   1 
ATOM   2196 C CA  . LEU A 1 301 ? 49.754 48.657 -3.982  1.000 41.295  0 301 LEU A CA  1 
ATOM   2197 C C   . LEU A 1 301 ? 50.094 47.515 -3.030  1.000 45.158  0 301 LEU A C   1 
ATOM   2198 O O   . LEU A 1 301 ? 51.143 47.504 -2.377  1.000 44.903  0 301 LEU A O   1 
ATOM   2199 C CB  . LEU A 1 301 ? 48.623 49.524 -3.433  1.000 47.573  0 301 LEU A CB  1 
ATOM   2200 C CG  . LEU A 1 301 ? 48.575 50.946 -3.990  1.000 63.939  0 301 LEU A CG  1 
ATOM   2201 C CD1 . LEU A 1 301 ? 47.192 51.514 -4.316  1.000 56.076  0 301 LEU A CD1 1 
ATOM   2202 C CD2 . LEU A 1 301 ? 49.290 51.822 -2.972  1.000 70.312  0 301 LEU A CD2 1 
ATOM   2203 N N   . GLN A 1 302 ? 49.195 46.526 -2.956  1.000 37.801  0 302 GLN A N   1 
ATOM   2204 C CA  . GLN A 1 302 ? 49.446 45.402 -2.076  1.000 38.676  0 302 GLN A CA  1 
ATOM   2205 C C   . GLN A 1 302 ? 50.772 44.728 -2.405  1.000 35.226  0 302 GLN A C   1 
ATOM   2206 O O   . GLN A 1 302 ? 51.530 44.366 -1.508  1.000 41.899  0 302 GLN A O   1 
ATOM   2207 C CB  . GLN A 1 302 ? 48.363 44.332 -2.218  1.000 34.996  0 302 GLN A CB  1 
ATOM   2208 C CG  . GLN A 1 302 ? 46.967 44.774 -1.854  1.000 36.146  0 302 GLN A CG  1 
ATOM   2209 C CD  . GLN A 1 302 ? 46.024 43.599 -1.670  1.000 41.260  0 302 GLN A CD  1 
ATOM   2210 O OE1 . GLN A 1 302 ? 46.390 42.422 -1.845  1.000 36.760  0 302 GLN A OE1 1 
ATOM   2211 N NE2 . GLN A 1 302 ? 44.786 43.907 -1.321  1.000 37.698  0 302 GLN A NE2 1 
ATOM   2212 N N   . ASP A 1 303 ? 50.983 44.433 -3.693  1.000 40.230  0 303 ASP A N   1 
ATOM   2213 C CA  . ASP A 1 303 ? 52.116 43.634 -4.134  1.000 37.316  0 303 ASP A CA  1 
ATOM   2214 C C   . ASP A 1 303 ? 53.429 44.358 -3.775  1.000 38.245  0 303 ASP A C   1 
ATOM   2215 O O   . ASP A 1 303 ? 54.355 43.767 -3.211  1.000 40.629  0 303 ASP A O   1 
ATOM   2216 C CB  . ASP A 1 303 ? 51.953 43.239 -5.603  1.000 39.817  0 303 ASP A CB  1 
ATOM   2217 C CG  . ASP A 1 303 ? 50.759 42.325 -5.936  1.000 42.327  0 303 ASP A CG  1 
ATOM   2218 O OD1 . ASP A 1 303 ? 49.989 41.954 -5.005  1.000 35.041  0 303 ASP A OD1 1 
ATOM   2219 O OD2 . ASP A 1 303 ? 50.560 42.013 -7.152  1.000 39.073  0 303 ASP A OD2 1 
ATOM   2220 N N   . PHE A 1 304 ? 53.470 45.665 -4.019  1.000 46.407  0 304 PHE A N   1 
ATOM   2221 C CA  . PHE A 1 304 ? 54.637 46.488 -3.686  1.000 47.860  0 304 PHE A CA  1 
ATOM   2222 C C   . PHE A 1 304 ? 55.028 46.331 -2.220  1.000 49.951  0 304 PHE A C   1 
ATOM   2223 O O   . PHE A 1 304 ? 56.191 46.081 -1.911  1.000 53.989  0 304 PHE A O   1 
ATOM   2224 C CB  . PHE A 1 304 ? 54.265 47.921 -4.069  1.000 52.144  0 304 PHE A CB  1 
ATOM   2225 C CG  . PHE A 1 304 ? 55.358 48.925 -3.759  1.000 65.025  0 304 PHE A CG  1 
ATOM   2226 C CD1 . PHE A 1 304 ? 56.559 48.897 -4.469  1.000 71.746  0 304 PHE A CD1 1 
ATOM   2227 C CD2 . PHE A 1 304 ? 55.166 49.911 -2.794  1.000 67.138  0 304 PHE A CD2 1 
ATOM   2228 C CE1 . PHE A 1 304 ? 57.555 49.829 -4.213  1.000 78.654  0 304 PHE A CE1 1 
ATOM   2229 C CE2 . PHE A 1 304 ? 56.162 50.845 -2.546  1.000 76.674  0 304 PHE A CE2 1 
ATOM   2230 C CZ  . PHE A 1 304 ? 57.354 50.804 -3.253  1.000 79.253  0 304 PHE A CZ  1 
ATOM   2231 N N   . LEU A 1 305 ? 54.045 46.417 -1.312  1.000 45.087  0 305 LEU A N   1 
ATOM   2232 C CA  . LEU A 1 305 ? 54.317 46.331 0.115   1.000 44.493  0 305 LEU A CA  1 
ATOM   2233 C C   . LEU A 1 305 ? 54.672 44.908 0.526   1.000 52.230  0 305 LEU A C   1 
ATOM   2234 O O   . LEU A 1 305 ? 55.639 44.682 1.258   1.000 56.564  0 305 LEU A O   1 
ATOM   2235 C CB  . LEU A 1 305 ? 53.109 46.886 0.871   1.000 46.708  0 305 LEU A CB  1 
ATOM   2236 C CG  . LEU A 1 305 ? 52.892 48.387 0.671   1.000 48.230  0 305 LEU A CG  1 
ATOM   2237 C CD1 . LEU A 1 305 ? 51.555 48.917 1.163   1.000 52.388  0 305 LEU A CD1 1 
ATOM   2238 C CD2 . LEU A 1 305 ? 54.019 49.155 1.362   1.000 55.781  0 305 LEU A CD2 1 
ATOM   2239 N N   . LEU A 1 306 ? 53.926 43.919 0.035   1.000 42.741  0 306 LEU A N   1 
ATOM   2240 C CA  . LEU A 1 306 ? 54.148 42.580 0.545   1.000 44.755  0 306 LEU A CA  1 
ATOM   2241 C C   . LEU A 1 306 ? 55.381 41.923 -0.064  1.000 47.509  0 306 LEU A C   1 
ATOM   2242 O O   . LEU A 1 306 ? 55.858 40.934 0.458   1.000 55.299  0 306 LEU A O   1 
ATOM   2243 C CB  . LEU A 1 306 ? 52.917 41.736 0.308   1.000 42.350  0 306 LEU A CB  1 
ATOM   2244 C CG  . LEU A 1 306 ? 51.666 42.204 1.042   1.000 49.650  0 306 LEU A CG  1 
ATOM   2245 C CD1 . LEU A 1 306 ? 50.551 41.300 0.592   1.000 55.310  0 306 LEU A CD1 1 
ATOM   2246 C CD2 . LEU A 1 306 ? 51.872 42.117 2.525   1.000 54.664  0 306 LEU A CD2 1 
ATOM   2247 N N   . LEU A 1 307 ? 55.888 42.413 -1.178  1.000 54.236  0 307 LEU A N   1 
ATOM   2248 C CA  . LEU A 1 307 ? 56.970 41.661 -1.790  1.000 63.121  0 307 LEU A CA  1 
ATOM   2249 C C   . LEU A 1 307 ? 58.307 42.197 -1.269  1.000 65.826  0 307 LEU A C   1 
ATOM   2250 O O   . LEU A 1 307 ? 59.317 41.508 -1.374  1.000 54.968  0 307 LEU A O   1 
ATOM   2251 C CB  . LEU A 1 307 ? 56.816 41.629 -3.316  1.000 62.252  0 307 LEU A CB  1 
ATOM   2252 C CG  . LEU A 1 307 ? 55.655 40.753 -3.838  1.000 65.628  0 307 LEU A CG  1 
ATOM   2253 C CD1 . LEU A 1 307 ? 55.453 40.836 -5.370  1.000 61.703  0 307 LEU A CD1 1 
ATOM   2254 C CD2 . LEU A 1 307 ? 55.827 39.282 -3.398  1.000 63.406  0 307 LEU A CD2 1 
ATOM   2255 N N   . LYS A 1 308 ? 58.263 43.340 -0.568  1.000 67.707  0 308 LYS A N   1 
ATOM   2256 C CA  . LYS A 1 308 ? 59.452 44.059 -0.123  1.000 75.164  0 308 LYS A CA  1 
ATOM   2257 C C   . LYS A 1 308 ? 60.495 43.125 0.490   1.000 65.196  0 308 LYS A C   1 
ATOM   2258 O O   . LYS A 1 308 ? 61.675 43.241 0.172   1.000 77.234  0 308 LYS A O   1 
ATOM   2259 C CB  . LYS A 1 308 ? 59.155 45.188 0.879   1.000 75.625  0 308 LYS A CB  1 
ATOM   2260 C CG  . LYS A 1 308 ? 59.000 46.570 0.251   1.000 80.127  0 308 LYS A CG  1 
ATOM   2261 C CD  . LYS A 1 308 ? 59.072 47.701 1.271   1.000 90.204  0 308 LYS A CD  1 
ATOM   2262 C CE  . LYS A 1 308 ? 58.256 48.917 0.906   1.000 98.961  0 308 LYS A CE  1 
ATOM   2263 N NZ  . LYS A 1 308 ? 58.737 49.665 -0.261  1.000 101.444 0 308 LYS A NZ  1 
ATOM   2264 N N   . GLN A 1 309 ? 60.062 42.203 1.345   1.000 72.037  0 309 GLN A N   1 
ATOM   2265 C CA  . GLN A 1 309 ? 60.999 41.410 2.124   1.000 92.603  0 309 GLN A CA  1 
ATOM   2266 C C   . GLN A 1 309 ? 61.347 40.078 1.441   1.000 96.917  0 309 GLN A C   1 
ATOM   2267 O O   . GLN A 1 309 ? 62.340 39.469 1.847   1.000 90.845  0 309 GLN A O   1 
ATOM   2268 C CB  . GLN A 1 309 ? 60.459 41.240 3.550   1.000 99.797  0 309 GLN A CB  1 
ATOM   2269 C CG  . GLN A 1 309 ? 59.683 39.946 3.812   1.000 108.295 0 309 GLN A CG  1 
ATOM   2270 C CD  . GLN A 1 309 ? 58.656 39.590 2.752   1.000 98.853  0 309 GLN A CD  1 
ATOM   2271 O OE1 . GLN A 1 309 ? 58.569 38.440 2.296   1.000 90.046  0 309 GLN A OE1 1 
ATOM   2272 N NE2 . GLN A 1 309 ? 57.862 40.572 2.347   1.000 93.002  0 309 GLN A NE2 1 
ATOM   2273 N N   . LYS A 1 310 ? 60.554 39.625 0.437   1.000 86.993  0 310 LYS A N   1 
ATOM   2274 C CA  . LYS A 1 310 ? 60.584 38.237 -0.035  1.000 73.849  0 310 LYS A CA  1 
ATOM   2275 C C   . LYS A 1 310 ? 62.003 37.923 -0.491  1.000 67.407  0 310 LYS A C   1 
ATOM   2276 O O   . LYS A 1 310 ? 62.717 38.806 -0.966  1.000 62.822  0 310 LYS A O   1 
ATOM   2277 C CB  . LYS A 1 310 ? 59.535 37.898 -1.106  1.000 71.284  0 310 LYS A CB  1 
ATOM   2278 N N   . VAL A 1 311 ? 62.442 36.681 -0.247  1.000 70.010  0 311 VAL A N   1 
ATOM   2279 C CA  . VAL A 1 311 ? 63.810 36.287 -0.564  1.000 64.110  0 311 VAL A CA  1 
ATOM   2280 C C   . VAL A 1 311 ? 63.952 36.183 -2.089  1.000 59.387  0 311 VAL A C   1 
ATOM   2281 O O   . VAL A 1 311 ? 63.094 35.591 -2.734  1.000 61.835  0 311 VAL A O   1 
ATOM   2282 C CB  . VAL A 1 311 ? 64.172 34.953 0.116   1.000 64.195  0 311 VAL A CB  1 
ATOM   2283 C CG1 . VAL A 1 311 ? 65.588 34.532 -0.240  1.000 66.933  0 311 VAL A CG1 1 
ATOM   2284 C CG2 . VAL A 1 311 ? 63.981 34.979 1.632   1.000 67.886  0 311 VAL A CG2 1 
ATOM   2285 N N   . GLU A 1 312 ? 65.015 36.765 -2.649  1.000 54.939  0 312 GLU A N   1 
ATOM   2286 C CA  . GLU A 1 312 ? 65.310 36.681 -4.074  1.000 60.518  0 312 GLU A CA  1 
ATOM   2287 C C   . GLU A 1 312 ? 65.509 35.216 -4.457  1.000 53.729  0 312 GLU A C   1 
ATOM   2288 O O   . GLU A 1 312 ? 66.127 34.451 -3.732  1.000 47.575  0 312 GLU A O   1 
ATOM   2289 C CB  . GLU A 1 312 ? 66.603 37.417 -4.415  1.000 67.582  0 312 GLU A CB  1 
ATOM   2290 C CG  . GLU A 1 312 ? 66.579 38.908 -4.089  1.000 84.291  0 312 GLU A CG  1 
ATOM   2291 C CD  . GLU A 1 312 ? 66.208 39.804 -5.259  1.000 95.249  0 312 GLU A CD  1 
ATOM   2292 O OE1 . GLU A 1 312 ? 65.065 40.321 -5.283  1.000 85.225  0 312 GLU A OE1 1 
ATOM   2293 O OE2 . GLU A 1 312 ? 67.083 40.006 -6.139  1.000 98.026  0 312 GLU A OE2 1 
ATOM   2294 N N   . LEU A 1 313 ? 64.988 34.807 -5.608  1.000 48.532  0 313 LEU A N   1 
ATOM   2295 C CA  . LEU A 1 313 ? 65.249 33.455 -6.075  1.000 46.758  0 313 LEU A CA  1 
ATOM   2296 C C   . LEU A 1 313 ? 66.661 33.410 -6.678  1.000 41.624  0 313 LEU A C   1 
ATOM   2297 O O   . LEU A 1 313 ? 67.110 34.378 -7.274  1.000 43.313  0 313 LEU A O   1 
ATOM   2298 C CB  . LEU A 1 313 ? 64.214 33.022 -7.117  1.000 52.052  0 313 LEU A CB  1 
ATOM   2299 C CG  . LEU A 1 313 ? 62.712 33.103 -6.787  1.000 53.349  0 313 LEU A CG  1 
ATOM   2300 C CD1 . LEU A 1 313 ? 62.043 31.945 -7.479  1.000 50.468  0 313 LEU A CD1 1 
ATOM   2301 C CD2 . LEU A 1 313 ? 62.282 33.144 -5.377  1.000 57.654  0 313 LEU A CD2 1 
ATOM   2302 N N   . ALA A 1 314 ? 67.298 32.244 -6.645  1.000 40.501  0 314 ALA A N   1 
ATOM   2303 C CA  . ALA A 1 314 ? 68.668 32.104 -7.144  1.000 44.668  0 314 ALA A CA  1 
ATOM   2304 C C   . ALA A 1 314 ? 68.731 32.204 -8.671  1.000 48.061  0 314 ALA A C   1 
ATOM   2305 O O   . ALA A 1 314 ? 69.560 32.929 -9.194  1.000 45.984  0 314 ALA A O   1 
ATOM   2306 C CB  . ALA A 1 314 ? 69.254 30.791 -6.654  1.000 43.682  0 314 ALA A CB  1 
ATOM   2307 N N   . ASN A 1 315 ? 67.812 31.519 -9.372  1.000 41.084  0 315 ASN A N   1 
ATOM   2308 C CA  . ASN A 1 315 ? 67.845 31.415 -10.824 1.000 41.879  0 315 ASN A CA  1 
ATOM   2309 C C   . ASN A 1 315 ? 66.438 31.458 -11.414 1.000 42.572  0 315 ASN A C   1 
ATOM   2310 O O   . ASN A 1 315 ? 65.985 30.458 -11.999 1.000 40.570  0 315 ASN A O   1 
ATOM   2311 C CB  . ASN A 1 315 ? 68.511 30.115 -11.254 1.000 38.603  0 315 ASN A CB  1 
ATOM   2312 C CG  . ASN A 1 315 ? 69.960 30.045 -10.808 1.000 41.338  0 315 ASN A CG  1 
ATOM   2313 O OD1 . ASN A 1 315 ? 70.806 30.780 -11.320 1.000 43.130  0 315 ASN A OD1 1 
ATOM   2314 N ND2 . ASN A 1 315 ? 70.252 29.171 -9.869  1.000 40.955  0 315 ASN A ND2 1 
ATOM   2315 N N   . PRO A 1 316 ? 65.764 32.625 -11.384 1.000 37.785  0 316 PRO A N   1 
ATOM   2316 C CA  . PRO A 1 316 ? 64.374 32.707 -11.833 1.000 40.900  0 316 PRO A CA  1 
ATOM   2317 C C   . PRO A 1 316 ? 64.173 32.492 -13.334 1.000 42.982  0 316 PRO A C   1 
ATOM   2318 O O   . PRO A 1 316 ? 63.051 32.243 -13.761 1.000 40.559  0 316 PRO A O   1 
ATOM   2319 C CB  . PRO A 1 316 ? 63.937 34.130 -11.411 1.000 42.592  0 316 PRO A CB  1 
ATOM   2320 C CG  . PRO A 1 316 ? 65.240 34.916 -11.326 1.000 45.533  0 316 PRO A CG  1 
ATOM   2321 C CD  . PRO A 1 316 ? 66.275 33.904 -10.869 1.000 46.062  0 316 PRO A CD  1 
ATOM   2322 N N   . LYS A 1 317 ? 65.241 32.639 -14.143 1.000 39.480  0 317 LYS A N   1 
ATOM   2323 C CA  . LYS A 1 317 ? 65.161 32.414 -15.570 1.000 37.562  0 317 LYS A CA  1 
ATOM   2324 C C   . LYS A 1 317 ? 65.370 30.947 -15.936 1.000 36.963  0 317 LYS A C   1 
ATOM   2325 O O   . LYS A 1 317 ? 65.325 30.639 -17.131 1.000 39.226  0 317 LYS A O   1 
ATOM   2326 C CB  . LYS A 1 317 ? 66.149 33.305 -16.313 1.000 38.972  0 317 LYS A CB  1 
ATOM   2327 C CG  . LYS A 1 317 ? 65.723 34.736 -16.214 1.000 47.097  0 317 LYS A CG  1 
ATOM   2328 C CD  . LYS A 1 317 ? 66.628 35.664 -16.979 1.000 53.444  0 317 LYS A CD  1 
ATOM   2329 C CE  . LYS A 1 317 ? 65.997 37.008 -16.976 1.000 64.009  0 317 LYS A CE  1 
ATOM   2330 N NZ  . LYS A 1 317 ? 67.101 37.946 -17.154 1.000 73.711  0 317 LYS A NZ  1 
ATOM   2331 N N   . ALA A 1 318 ? 65.603 30.080 -14.947 1.000 39.149  0 318 ALA A N   1 
ATOM   2332 C CA  . ALA A 1 318 ? 65.743 28.644 -15.155 1.000 38.256  0 318 ALA A CA  1 
ATOM   2333 C C   . ALA A 1 318 ? 64.385 27.936 -15.263 1.000 37.589  0 318 ALA A C   1 
ATOM   2334 O O   . ALA A 1 318 ? 64.134 26.928 -14.591 1.000 42.354  0 318 ALA A O   1 
ATOM   2335 C CB  . ALA A 1 318 ? 66.599 28.073 -14.066 1.000 38.242  0 318 ALA A CB  1 
ATOM   2336 N N   . VAL A 1 319 ? 63.590 28.367 -16.259 1.000 47.006  0 319 VAL A N   1 
ATOM   2337 C CA  . VAL A 1 319 ? 62.230 27.886 -16.503 1.000 45.447  0 319 VAL A CA  1 
ATOM   2338 C C   . VAL A 1 319 ? 62.141 27.099 -17.837 1.000 64.718  0 319 VAL A C   1 
ATOM   2339 O O   . VAL A 1 319 ? 63.002 27.333 -18.747 1.000 58.332  0 319 VAL A O   1 
ATOM   2340 C CB  . VAL A 1 319 ? 61.226 29.055 -16.424 1.000 41.919  0 319 VAL A CB  1 
ATOM   2341 C CG1 . VAL A 1 319 ? 61.194 29.608 -15.008 1.000 41.013  0 319 VAL A CG1 1 
ATOM   2342 C CG2 . VAL A 1 319 ? 61.465 30.178 -17.425 1.000 40.950  0 319 VAL A CG2 1 
ATOM   2343 O OXT . VAL A 1 319 ? 61.237 26.212 -17.914 1.000 60.298  0 319 VAL A OXT 1 
HETATM 2344 P PA  . NAD B 2 .   ? 46.034 27.122 18.241  1.000 33.366  0 401 NAD A PA  1 
HETATM 2345 O O1A . NAD B 2 .   ? 46.677 26.095 17.377  1.000 32.571  0 401 NAD A O1A 1 
HETATM 2346 O O2A . NAD B 2 .   ? 46.663 27.541 19.534  1.000 34.433  0 401 NAD A O2A 1 
HETATM 2347 O O5B . NAD B 2 .   ? 44.541 26.738 18.531  1.000 31.571  0 401 NAD A O5B 1 
HETATM 2348 C C5B . NAD B 2 .   ? 43.817 25.948 17.554  1.000 35.188  0 401 NAD A C5B 1 
HETATM 2349 C C4B . NAD B 2 .   ? 42.812 25.126 18.306  1.000 32.488  0 401 NAD A C4B 1 
HETATM 2350 O O4B . NAD B 2 .   ? 42.026 24.360 17.355  1.000 34.675  0 401 NAD A O4B 1 
HETATM 2351 C C3B . NAD B 2 .   ? 43.435 24.112 19.294  1.000 33.902  0 401 NAD A C3B 1 
HETATM 2352 O O3B . NAD B 2 .   ? 42.648 23.975 20.471  1.000 34.553  0 401 NAD A O3B 1 
HETATM 2353 C C2B . NAD B 2 .   ? 43.366 22.807 18.503  1.000 33.964  0 401 NAD A C2B 1 
HETATM 2354 O O2B . NAD B 2 .   ? 43.322 21.726 19.394  1.000 37.024  0 401 NAD A O2B 1 
HETATM 2355 C C1B . NAD B 2 .   ? 42.047 23.005 17.756  1.000 32.788  0 401 NAD A C1B 1 
HETATM 2356 N N9A . NAD B 2 .   ? 41.875 22.163 16.590  1.000 31.980  0 401 NAD A N9A 1 
HETATM 2357 C C8A . NAD B 2 .   ? 42.767 21.957 15.556  1.000 33.793  0 401 NAD A C8A 1 
HETATM 2358 N N7A . NAD B 2 .   ? 42.339 21.080 14.672  1.000 34.849  0 401 NAD A N7A 1 
HETATM 2359 C C5A . NAD B 2 .   ? 41.066 20.735 15.123  1.000 32.656  0 401 NAD A C5A 1 
HETATM 2360 C C6A . NAD B 2 .   ? 40.110 19.815 14.655  1.000 33.453  0 401 NAD A C6A 1 
HETATM 2361 N N6A . NAD B 2 .   ? 40.241 19.078 13.559  1.000 35.581  0 401 NAD A N6A 1 
HETATM 2362 N N1A . NAD B 2 .   ? 38.997 19.652 15.392  1.000 34.474  0 401 NAD A N1A 1 
HETATM 2363 C C2A . NAD B 2 .   ? 38.855 20.364 16.510  1.000 31.873  0 401 NAD A C2A 1 
HETATM 2364 N N3A . NAD B 2 .   ? 39.683 21.225 17.070  1.000 33.201  0 401 NAD A N3A 1 
HETATM 2365 C C4A . NAD B 2 .   ? 40.790 21.361 16.322  1.000 33.141  0 401 NAD A C4A 1 
HETATM 2366 O O3  . NAD B 2 .   ? 45.795 28.466 17.390  1.000 33.005  0 401 NAD A O3  1 
HETATM 2367 P PN  . NAD B 2 .   ? 44.873 29.750 17.508  1.000 33.090  0 401 NAD A PN  1 
HETATM 2368 O O1N . NAD B 2 .   ? 45.621 30.881 16.937  1.000 33.616  0 401 NAD A O1N 1 
HETATM 2369 O O2N . NAD B 2 .   ? 44.315 29.879 18.879  1.000 29.902  0 401 NAD A O2N 1 
HETATM 2370 O O5D . NAD B 2 .   ? 43.725 29.281 16.474  1.000 32.331  0 401 NAD A O5D 1 
HETATM 2371 C C5D . NAD B 2 .   ? 42.331 29.568 16.705  1.000 30.139  0 401 NAD A C5D 1 
HETATM 2372 C C4D . NAD B 2 .   ? 41.733 30.245 15.476  1.000 31.778  0 401 NAD A C4D 1 
HETATM 2373 O O4D . NAD B 2 .   ? 42.306 31.577 15.334  1.000 33.029  0 401 NAD A O4D 1 
HETATM 2374 C C3D . NAD B 2 .   ? 41.940 29.544 14.129  1.000 29.399  0 401 NAD A C3D 1 
HETATM 2375 O O3D . NAD B 2 .   ? 40.768 29.594 13.313  1.000 32.436  0 401 NAD A O3D 1 
HETATM 2376 C C2D . NAD B 2 .   ? 43.040 30.390 13.475  1.000 29.535  0 401 NAD A C2D 1 
HETATM 2377 O O2D . NAD B 2 .   ? 42.994 30.236 12.059  1.000 31.835  0 401 NAD A O2D 1 
HETATM 2378 C C1D . NAD B 2 .   ? 42.591 31.774 13.954  1.000 32.186  0 401 NAD A C1D 1 
HETATM 2379 N N1N . NAD B 2 .   ? 43.552 32.863 13.813  1.000 33.165  0 401 NAD A N1N 1 
HETATM 2380 C C2N . NAD B 2 .   ? 44.762 32.834 14.475  1.000 31.519  0 401 NAD A C2N 1 
HETATM 2381 C C3N . NAD B 2 .   ? 45.693 33.848 14.305  1.000 34.855  0 401 NAD A C3N 1 
HETATM 2382 C C7N . NAD B 2 .   ? 47.009 33.837 15.014  1.000 38.098  0 401 NAD A C7N 1 
HETATM 2383 O O7N . NAD B 2 .   ? 47.911 34.568 14.581  1.000 35.712  0 401 NAD A O7N 1 
HETATM 2384 N N7N . NAD B 2 .   ? 47.138 33.081 16.110  1.000 37.834  0 401 NAD A N7N 1 
HETATM 2385 C C4N . NAD B 2 .   ? 45.390 34.910 13.456  1.000 40.554  0 401 NAD A C4N 1 
HETATM 2386 C C5N . NAD B 2 .   ? 44.144 34.950 12.833  1.000 37.280  0 401 NAD A C5N 1 
HETATM 2387 C C6N . NAD B 2 .   ? 43.247 33.928 12.992  1.000 34.058  0 401 NAD A C6N 1 
HETATM 2388 C C1  . MLI C 3 .   ? 37.177 51.541 -3.338  0.500 66.287  0 402 MLI A C1  1 
HETATM 2389 C C2  . MLI C 3 .   ? 35.688 51.777 -3.615  0.500 69.388  0 402 MLI A C2  1 
HETATM 2390 C C3  . MLI C 3 .   ? 37.612 51.476 -1.862  0.500 73.504  0 402 MLI A C3  1 
HETATM 2391 O O6  . MLI C 3 .   ? 35.238 51.486 -4.751  0.500 66.098  0 402 MLI A O6  1 
HETATM 2392 O O7  . MLI C 3 .   ? 34.979 52.233 -2.695  0.500 66.151  0 402 MLI A O7  1 
HETATM 2393 O O8  . MLI C 3 .   ? 38.838 51.292 -1.607  0.500 55.705  0 402 MLI A O8  1 
HETATM 2394 O O9  . MLI C 3 .   ? 36.729 51.616 -0.963  0.500 74.163  0 402 MLI A O9  1 
HETATM 2395 O O   . HOH D 4 .   ? 54.608 29.563 10.247  1.000 54.599  0 501 HOH A O   1 
HETATM 2396 O O   . HOH D 4 .   ? 36.850 22.109 37.103  1.000 41.292  0 502 HOH A O   1 
HETATM 2397 O O   . HOH D 4 .   ? 70.786 29.451 -2.936  1.000 52.245  0 503 HOH A O   1 
HETATM 2398 O O   . HOH D 4 .   ? 51.488 29.306 22.814  1.000 54.436  0 504 HOH A O   1 
HETATM 2399 O O   . HOH D 4 .   ? 50.661 43.749 -8.908  1.000 59.482  0 505 HOH A O   1 
HETATM 2400 O O   . HOH D 4 .   ? 70.458 32.843 -12.638 1.000 46.920  0 506 HOH A O   1 
HETATM 2401 O O   . HOH D 4 .   ? 46.072 34.598 3.817   1.000 48.211  0 507 HOH A O   1 
HETATM 2402 O O   . HOH D 4 .   ? 68.297 21.321 -9.344  1.000 47.590  0 508 HOH A O   1 
HETATM 2403 O O   . HOH D 4 .   ? 61.075 18.411 7.934   1.000 59.253  0 509 HOH A O   1 
HETATM 2404 O O   . HOH D 4 .   ? 47.598 23.732 17.770  1.000 42.347  0 510 HOH A O   1 
HETATM 2405 O O   . HOH D 4 .   ? 17.659 21.985 22.721  1.000 40.424  0 511 HOH A O   1 
HETATM 2406 O O   . HOH D 4 .   ? 46.200 24.992 15.096  1.000 35.621  0 512 HOH A O   1 
HETATM 2407 O O   . HOH D 4 .   ? 57.946 32.427 -5.810  1.000 40.034  0 513 HOH A O   1 
HETATM 2408 O O   . HOH D 4 .   ? 36.131 15.329 7.004   1.000 48.899  0 514 HOH A O   1 
HETATM 2409 O O   . HOH D 4 .   ? 48.753 28.931 -3.175  1.000 34.584  0 515 HOH A O   1 
HETATM 2410 O O   . HOH D 4 .   ? 15.103 32.411 15.979  1.000 48.354  0 516 HOH A O   1 
HETATM 2411 O O   . HOH D 4 .   ? 22.651 17.180 14.192  1.000 45.598  0 517 HOH A O   1 
HETATM 2412 O O   . HOH D 4 .   ? 46.068 33.974 10.282  1.000 50.540  0 518 HOH A O   1 
HETATM 2413 O O   . HOH D 4 .   ? 22.014 37.702 11.066  1.000 35.064  0 519 HOH A O   1 
HETATM 2414 O O   . HOH D 4 .   ? 46.296 18.735 3.141   1.000 37.782  0 520 HOH A O   1 
HETATM 2415 O O   . HOH D 4 .   ? 21.328 19.423 14.411  1.000 53.063  0 521 HOH A O   1 
HETATM 2416 O O   . HOH D 4 .   ? 36.897 47.376 6.040   1.000 47.462  0 522 HOH A O   1 
HETATM 2417 O O   . HOH D 4 .   ? 43.791 19.174 13.559  1.000 47.513  0 523 HOH A O   1 
HETATM 2418 O O   . HOH D 4 .   ? 47.113 23.060 20.207  1.000 42.701  0 524 HOH A O   1 
HETATM 2419 O O   . HOH D 4 .   ? 25.910 18.568 7.618   1.000 39.820  0 525 HOH A O   1 
HETATM 2420 O O   . HOH D 4 .   ? 18.358 37.478 21.077  1.000 48.645  0 526 HOH A O   1 
HETATM 2421 O O   . HOH D 4 .   ? 61.643 33.611 -15.541 1.000 45.518  0 527 HOH A O   1 
HETATM 2422 O O   . HOH D 4 .   ? 40.770 17.376 34.723  1.000 44.194  0 528 HOH A O   1 
HETATM 2423 O O   . HOH D 4 .   ? 9.397  26.110 24.508  1.000 46.988  0 529 HOH A O   1 
HETATM 2424 O O   . HOH D 4 .   ? 21.045 37.682 18.926  1.000 46.136  0 530 HOH A O   1 
HETATM 2425 O O   . HOH D 4 .   ? 35.329 18.710 7.746   1.000 41.822  0 531 HOH A O   1 
HETATM 2426 O O   . HOH D 4 .   ? 48.577 24.263 2.062   1.000 45.295  0 532 HOH A O   1 
HETATM 2427 O O   . HOH D 4 .   ? 35.525 22.471 35.096  1.000 43.677  0 533 HOH A O   1 
HETATM 2428 O O   . HOH D 4 .   ? 29.101 39.109 10.266  1.000 32.228  0 534 HOH A O   1 
HETATM 2429 O O   . HOH D 4 .   ? 16.373 18.362 26.825  1.000 58.265  0 535 HOH A O   1 
HETATM 2430 O O   . HOH D 4 .   ? 43.817 22.795 27.829  1.000 40.076  0 536 HOH A O   1 
HETATM 2431 O O   . HOH D 4 .   ? 17.387 38.678 18.304  1.000 52.500  0 537 HOH A O   1 
HETATM 2432 O O   . HOH D 4 .   ? 45.359 30.167 25.683  1.000 36.564  0 538 HOH A O   1 
HETATM 2433 O O   . HOH D 4 .   ? 16.955 36.662 6.826   1.000 42.074  0 539 HOH A O   1 
HETATM 2434 O O   . HOH D 4 .   ? 50.168 33.161 14.186  1.000 46.115  0 540 HOH A O   1 
HETATM 2435 O O   . HOH D 4 .   ? 22.514 34.504 2.324   1.000 39.350  0 541 HOH A O   1 
HETATM 2436 O O   . HOH D 4 .   ? 45.965 17.176 30.897  1.000 47.722  0 542 HOH A O   1 
HETATM 2437 O O   . HOH D 4 .   ? 48.288 26.584 4.341   1.000 39.873  0 543 HOH A O   1 
HETATM 2438 O O   . HOH D 4 .   ? 59.257 25.695 -16.161 1.000 39.117  0 544 HOH A O   1 
HETATM 2439 O O   . HOH D 4 .   ? 44.935 53.820 9.920   1.000 42.426  0 545 HOH A O   1 
HETATM 2440 O O   . HOH D 4 .   ? 25.097 12.346 21.604  1.000 51.796  0 546 HOH A O   1 
HETATM 2441 O O   . HOH D 4 .   ? 28.935 39.911 1.333   1.000 32.794  0 547 HOH A O   1 
HETATM 2442 O O   . HOH D 4 .   ? 42.644 41.940 -0.719  1.000 35.293  0 548 HOH A O   1 
HETATM 2443 O O   . HOH D 4 .   ? 27.259 37.909 17.369  1.000 47.111  0 549 HOH A O   1 
HETATM 2444 O O   . HOH D 4 .   ? 32.561 39.776 2.299   1.000 33.782  0 550 HOH A O   1 
HETATM 2445 O O   . HOH D 4 .   ? 43.213 12.693 23.094  1.000 59.765  0 551 HOH A O   1 
HETATM 2446 O O   . HOH D 4 .   ? 46.870 30.145 -1.671  1.000 33.351  0 552 HOH A O   1 
HETATM 2447 O O   . HOH D 4 .   ? 44.948 14.865 -5.760  1.000 50.135  0 553 HOH A O   1 
HETATM 2448 O O   . HOH D 4 .   ? 31.183 27.725 32.328  1.000 40.921  0 554 HOH A O   1 
HETATM 2449 O O   . HOH D 4 .   ? 32.488 17.335 10.142  1.000 37.817  0 555 HOH A O   1 
HETATM 2450 O O   . HOH D 4 .   ? 45.300 27.625 30.117  1.000 58.015  0 556 HOH A O   1 
HETATM 2451 O O   . HOH D 4 .   ? 15.716 38.916 6.420   1.000 55.133  0 557 HOH A O   1 
HETATM 2452 O O   . HOH D 4 .   ? 18.915 30.891 28.599  1.000 41.008  0 558 HOH A O   1 
HETATM 2453 O O   . HOH D 4 .   ? 36.714 45.994 15.535  1.000 42.921  0 559 HOH A O   1 
HETATM 2454 O O   . HOH D 4 .   ? 42.321 28.314 19.932  1.000 30.493  0 560 HOH A O   1 
HETATM 2455 O O   . HOH D 4 .   ? 29.606 41.531 4.809   1.000 37.256  0 561 HOH A O   1 
HETATM 2456 O O   . HOH D 4 .   ? 50.454 31.161 16.235  1.000 44.642  0 562 HOH A O   1 
HETATM 2457 O O   . HOH D 4 .   ? 34.362 25.318 14.513  1.000 34.627  0 563 HOH A O   1 
HETATM 2458 O O   . HOH D 4 .   ? 45.730 20.693 20.228  1.000 46.442  0 564 HOH A O   1 
HETATM 2459 O O   . HOH D 4 .   ? 37.545 30.118 34.498  1.000 47.236  0 565 HOH A O   1 
HETATM 2460 O O   . HOH D 4 .   ? 38.721 44.118 1.877   1.000 43.918  0 566 HOH A O   1 
HETATM 2461 O O   . HOH D 4 .   ? 36.534 25.037 12.446  1.000 37.457  0 567 HOH A O   1 
HETATM 2462 O O   . HOH D 4 .   ? 39.875 44.549 -2.356  1.000 55.585  0 568 HOH A O   1 
HETATM 2463 O O   . HOH D 4 .   ? 38.113 28.934 10.295  1.000 36.011  0 569 HOH A O   1 
HETATM 2464 O O   . HOH D 4 .   ? 18.232 32.996 24.618  1.000 40.071  0 570 HOH A O   1 
HETATM 2465 O O   . HOH D 4 .   ? 48.373 21.516 4.487   1.000 40.406  0 571 HOH A O   1 
HETATM 2466 O O   . HOH D 4 .   ? 44.140 24.692 29.715  1.000 52.525  0 572 HOH A O   1 
HETATM 2467 O O   . HOH D 4 .   ? 11.568 37.863 10.731  1.000 53.393  0 573 HOH A O   1 
HETATM 2468 O O   . HOH D 4 .   ? 27.620 15.817 10.726  1.000 40.457  0 574 HOH A O   1 
HETATM 2469 O O   . HOH D 4 .   ? 43.281 43.759 -4.342  1.000 42.859  0 575 HOH A O   1 
HETATM 2470 O O   . HOH D 4 .   ? 18.761 33.432 29.131  1.000 47.558  0 576 HOH A O   1 
HETATM 2471 O O   . HOH D 4 .   ? 48.988 23.236 10.529  1.000 47.991  0 577 HOH A O   1 
HETATM 2472 O O   . HOH D 4 .   ? 20.098 32.149 0.675   1.000 42.072  0 578 HOH A O   1 
HETATM 2473 O O   . HOH D 4 .   ? 56.134 21.312 -7.356  1.000 51.844  0 579 HOH A O   1 
HETATM 2474 O O   . HOH D 4 .   ? 17.724 23.714 29.984  1.000 59.506  0 580 HOH A O   1 
HETATM 2475 O O   . HOH D 4 .   ? 34.950 39.966 3.511   1.000 49.015  0 581 HOH A O   1 
HETATM 2476 O O   . HOH D 4 .   ? 39.046 20.022 2.271   1.000 36.835  0 582 HOH A O   1 
HETATM 2477 O O   . HOH D 4 .   ? 55.773 23.639 -10.093 1.000 36.709  0 583 HOH A O   1 
HETATM 2478 O O   . HOH D 4 .   ? 28.282 23.883 30.514  1.000 42.496  0 584 HOH A O   1 
HETATM 2479 O O   . HOH D 4 .   ? 37.419 38.086 1.492   1.000 41.389  0 585 HOH A O   1 
HETATM 2480 O O   . HOH D 4 .   ? 39.236 41.247 0.929   1.000 41.394  0 586 HOH A O   1 
HETATM 2481 O O   . HOH D 4 .   ? 50.980 36.665 -0.885  1.000 39.135  0 587 HOH A O   1 
HETATM 2482 O O   . HOH D 4 .   ? 40.361 29.439 34.548  1.000 47.596  0 588 HOH A O   1 
HETATM 2483 O O   . HOH D 4 .   ? 55.267 25.261 5.879   1.000 55.321  0 589 HOH A O   1 
HETATM 2484 O O   . HOH D 4 .   ? 38.573 18.444 0.391   1.000 41.616  0 590 HOH A O   1 
HETATM 2485 O O   . HOH D 4 .   ? 21.124 23.889 9.970   1.000 43.641  0 591 HOH A O   1 
HETATM 2486 O O   . HOH D 4 .   ? 37.920 28.827 13.013  1.000 34.282  0 592 HOH A O   1 
HETATM 2487 O O   . HOH D 4 .   ? 58.226 19.732 -8.085  1.000 52.077  0 593 HOH A O   1 
HETATM 2488 O O   . HOH D 4 .   ? 26.018 29.898 35.192  1.000 45.771  0 594 HOH A O   1 
HETATM 2489 O O   . HOH D 4 .   ? 19.576 30.807 25.862  1.000 40.897  0 595 HOH A O   1 
HETATM 2490 O O   . HOH D 4 .   ? 29.794 43.821 25.794  1.000 53.928  0 596 HOH A O   1 
HETATM 2491 O O   . HOH D 4 .   ? 21.695 29.116 25.961  1.000 33.391  0 597 HOH A O   1 
HETATM 2492 O O   . HOH D 4 .   ? 53.317 25.639 7.636   1.000 47.267  0 598 HOH A O   1 
HETATM 2493 O O   . HOH D 4 .   ? 17.241 25.037 11.986  1.000 38.623  0 599 HOH A O   1 
HETATM 2494 O O   . HOH D 4 .   ? 48.209 24.957 12.931  1.000 38.318  0 600 HOH A O   1 
HETATM 2495 O O   . HOH D 4 .   ? 63.956 32.209 -19.127 1.000 41.747  0 601 HOH A O   1 
HETATM 2496 O O   . HOH D 4 .   ? 45.443 13.698 24.868  1.000 52.256  0 602 HOH A O   1 
HETATM 2497 O O   . HOH D 4 .   ? 47.976 30.304 2.609   1.000 44.293  0 603 HOH A O   1 
HETATM 2498 O O   . HOH D 4 .   ? 40.315 34.929 31.745  1.000 57.671  0 604 HOH A O   1 
HETATM 2499 O O   . HOH D 4 .   ? 33.382 13.981 24.912  1.000 51.842  0 605 HOH A O   1 
HETATM 2500 O O   . HOH D 4 .   ? 9.333  36.717 20.400  1.000 52.372  0 606 HOH A O   1 
HETATM 2501 O O   . HOH D 4 .   ? 18.989 40.212 27.475  1.000 62.048  0 607 HOH A O   1 
HETATM 2502 O O   . HOH D 4 .   ? 31.485 45.799 12.241  1.000 51.290  0 608 HOH A O   1 
HETATM 2503 O O   . HOH D 4 .   ? 48.459 19.005 4.728   1.000 56.414  0 609 HOH A O   1 
HETATM 2504 O O   . HOH D 4 .   ? 28.541 46.154 13.128  1.000 48.053  0 610 HOH A O   1 
HETATM 2505 O O   . HOH D 4 .   ? 36.251 44.797 8.097   1.000 65.203  0 611 HOH A O   1 
HETATM 2506 O O   . HOH D 4 .   ? 27.963 46.626 9.549   1.000 40.533  0 612 HOH A O   1 
HETATM 2507 O O   . HOH D 4 .   ? 59.467 24.918 -13.566 1.000 42.600  0 613 HOH A O   1 
HETATM 2508 O O   . HOH D 4 .   ? 42.413 16.025 -6.138  1.000 44.227  0 614 HOH A O   1 
HETATM 2509 O O   . HOH D 4 .   ? 40.402 37.112 28.098  1.000 42.279  0 615 HOH A O   1 
HETATM 2510 O O   . HOH D 4 .   ? 37.672 20.988 19.394  1.000 46.998  0 616 HOH A O   1 
HETATM 2511 O O   . HOH D 4 .   ? 42.761 45.190 19.064  1.000 44.260  0 617 HOH A O   1 
HETATM 2512 O O   . HOH D 4 .   ? 38.514 22.683 39.040  1.000 54.438  0 618 HOH A O   1 
HETATM 2513 O O   . HOH D 4 .   ? 20.064 39.874 21.084  1.000 53.956  0 619 HOH A O   1 
HETATM 2514 O O   . HOH D 4 .   ? 68.034 33.682 -13.573 1.000 40.134  0 620 HOH A O   1 
HETATM 2515 O O   . HOH D 4 .   ? 49.276 41.478 12.336  1.000 49.271  0 621 HOH A O   1 
HETATM 2516 O O   . HOH D 4 .   ? 49.799 45.069 16.122  1.000 55.061  0 622 HOH A O   1 
HETATM 2517 O O   . HOH D 4 .   ? 33.292 18.108 31.731  1.000 52.019  0 623 HOH A O   1 
HETATM 2518 O O   . HOH D 4 .   ? 31.107 44.249 8.190   1.000 24.733  0 624 HOH A O   1 
HETATM 2519 O O   . HOH D 4 .   ? 12.449 36.026 14.523  1.000 55.909  0 625 HOH A O   1 
HETATM 2520 O O   . HOH D 4 .   ? 66.078 25.485 0.072   1.000 50.248  0 626 HOH A O   1 
HETATM 2521 O O   . HOH D 4 .   ? 37.232 19.868 37.348  1.000 60.352  0 627 HOH A O   1 
HETATM 2522 O O   . HOH D 4 .   ? 47.947 43.172 14.238  1.000 34.831  0 628 HOH A O   1 
HETATM 2523 O O   . HOH D 4 .   ? 55.958 30.703 1.219   1.000 47.830  0 629 HOH A O   1 
HETATM 2524 O O   . HOH D 4 .   ? 39.107 39.137 27.299  1.000 54.511  0 630 HOH A O   1 
HETATM 2525 O O   . HOH D 4 .   ? 33.976 43.133 4.446   1.000 58.389  0 631 HOH A O   1 
HETATM 2526 O O   . HOH D 4 .   ? 23.367 12.813 23.803  1.000 59.496  0 632 HOH A O   1 
HETATM 2527 O O   . HOH D 4 .   ? 40.547 14.109 -5.924  1.000 50.295  0 633 HOH A O   1 
HETATM 2528 O O   . HOH D 4 .   ? 41.667 18.167 -7.582  1.000 43.031  0 634 HOH A O   1 
HETATM 2529 O O   . HOH D 4 .   ? 58.764 31.074 1.230   1.000 53.039  0 635 HOH A O   1 
HETATM 2530 O O   . HOH D 4 .   ? 46.147 22.644 16.196  1.000 52.143  0 636 HOH A O   1 
HETATM 2531 O O   . HOH D 4 .   ? 39.216 18.258 36.874  1.000 44.229  0 637 HOH A O   1 
HETATM 2532 O O   . HOH D 4 .   ? 47.720 34.435 6.095   1.000 54.493  0 638 HOH A O   1 
HETATM 2533 O O   . HOH D 4 .   ? 35.356 46.131 10.315  1.000 52.005  0 639 HOH A O   1 
HETATM 2534 O O   . HOH D 4 .   ? 56.744 21.319 -10.746 1.000 54.934  0 640 HOH A O   1 
HETATM 2535 O O   . HOH D 4 .   ? 33.516 44.954 6.253   1.000 53.813  0 641 HOH A O   1 
HETATM 2536 O O   . HOH D 4 .   ? 32.518 46.518 9.641   1.000 50.385  0 642 HOH A O   1 
HETATM 2537 O O   . HOH D 4 .   ? 42.215 53.947 9.287   1.000 52.265  0 643 HOH A O   1 
# 
