data_9BBT
# 
_entry.id   9BBT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BBT         pdb_00009bbt 10.2210/pdb9bbt/pdb 
WWPDB D_1000282099 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-16 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_struct_assembly      
2 2 'Structure model' pdbx_struct_assembly_gen  
3 2 'Structure model' pdbx_struct_assembly_prop 
4 2 'Structure model' pdbx_struct_oper_list     
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_pdbx_struct_assembly.details'             
2 2 'Structure model' '_pdbx_struct_assembly.method_details'      
3 2 'Structure model' '_pdbx_struct_assembly.oligomeric_count'    
4 2 'Structure model' '_pdbx_struct_assembly.oligomeric_details'  
5 2 'Structure model' '_pdbx_struct_assembly_gen.oper_expression' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BBT 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-07 
_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           N 
# 
_pdbx_contact_author.id                 4 
_pdbx_contact_author.email              olsens@uthscsa.edu 
_pdbx_contact_author.name_first         Shaun 
_pdbx_contact_author.name_last          Olsen 
_pdbx_contact_author.name_mi            K 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1265-7101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Afsar, M.'   1 0000-0002-3062-9219 
'Bury, P.'    2 0000-0003-3445-2649 
'Olsen, S.K.' 3 0000-0002-1265-7101 
'Nayak, A.'   4 0000-0001-8735-4132 
# 
_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                     'SARS-CoV-2 Mpro in complex with compound 6f inhibitor' 
_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 'Afsar, M.'   1 0000-0002-3062-9219 
primary 'Bury, P.'    2 0000-0003-3445-2649 
primary 'Olsen, S.K.' 3 0000-0002-1265-7101 
primary 'Nayak, A.'   4 0000-0001-8735-4132 
# 
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 '3C-like proteinase nsp5' 33825.547 1  3.4.22.69 ? ? ? 
2 non-polymer syn 
;N-[(2S)-1-({(2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-3',4'-dimethoxy[1,1'-biphenyl]-4-carboxamide
;
508.609   1  ?         ? ? ? 
3 water       nat water 18.015    22 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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 
;N-[(2S)-1-({(2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-3',4'-dimethoxy[1,1'-biphenyl]-4-carboxamide
;
A1ALH 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     866768 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ALH non-polymer         . 
;N-[(2S)-1-({(2R)-1-imino-3-[(3R)-2-oxopyrrolidin-3-yl]propan-2-yl}amino)-4-methyl-1-oxopentan-2-yl]-3',4'-dimethoxy[1,1'-biphenyl]-4-carboxamide
;
? 'C28 H36 N4 O5'  508.609 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ALA A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ALA A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP 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  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ALA A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ALA A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU ALA A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ALH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ALH 
_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 A1ALH 1  401 401 A1ALH LIG A . 
C 3 HOH   1  501 27  HOH   HOH A . 
C 3 HOH   2  502 22  HOH   HOH A . 
C 3 HOH   3  503 4   HOH   HOH A . 
C 3 HOH   4  504 6   HOH   HOH A . 
C 3 HOH   5  505 2   HOH   HOH A . 
C 3 HOH   6  506 12  HOH   HOH A . 
C 3 HOH   7  507 14  HOH   HOH A . 
C 3 HOH   8  508 3   HOH   HOH A . 
C 3 HOH   9  509 25  HOH   HOH A . 
C 3 HOH   10 510 8   HOH   HOH A . 
C 3 HOH   11 511 21  HOH   HOH A . 
C 3 HOH   12 512 19  HOH   HOH A . 
C 3 HOH   13 513 13  HOH   HOH A . 
C 3 HOH   14 514 23  HOH   HOH A . 
C 3 HOH   15 515 20  HOH   HOH A . 
C 3 HOH   16 516 24  HOH   HOH A . 
C 3 HOH   17 517 7   HOH   HOH A . 
C 3 HOH   18 518 26  HOH   HOH A . 
C 3 HOH   19 519 18  HOH   HOH A . 
C 3 HOH   20 520 17  HOH   HOH A . 
C 3 HOH   21 521 16  HOH   HOH A . 
C 3 HOH   22 522 15  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 ARG 60  ? CG  ? A ARG 60  CG  
2  1 Y 1 A ARG 60  ? CD  ? A ARG 60  CD  
3  1 Y 1 A ARG 60  ? NE  ? A ARG 60  NE  
4  1 Y 1 A ARG 60  ? CZ  ? A ARG 60  CZ  
5  1 Y 1 A ARG 60  ? NH1 ? A ARG 60  NH1 
6  1 Y 1 A ARG 60  ? NH2 ? A ARG 60  NH2 
7  1 Y 1 A ARG 76  ? CG  ? A ARG 76  CG  
8  1 Y 1 A ARG 76  ? CD  ? A ARG 76  CD  
9  1 Y 1 A ARG 76  ? NE  ? A ARG 76  NE  
10 1 Y 1 A ARG 76  ? CZ  ? A ARG 76  CZ  
11 1 Y 1 A ARG 76  ? NH1 ? A ARG 76  NH1 
12 1 Y 1 A ARG 76  ? NH2 ? A ARG 76  NH2 
13 1 Y 1 A ARG 217 ? CG  ? A ARG 217 CG  
14 1 Y 1 A ARG 217 ? CD  ? A ARG 217 CD  
15 1 Y 1 A ARG 217 ? NE  ? A ARG 217 NE  
16 1 Y 1 A ARG 217 ? CZ  ? A ARG 217 CZ  
17 1 Y 1 A ARG 217 ? NH1 ? A ARG 217 NH1 
18 1 Y 1 A ARG 217 ? NH2 ? A ARG 217 NH2 
19 1 Y 1 A ARG 222 ? CG  ? A ARG 222 CG  
20 1 Y 1 A ARG 222 ? CD  ? A ARG 222 CD  
21 1 Y 1 A ARG 222 ? NE  ? A ARG 222 NE  
22 1 Y 1 A ARG 222 ? CZ  ? A ARG 222 CZ  
23 1 Y 1 A ARG 222 ? NH1 ? A ARG 222 NH1 
24 1 Y 1 A ARG 222 ? NH2 ? A ARG 222 NH2 
25 1 Y 1 A GLU 270 ? CG  ? A GLU 270 CG  
26 1 Y 1 A GLU 270 ? CD  ? A GLU 270 CD  
27 1 Y 1 A GLU 270 ? OE1 ? A GLU 270 OE1 
28 1 Y 1 A GLU 270 ? OE2 ? A GLU 270 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   100.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BBT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     115.946 
_cell.length_a_esd                 ? 
_cell.length_b                     53.450 
_cell.length_b_esd                 ? 
_cell.length_c                     45.338 
_cell.length_c_esd                 ? 
_cell.volume                       276498.385 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BBT 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BBT 
_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             2.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.81 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    
'5%(w/v) PEG 20K, 25%(w/v) 1,1,1-tris(hydroxymethyl)propane, 1%(w/v) NDSB 195 0.01 M of each Polyamine 0.1 M GlyGly/AMPD' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 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         2021-11-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.979 
_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        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          56.18 
_reflns.entry_id                                       9BBT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.42 
_reflns.d_resolution_low                               57.26 
_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                                     10615 
_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                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.5 
_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                                0.068 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.159 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.42 
_reflns_shell.d_res_low                                     2.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.7 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1092 
_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                               0.991 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.335 
_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                                  2.354 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               65.13 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BBT 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.57 
_refine.ls_d_res_low                             48.40 
_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                     8262 
_refine.ls_number_reflns_R_free                  827 
_refine.ls_number_reflns_R_work                  7435 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.12 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1937 
_refine.ls_R_factor_R_free                       0.2339 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1891 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 28.4406 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.4087 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.57 
_refine_hist.d_res_low                        48.40 
_refine_hist.number_atoms_solvent             22 
_refine_hist.number_atoms_total               2378 
_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        2319 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_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' ? 0.0039 ? 2410 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6170 ? 3281 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0451 ? 372  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0051 ? 424  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.0235 ? 327  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.57 2.73  . . 107 959  74.44 . . . . 0.3093 . . . . . . . . . . . 0.2952 
'X-RAY DIFFRACTION' 2.73 2.94  . . 144 1304 97.77 . . . . 0.2912 . . . . . . . . . . . 0.3773 
'X-RAY DIFFRACTION' 2.94 3.23  . . 146 1305 98.24 . . . . 0.2232 . . . . . . . . . . . 0.3108 
'X-RAY DIFFRACTION' 3.23 3.70  . . 142 1285 96.81 . . . . 0.2001 . . . . . . . . . . . 0.2762 
'X-RAY DIFFRACTION' 3.70 4.66  . . 144 1292 96.64 . . . . 0.1601 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 4.66 48.40 . . 144 1290 94.22 . . . . 0.1570 . . . . . . . . . . . 0.1893 
# 
_struct.entry_id                     9BBT 
_struct.title                        'SARS-CoV-2 Mpro in complex with compound 6f inhibitor' 
_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        9BBT 
_struct_keywords.text            'Protease, Inhibitor, VIRAL PROTEIN, Hydrolase' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BBT 
_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                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_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       306 
# 
_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)' 5090  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  24880 ? 
# 
_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 
# 
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' 2_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 
# 
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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 TYR A 54  ? ILE A 59  ? TYR A 54  ILE A 59  1 ? 6  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? GLY A 258 ? THR A 243 GLY A 258 1 ? 16 
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        none 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_struct_conn.pdbx_ptnr1_label_alt_id       ? 
_struct_conn.pdbx_ptnr1_PDB_ins_code       ? 
_struct_conn.pdbx_ptnr1_standard_comp_id   ? 
_struct_conn.ptnr1_symmetry                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ALH 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C19 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ALH 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_struct_conn.pdbx_ptnr3_label_atom_id      ? 
_struct_conn.pdbx_ptnr3_label_seq_id       ? 
_struct_conn.pdbx_ptnr3_label_comp_id      ? 
_struct_conn.pdbx_ptnr3_label_asym_id      ? 
_struct_conn.pdbx_ptnr3_label_alt_id       ? 
_struct_conn.pdbx_ptnr3_PDB_ins_code       ? 
_struct_conn.details                       ? 
_struct_conn.pdbx_dist_value               1.629 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ALH 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ALH 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C19 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1ALH 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
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 LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N GLY A 79  ? N GLY A 79  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9BBT 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    NH1 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ARG 
_pdbx_validate_symm_contact.auth_seq_id_1     4 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    LYS 
_pdbx_validate_symm_contact.auth_seq_id_2     137 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 55.63   -136.85 
2 1 ASN A 51  ? ? -152.11 84.52   
3 1 ASN A 84  ? ? 58.07   -120.11 
4 1 LYS A 137 ? ? -104.28 69.96   
5 1 TYR A 154 ? ? 53.43   -92.36  
6 1 HIS A 164 ? ? -130.09 -36.71  
7 1 ARG A 188 ? ? -170.13 126.39  
8 1 ARG A 217 ? ? -145.49 30.53   
9 1 GLU A 290 ? ? -108.56 43.66   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-z 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         12.4011775964 
_pdbx_refine_tls.origin_y         -20.1401603107 
_pdbx_refine_tls.origin_z         4.50022386362 
_pdbx_refine_tls.T[1][1]          0.380750923095 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0188619183311 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0580681457557 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.334641034542 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0335651865496 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.35190540634 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.24337072127 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.466218758378 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0952715059681 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.63052227 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -1.4853051621 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          3.16423937103 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.00491145848009 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0710455031295 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.117882989099 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0210992709402 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.140852301904 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.171347908039 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0270971520066 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.129335020854 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.120723440765 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   C 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    S 
_pdbx_refine_tls_group.end_auth_seq_id     27 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 PHE 305 ? A PHE 305 
2 1 Y 1 A GLN 306 ? A GLN 306 
# 
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 
A1ALH C13  C N S 1   
A1ALH C17  C N N 2   
A1ALH C22  C Y N 3   
A1ALH C24  C Y N 4   
A1ALH C26  C Y N 5   
A1ALH C28  C Y N 6   
A1ALH C02  C N N 7   
A1ALH C04  C N S 8   
A1ALH C05  C N N 9   
A1ALH C06  C N N 10  
A1ALH C07  C N N 11  
A1ALH C08  C N N 12  
A1ALH C09  C N N 13  
A1ALH C11  C N S 14  
A1ALH C12  C N N 15  
A1ALH C14  C N N 16  
A1ALH C16  C N N 17  
A1ALH C19  C N N 18  
A1ALH C23  C Y N 19  
A1ALH C25  C Y N 20  
A1ALH C27  C Y N 21  
A1ALH C29  C Y N 22  
A1ALH C31  C N N 23  
A1ALH C32  C Y N 24  
A1ALH C33  C Y N 25  
A1ALH C35  C N N 26  
A1ALH C36  C Y N 27  
A1ALH C37  C Y N 28  
A1ALH N03  N N N 29  
A1ALH N10  N N N 30  
A1ALH N15  N N N 31  
A1ALH N20  N N N 32  
A1ALH O01  O N N 33  
A1ALH O18  O N N 34  
A1ALH O21  O N N 35  
A1ALH O30  O N N 36  
A1ALH O34  O N N 37  
A1ALH H131 H N N 38  
A1ALH H172 H N N 39  
A1ALH H171 H N N 40  
A1ALH H241 H N N 41  
A1ALH H041 H N N 42  
A1ALH H051 H N N 43  
A1ALH H052 H N N 44  
A1ALH H061 H N N 45  
A1ALH H073 H N N 46  
A1ALH H071 H N N 47  
A1ALH H072 H N N 48  
A1ALH H082 H N N 49  
A1ALH H083 H N N 50  
A1ALH H081 H N N 51  
A1ALH H111 H N N 52  
A1ALH H121 H N N 53  
A1ALH H122 H N N 54  
A1ALH H162 H N N 55  
A1ALH H161 H N N 56  
A1ALH H191 H N N 57  
A1ALH H231 H N N 58  
A1ALH H271 H N N 59  
A1ALH H312 H N N 60  
A1ALH H311 H N N 61  
A1ALH H313 H N N 62  
A1ALH H321 H N N 63  
A1ALH H331 H N N 64  
A1ALH H351 H N N 65  
A1ALH H353 H N N 66  
A1ALH H352 H N N 67  
A1ALH H361 H N N 68  
A1ALH H371 H N N 69  
A1ALH H031 H N N 70  
A1ALH H101 H N N 71  
A1ALH H151 H N N 72  
A1ALH H201 H N N 73  
ALA   N    N N N 74  
ALA   CA   C N S 75  
ALA   C    C N N 76  
ALA   O    O N N 77  
ALA   CB   C N N 78  
ALA   OXT  O N N 79  
ALA   H    H N N 80  
ALA   H2   H N N 81  
ALA   HA   H N N 82  
ALA   HB1  H N N 83  
ALA   HB2  H N N 84  
ALA   HB3  H N N 85  
ALA   HXT  H N N 86  
ARG   N    N N N 87  
ARG   CA   C N S 88  
ARG   C    C N N 89  
ARG   O    O N N 90  
ARG   CB   C N N 91  
ARG   CG   C N N 92  
ARG   CD   C N N 93  
ARG   NE   N N N 94  
ARG   CZ   C N N 95  
ARG   NH1  N N N 96  
ARG   NH2  N N N 97  
ARG   OXT  O N N 98  
ARG   H    H N N 99  
ARG   H2   H N N 100 
ARG   HA   H N N 101 
ARG   HB2  H N N 102 
ARG   HB3  H N N 103 
ARG   HG2  H N N 104 
ARG   HG3  H N N 105 
ARG   HD2  H N N 106 
ARG   HD3  H N N 107 
ARG   HE   H N N 108 
ARG   HH11 H N N 109 
ARG   HH12 H N N 110 
ARG   HH21 H N N 111 
ARG   HH22 H N N 112 
ARG   HXT  H N N 113 
ASN   N    N N N 114 
ASN   CA   C N S 115 
ASN   C    C N N 116 
ASN   O    O N N 117 
ASN   CB   C N N 118 
ASN   CG   C N N 119 
ASN   OD1  O N N 120 
ASN   ND2  N N N 121 
ASN   OXT  O N N 122 
ASN   H    H N N 123 
ASN   H2   H N N 124 
ASN   HA   H N N 125 
ASN   HB2  H N N 126 
ASN   HB3  H N N 127 
ASN   HD21 H N N 128 
ASN   HD22 H N N 129 
ASN   HXT  H N N 130 
ASP   N    N N N 131 
ASP   CA   C N S 132 
ASP   C    C N N 133 
ASP   O    O N N 134 
ASP   CB   C N N 135 
ASP   CG   C N N 136 
ASP   OD1  O N N 137 
ASP   OD2  O N N 138 
ASP   OXT  O N N 139 
ASP   H    H N N 140 
ASP   H2   H N N 141 
ASP   HA   H N N 142 
ASP   HB2  H N N 143 
ASP   HB3  H N N 144 
ASP   HD2  H N N 145 
ASP   HXT  H N N 146 
CYS   N    N N N 147 
CYS   CA   C N R 148 
CYS   C    C N N 149 
CYS   O    O N N 150 
CYS   CB   C N N 151 
CYS   SG   S N N 152 
CYS   OXT  O N N 153 
CYS   H    H N N 154 
CYS   H2   H N N 155 
CYS   HA   H N N 156 
CYS   HB2  H N N 157 
CYS   HB3  H N N 158 
CYS   HG   H N N 159 
CYS   HXT  H N N 160 
GLN   N    N N N 161 
GLN   CA   C N S 162 
GLN   C    C N N 163 
GLN   O    O N N 164 
GLN   CB   C N N 165 
GLN   CG   C N N 166 
GLN   CD   C N N 167 
GLN   OE1  O N N 168 
GLN   NE2  N N N 169 
GLN   OXT  O N N 170 
GLN   H    H N N 171 
GLN   H2   H N N 172 
GLN   HA   H N N 173 
GLN   HB2  H N N 174 
GLN   HB3  H N N 175 
GLN   HG2  H N N 176 
GLN   HG3  H N N 177 
GLN   HE21 H N N 178 
GLN   HE22 H N N 179 
GLN   HXT  H N N 180 
GLU   N    N N N 181 
GLU   CA   C N S 182 
GLU   C    C N N 183 
GLU   O    O N N 184 
GLU   CB   C N N 185 
GLU   CG   C N N 186 
GLU   CD   C N N 187 
GLU   OE1  O N N 188 
GLU   OE2  O N N 189 
GLU   OXT  O N N 190 
GLU   H    H N N 191 
GLU   H2   H N N 192 
GLU   HA   H N N 193 
GLU   HB2  H N N 194 
GLU   HB3  H N N 195 
GLU   HG2  H N N 196 
GLU   HG3  H N N 197 
GLU   HE2  H N N 198 
GLU   HXT  H N N 199 
GLY   N    N N N 200 
GLY   CA   C N N 201 
GLY   C    C N N 202 
GLY   O    O N N 203 
GLY   OXT  O N N 204 
GLY   H    H N N 205 
GLY   H2   H N N 206 
GLY   HA2  H N N 207 
GLY   HA3  H N N 208 
GLY   HXT  H N N 209 
HIS   N    N N N 210 
HIS   CA   C N S 211 
HIS   C    C N N 212 
HIS   O    O N N 213 
HIS   CB   C N N 214 
HIS   CG   C Y N 215 
HIS   ND1  N Y N 216 
HIS   CD2  C Y N 217 
HIS   CE1  C Y N 218 
HIS   NE2  N Y N 219 
HIS   OXT  O N N 220 
HIS   H    H N N 221 
HIS   H2   H N N 222 
HIS   HA   H N N 223 
HIS   HB2  H N N 224 
HIS   HB3  H N N 225 
HIS   HD1  H N N 226 
HIS   HD2  H N N 227 
HIS   HE1  H N N 228 
HIS   HE2  H N N 229 
HIS   HXT  H N N 230 
HOH   O    O N N 231 
HOH   H1   H N N 232 
HOH   H2   H N N 233 
ILE   N    N N N 234 
ILE   CA   C N S 235 
ILE   C    C N N 236 
ILE   O    O N N 237 
ILE   CB   C N S 238 
ILE   CG1  C N N 239 
ILE   CG2  C N N 240 
ILE   CD1  C N N 241 
ILE   OXT  O N N 242 
ILE   H    H N N 243 
ILE   H2   H N N 244 
ILE   HA   H N N 245 
ILE   HB   H N N 246 
ILE   HG12 H N N 247 
ILE   HG13 H N N 248 
ILE   HG21 H N N 249 
ILE   HG22 H N N 250 
ILE   HG23 H N N 251 
ILE   HD11 H N N 252 
ILE   HD12 H N N 253 
ILE   HD13 H N N 254 
ILE   HXT  H N N 255 
LEU   N    N N N 256 
LEU   CA   C N S 257 
LEU   C    C N N 258 
LEU   O    O N N 259 
LEU   CB   C N N 260 
LEU   CG   C N N 261 
LEU   CD1  C N N 262 
LEU   CD2  C N N 263 
LEU   OXT  O N N 264 
LEU   H    H N N 265 
LEU   H2   H N N 266 
LEU   HA   H N N 267 
LEU   HB2  H N N 268 
LEU   HB3  H N N 269 
LEU   HG   H N N 270 
LEU   HD11 H N N 271 
LEU   HD12 H N N 272 
LEU   HD13 H N N 273 
LEU   HD21 H N N 274 
LEU   HD22 H N N 275 
LEU   HD23 H N N 276 
LEU   HXT  H N N 277 
LYS   N    N N N 278 
LYS   CA   C N S 279 
LYS   C    C N N 280 
LYS   O    O N N 281 
LYS   CB   C N N 282 
LYS   CG   C N N 283 
LYS   CD   C N N 284 
LYS   CE   C N N 285 
LYS   NZ   N N N 286 
LYS   OXT  O N N 287 
LYS   H    H N N 288 
LYS   H2   H N N 289 
LYS   HA   H N N 290 
LYS   HB2  H N N 291 
LYS   HB3  H N N 292 
LYS   HG2  H N N 293 
LYS   HG3  H N N 294 
LYS   HD2  H N N 295 
LYS   HD3  H N N 296 
LYS   HE2  H N N 297 
LYS   HE3  H N N 298 
LYS   HZ1  H N N 299 
LYS   HZ2  H N N 300 
LYS   HZ3  H N N 301 
LYS   HXT  H N N 302 
MET   N    N N N 303 
MET   CA   C N S 304 
MET   C    C N N 305 
MET   O    O N N 306 
MET   CB   C N N 307 
MET   CG   C N N 308 
MET   SD   S N N 309 
MET   CE   C N N 310 
MET   OXT  O N N 311 
MET   H    H N N 312 
MET   H2   H N N 313 
MET   HA   H N N 314 
MET   HB2  H N N 315 
MET   HB3  H N N 316 
MET   HG2  H N N 317 
MET   HG3  H N N 318 
MET   HE1  H N N 319 
MET   HE2  H N N 320 
MET   HE3  H N N 321 
MET   HXT  H N N 322 
PHE   N    N N N 323 
PHE   CA   C N S 324 
PHE   C    C N N 325 
PHE   O    O N N 326 
PHE   CB   C N N 327 
PHE   CG   C Y N 328 
PHE   CD1  C Y N 329 
PHE   CD2  C Y N 330 
PHE   CE1  C Y N 331 
PHE   CE2  C Y N 332 
PHE   CZ   C Y N 333 
PHE   OXT  O N N 334 
PHE   H    H N N 335 
PHE   H2   H N N 336 
PHE   HA   H N N 337 
PHE   HB2  H N N 338 
PHE   HB3  H N N 339 
PHE   HD1  H N N 340 
PHE   HD2  H N N 341 
PHE   HE1  H N N 342 
PHE   HE2  H N N 343 
PHE   HZ   H N N 344 
PHE   HXT  H N N 345 
PRO   N    N N N 346 
PRO   CA   C N S 347 
PRO   C    C N N 348 
PRO   O    O N N 349 
PRO   CB   C N N 350 
PRO   CG   C N N 351 
PRO   CD   C N N 352 
PRO   OXT  O N N 353 
PRO   H    H N N 354 
PRO   HA   H N N 355 
PRO   HB2  H N N 356 
PRO   HB3  H N N 357 
PRO   HG2  H N N 358 
PRO   HG3  H N N 359 
PRO   HD2  H N N 360 
PRO   HD3  H N N 361 
PRO   HXT  H N N 362 
SER   N    N N N 363 
SER   CA   C N S 364 
SER   C    C N N 365 
SER   O    O N N 366 
SER   CB   C N N 367 
SER   OG   O N N 368 
SER   OXT  O N N 369 
SER   H    H N N 370 
SER   H2   H N N 371 
SER   HA   H N N 372 
SER   HB2  H N N 373 
SER   HB3  H N N 374 
SER   HG   H N N 375 
SER   HXT  H N N 376 
THR   N    N N N 377 
THR   CA   C N S 378 
THR   C    C N N 379 
THR   O    O N N 380 
THR   CB   C N R 381 
THR   OG1  O N N 382 
THR   CG2  C N N 383 
THR   OXT  O N N 384 
THR   H    H N N 385 
THR   H2   H N N 386 
THR   HA   H N N 387 
THR   HB   H N N 388 
THR   HG1  H N N 389 
THR   HG21 H N N 390 
THR   HG22 H N N 391 
THR   HG23 H N N 392 
THR   HXT  H N N 393 
TRP   N    N N N 394 
TRP   CA   C N S 395 
TRP   C    C N N 396 
TRP   O    O N N 397 
TRP   CB   C N N 398 
TRP   CG   C Y N 399 
TRP   CD1  C Y N 400 
TRP   CD2  C Y N 401 
TRP   NE1  N Y N 402 
TRP   CE2  C Y N 403 
TRP   CE3  C Y N 404 
TRP   CZ2  C Y N 405 
TRP   CZ3  C Y N 406 
TRP   CH2  C Y N 407 
TRP   OXT  O N N 408 
TRP   H    H N N 409 
TRP   H2   H N N 410 
TRP   HA   H N N 411 
TRP   HB2  H N N 412 
TRP   HB3  H N N 413 
TRP   HD1  H N N 414 
TRP   HE1  H N N 415 
TRP   HE3  H N N 416 
TRP   HZ2  H N N 417 
TRP   HZ3  H N N 418 
TRP   HH2  H N N 419 
TRP   HXT  H N N 420 
TYR   N    N N N 421 
TYR   CA   C N S 422 
TYR   C    C N N 423 
TYR   O    O N N 424 
TYR   CB   C N N 425 
TYR   CG   C Y N 426 
TYR   CD1  C Y N 427 
TYR   CD2  C Y N 428 
TYR   CE1  C Y N 429 
TYR   CE2  C Y N 430 
TYR   CZ   C Y N 431 
TYR   OH   O N N 432 
TYR   OXT  O N N 433 
TYR   H    H N N 434 
TYR   H2   H N N 435 
TYR   HA   H N N 436 
TYR   HB2  H N N 437 
TYR   HB3  H N N 438 
TYR   HD1  H N N 439 
TYR   HD2  H N N 440 
TYR   HE1  H N N 441 
TYR   HE2  H N N 442 
TYR   HH   H N N 443 
TYR   HXT  H N N 444 
VAL   N    N N N 445 
VAL   CA   C N S 446 
VAL   C    C N N 447 
VAL   O    O N N 448 
VAL   CB   C N N 449 
VAL   CG1  C N N 450 
VAL   CG2  C N N 451 
VAL   OXT  O N N 452 
VAL   H    H N N 453 
VAL   H2   H N N 454 
VAL   HA   H N N 455 
VAL   HB   H N N 456 
VAL   HG11 H N N 457 
VAL   HG12 H N N 458 
VAL   HG13 H N N 459 
VAL   HG21 H N N 460 
VAL   HG22 H N N 461 
VAL   HG23 H N N 462 
VAL   HXT  H N N 463 
# 
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 
A1ALH C02 O01  doub N N 1   
A1ALH C04 N03  sing N N 2   
A1ALH C06 C05  sing N N 3   
A1ALH C07 C06  sing N N 4   
A1ALH C08 C06  sing N N 5   
A1ALH C05 C04  sing N N 6   
A1ALH C09 C04  sing N N 7   
A1ALH C11 N10  sing N N 8   
A1ALH C13 C12  sing N N 9   
A1ALH C14 C13  sing N N 10  
A1ALH C16 N15  sing N N 11  
A1ALH C17 C16  sing N N 12  
A1ALH N15 C14  sing N N 13  
A1ALH O18 C14  doub N N 14  
A1ALH C12 C11  sing N N 15  
A1ALH C19 C11  sing N N 16  
A1ALH N20 C19  doub N N 17  
A1ALH N10 C09  sing N N 18  
A1ALH O21 C09  doub N N 19  
A1ALH N03 C02  sing N N 20  
A1ALH C22 C02  sing N N 21  
A1ALH C23 C22  doub Y N 22  
A1ALH C24 C23  sing Y N 23  
A1ALH C25 C24  doub Y N 24  
A1ALH C27 C26  doub Y N 25  
A1ALH C28 C27  sing Y N 26  
A1ALH C31 O30  sing N N 27  
A1ALH O30 C29  sing N N 28  
A1ALH C32 C29  sing Y N 29  
A1ALH C33 C32  doub Y N 30  
A1ALH C29 C28  doub Y N 31  
A1ALH O34 C28  sing N N 32  
A1ALH C35 O34  sing N N 33  
A1ALH C26 C25  sing N N 34  
A1ALH C36 C25  sing Y N 35  
A1ALH C37 C36  doub Y N 36  
A1ALH C13 C17  sing N N 37  
A1ALH C22 C37  sing Y N 38  
A1ALH C26 C33  sing Y N 39  
A1ALH C13 H131 sing N N 40  
A1ALH C17 H172 sing N N 41  
A1ALH C17 H171 sing N N 42  
A1ALH C24 H241 sing N N 43  
A1ALH C04 H041 sing N N 44  
A1ALH C05 H051 sing N N 45  
A1ALH C05 H052 sing N N 46  
A1ALH C06 H061 sing N N 47  
A1ALH C07 H073 sing N N 48  
A1ALH C07 H071 sing N N 49  
A1ALH C07 H072 sing N N 50  
A1ALH C08 H082 sing N N 51  
A1ALH C08 H083 sing N N 52  
A1ALH C08 H081 sing N N 53  
A1ALH C11 H111 sing N N 54  
A1ALH C12 H121 sing N N 55  
A1ALH C12 H122 sing N N 56  
A1ALH C16 H162 sing N N 57  
A1ALH C16 H161 sing N N 58  
A1ALH C19 H191 sing N N 59  
A1ALH C23 H231 sing N N 60  
A1ALH C27 H271 sing N N 61  
A1ALH C31 H312 sing N N 62  
A1ALH C31 H311 sing N N 63  
A1ALH C31 H313 sing N N 64  
A1ALH C32 H321 sing N N 65  
A1ALH C33 H331 sing N N 66  
A1ALH C35 H351 sing N N 67  
A1ALH C35 H353 sing N N 68  
A1ALH C35 H352 sing N N 69  
A1ALH C36 H361 sing N N 70  
A1ALH C37 H371 sing N N 71  
A1ALH N03 H031 sing N N 72  
A1ALH N10 H101 sing N N 73  
A1ALH N15 H151 sing N N 74  
A1ALH N20 H201 sing N N 75  
ALA   N   CA   sing N N 76  
ALA   N   H    sing N N 77  
ALA   N   H2   sing N N 78  
ALA   CA  C    sing N N 79  
ALA   CA  CB   sing N N 80  
ALA   CA  HA   sing N N 81  
ALA   C   O    doub N N 82  
ALA   C   OXT  sing N N 83  
ALA   CB  HB1  sing N N 84  
ALA   CB  HB2  sing N N 85  
ALA   CB  HB3  sing N N 86  
ALA   OXT HXT  sing N N 87  
ARG   N   CA   sing N N 88  
ARG   N   H    sing N N 89  
ARG   N   H2   sing N N 90  
ARG   CA  C    sing N N 91  
ARG   CA  CB   sing N N 92  
ARG   CA  HA   sing N N 93  
ARG   C   O    doub N N 94  
ARG   C   OXT  sing N N 95  
ARG   CB  CG   sing N N 96  
ARG   CB  HB2  sing N N 97  
ARG   CB  HB3  sing N N 98  
ARG   CG  CD   sing N N 99  
ARG   CG  HG2  sing N N 100 
ARG   CG  HG3  sing N N 101 
ARG   CD  NE   sing N N 102 
ARG   CD  HD2  sing N N 103 
ARG   CD  HD3  sing N N 104 
ARG   NE  CZ   sing N N 105 
ARG   NE  HE   sing N N 106 
ARG   CZ  NH1  sing N N 107 
ARG   CZ  NH2  doub N N 108 
ARG   NH1 HH11 sing N N 109 
ARG   NH1 HH12 sing N N 110 
ARG   NH2 HH21 sing N N 111 
ARG   NH2 HH22 sing N N 112 
ARG   OXT HXT  sing N N 113 
ASN   N   CA   sing N N 114 
ASN   N   H    sing N N 115 
ASN   N   H2   sing N N 116 
ASN   CA  C    sing N N 117 
ASN   CA  CB   sing N N 118 
ASN   CA  HA   sing N N 119 
ASN   C   O    doub N N 120 
ASN   C   OXT  sing N N 121 
ASN   CB  CG   sing N N 122 
ASN   CB  HB2  sing N N 123 
ASN   CB  HB3  sing N N 124 
ASN   CG  OD1  doub N N 125 
ASN   CG  ND2  sing N N 126 
ASN   ND2 HD21 sing N N 127 
ASN   ND2 HD22 sing N N 128 
ASN   OXT HXT  sing N N 129 
ASP   N   CA   sing N N 130 
ASP   N   H    sing N N 131 
ASP   N   H2   sing N N 132 
ASP   CA  C    sing N N 133 
ASP   CA  CB   sing N N 134 
ASP   CA  HA   sing N N 135 
ASP   C   O    doub N N 136 
ASP   C   OXT  sing N N 137 
ASP   CB  CG   sing N N 138 
ASP   CB  HB2  sing N N 139 
ASP   CB  HB3  sing N N 140 
ASP   CG  OD1  doub N N 141 
ASP   CG  OD2  sing N N 142 
ASP   OD2 HD2  sing N N 143 
ASP   OXT HXT  sing N N 144 
CYS   N   CA   sing N N 145 
CYS   N   H    sing N N 146 
CYS   N   H2   sing N N 147 
CYS   CA  C    sing N N 148 
CYS   CA  CB   sing N N 149 
CYS   CA  HA   sing N N 150 
CYS   C   O    doub N N 151 
CYS   C   OXT  sing N N 152 
CYS   CB  SG   sing N N 153 
CYS   CB  HB2  sing N N 154 
CYS   CB  HB3  sing N N 155 
CYS   SG  HG   sing N N 156 
CYS   OXT HXT  sing N N 157 
GLN   N   CA   sing N N 158 
GLN   N   H    sing N N 159 
GLN   N   H2   sing N N 160 
GLN   CA  C    sing N N 161 
GLN   CA  CB   sing N N 162 
GLN   CA  HA   sing N N 163 
GLN   C   O    doub N N 164 
GLN   C   OXT  sing N N 165 
GLN   CB  CG   sing N N 166 
GLN   CB  HB2  sing N N 167 
GLN   CB  HB3  sing N N 168 
GLN   CG  CD   sing N N 169 
GLN   CG  HG2  sing N N 170 
GLN   CG  HG3  sing N N 171 
GLN   CD  OE1  doub N N 172 
GLN   CD  NE2  sing N N 173 
GLN   NE2 HE21 sing N N 174 
GLN   NE2 HE22 sing N N 175 
GLN   OXT HXT  sing N N 176 
GLU   N   CA   sing N N 177 
GLU   N   H    sing N N 178 
GLU   N   H2   sing N N 179 
GLU   CA  C    sing N N 180 
GLU   CA  CB   sing N N 181 
GLU   CA  HA   sing N N 182 
GLU   C   O    doub N N 183 
GLU   C   OXT  sing N N 184 
GLU   CB  CG   sing N N 185 
GLU   CB  HB2  sing N N 186 
GLU   CB  HB3  sing N N 187 
GLU   CG  CD   sing N N 188 
GLU   CG  HG2  sing N N 189 
GLU   CG  HG3  sing N N 190 
GLU   CD  OE1  doub N N 191 
GLU   CD  OE2  sing N N 192 
GLU   OE2 HE2  sing N N 193 
GLU   OXT HXT  sing N N 194 
GLY   N   CA   sing N N 195 
GLY   N   H    sing N N 196 
GLY   N   H2   sing N N 197 
GLY   CA  C    sing N N 198 
GLY   CA  HA2  sing N N 199 
GLY   CA  HA3  sing N N 200 
GLY   C   O    doub N N 201 
GLY   C   OXT  sing N N 202 
GLY   OXT HXT  sing N N 203 
HIS   N   CA   sing N N 204 
HIS   N   H    sing N N 205 
HIS   N   H2   sing N N 206 
HIS   CA  C    sing N N 207 
HIS   CA  CB   sing N N 208 
HIS   CA  HA   sing N N 209 
HIS   C   O    doub N N 210 
HIS   C   OXT  sing N N 211 
HIS   CB  CG   sing N N 212 
HIS   CB  HB2  sing N N 213 
HIS   CB  HB3  sing N N 214 
HIS   CG  ND1  sing Y N 215 
HIS   CG  CD2  doub Y N 216 
HIS   ND1 CE1  doub Y N 217 
HIS   ND1 HD1  sing N N 218 
HIS   CD2 NE2  sing Y N 219 
HIS   CD2 HD2  sing N N 220 
HIS   CE1 NE2  sing Y N 221 
HIS   CE1 HE1  sing N N 222 
HIS   NE2 HE2  sing N N 223 
HIS   OXT HXT  sing N N 224 
HOH   O   H1   sing N N 225 
HOH   O   H2   sing N N 226 
ILE   N   CA   sing N N 227 
ILE   N   H    sing N N 228 
ILE   N   H2   sing N N 229 
ILE   CA  C    sing N N 230 
ILE   CA  CB   sing N N 231 
ILE   CA  HA   sing N N 232 
ILE   C   O    doub N N 233 
ILE   C   OXT  sing N N 234 
ILE   CB  CG1  sing N N 235 
ILE   CB  CG2  sing N N 236 
ILE   CB  HB   sing N N 237 
ILE   CG1 CD1  sing N N 238 
ILE   CG1 HG12 sing N N 239 
ILE   CG1 HG13 sing N N 240 
ILE   CG2 HG21 sing N N 241 
ILE   CG2 HG22 sing N N 242 
ILE   CG2 HG23 sing N N 243 
ILE   CD1 HD11 sing N N 244 
ILE   CD1 HD12 sing N N 245 
ILE   CD1 HD13 sing N N 246 
ILE   OXT HXT  sing N N 247 
LEU   N   CA   sing N N 248 
LEU   N   H    sing N N 249 
LEU   N   H2   sing N N 250 
LEU   CA  C    sing N N 251 
LEU   CA  CB   sing N N 252 
LEU   CA  HA   sing N N 253 
LEU   C   O    doub N N 254 
LEU   C   OXT  sing N N 255 
LEU   CB  CG   sing N N 256 
LEU   CB  HB2  sing N N 257 
LEU   CB  HB3  sing N N 258 
LEU   CG  CD1  sing N N 259 
LEU   CG  CD2  sing N N 260 
LEU   CG  HG   sing N N 261 
LEU   CD1 HD11 sing N N 262 
LEU   CD1 HD12 sing N N 263 
LEU   CD1 HD13 sing N N 264 
LEU   CD2 HD21 sing N N 265 
LEU   CD2 HD22 sing N N 266 
LEU   CD2 HD23 sing N N 267 
LEU   OXT HXT  sing N N 268 
LYS   N   CA   sing N N 269 
LYS   N   H    sing N N 270 
LYS   N   H2   sing N N 271 
LYS   CA  C    sing N N 272 
LYS   CA  CB   sing N N 273 
LYS   CA  HA   sing N N 274 
LYS   C   O    doub N N 275 
LYS   C   OXT  sing N N 276 
LYS   CB  CG   sing N N 277 
LYS   CB  HB2  sing N N 278 
LYS   CB  HB3  sing N N 279 
LYS   CG  CD   sing N N 280 
LYS   CG  HG2  sing N N 281 
LYS   CG  HG3  sing N N 282 
LYS   CD  CE   sing N N 283 
LYS   CD  HD2  sing N N 284 
LYS   CD  HD3  sing N N 285 
LYS   CE  NZ   sing N N 286 
LYS   CE  HE2  sing N N 287 
LYS   CE  HE3  sing N N 288 
LYS   NZ  HZ1  sing N N 289 
LYS   NZ  HZ2  sing N N 290 
LYS   NZ  HZ3  sing N N 291 
LYS   OXT HXT  sing N N 292 
MET   N   CA   sing N N 293 
MET   N   H    sing N N 294 
MET   N   H2   sing N N 295 
MET   CA  C    sing N N 296 
MET   CA  CB   sing N N 297 
MET   CA  HA   sing N N 298 
MET   C   O    doub N N 299 
MET   C   OXT  sing N N 300 
MET   CB  CG   sing N N 301 
MET   CB  HB2  sing N N 302 
MET   CB  HB3  sing N N 303 
MET   CG  SD   sing N N 304 
MET   CG  HG2  sing N N 305 
MET   CG  HG3  sing N N 306 
MET   SD  CE   sing N N 307 
MET   CE  HE1  sing N N 308 
MET   CE  HE2  sing N N 309 
MET   CE  HE3  sing N N 310 
MET   OXT HXT  sing N N 311 
PHE   N   CA   sing N N 312 
PHE   N   H    sing N N 313 
PHE   N   H2   sing N N 314 
PHE   CA  C    sing N N 315 
PHE   CA  CB   sing N N 316 
PHE   CA  HA   sing N N 317 
PHE   C   O    doub N N 318 
PHE   C   OXT  sing N N 319 
PHE   CB  CG   sing N N 320 
PHE   CB  HB2  sing N N 321 
PHE   CB  HB3  sing N N 322 
PHE   CG  CD1  doub Y N 323 
PHE   CG  CD2  sing Y N 324 
PHE   CD1 CE1  sing Y N 325 
PHE   CD1 HD1  sing N N 326 
PHE   CD2 CE2  doub Y N 327 
PHE   CD2 HD2  sing N N 328 
PHE   CE1 CZ   doub Y N 329 
PHE   CE1 HE1  sing N N 330 
PHE   CE2 CZ   sing Y N 331 
PHE   CE2 HE2  sing N N 332 
PHE   CZ  HZ   sing N N 333 
PHE   OXT HXT  sing N N 334 
PRO   N   CA   sing N N 335 
PRO   N   CD   sing N N 336 
PRO   N   H    sing N N 337 
PRO   CA  C    sing N N 338 
PRO   CA  CB   sing N N 339 
PRO   CA  HA   sing N N 340 
PRO   C   O    doub N N 341 
PRO   C   OXT  sing N N 342 
PRO   CB  CG   sing N N 343 
PRO   CB  HB2  sing N N 344 
PRO   CB  HB3  sing N N 345 
PRO   CG  CD   sing N N 346 
PRO   CG  HG2  sing N N 347 
PRO   CG  HG3  sing N N 348 
PRO   CD  HD2  sing N N 349 
PRO   CD  HD3  sing N N 350 
PRO   OXT HXT  sing N N 351 
SER   N   CA   sing N N 352 
SER   N   H    sing N N 353 
SER   N   H2   sing N N 354 
SER   CA  C    sing N N 355 
SER   CA  CB   sing N N 356 
SER   CA  HA   sing N N 357 
SER   C   O    doub N N 358 
SER   C   OXT  sing N N 359 
SER   CB  OG   sing N N 360 
SER   CB  HB2  sing N N 361 
SER   CB  HB3  sing N N 362 
SER   OG  HG   sing N N 363 
SER   OXT HXT  sing N N 364 
THR   N   CA   sing N N 365 
THR   N   H    sing N N 366 
THR   N   H2   sing N N 367 
THR   CA  C    sing N N 368 
THR   CA  CB   sing N N 369 
THR   CA  HA   sing N N 370 
THR   C   O    doub N N 371 
THR   C   OXT  sing N N 372 
THR   CB  OG1  sing N N 373 
THR   CB  CG2  sing N N 374 
THR   CB  HB   sing N N 375 
THR   OG1 HG1  sing N N 376 
THR   CG2 HG21 sing N N 377 
THR   CG2 HG22 sing N N 378 
THR   CG2 HG23 sing N N 379 
THR   OXT HXT  sing N N 380 
TRP   N   CA   sing N N 381 
TRP   N   H    sing N N 382 
TRP   N   H2   sing N N 383 
TRP   CA  C    sing N N 384 
TRP   CA  CB   sing N N 385 
TRP   CA  HA   sing N N 386 
TRP   C   O    doub N N 387 
TRP   C   OXT  sing N N 388 
TRP   CB  CG   sing N N 389 
TRP   CB  HB2  sing N N 390 
TRP   CB  HB3  sing N N 391 
TRP   CG  CD1  doub Y N 392 
TRP   CG  CD2  sing Y N 393 
TRP   CD1 NE1  sing Y N 394 
TRP   CD1 HD1  sing N N 395 
TRP   CD2 CE2  doub Y N 396 
TRP   CD2 CE3  sing Y N 397 
TRP   NE1 CE2  sing Y N 398 
TRP   NE1 HE1  sing N N 399 
TRP   CE2 CZ2  sing Y N 400 
TRP   CE3 CZ3  doub Y N 401 
TRP   CE3 HE3  sing N N 402 
TRP   CZ2 CH2  doub Y N 403 
TRP   CZ2 HZ2  sing N N 404 
TRP   CZ3 CH2  sing Y N 405 
TRP   CZ3 HZ3  sing N N 406 
TRP   CH2 HH2  sing N N 407 
TRP   OXT HXT  sing N N 408 
TYR   N   CA   sing N N 409 
TYR   N   H    sing N N 410 
TYR   N   H2   sing N N 411 
TYR   CA  C    sing N N 412 
TYR   CA  CB   sing N N 413 
TYR   CA  HA   sing N N 414 
TYR   C   O    doub N N 415 
TYR   C   OXT  sing N N 416 
TYR   CB  CG   sing N N 417 
TYR   CB  HB2  sing N N 418 
TYR   CB  HB3  sing N N 419 
TYR   CG  CD1  doub Y N 420 
TYR   CG  CD2  sing Y N 421 
TYR   CD1 CE1  sing Y N 422 
TYR   CD1 HD1  sing N N 423 
TYR   CD2 CE2  doub Y N 424 
TYR   CD2 HD2  sing N N 425 
TYR   CE1 CZ   doub Y N 426 
TYR   CE1 HE1  sing N N 427 
TYR   CE2 CZ   sing Y N 428 
TYR   CE2 HE2  sing N N 429 
TYR   CZ  OH   sing N N 430 
TYR   OH  HH   sing N N 431 
TYR   OXT HXT  sing N N 432 
VAL   N   CA   sing N N 433 
VAL   N   H    sing N N 434 
VAL   N   H2   sing N N 435 
VAL   CA  C    sing N N 436 
VAL   CA  CB   sing N N 437 
VAL   CA  HA   sing N N 438 
VAL   C   O    doub N N 439 
VAL   C   OXT  sing N N 440 
VAL   CB  CG1  sing N N 441 
VAL   CB  CG2  sing N N 442 
VAL   CB  HB   sing N N 443 
VAL   CG1 HG11 sing N N 444 
VAL   CG1 HG12 sing N N 445 
VAL   CG1 HG13 sing N N 446 
VAL   CG2 HG21 sing N N 447 
VAL   CG2 HG22 sing N N 448 
VAL   CG2 HG23 sing N N 449 
VAL   OXT HXT  sing N N 450 
# 
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 General Medical Sciences (NIH/NIGMS)' 'United States' R01GM115568 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' R01GM128731 2 
'Cancer Prevention and Research Institute of Texas (CPRIT)'                                'United States' RR200030    3 
# 
_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   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BBT 
_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]   0.008625 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001558 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018709 
_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]   0.022414 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . SER   A 1 1   ? -4.47402 -16.30707 -16.25529 1.000 69.32297  ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -3.19169 -15.61796 -16.30541 1.000 70.30805  ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -3.11647 -14.55907 -15.21550 1.000 66.78649  ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -3.15544 -13.36323 -15.50095 1.000 71.63316  ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -2.97610 -14.98775 -17.68342 1.000 77.75320  ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -2.70001 -15.97861 -18.66040 1.000 76.67667  ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? -3.02931 -15.01083 -13.96355 1.000 63.29391  ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? -2.86693 -14.13797 -12.82362 1.000 60.23953  ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? -1.51883 -14.35848 -12.15796 1.000 57.61493  ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? -0.67170 -15.10510 -12.65302 1.000 62.26002  ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? -1.33502 -13.69273 -11.01748 1.000 52.49550  ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? -0.10203 -13.83246 -10.24813 1.000 54.70382  ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? -0.40655 -13.73160 -8.76298  1.000 52.13565  ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? -0.82794 -12.67381 -8.28706  1.000 56.84933  ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? 0.93586  -12.77784 -10.64385 1.000 56.23111  ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? 2.34450  -13.16419 -10.28695 1.000 54.29904  ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? 3.07833  -14.00550 -11.10895 1.000 54.27080  ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? 2.92097  -12.71532 -9.10733  1.000 51.64776  ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? 4.37203  -14.37466 -10.77370 1.000 54.37893  ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? 4.20988  -13.07834 -8.76463  1.000 53.34363  ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? 4.93870  -13.91226 -9.60090  1.000 55.67520  ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? -0.16057 -14.81950 -8.03262  1.000 51.74343  ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? -0.38206 -14.87319 -6.59427  1.000 53.09239  ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? 0.79578  -15.57058 -5.92255  1.000 54.06155  ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? 1.60698  -16.23867 -6.57204  1.000 56.12279  ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? -1.69234 -15.59471 -6.25526  1.000 51.70157  ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? -2.29682 -15.14948 -4.94265  1.000 58.21313  ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? -3.69755 -15.68795 -4.74136  1.000 54.54067  ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? -4.54477 -14.70254 -4.08666  1.000 67.92083  ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? -5.75611 -14.35971 -4.50399  1.000 78.76645  ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? -6.31921 -14.94908 -5.54590  1.000 74.44755  ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? -6.42418 -13.40982 -3.85206  1.000 79.70774  ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? 0.89120  -15.40258 -4.60395  1.000 53.78328  ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? 1.91269  -16.09344 -3.82154  1.000 53.87242  ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? 1.55484  -17.57275 -3.73450  1.000 52.10771  ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? 0.61585  -17.95939 -3.03057  1.000 48.19801  ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? 2.03002  -15.47483 -2.43316  1.000 50.56416  ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? 3.43328  -15.48164 -1.85469  1.000 49.90359  ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? 3.51617  -14.51512 -0.68221  1.000 66.47130  ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? 3.24725  -13.08363 -1.13881  1.000 76.79053  ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? 2.41613  -12.30713 -0.16457  1.000 82.65851  ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? 2.29234  -18.39601 -4.46269  1.000 53.52843  ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? 2.03231  -19.82129 -4.56389  1.000 45.71114  ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? 2.95274  -20.57440 -3.61142  1.000 46.53559  ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? 4.03700  -20.10478 -3.25590  1.000 47.19555  ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? 2.24649  -20.30088 -6.00517  1.000 48.38903  ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? 1.39221  -21.48448 -6.45677  1.000 49.81266  ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? 0.85359  -21.30013 -8.18475  1.000 57.69827  ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? 2.41972  -21.34535 -9.05273  1.000 61.69024  ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? 2.50125  -21.74256 -3.18307  1.000 47.80544  ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? 3.31277  -22.62956 -2.37188  1.000 44.28774  ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? 3.34827  -23.99020 -3.04473  1.000 47.58377  ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? 2.39636  -24.38632 -3.72344  1.000 46.79878  ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? 2.77124  -22.74961 -0.93991  1.000 45.42801  ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? 4.46598  -24.68766 -2.86749  1.000 47.98709  ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? 4.61176  -26.02069 -3.41894  1.000 49.00142  ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? 3.54834  -26.94741 -2.83588  1.000 46.96362  ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? 3.16829  -26.81015 -1.67046  1.000 45.56145  ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? 5.99056  -26.58258 -3.09803  1.000 49.90219  ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? 7.08679  -26.04019 -3.95259  1.000 49.80956  ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? 7.19137  -26.40944 -5.28234  1.000 55.27871  ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? 8.04368  -25.19505 -3.41718  1.000 50.70905  ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? 8.22557  -25.92612 -6.07362  1.000 55.63309  ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? 9.08105  -24.71468 -4.20029  1.000 54.82601  ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? 9.16970  -25.08049 -5.53106  1.000 51.54893  ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? 3.05540  -27.90080 -3.62094  1.000 49.23232  ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? 2.18938  -28.93742 -3.04705  1.000 49.75318  ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? 2.89762  -29.63441 -1.89240  1.000 49.22322  ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? 4.07631  -29.98471 -1.98406  1.000 49.52008  ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? 1.93947  -29.88107 -4.22813  1.000 50.40876  ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? 2.15139  -29.02147 -5.44540  1.000 49.30076  ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? 3.25160  -28.07599 -5.06982  1.000 48.96751  ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? 2.17296  -29.81087 -0.79043  1.000 48.88577  ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? 2.74905  -30.28804 0.45841   1.000 48.63075  ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? 2.66531  -31.79625 0.62467   1.000 49.98700  ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? 3.25419  -32.32516 1.57240   1.000 51.62631  ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? 2.05527  -29.61890 1.64758   1.000 48.71889  ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? 0.65171  -29.69641 1.51680   1.000 46.06069  ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? 1.96849  -32.49407 -0.27615  1.000 48.29819  ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? 1.70594  -33.91250 -0.07414  1.000 48.39761  ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? 2.94763  -34.73058 0.21499   1.000 55.21426  ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? 2.95392  -35.57301 1.11688   1.000 57.28644  ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? 4.01970  -34.49183 -0.53850  1.000 54.30369  ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? 5.22198  -35.29190 -0.36543  1.000 50.97777  ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? 5.88967  -35.05288 0.98370   1.000 55.87119  ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? 6.71521  -35.87069 1.40320   1.000 56.27719  ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? 6.20052  -35.00265 -1.50159  1.000 56.29018  ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? 7.03010  -36.19761 -1.92148  1.000 63.41119  ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? 6.17641  -37.31282 -2.53104  1.000 72.24556  ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? 6.53258  -38.66725 -1.90625  1.000 79.61194  ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? 5.83992  -39.84391 -2.51534  1.000 71.14309  ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? 5.53647  -33.97186 1.68206   1.000 56.03722  ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? 6.19031  -33.61524 2.93922   1.000 55.80403  ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? 5.35063  -34.04817 4.13797   1.000 51.66507  ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? 5.89710  -34.48265 5.15938   1.000 51.94278  ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? 6.50136  -32.10629 2.99206   1.000 50.75716  ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? 7.23204  -31.75766 4.27529   1.000 50.56019  ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? 7.33689  -31.70227 1.79492   1.000 47.71682  ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? 4.02243  -33.93285 4.02753   1.000 51.16750  ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? 3.15254  -34.40844 5.10411   1.000 55.49974  ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? 3.43455  -35.86400 5.45502   1.000 54.17436  ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? 3.34532  -36.24533 6.62749   1.000 59.68578  ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? 1.67482  -34.24045 4.73472   1.000 51.89375  ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? 1.33837  -32.91883 4.04798   1.000 51.86912  ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? -0.05284 -32.90552 3.42409   1.000 54.78401  ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? -0.93115 -33.66156 3.89411   1.000 57.90068  ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? -0.27109 -32.13260 2.46408   1.000 52.58352  ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? 3.80439  -36.68256 4.46662   1.000 55.26791  ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? 4.14952  -38.07033 4.71351   1.000 55.53183  ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? 5.43758  -38.28785 5.47958   1.000 56.11120  ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? 5.85960  -39.43667 5.63923   1.000 62.19045  ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? 6.07607  -37.22011 5.95376   1.000 51.83296  ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? 7.26745  -37.32686 6.77789   1.000 51.95142  ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? 7.10600  -36.66796 8.13787   1.000 52.24819  ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? 8.05320  -36.67928 8.93096   1.000 54.53438  ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? 8.47612  -36.70597 6.06089   1.000 57.99639  ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? 8.64290  -37.14160 4.31668   1.000 62.55750  ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? 5.95023  -36.08569 8.43219   1.000 53.22550  ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? 5.75793  -35.39303 9.69591   1.000 52.43356  ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? 5.31984  -36.36312 10.77980  1.000 52.47895  ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? 4.36717  -37.12720 10.59829  1.000 51.63480  ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? 4.75226  -34.25505 9.54629   1.000 52.97841  ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? 5.21314  -33.22445 8.53537   1.000 51.36390  ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? 6.91810  -32.67740 8.83409   1.000 49.51722  ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? 6.83137  -32.11943 10.53889  1.000 47.86946  ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? 6.04111  -36.33591 11.89845  1.000 53.74604  ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? 5.73514  -37.13022 13.07465  1.000 54.58438  ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? 5.70953  -36.20562 14.28160  1.000 53.47442  ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? 6.12815  -35.05034 14.22372  1.000 56.66847  ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? 6.74804  -38.26795 13.29854  1.000 54.35255  ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? 6.76590  -39.20471 12.11072  1.000 54.75120  ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? 8.12567  -37.68572 13.54299  1.000 53.66158  ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? 5.21239  -36.73790 15.38407  1.000 56.59581  ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? 5.19316  -36.03553 16.65471  1.000 57.94548  ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? 6.29011  -36.61859 17.53203  1.000 57.92931  ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? 6.35509  -37.83897 17.71912  1.000 62.51077  ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? 3.82748  -36.17839 17.31861  1.000 60.81092  ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? 3.63645  -35.34663 18.55830  1.000 60.89481  ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? 2.56067  -35.92348 19.44402  1.000 63.01525  ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? 2.51169  -37.13290 19.66430  1.000 68.62746  ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? 1.67338  -35.06748 19.93598  1.000 62.42074  ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? 7.15637  -35.75416 18.04921  1.000 51.63425  ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? 8.24765  -36.15374 18.92816  1.000 54.03587  ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? 7.99543  -35.55111 20.30094  1.000 59.53505  ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? 7.75035  -34.34576 20.42533  1.000 67.14822  ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? 9.61237  -35.71076 18.37758  1.000 56.90340  ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? 10.73786 -36.34597 19.18333  1.000 54.36381  ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? 9.72991  -36.05671 16.89665  1.000 55.32270  ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? 8.05199  -36.38704 21.32646  1.000 60.48240  ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? 7.74052  -35.98411 22.68709  1.000 61.54384  ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? 8.86806  -36.43449 23.59969  1.000 66.02027  ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? 9.29755  -37.59163 23.53890  1.000 67.67667  ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? 6.40222  -36.58363 23.14010  1.000 64.98302  ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? 5.34637  -36.08723 22.30553  1.000 61.50494  ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? 6.11283  -36.25322 24.60223  1.000 60.39296  ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? 9.35539  -35.51784 24.43024  1.000 66.36467  ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? 10.37010 -35.82843 25.42742  1.000 64.76136  ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? 9.95432  -35.15227 26.72408  1.000 60.56696  ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? 9.86550  -33.92370 26.78481  1.000 62.21130  ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? 11.75709 -35.36380 24.97088  1.000 60.54723  ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? 13.09478 -35.76284 26.11117  1.000 75.45045  ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? 9.67124  -35.94575 27.74079  1.000 66.86479  ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? 9.13148  -35.38469 28.96802  1.000 67.79637  ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? 7.76505  -34.77964 28.71004  1.000 69.93382  ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? 6.82671  -35.46087 28.28090  1.000 75.55040  ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? 7.64524  -33.47777 28.95659  1.000 68.39280  ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? 6.41324  -32.73522 28.72112  1.000 66.72279  ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? 6.41765  -31.99444 27.38869  1.000 71.42747  ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? 5.37685  -31.92309 26.72228  1.000 74.97737  ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? 6.17551  -31.74935 29.87470  1.000 73.30468  ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? 5.58197  -32.44559 30.97758  1.000 82.63192  ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? 5.26063  -30.60556 29.46166  1.000 75.66144  ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? 7.56789  -31.45180 26.98399  1.000 65.47713  ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? 7.68810  -30.80479 25.68306  1.000 62.22592  ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? 7.37769  -31.78543 24.55955  1.000 61.01649  ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? 7.85912  -32.92147 24.55140  1.000 62.26285  ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? 9.10103  -30.24538 25.49204  1.000 64.75579  ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? 9.54128  -29.61278 26.69946  1.000 70.00843  ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? 9.13386  -29.23553 24.35070  1.000 61.35039  ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? 6.57421  -31.33447 23.60071  1.000 61.24246  ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? 6.27331  -32.10725 22.40543  1.000 63.84856  ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? 6.33189  -31.19212 21.19198  1.000 61.37525  ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? 5.84699  -30.05911 21.23872  1.000 67.22578  ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? 4.89955  -32.78147 22.50824  1.000 68.58576  ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? 4.49830  -33.25614 21.21734  1.000 68.27593  ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? 3.85784  -31.81236 23.05650  1.000 80.69190  ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? 6.93798  -31.67658 20.11208  1.000 59.22722  ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? 7.08925  -30.87052 18.90475  1.000 57.09371  ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? 6.99630  -31.77756 17.68315  1.000 56.09964  ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? 6.58985  -32.93916 17.78003  1.000 58.91442  ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? 8.39767  -30.06862 18.93865  1.000 56.27977  ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? 9.66397  -30.67354 19.55010  1.000 57.98043  ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? 10.27717 -31.74887 18.67287  1.000 55.06026  ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? 10.67072 -29.55683 19.80946  1.000 57.57128  ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? 7.36926  -31.23328 16.52513  1.000 54.90144  ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? 7.27190  -31.92454 15.24757  1.000 51.29445  ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? 8.62222  -32.49495 14.83074  1.000 51.75762  ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? 9.67863  -31.95503 15.16663  1.000 52.45695  ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? 6.75228  -30.98629 14.15386  1.000 49.48779  ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? 5.40558  -30.38533 14.49312  1.000 53.15973  ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? 4.39221  -31.08378 14.51680  1.000 53.73540  ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? 5.38220  -29.08149 14.74077  1.000 50.70765  ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? 8.57795  -33.58942 14.08317  1.000 52.72388  ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? 9.78646  -34.22143 13.59342  1.000 50.55340  ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? 9.66357  -34.59949 12.13592  1.000 52.29423  ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? 8.56845  -34.80098 11.61058  1.000 53.00498  ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? 10.81594 -34.69365 11.47833  1.000 54.51958  ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? 10.89705 -35.02809 10.06032  1.000 52.91593  ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? 11.45342 -36.44274 9.93731   1.000 59.73874  ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? 12.61660 -36.69457 10.27010  1.000 58.90558  ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? 11.74448 -34.00281 9.30797   1.000 52.50575  ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? 11.96763 -34.19972 7.80952   1.000 56.69318  ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? 10.90125 -33.45493 7.03608   1.000 55.50304  ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? 13.33141 -33.66330 7.41731   1.000 51.32968  ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? 10.61232 -37.35730 9.46065   1.000 60.38505  ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? 10.89549 -38.79006 9.42834   1.000 58.04500  ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? 11.26271 -39.17404 8.00019   1.000 56.79850  ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? 10.39376 -39.33186 7.13999   1.000 56.30246  ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? 9.68399  -39.57445 9.92270   1.000 57.77876  ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? 9.83254  -41.06664 9.92485   1.000 62.98054  ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? 10.99396 -41.78511 9.94319   1.000 63.42444  ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? 8.76857  -42.02516 9.89730   1.000 66.41580  ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? 10.71577 -43.13238 9.93499   1.000 62.77281  ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? 9.35726  -43.30473 9.90853   1.000 63.20739  ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? 7.37373  -41.92357 9.87115   1.000 63.77844  ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? 8.60067  -44.47294 9.89231   1.000 73.11617  ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? 6.62584  -43.08210 9.85342   1.000 67.64198  ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? 7.23971  -44.34180 9.86466   1.000 71.79672  ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? 12.55364 -39.32906 7.75033   1.000 60.72687  ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? 13.05723 -39.75426 6.45499   1.000 64.21374  ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? 13.88742 -41.00934 6.66228   1.000 67.97260  ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? 14.76116 -41.03913 7.53557   1.000 70.70697  ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? 13.89538 -38.65396 5.80196   1.000 59.92777  ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? 13.15812 -37.35138 5.49978   1.000 56.31980  ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? 14.13008 -36.31105 4.98354   1.000 57.12414  ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? 12.04815 -37.58983 4.49970   1.000 56.90002  ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? 13.61095 -42.03649 5.86987   1.000 67.07657  ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? 14.28783 -43.33422 6.01002   1.000 71.67974  ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? 14.07826 -43.79464 7.45514   1.000 70.63653  ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? 12.96997 -43.65373 7.99036   1.000 70.20951  ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? 15.73700 -43.21008 5.57272   1.000 67.15263  ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? 15.87294 -42.86870 4.09657   1.000 75.73867  ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? 15.18417 -43.51217 3.26833   1.000 77.43680  ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? 16.66021 -41.95241 3.76624   1.000 67.35206  ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? 15.10784 -44.32124 8.11498   1.000 71.30042  ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? 15.01731 -44.76891 9.49853   1.000 67.56885  ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? 15.51330 -43.71192 10.48116  1.000 69.63849  ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? 15.98171 -44.05212 11.57413  1.000 69.38301  ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? 15.79092 -46.07590 9.68539   1.000 68.99589  ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? 17.25661 -45.96503 9.27500   1.000 70.71808  ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? 17.66833 -44.91830 8.73211   1.000 73.81222  ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? 18.00475 -46.93392 9.49994   1.000 69.78647  ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? 15.41985 -42.43324 10.11291  1.000 67.78632  ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? 15.88279 -41.33007 10.94698  1.000 61.47155  ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? 14.75933 -40.31737 11.10494  1.000 60.93887  ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? 13.99138 -40.07589 10.16681  1.000 60.50123  ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? 17.13744 -40.65073 10.35840  1.000 61.64464  ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? 17.69364 -39.62301 11.33699  1.000 57.61311  ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? 18.19878 -41.68975 10.01662  1.000 56.95831  ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? 14.66679 -39.72440 12.29360  1.000 60.63716  ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? 13.71740 -38.65649 12.57969  1.000 57.40453  ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? 14.51174 -37.46316 13.09673  1.000 54.93383  ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? 15.25823 -37.58654 14.07649  1.000 58.14040  ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? 12.64952 -39.09851 13.59502  1.000 61.37233  ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? 11.93281 -37.89109 14.19624  1.000 52.35761  ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? 11.65499 -40.05640 12.94695  1.000 62.02493  ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? 14.35934 -36.31743 12.43285  1.000 52.82380  ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? 15.04355 -35.08002 12.78965  1.000 52.16917  ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? 14.07901 -34.13952 13.49788  1.000 53.58696  ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? 12.91405 -34.02423 13.10809  1.000 53.88328  ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? 15.61230 -34.38670 11.54718  1.000 51.80958  ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? 16.41581 -35.30258 10.65913  1.000 51.47002  ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? 15.78912 -36.12802 9.73630   1.000 54.34165  ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? 17.79776 -35.35102 10.74981  1.000 52.46931  ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? 16.51300 -36.97841 8.93122   1.000 55.09120  ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? 18.53296 -36.19521 9.94374   1.000 57.36055  ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? 17.88188 -37.00879 9.03572   1.000 58.58669  ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? 18.59489 -37.86149 8.22673   1.000 56.07240  ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? 14.56820 -33.46027 14.53102  1.000 52.68881  ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? 13.73513 -32.55288 15.30582  1.000 50.40615  ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? 14.63542 -31.53714 15.99551  1.000 51.23646  ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? 15.83940 -31.77691 16.15630  1.000 52.36201  ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? 12.89087 -33.31767 16.33797  1.000 50.52803  ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? 13.68191 -33.50701 17.94892  1.000 57.04055  ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? 14.08743 -30.39294 16.40673  1.000 50.16300  ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? 14.89028 -29.42469 17.16284  1.000 52.03837  ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? 15.38038 -30.01730 18.47558  1.000 52.74570  ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? 14.67796 -30.78281 19.13630  1.000 54.88390  ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? 13.91725 -28.26322 17.39477  1.000 47.73586  ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? 12.90182 -28.40023 16.31092  1.000 45.75504  ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? 12.74567 -29.86986 16.09531  1.000 41.71457  ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? 16.60119 -29.64947 18.85914  1.000 56.18445  ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? 17.20374 -30.27131 20.03119  1.000 56.47939  ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? 16.57700 -29.80019 21.33717  1.000 55.11389  ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? 16.72887 -30.47929 22.35553  1.000 58.39225  ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? 18.71333 -30.01762 20.04646  1.000 58.66095  ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? 19.12420 -28.56294 20.17672  1.000 57.91132  ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? 20.59960 -28.46405 20.50711  1.000 60.17794  ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? 21.09359 -27.09341 20.47004  1.000 60.92549  ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? 22.35952 -26.75331 20.67119  1.000 60.95358  ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? 23.28761 -27.66105 20.93244  1.000 59.61988  ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 22.70268 -25.47167 20.61236  1.000 56.74011  ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? 15.86294 -28.67570 21.33652  1.000 54.42398  ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? 15.28933 -28.15342 22.57045  1.000 58.42043  ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? 14.02988 -28.89776 22.99857  1.000 62.06407  ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? 13.32237 -28.43445 23.89994  1.000 59.77473  ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? 15.01739 -26.64633 22.44450  1.000 64.29418  ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? 13.97727 -26.28243 21.43001  1.000 60.85997  ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? 12.67585 -25.98354 21.77391  1.000 61.09504  ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? 14.05614 -26.12798 20.08733  1.000 57.29255  ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? 11.99275 -25.68119 20.68419  1.000 57.97975  ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? 12.80641 -25.76345 19.64724  1.000 60.07496  ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? 13.74530 -30.04385 22.37634  1.000 61.65360  ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? 12.72695 -30.94665 22.88989  1.000 61.99779  ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? 13.14662 -31.54504 24.22729  1.000 67.46206  ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? 12.28966 -31.99104 25.00225  1.000 64.13960  ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? 12.43171 -32.04733 21.85005  1.000 59.69862  ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? 13.58595 -33.03751 21.77652  1.000 58.85205  ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? 11.12497 -32.75497 22.16609  1.000 59.32589  ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? 14.44577 -31.55144 24.52966  1.000 64.26273  ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? 14.93789 -32.11655 25.78027  1.000 69.11740  ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? 14.99539 -31.02600 26.84211  1.000 67.62648  ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? 15.55761 -31.22503 27.92570  1.000 70.26918  ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? 16.31635 -32.77214 25.58692  1.000 68.27301  ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? 17.36105 -31.71148 25.23482  1.000 66.37339  ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? 16.24554 -33.84366 24.50862  1.000 65.83282  ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? 18.60271 -32.26705 24.56282  1.000 67.59681  ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? 14.40393 -29.87425 26.54500  1.000 66.01602  ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? 14.47143 -28.70785 27.41386  1.000 73.65741  ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? 13.21026 -28.61608 28.26195  1.000 70.13169  ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? 12.09498 -28.64140 27.73024  1.000 67.02386  ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? 14.63659 -27.42943 26.58965  1.000 73.16433  ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? 16.33389 -26.85515 26.41896  1.000 80.62900  ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? 13.38537 -28.50523 29.57416  1.000 67.95441  ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? 12.24441 -28.19938 30.41893  1.000 81.56656  ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? 11.88833 -26.72253 30.27393  1.000 92.22021  ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? 12.71991 -25.89208 29.89456  1.000 91.34645  ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? 12.53126 -28.55651 31.88084  1.000 83.21215  ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? 13.19796 -27.46799 32.53027  1.000 88.84274  ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? 13.39761 -29.80559 31.96690  1.000 73.19952  ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? 10.62320 -26.40062 30.56059  1.000 101.55143 ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? 10.13523 -25.04516 30.32241  1.000 98.13964  ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? 10.86111 -24.00303 31.16444  1.000 100.26385 ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? 10.77425 -22.80991 30.85632  1.000 101.99578 ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? 8.62564  -24.97522 30.56832  1.000 96.30035  ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? 7.90987  -25.56700 29.49350  1.000 91.41526  ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? 11.57951 -24.42082 32.20820  1.000 101.66869 ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? 12.44360 -23.51755 32.95692  1.000 96.93502  ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? 13.89892 -23.57064 32.50855  1.000 94.49288  ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? 14.67342 -22.67995 32.87366  1.000 95.04824  ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? 12.38258 -23.82896 34.45800  1.000 100.14354 ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 47  ? 12.84620 -25.22970 34.81995  1.000 99.89904  ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 47  ? 11.70504 -26.12703 35.25256  1.000 104.72414 ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 47  ? 10.55850 -25.87203 34.82259  1.000 106.49426 ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 47  ? 11.95418 -27.08349 36.01973  1.000 92.75959  ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 48  ? 14.29513 -24.58539 31.73752  1.000 94.46619  ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 48  ? 15.67338 -24.66927 31.27035  1.000 92.66881  ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 48  ? 15.90902 -23.91415 29.97005  1.000 88.77776  ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 48  ? 17.06391 -23.78047 29.55252  1.000 84.46739  ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 48  ? 16.08975 -26.13071 31.09338  1.000 88.72482  ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 48  ? 17.47570 -26.40970 31.64665  1.000 97.20060  ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 48  ? 17.88541 -25.72119 32.60588  1.000 93.13567  ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 48  ? 18.15877 -27.31507 31.12215  1.000 108.88261 ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 49  ? 14.85428 -23.41209 29.32727  1.000 91.20999  ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 49  ? 15.01996 -22.66519 28.08811  1.000 83.53039  ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 49  ? 15.72516 -21.32948 28.28969  1.000 81.87326  ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 49  ? 16.10775 -20.69801 27.29900  1.000 77.83961  ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 49  ? 13.65898 -22.43697 27.42701  1.000 84.24768  ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 49  ? 13.10657 -23.65246 26.69233  1.000 84.54251  ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 49  ? 11.33082 -23.55034 26.38332  1.000 101.29388 ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 49  ? 11.09324 -24.96600 25.30969  1.000 79.00384  ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 50  ? 15.91252 -20.88886 29.53554  1.000 83.95941  ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 50  ? 16.57786 -19.61249 29.78089  1.000 83.19382  ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 50  ? 18.06128 -19.67998 29.43455  1.000 85.06540  ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 50  ? 18.59523 -18.78009 28.77856  1.000 79.51289  ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 50  ? 16.37701 -19.18957 31.23695  1.000 87.02388  ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 50  ? 15.37983 -18.05419 31.48825  1.000 82.89654  ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 50  ? 15.96068 -16.71747 31.03866  1.000 77.78689  ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 50  ? 14.06457 -18.32732 30.77660  1.000 77.01032  ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 51  ? 18.74890 -20.73388 29.87497  1.000 89.28069  ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 51  ? 20.16556 -20.91898 29.55807  1.000 88.07513  ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 51  ? 20.47752 -22.40659 29.56318  1.000 86.68361  ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 51  ? 20.95204 -22.95627 30.56647  1.000 96.30042  ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 51  ? 21.07249 -20.18078 30.53994  1.000 88.16503  ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 51  ? 22.50653 -20.11627 30.06081  1.000 96.55397  ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 51  ? 22.79053 -20.36302 28.88652  1.000 90.27392  ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 51  ? 23.42450 -19.81218 30.97248  1.000 115.95080 ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 52  ? 20.23422 -23.09378 28.44920  1.000 84.42358  ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 52  ? 20.36727 -24.55517 28.44904  1.000 80.10053  ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 52  ? 21.74919 -25.04025 28.04088  1.000 76.43194  ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 52  ? 22.28855 -24.62285 27.01147  1.000 80.54067  ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 52  ? 19.29635 -24.99547 27.44384  1.000 76.44512  ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 52  ? 19.12222 -23.81578 26.51870  1.000 74.55241  ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 52  ? 19.68612 -22.58390 27.18118  1.000 81.45190  ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 53  ? 22.32890 -25.92658 28.84953  1.000 76.96476  ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 53  ? 23.58098 -26.60233 28.51025  1.000 80.57558  ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 53  ? 23.20783 -27.92643 27.86394  1.000 78.26335  ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 53  ? 23.10163 -28.95614 28.52928  1.000 83.71878  ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 53  ? 24.45141 -26.80587 29.74455  1.000 86.12656  ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 53  ? 25.80498 -27.41035 29.41032  1.000 89.09616  ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 53  ? 25.89571 -28.55684 28.97113  1.000 90.35330  ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 53  ? 26.86552 -26.63651 29.61539  1.000 88.99410  ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 54  ? 23.02678 -27.89960 26.54181  1.000 73.37812  ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 54  ? 22.43537 -29.03983 25.85117  1.000 74.22167  ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 54  ? 23.25834 -30.30988 26.01339  1.000 79.02336  ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 54  ? 22.70738 -31.41305 25.94736  1.000 79.81299  ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 54  ? 22.25193 -28.72785 24.36724  1.000 68.36675  ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 54  ? 21.10228 -27.79262 24.07315  1.000 65.81773  ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 54  ? 21.29200 -26.41830 24.03262  1.000 66.15959  ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 54  ? 19.81788 -28.28118 23.87993  1.000 61.44634  ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 54  ? 20.24343 -25.56076 23.76709  1.000 62.78475  ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 54  ? 18.76073 -27.42966 23.62184  1.000 62.09811  ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 54  ? 18.97905 -26.07273 23.56615  1.000 63.11133  ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 54  ? 17.92945 -25.22367 23.30965  1.000 64.91945  ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 55  ? 24.56655 -30.19037 26.22466  1.000 76.87346  ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 55  ? 25.37754 -31.39860 26.31776  1.000 88.66824  ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 55  ? 25.13788 -32.13147 27.63142  1.000 87.70649  ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 55  ? 25.07344 -33.36596 27.65243  1.000 87.91884  ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 55  ? 26.85840 -31.06580 26.14258  1.000 97.39222  ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 55  ? 27.35058 -31.07612 24.68781  1.000 102.56489 ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 55  ? 27.26216 -32.43325 23.97743  1.000 116.45936 ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 55  ? 27.90955 -32.56943 22.92066  1.000 116.62779 ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 55  ? 26.58431 -33.36764 24.46130  1.000 123.99395 ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 56  ? 24.98464 -31.39691 28.73274  1.000 87.13417  ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? 24.68851 -32.02483 30.01671  1.000 93.92374  ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? 23.20683 -32.34543 30.19255  1.000 91.37535  ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? 22.81035 -32.80479 31.27061  1.000 81.83360  ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? 25.17707 -31.13827 31.16901  1.000 92.57448  ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? 26.66463 -31.31458 31.45565  1.000 92.86069  ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? 27.45025 -31.48519 30.49639  1.000 93.56546  ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? 27.04813 -31.28369 32.64503  1.000 88.49741  ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 57  ? 22.38715 -32.11289 29.16710  1.000 89.30852  ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 57  ? 20.98885 -32.52760 29.14308  1.000 83.69758  ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 57  ? 20.77524 -33.80445 28.34595  1.000 84.82408  ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 57  ? 19.96278 -34.64809 28.73847  1.000 81.74594  ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 57  ? 20.10772 -31.42290 28.54852  1.000 80.80626  ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 57  ? 19.49496 -30.35419 29.45629  1.000 84.07944  ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 57  ? 20.51862 -29.75883 30.42199  1.000 86.48120  ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 57  ? 18.84807 -29.27192 28.60941  1.000 79.91407  ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 58  ? 21.48940 -33.95642 27.22749  1.000 84.46460  ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 58  ? 21.34751 -35.15316 26.40752  1.000 82.28476  ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 58  ? 21.96528 -36.37634 27.07144  1.000 82.86161  ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 58  ? 21.55389 -37.50569 26.78232  1.000 84.80318  ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 58  ? 21.97522 -34.92738 25.03220  1.000 77.36938  ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 58  ? 21.70371 -36.02591 24.00456  1.000 73.73260  ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 58  ? 20.21790 -36.30233 23.90216  1.000 73.54646  ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 58  ? 22.27707 -35.65103 22.65094  1.000 76.31172  ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 59  ? 22.94985 -36.18598 27.95287  1.000 81.40824  ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 59  ? 23.54412 -37.35056 28.59900  1.000 85.06451  ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 59  ? 22.54522 -37.99806 29.54662  1.000 83.48835  ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 59  ? 22.49259 -39.22812 29.65690  1.000 84.27336  ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 59  ? 24.85301 -36.99063 29.32823  1.000 89.71267  ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 59  ? 24.68835 -35.72967 30.17768  1.000 90.13878  ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 59  ? 26.00526 -36.86025 28.32886  1.000 81.88687  ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 59  ? 25.94684 -35.35375 30.94891  1.000 87.37125  ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 60  ? 21.72606 -37.19854 30.22516  1.000 86.80522  ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 60  ? 20.68681 -37.71598 31.10698  1.000 82.94241  ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 60  ? 19.48413 -38.27042 30.34582  1.000 86.60906  ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 60  ? 18.48659 -38.64337 30.97583  1.000 88.27531  ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 60  ? 20.23343 -36.62086 32.07679  1.000 77.42572  ? 60  ARG   A CB  1 
ATOM   461  N N   . LYS   A 1 61  ? 19.55770 -38.32991 29.01750  1.000 90.65645  ? 61  LYS   A N   1 
ATOM   462  C CA  . LYS   A 1 61  ? 18.48204 -38.83467 28.17484  1.000 87.27455  ? 61  LYS   A CA  1 
ATOM   463  C C   . LYS   A 1 61  ? 18.89899 -40.16371 27.55968  1.000 85.04641  ? 61  LYS   A C   1 
ATOM   464  O O   . LYS   A 1 61  ? 20.02425 -40.29993 27.06894  1.000 90.44681  ? 61  LYS   A O   1 
ATOM   465  C CB  . LYS   A 1 61  ? 18.13296 -37.83019 27.07223  1.000 82.36805  ? 61  LYS   A CB  1 
ATOM   466  C CG  . LYS   A 1 61  ? 17.43199 -36.57462 27.57031  1.000 80.49776  ? 61  LYS   A CG  1 
ATOM   467  C CD  . LYS   A 1 61  ? 16.06425 -36.89829 28.13871  1.000 78.63580  ? 61  LYS   A CD  1 
ATOM   468  C CE  . LYS   A 1 61  ? 15.63660 -35.88941 29.18990  1.000 80.21383  ? 61  LYS   A CE  1 
ATOM   469  N NZ  . LYS   A 1 61  ? 16.17787 -34.53323 28.92050  1.000 77.08669  ? 61  LYS   A NZ  1 
ATOM   470  N N   . SER   A 1 62  ? 17.99836 -41.13760 27.59726  1.000 82.49863  ? 62  SER   A N   1 
ATOM   471  C CA  . SER   A 1 62  ? 18.17330 -42.42085 26.93455  1.000 84.71473  ? 62  SER   A CA  1 
ATOM   472  C C   . SER   A 1 62  ? 17.19998 -42.52239 25.76554  1.000 82.82479  ? 62  SER   A C   1 
ATOM   473  O O   . SER   A 1 62  ? 16.42489 -41.60355 25.48731  1.000 79.79021  ? 62  SER   A O   1 
ATOM   474  C CB  . SER   A 1 62  ? 17.96750 -43.57776 27.91622  1.000 87.78470  ? 62  SER   A CB  1 
ATOM   475  O OG  . SER   A 1 62  ? 18.96694 -43.58571 28.92083  1.000 93.36295  ? 62  SER   A OG  1 
ATOM   476  N N   . ASN   A 1 63  ? 17.24063 -43.66806 25.08250  1.000 84.98387  ? 63  ASN   A N   1 
ATOM   477  C CA  . ASN   A 1 63  ? 16.36811 -43.87347 23.93056  1.000 83.49216  ? 63  ASN   A CA  1 
ATOM   478  C C   . ASN   A 1 63  ? 14.89452 -43.82414 24.32499  1.000 84.65680  ? 63  ASN   A C   1 
ATOM   479  O O   . ASN   A 1 63  ? 14.08614 -43.18385 23.64125  1.000 85.94531  ? 63  ASN   A O   1 
ATOM   480  C CB  . ASN   A 1 63  ? 16.70263 -45.20376 23.25337  1.000 76.29088  ? 63  ASN   A CB  1 
ATOM   481  C CG  . ASN   A 1 63  ? 18.06034 -45.18652 22.57908  1.000 77.72249  ? 63  ASN   A CG  1 
ATOM   482  O OD1 . ASN   A 1 63  ? 18.39590 -44.24777 21.85170  1.000 79.69032  ? 63  ASN   A OD1 1 
ATOM   483  N ND2 . ASN   A 1 63  ? 18.84680 -46.22916 22.80932  1.000 76.33951  ? 63  ASN   A ND2 1 
ATOM   484  N N   . HIS   A 1 64  ? 14.53035 -44.46900 25.43538  1.000 80.13757  ? 64  HIS   A N   1 
ATOM   485  C CA  . HIS   A 1 64  ? 13.12903 -44.63820 25.80127  1.000 80.32982  ? 64  HIS   A CA  1 
ATOM   486  C C   . HIS   A 1 64  ? 12.46525 -43.36361 26.31335  1.000 80.68102  ? 64  HIS   A C   1 
ATOM   487  O O   . HIS   A 1 64  ? 11.24841 -43.37090 26.52912  1.000 80.85281  ? 64  HIS   A O   1 
ATOM   488  C CB  . HIS   A 1 64  ? 12.99728 -45.74547 26.85169  1.000 90.23218  ? 64  HIS   A CB  1 
ATOM   489  C CG  . HIS   A 1 64  ? 13.80910 -45.50922 28.08617  1.000 90.51968  ? 64  HIS   A CG  1 
ATOM   490  N ND1 . HIS   A 1 64  ? 13.27429 -44.96892 29.23572  1.000 87.08720  ? 64  HIS   A ND1 1 
ATOM   491  C CD2 . HIS   A 1 64  ? 15.12029 -45.72652 28.34624  1.000 93.13832  ? 64  HIS   A CD2 1 
ATOM   492  C CE1 . HIS   A 1 64  ? 14.21964 -44.86760 30.15203  1.000 89.73557  ? 64  HIS   A CE1 1 
ATOM   493  N NE2 . HIS   A 1 64  ? 15.34875 -45.32332 29.63950  1.000 96.79848  ? 64  HIS   A NE2 1 
ATOM   494  N N   . ASN   A 1 65  ? 13.21453 -42.27836 26.51905  1.000 81.90274  ? 65  ASN   A N   1 
ATOM   495  C CA  . ASN   A 1 65  ? 12.59711 -41.01430 26.90340  1.000 77.92358  ? 65  ASN   A CA  1 
ATOM   496  C C   . ASN   A 1 65  ? 11.98657 -40.27501 25.72241  1.000 71.72261  ? 65  ASN   A C   1 
ATOM   497  O O   . ASN   A 1 65  ? 11.35349 -39.23469 25.92882  1.000 68.16238  ? 65  ASN   A O   1 
ATOM   498  C CB  . ASN   A 1 65  ? 13.61257 -40.09395 27.59050  1.000 78.59789  ? 65  ASN   A CB  1 
ATOM   499  C CG  . ASN   A 1 65  ? 14.53570 -40.83631 28.53608  1.000 87.48365  ? 65  ASN   A CG  1 
ATOM   500  O OD1 . ASN   A 1 65  ? 15.22623 -41.77263 28.13790  1.000 92.74305  ? 65  ASN   A OD1 1 
ATOM   501  N ND2 . ASN   A 1 65  ? 14.56479 -40.40902 29.79534  1.000 89.98695  ? 65  ASN   A ND2 1 
ATOM   502  N N   . PHE   A 1 66  ? 12.16339 -40.77830 24.50232  1.000 74.35752  ? 66  PHE   A N   1 
ATOM   503  C CA  . PHE   A 1 66  ? 11.69316 -40.12374 23.28579  1.000 75.00203  ? 66  PHE   A CA  1 
ATOM   504  C C   . PHE   A 1 66  ? 10.52556 -40.91790 22.71566  1.000 74.37042  ? 66  PHE   A C   1 
ATOM   505  O O   . PHE   A 1 66  ? 10.69969 -42.06863 22.29870  1.000 73.26345  ? 66  PHE   A O   1 
ATOM   506  C CB  . PHE   A 1 66  ? 12.81675 -40.01828 22.25306  1.000 74.67030  ? 66  PHE   A CB  1 
ATOM   507  C CG  . PHE   A 1 66  ? 13.94563 -39.11193 22.66223  1.000 75.75334  ? 66  PHE   A CG  1 
ATOM   508  C CD1 . PHE   A 1 66  ? 13.73402 -37.75685 22.86421  1.000 71.75729  ? 66  PHE   A CD1 1 
ATOM   509  C CD2 . PHE   A 1 66  ? 15.21838 -39.62508 22.86240  1.000 75.74582  ? 66  PHE   A CD2 1 
ATOM   510  C CE1 . PHE   A 1 66  ? 14.77547 -36.92724 23.23735  1.000 75.84660  ? 66  PHE   A CE1 1 
ATOM   511  C CE2 . PHE   A 1 66  ? 16.26245 -38.80371 23.24202  1.000 78.30140  ? 66  PHE   A CE2 1 
ATOM   512  C CZ  . PHE   A 1 66  ? 16.04182 -37.45180 23.42963  1.000 78.51712  ? 66  PHE   A CZ  1 
ATOM   513  N N   . LEU   A 1 67  ? 9.34672  -40.29955 22.68479  1.000 70.56217  ? 67  LEU   A N   1 
ATOM   514  C CA  . LEU   A 1 67  ? 8.12496  -40.93582 22.19369  1.000 68.30266  ? 67  LEU   A CA  1 
ATOM   515  C C   . LEU   A 1 67  ? 7.82236  -40.37465 20.80626  1.000 70.39415  ? 67  LEU   A C   1 
ATOM   516  O O   . LEU   A 1 67  ? 7.30119  -39.26397 20.67282  1.000 69.87630  ? 67  LEU   A O   1 
ATOM   517  C CB  . LEU   A 1 67  ? 6.97476  -40.69775 23.16837  1.000 67.69689  ? 67  LEU   A CB  1 
ATOM   518  C CG  . LEU   A 1 67  ? 5.53858  -40.89581 22.67909  1.000 72.70442  ? 67  LEU   A CG  1 
ATOM   519  C CD1 . LEU   A 1 67  ? 5.25380  -42.35975 22.38979  1.000 82.52153  ? 67  LEU   A CD1 1 
ATOM   520  C CD2 . LEU   A 1 67  ? 4.54231  -40.33264 23.68390  1.000 75.67614  ? 67  LEU   A CD2 1 
ATOM   521  N N   . VAL   A 1 68  ? 8.15546  -41.14105 19.77097  1.000 72.60657  ? 68  VAL   A N   1 
ATOM   522  C CA  . VAL   A 1 68  ? 7.95736  -40.72344 18.38722  1.000 70.48705  ? 68  VAL   A CA  1 
ATOM   523  C C   . VAL   A 1 68  ? 6.65294  -41.33274 17.90044  1.000 69.95590  ? 68  VAL   A C   1 
ATOM   524  O O   . VAL   A 1 68  ? 6.50893  -42.56075 17.86894  1.000 69.41831  ? 68  VAL   A O   1 
ATOM   525  C CB  . VAL   A 1 68  ? 9.12877  -41.15431 17.48904  1.000 71.32118  ? 68  VAL   A CB  1 
ATOM   526  C CG1 . VAL   A 1 68  ? 8.87732  -40.73231 16.04129  1.000 64.60845  ? 68  VAL   A CG1 1 
ATOM   527  C CG2 . VAL   A 1 68  ? 10.44119 -40.59666 18.00507  1.000 63.95043  ? 68  VAL   A CG2 1 
ATOM   528  N N   . GLN   A 1 69  ? 5.70351  -40.48310 17.51563  1.000 70.01792  ? 69  GLN   A N   1 
ATOM   529  C CA  . GLN   A 1 69  ? 4.40719  -40.93492 17.02788  1.000 69.95408  ? 69  GLN   A CA  1 
ATOM   530  C C   . GLN   A 1 69  ? 4.22117  -40.47187 15.59204  1.000 66.23820  ? 69  GLN   A C   1 
ATOM   531  O O   . GLN   A 1 69  ? 4.36124  -39.28075 15.29237  1.000 62.24540  ? 69  GLN   A O   1 
ATOM   532  C CB  . GLN   A 1 69  ? 3.27353  -40.41962 17.91171  1.000 71.39124  ? 69  GLN   A CB  1 
ATOM   533  C CG  . GLN   A 1 69  ? 2.63301  -41.50463 18.75077  1.000 75.96486  ? 69  GLN   A CG  1 
ATOM   534  C CD  . GLN   A 1 69  ? 1.77557  -40.94240 19.85752  1.000 81.60932  ? 69  GLN   A CD  1 
ATOM   535  O OE1 . GLN   A 1 69  ? 2.26580  -40.23776 20.73864  1.000 83.79071  ? 69  GLN   A OE1 1 
ATOM   536  N NE2 . GLN   A 1 69  ? 0.48833  -41.26182 19.82919  1.000 88.00331  ? 69  GLN   A NE2 1 
ATOM   537  N N   . ALA   A 1 70  ? 3.93126  -41.41700 14.71110  1.000 68.27244  ? 70  ALA   A N   1 
ATOM   538  C CA  . ALA   A 1 70  ? 3.55572  -41.14611 13.32908  1.000 69.08420  ? 70  ALA   A CA  1 
ATOM   539  C C   . ALA   A 1 70  ? 2.08849  -41.53554 13.22350  1.000 76.48806  ? 70  ALA   A C   1 
ATOM   540  O O   . ALA   A 1 70  ? 1.75727  -42.72140 13.13768  1.000 82.44825  ? 70  ALA   A O   1 
ATOM   541  C CB  . ALA   A 1 70  ? 4.42657  -41.92815 12.35191  1.000 68.81266  ? 70  ALA   A CB  1 
ATOM   542  N N   . GLY   A 1 71  ? 1.21080  -40.53820 13.24959  1.000 74.30632  ? 71  GLY   A N   1 
ATOM   543  C CA  . GLY   A 1 71  ? -0.19681 -40.83935 13.42105  1.000 81.39754  ? 71  GLY   A CA  1 
ATOM   544  C C   . GLY   A 1 71  ? -0.43084 -41.45821 14.78607  1.000 85.60673  ? 71  GLY   A C   1 
ATOM   545  O O   . GLY   A 1 71  ? 0.23204  -41.12274 15.77261  1.000 89.78802  ? 71  GLY   A O   1 
ATOM   546  N N   . ASN   A 1 72  ? -1.37622 -42.38768 14.85036  1.000 81.47360  ? 72  ASN   A N   1 
ATOM   547  C CA  . ASN   A 1 72  ? -1.67542 -43.08425 16.09146  1.000 92.86442  ? 72  ASN   A CA  1 
ATOM   548  C C   . ASN   A 1 72  ? -0.88498 -44.38303 16.23718  1.000 95.13450  ? 72  ASN   A C   1 
ATOM   549  O O   . ASN   A 1 72  ? -1.26033 -45.24277 17.04493  1.000 89.71125  ? 72  ASN   A O   1 
ATOM   550  C CB  . ASN   A 1 72  ? -3.18080 -43.34933 16.19318  1.000 108.05509 ? 72  ASN   A CB  1 
ATOM   551  C CG  . ASN   A 1 72  ? -3.97534 -42.08839 16.51799  1.000 111.47060 ? 72  ASN   A CG  1 
ATOM   552  O OD1 . ASN   A 1 72  ? -3.50858 -40.96531 16.29020  1.000 102.08363 ? 72  ASN   A OD1 1 
ATOM   553  N ND2 . ASN   A 1 72  ? -5.18118 -42.27001 17.05490  1.000 104.00439 ? 72  ASN   A ND2 1 
ATOM   554  N N   . VAL   A 1 73  ? 0.19445  -44.54034 15.47275  1.000 93.40307  ? 73  VAL   A N   1 
ATOM   555  C CA  . VAL   A 1 73  ? 1.09282  -45.68606 15.57350  1.000 86.96569  ? 73  VAL   A CA  1 
ATOM   556  C C   . VAL   A 1 73  ? 2.47835  -45.15746 15.91089  1.000 81.91032  ? 73  VAL   A C   1 
ATOM   557  O O   . VAL   A 1 73  ? 3.06219  -44.38790 15.13720  1.000 79.15733  ? 73  VAL   A O   1 
ATOM   558  C CB  . VAL   A 1 73  ? 1.12445  -46.51334 14.28098  1.000 85.40862  ? 73  VAL   A CB  1 
ATOM   559  C CG1 . VAL   A 1 73  ? 2.32633  -47.44521 14.28808  1.000 86.06306  ? 73  VAL   A CG1 1 
ATOM   560  C CG2 . VAL   A 1 73  ? -0.16339 -47.30220 14.13362  1.000 91.52924  ? 73  VAL   A CG2 1 
ATOM   561  N N   . GLN   A 1 74  ? 3.00424  -45.57520 17.05334  1.000 80.48430  ? 74  GLN   A N   1 
ATOM   562  C CA  . GLN   A 1 74  ? 4.21785  -44.98980 17.59357  1.000 81.85366  ? 74  GLN   A CA  1 
ATOM   563  C C   . GLN   A 1 74  ? 5.45519  -45.77533 17.15778  1.000 80.95009  ? 74  GLN   A C   1 
ATOM   564  O O   . GLN   A 1 74  ? 5.38938  -46.96266 16.83316  1.000 82.28166  ? 74  GLN   A O   1 
ATOM   565  C CB  . GLN   A 1 74  ? 4.12356  -44.92135 19.11732  1.000 83.01721  ? 74  GLN   A CB  1 
ATOM   566  C CG  . GLN   A 1 74  ? 4.42445  -46.22081 19.80749  1.000 81.15805  ? 74  GLN   A CG  1 
ATOM   567  C CD  . GLN   A 1 74  ? 5.75166  -46.17917 20.52650  1.000 88.07563  ? 74  GLN   A CD  1 
ATOM   568  O OE1 . GLN   A 1 74  ? 6.05805  -45.21277 21.22540  1.000 86.63766  ? 74  GLN   A OE1 1 
ATOM   569  N NE2 . GLN   A 1 74  ? 6.55951  -47.22004 20.34505  1.000 93.37332  ? 74  GLN   A NE2 1 
ATOM   570  N N   . LEU   A 1 75  ? 6.59401  -45.08404 17.15222  1.000 86.43973  ? 75  LEU   A N   1 
ATOM   571  C CA  . LEU   A 1 75  ? 7.86131  -45.62236 16.67416  1.000 80.68677  ? 75  LEU   A CA  1 
ATOM   572  C C   . LEU   A 1 75  ? 8.82296  -45.84348 17.83002  1.000 80.04419  ? 75  LEU   A C   1 
ATOM   573  O O   . LEU   A 1 75  ? 8.91152  -45.01515 18.74257  1.000 81.85373  ? 75  LEU   A O   1 
ATOM   574  C CB  . LEU   A 1 75  ? 8.51597  -44.67982 15.66387  1.000 74.74024  ? 75  LEU   A CB  1 
ATOM   575  C CG  . LEU   A 1 75  ? 8.48783  -45.09001 14.19638  1.000 72.87188  ? 75  LEU   A CG  1 
ATOM   576  C CD1 . LEU   A 1 75  ? 7.07421  -45.42247 13.76336  1.000 73.12673  ? 75  LEU   A CD1 1 
ATOM   577  C CD2 . LEU   A 1 75  ? 9.06223  -43.96422 13.35595  1.000 76.32455  ? 75  LEU   A CD2 1 
ATOM   578  N N   . ARG   A 1 76  ? 9.56184  -46.94813 17.77102  1.000 78.74683  ? 76  ARG   A N   1 
ATOM   579  C CA  . ARG   A 1 76  ? 10.56037 -47.25607 18.78261  1.000 79.66957  ? 76  ARG   A CA  1 
ATOM   580  C C   . ARG   A 1 76  ? 11.90341 -46.66049 18.37915  1.000 76.69855  ? 76  ARG   A C   1 
ATOM   581  O O   . ARG   A 1 76  ? 12.38345 -46.89678 17.26707  1.000 75.87894  ? 76  ARG   A O   1 
ATOM   582  C CB  . ARG   A 1 76  ? 10.67665 -48.76766 18.98259  1.000 77.32054  ? 76  ARG   A CB  1 
ATOM   583  N N   . VAL   A 1 77  ? 12.50007 -45.88481 19.28746  1.000 74.81466  ? 77  VAL   A N   1 
ATOM   584  C CA  . VAL   A 1 77  ? 13.80449 -45.26185 19.08367  1.000 75.72272  ? 77  VAL   A CA  1 
ATOM   585  C C   . VAL   A 1 77  ? 14.89524 -46.23528 19.50313  1.000 75.41541  ? 77  VAL   A C   1 
ATOM   586  O O   . VAL   A 1 77  ? 14.78959 -46.89606 20.54350  1.000 81.91439  ? 77  VAL   A O   1 
ATOM   587  C CB  . VAL   A 1 77  ? 13.90855 -43.94666 19.87655  1.000 79.15943  ? 77  VAL   A CB  1 
ATOM   588  C CG1 . VAL   A 1 77  ? 15.19270 -43.21656 19.52930  1.000 78.05936  ? 77  VAL   A CG1 1 
ATOM   589  C CG2 . VAL   A 1 77  ? 12.69098 -43.07040 19.61006  1.000 77.96669  ? 77  VAL   A CG2 1 
ATOM   590  N N   . ILE   A 1 78  ? 15.95738 -46.32627 18.70087  1.000 73.62142  ? 78  ILE   A N   1 
ATOM   591  C CA  . ILE   A 1 78  ? 17.00712 -47.30776 18.97052  1.000 77.68214  ? 78  ILE   A CA  1 
ATOM   592  C C   . ILE   A 1 78  ? 18.35073 -46.60639 19.13970  1.000 72.98356  ? 78  ILE   A C   1 
ATOM   593  O O   . ILE   A 1 78  ? 19.22985 -47.09144 19.85883  1.000 75.79173  ? 78  ILE   A O   1 
ATOM   594  C CB  . ILE   A 1 78  ? 17.03112 -48.41703 17.88470  1.000 77.37982  ? 78  ILE   A CB  1 
ATOM   595  C CG1 . ILE   A 1 78  ? 17.56350 -47.96182 16.51045  1.000 75.56791  ? 78  ILE   A CG1 1 
ATOM   596  C CG2 . ILE   A 1 78  ? 15.65158 -49.03585 17.73035  1.000 75.80783  ? 78  ILE   A CG2 1 
ATOM   597  C CD1 . ILE   A 1 78  ? 19.07541 -47.96098 16.36946  1.000 84.32762  ? 78  ILE   A CD1 1 
ATOM   598  N N   . GLY   A 1 79  ? 18.50047 -45.44797 18.51969  1.000 75.79651  ? 79  GLY   A N   1 
ATOM   599  C CA  . GLY   A 1 79  ? 19.72978 -44.68140 18.62495  1.000 71.09017  ? 79  GLY   A CA  1 
ATOM   600  C C   . GLY   A 1 79  ? 19.43810 -43.20999 18.46312  1.000 70.83745  ? 79  GLY   A C   1 
ATOM   601  O O   . GLY   A 1 79  ? 18.51466 -42.81762 17.74509  1.000 72.58054  ? 79  GLY   A O   1 
ATOM   602  N N   . HIS   A 1 80  ? 20.22945 -42.38740 19.14151  1.000 71.04840  ? 80  HIS   A N   1 
ATOM   603  C CA  . HIS   A 1 80  ? 20.01001 -40.94796 19.13720  1.000 70.50231  ? 80  HIS   A CA  1 
ATOM   604  C C   . HIS   A 1 80  ? 21.34622 -40.22925 19.19128  1.000 73.63662  ? 80  HIS   A C   1 
ATOM   605  O O   . HIS   A 1 80  ? 22.19025 -40.55018 20.03106  1.000 76.34760  ? 80  HIS   A O   1 
ATOM   606  C CB  . HIS   A 1 80  ? 19.13830 -40.50792 20.31813  1.000 72.52438  ? 80  HIS   A CB  1 
ATOM   607  C CG  . HIS   A 1 80  ? 19.73146 -40.81640 21.65784  1.000 81.54292  ? 80  HIS   A CG  1 
ATOM   608  N ND1 . HIS   A 1 80  ? 20.23567 -42.05707 21.98607  1.000 83.50864  ? 80  HIS   A ND1 1 
ATOM   609  C CD2 . HIS   A 1 80  ? 19.93271 -40.03044 22.74167  1.000 81.69567  ? 80  HIS   A CD2 1 
ATOM   610  C CE1 . HIS   A 1 80  ? 20.70266 -42.02651 23.22136  1.000 90.82847  ? 80  HIS   A CE1 1 
ATOM   611  N NE2 . HIS   A 1 80  ? 20.53185 -40.80782 23.70169  1.000 81.32809  ? 80  HIS   A NE2 1 
ATOM   612  N N   . SER   A 1 81  ? 21.52997 -39.25262 18.30679  1.000 70.55921  ? 81  SER   A N   1 
ATOM   613  C CA  . SER   A 1 81  ? 22.73490 -38.43825 18.29559  1.000 68.75473  ? 81  SER   A CA  1 
ATOM   614  C C   . SER   A 1 81  ? 22.35114 -36.98415 18.07512  1.000 75.64478  ? 81  SER   A C   1 
ATOM   615  O O   . SER   A 1 81  ? 21.23295 -36.66992 17.65790  1.000 73.51315  ? 81  SER   A O   1 
ATOM   616  C CB  . SER   A 1 81  ? 23.72134 -38.90892 17.22048  1.000 70.40935  ? 81  SER   A CB  1 
ATOM   617  O OG  . SER   A 1 81  ? 23.11641 -38.91933 15.93948  1.000 72.81947  ? 81  SER   A OG  1 
ATOM   618  N N   . MET   A 1 82  ? 23.29195 -36.09333 18.36501  1.000 75.95793  ? 82  MET   A N   1 
ATOM   619  C CA  . MET   A 1 82  ? 23.06375 -34.66256 18.23674  1.000 75.74242  ? 82  MET   A CA  1 
ATOM   620  C C   . MET   A 1 82  ? 24.00774 -34.07593 17.19741  1.000 72.39803  ? 82  MET   A C   1 
ATOM   621  O O   . MET   A 1 82  ? 25.19757 -34.40759 17.16826  1.000 71.75251  ? 82  MET   A O   1 
ATOM   622  C CB  . MET   A 1 82  ? 23.24431 -33.95464 19.58411  1.000 77.88882  ? 82  MET   A CB  1 
ATOM   623  C CG  . MET   A 1 82  ? 23.50845 -32.46786 19.48339  1.000 82.55748  ? 82  MET   A CG  1 
ATOM   624  S SD  . MET   A 1 82  ? 22.76135 -31.56904 20.85125  1.000 79.99082  ? 82  MET   A SD  1 
ATOM   625  C CE  . MET   A 1 82  ? 24.08146 -31.64083 22.06129  1.000 81.57440  ? 82  MET   A CE  1 
ATOM   626  N N   . GLN   A 1 83  ? 23.46381 -33.21603 16.33389  1.000 69.27847  ? 83  GLN   A N   1 
ATOM   627  C CA  . GLN   A 1 83  ? 24.24085 -32.51217 15.31371  1.000 70.56307  ? 83  GLN   A CA  1 
ATOM   628  C C   . GLN   A 1 83  ? 23.88304 -31.03229 15.34956  1.000 64.13708  ? 83  GLN   A C   1 
ATOM   629  O O   . GLN   A 1 83  ? 22.83882 -30.63146 14.82944  1.000 60.69831  ? 83  GLN   A O   1 
ATOM   630  C CB  . GLN   A 1 83  ? 24.00104 -33.08817 13.92635  1.000 67.75303  ? 83  GLN   A CB  1 
ATOM   631  C CG  . GLN   A 1 83  ? 25.05272 -32.63786 12.93890  1.000 66.93281  ? 83  GLN   A CG  1 
ATOM   632  C CD  . GLN   A 1 83  ? 24.82472 -33.18955 11.56141  1.000 70.06639  ? 83  GLN   A CD  1 
ATOM   633  O OE1 . GLN   A 1 83  ? 23.79360 -33.80441 11.29226  1.000 72.39036  ? 83  GLN   A OE1 1 
ATOM   634  N NE2 . GLN   A 1 83  ? 25.80204 -33.00245 10.68092  1.000 74.61911  ? 83  GLN   A NE2 1 
ATOM   635  N N   . ASN   A 1 84  ? 24.76782 -30.22707 15.93522  1.000 64.91988  ? 84  ASN   A N   1 
ATOM   636  C CA  . ASN   A 1 84  ? 24.56011 -28.78683 16.09610  1.000 62.77905  ? 84  ASN   A CA  1 
ATOM   637  C C   . ASN   A 1 84  ? 23.27196 -28.60310 16.88866  1.000 65.02026  ? 84  ASN   A C   1 
ATOM   638  O O   . ASN   A 1 84  ? 23.18143 -29.11544 18.01885  1.000 65.30641  ? 84  ASN   A O   1 
ATOM   639  C CB  . ASN   A 1 84  ? 24.59237 -28.10755 14.72322  1.000 61.91735  ? 84  ASN   A CB  1 
ATOM   640  C CG  . ASN   A 1 84  ? 25.82919 -28.45681 13.92265  1.000 61.83715  ? 84  ASN   A CG  1 
ATOM   641  O OD1 . ASN   A 1 84  ? 26.94938 -28.14451 14.32148  1.000 62.55088  ? 84  ASN   A OD1 1 
ATOM   642  N ND2 . ASN   A 1 84  ? 25.63014 -29.09581 12.77680  1.000 63.92942  ? 84  ASN   A ND2 1 
ATOM   643  N N   . CYS   A 1 85  ? 22.25913 -27.92837 16.35203  1.000 61.29021  ? 85  CYS   A N   1 
ATOM   644  C CA  . CYS   A 1 85  ? 21.01643 -27.67347 17.05872  1.000 60.16224  ? 85  CYS   A CA  1 
ATOM   645  C C   . CYS   A 1 85  ? 19.90832 -28.65010 16.66710  1.000 63.48956  ? 85  CYS   A C   1 
ATOM   646  O O   . CYS   A 1 85  ? 18.73513 -28.40263 16.97622  1.000 60.62319  ? 85  CYS   A O   1 
ATOM   647  C CB  . CYS   A 1 85  ? 20.57616 -26.22974 16.81189  1.000 58.91148  ? 85  CYS   A CB  1 
ATOM   648  S SG  . CYS   A 1 85  ? 21.75515 -24.98648 17.41608  1.000 58.18794  ? 85  CYS   A SG  1 
ATOM   649  N N   . VAL   A 1 86  ? 20.25165 -29.75015 15.99297  1.000 58.53224  ? 86  VAL   A N   1 
ATOM   650  C CA  . VAL   A 1 86  ? 19.27129 -30.74827 15.57882  1.000 58.87837  ? 86  VAL   A CA  1 
ATOM   651  C C   . VAL   A 1 86  ? 19.50976 -32.03286 16.35758  1.000 60.55105  ? 86  VAL   A C   1 
ATOM   652  O O   . VAL   A 1 86  ? 20.63623 -32.35185 16.75779  1.000 66.37080  ? 86  VAL   A O   1 
ATOM   653  C CB  . VAL   A 1 86  ? 19.30541 -31.02584 14.05840  1.000 59.75722  ? 86  VAL   A CB  1 
ATOM   654  C CG1 . VAL   A 1 86  ? 20.35118 -32.08012 13.71248  1.000 63.55525  ? 86  VAL   A CG1 1 
ATOM   655  C CG2 . VAL   A 1 86  ? 17.93975 -31.46649 13.57212  1.000 56.50438  ? 86  VAL   A CG2 1 
ATOM   656  N N   . LEU   A 1 87  ? 18.42987 -32.77275 16.57596  1.000 61.20781  ? 87  LEU   A N   1 
ATOM   657  C CA  . LEU   A 1 87  ? 18.48095 -34.07045 17.23175  1.000 63.66581  ? 87  LEU   A CA  1 
ATOM   658  C C   . LEU   A 1 87  ? 18.07596 -35.13727 16.22423  1.000 61.07107  ? 87  LEU   A C   1 
ATOM   659  O O   . LEU   A 1 87  ? 17.09577 -34.96585 15.48983  1.000 55.56307  ? 87  LEU   A O   1 
ATOM   660  C CB  . LEU   A 1 87  ? 17.56856 -34.08794 18.46129  1.000 60.62087  ? 87  LEU   A CB  1 
ATOM   661  C CG  . LEU   A 1 87  ? 17.37560 -35.35801 19.29133  1.000 63.22803  ? 87  LEU   A CG  1 
ATOM   662  C CD1 . LEU   A 1 87  ? 18.57619 -35.63136 20.18416  1.000 68.38566  ? 87  LEU   A CD1 1 
ATOM   663  C CD2 . LEU   A 1 87  ? 16.11848 -35.21697 20.13094  1.000 60.97124  ? 87  LEU   A CD2 1 
ATOM   664  N N   . LYS   A 1 88  ? 18.84354 -36.22047 16.17277  1.000 62.69644  ? 88  LYS   A N   1 
ATOM   665  C CA  . LYS   A 1 88  ? 18.60732 -37.31258 15.23898  1.000 61.77273  ? 88  LYS   A CA  1 
ATOM   666  C C   . LYS   A 1 88  ? 18.28365 -38.57983 16.01742  1.000 66.04963  ? 88  LYS   A C   1 
ATOM   667  O O   . LYS   A 1 88  ? 19.06182 -38.99218 16.88311  1.000 69.98312  ? 88  LYS   A O   1 
ATOM   668  C CB  . LYS   A 1 88  ? 19.82959 -37.54627 14.35168  1.000 63.46719  ? 88  LYS   A CB  1 
ATOM   669  C CG  . LYS   A 1 88  ? 20.10755 -36.45087 13.34607  1.000 63.26398  ? 88  LYS   A CG  1 
ATOM   670  C CD  . LYS   A 1 88  ? 21.60667 -36.24679 13.20156  1.000 67.23261  ? 88  LYS   A CD  1 
ATOM   671  C CE  . LYS   A 1 88  ? 22.10108 -36.76787 11.86345  1.000 68.52194  ? 88  LYS   A CE  1 
ATOM   672  N NZ  . LYS   A 1 88  ? 23.58113 -36.87052 11.82392  1.000 73.32430  ? 88  LYS   A NZ  1 
ATOM   673  N N   . LEU   A 1 89  ? 17.14761 -39.20060 15.70147  1.000 64.80887  ? 89  LEU   A N   1 
ATOM   674  C CA  . LEU   A 1 89  ? 16.68940 -40.41066 16.37776  1.000 66.26019  ? 89  LEU   A CA  1 
ATOM   675  C C   . LEU   A 1 89  ? 16.60968 -41.54802 15.36813  1.000 67.84415  ? 89  LEU   A C   1 
ATOM   676  O O   . LEU   A 1 89  ? 15.95667 -41.41377 14.32746  1.000 68.74300  ? 89  LEU   A O   1 
ATOM   677  C CB  . LEU   A 1 89  ? 15.32523 -40.19105 17.03926  1.000 66.53123  ? 89  LEU   A CB  1 
ATOM   678  C CG  . LEU   A 1 89  ? 15.13703 -38.96911 17.94509  1.000 65.79203  ? 89  LEU   A CG  1 
ATOM   679  C CD1 . LEU   A 1 89  ? 13.65772 -38.71596 18.22206  1.000 56.85902  ? 89  LEU   A CD1 1 
ATOM   680  C CD2 . LEU   A 1 89  ? 15.90756 -39.13364 19.24566  1.000 69.32780  ? 89  LEU   A CD2 1 
ATOM   681  N N   . LYS   A 1 90  ? 17.26319 -42.66419 15.68087  1.000 67.47591  ? 90  LYS   A N   1 
ATOM   682  C CA  . LYS   A 1 90  ? 17.24189 -43.85316 14.83667  1.000 69.65607  ? 90  LYS   A CA  1 
ATOM   683  C C   . LYS   A 1 90  ? 16.04668 -44.71858 15.22173  1.000 76.21288  ? 90  LYS   A C   1 
ATOM   684  O O   . LYS   A 1 90  ? 15.95514 -45.18411 16.36379  1.000 77.63166  ? 90  LYS   A O   1 
ATOM   685  C CB  . LYS   A 1 90  ? 18.54636 -44.63739 14.98842  1.000 74.59310  ? 90  LYS   A CB  1 
ATOM   686  C CG  . LYS   A 1 90  ? 19.25902 -44.96009 13.68312  1.000 73.49266  ? 90  LYS   A CG  1 
ATOM   687  C CD  . LYS   A 1 90  ? 18.81871 -46.30397 13.14458  1.000 72.52648  ? 90  LYS   A CD  1 
ATOM   688  C CE  . LYS   A 1 90  ? 19.74624 -46.78948 12.04952  1.000 77.59415  ? 90  LYS   A CE  1 
ATOM   689  N NZ  . LYS   A 1 90  ? 19.28785 -48.08819 11.47933  1.000 76.80225  ? 90  LYS   A NZ  1 
ATOM   690  N N   . VAL   A 1 91  ? 15.13476 -44.93466 14.27606  1.000 75.34555  ? 91  VAL   A N   1 
ATOM   691  C CA  . VAL   A 1 91  ? 13.93155 -45.72028 14.52182  1.000 77.29360  ? 91  VAL   A CA  1 
ATOM   692  C C   . VAL   A 1 91  ? 14.05580 -47.05239 13.79318  1.000 77.56888  ? 91  VAL   A C   1 
ATOM   693  O O   . VAL   A 1 91  ? 14.71763 -47.15756 12.75528  1.000 76.36831  ? 91  VAL   A O   1 
ATOM   694  C CB  . VAL   A 1 91  ? 12.65520 -44.96088 14.09257  1.000 77.73801  ? 91  VAL   A CB  1 
ATOM   695  C CG1 . VAL   A 1 91  ? 12.36058 -43.82554 15.06815  1.000 69.84752  ? 91  VAL   A CG1 1 
ATOM   696  C CG2 . VAL   A 1 91  ? 12.78839 -44.42643 12.67641  1.000 70.10181  ? 91  VAL   A CG2 1 
ATOM   697  N N   . ASP   A 1 92  ? 13.41329 -48.08345 14.35115  1.000 86.24446  ? 92  ASP   A N   1 
ATOM   698  C CA  . ASP   A 1 92  ? 13.47159 -49.44683 13.81264  1.000 85.77018  ? 92  ASP   A CA  1 
ATOM   699  C C   . ASP   A 1 92  ? 12.65963 -49.62008 12.51869  1.000 84.17834  ? 92  ASP   A C   1 
ATOM   700  O O   . ASP   A 1 92  ? 12.53035 -50.74502 12.01233  1.000 80.33864  ? 92  ASP   A O   1 
ATOM   701  C CB  . ASP   A 1 92  ? 13.00257 -50.43227 14.88762  1.000 89.82118  ? 92  ASP   A CB  1 
ATOM   702  C CG  . ASP   A 1 92  ? 11.49733 -50.64569 14.88036  1.000 95.04396  ? 92  ASP   A CG  1 
ATOM   703  O OD1 . ASP   A 1 92  ? 10.77372 -49.80078 15.45602  1.000 91.71323  ? 92  ASP   A OD1 1 
ATOM   704  O OD2 . ASP   A 1 92  ? 11.04457 -51.68718 14.34857  1.000 97.54466  ? 92  ASP   A OD2 1 
ATOM   705  N N   . THR   A 1 93  ? 12.13054 -48.53317 11.95924  1.000 86.74241  ? 93  THR   A N   1 
ATOM   706  C CA  . THR   A 1 93  ? 11.30367 -48.60003 10.76365  1.000 83.72646  ? 93  THR   A CA  1 
ATOM   707  C C   . THR   A 1 93  ? 11.68857 -47.46056 9.83305   1.000 76.64431  ? 93  THR   A C   1 
ATOM   708  O O   . THR   A 1 93  ? 11.79123 -46.30853 10.26500  1.000 70.80679  ? 93  THR   A O   1 
ATOM   709  C CB  . THR   A 1 93  ? 9.81277  -48.51456 11.11903  1.000 84.89888  ? 93  THR   A CB  1 
ATOM   710  O OG1 . THR   A 1 93  ? 9.42586  -49.69532 11.82962  1.000 83.88925  ? 93  THR   A OG1 1 
ATOM   711  C CG2 . THR   A 1 93  ? 8.96578  -48.41018 9.86004   1.000 81.10653  ? 93  THR   A CG2 1 
ATOM   712  N N   . ALA   A 1 94  ? 11.91695 -47.78839 8.56516   1.000 77.37729  ? 94  ALA   A N   1 
ATOM   713  C CA  . ALA   A 1 94  ? 12.12879 -46.77392 7.54505   1.000 74.35765  ? 94  ALA   A CA  1 
ATOM   714  C C   . ALA   A 1 94  ? 10.77893 -46.27647 7.04930   1.000 72.69091  ? 94  ALA   A C   1 
ATOM   715  O O   . ALA   A 1 94  ? 9.87840  -47.07557 6.77923   1.000 74.32904  ? 94  ALA   A O   1 
ATOM   716  C CB  . ALA   A 1 94  ? 12.94956 -47.34007 6.38731   1.000 73.30175  ? 94  ALA   A CB  1 
ATOM   717  N N   . ASN   A 1 95  ? 10.63475 -44.95967 6.94168   1.000 70.89163  ? 95  ASN   A N   1 
ATOM   718  C CA  . ASN   A 1 95  ? 9.36640  -44.37675 6.52632   1.000 66.84544  ? 95  ASN   A CA  1 
ATOM   719  C C   . ASN   A 1 95  ? 9.01682  -44.82455 5.11326   1.000 65.38741  ? 95  ASN   A C   1 
ATOM   720  O O   . ASN   A 1 95  ? 9.69927  -44.44393 4.15554   1.000 71.24197  ? 95  ASN   A O   1 
ATOM   721  C CB  . ASN   A 1 95  ? 9.43092  -42.85202 6.62246   1.000 67.61611  ? 95  ASN   A CB  1 
ATOM   722  C CG  . ASN   A 1 95  ? 8.18316  -42.17381 6.09465   1.000 64.07900  ? 95  ASN   A CG  1 
ATOM   723  O OD1 . ASN   A 1 95  ? 7.09966  -42.75355 6.07273   1.000 68.83194  ? 95  ASN   A OD1 1 
ATOM   724  N ND2 . ASN   A 1 95  ? 8.33143  -40.92607 5.67921   1.000 63.74952  ? 95  ASN   A ND2 1 
ATOM   725  N N   . PRO   A 1 96  ? 7.96693  -45.63163 4.94201   1.000 66.09209  ? 96  PRO   A N   1 
ATOM   726  C CA  . PRO   A 1 96  ? 7.60749  -46.08382 3.58880   1.000 66.97644  ? 96  PRO   A CA  1 
ATOM   727  C C   . PRO   A 1 96  ? 7.19212  -44.95535 2.65745   1.000 70.83014  ? 96  PRO   A C   1 
ATOM   728  O O   . PRO   A 1 96  ? 7.21029  -45.14622 1.43421   1.000 75.92121  ? 96  PRO   A O   1 
ATOM   729  C CB  . PRO   A 1 96  ? 6.45120  -47.06146 3.84187   1.000 67.68397  ? 96  PRO   A CB  1 
ATOM   730  C CG  . PRO   A 1 96  ? 5.87100  -46.63391 5.14372   1.000 64.90372  ? 96  PRO   A CG  1 
ATOM   731  C CD  . PRO   A 1 96  ? 7.02815  -46.13388 5.96148   1.000 66.53341  ? 96  PRO   A CD  1 
ATOM   732  N N   . LYS   A 1 97  ? 6.82325  -43.78858 3.18810   1.000 64.21785  ? 97  LYS   A N   1 
ATOM   733  C CA  . LYS   A 1 97  ? 6.49179  -42.62969 2.37179   1.000 65.91503  ? 97  LYS   A CA  1 
ATOM   734  C C   . LYS   A 1 97  ? 7.68107  -41.69788 2.17473   1.000 66.59647  ? 97  LYS   A C   1 
ATOM   735  O O   . LYS   A 1 97  ? 7.49058  -40.53320 1.80640   1.000 68.01786  ? 97  LYS   A O   1 
ATOM   736  C CB  . LYS   A 1 97  ? 5.31671  -41.86563 2.98441   1.000 64.00886  ? 97  LYS   A CB  1 
ATOM   737  C CG  . LYS   A 1 97  ? 3.95985  -42.44643 2.63059   1.000 73.02296  ? 97  LYS   A CG  1 
ATOM   738  C CD  . LYS   A 1 97  ? 2.89413  -42.04420 3.63947   1.000 77.60542  ? 97  LYS   A CD  1 
ATOM   739  C CE  . LYS   A 1 97  ? 1.62582  -42.86667 3.43743   1.000 85.68949  ? 97  LYS   A CE  1 
ATOM   740  N NZ  . LYS   A 1 97  ? 0.45330  -42.32598 4.18318   1.000 89.71036  ? 97  LYS   A NZ  1 
ATOM   741  N N   . THR   A 1 98  ? 8.89740  -42.18406 2.40706   1.000 64.48654  ? 98  THR   A N   1 
ATOM   742  C CA  . THR   A 1 98  ? 10.07550 -41.34068 2.24152   1.000 63.91434  ? 98  THR   A CA  1 
ATOM   743  C C   . THR   A 1 98  ? 10.21539 -40.94689 0.77510   1.000 65.08593  ? 98  THR   A C   1 
ATOM   744  O O   . THR   A 1 98  ? 10.17723 -41.81786 -0.10146  1.000 65.34981  ? 98  THR   A O   1 
ATOM   745  C CB  . THR   A 1 98  ? 11.34289 -42.05603 2.70505   1.000 66.15070  ? 98  THR   A CB  1 
ATOM   746  O OG1 . THR   A 1 98  ? 11.23550 -42.37332 4.09492   1.000 66.21787  ? 98  THR   A OG1 1 
ATOM   747  C CG2 . THR   A 1 98  ? 12.54967 -41.14474 2.51605   1.000 64.27057  ? 98  THR   A CG2 1 
ATOM   748  N N   . PRO   A 1 99  ? 10.35805 -39.66189 0.46437   1.000 66.10569  ? 99  PRO   A N   1 
ATOM   749  C CA  . PRO   A 1 99  ? 10.52825 -39.26021 -0.93888  1.000 64.89727  ? 99  PRO   A CA  1 
ATOM   750  C C   . PRO   A 1 99  ? 11.98509 -39.20328 -1.35851  1.000 64.33555  ? 99  PRO   A C   1 
ATOM   751  O O   . PRO   A 1 99  ? 12.88220 -39.42303 -0.53621  1.000 65.18029  ? 99  PRO   A O   1 
ATOM   752  C CB  . PRO   A 1 99  ? 9.88850  -37.87118 -0.97275  1.000 65.64754  ? 99  PRO   A CB  1 
ATOM   753  C CG  . PRO   A 1 99  ? 10.10694 -37.33277 0.41165   1.000 62.34484  ? 99  PRO   A CG  1 
ATOM   754  C CD  . PRO   A 1 99  ? 10.16644 -38.50361 1.35921   1.000 60.10844  ? 99  PRO   A CD  1 
ATOM   755  N N   . LYS   A 1 100 ? 12.23168 -38.92801 -2.63775  1.000 63.31933  ? 100 LYS   A N   1 
ATOM   756  C CA  . LYS   A 1 100 ? 13.56489 -38.51986 -3.05794  1.000 65.11437  ? 100 LYS   A CA  1 
ATOM   757  C C   . LYS   A 1 100 ? 13.82715 -37.15419 -2.44202  1.000 63.97480  ? 100 LYS   A C   1 
ATOM   758  O O   . LYS   A 1 100 ? 13.10592 -36.19471 -2.73141  1.000 67.84379  ? 100 LYS   A O   1 
ATOM   759  C CB  . LYS   A 1 100 ? 13.66829 -38.46784 -4.57948  1.000 71.69691  ? 100 LYS   A CB  1 
ATOM   760  C CG  . LYS   A 1 100 ? 12.87540 -39.53387 -5.31685  1.000 78.42039  ? 100 LYS   A CG  1 
ATOM   761  C CD  . LYS   A 1 100 ? 13.71915 -40.76966 -5.58459  1.000 84.32384  ? 100 LYS   A CD  1 
ATOM   762  C CE  . LYS   A 1 100 ? 14.51155 -40.63448 -6.87540  1.000 87.48755  ? 100 LYS   A CE  1 
ATOM   763  N NZ  . LYS   A 1 100 ? 13.63024 -40.32457 -8.03403  1.000 87.97565  ? 100 LYS   A NZ  1 
ATOM   764  N N   . TYR   A 1 101 ? 14.82317 -37.05911 -1.56312  1.000 62.42995  ? 101 TYR   A N   1 
ATOM   765  C CA  . TYR   A 1 101 ? 15.02050 -35.84009 -0.79354  1.000 62.54794  ? 101 TYR   A CA  1 
ATOM   766  C C   . TYR   A 1 101 ? 16.48198 -35.41174 -0.80106  1.000 61.66436  ? 101 TYR   A C   1 
ATOM   767  O O   . TYR   A 1 101 ? 17.38167 -36.15109 -1.21482  1.000 53.09097  ? 101 TYR   A O   1 
ATOM   768  C CB  . TYR   A 1 101 ? 14.52987 -36.00069 0.65226   1.000 61.68233  ? 101 TYR   A CB  1 
ATOM   769  C CG  . TYR   A 1 101 ? 15.36468 -36.92620 1.51268   1.000 60.36488  ? 101 TYR   A CG  1 
ATOM   770  C CD1 . TYR   A 1 101 ? 16.46561 -36.45007 2.22077   1.000 59.09438  ? 101 TYR   A CD1 1 
ATOM   771  C CD2 . TYR   A 1 101 ? 15.03039 -38.26473 1.64802   1.000 56.69308  ? 101 TYR   A CD2 1 
ATOM   772  C CE1 . TYR   A 1 101 ? 17.22203 -37.28763 3.01653   1.000 53.83421  ? 101 TYR   A CE1 1 
ATOM   773  C CE2 . TYR   A 1 101 ? 15.77596 -39.10644 2.44490   1.000 61.35598  ? 101 TYR   A CE2 1 
ATOM   774  C CZ  . TYR   A 1 101 ? 16.87139 -38.61400 3.12570   1.000 60.68184  ? 101 TYR   A CZ  1 
ATOM   775  O OH  . TYR   A 1 101 ? 17.61651 -39.45715 3.91717   1.000 69.59025  ? 101 TYR   A OH  1 
ATOM   776  N N   . LYS   A 1 102 ? 16.69543 -34.19628 -0.29974  1.000 56.67809  ? 102 LYS   A N   1 
ATOM   777  C CA  . LYS   A 1 102 ? 17.99917 -33.55310 -0.27263  1.000 56.12620  ? 102 LYS   A CA  1 
ATOM   778  C C   . LYS   A 1 102 ? 18.03118 -32.55224 0.87244   1.000 57.15990  ? 102 LYS   A C   1 
ATOM   779  O O   . LYS   A 1 102 ? 17.00441 -31.96339 1.22813   1.000 56.95019  ? 102 LYS   A O   1 
ATOM   780  C CB  . LYS   A 1 102 ? 18.29083 -32.84784 -1.59960  1.000 56.70117  ? 102 LYS   A CB  1 
ATOM   781  C CG  . LYS   A 1 102 ? 19.72672 -32.94235 -2.06062  1.000 58.29964  ? 102 LYS   A CG  1 
ATOM   782  C CD  . LYS   A 1 102 ? 19.98042 -32.01202 -3.23940  1.000 65.54427  ? 102 LYS   A CD  1 
ATOM   783  C CE  . LYS   A 1 102 ? 18.84589 -32.07853 -4.24846  1.000 66.99983  ? 102 LYS   A CE  1 
ATOM   784  N NZ  . LYS   A 1 102 ? 19.22377 -31.45832 -5.54375  1.000 77.05883  ? 102 LYS   A NZ  1 
ATOM   785  N N   . PHE   A 1 103 ? 19.22115 -32.36444 1.44241   1.000 54.84393  ? 103 PHE   A N   1 
ATOM   786  C CA  . PHE   A 1 103 ? 19.45867 -31.34456 2.46019   1.000 54.02494  ? 103 PHE   A CA  1 
ATOM   787  C C   . PHE   A 1 103 ? 20.36861 -30.28875 1.84377   1.000 55.89744  ? 103 PHE   A C   1 
ATOM   788  O O   . PHE   A 1 103 ? 21.54714 -30.55294 1.58138   1.000 54.53666  ? 103 PHE   A O   1 
ATOM   789  C CB  . PHE   A 1 103 ? 20.07968 -31.94166 3.72281   1.000 54.06245  ? 103 PHE   A CB  1 
ATOM   790  C CG  . PHE   A 1 103 ? 19.16087 -32.86538 4.48381   1.000 54.47158  ? 103 PHE   A CG  1 
ATOM   791  C CD1 . PHE   A 1 103 ? 17.79165 -32.84180 4.27268   1.000 56.18673  ? 103 PHE   A CD1 1 
ATOM   792  C CD2 . PHE   A 1 103 ? 19.67489 -33.76568 5.40483   1.000 55.27920  ? 103 PHE   A CD2 1 
ATOM   793  C CE1 . PHE   A 1 103 ? 16.95095 -33.69463 4.96958   1.000 58.40919  ? 103 PHE   A CE1 1 
ATOM   794  C CE2 . PHE   A 1 103 ? 18.84079 -34.62513 6.10202   1.000 59.20245  ? 103 PHE   A CE2 1 
ATOM   795  C CZ  . PHE   A 1 103 ? 17.47787 -34.58789 5.88590   1.000 59.24577  ? 103 PHE   A CZ  1 
ATOM   796  N N   . VAL   A 1 104 ? 19.81898 -29.10167 1.60346   1.000 50.34405  ? 104 VAL   A N   1 
ATOM   797  C CA  . VAL   A 1 104 ? 20.54408 -28.00765 0.97335   1.000 50.77815  ? 104 VAL   A CA  1 
ATOM   798  C C   . VAL   A 1 104 ? 20.41278 -26.76382 1.84229   1.000 54.86569  ? 104 VAL   A C   1 
ATOM   799  O O   . VAL   A 1 104 ? 19.34177 -26.48673 2.39524   1.000 53.13987  ? 104 VAL   A O   1 
ATOM   800  C CB  . VAL   A 1 104 ? 20.03188 -27.74191 -0.46090  1.000 52.18734  ? 104 VAL   A CB  1 
ATOM   801  C CG1 . VAL   A 1 104 ? 18.52511 -27.61241 -0.48232  1.000 51.81003  ? 104 VAL   A CG1 1 
ATOM   802  C CG2 . VAL   A 1 104 ? 20.68065 -26.49264 -1.04758  1.000 66.13234  ? 104 VAL   A CG2 1 
ATOM   803  N N   . ARG   A 1 105 ? 21.51444 -26.03225 1.98625   1.000 52.40839  ? 105 ARG   A N   1 
ATOM   804  C CA  . ARG   A 1 105 ? 21.50251 -24.73182 2.63913   1.000 50.60276  ? 105 ARG   A CA  1 
ATOM   805  C C   . ARG   A 1 105 ? 21.21783 -23.67200 1.58272   1.000 48.05585  ? 105 ARG   A C   1 
ATOM   806  O O   . ARG   A 1 105 ? 21.98675 -23.52224 0.62929   1.000 54.52182  ? 105 ARG   A O   1 
ATOM   807  C CB  . ARG   A 1 105 ? 22.83509 -24.46134 3.33699   1.000 47.02004  ? 105 ARG   A CB  1 
ATOM   808  C CG  . ARG   A 1 105 ? 22.88601 -23.14785 4.08921   1.000 49.91258  ? 105 ARG   A CG  1 
ATOM   809  C CD  . ARG   A 1 105 ? 23.99034 -23.15858 5.12903   1.000 52.95262  ? 105 ARG   A CD  1 
ATOM   810  N NE  . ARG   A 1 105 ? 23.93076 -21.97547 5.97807   1.000 56.63716  ? 105 ARG   A NE  1 
ATOM   811  C CZ  . ARG   A 1 105 ? 23.44506 -21.96535 7.21298   1.000 55.99671  ? 105 ARG   A CZ  1 
ATOM   812  N NH1 . ARG   A 1 105 ? 22.98309 -23.06879 7.78622   1.000 50.22860  ? 105 ARG   A NH1 1 
ATOM   813  N NH2 . ARG   A 1 105 ? 23.41309 -20.81850 7.88705   1.000 53.79867  ? 105 ARG   A NH2 1 
ATOM   814  N N   . ILE   A 1 106 ? 20.10916 -22.95229 1.73804   1.000 51.69286  ? 106 ILE   A N   1 
ATOM   815  C CA  . ILE   A 1 106 ? 19.73878 -21.92471 0.77076   1.000 54.17255  ? 106 ILE   A CA  1 
ATOM   816  C C   . ILE   A 1 106 ? 20.44569 -20.62933 1.13079   1.000 56.12652  ? 106 ILE   A C   1 
ATOM   817  O O   . ILE   A 1 106 ? 21.10307 -20.53248 2.17325   1.000 56.75873  ? 106 ILE   A O   1 
ATOM   818  C CB  . ILE   A 1 106 ? 18.21527 -21.70726 0.69876   1.000 56.26014  ? 106 ILE   A CB  1 
ATOM   819  C CG1 . ILE   A 1 106 ? 17.60154 -21.71035 2.09951   1.000 54.58399  ? 106 ILE   A CG1 1 
ATOM   820  C CG2 . ILE   A 1 106 ? 17.56821 -22.74726 -0.20027  1.000 60.28248  ? 106 ILE   A CG2 1 
ATOM   821  C CD1 . ILE   A 1 106 ? 17.60318 -20.35932 2.76454   1.000 52.70450  ? 106 ILE   A CD1 1 
ATOM   822  N N   . GLN   A 1 107 ? 20.30279 -19.63013 0.27732   1.000 55.70776  ? 107 GLN   A N   1 
ATOM   823  C CA  . GLN   A 1 107 ? 20.96809 -18.35503 0.42947   1.000 54.60160  ? 107 GLN   A CA  1 
ATOM   824  C C   . GLN   A 1 107 ? 19.95059 -17.25601 0.68652   1.000 55.87096  ? 107 GLN   A C   1 
ATOM   825  O O   . GLN   A 1 107 ? 18.77068 -17.39578 0.34105   1.000 51.41766  ? 107 GLN   A O   1 
ATOM   826  C CB  . GLN   A 1 107 ? 21.78511 -18.03014 -0.82758  1.000 59.80705  ? 107 GLN   A CB  1 
ATOM   827  C CG  . GLN   A 1 107 ? 22.93590 -18.98663 -1.06561  1.000 66.44236  ? 107 GLN   A CG  1 
ATOM   828  C CD  . GLN   A 1 107 ? 23.93080 -18.45054 -2.06839  1.000 83.18633  ? 107 GLN   A CD  1 
ATOM   829  O OE1 . GLN   A 1 107 ? 24.14414 -19.04008 -3.12864  1.000 91.98258  ? 107 GLN   A OE1 1 
ATOM   830  N NE2 . GLN   A 1 107 ? 24.54738 -17.32024 -1.73948  1.000 85.73822  ? 107 GLN   A NE2 1 
ATOM   831  N N   . PRO   A 1 108 ? 20.36398 -16.15391 1.31591   1.000 56.24434  ? 108 PRO   A N   1 
ATOM   832  C CA  . PRO   A 1 108 ? 19.44320 -15.02597 1.48951   1.000 52.90351  ? 108 PRO   A CA  1 
ATOM   833  C C   . PRO   A 1 108 ? 18.83134 -14.63207 0.15457   1.000 50.23714  ? 108 PRO   A C   1 
ATOM   834  O O   . PRO   A 1 108 ? 19.50792 -14.59711 -0.87573  1.000 55.02204  ? 108 PRO   A O   1 
ATOM   835  C CB  . PRO   A 1 108 ? 20.33636 -13.91502 2.05226   1.000 49.98073  ? 108 PRO   A CB  1 
ATOM   836  C CG  . PRO   A 1 108 ? 21.48733 -14.62258 2.66641   1.000 55.50304  ? 108 PRO   A CG  1 
ATOM   837  C CD  . PRO   A 1 108 ? 21.69893 -15.87625 1.87684   1.000 54.80593  ? 108 PRO   A CD  1 
ATOM   838  N N   . GLY   A 1 109 ? 17.52832 -14.36963 0.17568   1.000 47.39475  ? 109 GLY   A N   1 
ATOM   839  C CA  . GLY   A 1 109 ? 16.78170 -14.00664 -0.99742  1.000 47.08454  ? 109 GLY   A CA  1 
ATOM   840  C C   . GLY   A 1 109 ? 16.01364 -15.15481 -1.61266  1.000 47.45004  ? 109 GLY   A C   1 
ATOM   841  O O   . GLY   A 1 109 ? 14.96375 -14.92840 -2.22419  1.000 51.81724  ? 109 GLY   A O   1 
ATOM   842  N N   . GLN   A 1 110 ? 16.50587 -16.37999 -1.45779  1.000 51.71378  ? 110 GLN   A N   1 
ATOM   843  C CA  . GLN   A 1 110 ? 15.79971 -17.53235 -1.99094  1.000 50.97585  ? 110 GLN   A CA  1 
ATOM   844  C C   . GLN   A 1 110 ? 14.50621 -17.77917 -1.22427  1.000 51.00281  ? 110 GLN   A C   1 
ATOM   845  O O   . GLN   A 1 110 ? 14.34436 -17.38234 -0.06504  1.000 47.09982  ? 110 GLN   A O   1 
ATOM   846  C CB  . GLN   A 1 110 ? 16.68378 -18.77105 -1.94260  1.000 51.65950  ? 110 GLN   A CB  1 
ATOM   847  C CG  . GLN   A 1 110 ? 18.03466 -18.54207 -2.57302  1.000 57.00296  ? 110 GLN   A CG  1 
ATOM   848  C CD  . GLN   A 1 110 ? 18.69259 -19.83078 -2.96663  1.000 61.19999  ? 110 GLN   A CD  1 
ATOM   849  O OE1 . GLN   A 1 110 ? 19.36905 -20.46853 -2.16233  1.000 65.85637  ? 110 GLN   A OE1 1 
ATOM   850  N NE2 . GLN   A 1 110 ? 18.47975 -20.24088 -4.21195  1.000 70.60481  ? 110 GLN   A NE2 1 
ATOM   851  N N   . THR   A 1 111 ? 13.57483 -18.44435 -1.89567  1.000 48.81935  ? 111 THR   A N   1 
ATOM   852  C CA  . THR   A 1 111 ? 12.25301 -18.69116 -1.35219  1.000 50.23902  ? 111 THR   A CA  1 
ATOM   853  C C   . THR   A 1 111 ? 12.04430 -20.18620 -1.16725  1.000 46.73557  ? 111 THR   A C   1 
ATOM   854  O O   . THR   A 1 111 ? 12.74249 -21.01074 -1.76153  1.000 52.42806  ? 111 THR   A O   1 
ATOM   855  C CB  . THR   A 1 111 ? 11.16154 -18.11673 -2.26276  1.000 52.16632  ? 111 THR   A CB  1 
ATOM   856  O OG1 . THR   A 1 111 ? 11.32168 -18.63977 -3.58621  1.000 53.07197  ? 111 THR   A OG1 1 
ATOM   857  C CG2 . THR   A 1 111 ? 11.24612 -16.59698 -2.30715  1.000 52.48983  ? 111 THR   A CG2 1 
ATOM   858  N N   . PHE   A 1 112 ? 11.07153 -20.52439 -0.32664  1.000 48.09723  ? 112 PHE   A N   1 
ATOM   859  C CA  . PHE   A 1 112 ? 10.73514 -21.91512 -0.06477  1.000 46.55280  ? 112 PHE   A CA  1 
ATOM   860  C C   . PHE   A 1 112 ? 9.34828  -21.97140 0.55067   1.000 47.59386  ? 112 PHE   A C   1 
ATOM   861  O O   . PHE   A 1 112 ? 8.85406  -20.98303 1.09902   1.000 46.65753  ? 112 PHE   A O   1 
ATOM   862  C CB  . PHE   A 1 112 ? 11.76027 -22.57931 0.85755   1.000 44.65799  ? 112 PHE   A CB  1 
ATOM   863  C CG  . PHE   A 1 112 ? 11.99381 -21.83551 2.13891   1.000 45.97504  ? 112 PHE   A CG  1 
ATOM   864  C CD1 . PHE   A 1 112 ? 11.21897 -22.09689 3.25636   1.000 44.63831  ? 112 PHE   A CD1 1 
ATOM   865  C CD2 . PHE   A 1 112 ? 13.00078 -20.88546 2.23211   1.000 48.43452  ? 112 PHE   A CD2 1 
ATOM   866  C CE1 . PHE   A 1 112 ? 11.43750 -21.42340 4.44106   1.000 45.32250  ? 112 PHE   A CE1 1 
ATOM   867  C CE2 . PHE   A 1 112 ? 13.22639 -20.20537 3.41421   1.000 46.33467  ? 112 PHE   A CE2 1 
ATOM   868  C CZ  . PHE   A 1 112 ? 12.44261 -20.47375 4.52244   1.000 51.39761  ? 112 PHE   A CZ  1 
ATOM   869  N N   . SER   A 1 113 ? 8.72501  -23.14378 0.44603   1.000 49.31540  ? 113 SER   A N   1 
ATOM   870  C CA  . SER   A 1 113 ? 7.42481  -23.38707 1.05546   1.000 45.92290  ? 113 SER   A CA  1 
ATOM   871  C C   . SER   A 1 113 ? 7.59596  -23.88673 2.48326   1.000 44.59600  ? 113 SER   A C   1 
ATOM   872  O O   . SER   A 1 113 ? 8.52887  -24.63824 2.78300   1.000 41.35634  ? 113 SER   A O   1 
ATOM   873  C CB  . SER   A 1 113 ? 6.62351  -24.40284 0.24232   1.000 45.37289  ? 113 SER   A CB  1 
ATOM   874  O OG  . SER   A 1 113 ? 6.11728  -23.81694 -0.94074  1.000 51.86124  ? 113 SER   A OG  1 
ATOM   875  N N   . VAL   A 1 114 ? 6.68613  -23.46529 3.35970   1.000 40.75098  ? 114 VAL   A N   1 
ATOM   876  C CA  . VAL   A 1 114 ? 6.70246  -23.84279 4.76867   1.000 42.21385  ? 114 VAL   A CA  1 
ATOM   877  C C   . VAL   A 1 114 ? 5.43626  -24.63320 5.07151   1.000 40.55501  ? 114 VAL   A C   1 
ATOM   878  O O   . VAL   A 1 114 ? 4.32727  -24.17232 4.78215   1.000 40.92002  ? 114 VAL   A O   1 
ATOM   879  C CB  . VAL   A 1 114 ? 6.81152  -22.61551 5.68726   1.000 46.85527  ? 114 VAL   A CB  1 
ATOM   880  C CG1 . VAL   A 1 114 ? 6.43301  -22.98965 7.12280   1.000 42.25082  ? 114 VAL   A CG1 1 
ATOM   881  C CG2 . VAL   A 1 114 ? 8.21320  -22.05572 5.63437   1.000 40.31605  ? 114 VAL   A CG2 1 
ATOM   882  N N   . LEU   A 1 115 ? 5.60003  -25.81586 5.65841   1.000 45.79173  ? 115 LEU   A N   1 
ATOM   883  C CA  . LEU   A 1 115 ? 4.47762  -26.64160 6.09296   1.000 40.08265  ? 115 LEU   A CA  1 
ATOM   884  C C   . LEU   A 1 115 ? 4.36549  -26.49799 7.60660   1.000 42.84785  ? 115 LEU   A C   1 
ATOM   885  O O   . LEU   A 1 115 ? 5.10316  -27.14051 8.35696   1.000 46.46524  ? 115 LEU   A O   1 
ATOM   886  C CB  . LEU   A 1 115 ? 4.68250  -28.09532 5.69534   1.000 43.33004  ? 115 LEU   A CB  1 
ATOM   887  C CG  . LEU   A 1 115 ? 3.51738  -28.97702 6.13557   1.000 44.46698  ? 115 LEU   A CG  1 
ATOM   888  C CD1 . LEU   A 1 115 ? 2.22993  -28.49103 5.48519   1.000 42.83513  ? 115 LEU   A CD1 1 
ATOM   889  C CD2 . LEU   A 1 115 ? 3.77854  -30.44260 5.83587   1.000 49.80261  ? 115 LEU   A CD2 1 
ATOM   890  N N   . ALA   A 1 116 ? 3.44836  -25.64713 8.05467   1.000 42.69373  ? 116 ALA   A N   1 
ATOM   891  C CA  . ALA   A 1 116 ? 3.28216  -25.37010 9.47639   1.000 43.22652  ? 116 ALA   A CA  1 
ATOM   892  C C   . ALA   A 1 116 ? 2.57171  -26.53840 10.14791  1.000 50.08894  ? 116 ALA   A C   1 
ATOM   893  O O   . ALA   A 1 116 ? 1.43636  -26.87097 9.78648   1.000 48.13682  ? 116 ALA   A O   1 
ATOM   894  C CB  . ALA   A 1 116 ? 2.49367  -24.07723 9.67527   1.000 47.69871  ? 116 ALA   A CB  1 
ATOM   895  N N   . CYS   A 1 117 ? 3.22406  -27.14711 11.13639  1.000 48.96862  ? 117 CYS   A N   1 
ATOM   896  C CA  . CYS   A 1 117 ? 2.70264  -28.34193 11.78129  1.000 54.53826  ? 117 CYS   A CA  1 
ATOM   897  C C   . CYS   A 1 117 ? 2.47117  -28.11267 13.26837  1.000 50.78343  ? 117 CYS   A C   1 
ATOM   898  O O   . CYS   A 1 117 ? 3.14587  -27.30404 13.91061  1.000 50.19090  ? 117 CYS   A O   1 
ATOM   899  C CB  . CYS   A 1 117 ? 3.64937  -29.53231 11.58751  1.000 55.25245  ? 117 CYS   A CB  1 
ATOM   900  S SG  . CYS   A 1 117 ? 3.65886  -30.20339 9.91345   1.000 54.81209  ? 117 CYS   A SG  1 
ATOM   901  N N   . TYR   A 1 118 ? 1.51311  -28.85501 13.81237  1.000 57.48187  ? 118 TYR   A N   1 
ATOM   902  C CA  . TYR   A 1 118 ? 1.22702  -28.83633 15.24110  1.000 56.60144  ? 118 TYR   A CA  1 
ATOM   903  C C   . TYR   A 1 118 ? 0.88297  -30.24963 15.67828  1.000 55.23390  ? 118 TYR   A C   1 
ATOM   904  O O   . TYR   A 1 118 ? -0.00233 -30.88324 15.09392  1.000 55.10349  ? 118 TYR   A O   1 
ATOM   905  C CB  . TYR   A 1 118 ? 0.09356  -27.86396 15.55729  1.000 51.85380  ? 118 TYR   A CB  1 
ATOM   906  C CG  . TYR   A 1 118 ? 0.47477  -26.44545 15.21284  1.000 55.17639  ? 118 TYR   A CG  1 
ATOM   907  C CD1 . TYR   A 1 118 ? 1.34097  -25.72616 16.02388  1.000 52.98167  ? 118 TYR   A CD1 1 
ATOM   908  C CD2 . TYR   A 1 118 ? -0.00895 -25.83365 14.06754  1.000 52.93804  ? 118 TYR   A CD2 1 
ATOM   909  C CE1 . TYR   A 1 118 ? 1.70180  -24.43431 15.71175  1.000 52.85162  ? 118 TYR   A CE1 1 
ATOM   910  C CE2 . TYR   A 1 118 ? 0.34664  -24.54130 13.74862  1.000 54.91673  ? 118 TYR   A CE2 1 
ATOM   911  C CZ  . TYR   A 1 118 ? 1.20432  -23.84725 14.57200  1.000 52.83937  ? 118 TYR   A CZ  1 
ATOM   912  O OH  . TYR   A 1 118 ? 1.56188  -22.55938 14.25193  1.000 53.72320  ? 118 TYR   A OH  1 
ATOM   913  N N   . ASN   A 1 119 ? 1.60702  -30.74529 16.68421  1.000 55.77118  ? 119 ASN   A N   1 
ATOM   914  C CA  . ASN   A 1 119 ? 1.45077  -32.10988 17.18313  1.000 54.72980  ? 119 ASN   A CA  1 
ATOM   915  C C   . ASN   A 1 119 ? 1.64746  -33.13872 16.07519  1.000 57.49518  ? 119 ASN   A C   1 
ATOM   916  O O   . ASN   A 1 119 ? 1.00760  -34.19348 16.07454  1.000 55.64310  ? 119 ASN   A O   1 
ATOM   917  C CB  . ASN   A 1 119 ? 0.09046  -32.29816 17.85665  1.000 55.66944  ? 119 ASN   A CB  1 
ATOM   918  C CG  . ASN   A 1 119 ? -0.05266 -31.46472 19.10933  1.000 60.88686  ? 119 ASN   A CG  1 
ATOM   919  O OD1 . ASN   A 1 119 ? 0.63927  -31.69369 20.10442  1.000 61.66655  ? 119 ASN   A OD1 1 
ATOM   920  N ND2 . ASN   A 1 119 ? -0.94623 -30.47918 19.06547  1.000 60.53795  ? 119 ASN   A ND2 1 
ATOM   921  N N   . GLY   A 1 120 ? 2.52902  -32.83421 15.11920  1.000 55.87662  ? 120 GLY   A N   1 
ATOM   922  C CA  . GLY   A 1 120 ? 2.81718  -33.73400 14.02445  1.000 54.13307  ? 120 GLY   A CA  1 
ATOM   923  C C   . GLY   A 1 120 ? 1.82670  -33.70299 12.88377  1.000 57.19723  ? 120 GLY   A C   1 
ATOM   924  O O   . GLY   A 1 120 ? 2.10619  -34.29102 11.82994  1.000 61.15118  ? 120 GLY   A O   1 
ATOM   925  N N   . SER   A 1 121 ? 0.67576  -33.05046 13.05341  1.000 54.30279  ? 121 SER   A N   1 
ATOM   926  C CA  . SER   A 1 121 ? -0.26279 -32.94219 11.94602  1.000 56.13459  ? 121 SER   A CA  1 
ATOM   927  C C   . SER   A 1 121 ? -0.10070 -31.60490 11.23717  1.000 57.52513  ? 121 SER   A C   1 
ATOM   928  O O   . SER   A 1 121 ? 0.13406  -30.58041 11.88715  1.000 55.47753  ? 121 SER   A O   1 
ATOM   929  C CB  . SER   A 1 121 ? -1.70469 -33.08501 12.43195  1.000 58.58071  ? 121 SER   A CB  1 
ATOM   930  O OG  . SER   A 1 121 ? -1.86316 -34.26118 13.20516  1.000 62.81609  ? 121 SER   A OG  1 
ATOM   931  N N   . PRO   A 1 122 ? -0.20114 -31.58429 9.91055   1.000 59.64580  ? 122 PRO   A N   1 
ATOM   932  C CA  . PRO   A 1 122 ? -0.03958 -30.32002 9.18851   1.000 55.32625  ? 122 PRO   A CA  1 
ATOM   933  C C   . PRO   A 1 122 ? -1.24655 -29.42651 9.39170   1.000 53.92392  ? 122 PRO   A C   1 
ATOM   934  O O   . PRO   A 1 122 ? -2.38990 -29.88568 9.38957   1.000 62.26549  ? 122 PRO   A O   1 
ATOM   935  C CB  . PRO   A 1 122 ? 0.09540  -30.75412 7.72325   1.000 55.72503  ? 122 PRO   A CB  1 
ATOM   936  C CG  . PRO   A 1 122 ? 0.38206  -32.22728 7.76912   1.000 59.80791  ? 122 PRO   A CG  1 
ATOM   937  C CD  . PRO   A 1 122 ? -0.32263 -32.72536 8.99214   1.000 62.82811  ? 122 PRO   A CD  1 
ATOM   938  N N   . SER   A 1 123 ? -0.97843 -28.13693 9.57566   1.000 56.51770  ? 123 SER   A N   1 
ATOM   939  C CA  . SER   A 1 123 ? -2.02161 -27.13501 9.73630   1.000 60.40937  ? 123 SER   A CA  1 
ATOM   940  C C   . SER   A 1 123 ? -2.18670 -26.24173 8.51490   1.000 56.48833  ? 123 SER   A C   1 
ATOM   941  O O   . SER   A 1 123 ? -3.28368 -25.73072 8.27614   1.000 54.87688  ? 123 SER   A O   1 
ATOM   942  C CB  . SER   A 1 123 ? -1.72556 -26.26823 10.96756  1.000 62.86430  ? 123 SER   A CB  1 
ATOM   943  O OG  . SER   A 1 123 ? -2.65596 -25.21148 11.10377  1.000 71.83593  ? 123 SER   A OG  1 
ATOM   944  N N   . GLY   A 1 124 ? -1.13636 -26.05912 7.72933   1.000 52.05128  ? 124 GLY   A N   1 
ATOM   945  C CA  . GLY   A 1 124 ? -1.23394 -25.23850 6.54187   1.000 53.55603  ? 124 GLY   A CA  1 
ATOM   946  C C   . GLY   A 1 124 ? 0.12538  -25.06870 5.91175   1.000 45.55867  ? 124 GLY   A C   1 
ATOM   947  O O   . GLY   A 1 124 ? 1.15560  -25.44888 6.47447   1.000 44.13837  ? 124 GLY   A O   1 
ATOM   948  N N   . VAL   A 1 125 ? 0.11236  -24.47622 4.72253   1.000 45.90935  ? 125 VAL   A N   1 
ATOM   949  C CA  . VAL   A 1 125 ? 1.32315  -24.25515 3.94212   1.000 45.81650  ? 125 VAL   A CA  1 
ATOM   950  C C   . VAL   A 1 125 ? 1.33112  -22.82411 3.40676   1.000 41.61801  ? 125 VAL   A C   1 
ATOM   951  O O   . VAL   A 1 125 ? 0.29370  -22.28688 3.00120   1.000 45.97256  ? 125 VAL   A O   1 
ATOM   952  C CB  . VAL   A 1 125 ? 1.45066  -25.30751 2.81238   1.000 44.06838  ? 125 VAL   A CB  1 
ATOM   953  C CG1 . VAL   A 1 125 ? 0.62849  -24.93704 1.61453   1.000 45.91025  ? 125 VAL   A CG1 1 
ATOM   954  C CG2 . VAL   A 1 125 ? 2.89330  -25.47768 2.40325   1.000 45.66034  ? 125 VAL   A CG2 1 
ATOM   955  N N   . TYR   A 1 126 ? 2.49673  -22.18653 3.45897   1.000 42.36308  ? 126 TYR   A N   1 
ATOM   956  C CA  . TYR   A 1 126 ? 2.65740  -20.84140 2.92282   1.000 44.79658  ? 126 TYR   A CA  1 
ATOM   957  C C   . TYR   A 1 126 ? 4.08957  -20.66264 2.43515   1.000 45.08148  ? 126 TYR   A C   1 
ATOM   958  O O   . TYR   A 1 126 ? 5.00179  -21.39309 2.83745   1.000 41.63900  ? 126 TYR   A O   1 
ATOM   959  C CB  . TYR   A 1 126 ? 2.29622  -19.76200 3.95827   1.000 42.88969  ? 126 TYR   A CB  1 
ATOM   960  C CG  . TYR   A 1 126 ? 2.95080  -19.92968 5.31800   1.000 43.93923  ? 126 TYR   A CG  1 
ATOM   961  C CD1 . TYR   A 1 126 ? 4.24370  -19.48358 5.55785   1.000 44.52274  ? 126 TYR   A CD1 1 
ATOM   962  C CD2 . TYR   A 1 126 ? 2.26768  -20.52796 6.36252   1.000 43.87896  ? 126 TYR   A CD2 1 
ATOM   963  C CE1 . TYR   A 1 126 ? 4.83589  -19.63455 6.79913   1.000 42.80575  ? 126 TYR   A CE1 1 
ATOM   964  C CE2 . TYR   A 1 126 ? 2.85006  -20.68370 7.60039   1.000 45.67825  ? 126 TYR   A CE2 1 
ATOM   965  C CZ  . TYR   A 1 126 ? 4.13326  -20.23649 7.81510   1.000 46.72349  ? 126 TYR   A CZ  1 
ATOM   966  O OH  . TYR   A 1 126 ? 4.70369  -20.39241 9.05743   1.000 44.73740  ? 126 TYR   A OH  1 
ATOM   967  N N   . GLN   A 1 127 ? 4.27393  -19.66523 1.56957   1.000 44.99899  ? 127 GLN   A N   1 
ATOM   968  C CA  . GLN   A 1 127 ? 5.56486  -19.37860 0.95759   1.000 45.84677  ? 127 GLN   A CA  1 
ATOM   969  C C   . GLN   A 1 127 ? 6.33137  -18.32180 1.74787   1.000 48.60253  ? 127 GLN   A C   1 
ATOM   970  O O   . GLN   A 1 127 ? 5.76242  -17.32729 2.20102   1.000 53.54607  ? 127 GLN   A O   1 
ATOM   971  C CB  . GLN   A 1 127 ? 5.37308  -18.91445 -0.48767  1.000 44.54609  ? 127 GLN   A CB  1 
ATOM   972  C CG  . GLN   A 1 127 ? 6.66294  -18.79088 -1.28180  1.000 50.16876  ? 127 GLN   A CG  1 
ATOM   973  C CD  . GLN   A 1 127 ? 7.20194  -20.13481 -1.73923  1.000 52.10576  ? 127 GLN   A CD  1 
ATOM   974  O OE1 . GLN   A 1 127 ? 6.69339  -21.18859 -1.35508  1.000 52.90159  ? 127 GLN   A OE1 1 
ATOM   975  N NE2 . GLN   A 1 127 ? 8.22669  -20.10293 -2.57910  1.000 57.19922  ? 127 GLN   A NE2 1 
ATOM   976  N N   . CYS   A 1 128 ? 7.63479  -18.53741 1.88947   1.000 48.31373  ? 128 CYS   A N   1 
ATOM   977  C CA  . CYS   A 1 128 ? 8.50712  -17.68010 2.67711   1.000 50.57762  ? 128 CYS   A CA  1 
ATOM   978  C C   . CYS   A 1 128 ? 9.77658  -17.34983 1.90058   1.000 56.65376  ? 128 CYS   A C   1 
ATOM   979  O O   . CYS   A 1 128 ? 10.13831 -18.02852 0.93370   1.000 49.77031  ? 128 CYS   A O   1 
ATOM   980  C CB  . CYS   A 1 128 ? 8.88929  -18.34656 4.00363   1.000 46.52731  ? 128 CYS   A CB  1 
ATOM   981  S SG  . CYS   A 1 128 ? 7.89725  -17.81849 5.39870   1.000 67.42491  ? 128 CYS   A SG  1 
ATOM   982  N N   . ALA   A 1 129 ? 10.46641 -16.30078 2.35352   1.000 53.45788  ? 129 ALA   A N   1 
ATOM   983  C CA  . ALA   A 1 129 ? 11.76526 -15.92314 1.81313   1.000 51.93695  ? 129 ALA   A CA  1 
ATOM   984  C C   . ALA   A 1 129 ? 12.77092 -15.77829 2.94579   1.000 49.81321  ? 129 ALA   A C   1 
ATOM   985  O O   . ALA   A 1 129 ? 12.42681 -15.32160 4.03899   1.000 57.94281  ? 129 ALA   A O   1 
ATOM   986  C CB  . ALA   A 1 129 ? 11.68633 -14.61927 1.01798   1.000 50.38503  ? 129 ALA   A CB  1 
ATOM   987  N N   . MET   A 1 130 ? 14.01012 -16.18134 2.68189   1.000 44.79931  ? 130 MET   A N   1 
ATOM   988  C CA  . MET   A 1 130 ? 15.10300 -16.02933 3.63829   1.000 46.04239  ? 130 MET   A CA  1 
ATOM   989  C C   . MET   A 1 130 ? 15.60751 -14.59587 3.55655   1.000 50.23847  ? 130 MET   A C   1 
ATOM   990  O O   . MET   A 1 130 ? 16.27500 -14.21524 2.59346   1.000 51.60809  ? 130 MET   A O   1 
ATOM   991  C CB  . MET   A 1 130 ? 16.21006 -17.03510 3.34311   1.000 52.67262  ? 130 MET   A CB  1 
ATOM   992  C CG  . MET   A 1 130 ? 17.44219 -16.89534 4.21790   1.000 53.84989  ? 130 MET   A CG  1 
ATOM   993  S SD  . MET   A 1 130 ? 17.02516 -17.13284 5.95371   1.000 58.43205  ? 130 MET   A SD  1 
ATOM   994  C CE  . MET   A 1 130 ? 16.80606 -18.90208 6.01201   1.000 50.27286  ? 130 MET   A CE  1 
ATOM   995  N N   . ARG   A 1 131 ? 15.28277 -13.79003 4.56489   1.000 52.94746  ? 131 ARG   A N   1 
ATOM   996  C CA  . ARG   A 1 131 ? 15.64187 -12.38212 4.52767   1.000 54.14036  ? 131 ARG   A CA  1 
ATOM   997  C C   . ARG   A 1 131 ? 17.15998 -12.20888 4.60894   1.000 53.88378  ? 131 ARG   A C   1 
ATOM   998  O O   . ARG   A 1 131 ? 17.86379 -13.06528 5.15054   1.000 53.08563  ? 131 ARG   A O   1 
ATOM   999  C CB  . ARG   A 1 131 ? 14.96329 -11.62110 5.66570   1.000 55.34045  ? 131 ARG   A CB  1 
ATOM   1000 C CG  . ARG   A 1 131 ? 13.47084 -11.89104 5.81431   1.000 56.52872  ? 131 ARG   A CG  1 
ATOM   1001 C CD  . ARG   A 1 131 ? 12.64280 -11.21811 4.72706   1.000 58.37936  ? 131 ARG   A CD  1 
ATOM   1002 N NE  . ARG   A 1 131 ? 13.27007 -10.01022 4.20517   1.000 62.53434  ? 131 ARG   A NE  1 
ATOM   1003 C CZ  . ARG   A 1 131 ? 12.93912 -9.43430  3.05743   1.000 62.45818  ? 131 ARG   A CZ  1 
ATOM   1004 N NH1 . ARG   A 1 131 ? 11.99318 -9.93819  2.28108   1.000 58.06247  ? 131 ARG   A NH1 1 
ATOM   1005 N NH2 . ARG   A 1 131 ? 13.57112 -8.32390  2.68067   1.000 59.46412  ? 131 ARG   A NH2 1 
ATOM   1006 N N   . PRO   A 1 132 ? 17.68840 -11.10910 4.06379   1.000 53.80833  ? 132 PRO   A N   1 
ATOM   1007 C CA  . PRO   A 1 132 ? 19.14489 -10.89486 4.10607   1.000 53.85473  ? 132 PRO   A CA  1 
ATOM   1008 C C   . PRO   A 1 132 ? 19.75002 -10.96523 5.49794   1.000 52.54416  ? 132 PRO   A C   1 
ATOM   1009 O O   . PRO   A 1 132 ? 20.94443 -11.26685 5.61655   1.000 54.17662  ? 132 PRO   A O   1 
ATOM   1010 C CB  . PRO   A 1 132 ? 19.30746 -9.49862  3.49151   1.000 53.33748  ? 132 PRO   A CB  1 
ATOM   1011 C CG  . PRO   A 1 132 ? 18.15307 -9.38511  2.55423   1.000 55.56908  ? 132 PRO   A CG  1 
ATOM   1012 C CD  . PRO   A 1 132 ? 17.00888 -10.11261 3.21593   1.000 54.39241  ? 132 PRO   A CD  1 
ATOM   1013 N N   . ASN   A 1 133 ? 18.98378 -10.70633 6.55368   1.000 50.05262  ? 133 ASN   A N   1 
ATOM   1014 C CA  . ASN   A 1 133 ? 19.49214 -10.88907 7.90488   1.000 52.66919  ? 133 ASN   A CA  1 
ATOM   1015 C C   . ASN   A 1 133 ? 19.23958 -12.29366 8.43669   1.000 51.57071  ? 133 ASN   A C   1 
ATOM   1016 O O   . ASN   A 1 133 ? 19.37472 -12.52077 9.64258   1.000 53.79509  ? 133 ASN   A O   1 
ATOM   1017 C CB  . ASN   A 1 133 ? 18.88961 -9.84672  8.84625   1.000 54.98340  ? 133 ASN   A CB  1 
ATOM   1018 C CG  . ASN   A 1 133 ? 17.39147 -9.86024  8.83053   1.000 55.22517  ? 133 ASN   A CG  1 
ATOM   1019 O OD1 . ASN   A 1 133 ? 16.78114 -10.59921 8.06339   1.000 54.61091  ? 133 ASN   A OD1 1 
ATOM   1020 N ND2 . ASN   A 1 133 ? 16.78127 -9.03528  9.67150   1.000 60.03601  ? 133 ASN   A ND2 1 
ATOM   1021 N N   . PHE   A 1 134 ? 18.87427 -13.23243 7.56531   1.000 51.34568  ? 134 PHE   A N   1 
ATOM   1022 C CA  . PHE   A 1 134 ? 18.75292 -14.65006 7.89086   1.000 52.30487  ? 134 PHE   A CA  1 
ATOM   1023 C C   . PHE   A 1 134 ? 17.59931 -14.94105 8.83666   1.000 51.91832  ? 134 PHE   A C   1 
ATOM   1024 O O   . PHE   A 1 134 ? 17.58432 -15.98069 9.50232   1.000 52.46392  ? 134 PHE   A O   1 
ATOM   1025 C CB  . PHE   A 1 134 ? 20.06517 -15.19696 8.45747   1.000 49.33071  ? 134 PHE   A CB  1 
ATOM   1026 C CG  . PHE   A 1 134 ? 21.20121 -15.13085 7.48625   1.000 51.24125  ? 134 PHE   A CG  1 
ATOM   1027 C CD1 . PHE   A 1 134 ? 21.45058 -16.18468 6.62484   1.000 51.76010  ? 134 PHE   A CD1 1 
ATOM   1028 C CD2 . PHE   A 1 134 ? 21.99889 -14.00074 7.40531   1.000 54.38933  ? 134 PHE   A CD2 1 
ATOM   1029 C CE1 . PHE   A 1 134 ? 22.49246 -16.12603 5.71523   1.000 54.87693  ? 134 PHE   A CE1 1 
ATOM   1030 C CE2 . PHE   A 1 134 ? 23.03912 -13.93409 6.49749   1.000 49.42884  ? 134 PHE   A CE2 1 
ATOM   1031 C CZ  . PHE   A 1 134 ? 23.28834 -15.00262 5.65340   1.000 49.86381  ? 134 PHE   A CZ  1 
ATOM   1032 N N   . THR   A 1 135 ? 16.63581 -14.03553 8.91169   1.000 54.25434  ? 135 THR   A N   1 
ATOM   1033 C CA  . THR   A 1 135 ? 15.36370 -14.28982 9.56419   1.000 53.68424  ? 135 THR   A CA  1 
ATOM   1034 C C   . THR   A 1 135 ? 14.30602 -14.56026 8.50268   1.000 53.21537  ? 135 THR   A C   1 
ATOM   1035 O O   . THR   A 1 135 ? 14.54205 -14.40113 7.30470   1.000 53.04473  ? 135 THR   A O   1 
ATOM   1036 C CB  . THR   A 1 135 ? 14.95578 -13.10355 10.44606  1.000 50.68187  ? 135 THR   A CB  1 
ATOM   1037 O OG1 . THR   A 1 135 ? 14.36427 -12.07831 9.63605   1.000 50.86291  ? 135 THR   A OG1 1 
ATOM   1038 C CG2 . THR   A 1 135 ? 16.16385 -12.53692 11.16814  1.000 52.17732  ? 135 THR   A CG2 1 
ATOM   1039 N N   . ILE   A 1 136 ? 13.13316 -15.00084 8.95223   1.000 51.38576  ? 136 ILE   A N   1 
ATOM   1040 C CA  . ILE   A 1 136 ? 11.97358 -15.14515 8.08058   1.000 52.44209  ? 136 ILE   A CA  1 
ATOM   1041 C C   . ILE   A 1 136 ? 10.76060 -14.57446 8.80141   1.000 53.53220  ? 136 ILE   A C   1 
ATOM   1042 O O   . ILE   A 1 136 ? 10.68307 -14.57981 10.03437  1.000 52.33289  ? 136 ILE   A O   1 
ATOM   1043 C CB  . ILE   A 1 136 ? 11.73007 -16.61464 7.63712   1.000 56.27281  ? 136 ILE   A CB  1 
ATOM   1044 C CG1 . ILE   A 1 136 ? 11.00090 -17.41753 8.72202   1.000 56.54565  ? 136 ILE   A CG1 1 
ATOM   1045 C CG2 . ILE   A 1 136 ? 13.03618 -17.29924 7.19783   1.000 47.94632  ? 136 ILE   A CG2 1 
ATOM   1046 C CD1 . ILE   A 1 136 ? 10.27093 -18.63717 8.18569   1.000 51.76533  ? 136 ILE   A CD1 1 
ATOM   1047 N N   . LYS   A 1 137 ? 9.82204  -14.05122 8.02068   1.000 54.35404  ? 137 LYS   A N   1 
ATOM   1048 C CA  . LYS   A 1 137 ? 8.60816  -13.44551 8.55040   1.000 58.00455  ? 137 LYS   A CA  1 
ATOM   1049 C C   . LYS   A 1 137 ? 7.44385  -14.40924 8.34130   1.000 68.41872  ? 137 LYS   A C   1 
ATOM   1050 O O   . LYS   A 1 137 ? 6.54616  -14.17108 7.53195   1.000 78.56975  ? 137 LYS   A O   1 
ATOM   1051 C CB  . LYS   A 1 137 ? 8.35063  -12.07978 7.87886   1.000 63.41679  ? 137 LYS   A CB  1 
ATOM   1052 C CG  . LYS   A 1 137 ? 9.56540  -11.15855 7.82740   1.000 64.17493  ? 137 LYS   A CG  1 
ATOM   1053 C CD  . LYS   A 1 137 ? 9.23812  -9.82141  7.16450   1.000 69.39564  ? 137 LYS   A CD  1 
ATOM   1054 C CE  . LYS   A 1 137 ? 8.98277  -9.98227  5.65959   1.000 77.67167  ? 137 LYS   A CE  1 
ATOM   1055 N NZ  . LYS   A 1 137 ? 9.49935  -8.82489  4.85801   1.000 68.66125  ? 137 LYS   A NZ  1 
ATOM   1056 N N   . GLY   A 1 138 ? 7.46490  -15.51173 9.09193   1.000 63.33299  ? 138 GLY   A N   1 
ATOM   1057 C CA  . GLY   A 1 138 ? 6.45538  -16.54572 8.99169   1.000 55.09041  ? 138 GLY   A CA  1 
ATOM   1058 C C   . GLY   A 1 138 ? 5.34663  -16.38612 10.01085  1.000 54.38740  ? 138 GLY   A C   1 
ATOM   1059 O O   . GLY   A 1 138 ? 5.17278  -15.32956 10.62223  1.000 54.83175  ? 138 GLY   A O   1 
ATOM   1060 N N   . SER   A 1 139 ? 4.57634  -17.46261 10.18296  1.000 53.55433  ? 139 SER   A N   1 
ATOM   1061 C CA  . SER   A 1 139 ? 3.47673  -17.51888 11.14268  1.000 52.54806  ? 139 SER   A CA  1 
ATOM   1062 C C   . SER   A 1 139 ? 3.60706  -18.80834 11.94061  1.000 51.44195  ? 139 SER   A C   1 
ATOM   1063 O O   . SER   A 1 139 ? 3.37487  -19.89682 11.40467  1.000 52.77284  ? 139 SER   A O   1 
ATOM   1064 C CB  . SER   A 1 139 ? 2.12339  -17.45264 10.43785  1.000 52.12255  ? 139 SER   A CB  1 
ATOM   1065 O OG  . SER   A 1 139 ? 1.06836  -17.69691 11.35098  1.000 51.25731  ? 139 SER   A OG  1 
ATOM   1066 N N   . PHE   A 1 140 ? 3.95294  -18.68742 13.22227  1.000 50.60855  ? 140 PHE   A N   1 
ATOM   1067 C CA  . PHE   A 1 140 ? 4.29062  -19.84260 14.03946  1.000 51.55936  ? 140 PHE   A CA  1 
ATOM   1068 C C   . PHE   A 1 140 ? 3.79832  -19.64875 15.46404  1.000 55.36930  ? 140 PHE   A C   1 
ATOM   1069 O O   . PHE   A 1 140 ? 3.96191  -18.57331 16.04237  1.000 60.00177  ? 140 PHE   A O   1 
ATOM   1070 C CB  . PHE   A 1 140 ? 5.80213  -20.08055 14.06252  1.000 52.78612  ? 140 PHE   A CB  1 
ATOM   1071 C CG  . PHE   A 1 140 ? 6.36318  -20.57394 12.76241  1.000 49.46068  ? 140 PHE   A CG  1 
ATOM   1072 C CD1 . PHE   A 1 140 ? 5.94754  -21.78219 12.22344  1.000 46.86616  ? 140 PHE   A CD1 1 
ATOM   1073 C CD2 . PHE   A 1 140 ? 7.32489  -19.83544 12.08815  1.000 48.38449  ? 140 PHE   A CD2 1 
ATOM   1074 C CE1 . PHE   A 1 140 ? 6.47566  -22.23872 11.02580  1.000 53.10545  ? 140 PHE   A CE1 1 
ATOM   1075 C CE2 . PHE   A 1 140 ? 7.86437  -20.28740 10.89446  1.000 49.56012  ? 140 PHE   A CE2 1 
ATOM   1076 C CZ  . PHE   A 1 140 ? 7.44344  -21.48828 10.35854  1.000 46.31244  ? 140 PHE   A CZ  1 
ATOM   1077 N N   . LEU   A 1 141 ? 3.22259  -20.70162 16.03147  1.000 51.56857  ? 141 LEU   A N   1 
ATOM   1078 C CA  . LEU   A 1 141 ? 2.75447  -20.70870 17.40855  1.000 54.99490  ? 141 LEU   A CA  1 
ATOM   1079 C C   . LEU   A 1 141 ? 3.49296  -21.79443 18.18824  1.000 55.77377  ? 141 LEU   A C   1 
ATOM   1080 O O   . LEU   A 1 141 ? 4.38156  -22.47113 17.66771  1.000 55.90869  ? 141 LEU   A O   1 
ATOM   1081 C CB  . LEU   A 1 141 ? 1.24096  -20.91415 17.45889  1.000 54.21362  ? 141 LEU   A CB  1 
ATOM   1082 C CG  . LEU   A 1 141 ? 0.38925  -19.98406 16.59415  1.000 59.37438  ? 141 LEU   A CG  1 
ATOM   1083 C CD1 . LEU   A 1 141 ? -0.94930 -20.63404 16.31756  1.000 60.30645  ? 141 LEU   A CD1 1 
ATOM   1084 C CD2 . LEU   A 1 141 ? 0.19821  -18.62412 17.26661  1.000 57.61726  ? 141 LEU   A CD2 1 
ATOM   1085 N N   . ASN   A 1 142 ? 3.11456  -21.95374 19.45103  1.000 58.55366  ? 142 ASN   A N   1 
ATOM   1086 C CA  . ASN   A 1 142 ? 3.72289  -22.97622 20.28820  1.000 58.69532  ? 142 ASN   A CA  1 
ATOM   1087 C C   . ASN   A 1 142 ? 3.49052  -24.35754 19.69207  1.000 58.60292  ? 142 ASN   A C   1 
ATOM   1088 O O   . ASN   A 1 142 ? 2.40537  -24.66596 19.19703  1.000 61.04991  ? 142 ASN   A O   1 
ATOM   1089 C CB  . ASN   A 1 142 ? 3.14592  -22.89722 21.69655  1.000 54.68196  ? 142 ASN   A CB  1 
ATOM   1090 C CG  . ASN   A 1 142 ? 3.48953  -21.60164 22.37941  1.000 56.19949  ? 142 ASN   A CG  1 
ATOM   1091 O OD1 . ASN   A 1 142 ? 3.15995  -20.52594 21.88277  1.000 71.62253  ? 142 ASN   A OD1 1 
ATOM   1092 N ND2 . ASN   A 1 142 ? 4.15043  -21.68944 23.52494  1.000 56.71582  ? 142 ASN   A ND2 1 
ATOM   1093 N N   . GLY   A 1 143 ? 4.52349  -25.18846 19.72683  1.000 59.76240  ? 143 GLY   A N   1 
ATOM   1094 C CA  . GLY   A 1 143 ? 4.44112  -26.49673 19.11905  1.000 60.68377  ? 143 GLY   A CA  1 
ATOM   1095 C C   . GLY   A 1 143 ? 4.73170  -26.54118 17.63412  1.000 54.43565  ? 143 GLY   A C   1 
ATOM   1096 O O   . GLY   A 1 143 ? 4.75932  -27.63687 17.06130  1.000 60.82508  ? 143 GLY   A O   1 
ATOM   1097 N N   . SER   A 1 144 ? 4.94493  -25.39690 16.98588  1.000 50.89410  ? 144 SER   A N   1 
ATOM   1098 C CA  . SER   A 1 144 ? 5.25539  -25.39703 15.56207  1.000 50.77261  ? 144 SER   A CA  1 
ATOM   1099 C C   . SER   A 1 144 ? 6.69320  -25.79343 15.26309  1.000 48.30872  ? 144 SER   A C   1 
ATOM   1100 O O   . SER   A 1 144 ? 7.00975  -26.06362 14.10106  1.000 43.08342  ? 144 SER   A O   1 
ATOM   1101 C CB  . SER   A 1 144 ? 4.99121  -24.01962 14.95643  1.000 50.91424  ? 144 SER   A CB  1 
ATOM   1102 O OG  . SER   A 1 144 ? 5.83717  -23.04773 15.54230  1.000 50.95373  ? 144 SER   A OG  1 
ATOM   1103 N N   . CYS   A 1 145 ? 7.56462  -25.82793 16.26726  1.000 50.13800  ? 145 CYS   A N   1 
ATOM   1104 C CA  . CYS   A 1 145 ? 8.96037  -26.15514 16.02386  1.000 46.84352  ? 145 CYS   A CA  1 
ATOM   1105 C C   . CYS   A 1 145 ? 9.09071  -27.55462 15.43857  1.000 45.51130  ? 145 CYS   A C   1 
ATOM   1106 O O   . CYS   A 1 145 ? 8.31896  -28.46094 15.76147  1.000 46.97303  ? 145 CYS   A O   1 
ATOM   1107 C CB  . CYS   A 1 145 ? 9.75996  -26.03392 17.31648  1.000 50.73008  ? 145 CYS   A CB  1 
ATOM   1108 S SG  . CYS   A 1 145 ? 9.90513  -24.32491 17.86711  1.000 62.39854  ? 145 CYS   A SG  1 
ATOM   1109 N N   . GLY   A 1 146 ? 10.07453 -27.72268 14.56216  1.000 43.93872  ? 146 GLY   A N   1 
ATOM   1110 C CA  . GLY   A 1 146 ? 10.22659 -28.92418 13.78767  1.000 41.78282  ? 146 GLY   A CA  1 
ATOM   1111 C C   . GLY   A 1 146 ? 9.53239  -28.88656 12.44453  1.000 42.42113  ? 146 GLY   A C   1 
ATOM   1112 O O   . GLY   A 1 146 ? 9.77261  -29.77236 11.61540  1.000 46.88778  ? 146 GLY   A O   1 
ATOM   1113 N N   . SER   A 1 147 ? 8.66243  -27.90455 12.21738  1.000 37.64213  ? 147 SER   A N   1 
ATOM   1114 C CA  . SER   A 1 147 ? 8.11176  -27.70887 10.88639  1.000 39.87773  ? 147 SER   A CA  1 
ATOM   1115 C C   . SER   A 1 147 ? 9.23718  -27.32128 9.93958   1.000 44.21550  ? 147 SER   A C   1 
ATOM   1116 O O   . SER   A 1 147 ? 10.16993 -26.60842 10.31807  1.000 41.28701  ? 147 SER   A O   1 
ATOM   1117 C CB  . SER   A 1 147 ? 7.03157  -26.63293 10.90868  1.000 40.10071  ? 147 SER   A CB  1 
ATOM   1118 O OG  . SER   A 1 147 ? 5.97086  -27.00358 11.77650  1.000 47.60610  ? 147 SER   A OG  1 
ATOM   1119 N N   . VAL   A 1 148 ? 9.17179  -27.81141 8.71296   1.000 41.04630  ? 148 VAL   A N   1 
ATOM   1120 C CA  . VAL   A 1 148 ? 10.29840 -27.66460 7.80857   1.000 47.57063  ? 148 VAL   A CA  1 
ATOM   1121 C C   . VAL   A 1 148 ? 9.91430  -26.76602 6.64525   1.000 46.30886  ? 148 VAL   A C   1 
ATOM   1122 O O   . VAL   A 1 148 ? 8.73176  -26.55696 6.34663   1.000 43.41361  ? 148 VAL   A O   1 
ATOM   1123 C CB  . VAL   A 1 148 ? 10.81670 -29.02909 7.31332   1.000 42.45144  ? 148 VAL   A CB  1 
ATOM   1124 C CG1 . VAL   A 1 148 ? 11.17031 -29.90069 8.50550   1.000 45.40994  ? 148 VAL   A CG1 1 
ATOM   1125 C CG2 . VAL   A 1 148 ? 9.79216  -29.70039 6.41441   1.000 35.79883  ? 148 VAL   A CG2 1 
ATOM   1126 N N   . GLY   A 1 149 ? 10.93879 -26.19829 6.01957   1.000 40.76832  ? 149 GLY   A N   1 
ATOM   1127 C CA  . GLY   A 1 149 ? 10.80121 -25.44519 4.78282   1.000 45.33513  ? 149 GLY   A CA  1 
ATOM   1128 C C   . GLY   A 1 149 ? 11.46142 -26.23244 3.65998   1.000 44.00024  ? 149 GLY   A C   1 
ATOM   1129 O O   . GLY   A 1 149 ? 12.47650 -26.89921 3.87719   1.000 43.51225  ? 149 GLY   A O   1 
ATOM   1130 N N   . PHE   A 1 150 ? 10.87721 -26.15612 2.47098   1.000 40.04331  ? 150 PHE   A N   1 
ATOM   1131 C CA  . PHE   A 1 150 ? 11.28468 -27.07183 1.41990   1.000 48.15644  ? 150 PHE   A CA  1 
ATOM   1132 C C   . PHE   A 1 150 ? 11.00830 -26.46333 0.05524   1.000 48.95457  ? 150 PHE   A C   1 
ATOM   1133 O O   . PHE   A 1 150 ? 10.15744 -25.58471 -0.09985  1.000 50.76944  ? 150 PHE   A O   1 
ATOM   1134 C CB  . PHE   A 1 150 ? 10.55962 -28.41885 1.55352   1.000 46.45145  ? 150 PHE   A CB  1 
ATOM   1135 C CG  . PHE   A 1 150 ? 9.06898  -28.31439 1.42462   1.000 45.24871  ? 150 PHE   A CG  1 
ATOM   1136 C CD1 . PHE   A 1 150 ? 8.28837  -27.92251 2.50842   1.000 44.40364  ? 150 PHE   A CD1 1 
ATOM   1137 C CD2 . PHE   A 1 150 ? 8.44495  -28.60498 0.22088   1.000 42.46597  ? 150 PHE   A CD2 1 
ATOM   1138 C CE1 . PHE   A 1 150 ? 6.91130  -27.81069 2.39095   1.000 41.51823  ? 150 PHE   A CE1 1 
ATOM   1139 C CE2 . PHE   A 1 150 ? 7.06991  -28.50565 0.09534   1.000 44.53379  ? 150 PHE   A CE2 1 
ATOM   1140 C CZ  . PHE   A 1 150 ? 6.29874  -28.10618 1.18236   1.000 45.31942  ? 150 PHE   A CZ  1 
ATOM   1141 N N   . ASN   A 1 151 ? 11.74703 -26.95010 -0.93362  1.000 45.63127  ? 151 ASN   A N   1 
ATOM   1142 C CA  . ASN   A 1 151 ? 11.45497 -26.72444 -2.33740  1.000 47.79422  ? 151 ASN   A CA  1 
ATOM   1143 C C   . ASN   A 1 151 ? 11.26169 -28.07472 -3.00950  1.000 53.33766  ? 151 ASN   A C   1 
ATOM   1144 O O   . ASN   A 1 151 ? 11.74831 -29.09980 -2.52519  1.000 56.91490  ? 151 ASN   A O   1 
ATOM   1145 C CB  . ASN   A 1 151 ? 12.58418 -25.95806 -3.03229  1.000 50.59536  ? 151 ASN   A CB  1 
ATOM   1146 C CG  . ASN   A 1 151 ? 12.61207 -24.50286 -2.65688  1.000 47.68766  ? 151 ASN   A CG  1 
ATOM   1147 O OD1 . ASN   A 1 151 ? 11.79734 -23.71383 -3.13012  1.000 51.69015  ? 151 ASN   A OD1 1 
ATOM   1148 N ND2 . ASN   A 1 151 ? 13.55461 -24.13261 -1.80004  1.000 49.80838  ? 151 ASN   A ND2 1 
ATOM   1149 N N   . ILE   A 1 152 ? 10.55419 -28.07637 -4.13708  1.000 54.29150  ? 152 ILE   A N   1 
ATOM   1150 C CA  . ILE   A 1 152 ? 10.33209 -29.29553 -4.90701  1.000 62.93000  ? 152 ILE   A CA  1 
ATOM   1151 C C   . ILE   A 1 152 ? 10.78494 -29.07852 -6.34555  1.000 65.80026  ? 152 ILE   A C   1 
ATOM   1152 O O   . ILE   A 1 152 ? 10.33324 -28.13779 -7.00832  1.000 64.74040  ? 152 ILE   A O   1 
ATOM   1153 C CB  . ILE   A 1 152 ? 8.85935  -29.74096 -4.86560  1.000 57.51714  ? 152 ILE   A CB  1 
ATOM   1154 C CG1 . ILE   A 1 152 ? 8.52266  -30.31079 -3.48781  1.000 54.15838  ? 152 ILE   A CG1 1 
ATOM   1155 C CG2 . ILE   A 1 152 ? 8.58949  -30.77067 -5.95009  1.000 64.99106  ? 152 ILE   A CG2 1 
ATOM   1156 C CD1 . ILE   A 1 152 ? 7.05299  -30.36313 -3.19500  1.000 50.43504  ? 152 ILE   A CD1 1 
ATOM   1157 N N   . ASP   A 1 153 ? 11.67400 -29.95310 -6.82587  1.000 67.82365  ? 153 ASP   A N   1 
ATOM   1158 C CA  . ASP   A 1 153 ? 12.11950 -29.96328 -8.21878  1.000 73.04337  ? 153 ASP   A CA  1 
ATOM   1159 C C   . ASP   A 1 153 ? 11.71002 -31.29045 -8.84911  1.000 71.34675  ? 153 ASP   A C   1 
ATOM   1160 O O   . ASP   A 1 153 ? 12.33426 -32.32498 -8.58674  1.000 70.67850  ? 153 ASP   A O   1 
ATOM   1161 C CB  . ASP   A 1 153 ? 13.63087 -29.75411 -8.32937  1.000 79.35026  ? 153 ASP   A CB  1 
ATOM   1162 C CG  . ASP   A 1 153 ? 14.16090 -28.72189 -7.34217  1.000 89.67023  ? 153 ASP   A CG  1 
ATOM   1163 O OD1 . ASP   A 1 153 ? 15.31287 -28.88772 -6.88620  1.000 97.60149  ? 153 ASP   A OD1 1 
ATOM   1164 O OD2 . ASP   A 1 153 ? 13.43766 -27.75020 -7.02486  1.000 77.22638  ? 153 ASP   A OD2 1 
ATOM   1165 N N   . TYR   A 1 154 ? 10.68513 -31.24801 -9.70548  1.000 72.84558  ? 154 TYR   A N   1 
ATOM   1166 C CA  . TYR   A 1 154 ? 10.05157 -32.43617 -10.27527 1.000 77.53573  ? 154 TYR   A CA  1 
ATOM   1167 C C   . TYR   A 1 154 ? 9.61810  -33.40291 -9.17973  1.000 81.87870  ? 154 TYR   A C   1 
ATOM   1168 O O   . TYR   A 1 154 ? 8.50047  -33.30027 -8.66143  1.000 83.03426  ? 154 TYR   A O   1 
ATOM   1169 C CB  . TYR   A 1 154 ? 10.97745 -33.14622 -11.27118 1.000 78.97033  ? 154 TYR   A CB  1 
ATOM   1170 C CG  . TYR   A 1 154 ? 10.35766 -34.37294 -11.93688 1.000 85.82586  ? 154 TYR   A CG  1 
ATOM   1171 C CD1 . TYR   A 1 154 ? 8.97276  -34.53924 -12.00482 1.000 86.91342  ? 154 TYR   A CD1 1 
ATOM   1172 C CD2 . TYR   A 1 154 ? 11.15880 -35.35924 -12.50482 1.000 87.82205  ? 154 TYR   A CD2 1 
ATOM   1173 C CE1 . TYR   A 1 154 ? 8.40803  -35.65475 -12.60643 1.000 81.53931  ? 154 TYR   A CE1 1 
ATOM   1174 C CE2 . TYR   A 1 154 ? 10.60251 -36.47533 -13.11494 1.000 88.35926  ? 154 TYR   A CE2 1 
ATOM   1175 C CZ  . TYR   A 1 154 ? 9.22696  -36.61552 -13.16237 1.000 89.88205  ? 154 TYR   A CZ  1 
ATOM   1176 O OH  . TYR   A 1 154 ? 8.67199  -37.72019 -13.76772 1.000 92.53729  ? 154 TYR   A OH  1 
ATOM   1177 N N   . ASP   A 1 155 ? 10.48754 -34.35469 -8.83497  1.000 79.75125  ? 155 ASP   A N   1 
ATOM   1178 C CA  . ASP   A 1 155 ? 10.15207 -35.39795 -7.87773  1.000 77.21802  ? 155 ASP   A CA  1 
ATOM   1179 C C   . ASP   A 1 155 ? 11.00459 -35.36855 -6.61842  1.000 78.21864  ? 155 ASP   A C   1 
ATOM   1180 O O   . ASP   A 1 155 ? 10.76576 -36.17762 -5.71343  1.000 76.45548  ? 155 ASP   A O   1 
ATOM   1181 C CB  . ASP   A 1 155 ? 10.26443 -36.78591 -8.53472  1.000 89.37253  ? 155 ASP   A CB  1 
ATOM   1182 C CG  . ASP   A 1 155 ? 11.71121 -37.19667 -8.83023  1.000 85.11682  ? 155 ASP   A CG  1 
ATOM   1183 O OD1 . ASP   A 1 155 ? 12.56367 -36.30651 -9.05007  1.000 85.57933  ? 155 ASP   A OD1 1 
ATOM   1184 O OD2 . ASP   A 1 155 ? 11.99032 -38.41964 -8.84618  1.000 76.50151  ? 155 ASP   A OD2 1 
ATOM   1185 N N   . CYS   A 1 156 ? 11.98624 -34.47564 -6.52734  1.000 75.82242  ? 156 CYS   A N   1 
ATOM   1186 C CA  . CYS   A 1 156 ? 12.90179 -34.45394 -5.39606  1.000 70.34035  ? 156 CYS   A CA  1 
ATOM   1187 C C   . CYS   A 1 156 ? 12.61121 -33.26751 -4.48832  1.000 64.60978  ? 156 CYS   A C   1 
ATOM   1188 O O   . CYS   A 1 156 ? 12.48757 -32.12913 -4.95656  1.000 66.86817  ? 156 CYS   A O   1 
ATOM   1189 C CB  . CYS   A 1 156 ? 14.35611 -34.40002 -5.85409  1.000 65.96130  ? 156 CYS   A CB  1 
ATOM   1190 S SG  . CYS   A 1 156 ? 15.44975 -33.93585 -4.49249  1.000 73.75229  ? 156 CYS   A SG  1 
ATOM   1191 N N   . VAL   A 1 157 ? 12.53794 -33.53578 -3.19177  1.000 60.48731  ? 157 VAL   A N   1 
ATOM   1192 C CA  . VAL   A 1 157 ? 12.25578 -32.51028 -2.19527  1.000 63.07109  ? 157 VAL   A CA  1 
ATOM   1193 C C   . VAL   A 1 157 ? 13.56911 -31.99636 -1.62837  1.000 59.21034  ? 157 VAL   A C   1 
ATOM   1194 O O   . VAL   A 1 157 ? 14.40084 -32.77780 -1.15433  1.000 64.62509  ? 157 VAL   A O   1 
ATOM   1195 C CB  . VAL   A 1 157 ? 11.35916 -33.06306 -1.07660  1.000 56.08760  ? 157 VAL   A CB  1 
ATOM   1196 C CG1 . VAL   A 1 157 ? 11.17585 -32.01929 0.00832   1.000 53.98621  ? 157 VAL   A CG1 1 
ATOM   1197 C CG2 . VAL   A 1 157 ? 10.02332 -33.50649 -1.64366  1.000 54.50614  ? 157 VAL   A CG2 1 
ATOM   1198 N N   . SER   A 1 158 ? 13.75533 -30.68546 -1.66806  1.000 52.70754  ? 158 SER   A N   1 
ATOM   1199 C CA  . SER   A 1 158 ? 14.94494 -30.04875 -1.11587  1.000 51.66336  ? 158 SER   A CA  1 
ATOM   1200 C C   . SER   A 1 158 ? 14.55773 -29.44216 0.22770   1.000 54.88590  ? 158 SER   A C   1 
ATOM   1201 O O   . SER   A 1 158 ? 13.89060 -28.40551 0.28951   1.000 52.65273  ? 158 SER   A O   1 
ATOM   1202 C CB  . SER   A 1 158 ? 15.49356 -29.00783 -2.08306  1.000 50.79114  ? 158 SER   A CB  1 
ATOM   1203 O OG  . SER   A 1 158 ? 16.04666 -29.64346 -3.22340  1.000 61.56141  ? 158 SER   A OG  1 
ATOM   1204 N N   . PHE   A 1 159 ? 14.95548 -30.11020 1.30463   1.000 53.74133  ? 159 PHE   A N   1 
ATOM   1205 C CA  . PHE   A 1 159 ? 14.69751 -29.61358 2.64803   1.000 50.73736  ? 159 PHE   A CA  1 
ATOM   1206 C C   . PHE   A 1 159 ? 15.76302 -28.59381 3.01818   1.000 54.35013  ? 159 PHE   A C   1 
ATOM   1207 O O   . PHE   A 1 159 ? 16.95055 -28.92663 3.09612   1.000 54.15607  ? 159 PHE   A O   1 
ATOM   1208 C CB  . PHE   A 1 159 ? 14.68796 -30.76075 3.65118   1.000 56.03522  ? 159 PHE   A CB  1 
ATOM   1209 C CG  . PHE   A 1 159 ? 13.50810 -31.67475 3.51754   1.000 56.13778  ? 159 PHE   A CG  1 
ATOM   1210 C CD1 . PHE   A 1 159 ? 12.25869 -31.27773 3.95087   1.000 50.09922  ? 159 PHE   A CD1 1 
ATOM   1211 C CD2 . PHE   A 1 159 ? 13.65337 -32.93482 2.96806   1.000 56.42946  ? 159 PHE   A CD2 1 
ATOM   1212 C CE1 . PHE   A 1 159 ? 11.17768 -32.11992 3.83353   1.000 56.89267  ? 159 PHE   A CE1 1 
ATOM   1213 C CE2 . PHE   A 1 159 ? 12.57735 -33.78101 2.84876   1.000 55.63066  ? 159 PHE   A CE2 1 
ATOM   1214 C CZ  . PHE   A 1 159 ? 11.33832 -33.37533 3.28468   1.000 57.32878  ? 159 PHE   A CZ  1 
ATOM   1215 N N   . CYS   A 1 160 ? 15.34247 -27.35508 3.25626   1.000 50.23694  ? 160 CYS   A N   1 
ATOM   1216 C CA  . CYS   A 1 160 ? 16.27967 -26.28575 3.54771   1.000 53.49253  ? 160 CYS   A CA  1 
ATOM   1217 C C   . CYS   A 1 160 ? 16.09988 -25.63559 4.91348   1.000 57.61947  ? 160 CYS   A C   1 
ATOM   1218 O O   . CYS   A 1 160 ? 17.05410 -25.02554 5.40725   1.000 62.94708  ? 160 CYS   A O   1 
ATOM   1219 C CB  . CYS   A 1 160 ? 16.19506 -25.19756 2.46487   1.000 51.20126  ? 160 CYS   A CB  1 
ATOM   1220 S SG  . CYS   A 1 160 ? 14.55662 -24.47600 2.25134   1.000 51.56766  ? 160 CYS   A SG  1 
ATOM   1221 N N   . TYR   A 1 161 ? 14.93262 -25.75480 5.54558   1.000 50.88562  ? 161 TYR   A N   1 
ATOM   1222 C CA  . TYR   A 1 161 ? 14.65159 -24.99622 6.75659   1.000 48.24170  ? 161 TYR   A CA  1 
ATOM   1223 C C   . TYR   A 1 161 ? 13.93708 -25.86943 7.77697   1.000 51.41844  ? 161 TYR   A C   1 
ATOM   1224 O O   . TYR   A 1 161 ? 13.12569 -26.72643 7.42106   1.000 52.18095  ? 161 TYR   A O   1 
ATOM   1225 C CB  . TYR   A 1 161 ? 13.79363 -23.75752 6.44881   1.000 44.54801  ? 161 TYR   A CB  1 
ATOM   1226 C CG  . TYR   A 1 161 ? 13.48654 -22.89840 7.65754   1.000 45.85685  ? 161 TYR   A CG  1 
ATOM   1227 C CD1 . TYR   A 1 161 ? 14.37960 -21.92487 8.08899   1.000 46.49384  ? 161 TYR   A CD1 1 
ATOM   1228 C CD2 . TYR   A 1 161 ? 12.30498 -23.06646 8.37372   1.000 45.61814  ? 161 TYR   A CD2 1 
ATOM   1229 C CE1 . TYR   A 1 161 ? 14.10169 -21.13482 9.19813   1.000 49.32903  ? 161 TYR   A CE1 1 
ATOM   1230 C CE2 . TYR   A 1 161 ? 12.01754 -22.28132 9.48073   1.000 44.37278  ? 161 TYR   A CE2 1 
ATOM   1231 C CZ  . TYR   A 1 161 ? 12.91928 -21.31997 9.89163   1.000 47.89817  ? 161 TYR   A CZ  1 
ATOM   1232 O OH  . TYR   A 1 161 ? 12.63948 -20.53854 10.99341  1.000 45.41264  ? 161 TYR   A OH  1 
ATOM   1233 N N   . MET   A 1 162 ? 14.24043 -25.63770 9.05432   1.000 48.25120  ? 162 MET   A N   1 
ATOM   1234 C CA  . MET   A 1 162 ? 13.48316 -26.23910 10.14320  1.000 47.06761  ? 162 MET   A CA  1 
ATOM   1235 C C   . MET   A 1 162 ? 13.28727 -25.17892 11.21479  1.000 47.06512  ? 162 MET   A C   1 
ATOM   1236 O O   . MET   A 1 162 ? 14.24775 -24.50177 11.59292  1.000 46.81354  ? 162 MET   A O   1 
ATOM   1237 C CB  . MET   A 1 162 ? 14.19544 -27.46080 10.73201  1.000 44.44380  ? 162 MET   A CB  1 
ATOM   1238 C CG  . MET   A 1 162 ? 13.48943 -28.01054 11.95898  1.000 45.63113  ? 162 MET   A CG  1 
ATOM   1239 S SD  . MET   A 1 162 ? 14.22784 -29.49872 12.65645  1.000 54.77043  ? 162 MET   A SD  1 
ATOM   1240 C CE  . MET   A 1 162 ? 12.97259 -30.70870 12.22482  1.000 47.81880  ? 162 MET   A CE  1 
ATOM   1241 N N   . HIS   A 1 163 ? 12.05613 -25.03890 11.70609  1.000 41.49298  ? 163 HIS   A N   1 
ATOM   1242 C CA  . HIS   A 1 163 ? 11.73092 -23.94465 12.60876  1.000 42.39492  ? 163 HIS   A CA  1 
ATOM   1243 C C   . HIS   A 1 163 ? 12.20739 -24.22454 14.02522  1.000 43.13854  ? 163 HIS   A C   1 
ATOM   1244 O O   . HIS   A 1 163 ? 12.06637 -25.33791 14.53668  1.000 43.70069  ? 163 HIS   A O   1 
ATOM   1245 C CB  . HIS   A 1 163 ? 10.23069 -23.67577 12.62142  1.000 45.16076  ? 163 HIS   A CB  1 
ATOM   1246 C CG  . HIS   A 1 163 ? 9.85875  -22.46517 13.41592  1.000 49.65475  ? 163 HIS   A CG  1 
ATOM   1247 N ND1 . HIS   A 1 163 ? 10.50405 -21.25545 13.26532  1.000 45.44645  ? 163 HIS   A ND1 1 
ATOM   1248 C CD2 . HIS   A 1 163 ? 8.92845  -22.27981 14.38217  1.000 46.30801  ? 163 HIS   A CD2 1 
ATOM   1249 C CE1 . HIS   A 1 163 ? 9.98098  -20.37461 14.09816  1.000 48.05999  ? 163 HIS   A CE1 1 
ATOM   1250 N NE2 . HIS   A 1 163 ? 9.02334  -20.97064 14.78799  1.000 52.80962  ? 163 HIS   A NE2 1 
ATOM   1251 N N   . HIS   A 1 164 ? 12.74659 -23.19081 14.66363  1.000 44.80424  ? 164 HIS   A N   1 
ATOM   1252 C CA  . HIS   A 1 164 ? 13.32281 -23.29387 15.99578  1.000 47.28126  ? 164 HIS   A CA  1 
ATOM   1253 C C   . HIS   A 1 164 ? 12.81977 -22.23362 16.96353  1.000 54.46689  ? 164 HIS   A C   1 
ATOM   1254 O O   . HIS   A 1 164 ? 12.64021 -22.53603 18.14437  1.000 57.58729  ? 164 HIS   A O   1 
ATOM   1255 C CB  . HIS   A 1 164 ? 14.84851 -23.19484 15.90415  1.000 49.20739  ? 164 HIS   A CB  1 
ATOM   1256 C CG  . HIS   A 1 164 ? 15.53790 -24.51380 15.75556  1.000 48.80306  ? 164 HIS   A CG  1 
ATOM   1257 N ND1 . HIS   A 1 164 ? 15.45018 -25.26846 14.60648  1.000 47.64759  ? 164 HIS   A ND1 1 
ATOM   1258 C CD2 . HIS   A 1 164 ? 16.33628 -25.20610 16.60273  1.000 49.56975  ? 164 HIS   A CD2 1 
ATOM   1259 C CE1 . HIS   A 1 164 ? 16.15674 -26.37452 14.75553  1.000 49.97706  ? 164 HIS   A CE1 1 
ATOM   1260 N NE2 . HIS   A 1 164 ? 16.70536 -26.36090 15.95738  1.000 52.10723  ? 164 HIS   A NE2 1 
ATOM   1261 N N   . MET   A 1 165 ? 12.58786 -21.00446 16.50306  1.000 52.41417  ? 165 MET   A N   1 
ATOM   1262 C CA  . MET   A 1 165 ? 12.55434 -19.88000 17.42883  1.000 52.70433  ? 165 MET   A CA  1 
ATOM   1263 C C   . MET   A 1 165 ? 11.85257 -18.68433 16.80157  1.000 53.35771  ? 165 MET   A C   1 
ATOM   1264 O O   . MET   A 1 165 ? 11.76939 -18.55877 15.57747  1.000 55.39524  ? 165 MET   A O   1 
ATOM   1265 C CB  . MET   A 1 165 ? 13.97328 -19.49117 17.83192  1.000 53.93244  ? 165 MET   A CB  1 
ATOM   1266 C CG  . MET   A 1 165 ? 14.08763 -18.75642 19.13157  1.000 60.61641  ? 165 MET   A CG  1 
ATOM   1267 S SD  . MET   A 1 165 ? 15.82079 -18.44873 19.46041  1.000 72.55062  ? 165 MET   A SD  1 
ATOM   1268 C CE  . MET   A 1 165 ? 16.47634 -18.49292 17.79633  1.000 56.60875  ? 165 MET   A CE  1 
ATOM   1269 N N   . GLU   A 1 166 ? 11.36871 -17.79234 17.66546  1.000 55.55716  ? 166 GLU   A N   1 
ATOM   1270 C CA  . GLU   A 1 166 ? 10.79291 -16.51713 17.25724  1.000 59.88874  ? 166 GLU   A CA  1 
ATOM   1271 C C   . GLU   A 1 166 ? 11.59840 -15.37353 17.86097  1.000 57.50927  ? 166 GLU   A C   1 
ATOM   1272 O O   . GLU   A 1 166 ? 11.94997 -15.40329 19.04373  1.000 60.83524  ? 166 GLU   A O   1 
ATOM   1273 C CB  . GLU   A 1 166 ? 9.32578  -16.41059 17.68147  1.000 62.65036  ? 166 GLU   A CB  1 
ATOM   1274 C CG  . GLU   A 1 166 ? 8.61765  -15.14686 17.20968  1.000 67.08950  ? 166 GLU   A CG  1 
ATOM   1275 C CD  . GLU   A 1 166 ? 7.14911  -15.13082 17.59748  1.000 65.33374  ? 166 GLU   A CD  1 
ATOM   1276 O OE1 . GLU   A 1 166 ? 6.83921  -15.52495 18.73868  1.000 75.28153  ? 166 GLU   A OE1 1 
ATOM   1277 O OE2 . GLU   A 1 166 ? 6.30480  -14.73598 16.76435  1.000 70.27893  ? 166 GLU   A OE2 1 
ATOM   1278 N N   . LEU   A 1 167 ? 11.88953 -14.37473 17.05185  1.000 59.16705  ? 167 LEU   A N   1 
ATOM   1279 C CA  . LEU   A 1 167 ? 12.74732 -13.29441 17.50723  1.000 59.56355  ? 167 LEU   A CA  1 
ATOM   1280 C C   . LEU   A 1 167 ? 11.91703 -12.15425 18.07769  1.000 64.05342  ? 167 LEU   A C   1 
ATOM   1281 O O   . LEU   A 1 167 ? 10.71504 -12.05502 17.81151  1.000 67.42686  ? 167 LEU   A O   1 
ATOM   1282 C CB  . LEU   A 1 167 ? 13.61344 -12.79847 16.35235  1.000 58.08965  ? 167 LEU   A CB  1 
ATOM   1283 C CG  . LEU   A 1 167 ? 14.77798 -13.70977 15.96477  1.000 58.59391  ? 167 LEU   A CG  1 
ATOM   1284 C CD1 . LEU   A 1 167 ? 15.18214 -13.47716 14.51922  1.000 59.09749  ? 167 LEU   A CD1 1 
ATOM   1285 C CD2 . LEU   A 1 167 ? 15.95840 -13.47922 16.88612  1.000 61.01701  ? 167 LEU   A CD2 1 
ATOM   1286 N N   . PRO   A 1 168 ? 12.53036 -11.28357 18.88777  1.000 65.93755  ? 168 PRO   A N   1 
ATOM   1287 C CA  . PRO   A 1 168 ? 11.76890 -10.17061 19.48389  1.000 65.73983  ? 168 PRO   A CA  1 
ATOM   1288 C C   . PRO   A 1 168 ? 11.04474 -9.28241  18.48278  1.000 66.02512  ? 168 PRO   A C   1 
ATOM   1289 O O   . PRO   A 1 168 ? 9.97889  -8.74546  18.81483  1.000 65.80875  ? 168 PRO   A O   1 
ATOM   1290 C CB  . PRO   A 1 168 ? 12.83657 -9.37803  20.25102  1.000 62.42223  ? 168 PRO   A CB  1 
ATOM   1291 C CG  . PRO   A 1 168 ? 13.97646 -10.30364 20.45109  1.000 64.46164  ? 168 PRO   A CG  1 
ATOM   1292 C CD  . PRO   A 1 168 ? 13.81334 -11.51434 19.57583  1.000 69.16434  ? 168 PRO   A CD  1 
ATOM   1293 N N   . THR   A 1 169 ? 11.57311 -9.09927  17.27441  1.000 61.05963  ? 169 THR   A N   1 
ATOM   1294 C CA  . THR   A 1 169 ? 10.89592 -8.22595  16.32245  1.000 64.84908  ? 169 THR   A CA  1 
ATOM   1295 C C   . THR   A 1 169 ? 9.70870  -8.90341  15.64974  1.000 63.10500  ? 169 THR   A C   1 
ATOM   1296 O O   . THR   A 1 169 ? 9.13966  -8.33540  14.71009  1.000 65.74280  ? 169 THR   A O   1 
ATOM   1297 C CB  . THR   A 1 169 ? 11.87539 -7.70577  15.25987  1.000 54.67692  ? 169 THR   A CB  1 
ATOM   1298 O OG1 . THR   A 1 169 ? 12.46292 -8.80452  14.55604  1.000 63.07852  ? 169 THR   A OG1 1 
ATOM   1299 C CG2 . THR   A 1 169 ? 12.97953 -6.86942  15.90458  1.000 54.95610  ? 169 THR   A CG2 1 
ATOM   1300 N N   . GLY   A 1 170 ? 9.31850  -10.09003 16.11490  1.000 58.28514  ? 170 GLY   A N   1 
ATOM   1301 C CA  . GLY   A 1 170 ? 8.18223  -10.79803 15.57397  1.000 59.21825  ? 170 GLY   A CA  1 
ATOM   1302 C C   . GLY   A 1 170 ? 8.49725  -11.72262 14.42391  1.000 56.69230  ? 170 GLY   A C   1 
ATOM   1303 O O   . GLY   A 1 170 ? 7.59910  -12.44068 13.96610  1.000 56.39546  ? 170 GLY   A O   1 
ATOM   1304 N N   . VAL   A 1 171 ? 9.73772  -11.71946 13.93837  1.000 55.02177  ? 171 VAL   A N   1 
ATOM   1305 C CA  . VAL   A 1 171 ? 10.16649 -12.57130 12.83417  1.000 54.92917  ? 171 VAL   A CA  1 
ATOM   1306 C C   . VAL   A 1 171 ? 10.67274 -13.89185 13.39851  1.000 56.65535  ? 171 VAL   A C   1 
ATOM   1307 O O   . VAL   A 1 171 ? 10.64102 -14.11064 14.61524  1.000 57.70103  ? 171 VAL   A O   1 
ATOM   1308 C CB  . VAL   A 1 171 ? 11.24864 -11.88110 11.98512  1.000 54.78755  ? 171 VAL   A CB  1 
ATOM   1309 C CG1 . VAL   A 1 171 ? 10.69168 -10.62319 11.32849  1.000 49.96190  ? 171 VAL   A CG1 1 
ATOM   1310 C CG2 . VAL   A 1 171 ? 12.45239 -11.55191 12.84610  1.000 52.17519  ? 171 VAL   A CG2 1 
ATOM   1311 N N   . HIS   A 1 172 ? 11.15711 -14.77737 12.52947  1.000 56.65259  ? 172 HIS   A N   1 
ATOM   1312 C CA  . HIS   A 1 172 ? 11.45700 -16.14294 12.93208  1.000 53.06085  ? 172 HIS   A CA  1 
ATOM   1313 C C   . HIS   A 1 172 ? 12.84624 -16.57007 12.47600  1.000 53.62930  ? 172 HIS   A C   1 
ATOM   1314 O O   . HIS   A 1 172 ? 13.36201 -16.10580 11.45437  1.000 49.97078  ? 172 HIS   A O   1 
ATOM   1315 C CB  . HIS   A 1 172 ? 10.39276 -17.10344 12.40102  1.000 49.86077  ? 172 HIS   A CB  1 
ATOM   1316 C CG  . HIS   A 1 172 ? 9.01373  -16.78245 12.88645  1.000 57.37096  ? 172 HIS   A CG  1 
ATOM   1317 N ND1 . HIS   A 1 172 ? 8.14271  -15.97587 12.18526  1.000 55.68341  ? 172 HIS   A ND1 1 
ATOM   1318 C CD2 . HIS   A 1 172 ? 8.37445  -17.11954 14.03127  1.000 55.67115  ? 172 HIS   A CD2 1 
ATOM   1319 C CE1 . HIS   A 1 172 ? 7.01560  -15.85674 12.86358  1.000 54.17234  ? 172 HIS   A CE1 1 
ATOM   1320 N NE2 . HIS   A 1 172 ? 7.13068  -16.53960 13.98781  1.000 54.69484  ? 172 HIS   A NE2 1 
ATOM   1321 N N   . ALA   A 1 173 ? 13.44824 -17.46126 13.26490  1.000 50.92731  ? 173 ALA   A N   1 
ATOM   1322 C CA  . ALA   A 1 173 ? 14.78726 -17.97188 13.02221  1.000 47.80809  ? 173 ALA   A CA  1 
ATOM   1323 C C   . ALA   A 1 173 ? 14.77794 -19.48773 13.13333  1.000 48.61384  ? 173 ALA   A C   1 
ATOM   1324 O O   . ALA   A 1 173 ? 13.98308 -20.06765 13.87696  1.000 48.08902  ? 173 ALA   A O   1 
ATOM   1325 C CB  . ALA   A 1 173 ? 15.80246 -17.38843 14.01213  1.000 48.67408  ? 173 ALA   A CB  1 
ATOM   1326 N N   . GLY   A 1 174 ? 15.67117 -20.12591 12.38950  1.000 49.55186  ? 174 GLY   A N   1 
ATOM   1327 C CA  . GLY   A 1 174 ? 15.76594 -21.56524 12.43809  1.000 48.12968  ? 174 GLY   A CA  1 
ATOM   1328 C C   . GLY   A 1 174 ? 17.06864 -22.05822 11.85199  1.000 51.13852  ? 174 GLY   A C   1 
ATOM   1329 O O   . GLY   A 1 174 ? 17.98902 -21.28218 11.57869  1.000 50.09575  ? 174 GLY   A O   1 
ATOM   1330 N N   . THR   A 1 175 ? 17.12989 -23.36858 11.65134  1.000 49.11135  ? 175 THR   A N   1 
ATOM   1331 C CA  . THR   A 1 175 ? 18.33346 -24.02734 11.17241  1.000 50.99936  ? 175 THR   A CA  1 
ATOM   1332 C C   . THR   A 1 175 ? 18.08904 -24.67736 9.81758   1.000 51.64545  ? 175 THR   A C   1 
ATOM   1333 O O   . THR   A 1 175 ? 16.94829 -24.84046 9.37185   1.000 46.82107  ? 175 THR   A O   1 
ATOM   1334 C CB  . THR   A 1 175 ? 18.81709 -25.07963 12.17663  1.000 47.83103  ? 175 THR   A CB  1 
ATOM   1335 O OG1 . THR   A 1 175 ? 17.91433 -26.19250 12.17170  1.000 48.38347  ? 175 THR   A OG1 1 
ATOM   1336 C CG2 . THR   A 1 175 ? 18.90039 -24.49309 13.56809  1.000 50.21441  ? 175 THR   A CG2 1 
ATOM   1337 N N   . ASP   A 1 176 ? 19.19225 -25.03158 9.15652   1.000 50.43928  ? 176 ASP   A N   1 
ATOM   1338 C CA  . ASP   A 1 176 ? 19.13385 -25.95867 8.04088   1.000 52.83634  ? 176 ASP   A CA  1 
ATOM   1339 C C   . ASP   A 1 176 ? 18.88626 -27.35963 8.58912   1.000 55.93306  ? 176 ASP   A C   1 
ATOM   1340 O O   . ASP   A 1 176 ? 18.83129 -27.57622 9.80380   1.000 52.26383  ? 176 ASP   A O   1 
ATOM   1341 C CB  . ASP   A 1 176 ? 20.41553 -25.89052 7.20654   1.000 57.98067  ? 176 ASP   A CB  1 
ATOM   1342 C CG  . ASP   A 1 176 ? 21.67673 -26.20794 8.01088   1.000 61.78055  ? 176 ASP   A CG  1 
ATOM   1343 O OD1 . ASP   A 1 176 ? 21.57305 -26.57507 9.20273   1.000 60.50770  ? 176 ASP   A OD1 1 
ATOM   1344 O OD2 . ASP   A 1 176 ? 22.78606 -26.07604 7.44618   1.000 61.62413  ? 176 ASP   A OD2 1 
ATOM   1345 N N   . LEU   A 1 177 ? 18.74976 -28.33239 7.69376   1.000 56.56494  ? 177 LEU   A N   1 
ATOM   1346 C CA  . LEU   A 1 177 ? 18.47011 -29.69438 8.12723   1.000 53.28552  ? 177 LEU   A CA  1 
ATOM   1347 C C   . LEU   A 1 177 ? 19.68933 -30.39363 8.69387   1.000 52.97497  ? 177 LEU   A C   1 
ATOM   1348 O O   . LEU   A 1 177 ? 19.61676 -31.58645 9.00331   1.000 56.45081  ? 177 LEU   A O   1 
ATOM   1349 C CB  . LEU   A 1 177 ? 17.88326 -30.51986 6.98169   1.000 54.64616  ? 177 LEU   A CB  1 
ATOM   1350 C CG  . LEU   A 1 177 ? 16.36968 -30.64519 7.09141   1.000 53.58377  ? 177 LEU   A CG  1 
ATOM   1351 C CD1 . LEU   A 1 177 ? 16.00115 -31.18095 8.47138   1.000 49.53634  ? 177 LEU   A CD1 1 
ATOM   1352 C CD2 . LEU   A 1 177 ? 15.68005 -29.32137 6.82411   1.000 51.35825  ? 177 LEU   A CD2 1 
ATOM   1353 N N   . GLU   A 1 178 ? 20.80102 -29.68327 8.82818   1.000 58.21708  ? 178 GLU   A N   1 
ATOM   1354 C CA  . GLU   A 1 178 ? 21.97976 -30.18845 9.50841   1.000 62.91526  ? 178 GLU   A CA  1 
ATOM   1355 C C   . GLU   A 1 178 ? 22.13068 -29.58687 10.89609  1.000 60.20391  ? 178 GLU   A C   1 
ATOM   1356 O O   . GLU   A 1 178 ? 23.13876 -29.83504 11.56632  1.000 63.21604  ? 178 GLU   A O   1 
ATOM   1357 C CB  . GLU   A 1 178 ? 23.22355 -29.90719 8.66899   1.000 63.38796  ? 178 GLU   A CB  1 
ATOM   1358 C CG  . GLU   A 1 178 ? 24.32965 -30.90474 8.85411   1.000 71.59533  ? 178 GLU   A CG  1 
ATOM   1359 C CD  . GLU   A 1 178 ? 25.50779 -30.61547 7.95544   1.000 80.18782  ? 178 GLU   A CD  1 
ATOM   1360 O OE1 . GLU   A 1 178 ? 25.36019 -30.78251 6.72624   1.000 79.42997  ? 178 GLU   A OE1 1 
ATOM   1361 O OE2 . GLU   A 1 178 ? 26.57210 -30.21218 8.47890   1.000 78.30313  ? 178 GLU   A OE2 1 
ATOM   1362 N N   . GLY   A 1 179 ? 21.15378 -28.79229 11.33255  1.000 58.28627  ? 179 GLY   A N   1 
ATOM   1363 C CA  . GLY   A 1 179 ? 21.16287 -28.18912 12.64545  1.000 57.20703  ? 179 GLY   A CA  1 
ATOM   1364 C C   . GLY   A 1 179 ? 21.91351 -26.88159 12.75349  1.000 58.01089  ? 179 GLY   A C   1 
ATOM   1365 O O   . GLY   A 1 179 ? 21.99995 -26.33049 13.85820  1.000 57.41738  ? 179 GLY   A O   1 
ATOM   1366 N N   . ASN   A 1 180 ? 22.45983 -26.36845 11.65217  1.000 56.44165  ? 180 ASN   A N   1 
ATOM   1367 C CA  . ASN   A 1 180 ? 23.21798 -25.12352 11.66265  1.000 50.91005  ? 180 ASN   A CA  1 
ATOM   1368 C C   . ASN   A 1 180 ? 22.27532 -23.95106 11.43388  1.000 50.69137  ? 180 ASN   A C   1 
ATOM   1369 O O   . ASN   A 1 180 ? 21.57044 -23.89703 10.42036  1.000 48.64708  ? 180 ASN   A O   1 
ATOM   1370 C CB  . ASN   A 1 180 ? 24.31822 -25.14602 10.60495  1.000 53.25814  ? 180 ASN   A CB  1 
ATOM   1371 C CG  . ASN   A 1 180 ? 25.41959 -26.11408 10.94427  1.000 60.10477  ? 180 ASN   A CG  1 
ATOM   1372 O OD1 . ASN   A 1 180 ? 26.04174 -26.00902 11.99993  1.000 60.93369  ? 180 ASN   A OD1 1 
ATOM   1373 N ND2 . ASN   A 1 180 ? 25.67445 -27.06275 10.05273  1.000 66.57315  ? 180 ASN   A ND2 1 
ATOM   1374 N N   . PHE   A 1 181 ? 22.27040 -23.01843 12.37690  1.000 48.89670  ? 181 PHE   A N   1 
ATOM   1375 C CA  . PHE   A 1 181 ? 21.36909 -21.88075 12.30954  1.000 54.03326  ? 181 PHE   A CA  1 
ATOM   1376 C C   . PHE   A 1 181 ? 21.67227 -21.00204 11.10153  1.000 51.53682  ? 181 PHE   A C   1 
ATOM   1377 O O   . PHE   A 1 181 ? 22.83106 -20.79939 10.73181  1.000 50.08875  ? 181 PHE   A O   1 
ATOM   1378 C CB  . PHE   A 1 181 ? 21.48450 -21.04831 13.58304  1.000 55.12612  ? 181 PHE   A CB  1 
ATOM   1379 C CG  . PHE   A 1 181 ? 20.28378 -21.12261 14.45349  1.000 50.18296  ? 181 PHE   A CG  1 
ATOM   1380 C CD1 . PHE   A 1 181 ? 19.17611 -20.33801 14.18545  1.000 50.36765  ? 181 PHE   A CD1 1 
ATOM   1381 C CD2 . PHE   A 1 181 ? 20.26219 -21.96641 15.54793  1.000 51.02552  ? 181 PHE   A CD2 1 
ATOM   1382 C CE1 . PHE   A 1 181 ? 18.05439 -20.40156 14.98287  1.000 49.34955  ? 181 PHE   A CE1 1 
ATOM   1383 C CE2 . PHE   A 1 181 ? 19.14927 -22.03609 16.35350  1.000 56.11245  ? 181 PHE   A CE2 1 
ATOM   1384 C CZ  . PHE   A 1 181 ? 18.03827 -21.24878 16.07037  1.000 54.02872  ? 181 PHE   A CZ  1 
ATOM   1385 N N   . TYR   A 1 182 ? 20.61679 -20.47926 10.48418  1.000 50.92501  ? 182 TYR   A N   1 
ATOM   1386 C CA  . TYR   A 1 182 ? 20.75543 -19.38607 9.53075   1.000 47.87282  ? 182 TYR   A CA  1 
ATOM   1387 C C   . TYR   A 1 182 ? 20.92001 -18.09751 10.32689  1.000 52.25453  ? 182 TYR   A C   1 
ATOM   1388 O O   . TYR   A 1 182 ? 19.98565 -17.65955 11.00439  1.000 60.32802  ? 182 TYR   A O   1 
ATOM   1389 C CB  . TYR   A 1 182 ? 19.53689 -19.30102 8.61737   1.000 49.51351  ? 182 TYR   A CB  1 
ATOM   1390 C CG  . TYR   A 1 182 ? 19.44338 -20.37953 7.56830   1.000 51.19030  ? 182 TYR   A CG  1 
ATOM   1391 C CD1 . TYR   A 1 182 ? 20.17209 -20.29846 6.38701   1.000 49.69252  ? 182 TYR   A CD1 1 
ATOM   1392 C CD2 . TYR   A 1 182 ? 18.60274 -21.46960 7.74854   1.000 50.07681  ? 182 TYR   A CD2 1 
ATOM   1393 C CE1 . TYR   A 1 182 ? 20.07400 -21.28321 5.41857   1.000 51.77742  ? 182 TYR   A CE1 1 
ATOM   1394 C CE2 . TYR   A 1 182 ? 18.50045 -22.45879 6.79476   1.000 51.08398  ? 182 TYR   A CE2 1 
ATOM   1395 C CZ  . TYR   A 1 182 ? 19.23717 -22.36552 5.62899   1.000 54.84455  ? 182 TYR   A CZ  1 
ATOM   1396 O OH  . TYR   A 1 182 ? 19.13563 -23.35824 4.67499   1.000 49.54333  ? 182 TYR   A OH  1 
ATOM   1397 N N   . GLY   A 1 183 ? 22.10034 -17.49213 10.26219  1.000 54.41406  ? 183 GLY   A N   1 
ATOM   1398 C CA  . GLY   A 1 183 ? 22.35092 -16.26092 10.97128  1.000 52.52769  ? 183 GLY   A CA  1 
ATOM   1399 C C   . GLY   A 1 183 ? 22.96961 -16.49377 12.33361  1.000 55.26692  ? 183 GLY   A C   1 
ATOM   1400 O O   . GLY   A 1 183 ? 23.20501 -17.63190 12.75239  1.000 59.26562  ? 183 GLY   A O   1 
ATOM   1401 N N   . PRO   A 1 184 ? 23.22876 -15.40979 13.06241  1.000 57.52536  ? 184 PRO   A N   1 
ATOM   1402 C CA  . PRO   A 1 184 ? 23.92353 -15.50330 14.35492  1.000 58.11215  ? 184 PRO   A CA  1 
ATOM   1403 C C   . PRO   A 1 184 ? 22.94959 -15.73789 15.50780  1.000 60.73948  ? 184 PRO   A C   1 
ATOM   1404 O O   . PRO   A 1 184 ? 22.87879 -14.96282 16.46690  1.000 60.30438  ? 184 PRO   A O   1 
ATOM   1405 C CB  . PRO   A 1 184 ? 24.61151 -14.13822 14.44840  1.000 60.79490  ? 184 PRO   A CB  1 
ATOM   1406 C CG  . PRO   A 1 184 ? 23.68871 -13.19945 13.67746  1.000 59.25117  ? 184 PRO   A CG  1 
ATOM   1407 C CD  . PRO   A 1 184 ? 22.77528 -14.03544 12.79923  1.000 56.28883  ? 184 PRO   A CD  1 
ATOM   1408 N N   . PHE   A 1 185 ? 22.17929 -16.81468 15.40897  1.000 59.29066  ? 185 PHE   A N   1 
ATOM   1409 C CA  . PHE   A 1 185 ? 21.17141 -17.13697 16.40324  1.000 58.89680  ? 185 PHE   A CA  1 
ATOM   1410 C C   . PHE   A 1 185 ? 21.50160 -18.45812 17.08506  1.000 58.69750  ? 185 PHE   A C   1 
ATOM   1411 O O   . PHE   A 1 185 ? 22.21235 -19.30466 16.53389  1.000 58.46319  ? 185 PHE   A O   1 
ATOM   1412 C CB  . PHE   A 1 185 ? 19.77926 -17.19127 15.77075  1.000 59.03193  ? 185 PHE   A CB  1 
ATOM   1413 C CG  . PHE   A 1 185 ? 19.46768 -16.00384 14.90563  1.000 57.06214  ? 185 PHE   A CG  1 
ATOM   1414 C CD1 . PHE   A 1 185 ? 19.43934 -14.72777 15.44637  1.000 58.11030  ? 185 PHE   A CD1 1 
ATOM   1415 C CD2 . PHE   A 1 185 ? 19.20176 -16.16039 13.55689  1.000 52.35571  ? 185 PHE   A CD2 1 
ATOM   1416 C CE1 . PHE   A 1 185 ? 19.15547 -13.62635 14.65679  1.000 57.89866  ? 185 PHE   A CE1 1 
ATOM   1417 C CE2 . PHE   A 1 185 ? 18.91199 -15.06470 12.76188  1.000 53.28254  ? 185 PHE   A CE2 1 
ATOM   1418 C CZ  . PHE   A 1 185 ? 18.89105 -13.79453 13.31432  1.000 54.68558  ? 185 PHE   A CZ  1 
ATOM   1419 N N   . VAL   A 1 186 ? 20.99228 -18.60658 18.30848  1.000 60.54442  ? 186 VAL   A N   1 
ATOM   1420 C CA  . VAL   A 1 186 ? 21.18054 -19.79818 19.12738  1.000 61.28961  ? 186 VAL   A CA  1 
ATOM   1421 C C   . VAL   A 1 186 ? 19.84365 -20.14069 19.77429  1.000 59.08576  ? 186 VAL   A C   1 
ATOM   1422 O O   . VAL   A 1 186 ? 18.98644 -19.27129 19.95543  1.000 59.77218  ? 186 VAL   A O   1 
ATOM   1423 C CB  . VAL   A 1 186 ? 22.27185 -19.58940 20.20157  1.000 57.30406  ? 186 VAL   A CB  1 
ATOM   1424 C CG1 . VAL   A 1 186 ? 23.62508 -19.34031 19.55114  1.000 56.11932  ? 186 VAL   A CG1 1 
ATOM   1425 C CG2 . VAL   A 1 186 ? 21.89923 -18.43434 21.11318  1.000 56.01544  ? 186 VAL   A CG2 1 
ATOM   1426 N N   . ASP   A 1 187 ? 19.66112 -21.41770 20.12125  1.000 61.87108  ? 187 ASP   A N   1 
ATOM   1427 C CA  . ASP   A 1 187 ? 18.41171 -21.87491 20.74032  1.000 64.25263  ? 187 ASP   A CA  1 
ATOM   1428 C C   . ASP   A 1 187 ? 18.44802 -21.55049 22.23125  1.000 63.28192  ? 187 ASP   A C   1 
ATOM   1429 O O   . ASP   A 1 187 ? 18.98717 -22.31375 23.03542  1.000 63.66582  ? 187 ASP   A O   1 
ATOM   1430 C CB  . ASP   A 1 187 ? 18.17971 -23.36605 20.50065  1.000 59.47687  ? 187 ASP   A CB  1 
ATOM   1431 C CG  . ASP   A 1 187 ? 19.46220 -24.16895 20.44126  1.000 61.01805  ? 187 ASP   A CG  1 
ATOM   1432 O OD1 . ASP   A 1 187 ? 20.48384 -23.72965 21.00541  1.000 66.64475  ? 187 ASP   A OD1 1 
ATOM   1433 O OD2 . ASP   A 1 187 ? 19.43968 -25.26030 19.83812  1.000 62.88215  ? 187 ASP   A OD2 1 
ATOM   1434 N N   . ARG   A 1 188 ? 17.83635 -20.42498 22.60437  1.000 61.10751  ? 188 ARG   A N   1 
ATOM   1435 C CA  . ARG   A 1 188 ? 17.99567 -19.85234 23.93509  1.000 66.02117  ? 188 ARG   A CA  1 
ATOM   1436 C C   . ARG   A 1 188 ? 16.99210 -18.71864 24.13433  1.000 67.98048  ? 188 ARG   A C   1 
ATOM   1437 O O   . ARG   A 1 188 ? 16.92573 -17.79675 23.31360  1.000 63.50524  ? 188 ARG   A O   1 
ATOM   1438 C CB  . ARG   A 1 188 ? 19.43235 -19.34831 24.10864  1.000 65.78936  ? 188 ARG   A CB  1 
ATOM   1439 C CG  . ARG   A 1 188 ? 19.68673 -18.46339 25.31516  1.000 71.23261  ? 188 ARG   A CG  1 
ATOM   1440 C CD  . ARG   A 1 188 ? 20.56946 -19.16766 26.31814  1.000 84.68247  ? 188 ARG   A CD  1 
ATOM   1441 N NE  . ARG   A 1 188 ? 20.69788 -18.42361 27.56549  1.000 90.60026  ? 188 ARG   A NE  1 
ATOM   1442 C CZ  . ARG   A 1 188 ? 21.49940 -17.38188 27.74329  1.000 86.43618  ? 188 ARG   A CZ  1 
ATOM   1443 N NH1 . ARG   A 1 188 ? 22.26727 -16.92358 26.76752  1.000 84.55516  ? 188 ARG   A NH1 1 
ATOM   1444 N NH2 . ARG   A 1 188 ? 21.52794 -16.78202 28.92926  1.000 84.86848  ? 188 ARG   A NH2 1 
ATOM   1445 N N   . GLN   A 1 189 ? 16.19786 -18.77402 25.20638  1.000 67.16537  ? 189 GLN   A N   1 
ATOM   1446 C CA  . GLN   A 1 189 ? 15.22993 -17.71375 25.46544  1.000 65.19230  ? 189 GLN   A CA  1 
ATOM   1447 C C   . GLN   A 1 189 ? 15.93208 -16.44812 25.94074  1.000 64.18290  ? 189 GLN   A C   1 
ATOM   1448 O O   . GLN   A 1 189 ? 16.09827 -16.21869 27.14294  1.000 63.30242  ? 189 GLN   A O   1 
ATOM   1449 C CB  . GLN   A 1 189 ? 14.18533 -18.15654 26.48650  1.000 64.44542  ? 189 GLN   A CB  1 
ATOM   1450 C CG  . GLN   A 1 189 ? 13.06088 -17.14946 26.67314  1.000 62.23190  ? 189 GLN   A CG  1 
ATOM   1451 C CD  . GLN   A 1 189 ? 11.95069 -17.66667 27.56911  1.000 65.79229  ? 189 GLN   A CD  1 
ATOM   1452 O OE1 . GLN   A 1 189 ? 11.40985 -18.74790 27.33841  1.000 66.39049  ? 189 GLN   A OE1 1 
ATOM   1453 N NE2 . GLN   A 1 189 ? 11.60627 -16.89560 28.59936  1.000 59.41215  ? 189 GLN   A NE2 1 
ATOM   1454 N N   . THR   A 1 190 ? 16.35584 -15.62409 24.99173  1.000 63.11755  ? 190 THR   A N   1 
ATOM   1455 C CA  . THR   A 1 190 ? 16.97534 -14.34739 25.29557  1.000 65.39787  ? 190 THR   A CA  1 
ATOM   1456 C C   . THR   A 1 190 ? 16.74783 -13.41654 24.11376  1.000 62.95812  ? 190 THR   A C   1 
ATOM   1457 O O   . THR   A 1 190 ? 16.53914 -13.86314 22.98028  1.000 59.68067  ? 190 THR   A O   1 
ATOM   1458 C CB  . THR   A 1 190 ? 18.47368 -14.49656 25.59644  1.000 65.50887  ? 190 THR   A CB  1 
ATOM   1459 O OG1 . THR   A 1 190 ? 19.03681 -13.21210 25.89179  1.000 65.53489  ? 190 THR   A OG1 1 
ATOM   1460 C CG2 . THR   A 1 190 ? 19.19876 -15.10942 24.41328  1.000 63.41584  ? 190 THR   A CG2 1 
ATOM   1461 N N   . ALA   A 1 191 ? 16.75200 -12.11592 24.39975  1.000 62.72815  ? 191 ALA   A N   1 
ATOM   1462 C CA  . ALA   A 1 191 ? 16.56875 -11.10934 23.36343  1.000 66.60223  ? 191 ALA   A CA  1 
ATOM   1463 C C   . ALA   A 1 191 ? 17.70817 -11.18236 22.35698  1.000 67.17080  ? 191 ALA   A C   1 
ATOM   1464 O O   . ALA   A 1 191 ? 18.86196 -10.90550 22.69869  1.000 68.15910  ? 191 ALA   A O   1 
ATOM   1465 C CB  . ALA   A 1 191 ? 16.48522 -9.71237  23.97953  1.000 63.60793  ? 191 ALA   A CB  1 
ATOM   1466 N N   . GLN   A 1 192 ? 17.40193 -11.56840 21.12242  1.000 65.58836  ? 192 GLN   A N   1 
ATOM   1467 C CA  . GLN   A 1 192 ? 18.40049 -11.69448 20.06641  1.000 70.16360  ? 192 GLN   A CA  1 
ATOM   1468 C C   . GLN   A 1 192 ? 18.09941 -10.65781 18.99355  1.000 71.79938  ? 192 GLN   A C   1 
ATOM   1469 O O   . GLN   A 1 192 ? 17.09401 -10.75944 18.28210  1.000 68.56195  ? 192 GLN   A O   1 
ATOM   1470 C CB  . GLN   A 1 192 ? 18.41901 -13.10698 19.48780  1.000 67.07729  ? 192 GLN   A CB  1 
ATOM   1471 C CG  . GLN   A 1 192 ? 18.74655 -14.17788 20.51080  1.000 66.05025  ? 192 GLN   A CG  1 
ATOM   1472 C CD  . GLN   A 1 192 ? 19.25174 -15.44862 19.87238  1.000 62.78516  ? 192 GLN   A CD  1 
ATOM   1473 O OE1 . GLN   A 1 192 ? 20.05691 -15.40803 18.94307  1.000 66.18443  ? 192 GLN   A OE1 1 
ATOM   1474 N NE2 . GLN   A 1 192 ? 18.79442 -16.58890 20.37633  1.000 60.20692  ? 192 GLN   A NE2 1 
ATOM   1475 N N   . ALA   A 1 193 ? 18.97192 -9.66313  18.88218  1.000 68.13312  ? 193 ALA   A N   1 
ATOM   1476 C CA  . ALA   A 1 193 ? 18.77508 -8.57562  17.93418  1.000 74.42522  ? 193 ALA   A CA  1 
ATOM   1477 C C   . ALA   A 1 193 ? 19.04792 -9.08990  16.52819  1.000 77.52865  ? 193 ALA   A C   1 
ATOM   1478 O O   . ALA   A 1 193 ? 20.18628 -9.43463  16.19428  1.000 80.02320  ? 193 ALA   A O   1 
ATOM   1479 C CB  . ALA   A 1 193 ? 19.68192 -7.39716  18.27668  1.000 87.53461  ? 193 ALA   A CB  1 
ATOM   1480 N N   . ALA   A 1 194 ? 18.00418 -9.16174  15.70903  1.000 77.92521  ? 194 ALA   A N   1 
ATOM   1481 C CA  . ALA   A 1 194 ? 18.20394 -9.41081  14.29194  1.000 73.56636  ? 194 ALA   A CA  1 
ATOM   1482 C C   . ALA   A 1 194 ? 18.84774 -8.19507  13.63978  1.000 72.84826  ? 194 ALA   A C   1 
ATOM   1483 O O   . ALA   A 1 194 ? 18.64831 -7.05274  14.06367  1.000 76.07648  ? 194 ALA   A O   1 
ATOM   1484 C CB  . ALA   A 1 194 ? 16.87790 -9.73283  13.60446  1.000 68.92384  ? 194 ALA   A CB  1 
ATOM   1485 N N   . GLY   A 1 195 ? 19.63490 -8.44918  12.60686  1.000 71.27364  ? 195 GLY   A N   1 
ATOM   1486 C CA  . GLY   A 1 195 ? 20.22551 -7.36587  11.85501  1.000 75.37327  ? 195 GLY   A CA  1 
ATOM   1487 C C   . GLY   A 1 195 ? 19.18873 -6.58000  11.07129  1.000 71.29462  ? 195 GLY   A C   1 
ATOM   1488 O O   . GLY   A 1 195 ? 18.01312 -6.93765  10.97908  1.000 68.66560  ? 195 GLY   A O   1 
ATOM   1489 N N   . THR   A 1 196 ? 19.64863 -5.47187  10.49641  1.000 72.60409  ? 196 THR   A N   1 
ATOM   1490 C CA  . THR   A 1 196 ? 18.78733 -4.64613  9.66227   1.000 69.51235  ? 196 THR   A CA  1 
ATOM   1491 C C   . THR   A 1 196 ? 18.37053 -5.40582  8.41235   1.000 67.56849  ? 196 THR   A C   1 
ATOM   1492 O O   . THR   A 1 196 ? 19.20951 -5.96324  7.69786   1.000 70.90473  ? 196 THR   A O   1 
ATOM   1493 C CB  . THR   A 1 196 ? 19.50837 -3.35750  9.27853   1.000 67.95276  ? 196 THR   A CB  1 
ATOM   1494 O OG1 . THR   A 1 196 ? 20.10717 -2.78071  10.44632  1.000 71.97448  ? 196 THR   A OG1 1 
ATOM   1495 C CG2 . THR   A 1 196 ? 18.53492 -2.36975  8.65427   1.000 67.60315  ? 196 THR   A CG2 1 
ATOM   1496 N N   . ASP   A 1 197 ? 17.06977 -5.42235  8.14606   1.000 61.74992  ? 197 ASP   A N   1 
ATOM   1497 C CA  . ASP   A 1 197 ? 16.52162 -6.18692  7.03248   1.000 67.36221  ? 197 ASP   A CA  1 
ATOM   1498 C C   . ASP   A 1 197 ? 16.50592 -5.31347  5.78373   1.000 80.55581  ? 197 ASP   A C   1 
ATOM   1499 O O   . ASP   A 1 197 ? 15.68340 -4.39866  5.66525   1.000 87.28866  ? 197 ASP   A O   1 
ATOM   1500 C CB  . ASP   A 1 197 ? 15.12097 -6.69309  7.35790   1.000 69.18764  ? 197 ASP   A CB  1 
ATOM   1501 C CG  . ASP   A 1 197 ? 14.73027 -7.88579  6.51599   1.000 70.02368  ? 197 ASP   A CG  1 
ATOM   1502 O OD1 . ASP   A 1 197 ? 15.62203 -8.45219  5.84312   1.000 58.75477  ? 197 ASP   A OD1 1 
ATOM   1503 O OD2 . ASP   A 1 197 ? 13.53343 -8.25169  6.52430   1.000 76.78385  ? 197 ASP   A OD2 1 
ATOM   1504 N N   . THR   A 1 198 ? 17.41119 -5.59762  4.85250   1.000 74.39884  ? 198 THR   A N   1 
ATOM   1505 C CA  . THR   A 1 198 ? 17.38137 -4.93669  3.56091   1.000 70.78935  ? 198 THR   A CA  1 
ATOM   1506 C C   . THR   A 1 198 ? 16.33639 -5.59682  2.65923   1.000 66.73630  ? 198 THR   A C   1 
ATOM   1507 O O   . THR   A 1 198 ? 15.79018 -6.65911  2.96642   1.000 63.39542  ? 198 THR   A O   1 
ATOM   1508 C CB  . THR   A 1 198 ? 18.76918 -4.96192  2.91963   1.000 67.81873  ? 198 THR   A CB  1 
ATOM   1509 O OG1 . THR   A 1 198 ? 18.98829 -6.22695  2.28292   1.000 69.10042  ? 198 THR   A OG1 1 
ATOM   1510 C CG2 . THR   A 1 198 ? 19.83959 -4.74235  3.97814   1.000 65.43837  ? 198 THR   A CG2 1 
ATOM   1511 N N   . THR   A 1 199 ? 16.03488 -4.93570  1.54516   1.000 68.81501  ? 199 THR   A N   1 
ATOM   1512 C CA  . THR   A 1 199 ? 15.06587 -5.44343  0.58156   1.000 65.45323  ? 199 THR   A CA  1 
ATOM   1513 C C   . THR   A 1 199 ? 15.78939 -6.20334  -0.52251  1.000 63.16456  ? 199 THR   A C   1 
ATOM   1514 O O   . THR   A 1 199 ? 16.80025 -5.72661  -1.04884  1.000 65.48886  ? 199 THR   A O   1 
ATOM   1515 C CB  . THR   A 1 199 ? 14.23981 -4.29885  -0.00819  1.000 63.00930  ? 199 THR   A CB  1 
ATOM   1516 O OG1 . THR   A 1 199 ? 13.68762 -3.51184  1.05473   1.000 64.95931  ? 199 THR   A OG1 1 
ATOM   1517 C CG2 . THR   A 1 199 ? 13.11567 -4.83607  -0.87916  1.000 62.09053  ? 199 THR   A CG2 1 
ATOM   1518 N N   . ILE   A 1 200 ? 15.28044 -7.39109  -0.85986  1.000 60.78613  ? 200 ILE   A N   1 
ATOM   1519 C CA  . ILE   A 1 200 ? 15.91263 -8.21820  -1.88310  1.000 54.04419  ? 200 ILE   A CA  1 
ATOM   1520 C C   . ILE   A 1 200 ? 15.64341 -7.59288  -3.24538  1.000 56.30784  ? 200 ILE   A C   1 
ATOM   1521 O O   . ILE   A 1 200 ? 14.58749 -7.81064  -3.85374  1.000 50.49333  ? 200 ILE   A O   1 
ATOM   1522 C CB  . ILE   A 1 200 ? 15.43996 -9.68185  -1.82616  1.000 53.65837  ? 200 ILE   A CB  1 
ATOM   1523 C CG1 . ILE   A 1 200 ? 15.74579 -10.29662 -0.45571  1.000 57.55967  ? 200 ILE   A CG1 1 
ATOM   1524 C CG2 . ILE   A 1 200 ? 16.12565 -10.50065 -2.90434  1.000 50.89933  ? 200 ILE   A CG2 1 
ATOM   1525 C CD1 . ILE   A 1 200 ? 14.54448 -10.87430 0.24246   1.000 53.49625  ? 200 ILE   A CD1 1 
ATOM   1526 N N   . THR   A 1 201 ? 16.62081 -6.81674  -3.72454  1.000 57.19823  ? 201 THR   A N   1 
ATOM   1527 C CA  . THR   A 1 201 ? 16.43511 -5.97534  -4.90178  1.000 51.67432  ? 201 THR   A CA  1 
ATOM   1528 C C   . THR   A 1 201 ? 16.11657 -6.79496  -6.13883  1.000 49.77209  ? 201 THR   A C   1 
ATOM   1529 O O   . THR   A 1 201 ? 15.25520 -6.41464  -6.94076  1.000 50.59931  ? 201 THR   A O   1 
ATOM   1530 C CB  . THR   A 1 201 ? 17.69451 -5.14992  -5.14345  1.000 53.20764  ? 201 THR   A CB  1 
ATOM   1531 O OG1 . THR   A 1 201 ? 18.03525 -4.43549  -3.95098  1.000 56.78721  ? 201 THR   A OG1 1 
ATOM   1532 C CG2 . THR   A 1 201 ? 17.48650 -4.18663  -6.28756  1.000 56.44479  ? 201 THR   A CG2 1 
ATOM   1533 N N   . VAL   A 1 202 ? 16.82205 -7.91039  -6.32501  1.000 52.64768  ? 202 VAL   A N   1 
ATOM   1534 C CA  . VAL   A 1 202 ? 16.61849 -8.72287  -7.51671  1.000 51.55099  ? 202 VAL   A CA  1 
ATOM   1535 C C   . VAL   A 1 202 ? 15.21082 -9.29946  -7.52535  1.000 52.08586  ? 202 VAL   A C   1 
ATOM   1536 O O   . VAL   A 1 202 ? 14.60708 -9.47520  -8.59155  1.000 51.12907  ? 202 VAL   A O   1 
ATOM   1537 C CB  . VAL   A 1 202 ? 17.69914 -9.82036  -7.58555  1.000 54.12947  ? 202 VAL   A CB  1 
ATOM   1538 C CG1 . VAL   A 1 202 ? 17.76047 -10.59005 -6.26470  1.000 60.00785  ? 202 VAL   A CG1 1 
ATOM   1539 C CG2 . VAL   A 1 202 ? 17.47769 -10.73993 -8.77809  1.000 51.40097  ? 202 VAL   A CG2 1 
ATOM   1540 N N   . ASN   A 1 203 ? 14.65106 -9.56758  -6.34112  1.000 54.02087  ? 203 ASN   A N   1 
ATOM   1541 C CA  . ASN   A 1 203 ? 13.30066 -10.11283 -6.26000  1.000 47.96925  ? 203 ASN   A CA  1 
ATOM   1542 C C   . ASN   A 1 203 ? 12.25703 -9.06701  -6.62315  1.000 49.21871  ? 203 ASN   A C   1 
ATOM   1543 O O   . ASN   A 1 203 ? 11.26135 -9.38553  -7.28408  1.000 50.16189  ? 203 ASN   A O   1 
ATOM   1544 C CB  . ASN   A 1 203 ? 13.03208 -10.65011 -4.85860  1.000 51.87042  ? 203 ASN   A CB  1 
ATOM   1545 C CG  . ASN   A 1 203 ? 13.63459 -12.02129 -4.62009  1.000 51.95939  ? 203 ASN   A CG  1 
ATOM   1546 O OD1 . ASN   A 1 203 ? 14.40511 -12.52774 -5.43133  1.000 52.70517  ? 203 ASN   A OD1 1 
ATOM   1547 N ND2 . ASN   A 1 203 ? 13.29260 -12.62362 -3.48487  1.000 51.49009  ? 203 ASN   A ND2 1 
ATOM   1548 N N   . VAL   A 1 204 ? 12.44812 -7.82076  -6.17695  1.000 47.15103  ? 204 VAL   A N   1 
ATOM   1549 C CA  . VAL   A 1 204 ? 11.50443 -6.75962  -6.52896  1.000 50.41640  ? 204 VAL   A CA  1 
ATOM   1550 C C   . VAL   A 1 204 ? 11.44138 -6.59044  -8.03883  1.000 51.82076  ? 204 VAL   A C   1 
ATOM   1551 O O   . VAL   A 1 204 ? 10.35666 -6.45365  -8.62017  1.000 50.73503  ? 204 VAL   A O   1 
ATOM   1552 C CB  . VAL   A 1 204 ? 11.88163 -5.43689  -5.83416  1.000 50.90588  ? 204 VAL   A CB  1 
ATOM   1553 C CG1 . VAL   A 1 204 ? 11.05176 -4.29437  -6.38843  1.000 49.86517  ? 204 VAL   A CG1 1 
ATOM   1554 C CG2 . VAL   A 1 204 ? 11.67068 -5.53979  -4.34722  1.000 50.82361  ? 204 VAL   A CG2 1 
ATOM   1555 N N   . LEU   A 1 205 ? 12.60364 -6.60904  -8.69744  1.000 47.32138  ? 205 LEU   A N   1 
ATOM   1556 C CA  . LEU   A 1 205 ? 12.63539 -6.46561  -10.14660 1.000 49.96432  ? 205 LEU   A CA  1 
ATOM   1557 C C   . LEU   A 1 205 ? 11.89936 -7.61075  -10.83243 1.000 47.61159  ? 205 LEU   A C   1 
ATOM   1558 O O   . LEU   A 1 205 ? 11.11926 -7.38452  -11.76417 1.000 53.33045  ? 205 LEU   A O   1 
ATOM   1559 C CB  . LEU   A 1 205 ? 14.08308 -6.37976  -10.62923 1.000 54.18669  ? 205 LEU   A CB  1 
ATOM   1560 C CG  . LEU   A 1 205 ? 14.81783 -5.12182  -10.17033 1.000 47.46981  ? 205 LEU   A CG  1 
ATOM   1561 C CD1 . LEU   A 1 205 ? 16.32393 -5.32190  -10.20373 1.000 49.02497  ? 205 LEU   A CD1 1 
ATOM   1562 C CD2 . LEU   A 1 205 ? 14.40685 -3.94034  -11.02354 1.000 53.18635  ? 205 LEU   A CD2 1 
ATOM   1563 N N   . ALA   A 1 206 ? 12.12567 -8.84712  -10.38207 1.000 51.47166  ? 206 ALA   A N   1 
ATOM   1564 C CA  . ALA   A 1 206 ? 11.40042 -9.98504  -10.94555 1.000 53.17112  ? 206 ALA   A CA  1 
ATOM   1565 C C   . ALA   A 1 206 ? 9.89284  -9.84476  -10.73985 1.000 55.46075  ? 206 ALA   A C   1 
ATOM   1566 O O   . ALA   A 1 206 ? 9.10094  -10.18528 -11.62844 1.000 52.96959  ? 206 ALA   A O   1 
ATOM   1567 C CB  . ALA   A 1 206 ? 11.91156 -11.28489 -10.32671 1.000 48.08847  ? 206 ALA   A CB  1 
ATOM   1568 N N   . TRP   A 1 207 ? 9.47912  -9.34123  -9.57367  1.000 50.96724  ? 207 TRP   A N   1 
ATOM   1569 C CA  . TRP   A 1 207 ? 8.06450  -9.07698  -9.33680  1.000 49.57120  ? 207 TRP   A CA  1 
ATOM   1570 C C   . TRP   A 1 207 ? 7.53478  -8.01073  -10.28896 1.000 52.42069  ? 207 TRP   A C   1 
ATOM   1571 O O   . TRP   A 1 207 ? 6.42576  -8.13941  -10.81898 1.000 54.96183  ? 207 TRP   A O   1 
ATOM   1572 C CB  . TRP   A 1 207 ? 7.85680  -8.65919  -7.88249  1.000 51.42191  ? 207 TRP   A CB  1 
ATOM   1573 C CG  . TRP   A 1 207 ? 6.43659  -8.37072  -7.49821  1.000 54.37476  ? 207 TRP   A CG  1 
ATOM   1574 C CD1 . TRP   A 1 207 ? 5.42244  -9.27409  -7.35576  1.000 53.80822  ? 207 TRP   A CD1 1 
ATOM   1575 C CD2 . TRP   A 1 207 ? 5.88112  -7.09093  -7.17285  1.000 55.56065  ? 207 TRP   A CD2 1 
ATOM   1576 N NE1 . TRP   A 1 207 ? 4.26953  -8.63271  -6.97306  1.000 53.92907  ? 207 TRP   A NE1 1 
ATOM   1577 C CE2 . TRP   A 1 207 ? 4.52697  -7.29283  -6.85211  1.000 55.70002  ? 207 TRP   A CE2 1 
ATOM   1578 C CE3 . TRP   A 1 207 ? 6.39786  -5.79285  -7.12786  1.000 56.55658  ? 207 TRP   A CE3 1 
ATOM   1579 C CZ2 . TRP   A 1 207 ? 3.68447  -6.24707  -6.49305  1.000 63.43749  ? 207 TRP   A CZ2 1 
ATOM   1580 C CZ3 . TRP   A 1 207 ? 5.55895  -4.75529  -6.77192  1.000 58.64484  ? 207 TRP   A CZ3 1 
ATOM   1581 C CH2 . TRP   A 1 207 ? 4.21907  -4.98691  -6.45917  1.000 63.43617  ? 207 TRP   A CH2 1 
ATOM   1582 N N   . LEU   A 1 208 ? 8.30981  -6.94845  -10.52280 1.000 48.74192  ? 208 LEU   A N   1 
ATOM   1583 C CA  . LEU   A 1 208 ? 7.88420  -5.94798  -11.49680 1.000 52.63644  ? 208 LEU   A CA  1 
ATOM   1584 C C   . LEU   A 1 208 ? 7.78459  -6.54183  -12.89453 1.000 56.54898  ? 208 LEU   A C   1 
ATOM   1585 O O   . LEU   A 1 208 ? 6.96826  -6.08956  -13.70666 1.000 56.74862  ? 208 LEU   A O   1 
ATOM   1586 C CB  . LEU   A 1 208 ? 8.84377  -4.76010  -11.50602 1.000 52.64559  ? 208 LEU   A CB  1 
ATOM   1587 C CG  . LEU   A 1 208 ? 8.71314  -3.77339  -10.35221 1.000 54.55998  ? 208 LEU   A CG  1 
ATOM   1588 C CD1 . LEU   A 1 208 ? 9.96712  -2.92385  -10.25387 1.000 48.40585  ? 208 LEU   A CD1 1 
ATOM   1589 C CD2 . LEU   A 1 208 ? 7.46558  -2.91331  -10.50582 1.000 56.56338  ? 208 LEU   A CD2 1 
ATOM   1590 N N   . TYR   A 1 209 ? 8.61254  -7.54570  -13.19567 1.000 56.64250  ? 209 TYR   A N   1 
ATOM   1591 C CA  . TYR   A 1 209 ? 8.52643  -8.21733  -14.48735 1.000 56.36125  ? 209 TYR   A CA  1 
ATOM   1592 C C   . TYR   A 1 209 ? 7.25314  -9.05050  -14.58454 1.000 61.66367  ? 209 TYR   A C   1 
ATOM   1593 O O   . TYR   A 1 209 ? 6.57726  -9.04374  -15.62057 1.000 59.63157  ? 209 TYR   A O   1 
ATOM   1594 C CB  . TYR   A 1 209 ? 9.76591  -9.08599  -14.70472 1.000 54.07867  ? 209 TYR   A CB  1 
ATOM   1595 C CG  . TYR   A 1 209 ? 10.91774 -8.37892  -15.39136 1.000 56.52126  ? 209 TYR   A CG  1 
ATOM   1596 C CD1 . TYR   A 1 209 ? 10.87529 -8.09703  -16.74811 1.000 56.72755  ? 209 TYR   A CD1 1 
ATOM   1597 C CD2 . TYR   A 1 209 ? 12.05000 -7.99806  -14.68148 1.000 54.25350  ? 209 TYR   A CD2 1 
ATOM   1598 C CE1 . TYR   A 1 209 ? 11.92522 -7.45818  -17.37847 1.000 57.06640  ? 209 TYR   A CE1 1 
ATOM   1599 C CE2 . TYR   A 1 209 ? 13.10633 -7.35534  -15.30732 1.000 55.65757  ? 209 TYR   A CE2 1 
ATOM   1600 C CZ  . TYR   A 1 209 ? 13.03526 -7.08737  -16.65596 1.000 56.24763  ? 209 TYR   A CZ  1 
ATOM   1601 O OH  . TYR   A 1 209 ? 14.07299 -6.44675  -17.29309 1.000 61.71283  ? 209 TYR   A OH  1 
ATOM   1602 N N   . ALA   A 1 210 ? 6.90828  -9.77156  -13.51175 1.000 65.37347  ? 210 ALA   A N   1 
ATOM   1603 C CA  . ALA   A 1 210 ? 5.65031  -10.51054 -13.47150 1.000 60.34434  ? 210 ALA   A CA  1 
ATOM   1604 C C   . ALA   A 1 210 ? 4.44611  -9.59868  -13.63674 1.000 61.49062  ? 210 ALA   A C   1 
ATOM   1605 O O   . ALA   A 1 210 ? 3.39621  -10.05305 -14.10571 1.000 63.83449  ? 210 ALA   A O   1 
ATOM   1606 C CB  . ALA   A 1 210 ? 5.52569  -11.28330 -12.15681 1.000 53.36090  ? 210 ALA   A CB  1 
ATOM   1607 N N   . ALA   A 1 211 ? 4.57237  -8.32674  -13.25457 1.000 58.88642  ? 211 ALA   A N   1 
ATOM   1608 C CA  . ALA   A 1 211 ? 3.47811  -7.38398  -13.44608 1.000 57.73068  ? 211 ALA   A CA  1 
ATOM   1609 C C   . ALA   A 1 211 ? 3.30297  -7.05345  -14.92010 1.000 63.83026  ? 211 ALA   A C   1 
ATOM   1610 O O   . ALA   A 1 211 ? 2.18443  -7.09376  -15.44738 1.000 66.24909  ? 211 ALA   A O   1 
ATOM   1611 C CB  . ALA   A 1 211 ? 3.73021  -6.11501  -12.63197 1.000 55.06144  ? 211 ALA   A CB  1 
ATOM   1612 N N   . VAL   A 1 212 ? 4.40479  -6.72329  -15.60103 1.000 64.64185  ? 212 VAL   A N   1 
ATOM   1613 C CA  . VAL   A 1 212 ? 4.34401  -6.42104  -17.02839 1.000 63.65315  ? 212 VAL   A CA  1 
ATOM   1614 C C   . VAL   A 1 212 ? 3.77543  -7.60846  -17.79476 1.000 62.79853  ? 212 VAL   A C   1 
ATOM   1615 O O   . VAL   A 1 212 ? 2.97062  -7.44413  -18.72038 1.000 63.89027  ? 212 VAL   A O   1 
ATOM   1616 C CB  . VAL   A 1 212 ? 5.73940  -6.01448  -17.54163 1.000 64.00502  ? 212 VAL   A CB  1 
ATOM   1617 C CG1 . VAL   A 1 212 ? 5.76425  -5.94837  -19.06466 1.000 57.82660  ? 212 VAL   A CG1 1 
ATOM   1618 C CG2 . VAL   A 1 212 ? 6.15049  -4.68017  -16.93515 1.000 64.95320  ? 212 VAL   A CG2 1 
ATOM   1619 N N   . ILE   A 1 213 ? 4.16839  -8.82333  -17.40720 1.000 59.40268  ? 213 ILE   A N   1 
ATOM   1620 C CA  . ILE   A 1 213 ? 3.58339  -10.02224 -17.99812 1.000 61.28040  ? 213 ILE   A CA  1 
ATOM   1621 C C   . ILE   A 1 213 ? 2.07717  -10.03992 -17.77972 1.000 68.41677  ? 213 ILE   A C   1 
ATOM   1622 O O   . ILE   A 1 213 ? 1.31443  -10.49615 -18.64002 1.000 74.97302  ? 213 ILE   A O   1 
ATOM   1623 C CB  . ILE   A 1 213 ? 4.24804  -11.27925 -17.40927 1.000 66.29606  ? 213 ILE   A CB  1 
ATOM   1624 C CG1 . ILE   A 1 213 ? 5.74422  -11.29030 -17.71927 1.000 66.66230  ? 213 ILE   A CG1 1 
ATOM   1625 C CG2 . ILE   A 1 213 ? 3.57499  -12.53482 -17.93249 1.000 68.88765  ? 213 ILE   A CG2 1 
ATOM   1626 C CD1 . ILE   A 1 213 ? 6.41497  -12.62427 -17.45808 1.000 65.30400  ? 213 ILE   A CD1 1 
ATOM   1627 N N   . ASN   A 1 214 ? 1.62199  -9.52140  -16.63825 1.000 64.39876  ? 214 ASN   A N   1 
ATOM   1628 C CA  . ASN   A 1 214 ? 0.23413  -9.64590  -16.21893 1.000 62.36207  ? 214 ASN   A CA  1 
ATOM   1629 C C   . ASN   A 1 214 ? -0.59462 -8.39836  -16.51069 1.000 69.06980  ? 214 ASN   A C   1 
ATOM   1630 O O   . ASN   A 1 214 ? -1.62375 -8.18265  -15.86129 1.000 74.51956  ? 214 ASN   A O   1 
ATOM   1631 C CB  . ASN   A 1 214 ? 0.18028  -9.97950  -14.73160 1.000 66.74524  ? 214 ASN   A CB  1 
ATOM   1632 C CG  . ASN   A 1 214 ? -0.10006 -11.44049 -14.48236 1.000 72.42691  ? 214 ASN   A CG  1 
ATOM   1633 O OD1 . ASN   A 1 214 ? -1.23811 -11.83452 -14.23685 1.000 72.68681  ? 214 ASN   A OD1 1 
ATOM   1634 N ND2 . ASN   A 1 214 ? 0.94318  -12.26330 -14.56932 1.000 68.91940  ? 214 ASN   A ND2 1 
ATOM   1635 N N   . GLY   A 1 215 ? -0.17462 -7.57512  -17.47034 1.000 64.05865  ? 215 GLY   A N   1 
ATOM   1636 C CA  . GLY   A 1 215 ? -0.92779 -6.41281  -17.88177 1.000 62.22277  ? 215 GLY   A CA  1 
ATOM   1637 C C   . GLY   A 1 215 ? -0.67232 -5.15934  -17.06691 1.000 67.99440  ? 215 GLY   A C   1 
ATOM   1638 O O   . GLY   A 1 215 ? -0.86489 -4.05265  -17.57860 1.000 68.06611  ? 215 GLY   A O   1 
ATOM   1639 N N   . ASP   A 1 216 ? -0.24918 -5.30178  -15.81216 1.000 71.45687  ? 216 ASP   A N   1 
ATOM   1640 C CA  . ASP   A 1 216 ? 0.00958  -4.14702  -14.95598 1.000 72.59689  ? 216 ASP   A CA  1 
ATOM   1641 C C   . ASP   A 1 216 ? 1.33218  -3.50887  -15.36129 1.000 71.62442  ? 216 ASP   A C   1 
ATOM   1642 O O   . ASP   A 1 216 ? 2.40345  -4.03513  -15.04556 1.000 74.06534  ? 216 ASP   A O   1 
ATOM   1643 C CB  . ASP   A 1 216 ? 0.03959  -4.57142  -13.49154 1.000 67.75174  ? 216 ASP   A CB  1 
ATOM   1644 C CG  . ASP   A 1 216 ? -0.64598 -3.57501  -12.58373 1.000 75.88118  ? 216 ASP   A CG  1 
ATOM   1645 O OD1 . ASP   A 1 216 ? -0.85007 -2.41696  -13.01300 1.000 77.55861  ? 216 ASP   A OD1 1 
ATOM   1646 O OD2 . ASP   A 1 216 ? -0.96265 -3.94593  -11.43258 1.000 78.72305  ? 216 ASP   A OD2 1 
ATOM   1647 N N   . ARG   A 1 217 ? 1.26905  -2.36127  -16.05250 1.000 74.59875  ? 217 ARG   A N   1 
ATOM   1648 C CA  . ARG   A 1 217 ? 2.48364  -1.78324  -16.61793 1.000 74.72626  ? 217 ARG   A CA  1 
ATOM   1649 C C   . ARG   A 1 217 ? 2.47442  -0.25671  -16.60558 1.000 72.41026  ? 217 ARG   A C   1 
ATOM   1650 O O   . ARG   A 1 217 ? 3.08949  0.36731   -17.47707 1.000 67.87656  ? 217 ARG   A O   1 
ATOM   1651 C CB  . ARG   A 1 217 ? 2.69649  -2.28600  -18.05146 1.000 72.86066  ? 217 ARG   A CB  1 
ATOM   1652 N N   . TRP   A 1 218 ? 1.80509  0.36072   -15.62828 1.000 75.00268  ? 218 TRP   A N   1 
ATOM   1653 C CA  . TRP   A 1 218 ? 1.76826  1.81820   -15.54536 1.000 71.34569  ? 218 TRP   A CA  1 
ATOM   1654 C C   . TRP   A 1 218 ? 3.07012  2.41807   -15.02643 1.000 75.71713  ? 218 TRP   A C   1 
ATOM   1655 O O   . TRP   A 1 218 ? 3.24767  3.63847   -15.11921 1.000 78.31393  ? 218 TRP   A O   1 
ATOM   1656 C CB  . TRP   A 1 218 ? 0.60343  2.26766   -14.65484 1.000 73.84090  ? 218 TRP   A CB  1 
ATOM   1657 C CG  . TRP   A 1 218 ? 0.73073  1.82104   -13.22694 1.000 76.43543  ? 218 TRP   A CG  1 
ATOM   1658 C CD1 . TRP   A 1 218 ? 0.19743  0.69463   -12.67079 1.000 73.97303  ? 218 TRP   A CD1 1 
ATOM   1659 C CD2 . TRP   A 1 218 ? 1.44657  2.48572   -12.17693 1.000 74.63636  ? 218 TRP   A CD2 1 
ATOM   1660 N NE1 . TRP   A 1 218 ? 0.53498  0.61797   -11.34104 1.000 73.07408  ? 218 TRP   A NE1 1 
ATOM   1661 C CE2 . TRP   A 1 218 ? 1.30144  1.70539   -11.01347 1.000 74.39356  ? 218 TRP   A CE2 1 
ATOM   1662 C CE3 . TRP   A 1 218 ? 2.19505  3.66294   -12.10840 1.000 70.32232  ? 218 TRP   A CE3 1 
ATOM   1663 C CZ2 . TRP   A 1 218 ? 1.87694  2.06511   -9.79717  1.000 73.14512  ? 218 TRP   A CZ2 1 
ATOM   1664 C CZ3 . TRP   A 1 218 ? 2.76519  4.01629   -10.90205 1.000 71.42118  ? 218 TRP   A CZ3 1 
ATOM   1665 C CH2 . TRP   A 1 218 ? 2.60191  3.22210   -9.76233  1.000 72.57837  ? 218 TRP   A CH2 1 
ATOM   1666 N N   . PHE   A 1 219 ? 3.98247  1.59871   -14.49991 1.000 73.98327  ? 219 PHE   A N   1 
ATOM   1667 C CA  . PHE   A 1 219 ? 5.19203  2.09485   -13.85404 1.000 73.99263  ? 219 PHE   A CA  1 
ATOM   1668 C C   . PHE   A 1 219 ? 6.38241  2.21977   -14.79806 1.000 74.16505  ? 219 PHE   A C   1 
ATOM   1669 O O   . PHE   A 1 219 ? 7.36745  2.87729   -14.44215 1.000 75.01231  ? 219 PHE   A O   1 
ATOM   1670 C CB  . PHE   A 1 219 ? 5.57554  1.17908   -12.68722 1.000 71.50490  ? 219 PHE   A CB  1 
ATOM   1671 C CG  . PHE   A 1 219 ? 5.57628  -0.27558  -13.04425 1.000 69.62840  ? 219 PHE   A CG  1 
ATOM   1672 C CD1 . PHE   A 1 219 ? 4.42485  -1.03206  -12.92524 1.000 69.95370  ? 219 PHE   A CD1 1 
ATOM   1673 C CD2 . PHE   A 1 219 ? 6.72517  -0.88399  -13.51415 1.000 67.22612  ? 219 PHE   A CD2 1 
ATOM   1674 C CE1 . PHE   A 1 219 ? 4.41990  -2.36844  -13.26352 1.000 68.11217  ? 219 PHE   A CE1 1 
ATOM   1675 C CE2 . PHE   A 1 219 ? 6.72530  -2.22248  -13.85345 1.000 67.36105  ? 219 PHE   A CE2 1 
ATOM   1676 C CZ  . PHE   A 1 219 ? 5.57265  -2.96535  -13.72554 1.000 67.98378  ? 219 PHE   A CZ  1 
ATOM   1677 N N   . LEU   A 1 220 ? 6.33296  1.60118   -15.97468 1.000 71.75330  ? 220 LEU   A N   1 
ATOM   1678 C CA  . LEU   A 1 220 ? 7.43235  1.72822   -16.92259 1.000 71.71149  ? 220 LEU   A CA  1 
ATOM   1679 C C   . LEU   A 1 220 ? 7.52344  3.16868   -17.40129 1.000 75.73011  ? 220 LEU   A C   1 
ATOM   1680 O O   . LEU   A 1 220 ? 6.56777  3.69892   -17.97480 1.000 79.45166  ? 220 LEU   A O   1 
ATOM   1681 C CB  . LEU   A 1 220 ? 7.23857  0.78287   -18.10513 1.000 71.21260  ? 220 LEU   A CB  1 
ATOM   1682 C CG  . LEU   A 1 220 ? 6.89226  -0.66709  -17.76647 1.000 72.22311  ? 220 LEU   A CG  1 
ATOM   1683 C CD1 . LEU   A 1 220 ? 6.22774  -1.37226  -18.94323 1.000 67.31105  ? 220 LEU   A CD1 1 
ATOM   1684 C CD2 . LEU   A 1 220 ? 8.13692  -1.41067  -17.31482 1.000 74.14302  ? 220 LEU   A CD2 1 
ATOM   1685 N N   . ASN   A 1 221 ? 8.66172  3.80727   -17.15748 1.000 78.30161  ? 221 ASN   A N   1 
ATOM   1686 C CA  . ASN   A 1 221 ? 8.87633  5.17573   -17.59370 1.000 80.29137  ? 221 ASN   A CA  1 
ATOM   1687 C C   . ASN   A 1 221 ? 9.81097  5.20123   -18.79865 1.000 81.97093  ? 221 ASN   A C   1 
ATOM   1688 O O   . ASN   A 1 221 ? 10.29029 4.17069   -19.27502 1.000 84.99337  ? 221 ASN   A O   1 
ATOM   1689 C CB  . ASN   A 1 221 ? 9.43030  6.03480   -16.45466 1.000 79.34555  ? 221 ASN   A CB  1 
ATOM   1690 C CG  . ASN   A 1 221 ? 10.72004 5.48502   -15.87391 1.000 83.40316  ? 221 ASN   A CG  1 
ATOM   1691 O OD1 . ASN   A 1 221 ? 11.32664 4.56092   -16.42009 1.000 83.95591  ? 221 ASN   A OD1 1 
ATOM   1692 N ND2 . ASN   A 1 221 ? 11.15473 6.06688   -14.76163 1.000 83.24961  ? 221 ASN   A ND2 1 
ATOM   1693 N N   . ARG   A 1 222 ? 10.07606 6.40956   -19.29157 1.000 83.15617  ? 222 ARG   A N   1 
ATOM   1694 C CA  . ARG   A 1 222 ? 10.94748 6.62366   -20.43840 1.000 86.80408  ? 222 ARG   A CA  1 
ATOM   1695 C C   . ARG   A 1 222 ? 12.37707 6.95517   -20.02444 1.000 86.24060  ? 222 ARG   A C   1 
ATOM   1696 O O   . ARG   A 1 222 ? 13.09481 7.63526   -20.76488 1.000 96.62730  ? 222 ARG   A O   1 
ATOM   1697 C CB  . ARG   A 1 222 ? 10.38236 7.73145   -21.32774 1.000 85.61682  ? 222 ARG   A CB  1 
ATOM   1698 N N   . PHE   A 1 223 ? 12.80568 6.49214   -18.85614 1.000 88.43552  ? 223 PHE   A N   1 
ATOM   1699 C CA  . PHE   A 1 223 ? 14.12459 6.79761   -18.32115 1.000 84.85605  ? 223 PHE   A CA  1 
ATOM   1700 C C   . PHE   A 1 223 ? 15.01655 5.56209   -18.38705 1.000 83.90375  ? 223 PHE   A C   1 
ATOM   1701 O O   . PHE   A 1 223 ? 14.56863 4.45434   -18.69569 1.000 85.94465  ? 223 PHE   A O   1 
ATOM   1702 C CB  . PHE   A 1 223 ? 14.01858 7.29770   -16.87429 1.000 86.00108  ? 223 PHE   A CB  1 
ATOM   1703 C CG  . PHE   A 1 223 ? 13.33255 8.63642   -16.72687 1.000 88.10551  ? 223 PHE   A CG  1 
ATOM   1704 C CD1 . PHE   A 1 223 ? 13.07999 9.15457   -15.46786 1.000 89.43753  ? 223 PHE   A CD1 1 
ATOM   1705 C CD2 . PHE   A 1 223 ? 12.96787 9.38687   -17.83517 1.000 90.05132  ? 223 PHE   A CD2 1 
ATOM   1706 C CE1 . PHE   A 1 223 ? 12.45562 10.37873  -15.31046 1.000 89.13701  ? 223 PHE   A CE1 1 
ATOM   1707 C CE2 . PHE   A 1 223 ? 12.34521 10.61971  -17.68332 1.000 87.96038  ? 223 PHE   A CE2 1 
ATOM   1708 C CZ  . PHE   A 1 223 ? 12.09234 11.11449  -16.41972 1.000 85.45865  ? 223 PHE   A CZ  1 
ATOM   1709 N N   . THR   A 1 224 ? 16.29838 5.76461   -18.08651 1.000 81.99086  ? 224 THR   A N   1 
ATOM   1710 C CA  . THR   A 1 224 ? 17.26655 4.67533   -18.06681 1.000 82.28495  ? 224 THR   A CA  1 
ATOM   1711 C C   . THR   A 1 224 ? 18.34517 4.98961   -17.03673 1.000 81.07969  ? 224 THR   A C   1 
ATOM   1712 O O   . THR   A 1 224 ? 18.51284 6.13792   -16.61769 1.000 83.13424  ? 224 THR   A O   1 
ATOM   1713 C CB  . THR   A 1 224 ? 17.87493 4.43689   -19.45701 1.000 83.47988  ? 224 THR   A CB  1 
ATOM   1714 O OG1 . THR   A 1 224 ? 18.12477 3.03681   -19.63428 1.000 82.07922  ? 224 THR   A OG1 1 
ATOM   1715 C CG2 . THR   A 1 224 ? 19.17447 5.21718   -19.63428 1.000 72.28726  ? 224 THR   A CG2 1 
ATOM   1716 N N   . THR   A 1 225 ? 19.06550 3.95240   -16.61098 1.000 75.82141  ? 225 THR   A N   1 
ATOM   1717 C CA  . THR   A 1 225 ? 20.13865 4.13527   -15.64184 1.000 82.95118  ? 225 THR   A CA  1 
ATOM   1718 C C   . THR   A 1 225 ? 21.25089 3.13399   -15.92768 1.000 85.56903  ? 225 THR   A C   1 
ATOM   1719 O O   . THR   A 1 225 ? 21.12053 2.24435   -16.77353 1.000 86.24284  ? 225 THR   A O   1 
ATOM   1720 C CB  . THR   A 1 225 ? 19.64218 3.97374   -14.19438 1.000 81.61625  ? 225 THR   A CB  1 
ATOM   1721 O OG1 . THR   A 1 225 ? 18.30613 4.47417   -14.08192 1.000 90.28266  ? 225 THR   A OG1 1 
ATOM   1722 C CG2 . THR   A 1 225 ? 20.53022 4.75595   -13.22906 1.000 78.67248  ? 225 THR   A CG2 1 
ATOM   1723 N N   . THR   A 1 226 ? 22.35668 3.30029   -15.21148 1.000 84.80262  ? 226 THR   A N   1 
ATOM   1724 C CA  . THR   A 1 226 ? 23.45391 2.34893   -15.19198 1.000 80.70448  ? 226 THR   A CA  1 
ATOM   1725 C C   . THR   A 1 226 ? 23.40942 1.55787   -13.88747 1.000 77.61702  ? 226 THR   A C   1 
ATOM   1726 O O   . THR   A 1 226 ? 22.80223 1.97874   -12.89655 1.000 71.99553  ? 226 THR   A O   1 
ATOM   1727 C CB  . THR   A 1 226 ? 24.79797 3.07229   -15.33491 1.000 86.78910  ? 226 THR   A CB  1 
ATOM   1728 O OG1 . THR   A 1 226 ? 24.70817 4.04358   -16.38462 1.000 103.10436 ? 226 THR   A OG1 1 
ATOM   1729 C CG2 . THR   A 1 226 ? 25.90890 2.08853   -15.68701 1.000 91.05137  ? 226 THR   A CG2 1 
ATOM   1730 N N   . LEU   A 1 227 ? 24.05156 0.38665   -13.90754 1.000 78.74367  ? 227 LEU   A N   1 
ATOM   1731 C CA  . LEU   A 1 227 ? 24.11265 -0.45748  -12.71907 1.000 70.45194  ? 227 LEU   A CA  1 
ATOM   1732 C C   . LEU   A 1 227 ? 24.74866 0.26310   -11.53957 1.000 71.79285  ? 227 LEU   A C   1 
ATOM   1733 O O   . LEU   A 1 227 ? 24.37927 0.01288   -10.38838 1.000 70.69473  ? 227 LEU   A O   1 
ATOM   1734 C CB  . LEU   A 1 227 ? 24.88884 -1.73448  -13.03248 1.000 66.11861  ? 227 LEU   A CB  1 
ATOM   1735 C CG  . LEU   A 1 227 ? 24.73882 -2.93638  -12.09911 1.000 66.02475  ? 227 LEU   A CG  1 
ATOM   1736 C CD1 . LEU   A 1 227 ? 23.30453 -3.11469  -11.61421 1.000 60.95189  ? 227 LEU   A CD1 1 
ATOM   1737 C CD2 . LEU   A 1 227 ? 25.23280 -4.18788  -12.80046 1.000 67.84985  ? 227 LEU   A CD2 1 
ATOM   1738 N N   . ASN   A 1 228 ? 25.70852 1.14925   -11.79704 1.000 78.56284  ? 228 ASN   A N   1 
ATOM   1739 C CA  . ASN   A 1 228 ? 26.37033 1.84238   -10.69824 1.000 77.82623  ? 228 ASN   A CA  1 
ATOM   1740 C C   . ASN   A 1 228 ? 25.46661 2.91023   -10.10010 1.000 76.24592  ? 228 ASN   A C   1 
ATOM   1741 O O   . ASN   A 1 228 ? 25.31808 2.99640   -8.87556  1.000 75.26513  ? 228 ASN   A O   1 
ATOM   1742 C CB  . ASN   A 1 228 ? 27.68706 2.45134   -11.17539 1.000 72.67448  ? 228 ASN   A CB  1 
ATOM   1743 C CG  . ASN   A 1 228 ? 28.66638 1.40326   -11.64304 1.000 75.65994  ? 228 ASN   A CG  1 
ATOM   1744 O OD1 . ASN   A 1 228 ? 29.45080 0.87699   -10.85154 1.000 72.98787  ? 228 ASN   A OD1 1 
ATOM   1745 N ND2 . ASN   A 1 228 ? 28.63234 1.09406   -12.93395 1.000 74.63211  ? 228 ASN   A ND2 1 
ATOM   1746 N N   . ASP   A 1 229 ? 24.85015 3.73320   -10.94948 1.000 74.24445  ? 229 ASP   A N   1 
ATOM   1747 C CA  . ASP   A 1 229 ? 23.99813 4.79476   -10.43131 1.000 82.26934  ? 229 ASP   A CA  1 
ATOM   1748 C C   . ASP   A 1 229 ? 22.75626 4.23254   -9.75652  1.000 82.20238  ? 229 ASP   A C   1 
ATOM   1749 O O   . ASP   A 1 229 ? 22.33245 4.74128   -8.71217  1.000 78.99652  ? 229 ASP   A O   1 
ATOM   1750 C CB  . ASP   A 1 229 ? 23.60683 5.76276   -11.54204 1.000 84.98363  ? 229 ASP   A CB  1 
ATOM   1751 C CG  . ASP   A 1 229 ? 23.31885 7.14590   -11.00872 1.000 95.06990  ? 229 ASP   A CG  1 
ATOM   1752 O OD1 . ASP   A 1 229 ? 23.63674 7.39513   -9.82659  1.000 105.67809 ? 229 ASP   A OD1 1 
ATOM   1753 O OD2 . ASP   A 1 229 ? 22.77351 7.98200   -11.75244 1.000 99.82970  ? 229 ASP   A OD2 1 
ATOM   1754 N N   . PHE   A 1 230 ? 22.15467 3.19097   -10.33780 1.000 77.56949  ? 230 PHE   A N   1 
ATOM   1755 C CA  . PHE   A 1 230 ? 21.00508 2.56603   -9.69479  1.000 74.88500  ? 230 PHE   A CA  1 
ATOM   1756 C C   . PHE   A 1 230 ? 21.37643 2.03828   -8.31440  1.000 74.37679  ? 230 PHE   A C   1 
ATOM   1757 O O   . PHE   A 1 230 ? 20.60478 2.18297   -7.35943  1.000 75.02323  ? 230 PHE   A O   1 
ATOM   1758 C CB  . PHE   A 1 230 ? 20.44978 1.44186   -10.57294 1.000 72.09586  ? 230 PHE   A CB  1 
ATOM   1759 C CG  . PHE   A 1 230 ? 19.70331 0.38608   -9.80699  1.000 68.72028  ? 230 PHE   A CG  1 
ATOM   1760 C CD1 . PHE   A 1 230 ? 18.38451 0.59340   -9.43052  1.000 66.15856  ? 230 PHE   A CD1 1 
ATOM   1761 C CD2 . PHE   A 1 230 ? 20.31187 -0.81059  -9.46223  1.000 71.39529  ? 230 PHE   A CD2 1 
ATOM   1762 C CE1 . PHE   A 1 230 ? 17.68865 -0.36705  -8.72145  1.000 61.83778  ? 230 PHE   A CE1 1 
ATOM   1763 C CE2 . PHE   A 1 230 ? 19.61881 -1.77653  -8.74852  1.000 65.68946  ? 230 PHE   A CE2 1 
ATOM   1764 C CZ  . PHE   A 1 230 ? 18.30582 -1.55289  -8.38034  1.000 62.37183  ? 230 PHE   A CZ  1 
ATOM   1765 N N   . ASN   A 1 231 ? 22.56220 1.43281   -8.18755  1.000 72.74622  ? 231 ASN   A N   1 
ATOM   1766 C CA  . ASN   A 1 231 ? 22.99298 0.90218   -6.89574  1.000 74.58002  ? 231 ASN   A CA  1 
ATOM   1767 C C   . ASN   A 1 231 ? 23.11800 2.00509   -5.85495  1.000 81.18353  ? 231 ASN   A C   1 
ATOM   1768 O O   . ASN   A 1 231 ? 22.81694 1.78754   -4.67630  1.000 82.26376  ? 231 ASN   A O   1 
ATOM   1769 C CB  . ASN   A 1 231 ? 24.32506 0.16862   -7.04154  1.000 72.47069  ? 231 ASN   A CB  1 
ATOM   1770 C CG  . ASN   A 1 231 ? 24.15935 -1.25599  -7.51875  1.000 67.74211  ? 231 ASN   A CG  1 
ATOM   1771 O OD1 . ASN   A 1 231 ? 23.28767 -1.98370  -7.04822  1.000 64.22883  ? 231 ASN   A OD1 1 
ATOM   1772 N ND2 . ASN   A 1 231 ? 24.99624 -1.66125  -8.46709  1.000 71.01477  ? 231 ASN   A ND2 1 
ATOM   1773 N N   . LEU   A 1 232 ? 23.55671 3.19431   -6.27616  1.000 81.60507  ? 232 LEU   A N   1 
ATOM   1774 C CA  . LEU   A 1 232 ? 23.77906 4.29278   -5.34096  1.000 83.20189  ? 232 LEU   A CA  1 
ATOM   1775 C C   . LEU   A 1 232 ? 22.48652 4.68661   -4.63656  1.000 83.62123  ? 232 LEU   A C   1 
ATOM   1776 O O   . LEU   A 1 232 ? 22.45577 4.85221   -3.41148  1.000 84.42721  ? 232 LEU   A O   1 
ATOM   1777 C CB  . LEU   A 1 232 ? 24.37934 5.48458   -6.08494  1.000 81.21615  ? 232 LEU   A CB  1 
ATOM   1778 C CG  . LEU   A 1 232 ? 25.89232 5.68764   -5.94035  1.000 89.62717  ? 232 LEU   A CG  1 
ATOM   1779 C CD1 . LEU   A 1 232 ? 26.65334 4.38544   -6.17737  1.000 88.83170  ? 232 LEU   A CD1 1 
ATOM   1780 C CD2 . LEU   A 1 232 ? 26.38441 6.77336   -6.89484  1.000 82.18302  ? 232 LEU   A CD2 1 
ATOM   1781 N N   . VAL   A 1 233 ? 21.40047 4.83316   -5.39705  1.000 83.84850  ? 233 VAL   A N   1 
ATOM   1782 C CA  . VAL   A 1 233 ? 20.11907 5.14464   -4.78196  1.000 84.77181  ? 233 VAL   A CA  1 
ATOM   1783 C C   . VAL   A 1 233 ? 19.52603 3.93114   -4.07118  1.000 84.36416  ? 233 VAL   A C   1 
ATOM   1784 O O   . VAL   A 1 233 ? 18.66183 4.09007   -3.20099  1.000 86.15293  ? 233 VAL   A O   1 
ATOM   1785 C CB  . VAL   A 1 233 ? 19.14930 5.70628   -5.83909  1.000 83.42139  ? 233 VAL   A CB  1 
ATOM   1786 C CG1 . VAL   A 1 233 ? 19.39597 7.19279   -6.04549  1.000 79.40802  ? 233 VAL   A CG1 1 
ATOM   1787 C CG2 . VAL   A 1 233 ? 19.30742 4.96523   -7.15005  1.000 81.30185  ? 233 VAL   A CG2 1 
ATOM   1788 N N   . ALA   A 1 234 ? 19.98072 2.71849   -4.40210  1.000 81.22458  ? 234 ALA   A N   1 
ATOM   1789 C CA  . ALA   A 1 234 ? 19.43050 1.52371   -3.76589  1.000 79.42499  ? 234 ALA   A CA  1 
ATOM   1790 C C   . ALA   A 1 234 ? 19.88450 1.40045   -2.31634  1.000 80.32744  ? 234 ALA   A C   1 
ATOM   1791 O O   . ALA   A 1 234 ? 19.13223 0.91040   -1.46573  1.000 77.78964  ? 234 ALA   A O   1 
ATOM   1792 C CB  . ALA   A 1 234 ? 19.81985 0.27548   -4.55659  1.000 73.38560  ? 234 ALA   A CB  1 
ATOM   1793 N N   . MET   A 1 235 ? 21.10881 1.83598   -2.01174  1.000 77.88535  ? 235 MET   A N   1 
ATOM   1794 C CA  . MET   A 1 235 ? 21.58386 1.75387   -0.63505  1.000 81.69922  ? 235 MET   A CA  1 
ATOM   1795 C C   . MET   A 1 235 ? 20.96067 2.82879   0.24698   1.000 83.01558  ? 235 MET   A C   1 
ATOM   1796 O O   . MET   A 1 235 ? 20.79702 2.61618   1.45515   1.000 83.57541  ? 235 MET   A O   1 
ATOM   1797 C CB  . MET   A 1 235 ? 23.10840 1.83460   -0.60148  1.000 85.73741  ? 235 MET   A CB  1 
ATOM   1798 C CG  . MET   A 1 235 ? 23.77379 1.13856   -1.77623  1.000 94.19798  ? 235 MET   A CG  1 
ATOM   1799 S SD  . MET   A 1 235 ? 25.56209 1.36464   -1.84909  1.000 152.21752 ? 235 MET   A SD  1 
ATOM   1800 C CE  . MET   A 1 235 ? 26.01432 0.09573   -3.03315  1.000 103.85012 ? 235 MET   A CE  1 
ATOM   1801 N N   . LYS   A 1 236 ? 20.60033 3.97863   -0.32590  1.000 79.95148  ? 236 LYS   A N   1 
ATOM   1802 C CA  . LYS   A 1 236 ? 19.88842 4.97669   0.46396   1.000 82.60514  ? 236 LYS   A CA  1 
ATOM   1803 C C   . LYS   A 1 236 ? 18.50408 4.48383   0.86217   1.000 81.48355  ? 236 LYS   A C   1 
ATOM   1804 O O   . LYS   A 1 236 ? 17.96827 4.90735   1.89398   1.000 80.47781  ? 236 LYS   A O   1 
ATOM   1805 C CB  . LYS   A 1 236 ? 19.78457 6.29495   -0.30436  1.000 88.32845  ? 236 LYS   A CB  1 
ATOM   1806 C CG  . LYS   A 1 236 ? 19.35373 7.48218   0.55358   1.000 91.01827  ? 236 LYS   A CG  1 
ATOM   1807 C CD  . LYS   A 1 236 ? 19.91426 7.39534   1.97246   1.000 95.09689  ? 236 LYS   A CD  1 
ATOM   1808 C CE  . LYS   A 1 236 ? 20.10416 8.77704   2.58411   1.000 93.33199  ? 236 LYS   A CE  1 
ATOM   1809 N NZ  . LYS   A 1 236 ? 21.05853 8.76026   3.72806   1.000 96.00078  ? 236 LYS   A NZ  1 
ATOM   1810 N N   . TYR   A 1 237 ? 17.91939 3.58633   0.06738   1.000 82.25986  ? 237 TYR   A N   1 
ATOM   1811 C CA  . TYR   A 1 237 ? 16.61627 3.00242   0.34845   1.000 76.49594  ? 237 TYR   A CA  1 
ATOM   1812 C C   . TYR   A 1 237 ? 16.72168 1.60169   0.93726   1.000 75.11446  ? 237 TYR   A C   1 
ATOM   1813 O O   . TYR   A 1 237 ? 15.74191 0.84962   0.90666   1.000 70.71289  ? 237 TYR   A O   1 
ATOM   1814 C CB  . TYR   A 1 237 ? 15.76539 2.97856   -0.91989  1.000 73.14264  ? 237 TYR   A CB  1 
ATOM   1815 C CG  . TYR   A 1 237 ? 14.83441 4.15972   -1.04516  1.000 77.01202  ? 237 TYR   A CG  1 
ATOM   1816 C CD1 . TYR   A 1 237 ? 15.05728 5.14652   -1.99190  1.000 77.17262  ? 237 TYR   A CD1 1 
ATOM   1817 C CD2 . TYR   A 1 237 ? 13.72975 4.28804   -0.21055  1.000 81.24517  ? 237 TYR   A CD2 1 
ATOM   1818 C CE1 . TYR   A 1 237 ? 14.20401 6.22742   -2.10610  1.000 80.68455  ? 237 TYR   A CE1 1 
ATOM   1819 C CE2 . TYR   A 1 237 ? 12.87159 5.36380   -0.31574  1.000 73.50245  ? 237 TYR   A CE2 1 
ATOM   1820 C CZ  . TYR   A 1 237 ? 13.11415 6.33085   -1.26496  1.000 80.15045  ? 237 TYR   A CZ  1 
ATOM   1821 O OH  . TYR   A 1 237 ? 12.26480 7.40721   -1.37955  1.000 90.43904  ? 237 TYR   A OH  1 
ATOM   1822 N N   . ASN   A 1 238 ? 17.89067 1.24139   1.47066   1.000 73.64249  ? 238 ASN   A N   1 
ATOM   1823 C CA  . ASN   A 1 238 ? 18.10748 -0.05528  2.11714   1.000 76.77118  ? 238 ASN   A CA  1 
ATOM   1824 C C   . ASN   A 1 238 ? 17.74101 -1.21068  1.19329   1.000 74.43635  ? 238 ASN   A C   1 
ATOM   1825 O O   . ASN   A 1 238 ? 17.06350 -2.16076  1.59096   1.000 76.55033  ? 238 ASN   A O   1 
ATOM   1826 C CB  . ASN   A 1 238 ? 17.34544 -0.15545  3.43917   1.000 83.13241  ? 238 ASN   A CB  1 
ATOM   1827 C CG  . ASN   A 1 238 ? 18.17634 0.29984   4.61783   1.000 99.69902  ? 238 ASN   A CG  1 
ATOM   1828 O OD1 . ASN   A 1 238 ? 19.34349 -0.07378  4.74589   1.000 100.64371 ? 238 ASN   A OD1 1 
ATOM   1829 N ND2 . ASN   A 1 238 ? 17.58596 1.11993   5.48119   1.000 106.63252 ? 238 ASN   A ND2 1 
ATOM   1830 N N   . TYR   A 1 239 ? 18.18761 -1.12318  -0.05075  1.000 75.56030  ? 239 TYR   A N   1 
ATOM   1831 C CA  . TYR   A 1 239 ? 18.03541 -2.20397  -1.00684  1.000 69.92887  ? 239 TYR   A CA  1 
ATOM   1832 C C   . TYR   A 1 239 ? 19.36781 -2.92216  -1.17520  1.000 68.81368  ? 239 TYR   A C   1 
ATOM   1833 O O   . TYR   A 1 239 ? 20.44018 -2.32662  -1.02713  1.000 65.40790  ? 239 TYR   A O   1 
ATOM   1834 C CB  . TYR   A 1 239 ? 17.54212 -1.67272  -2.35468  1.000 68.89414  ? 239 TYR   A CB  1 
ATOM   1835 C CG  . TYR   A 1 239 ? 16.03626 -1.62949  -2.49387  1.000 63.99546  ? 239 TYR   A CG  1 
ATOM   1836 C CD1 . TYR   A 1 239 ? 15.23864 -1.08969  -1.49562  1.000 65.36839  ? 239 TYR   A CD1 1 
ATOM   1837 C CD2 . TYR   A 1 239 ? 15.41510 -2.12660  -3.62914  1.000 60.78706  ? 239 TYR   A CD2 1 
ATOM   1838 C CE1 . TYR   A 1 239 ? 13.86151 -1.05184  -1.62566  1.000 67.79118  ? 239 TYR   A CE1 1 
ATOM   1839 C CE2 . TYR   A 1 239 ? 14.04411 -2.09430  -3.76830  1.000 62.83319  ? 239 TYR   A CE2 1 
ATOM   1840 C CZ  . TYR   A 1 239 ? 13.26928 -1.55999  -2.76621  1.000 67.13936  ? 239 TYR   A CZ  1 
ATOM   1841 O OH  . TYR   A 1 239 ? 11.89857 -1.53677  -2.91181  1.000 63.31764  ? 239 TYR   A OH  1 
ATOM   1842 N N   . GLU   A 1 240 ? 19.28696 -4.21491  -1.46596  1.000 66.24454  ? 240 GLU   A N   1 
ATOM   1843 C CA  . GLU   A 1 240 ? 20.48950 -4.98707  -1.73372  1.000 68.66716  ? 240 GLU   A CA  1 
ATOM   1844 C C   . GLU   A 1 240 ? 21.19585 -4.43446  -2.97062  1.000 64.39059  ? 240 GLU   A C   1 
ATOM   1845 O O   . GLU   A 1 240 ? 20.54037 -4.09277  -3.96168  1.000 63.68580  ? 240 GLU   A O   1 
ATOM   1846 C CB  . GLU   A 1 240 ? 20.13960 -6.46018  -1.94373  1.000 66.78184  ? 240 GLU   A CB  1 
ATOM   1847 C CG  . GLU   A 1 240 ? 19.94144 -7.23435  -0.65312  1.000 71.29153  ? 240 GLU   A CG  1 
ATOM   1848 C CD  . GLU   A 1 240 ? 21.21522 -7.34775  0.14996   1.000 79.22604  ? 240 GLU   A CD  1 
ATOM   1849 O OE1 . GLU   A 1 240 ? 22.22508 -7.83610  -0.40235  1.000 81.47951  ? 240 GLU   A OE1 1 
ATOM   1850 O OE2 . GLU   A 1 240 ? 21.20917 -6.93563  1.32902   1.000 84.58775  ? 240 GLU   A OE2 1 
ATOM   1851 N N   . PRO   A 1 241 ? 22.51838 -4.31284  -2.94722  1.000 64.22661  ? 241 PRO   A N   1 
ATOM   1852 C CA  . PRO   A 1 241 ? 23.22869 -3.88697  -4.15841  1.000 66.01161  ? 241 PRO   A CA  1 
ATOM   1853 C C   . PRO   A 1 241 ? 23.04462 -4.91511  -5.26568  1.000 65.98865  ? 241 PRO   A C   1 
ATOM   1854 O O   . PRO   A 1 241 ? 23.21332 -6.11947  -5.05484  1.000 69.77756  ? 241 PRO   A O   1 
ATOM   1855 C CB  . PRO   A 1 241 ? 24.69041 -3.79422  -3.70711  1.000 65.48769  ? 241 PRO   A CB  1 
ATOM   1856 C CG  . PRO   A 1 241 ? 24.77318 -4.61044  -2.46657  1.000 70.63708  ? 241 PRO   A CG  1 
ATOM   1857 C CD  . PRO   A 1 241 ? 23.42676 -4.55904  -1.81698  1.000 70.83593  ? 241 PRO   A CD  1 
ATOM   1858 N N   . LEU   A 1 242 ? 22.67221 -4.43255  -6.44754  1.000 64.72351  ? 242 LEU   A N   1 
ATOM   1859 C CA  . LEU   A 1 242 ? 22.48570 -5.30571  -7.59766  1.000 61.22387  ? 242 LEU   A CA  1 
ATOM   1860 C C   . LEU   A 1 242 ? 23.82575 -5.61942  -8.25144  1.000 61.09792  ? 242 LEU   A C   1 
ATOM   1861 O O   . LEU   A 1 242 ? 24.58813 -4.70979  -8.59849  1.000 54.84531  ? 242 LEU   A O   1 
ATOM   1862 C CB  . LEU   A 1 242 ? 21.55213 -4.65752  -8.61470  1.000 60.03198  ? 242 LEU   A CB  1 
ATOM   1863 C CG  . LEU   A 1 242 ? 20.76898 -5.62518  -9.49934  1.000 60.92629  ? 242 LEU   A CG  1 
ATOM   1864 C CD1 . LEU   A 1 242 ? 19.69398 -6.35047  -8.69886  1.000 55.71753  ? 242 LEU   A CD1 1 
ATOM   1865 C CD2 . LEU   A 1 242 ? 20.18003 -4.89918  -10.69956 1.000 55.53101  ? 242 LEU   A CD2 1 
ATOM   1866 N N   . THR   A 1 243 ? 24.10583 -6.90642  -8.42738  1.000 59.80152  ? 243 THR   A N   1 
ATOM   1867 C CA  . THR   A 1 243 ? 25.32969 -7.35640  -9.07424  1.000 63.07899  ? 243 THR   A CA  1 
ATOM   1868 C C   . THR   A 1 243 ? 25.06450 -7.72613  -10.52918 1.000 57.28270  ? 243 THR   A C   1 
ATOM   1869 O O   . THR   A 1 243 ? 23.92115 -7.82328  -10.98038 1.000 55.74790  ? 243 THR   A O   1 
ATOM   1870 C CB  . THR   A 1 243 ? 25.93118 -8.55487  -8.33416  1.000 60.50369  ? 243 THR   A CB  1 
ATOM   1871 O OG1 . THR   A 1 243 ? 25.04989 -9.67928  -8.45556  1.000 62.10290  ? 243 THR   A OG1 1 
ATOM   1872 C CG2 . THR   A 1 243 ? 26.15363 -8.22881  -6.86310  1.000 52.35932  ? 243 THR   A CG2 1 
ATOM   1873 N N   . GLN   A 1 244 ? 26.15344 -7.92511  -11.27224 1.000 58.58469  ? 244 GLN   A N   1 
ATOM   1874 C CA  . GLN   A 1 244 ? 26.01214 -8.42983  -12.63104 1.000 62.37830  ? 244 GLN   A CA  1 
ATOM   1875 C C   . GLN   A 1 244 ? 25.40641 -9.82646  -12.63628 1.000 62.56071  ? 244 GLN   A C   1 
ATOM   1876 O O   . GLN   A 1 244 ? 24.69880 -10.19106 -13.58283 1.000 62.27661  ? 244 GLN   A O   1 
ATOM   1877 C CB  . GLN   A 1 244 ? 27.36469 -8.42224  -13.34050 1.000 60.18439  ? 244 GLN   A CB  1 
ATOM   1878 C CG  . GLN   A 1 244 ? 27.48182 -7.33355  -14.38549 1.000 70.22835  ? 244 GLN   A CG  1 
ATOM   1879 C CD  . GLN   A 1 244 ? 26.43205 -7.47127  -15.46564 1.000 72.04149  ? 244 GLN   A CD  1 
ATOM   1880 O OE1 . GLN   A 1 244 ? 26.14986 -8.57433  -15.93015 1.000 72.35231  ? 244 GLN   A OE1 1 
ATOM   1881 N NE2 . GLN   A 1 244 ? 25.84053 -6.35124  -15.86703 1.000 74.72065  ? 244 GLN   A NE2 1 
ATOM   1882 N N   . ASP   A 1 245 ? 25.66217 -10.60902 -11.58430 1.000 62.62958  ? 245 ASP   A N   1 
ATOM   1883 C CA  . ASP   A 1 245 ? 25.04333 -11.92384 -11.45373 1.000 58.98688  ? 245 ASP   A CA  1 
ATOM   1884 C C   . ASP   A 1 245 ? 23.52297 -11.81239 -11.42655 1.000 56.76027  ? 245 ASP   A C   1 
ATOM   1885 O O   . ASP   A 1 245 ? 22.82330 -12.51736 -12.16309 1.000 57.25221  ? 245 ASP   A O   1 
ATOM   1886 C CB  . ASP   A 1 245 ? 25.55648 -12.60532 -10.18809 1.000 64.87607  ? 245 ASP   A CB  1 
ATOM   1887 C CG  . ASP   A 1 245 ? 26.73663 -13.50719 -10.45298 1.000 72.40478  ? 245 ASP   A CG  1 
ATOM   1888 O OD1 . ASP   A 1 245 ? 27.20916 -14.16380 -9.50009  1.000 81.11899  ? 245 ASP   A OD1 1 
ATOM   1889 O OD2 . ASP   A 1 245 ? 27.19565 -13.55220 -11.61233 1.000 81.59820  ? 245 ASP   A OD2 1 
ATOM   1890 N N   . HIS   A 1 246 ? 22.99430 -10.92537 -10.57723 1.000 52.72668  ? 246 HIS   A N   1 
ATOM   1891 C CA  . HIS   A 1 246 ? 21.55227 -10.69880 -10.53663 1.000 57.91272  ? 246 HIS   A CA  1 
ATOM   1892 C C   . HIS   A 1 246 ? 21.01490 -10.29474 -11.90178 1.000 56.63472  ? 246 HIS   A C   1 
ATOM   1893 O O   . HIS   A 1 246 ? 19.95675 -10.77473 -12.32632 1.000 58.16781  ? 246 HIS   A O   1 
ATOM   1894 C CB  . HIS   A 1 246 ? 21.21493 -9.62350  -9.50332  1.000 58.85393  ? 246 HIS   A CB  1 
ATOM   1895 C CG  . HIS   A 1 246 ? 21.52656 -10.01717 -8.09390  1.000 60.18803  ? 246 HIS   A CG  1 
ATOM   1896 N ND1 . HIS   A 1 246 ? 21.83362 -9.09628  -7.11535  1.000 60.60667  ? 246 HIS   A ND1 1 
ATOM   1897 C CD2 . HIS   A 1 246 ? 21.56343 -11.22980 -7.49420  1.000 52.89012  ? 246 HIS   A CD2 1 
ATOM   1898 C CE1 . HIS   A 1 246 ? 22.06208 -9.72620  -5.97744  1.000 56.85181  ? 246 HIS   A CE1 1 
ATOM   1899 N NE2 . HIS   A 1 246 ? 21.90369 -11.02164 -6.17997  1.000 61.52361  ? 246 HIS   A NE2 1 
ATOM   1900 N N   . VAL   A 1 247 ? 21.72218 -9.40268  -12.59796 1.000 51.46400  ? 247 VAL   A N   1 
ATOM   1901 C CA  . VAL   A 1 247 ? 21.26601 -8.96915  -13.91299 1.000 55.07141  ? 247 VAL   A CA  1 
ATOM   1902 C C   . VAL   A 1 247 ? 21.10722 -10.17274 -14.83467 1.000 60.75935  ? 247 VAL   A C   1 
ATOM   1903 O O   . VAL   A 1 247 ? 20.11322 -10.28775 -15.56429 1.000 60.35541  ? 247 VAL   A O   1 
ATOM   1904 C CB  . VAL   A 1 247 ? 22.23561 -7.92081  -14.49528 1.000 60.42010  ? 247 VAL   A CB  1 
ATOM   1905 C CG1 . VAL   A 1 247 ? 22.17183 -7.89467  -16.02430 1.000 59.62459  ? 247 VAL   A CG1 1 
ATOM   1906 C CG2 . VAL   A 1 247 ? 21.95482 -6.54742  -13.90705 1.000 59.49913  ? 247 VAL   A CG2 1 
ATOM   1907 N N   . ASP   A 1 248 ? 22.06298 -11.11054 -14.78318 1.000 57.78251  ? 248 ASP   A N   1 
ATOM   1908 C CA  . ASP   A 1 248 ? 22.02353 -12.26900 -15.67114 1.000 55.35649  ? 248 ASP   A CA  1 
ATOM   1909 C C   . ASP   A 1 248 ? 20.89843 -13.22913 -15.30548 1.000 58.18132  ? 248 ASP   A C   1 
ATOM   1910 O O   . ASP   A 1 248 ? 20.38826 -13.94637 -16.17395 1.000 62.41341  ? 248 ASP   A O   1 
ATOM   1911 C CB  . ASP   A 1 248 ? 23.36613 -12.99767 -15.64582 1.000 61.48722  ? 248 ASP   A CB  1 
ATOM   1912 C CG  . ASP   A 1 248 ? 24.49318 -12.16777 -16.22897 1.000 61.27143  ? 248 ASP   A CG  1 
ATOM   1913 O OD1 . ASP   A 1 248 ? 24.22368 -11.32803 -17.11631 1.000 63.92274  ? 248 ASP   A OD1 1 
ATOM   1914 O OD2 . ASP   A 1 248 ? 25.65042 -12.35445 -15.79459 1.000 59.54776  ? 248 ASP   A OD2 1 
ATOM   1915 N N   . ILE   A 1 249 ? 20.49942 -13.26518 -14.03619 1.000 55.75768  ? 249 ILE   A N   1 
ATOM   1916 C CA  . ILE   A 1 249 ? 19.39191 -14.12974 -13.64855 1.000 57.19809  ? 249 ILE   A CA  1 
ATOM   1917 C C   . ILE   A 1 249 ? 18.07599 -13.57621 -14.18466 1.000 56.40714  ? 249 ILE   A C   1 
ATOM   1918 O O   . ILE   A 1 249 ? 17.21080 -14.32810 -14.65113 1.000 57.43315  ? 249 ILE   A O   1 
ATOM   1919 C CB  . ILE   A 1 249 ? 19.36870 -14.29626 -12.12017 1.000 53.58526  ? 249 ILE   A CB  1 
ATOM   1920 C CG1 . ILE   A 1 249 ? 20.46914 -15.25895 -11.68358 1.000 58.98828  ? 249 ILE   A CG1 1 
ATOM   1921 C CG2 . ILE   A 1 249 ? 18.05433 -14.85619 -11.67813 1.000 56.43078  ? 249 ILE   A CG2 1 
ATOM   1922 C CD1 . ILE   A 1 249 ? 20.98317 -15.00218 -10.29142 1.000 59.03707  ? 249 ILE   A CD1 1 
ATOM   1923 N N   . LEU   A 1 250 ? 17.91267 -12.25223 -14.15254 1.000 54.81810  ? 250 LEU   A N   1 
ATOM   1924 C CA  . LEU   A 1 250 ? 16.69733 -11.62857 -14.66210 1.000 54.66370  ? 250 LEU   A CA  1 
ATOM   1925 C C   . LEU   A 1 250 ? 16.60360 -11.67880 -16.17877 1.000 55.95383  ? 250 LEU   A C   1 
ATOM   1926 O O   . LEU   A 1 250 ? 15.53544 -11.38037 -16.72374 1.000 52.21854  ? 250 LEU   A O   1 
ATOM   1927 C CB  . LEU   A 1 250 ? 16.61945 -10.17620 -14.19175 1.000 51.31101  ? 250 LEU   A CB  1 
ATOM   1928 C CG  . LEU   A 1 250 ? 16.41888 -9.99488  -12.68940 1.000 46.79430  ? 250 LEU   A CG  1 
ATOM   1929 C CD1 . LEU   A 1 250 ? 16.75426 -8.58121  -12.26956 1.000 47.02332  ? 250 LEU   A CD1 1 
ATOM   1930 C CD2 . LEU   A 1 250 ? 14.99323 -10.34835 -12.31103 1.000 49.14222  ? 250 LEU   A CD2 1 
ATOM   1931 N N   . GLY   A 1 251 ? 17.68384 -12.06021 -16.85800 1.000 56.91642  ? 251 GLY   A N   1 
ATOM   1932 C CA  . GLY   A 1 251 ? 17.76976 -12.02274 -18.29920 1.000 58.52038  ? 251 GLY   A CA  1 
ATOM   1933 C C   . GLY   A 1 251 ? 16.66288 -12.75796 -19.02690 1.000 60.28154  ? 251 GLY   A C   1 
ATOM   1934 O O   . GLY   A 1 251 ? 15.99773 -12.19759 -19.90503 1.000 60.15394  ? 251 GLY   A O   1 
ATOM   1935 N N   . PRO   A 1 252 ? 16.47757 -14.04490 -18.71423 1.000 63.83643  ? 252 PRO   A N   1 
ATOM   1936 C CA  . PRO   A 1 252 ? 15.28543 -14.75223 -19.21465 1.000 71.21460  ? 252 PRO   A CA  1 
ATOM   1937 C C   . PRO   A 1 252 ? 13.99899 -13.95004 -19.08640 1.000 66.53389  ? 252 PRO   A C   1 
ATOM   1938 O O   . PRO   A 1 252 ? 13.23639 -13.85609 -20.05801 1.000 62.82102  ? 252 PRO   A O   1 
ATOM   1939 C CB  . PRO   A 1 252 ? 15.26951 -16.02143 -18.35475 1.000 64.67471  ? 252 PRO   A CB  1 
ATOM   1940 C CG  . PRO   A 1 252 ? 16.72971 -16.30587 -18.14118 1.000 66.81504  ? 252 PRO   A CG  1 
ATOM   1941 C CD  . PRO   A 1 252 ? 17.41939 -14.96099 -18.04295 1.000 60.48922  ? 252 PRO   A CD  1 
ATOM   1942 N N   . LEU   A 1 253 ? 13.75152 -13.34839 -17.91897 1.000 60.22993  ? 253 LEU   A N   1 
ATOM   1943 C CA  . LEU   A 1 253 ? 12.58862 -12.48148 -17.75566 1.000 58.73113  ? 253 LEU   A CA  1 
ATOM   1944 C C   . LEU   A 1 253 ? 12.68269 -11.25852 -18.65980 1.000 61.14753  ? 253 LEU   A C   1 
ATOM   1945 O O   . LEU   A 1 253 ? 11.70288 -10.88046 -19.31261 1.000 62.53002  ? 253 LEU   A O   1 
ATOM   1946 C CB  . LEU   A 1 253 ? 12.46681 -12.05262 -16.29559 1.000 56.29905  ? 253 LEU   A CB  1 
ATOM   1947 C CG  . LEU   A 1 253 ? 11.83029 -13.06109 -15.34558 1.000 50.40184  ? 253 LEU   A CG  1 
ATOM   1948 C CD1 . LEU   A 1 253 ? 11.73608 -12.48265 -13.94831 1.000 51.27586  ? 253 LEU   A CD1 1 
ATOM   1949 C CD2 . LEU   A 1 253 ? 10.46612 -13.48963 -15.84916 1.000 55.13146  ? 253 LEU   A CD2 1 
ATOM   1950 N N   . SER   A 1 254 ? 13.85340 -10.62275 -18.70677 1.000 63.04693  ? 254 SER   A N   1 
ATOM   1951 C CA  . SER   A 1 254 ? 14.03640 -9.49419  -19.61024 1.000 60.94222  ? 254 SER   A CA  1 
ATOM   1952 C C   . SER   A 1 254 ? 13.71342 -9.87736  -21.04818 1.000 62.18175  ? 254 SER   A C   1 
ATOM   1953 O O   . SER   A 1 254 ? 13.13812 -9.07364  -21.78777 1.000 64.17568  ? 254 SER   A O   1 
ATOM   1954 C CB  . SER   A 1 254 ? 15.46784 -8.96378  -19.50213 1.000 57.43287  ? 254 SER   A CB  1 
ATOM   1955 O OG  . SER   A 1 254 ? 15.66798 -7.83532  -20.33932 1.000 63.90661  ? 254 SER   A OG  1 
ATOM   1956 N N   . ALA   A 1 255 ? 14.04348 -11.10525 -21.45412 1.000 61.63904  ? 255 ALA   A N   1 
ATOM   1957 C CA  . ALA   A 1 255 ? 13.82426 -11.49922 -22.84158 1.000 60.37336  ? 255 ALA   A CA  1 
ATOM   1958 C C   . ALA   A 1 255 ? 12.34298 -11.67423 -23.14713 1.000 66.63939  ? 255 ALA   A C   1 
ATOM   1959 O O   . ALA   A 1 255 ? 11.89043 -11.35726 -24.25238 1.000 69.79261  ? 255 ALA   A O   1 
ATOM   1960 C CB  . ALA   A 1 255 ? 14.58847 -12.78338 -23.15038 1.000 66.66703  ? 255 ALA   A CB  1 
ATOM   1961 N N   . GLN   A 1 256 ? 11.56958 -12.16786 -22.18382 1.000 62.76130  ? 256 GLN   A N   1 
ATOM   1962 C CA  . GLN   A 1 256 ? 10.15956 -12.41980 -22.44237 1.000 68.67820  ? 256 GLN   A CA  1 
ATOM   1963 C C   . GLN   A 1 256 ? 9.34041  -11.13065 -22.47346 1.000 71.98513  ? 256 GLN   A C   1 
ATOM   1964 O O   . GLN   A 1 256 ? 8.29628  -11.08162 -23.13512 1.000 72.18574  ? 256 GLN   A O   1 
ATOM   1965 C CB  . GLN   A 1 256 ? 9.60531  -13.37895 -21.38901 1.000 75.13944  ? 256 GLN   A CB  1 
ATOM   1966 C CG  . GLN   A 1 256 ? 8.38353  -14.14876 -21.84572 1.000 85.75439  ? 256 GLN   A CG  1 
ATOM   1967 C CD  . GLN   A 1 256 ? 7.30080  -14.18313 -20.79645 1.000 98.98745  ? 256 GLN   A CD  1 
ATOM   1968 O OE1 . GLN   A 1 256 ? 6.64753  -13.17279 -20.53283 1.000 107.26099 ? 256 GLN   A OE1 1 
ATOM   1969 N NE2 . GLN   A 1 256 ? 7.10829  -15.34235 -20.18057 1.000 110.12643 ? 256 GLN   A NE2 1 
ATOM   1970 N N   . THR   A 1 257 ? 9.78795  -10.08236 -21.77677 1.000 78.41353  ? 257 THR   A N   1 
ATOM   1971 C CA  . THR   A 1 257 ? 9.06205  -8.81713  -21.73126 1.000 71.27640  ? 257 THR   A CA  1 
ATOM   1972 C C   . THR   A 1 257 ? 9.60930  -7.76462  -22.68601 1.000 67.80823  ? 257 THR   A C   1 
ATOM   1973 O O   . THR   A 1 257 ? 8.93654  -6.75369  -22.90964 1.000 69.24331  ? 257 THR   A O   1 
ATOM   1974 C CB  . THR   A 1 257 ? 9.06943  -8.23669  -20.31013 1.000 65.53905  ? 257 THR   A CB  1 
ATOM   1975 O OG1 . THR   A 1 257 ? 10.38402 -8.34853  -19.75672 1.000 66.64862  ? 257 THR   A OG1 1 
ATOM   1976 C CG2 . THR   A 1 257 ? 8.07736  -8.96852  -19.42117 1.000 64.73777  ? 257 THR   A CG2 1 
ATOM   1977 N N   . GLY   A 1 258 ? 10.80304 -7.96548  -23.24387 1.000 70.36595  ? 258 GLY   A N   1 
ATOM   1978 C CA  . GLY   A 1 258 ? 11.40686 -6.97276  -24.11418 1.000 65.78827  ? 258 GLY   A CA  1 
ATOM   1979 C C   . GLY   A 1 258 ? 11.86070 -5.70450  -23.42842 1.000 62.30325  ? 258 GLY   A C   1 
ATOM   1980 O O   . GLY   A 1 258 ? 12.12853 -4.70914  -24.10757 1.000 68.17569  ? 258 GLY   A O   1 
ATOM   1981 N N   . ILE   A 1 259 ? 11.94164 -5.70441  -22.10292 1.000 67.66604  ? 259 ILE   A N   1 
ATOM   1982 C CA  . ILE   A 1 259 ? 12.40067 -4.56197  -21.32365 1.000 64.33221  ? 259 ILE   A CA  1 
ATOM   1983 C C   . ILE   A 1 259 ? 13.77524 -4.90612  -20.78147 1.000 62.58706  ? 259 ILE   A C   1 
ATOM   1984 O O   . ILE   A 1 259 ? 13.90759 -5.80926  -19.94415 1.000 58.03206  ? 259 ILE   A O   1 
ATOM   1985 C CB  . ILE   A 1 259 ? 11.43321 -4.22793  -20.17663 1.000 68.89969  ? 259 ILE   A CB  1 
ATOM   1986 C CG1 . ILE   A 1 259 ? 9.99451  -4.14556  -20.68359 1.000 65.33409  ? 259 ILE   A CG1 1 
ATOM   1987 C CG2 . ILE   A 1 259 ? 11.84583 -2.94149  -19.47103 1.000 65.99324  ? 259 ILE   A CG2 1 
ATOM   1988 C CD1 . ILE   A 1 259 ? 8.97845  -4.16744  -19.58051 1.000 67.24367  ? 259 ILE   A CD1 1 
ATOM   1989 N N   . ALA   A 1 260 ? 14.79536 -4.19388  -21.25942 1.000 65.48745  ? 260 ALA   A N   1 
ATOM   1990 C CA  . ALA   A 1 260 ? 16.14440 -4.39849  -20.75338 1.000 62.01662  ? 260 ALA   A CA  1 
ATOM   1991 C C   . ALA   A 1 260 ? 16.15069 -4.32884  -19.23355 1.000 62.61122  ? 260 ALA   A C   1 
ATOM   1992 O O   . ALA   A 1 260 ? 15.37074 -3.59569  -18.61859 1.000 62.73879  ? 260 ALA   A O   1 
ATOM   1993 C CB  . ALA   A 1 260 ? 17.10019 -3.35937  -21.32959 1.000 61.61490  ? 260 ALA   A CB  1 
ATOM   1994 N N   . VAL   A 1 261 ? 17.02078 -5.13215  -18.62633 1.000 62.06703  ? 261 VAL   A N   1 
ATOM   1995 C CA  . VAL   A 1 261 ? 17.09423 -5.16636  -17.17144 1.000 59.26333  ? 261 VAL   A CA  1 
ATOM   1996 C C   . VAL   A 1 261 ? 17.42512 -3.78443  -16.62339 1.000 62.74235  ? 261 VAL   A C   1 
ATOM   1997 O O   . VAL   A 1 261 ? 16.83131 -3.33238  -15.63630 1.000 60.95437  ? 261 VAL   A O   1 
ATOM   1998 C CB  . VAL   A 1 261 ? 18.11362 -6.22769  -16.71956 1.000 55.63851  ? 261 VAL   A CB  1 
ATOM   1999 C CG1 . VAL   A 1 261 ? 18.46564 -6.03966  -15.26089 1.000 55.20686  ? 261 VAL   A CG1 1 
ATOM   2000 C CG2 . VAL   A 1 261 ? 17.55541 -7.61765  -16.95601 1.000 54.69388  ? 261 VAL   A CG2 1 
ATOM   2001 N N   . LEU   A 1 262 ? 18.35547 -3.07852  -17.26844 1.000 62.34548  ? 262 LEU   A N   1 
ATOM   2002 C CA  . LEU   A 1 262 ? 18.74301 -1.76731  -16.76555 1.000 61.50409  ? 262 LEU   A CA  1 
ATOM   2003 C C   . LEU   A 1 262 ? 17.60469 -0.75827  -16.88171 1.000 67.87087  ? 262 LEU   A C   1 
ATOM   2004 O O   . LEU   A 1 262 ? 17.51173 0.16507   -16.06312 1.000 70.67094  ? 262 LEU   A O   1 
ATOM   2005 C CB  . LEU   A 1 262 ? 19.98865 -1.26729  -17.49599 1.000 69.87785  ? 262 LEU   A CB  1 
ATOM   2006 C CG  . LEU   A 1 262 ? 21.24878 -2.13837  -17.52226 1.000 72.99483  ? 262 LEU   A CG  1 
ATOM   2007 C CD1 . LEU   A 1 262 ? 21.19290 -3.23666  -18.58728 1.000 71.34082  ? 262 LEU   A CD1 1 
ATOM   2008 C CD2 . LEU   A 1 262 ? 22.47724 -1.25671  -17.71850 1.000 67.04538  ? 262 LEU   A CD2 1 
ATOM   2009 N N   . ASP   A 1 263 ? 16.73072 -0.91365  -17.87996 1.000 67.12804  ? 263 ASP   A N   1 
ATOM   2010 C CA  . ASP   A 1 263 ? 15.58028 -0.02172  -17.98721 1.000 66.79408  ? 263 ASP   A CA  1 
ATOM   2011 C C   . ASP   A 1 263 ? 14.56259 -0.29803  -16.88840 1.000 68.79176  ? 263 ASP   A C   1 
ATOM   2012 O O   . ASP   A 1 263 ? 13.90662 0.63038   -16.39921 1.000 67.70698  ? 263 ASP   A O   1 
ATOM   2013 C CB  . ASP   A 1 263 ? 14.93190 -0.16007  -19.36337 1.000 65.69261  ? 263 ASP   A CB  1 
ATOM   2014 C CG  . ASP   A 1 263 ? 15.77051 0.45828   -20.46431 1.000 77.34426  ? 263 ASP   A CG  1 
ATOM   2015 O OD1 . ASP   A 1 263 ? 16.69551 1.23899   -20.14451 1.000 78.31314  ? 263 ASP   A OD1 1 
ATOM   2016 O OD2 . ASP   A 1 263 ? 15.50990 0.16159   -21.64985 1.000 83.02276  ? 263 ASP   A OD2 1 
ATOM   2017 N N   . MET   A 1 264 ? 14.42189 -1.56314  -16.48847 1.000 66.90686  ? 264 MET   A N   1 
ATOM   2018 C CA  . MET   A 1 264 ? 13.56245 -1.89154  -15.35797 1.000 64.84722  ? 264 MET   A CA  1 
ATOM   2019 C C   . MET   A 1 264 ? 14.11599 -1.30737  -14.06349 1.000 65.37003  ? 264 MET   A C   1 
ATOM   2020 O O   . MET   A 1 264 ? 13.35165 -0.83271  -13.21559 1.000 66.33410  ? 264 MET   A O   1 
ATOM   2021 C CB  . MET   A 1 264 ? 13.39473 -3.40942  -15.25390 1.000 61.74458  ? 264 MET   A CB  1 
ATOM   2022 C CG  . MET   A 1 264 ? 12.30690 -3.86023  -14.29361 1.000 60.74052  ? 264 MET   A CG  1 
ATOM   2023 S SD  . MET   A 1 264 ? 10.64871 -3.52861  -14.91858 1.000 65.65848  ? 264 MET   A SD  1 
ATOM   2024 C CE  . MET   A 1 264 ? 10.20012 -2.14155  -13.88410 1.000 65.97805  ? 264 MET   A CE  1 
ATOM   2025 N N   . CYS   A 1 265 ? 15.44266 -1.31931  -13.89697 1.000 66.19288  ? 265 CYS   A N   1 
ATOM   2026 C CA  . CYS   A 1 265 ? 16.03843 -0.65710  -12.74079 1.000 66.39673  ? 265 CYS   A CA  1 
ATOM   2027 C C   . CYS   A 1 265 ? 15.72314 0.82961   -12.73310 1.000 70.32615  ? 265 CYS   A C   1 
ATOM   2028 O O   . CYS   A 1 265 ? 15.52860 1.41724   -11.66247 1.000 70.74645  ? 265 CYS   A O   1 
ATOM   2029 C CB  . CYS   A 1 265 ? 17.55007 -0.87099  -12.72137 1.000 60.24679  ? 265 CYS   A CB  1 
ATOM   2030 S SG  . CYS   A 1 265 ? 18.04763 -2.58613  -12.81810 1.000 65.86437  ? 265 CYS   A SG  1 
ATOM   2031 N N   . ALA   A 1 266 ? 15.66178 1.45057   -13.91323 1.000 68.65979  ? 266 ALA   A N   1 
ATOM   2032 C CA  . ALA   A 1 266 ? 15.30354 2.86123   -13.98528 1.000 72.02379  ? 266 ALA   A CA  1 
ATOM   2033 C C   . ALA   A 1 266 ? 13.87699 3.09476   -13.50817 1.000 76.42206  ? 266 ALA   A C   1 
ATOM   2034 O O   . ALA   A 1 266 ? 13.62160 4.02487   -12.73517 1.000 79.96726  ? 266 ALA   A O   1 
ATOM   2035 C CB  . ALA   A 1 266 ? 15.47786 3.37475   -15.40969 1.000 77.47523  ? 266 ALA   A CB  1 
ATOM   2036 N N   . SER   A 1 267 ? 12.93181 2.26559   -13.95754 1.000 75.27571  ? 267 SER   A N   1 
ATOM   2037 C CA  . SER   A 1 267 ? 11.55527 2.41794   -13.49841 1.000 76.09809  ? 267 SER   A CA  1 
ATOM   2038 C C   . SER   A 1 267 ? 11.44500 2.17595   -11.99676 1.000 74.04457  ? 267 SER   A C   1 
ATOM   2039 O O   . SER   A 1 267 ? 10.67500 2.85611   -11.30896 1.000 79.60105  ? 267 SER   A O   1 
ATOM   2040 C CB  . SER   A 1 267 ? 10.62838 1.48352   -14.27883 1.000 75.96852  ? 267 SER   A CB  1 
ATOM   2041 O OG  . SER   A 1 267 ? 10.73104 1.70906   -15.67672 1.000 78.00817  ? 267 SER   A OG  1 
ATOM   2042 N N   . LEU   A 1 268 ? 12.22243 1.22750   -11.46423 1.000 70.72453  ? 268 LEU   A N   1 
ATOM   2043 C CA  . LEU   A 1 268 ? 12.22678 1.00878   -10.02001 1.000 67.41249  ? 268 LEU   A CA  1 
ATOM   2044 C C   . LEU   A 1 268 ? 12.88188 2.16667   -9.27466  1.000 72.27703  ? 268 LEU   A C   1 
ATOM   2045 O O   . LEU   A 1 268 ? 12.46662 2.49445   -8.15656  1.000 73.75034  ? 268 LEU   A O   1 
ATOM   2046 C CB  . LEU   A 1 268 ? 12.93231 -0.30477  -9.68290  1.000 63.69470  ? 268 LEU   A CB  1 
ATOM   2047 C CG  . LEU   A 1 268 ? 13.22311 -0.56918  -8.20156  1.000 64.73191  ? 268 LEU   A CG  1 
ATOM   2048 C CD1 . LEU   A 1 268 ? 11.94607 -0.57576  -7.37418  1.000 62.82793  ? 268 LEU   A CD1 1 
ATOM   2049 C CD2 . LEU   A 1 268 ? 13.97097 -1.87703  -8.02813  1.000 58.28520  ? 268 LEU   A CD2 1 
ATOM   2050 N N   . LYS   A 1 269 ? 13.89960 2.79391   -9.86960  1.000 73.08298  ? 269 LYS   A N   1 
ATOM   2051 C CA  . LYS   A 1 269 ? 14.52468 3.96009   -9.25261  1.000 72.75996  ? 269 LYS   A CA  1 
ATOM   2052 C C   . LYS   A 1 269 ? 13.49560 5.05724   -9.00203  1.000 75.55636  ? 269 LYS   A C   1 
ATOM   2053 O O   . LYS   A 1 269 ? 13.28965 5.49044   -7.86196  1.000 74.53531  ? 269 LYS   A O   1 
ATOM   2054 C CB  . LYS   A 1 269 ? 15.66362 4.47051   -10.14203 1.000 75.78667  ? 269 LYS   A CB  1 
ATOM   2055 C CG  . LYS   A 1 269 ? 16.55916 5.51991   -9.49003  1.000 77.03697  ? 269 LYS   A CG  1 
ATOM   2056 C CD  . LYS   A 1 269 ? 17.74318 5.89018   -10.37960 1.000 74.65524  ? 269 LYS   A CD  1 
ATOM   2057 C CE  . LYS   A 1 269 ? 17.66281 7.33271   -10.84727 1.000 78.11815  ? 269 LYS   A CE  1 
ATOM   2058 N NZ  . LYS   A 1 269 ? 18.20060 7.49133   -12.22325 1.000 74.16986  ? 269 LYS   A NZ  1 
ATOM   2059 N N   . GLU   A 1 270 ? 12.82295 5.50504   -10.06638 1.000 75.77065  ? 270 GLU   A N   1 
ATOM   2060 C CA  . GLU   A 1 270 ? 11.82138 6.55668   -9.93052  1.000 76.78848  ? 270 GLU   A CA  1 
ATOM   2061 C C   . GLU   A 1 270 ? 10.66083 6.11643   -9.05014  1.000 79.87421  ? 270 GLU   A C   1 
ATOM   2062 O O   . GLU   A 1 270 ? 10.06526 6.94565   -8.35355  1.000 82.53500  ? 270 GLU   A O   1 
ATOM   2063 C CB  . GLU   A 1 270 ? 11.31520 6.98270   -11.30988 1.000 80.00147  ? 270 GLU   A CB  1 
ATOM   2064 N N   . LEU   A 1 271 ? 10.32784 4.82105   -9.06331  1.000 78.67232  ? 271 LEU   A N   1 
ATOM   2065 C CA  . LEU   A 1 271 ? 9.29198  4.31286   -8.16768  1.000 76.01571  ? 271 LEU   A CA  1 
ATOM   2066 C C   . LEU   A 1 271 ? 9.71465  4.43553   -6.71095  1.000 77.07660  ? 271 LEU   A C   1 
ATOM   2067 O O   . LEU   A 1 271 ? 8.89587  4.76249   -5.84361  1.000 79.68558  ? 271 LEU   A O   1 
ATOM   2068 C CB  . LEU   A 1 271 ? 8.96293  2.85798   -8.50645  1.000 70.69226  ? 271 LEU   A CB  1 
ATOM   2069 C CG  . LEU   A 1 271 ? 7.64668  2.55347   -9.23180  1.000 69.72090  ? 271 LEU   A CG  1 
ATOM   2070 C CD1 . LEU   A 1 271 ? 6.45497  2.71280   -8.30560  1.000 68.74569  ? 271 LEU   A CD1 1 
ATOM   2071 C CD2 . LEU   A 1 271 ? 7.48465  3.44106   -10.45951 1.000 77.44941  ? 271 LEU   A CD2 1 
ATOM   2072 N N   . LEU   A 1 272 ? 10.98867 4.17706   -6.41974  1.000 72.82700  ? 272 LEU   A N   1 
ATOM   2073 C CA  . LEU   A 1 272 ? 11.45057 4.29769   -5.04322  1.000 76.61405  ? 272 LEU   A CA  1 
ATOM   2074 C C   . LEU   A 1 272 ? 11.46111 5.75203   -4.59168  1.000 80.73775  ? 272 LEU   A C   1 
ATOM   2075 O O   . LEU   A 1 272 ? 11.09931 6.05548   -3.45065  1.000 81.07398  ? 272 LEU   A O   1 
ATOM   2076 C CB  . LEU   A 1 272 ? 12.83967 3.68353   -4.89809  1.000 71.91088  ? 272 LEU   A CB  1 
ATOM   2077 C CG  . LEU   A 1 272 ? 12.84393 2.22977   -4.43912  1.000 73.05834  ? 272 LEU   A CG  1 
ATOM   2078 C CD1 . LEU   A 1 272 ? 14.08755 1.51147   -4.94119  1.000 70.03530  ? 272 LEU   A CD1 1 
ATOM   2079 C CD2 . LEU   A 1 272 ? 12.73836 2.16020   -2.92927  1.000 74.14879  ? 272 LEU   A CD2 1 
ATOM   2080 N N   . GLN   A 1 273 ? 11.85219 6.66699   -5.47619  1.000 78.62536  ? 273 GLN   A N   1 
ATOM   2081 C CA  . GLN   A 1 273 ? 12.03967 8.06063   -5.09755  1.000 86.20072  ? 273 GLN   A CA  1 
ATOM   2082 C C   . GLN   A 1 273 ? 10.75470 8.87824   -5.11051  1.000 87.19553  ? 273 GLN   A C   1 
ATOM   2083 O O   . GLN   A 1 273 ? 10.73758 9.98008   -4.55028  1.000 80.66846  ? 273 GLN   A O   1 
ATOM   2084 C CB  . GLN   A 1 273 ? 13.06316 8.71706   -6.02648  1.000 87.40076  ? 273 GLN   A CB  1 
ATOM   2085 C CG  . GLN   A 1 273 ? 14.38975 7.98489   -6.08605  1.000 87.55511  ? 273 GLN   A CG  1 
ATOM   2086 C CD  . GLN   A 1 273 ? 15.53521 8.90307   -6.45074  1.000 89.35071  ? 273 GLN   A CD  1 
ATOM   2087 O OE1 . GLN   A 1 273 ? 16.13135 9.53932   -5.58254  1.000 94.88804  ? 273 GLN   A OE1 1 
ATOM   2088 N NE2 . GLN   A 1 273 ? 15.84326 8.98659   -7.74451  1.000 84.09268  ? 273 GLN   A NE2 1 
ATOM   2089 N N   . ASN   A 1 274 ? 9.68441  8.37289   -5.72810  1.000 87.17621  ? 274 ASN   A N   1 
ATOM   2090 C CA  . ASN   A 1 274 ? 8.44815  9.12673   -5.87658  1.000 85.73060  ? 274 ASN   A CA  1 
ATOM   2091 C C   . ASN   A 1 274 ? 7.20829  8.39969   -5.36533  1.000 85.15227  ? 274 ASN   A C   1 
ATOM   2092 O O   . ASN   A 1 274 ? 6.13473  9.01025   -5.31815  1.000 84.17210  ? 274 ASN   A O   1 
ATOM   2093 C CB  . ASN   A 1 274 ? 8.23252  9.50821   -7.35213  1.000 87.22383  ? 274 ASN   A CB  1 
ATOM   2094 C CG  . ASN   A 1 274 ? 9.49124  10.07404  -8.00945  1.000 91.95997  ? 274 ASN   A CG  1 
ATOM   2095 O OD1 . ASN   A 1 274 ? 9.89577  9.62506   -9.08382  1.000 94.78438  ? 274 ASN   A OD1 1 
ATOM   2096 N ND2 . ASN   A 1 274 ? 10.10004 11.07554  -7.37716  1.000 90.56394  ? 274 ASN   A ND2 1 
ATOM   2097 N N   . GLY   A 1 275 ? 7.31515  7.12796   -4.98927  1.000 83.84746  ? 275 GLY   A N   1 
ATOM   2098 C CA  . GLY   A 1 275 ? 6.19355  6.39311   -4.44199  1.000 90.63384  ? 275 GLY   A CA  1 
ATOM   2099 C C   . GLY   A 1 275 ? 5.17191  5.98635   -5.49150  1.000 93.12696  ? 275 GLY   A C   1 
ATOM   2100 O O   . GLY   A 1 275 ? 5.20874  6.40589   -6.64993  1.000 92.88312  ? 275 GLY   A O   1 
ATOM   2101 N N   . MET   A 1 276 ? 4.22545  5.14575   -5.06042  1.000 92.23452  ? 276 MET   A N   1 
ATOM   2102 C CA  . MET   A 1 276 ? 3.17174  4.66381   -5.94626  1.000 86.44970  ? 276 MET   A CA  1 
ATOM   2103 C C   . MET   A 1 276 ? 2.00849  5.63412   -6.08848  1.000 89.74797  ? 276 MET   A C   1 
ATOM   2104 O O   . MET   A 1 276 ? 1.12792  5.39096   -6.92117  1.000 85.93932  ? 276 MET   A O   1 
ATOM   2105 C CB  . MET   A 1 276 ? 2.64638  3.31542   -5.46029  1.000 82.10078  ? 276 MET   A CB  1 
ATOM   2106 C CG  . MET   A 1 276 ? 3.28393  2.14428   -6.16906  1.000 78.10110  ? 276 MET   A CG  1 
ATOM   2107 S SD  . MET   A 1 276 ? 3.75507  0.84337   -5.03051  1.000 86.71603  ? 276 MET   A SD  1 
ATOM   2108 C CE  . MET   A 1 276 ? 5.10511  1.65238   -4.17196  1.000 79.52007  ? 276 MET   A CE  1 
ATOM   2109 N N   . ASN   A 1 277 ? 1.98125  6.71299   -5.30406  1.000 94.44178  ? 277 ASN   A N   1 
ATOM   2110 C CA  . ASN   A 1 277 ? 0.95796  7.75049   -5.43058  1.000 89.40375  ? 277 ASN   A CA  1 
ATOM   2111 C C   . ASN   A 1 277 ? -0.44703 7.16730   -5.29049  1.000 88.96968  ? 277 ASN   A C   1 
ATOM   2112 O O   . ASN   A 1 277 ? -1.38010 7.56860   -5.99143  1.000 85.49413  ? 277 ASN   A O   1 
ATOM   2113 C CB  . ASN   A 1 277 ? 1.10585  8.51020   -6.75224  1.000 90.33828  ? 277 ASN   A CB  1 
ATOM   2114 C CG  . ASN   A 1 277 ? 1.76846  9.86485   -6.57663  1.000 98.19273  ? 277 ASN   A CG  1 
ATOM   2115 O OD1 . ASN   A 1 277 ? 1.59209  10.52580  -5.55358  1.000 96.44465  ? 277 ASN   A OD1 1 
ATOM   2116 N ND2 . ASN   A 1 277 ? 2.53006  10.28803  -7.57944  1.000 103.34129 ? 277 ASN   A ND2 1 
ATOM   2117 N N   . GLY   A 1 278 ? -0.59932 6.20944   -4.37577  1.000 83.95715  ? 278 GLY   A N   1 
ATOM   2118 C CA  . GLY   A 1 278 ? -1.87486 5.56172   -4.15938  1.000 84.52930  ? 278 GLY   A CA  1 
ATOM   2119 C C   . GLY   A 1 278 ? -2.24531 4.51027   -5.18141  1.000 84.65263  ? 278 GLY   A C   1 
ATOM   2120 O O   . GLY   A 1 278 ? -3.29069 3.86415   -5.03057  1.000 82.10879  ? 278 GLY   A O   1 
ATOM   2121 N N   . ARG   A 1 279 ? -1.43654 4.32301   -6.21870  1.000 85.57563  ? 279 ARG   A N   1 
ATOM   2122 C CA  . ARG   A 1 279 ? -1.67262 3.25693   -7.17376  1.000 80.44057  ? 279 ARG   A CA  1 
ATOM   2123 C C   . ARG   A 1 279 ? -1.20861 1.92338   -6.59037  1.000 76.83744  ? 279 ARG   A C   1 
ATOM   2124 O O   . ARG   A 1 279 ? -0.63420 1.85049   -5.50005  1.000 75.84432  ? 279 ARG   A O   1 
ATOM   2125 C CB  . ARG   A 1 279 ? -0.95862 3.55396   -8.49296  1.000 81.46873  ? 279 ARG   A CB  1 
ATOM   2126 C CG  . ARG   A 1 279 ? -1.62551 4.62750   -9.34850  1.000 79.92637  ? 279 ARG   A CG  1 
ATOM   2127 C CD  . ARG   A 1 279 ? -0.72227 5.84678   -9.51679  1.000 79.43262  ? 279 ARG   A CD  1 
ATOM   2128 N NE  . ARG   A 1 279 ? -1.27976 6.83128   -10.44015 1.000 90.49446  ? 279 ARG   A NE  1 
ATOM   2129 C CZ  . ARG   A 1 279 ? -2.26941 7.67031   -10.15473 1.000 88.73482  ? 279 ARG   A CZ  1 
ATOM   2130 N NH1 . ARG   A 1 279 ? -2.83796 7.69377   -8.95888  1.000 82.31639  ? 279 ARG   A NH1 1 
ATOM   2131 N NH2 . ARG   A 1 279 ? -2.70061 8.50755   -11.09450 1.000 81.07587  ? 279 ARG   A NH2 1 
ATOM   2132 N N   . THR   A 1 280 ? -1.47349 0.85255   -7.32998  1.000 75.91050  ? 280 THR   A N   1 
ATOM   2133 C CA  . THR   A 1 280 ? -1.11796 -0.48700  -6.89261  1.000 74.56293  ? 280 THR   A CA  1 
ATOM   2134 C C   . THR   A 1 280 ? -0.56821 -1.27736  -8.06851  1.000 70.32423  ? 280 THR   A C   1 
ATOM   2135 O O   . THR   A 1 280 ? -0.96582 -1.07181  -9.21799  1.000 72.64898  ? 280 THR   A O   1 
ATOM   2136 C CB  . THR   A 1 280 ? -2.32003 -1.22445  -6.29210  1.000 70.46920  ? 280 THR   A CB  1 
ATOM   2137 O OG1 . THR   A 1 280 ? -3.46539 -1.02657  -7.12982  1.000 68.42672  ? 280 THR   A OG1 1 
ATOM   2138 C CG2 . THR   A 1 280 ? -2.61804 -0.70777  -4.89450  1.000 73.25114  ? 280 THR   A CG2 1 
ATOM   2139 N N   . ILE   A 1 281 ? 0.34719  -2.18995  -7.76414  1.000 63.27104  ? 281 ILE   A N   1 
ATOM   2140 C CA  . ILE   A 1 281 ? 0.96087  -3.06397  -8.75442  1.000 63.03483  ? 281 ILE   A CA  1 
ATOM   2141 C C   . ILE   A 1 281 ? 0.62510  -4.49690  -8.37305  1.000 63.63866  ? 281 ILE   A C   1 
ATOM   2142 O O   . ILE   A 1 281 ? 0.97533  -4.94861  -7.27401  1.000 58.59817  ? 281 ILE   A O   1 
ATOM   2143 C CB  . ILE   A 1 281 ? 2.48187  -2.86340  -8.82788  1.000 62.57424  ? 281 ILE   A CB  1 
ATOM   2144 C CG1 . ILE   A 1 281 ? 2.81695  -1.42619  -9.23435  1.000 62.13016  ? 281 ILE   A CG1 1 
ATOM   2145 C CG2 . ILE   A 1 281 ? 3.09204  -3.85394  -9.80158  1.000 58.97679  ? 281 ILE   A CG2 1 
ATOM   2146 C CD1 . ILE   A 1 281 ? 4.29876  -1.12199  -9.22764  1.000 58.44639  ? 281 ILE   A CD1 1 
ATOM   2147 N N   . LEU   A 1 282 ? -0.04823 -5.21046  -9.27686  1.000 61.55357  ? 282 LEU   A N   1 
ATOM   2148 C CA  . LEU   A 1 282 ? -0.44971 -6.59636  -9.03147  1.000 60.15758  ? 282 LEU   A CA  1 
ATOM   2149 C C   . LEU   A 1 282 ? -1.24506 -6.71703  -7.73282  1.000 61.39986  ? 282 LEU   A C   1 
ATOM   2150 O O   . LEU   A 1 282 ? -1.08736 -7.67631  -6.97352  1.000 59.56191  ? 282 LEU   A O   1 
ATOM   2151 C CB  . LEU   A 1 282 ? 0.76162  -7.53372  -9.00815  1.000 59.19090  ? 282 LEU   A CB  1 
ATOM   2152 C CG  . LEU   A 1 282 ? 1.33988  -8.02937  -10.33410 1.000 59.48161  ? 282 LEU   A CG  1 
ATOM   2153 C CD1 . LEU   A 1 282 ? 2.54675  -8.91694  -10.08397 1.000 52.71098  ? 282 LEU   A CD1 1 
ATOM   2154 C CD2 . LEU   A 1 282 ? 0.28906  -8.76713  -11.14522 1.000 62.77407  ? 282 LEU   A CD2 1 
ATOM   2155 N N   . GLY   A 1 283 ? -2.08906 -5.72225  -7.46471  1.000 61.55594  ? 283 GLY   A N   1 
ATOM   2156 C CA  . GLY   A 1 283 ? -2.95270 -5.74320  -6.30281  1.000 63.20619  ? 283 GLY   A CA  1 
ATOM   2157 C C   . GLY   A 1 283 ? -2.28199 -5.44895  -4.98148  1.000 67.95109  ? 283 GLY   A C   1 
ATOM   2158 O O   . GLY   A 1 283 ? -2.88044 -5.71385  -3.93115  1.000 80.13002  ? 283 GLY   A O   1 
ATOM   2159 N N   . SER   A 1 284 ? -1.06225 -4.91906  -4.99300  1.000 63.61613  ? 284 SER   A N   1 
ATOM   2160 C CA  . SER   A 1 284 ? -0.37456 -4.51272  -3.77777  1.000 66.31014  ? 284 SER   A CA  1 
ATOM   2161 C C   . SER   A 1 284 ? 0.06410  -3.06367  -3.92456  1.000 68.27408  ? 284 SER   A C   1 
ATOM   2162 O O   . SER   A 1 284 ? 0.42473  -2.62612  -5.02142  1.000 70.43013  ? 284 SER   A O   1 
ATOM   2163 C CB  . SER   A 1 284 ? 0.83395  -5.41666  -3.49549  1.000 68.03360  ? 284 SER   A CB  1 
ATOM   2164 O OG  . SER   A 1 284 ? 1.81150  -4.75166  -2.71379  1.000 67.42053  ? 284 SER   A OG  1 
ATOM   2165 N N   . ALA   A 1 285 ? 0.01154  -2.31586  -2.82571  1.000 66.07561  ? 285 ALA   A N   1 
ATOM   2166 C CA  . ALA   A 1 285 ? 0.50333  -0.94639  -2.81411  1.000 68.21578  ? 285 ALA   A CA  1 
ATOM   2167 C C   . ALA   A 1 285 ? 1.94125  -0.85166  -2.32740  1.000 67.26805  ? 285 ALA   A C   1 
ATOM   2168 O O   . ALA   A 1 285 ? 2.47120  0.25749   -2.20773  1.000 69.65124  ? 285 ALA   A O   1 
ATOM   2169 C CB  . ALA   A 1 285 ? -0.40458 -0.06277  -1.95543  1.000 68.82677  ? 285 ALA   A CB  1 
ATOM   2170 N N   . LEU   A 1 286 ? 2.57764  -1.98603  -2.05589  1.000 67.12001  ? 286 LEU   A N   1 
ATOM   2171 C CA  . LEU   A 1 286 ? 3.98275  -2.06518  -1.69084  1.000 68.91951  ? 286 LEU   A CA  1 
ATOM   2172 C C   . LEU   A 1 286 ? 4.77353  -2.78975  -2.77256  1.000 66.44301  ? 286 LEU   A C   1 
ATOM   2173 O O   . LEU   A 1 286 ? 4.22013  -3.50843  -3.60878  1.000 64.50453  ? 286 LEU   A O   1 
ATOM   2174 C CB  . LEU   A 1 286 ? 4.16282  -2.78383  -0.34622  1.000 65.49382  ? 286 LEU   A CB  1 
ATOM   2175 C CG  . LEU   A 1 286 ? 3.67126  -2.10147  0.92528   1.000 71.85690  ? 286 LEU   A CG  1 
ATOM   2176 C CD1 . LEU   A 1 286 ? 4.53379  -2.53188  2.09548   1.000 68.85654  ? 286 LEU   A CD1 1 
ATOM   2177 C CD2 . LEU   A 1 286 ? 3.75363  -0.59257  0.75178   1.000 76.35722  ? 286 LEU   A CD2 1 
ATOM   2178 N N   . LEU   A 1 287 ? 6.08414  -2.58308  -2.74995  1.000 64.81432  ? 287 LEU   A N   1 
ATOM   2179 C CA  . LEU   A 1 287 ? 6.98219  -3.33909  -3.60764  1.000 60.25849  ? 287 LEU   A CA  1 
ATOM   2180 C C   . LEU   A 1 287 ? 7.26308  -4.68655  -2.94980  1.000 60.73641  ? 287 LEU   A C   1 
ATOM   2181 O O   . LEU   A 1 287 ? 7.82169  -4.73906  -1.84799  1.000 59.82579  ? 287 LEU   A O   1 
ATOM   2182 C CB  . LEU   A 1 287 ? 8.26706  -2.55057  -3.84662  1.000 57.45889  ? 287 LEU   A CB  1 
ATOM   2183 C CG  . LEU   A 1 287 ? 8.04002  -1.24572  -4.61444  1.000 60.98368  ? 287 LEU   A CG  1 
ATOM   2184 C CD1 . LEU   A 1 287 ? 9.34684  -0.51627  -4.83956  1.000 63.25872  ? 287 LEU   A CD1 1 
ATOM   2185 C CD2 . LEU   A 1 287 ? 7.34011  -1.51575  -5.93707  1.000 61.75560  ? 287 LEU   A CD2 1 
ATOM   2186 N N   . GLU   A 1 288 ? 6.85183  -5.76925  -3.61290  1.000 56.54005  ? 288 GLU   A N   1 
ATOM   2187 C CA  . GLU   A 1 288 ? 7.01184  -7.12409  -3.09882  1.000 59.79421  ? 288 GLU   A CA  1 
ATOM   2188 C C   . GLU   A 1 288 ? 8.38538  -7.67514  -3.46052  1.000 55.81168  ? 288 GLU   A C   1 
ATOM   2189 O O   . GLU   A 1 288 ? 8.83658  -7.53354  -4.59933  1.000 59.04283  ? 288 GLU   A O   1 
ATOM   2190 C CB  . GLU   A 1 288 ? 5.92976  -8.03891  -3.67404  1.000 62.20201  ? 288 GLU   A CB  1 
ATOM   2191 C CG  . GLU   A 1 288 ? 4.51843  -7.67177  -3.26381  1.000 65.51581  ? 288 GLU   A CG  1 
ATOM   2192 C CD  . GLU   A 1 288 ? 4.13336  -8.27235  -1.93072  1.000 86.49075  ? 288 GLU   A CD  1 
ATOM   2193 O OE1 . GLU   A 1 288 ? 4.64215  -7.78878  -0.89656  1.000 88.09673  ? 288 GLU   A OE1 1 
ATOM   2194 O OE2 . GLU   A 1 288 ? 3.32231  -9.22249  -1.91465  1.000 100.03901 ? 288 GLU   A OE2 1 
ATOM   2195 N N   . ASP   A 1 289 ? 9.04023  -8.33666  -2.49556  1.000 53.21215  ? 289 ASP   A N   1 
ATOM   2196 C CA  . ASP   A 1 289 ? 10.39049 -8.84855  -2.71718  1.000 51.95504  ? 289 ASP   A CA  1 
ATOM   2197 C C   . ASP   A 1 289 ? 10.54190 -10.32463 -2.35924  1.000 56.91382  ? 289 ASP   A C   1 
ATOM   2198 O O   . ASP   A 1 289 ? 11.67014 -10.80298 -2.20328  1.000 54.40652  ? 289 ASP   A O   1 
ATOM   2199 C CB  . ASP   A 1 289 ? 11.41920 -8.01575  -1.94338  1.000 55.87595  ? 289 ASP   A CB  1 
ATOM   2200 C CG  . ASP   A 1 289 ? 11.34550 -8.22769  -0.44511  1.000 60.79672  ? 289 ASP   A CG  1 
ATOM   2201 O OD1 . ASP   A 1 289 ? 10.22998 -8.46831  0.06800   1.000 62.93707  ? 289 ASP   A OD1 1 
ATOM   2202 O OD2 . ASP   A 1 289 ? 12.40454 -8.13256  0.21891   1.000 57.86932  ? 289 ASP   A OD2 1 
ATOM   2203 N N   . GLU   A 1 290 ? 9.44374  -11.06119 -2.22533  1.000 57.94656  ? 290 GLU   A N   1 
ATOM   2204 C CA  . GLU   A 1 290 ? 9.48455  -12.49343 -1.94424  1.000 52.21725  ? 290 GLU   A CA  1 
ATOM   2205 C C   . GLU   A 1 290 ? 9.06025  -13.30514 -3.16270  1.000 53.51293  ? 290 GLU   A C   1 
ATOM   2206 O O   . GLU   A 1 290 ? 8.28262  -14.25494 -3.06355  1.000 52.42276  ? 290 GLU   A O   1 
ATOM   2207 C CB  . GLU   A 1 290 ? 8.61854  -12.83685 -0.73843  1.000 49.42604  ? 290 GLU   A CB  1 
ATOM   2208 C CG  . GLU   A 1 290 ? 8.75745  -11.85283 0.39999   1.000 62.61557  ? 290 GLU   A CG  1 
ATOM   2209 C CD  . GLU   A 1 290 ? 8.97685  -12.53277 1.73538   1.000 75.02001  ? 290 GLU   A CD  1 
ATOM   2210 O OE1 . GLU   A 1 290 ? 8.30571  -13.55652 1.99510   1.000 77.24214  ? 290 GLU   A OE1 1 
ATOM   2211 O OE2 . GLU   A 1 290 ? 9.82047  -12.04531 2.52206   1.000 66.98259  ? 290 GLU   A OE2 1 
ATOM   2212 N N   . PHE   A 1 291 ? 9.56145  -12.91436 -4.32982  1.000 52.96134  ? 291 PHE   A N   1 
ATOM   2213 C CA  . PHE   A 1 291 ? 9.37565  -13.65435 -5.57417  1.000 51.34074  ? 291 PHE   A CA  1 
ATOM   2214 C C   . PHE   A 1 291 ? 10.73159 -13.65665 -6.27283  1.000 50.23003  ? 291 PHE   A C   1 
ATOM   2215 O O   . PHE   A 1 291 ? 11.13699 -12.63948 -6.84294  1.000 48.30473  ? 291 PHE   A O   1 
ATOM   2216 C CB  . PHE   A 1 291 ? 8.30029  -13.02187 -6.45569  1.000 55.43350  ? 291 PHE   A CB  1 
ATOM   2217 C CG  . PHE   A 1 291 ? 6.89986  -13.14732 -5.91318  1.000 54.98031  ? 291 PHE   A CG  1 
ATOM   2218 C CD1 . PHE   A 1 291 ? 6.22284  -14.35493 -5.97552  1.000 54.14149  ? 291 PHE   A CD1 1 
ATOM   2219 C CD2 . PHE   A 1 291 ? 6.24739  -12.04635 -5.37634  1.000 52.25653  ? 291 PHE   A CD2 1 
ATOM   2220 C CE1 . PHE   A 1 291 ? 4.92884  -14.46791 -5.48965  1.000 55.68437  ? 291 PHE   A CE1 1 
ATOM   2221 C CE2 . PHE   A 1 291 ? 4.95767  -12.15205 -4.88927  1.000 54.60384  ? 291 PHE   A CE2 1 
ATOM   2222 C CZ  . PHE   A 1 291 ? 4.29743  -13.36514 -4.94502  1.000 55.65389  ? 291 PHE   A CZ  1 
ATOM   2223 N N   . THR   A 1 292 ? 11.44479 -14.78018 -6.20803  1.000 52.38960  ? 292 THR   A N   1 
ATOM   2224 C CA  . THR   A 1 292 ? 12.69924 -14.88932 -6.93373  1.000 49.41405  ? 292 THR   A CA  1 
ATOM   2225 C C   . THR   A 1 292 ? 12.43288 -14.92542 -8.43574  1.000 50.91378  ? 292 THR   A C   1 
ATOM   2226 O O   . THR   A 1 292 ? 11.34606 -15.31290 -8.87326  1.000 51.03949  ? 292 THR   A O   1 
ATOM   2227 C CB  . THR   A 1 292 ? 13.46534 -16.14724 -6.53171  1.000 48.83286  ? 292 THR   A CB  1 
ATOM   2228 O OG1 . THR   A 1 292 ? 12.73161 -17.30219 -6.95268  1.000 55.59131  ? 292 THR   A OG1 1 
ATOM   2229 C CG2 . THR   A 1 292 ? 13.69809 -16.20071 -5.03109  1.000 48.21869  ? 292 THR   A CG2 1 
ATOM   2230 N N   . PRO   A 1 293 ? 13.40746 -14.52038 -9.24660  1.000 45.63205  ? 293 PRO   A N   1 
ATOM   2231 C CA  . PRO   A 1 293 ? 13.26073 -14.70449 -10.69693 1.000 46.88440  ? 293 PRO   A CA  1 
ATOM   2232 C C   . PRO   A 1 293 ? 12.81979 -16.10909 -11.07603 1.000 52.99961  ? 293 PRO   A C   1 
ATOM   2233 O O   . PRO   A 1 293 ? 11.99377 -16.27083 -11.98161 1.000 54.87171  ? 293 PRO   A O   1 
ATOM   2234 C CB  . PRO   A 1 293 ? 14.66223 -14.37635 -11.22034 1.000 50.14743  ? 293 PRO   A CB  1 
ATOM   2235 C CG  . PRO   A 1 293 ? 15.20704 -13.41491 -10.22128 1.000 47.38020  ? 293 PRO   A CG  1 
ATOM   2236 C CD  . PRO   A 1 293 ? 14.67513 -13.85822 -8.89476  1.000 48.40645  ? 293 PRO   A CD  1 
ATOM   2237 N N   . PHE   A 1 294 ? 13.32854 -17.13206 -10.38313 1.000 55.22925  ? 294 PHE   A N   1 
ATOM   2238 C CA  . PHE   A 1 294 ? 12.86682 -18.49596 -10.62698 1.000 57.54716  ? 294 PHE   A CA  1 
ATOM   2239 C C   . PHE   A 1 294 ? 11.37085 -18.62688 -10.35095 1.000 60.11365  ? 294 PHE   A C   1 
ATOM   2240 O O   . PHE   A 1 294 ? 10.63132 -19.17374 -11.17639 1.000 62.89850  ? 294 PHE   A O   1 
ATOM   2241 C CB  . PHE   A 1 294 ? 13.67361 -19.47614 -9.77034  1.000 59.28126  ? 294 PHE   A CB  1 
ATOM   2242 C CG  . PHE   A 1 294 ? 13.64700 -20.90594 -10.26387 1.000 77.81424  ? 294 PHE   A CG  1 
ATOM   2243 C CD1 . PHE   A 1 294 ? 12.84308 -21.28643 -11.32956 1.000 79.34087  ? 294 PHE   A CD1 1 
ATOM   2244 C CD2 . PHE   A 1 294 ? 14.43873 -21.87268 -9.65441  1.000 82.11726  ? 294 PHE   A CD2 1 
ATOM   2245 C CE1 . PHE   A 1 294 ? 12.82552 -22.60422 -11.77516 1.000 85.27633  ? 294 PHE   A CE1 1 
ATOM   2246 C CE2 . PHE   A 1 294 ? 14.42532 -23.19071 -10.09359 1.000 81.97669  ? 294 PHE   A CE2 1 
ATOM   2247 C CZ  . PHE   A 1 294 ? 13.61957 -23.55591 -11.15670 1.000 81.10011  ? 294 PHE   A CZ  1 
ATOM   2248 N N   . ASP   A 1 295 ? 10.90352 -18.10908 -9.20754  1.000 54.85002  ? 295 ASP   A N   1 
ATOM   2249 C CA  . ASP   A 1 295 ? 9.48743  -18.22483 -8.85542  1.000 56.93154  ? 295 ASP   A CA  1 
ATOM   2250 C C   . ASP   A 1 295 ? 8.58852  -17.62094 -9.92523  1.000 60.98506  ? 295 ASP   A C   1 
ATOM   2251 O O   . ASP   A 1 295 ? 7.52641  -18.17204 -10.23533 1.000 62.11726  ? 295 ASP   A O   1 
ATOM   2252 C CB  . ASP   A 1 295 ? 9.20516  -17.53912 -7.51984  1.000 53.49531  ? 295 ASP   A CB  1 
ATOM   2253 C CG  . ASP   A 1 295 ? 9.88624  -18.21556 -6.35733  1.000 58.00042  ? 295 ASP   A CG  1 
ATOM   2254 O OD1 . ASP   A 1 295 ? 10.14997 -19.43561 -6.43509  1.000 64.28158  ? 295 ASP   A OD1 1 
ATOM   2255 O OD2 . ASP   A 1 295 ? 10.15384 -17.51553 -5.35734  1.000 56.48830  ? 295 ASP   A OD2 1 
ATOM   2256 N N   . VAL   A 1 296 ? 8.98021  -16.47235 -10.48085 1.000 59.27270  ? 296 VAL   A N   1 
ATOM   2257 C CA  . VAL   A 1 296 ? 8.12983  -15.81493 -11.46645 1.000 55.28881  ? 296 VAL   A CA  1 
ATOM   2258 C C   . VAL   A 1 296 ? 8.01641  -16.67177 -12.71888 1.000 60.01793  ? 296 VAL   A C   1 
ATOM   2259 O O   . VAL   A 1 296 ? 6.92412  -16.83790 -13.27365 1.000 66.34374  ? 296 VAL   A O   1 
ATOM   2260 C CB  . VAL   A 1 296 ? 8.66216  -14.40341 -11.78306 1.000 51.68840  ? 296 VAL   A CB  1 
ATOM   2261 C CG1 . VAL   A 1 296 ? 8.01189  -13.85842 -13.04366 1.000 55.40871  ? 296 VAL   A CG1 1 
ATOM   2262 C CG2 . VAL   A 1 296 ? 8.42191  -13.46025 -10.61483 1.000 45.72143  ? 296 VAL   A CG2 1 
ATOM   2263 N N   . VAL   A 1 297 ? 9.13555  -17.25438 -13.16254 1.000 58.61592  ? 297 VAL   A N   1 
ATOM   2264 C CA  . VAL   A 1 297 ? 9.15197  -18.03187 -14.40157 1.000 61.74557  ? 297 VAL   A CA  1 
ATOM   2265 C C   . VAL   A 1 297 ? 8.31030  -19.29304 -14.26305 1.000 66.00766  ? 297 VAL   A C   1 
ATOM   2266 O O   . VAL   A 1 297 ? 7.47078  -19.59690 -15.11917 1.000 66.57567  ? 297 VAL   A O   1 
ATOM   2267 C CB  . VAL   A 1 297 ? 10.59859 -18.37229 -14.80069 1.000 57.82342  ? 297 VAL   A CB  1 
ATOM   2268 C CG1 . VAL   A 1 297 ? 10.61729 -19.11516 -16.11727 1.000 47.09303  ? 297 VAL   A CG1 1 
ATOM   2269 C CG2 . VAL   A 1 297 ? 11.41665 -17.11259 -14.90328 1.000 54.02311  ? 297 VAL   A CG2 1 
ATOM   2270 N N   . ARG   A 1 298 ? 8.54165  -20.05946 -13.19649 1.000 66.42728  ? 298 ARG   A N   1 
ATOM   2271 C CA  . ARG   A 1 298 ? 7.80695  -21.30590 -13.01117 1.000 67.57577  ? 298 ARG   A CA  1 
ATOM   2272 C C   . ARG   A 1 298 ? 6.30933  -21.06969 -12.86500 1.000 68.14235  ? 298 ARG   A C   1 
ATOM   2273 O O   . ARG   A 1 298 ? 5.50923  -21.92281 -13.26516 1.000 71.07025  ? 298 ARG   A O   1 
ATOM   2274 C CB  . ARG   A 1 298 ? 8.36283  -22.06690 -11.80664 1.000 67.65631  ? 298 ARG   A CB  1 
ATOM   2275 C CG  . ARG   A 1 298 ? 7.94470  -21.50225 -10.47275 1.000 70.46835  ? 298 ARG   A CG  1 
ATOM   2276 C CD  . ARG   A 1 298 ? 8.63921  -22.23423 -9.32819  1.000 84.24546  ? 298 ARG   A CD  1 
ATOM   2277 N NE  . ARG   A 1 298 ? 7.86816  -22.22445 -8.08687  1.000 86.31532  ? 298 ARG   A NE  1 
ATOM   2278 C CZ  . ARG   A 1 298 ? 6.60251  -22.60869 -7.96579  1.000 76.79081  ? 298 ARG   A CZ  1 
ATOM   2279 N NH1 . ARG   A 1 298 ? 5.93190  -23.12800 -8.98297  1.000 70.95482  ? 298 ARG   A NH1 1 
ATOM   2280 N NH2 . ARG   A 1 298 ? 5.99692  -22.48222 -6.78689  1.000 63.41388  ? 298 ARG   A NH2 1 
ATOM   2281 N N   . GLN   A 1 299 ? 5.90854  -19.91990 -12.32037 1.000 68.81357  ? 299 GLN   A N   1 
ATOM   2282 C CA  . GLN   A 1 299 ? 4.48584  -19.61036 -12.22147 1.000 68.92322  ? 299 GLN   A CA  1 
ATOM   2283 C C   . GLN   A 1 299 ? 3.90425  -19.24070 -13.58230 1.000 71.72963  ? 299 GLN   A C   1 
ATOM   2284 O O   . GLN   A 1 299 ? 2.76704  -19.60758 -13.89275 1.000 73.61068  ? 299 GLN   A O   1 
ATOM   2285 C CB  . GLN   A 1 299 ? 4.25376  -18.48744 -11.19969 1.000 65.48215  ? 299 GLN   A CB  1 
ATOM   2286 C CG  . GLN   A 1 299 ? 2.88457  -17.81473 -11.28673 1.000 62.18964  ? 299 GLN   A CG  1 
ATOM   2287 C CD  . GLN   A 1 299 ? 2.32904  -17.36842 -9.93931  1.000 56.89259  ? 299 GLN   A CD  1 
ATOM   2288 O OE1 . GLN   A 1 299 ? 1.15480  -17.02320 -9.83514  1.000 53.91595  ? 299 GLN   A OE1 1 
ATOM   2289 N NE2 . GLN   A 1 299 ? 3.16810  -17.37111 -8.90801  1.000 58.03549  ? 299 GLN   A NE2 1 
ATOM   2290 N N   . CYS   A 1 300 ? 4.66817  -18.54034 -14.41590 1.000 74.43934  ? 300 CYS   A N   1 
ATOM   2291 C CA  . CYS   A 1 300 ? 4.23345  -18.20471 -15.76582 1.000 74.07772  ? 300 CYS   A CA  1 
ATOM   2292 C C   . CYS   A 1 300 ? 4.54899  -19.30716 -16.78065 1.000 78.36905  ? 300 CYS   A C   1 
ATOM   2293 O O   . CYS   A 1 300 ? 4.39559  -19.08625 -17.98829 1.000 74.44549  ? 300 CYS   A O   1 
ATOM   2294 C CB  . CYS   A 1 300 ? 4.86492  -16.87687 -16.19975 1.000 73.55315  ? 300 CYS   A CB  1 
ATOM   2295 S SG  . CYS   A 1 300 ? 4.52327  -15.48647 -15.06767 1.000 75.12148  ? 300 CYS   A SG  1 
ATOM   2296 N N   . SER   A 1 301 ? 4.97676  -20.48791 -16.31359 1.000 76.27337  ? 301 SER   A N   1 
ATOM   2297 C CA  . SER   A 1 301 ? 5.26318  -21.62577 -17.18014 1.000 69.11762  ? 301 SER   A CA  1 
ATOM   2298 C C   . SER   A 1 301 ? 4.52408  -22.90013 -16.79841 1.000 77.16565  ? 301 SER   A C   1 
ATOM   2299 O O   . SER   A 1 301 ? 4.59799  -23.87561 -17.55508 1.000 83.80847  ? 301 SER   A O   1 
ATOM   2300 C CB  . SER   A 1 301 ? 6.76836  -21.93380 -17.19236 1.000 69.27127  ? 301 SER   A CB  1 
ATOM   2301 O OG  . SER   A 1 301 ? 7.46315  -21.05715 -18.05786 1.000 81.27165  ? 301 SER   A OG  1 
ATOM   2302 N N   . GLY   A 1 302 ? 3.83230  -22.93323 -15.66254 1.000 71.64802  ? 302 GLY   A N   1 
ATOM   2303 C CA  . GLY   A 1 302 ? 3.13154  -24.13360 -15.23606 1.000 66.24678  ? 302 GLY   A CA  1 
ATOM   2304 C C   . GLY   A 1 302 ? 4.04159  -25.28751 -14.86929 1.000 73.45518  ? 302 GLY   A C   1 
ATOM   2305 O O   . GLY   A 1 302 ? 3.75498  -26.43793 -15.22767 1.000 69.21024  ? 302 GLY   A O   1 
ATOM   2306 N N   . VAL   A 1 303 ? 5.13508  -25.00935 -14.15934 1.000 72.62315  ? 303 VAL   A N   1 
ATOM   2307 C CA  . VAL   A 1 303 ? 6.09270  -26.05174 -13.80788 1.000 77.08557  ? 303 VAL   A CA  1 
ATOM   2308 C C   . VAL   A 1 303 ? 5.47839  -26.97395 -12.76299 1.000 79.45635  ? 303 VAL   A C   1 
ATOM   2309 O O   . VAL   A 1 303 ? 4.97066  -26.51709 -11.73019 1.000 80.88140  ? 303 VAL   A O   1 
ATOM   2310 C CB  . VAL   A 1 303 ? 7.40352  -25.42550 -13.30698 1.000 74.09723  ? 303 VAL   A CB  1 
ATOM   2311 C CG1 . VAL   A 1 303 ? 8.17712  -26.41542 -12.44858 1.000 71.41031  ? 303 VAL   A CG1 1 
ATOM   2312 C CG2 . VAL   A 1 303 ? 8.24757  -24.94767 -14.48646 1.000 73.92844  ? 303 VAL   A CG2 1 
ATOM   2313 N N   . THR   A 1 304 ? 5.51650  -28.27823 -13.02635 1.000 76.08633  ? 304 THR   A N   1 
ATOM   2314 C CA  . THR   A 1 304 ? 4.92344  -29.24989 -12.10975 1.000 72.37241  ? 304 THR   A CA  1 
ATOM   2315 C C   . THR   A 1 304 ? 5.97811  -30.18874 -11.52852 1.000 74.03993  ? 304 THR   A C   1 
ATOM   2316 O O   . THR   A 1 304 ? 5.72468  -30.89960 -10.55431 1.000 75.47645  ? 304 THR   A O   1 
ATOM   2317 C CB  . THR   A 1 304 ? 3.82540  -30.08791 -12.80261 1.000 65.63761  ? 304 THR   A CB  1 
ATOM   2318 O OG1 . THR   A 1 304 ? 4.33743  -30.65989 -14.01441 1.000 67.74369  ? 304 THR   A OG1 1 
ATOM   2319 C CG2 . THR   A 1 304 ? 2.62637  -29.21170 -13.13719 1.000 61.44484  ? 304 THR   A CG2 1 
HETATM 2320 C C13 . A1ALH B 2 .   ? 8.22826  -20.15958 18.85915  1.000 60.89320  ? 401 A1ALH A C13 1 
HETATM 2321 C C17 . A1ALH B 2 .   ? 7.39197  -19.88745 20.13537  1.000 60.39458  ? 401 A1ALH A C17 1 
HETATM 2322 C C22 . A1ALH B 2 .   ? 11.64862 -17.16389 21.92708  1.000 58.56080  ? 401 A1ALH A C22 1 
HETATM 2323 C C24 . A1ALH B 2 .   ? 10.79698 -14.90161 22.45637  1.000 60.12781  ? 401 A1ALH A C24 1 
HETATM 2324 C C26 . A1ALH B 2 .   ? 12.07674 -12.94821 23.63629  1.000 58.26962  ? 401 A1ALH A C26 1 
HETATM 2325 C C28 . A1ALH B 2 .   ? 11.46978 -10.49410 23.52536  1.000 60.83432  ? 401 A1ALH A C28 1 
HETATM 2326 C C02 . A1ALH B 2 .   ? 11.51487 -18.57168 21.33246  1.000 58.44280  ? 401 A1ALH A C02 1 
HETATM 2327 C C04 . A1ALH B 2 .   ? 12.12520 -21.10538 21.39677  1.000 56.05907  ? 401 A1ALH A C04 1 
HETATM 2328 C C05 . A1ALH B 2 .   ? 12.69927 -22.07922 22.49405  1.000 55.76580  ? 401 A1ALH A C05 1 
HETATM 2329 C C06 . A1ALH B 2 .   ? 14.24225 -22.25780 22.43875  1.000 62.03727  ? 401 A1ALH A C06 1 
HETATM 2330 C C07 . A1ALH B 2 .   ? 14.80539 -23.09638 23.60120  1.000 64.00277  ? 401 A1ALH A C07 1 
HETATM 2331 C C08 . A1ALH B 2 .   ? 14.71902 -22.84395 21.10325  1.000 62.27156  ? 401 A1ALH A C08 1 
HETATM 2332 C C09 . A1ALH B 2 .   ? 10.64284 -21.49276 21.07042  1.000 54.24739  ? 401 A1ALH A C09 1 
HETATM 2333 C C11 . A1ALH B 2 .   ? 8.90336  -22.60032 19.53922  1.000 55.70730  ? 401 A1ALH A C11 1 
HETATM 2334 C C12 . A1ALH B 2 .   ? 8.24470  -21.65269 18.48621  1.000 56.11127  ? 401 A1ALH A C12 1 
HETATM 2335 C C14 . A1ALH B 2 .   ? 7.50217  -19.33963 17.77977  1.000 60.49423  ? 401 A1ALH A C14 1 
HETATM 2336 C C16 . A1ALH B 2 .   ? 6.04711  -19.28971 19.68304  1.000 62.83518  ? 401 A1ALH A C16 1 
HETATM 2337 C C19 . A1ALH B 2 .   ? 8.81859  -24.06443 19.05193  1.000 53.11771  ? 401 A1ALH A C19 1 
HETATM 2338 C C23 . A1ALH B 2 .   ? 10.63913 -16.19782 21.91997  1.000 58.71470  ? 401 A1ALH A C23 1 
HETATM 2339 C C25 . A1ALH B 2 .   ? 11.96457 -14.39786 23.07096  1.000 61.80304  ? 401 A1ALH A C25 1 
HETATM 2340 C C27 . A1ALH B 2 .   ? 11.40298 -11.83213 23.06713  1.000 59.19142  ? 401 A1ALH A C27 1 
HETATM 2341 C C29 . A1ALH B 2 .   ? 12.27242 -10.16805 24.64483  1.000 57.93768  ? 401 A1ALH A C29 1 
HETATM 2342 C C31 . A1ALH B 2 .   ? 13.27022 -7.99606  24.50024  1.000 67.27146  ? 401 A1ALH A C31 1 
HETATM 2343 C C32 . A1ALH B 2 .   ? 12.96056 -11.24431 25.22699  1.000 60.16270  ? 401 A1ALH A C32 1 
HETATM 2344 C C33 . A1ALH B 2 .   ? 12.86964 -12.57001 24.74325  1.000 56.50287  ? 401 A1ALH A C33 1 
HETATM 2345 C C35 . A1ALH B 2 .   ? 9.55985  -9.83890  22.21035  1.000 61.39417  ? 401 A1ALH A C35 1 
HETATM 2346 C C36 . A1ALH B 2 .   ? 12.97605 -15.39025 23.06112  1.000 60.32186  ? 401 A1ALH A C36 1 
HETATM 2347 C C37 . A1ALH B 2 .   ? 12.83019 -16.69435 22.52480  1.000 58.09672  ? 401 A1ALH A C37 1 
HETATM 2348 N N03 . A1ALH B 2 .   ? 12.16952 -19.70051 21.90664  1.000 62.39392  ? 401 A1ALH A N03 1 
HETATM 2349 N N10 . A1ALH B 2 .   ? 10.31441 -22.21162 19.88839  1.000 54.26307  ? 401 A1ALH A N10 1 
HETATM 2350 N N15 . A1ALH B 2 .   ? 6.28998  -18.88060 18.30029  1.000 63.60644  ? 401 A1ALH A N15 1 
HETATM 2351 N N20 . A1ALH B 2 .   ? 7.95115  -24.92332 19.32163  1.000 56.02135  ? 401 A1ALH A N20 1 
HETATM 2352 O O01 . A1ALH B 2 .   ? 10.86672 -18.72973 20.31792  1.000 53.78364  ? 401 A1ALH A O01 1 
HETATM 2353 O O18 . A1ALH B 2 .   ? 7.87552  -19.10690 16.64637  1.000 54.44770  ? 401 A1ALH A O18 1 
HETATM 2354 O O21 . A1ALH B 2 .   ? 9.76077  -21.16054 21.82551  1.000 62.06749  ? 401 A1ALH A O21 1 
HETATM 2355 O O30 . A1ALH B 2 .   ? 12.38515 -8.89687  25.14571  1.000 60.99117  ? 401 A1ALH A O30 1 
HETATM 2356 O O34 . A1ALH B 2 .   ? 10.76026 -9.48312  22.89724  1.000 61.82252  ? 401 A1ALH A O34 1 
HETATM 2357 O O   . HOH   C 3 .   ? 4.12555  -23.96696 -9.94130  1.000 79.30031  ? 501 HOH   A O   1 
HETATM 2358 O O   . HOH   C 3 .   ? 4.62697  -24.17479 -6.26444  1.000 58.49606  ? 502 HOH   A O   1 
HETATM 2359 O O   . HOH   C 3 .   ? 16.93650 -6.44391  15.53099  1.000 68.62963  ? 503 HOH   A O   1 
HETATM 2360 O O   . HOH   C 3 .   ? 10.32763 -0.69810  -1.22732  1.000 51.69909  ? 504 HOH   A O   1 
HETATM 2361 O O   . HOH   C 3 .   ? 18.64430 -28.15896 4.79009   1.000 52.46599  ? 505 HOH   A O   1 
HETATM 2362 O O   . HOH   C 3 .   ? 0.23766  -21.78789 12.23605  1.000 56.19239  ? 506 HOH   A O   1 
HETATM 2363 O O   . HOH   C 3 .   ? 6.38267  -29.14928 -8.49920  1.000 61.67259  ? 507 HOH   A O   1 
HETATM 2364 O O   . HOH   C 3 .   ? 28.72871 -6.95626  -10.72557 1.000 65.59236  ? 508 HOH   A O   1 
HETATM 2365 O O   . HOH   C 3 .   ? 17.34014 1.12099   -23.59813 1.000 71.61291  ? 509 HOH   A O   1 
HETATM 2366 O O   . HOH   C 3 .   ? 8.73515  -19.05664 23.56755  1.000 64.21549  ? 510 HOH   A O   1 
HETATM 2367 O O   . HOH   C 3 .   ? -3.08097 -10.92776 -9.09186  1.000 54.58730  ? 511 HOH   A O   1 
HETATM 2368 O O   . HOH   C 3 .   ? 28.18219 -29.75945 11.24952  1.000 60.36844  ? 512 HOH   A O   1 
HETATM 2369 O O   . HOH   C 3 .   ? 25.10705 -18.67412 6.48432   1.000 51.64425  ? 513 HOH   A O   1 
HETATM 2370 O O   . HOH   C 3 .   ? 21.43684 -41.40200 15.05234  1.000 69.69474  ? 514 HOH   A O   1 
HETATM 2371 O O   . HOH   C 3 .   ? 8.65542  -6.54869  20.65609  1.000 57.07700  ? 515 HOH   A O   1 
HETATM 2372 O O   . HOH   C 3 .   ? 23.90196 -19.05997 4.10643   1.000 51.54339  ? 516 HOH   A O   1 
HETATM 2373 O O   . HOH   C 3 .   ? 28.50347 -11.09987 -8.19218  1.000 77.94436  ? 517 HOH   A O   1 
HETATM 2374 O O   . HOH   C 3 .   ? 9.60218  -41.38336 29.27604  1.000 70.55454  ? 518 HOH   A O   1 
HETATM 2375 O O   . HOH   C 3 .   ? 20.30201 -10.87925 -2.70905  1.000 59.74895  ? 519 HOH   A O   1 
HETATM 2376 O O   . HOH   C 3 .   ? 27.08247 -23.36390 7.81966   1.000 51.15200  ? 520 HOH   A O   1 
HETATM 2377 O O   . HOH   C 3 .   ? 23.06881 -43.26163 16.29284  1.000 75.13733  ? 521 HOH   A O   1 
HETATM 2378 O O   . HOH   C 3 .   ? 24.78527 -22.10635 22.28538  1.000 57.92248  ? 522 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.84106 1.11202 0.68088 -0.08400 -0.14468 0.16365  1   SER   A N   
2    C CA  . SER   A 1   ? 0.86836 1.11072 0.69231 -0.06860 -0.12513 0.16091  1   SER   A CA  
3    C C   . SER   A 1   ? 0.81014 1.04629 0.68115 -0.04320 -0.11071 0.17474  1   SER   A C   
4    O O   . SER   A 1   ? 0.86312 1.10989 0.74873 -0.03024 -0.11143 0.19952  1   SER   A O   
5    C CB  . SER   A 1   ? 0.96825 1.22660 0.75941 -0.07360 -0.13467 0.17791  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.97532 1.22750 0.71054 -0.09552 -0.14163 0.15770  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.76491 0.98212 0.65785 -0.03673 -0.09793 0.15873  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.71826 0.92278 0.64778 -0.01434 -0.08243 0.16515  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.70366 0.86716 0.61829 -0.00918 -0.06231 0.14297  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.78009 0.92668 0.65883 -0.01998 -0.05877 0.12529  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.63449 0.78288 0.57722 0.00791  -0.04894 0.14434  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.67703 0.79062 0.61085 0.01245  -0.03178 0.12612  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.63744 0.74246 0.60102 0.02394  -0.02207 0.12116  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.68828 0.79479 0.67695 0.03901  -0.01870 0.13449  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.70510 0.80211 0.62931 0.01966  -0.02446 0.13463  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.69559 0.76507 0.60245 0.01777  -0.01062 0.11674  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.70704 0.77391 0.58110 0.00660  -0.00908 0.10506  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.66393 0.71124 0.58721 0.02732  0.00100  0.11141  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.71886 0.76487 0.58242 0.00706  0.00465  0.09113  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.69594 0.72357 0.60730 0.02487  0.01185  0.09796  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.73414 0.76285 0.61842 0.01570  0.01411  0.08903  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.63773 0.73164 0.59664 0.01750  -0.01655 0.10207  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.64979 0.73650 0.63098 0.02619  -0.00676 0.09622  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.67639 0.73548 0.64222 0.02289  0.00397  0.07710  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.71405 0.76276 0.65560 0.01369  0.00383  0.06739  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.61662 0.73001 0.61780 0.02078  -0.01379 0.09927  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.68775 0.80566 0.71842 0.03518  -0.00369 0.10309  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.62082 0.77422 0.67726 0.03077  -0.01060 0.11238  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.77396 0.94399 0.86273 0.05031  -0.00313 0.12669  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.88929 1.09733 1.00615 0.05450  -0.01148 0.14701  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.82575 1.06147 0.94145 0.03731  -0.03022 0.15564  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.88765 1.10657 1.03432 0.07653  -0.00075 0.15898  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.67182 0.72004 0.65166 0.03140  0.01393  0.07237  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.68344 0.71036 0.65310 0.02842  0.02252  0.05743  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.66041 0.69256 0.62689 0.01656  0.01904  0.04865  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.60087 0.64626 0.58417 0.01571  0.01826  0.05085  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.64123 0.65692 0.62306 0.03909  0.03226  0.05565  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.64469 0.63685 0.61457 0.03836  0.03938  0.04633  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.85670 0.83578 0.83313 0.04792  0.04647  0.04551  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.98729 0.96105 0.96935 0.05715  0.04582  0.05542  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 1.05872 1.02878 1.05316 0.07005  0.05244  0.05611  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.68923 0.71017 0.63443 0.00755  0.01785  0.03919  6   MET   A N   
43   C CA  . MET   A 6   ? 0.59361 0.61152 0.53168 -0.00481 0.01404  0.02937  6   MET   A CA  
44   C C   . MET   A 6   ? 0.61132 0.60823 0.54859 -0.00313 0.02403  0.01945  6   MET   A C   
45   O O   . MET   A 6   ? 0.62437 0.60962 0.55922 0.00487  0.03237  0.01830  6   MET   A O   
46   C CB  . MET   A 6   ? 0.63762 0.65214 0.54880 -0.01481 0.00761  0.02318  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.65718 0.67470 0.56078 -0.03134 -0.00324 0.01649  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.76032 0.79351 0.63844 -0.04325 -0.01840 0.01933  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.83120 0.83953 0.67322 -0.03858 -0.00645 0.00676  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.62714 0.62075 0.56850 -0.01174 0.02205  0.01444  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.58928 0.56312 0.53033 -0.01101 0.02999  0.00729  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.64172 0.59824 0.56800 -0.02240 0.02682  -0.00385 7   ALA   A C   
53   O O   . ALA   A 7   ? 0.63106 0.59437 0.55271 -0.03469 0.01639  -0.00518 7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.59419 0.57613 0.55574 -0.00939 0.03272  0.01373  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.65693 0.59042 0.57595 -0.01829 0.03561  -0.01165 8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.68295 0.59173 0.58716 -0.02635 0.03553  -0.02419 8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.65360 0.56067 0.57014 -0.03949 0.02796  -0.02226 8   PHE   A C   
58   O O   . PHE   A 8   ? 0.62418 0.54440 0.56255 -0.03776 0.02880  -0.01125 8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.70223 0.58894 0.60488 -0.01570 0.04832  -0.02910 8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.70656 0.59179 0.59419 -0.00594 0.05671  -0.03321 8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.78911 0.66196 0.64927 -0.00955 0.05781  -0.04598 8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.71024 0.60660 0.60987 0.00557  0.06372  -0.02420 8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.79763 0.67232 0.64385 -0.00012 0.06781  -0.04817 8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.76521 0.66352 0.65441 0.01328  0.07201  -0.02538 8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.73554 0.62439 0.59870 0.01128  0.07510  -0.03666 8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.69281 0.58351 0.59428 -0.05398 0.02061  -0.03275 9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.69739 0.58128 0.61173 -0.06873 0.01379  -0.03046 9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.69224 0.55746 0.62056 -0.06097 0.02413  -0.02682 9   PRO   A C   
69   O O   . PRO   A 9   ? 0.70718 0.54809 0.62627 -0.04972 0.03458  -0.03421 9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.72355 0.58083 0.61092 -0.08482 0.00585  -0.04733 9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.71389 0.58226 0.57705 -0.08142 0.00386  -0.05330 9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.70473 0.58158 0.57423 -0.05937 0.01780  -0.04731 9   PRO   A CD  
73   N N   . SER   A 10  ? 0.67499 0.55539 0.62706 -0.06630 0.02164  -0.01314 10  SER   A N   
74   C CA  . SER   A 10  ? 0.66976 0.54136 0.63662 -0.05896 0.03015  -0.00447 10  SER   A CA  
75   C C   . SER   A 10  ? 0.69723 0.53596 0.66608 -0.07026 0.02868  -0.00667 10  SER   A C   
76   O O   . SER   A 10  ? 0.71802 0.54544 0.69810 -0.06366 0.03555  0.00164  10  SER   A O   
77   C CB  . SER   A 10  ? 0.65205 0.55856 0.64049 -0.05741 0.03051  0.01253  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.60768 0.53530 0.60712 -0.07260 0.02098  0.01853  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.68533 0.50704 0.64274 -0.08789 0.01901  -0.01706 11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.69673 0.48456 0.65760 -0.10227 0.01579  -0.01825 11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.79744 0.54513 0.75532 -0.08853 0.02792  -0.02242 11  GLY   A C   
82   O O   . GLY   A 11  ? 0.82294 0.55608 0.79761 -0.09136 0.02971  -0.01080 11  GLY   A O   
83   N N   . LYS   A 12  ? 0.79761 0.52939 0.73629 -0.07271 0.03703  -0.03665 12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.76758 0.46304 0.70631 -0.05732 0.04984  -0.04005 12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.81434 0.52951 0.77900 -0.04268 0.05670  -0.01883 12  LYS   A C   
86   O O   . LYS   A 12  ? 0.82516 0.51423 0.79889 -0.03202 0.06492  -0.01437 12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.84763 0.52943 0.76171 -0.04276 0.05985  -0.05843 12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.95884 0.58815 0.86235 -0.03360 0.07144  -0.07211 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 1.09157 0.67694 0.97649 -0.05491 0.06293  -0.08833 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 1.19571 0.73424 1.09494 -0.05133 0.06926  -0.08449 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 1.11299 0.59772 0.99240 -0.07215 0.06205  -0.10244 12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.79794 0.55735 0.77387 -0.04203 0.05328  -0.00544 13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.78213 0.56215 0.77601 -0.02982 0.05846  0.01268  13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.71992 0.51158 0.73153 -0.04133 0.05347  0.03104  13  VAL   A C   
95   O O   . VAL   A 13  ? 0.71951 0.50964 0.74443 -0.03513 0.05715  0.04645  13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.70726 0.52335 0.69793 -0.02042 0.05976  0.01393  13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.69404 0.52857 0.69844 -0.01039 0.06340  0.03047  13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.67724 0.48421 0.65158 -0.01035 0.06532  -0.00118 13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.70802 0.51497 0.72114 -0.05824 0.04510  0.03175  14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.75241 0.57285 0.78348 -0.07056 0.04175  0.05041  14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.74547 0.52786 0.78505 -0.07555 0.04259  0.05761  14  GLU   A C   
102  O O   . GLU   A 14  ? 0.80708 0.59879 0.86192 -0.07742 0.04398  0.07815  14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.69841 0.53974 0.73357 -0.08939 0.03245  0.05029  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.69114 0.56206 0.71759 -0.08463 0.03031  0.04131  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.72031 0.60917 0.75207 -0.10356 0.01908  0.04091  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.75270 0.64636 0.80091 -0.12048 0.01414  0.05292  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.69200 0.59281 0.71312 -0.10235 0.01446  0.03081  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.77796 0.51561 0.80636 -0.07687 0.04261  0.04128  15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.79359 0.48668 0.82969 -0.07901 0.04473  0.04642  15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.79955 0.48604 0.84639 -0.05771 0.05453  0.05931  15  GLY   A C   
111  O O   . GLY   A 15  ? 0.88707 0.53371 0.94218 -0.05523 0.05774  0.06459  15  GLY   A O   
112  N N   . CYS   A 16  ? 0.73261 0.45633 0.78048 -0.04284 0.05854  0.06537  16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.72879 0.45614 0.78899 -0.02506 0.06491  0.08114  16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.71510 0.48654 0.78355 -0.02636 0.06216  0.10277  16  CYS   A C   
115  O O   . CYS   A 16  ? 0.73784 0.51889 0.81533 -0.01428 0.06467  0.11832  16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.80764 0.53603 0.85994 -0.00536 0.07251  0.06811  16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.88662 0.57153 0.91875 -0.00251 0.07825  0.03766  16  CYS   A SG  
118  N N   . MET   A 17  ? 0.71915 0.51904 0.78413 -0.04014 0.05741  0.10445  17  MET   A N   
119  C CA  . MET   A 17  ? 0.69492 0.53534 0.76197 -0.04037 0.05717  0.12150  17  MET   A CA  
120  C C   . MET   A 17  ? 0.69112 0.53096 0.77188 -0.05040 0.05582  0.14608  17  MET   A C   
121  O O   . MET   A 17  ? 0.68241 0.50864 0.77084 -0.06616 0.05281  0.14899  17  MET   A O   
122  C CB  . MET   A 17  ? 0.69397 0.56680 0.75216 -0.04665 0.05582  0.11272  17  MET   A CB  
123  C CG  . MET   A 17  ? 0.67729 0.55206 0.72224 -0.03678 0.05673  0.09206  17  MET   A CG  
124  S SD  . MET   A 17  ? 0.65434 0.53166 0.69543 -0.01787 0.06058  0.09345  17  MET   A SD  
125  C CE  . MET   A 17  ? 0.62223 0.53473 0.66186 -0.01900 0.06011  0.11273  17  MET   A CE  
126  N N   . VAL   A 18  ? 0.70099 0.55646 0.78466 -0.04269 0.05702  0.16515  18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.70602 0.56766 0.80028 -0.05097 0.05598  0.19270  18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.68096 0.58753 0.76329 -0.04963 0.05700  0.20438  18  VAL   A C   
129  O O   . VAL   A 18  ? 0.71996 0.64553 0.78765 -0.04103 0.05782  0.19142  18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.70834 0.53914 0.81766 -0.04257 0.05567  0.20883  18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.72792 0.50756 0.84482 -0.04296 0.05668  0.19415  18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.69598 0.54041 0.80250 -0.02434 0.05616  0.21063  18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.71404 0.63546 0.80088 -0.05915 0.05717  0.22909  19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.72302 0.68446 0.79418 -0.05894 0.05898  0.24208  19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.72209 0.68237 0.79659 -0.05312 0.05467  0.26612  19  GLN   A C   
136  O O   . GLN   A 19  ? 0.78093 0.72030 0.87389 -0.05697 0.05273  0.28673  19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.75086 0.73681 0.82287 -0.07368 0.06369  0.25518  19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.74549 0.77305 0.79518 -0.07301 0.06881  0.26360  19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.76297 0.81322 0.81810 -0.08692 0.07439  0.28779  19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.83303 0.86813 0.90637 -0.09599 0.07114  0.31072  19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.74828 0.83429 0.78913 -0.08822 0.08397  0.28356  19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.64078 0.62249 0.69860 -0.04460 0.05211  0.26445  20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.66789 0.65724 0.72799 -0.03959 0.04563  0.28867  20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.73326 0.76209 0.76671 -0.04680 0.04505  0.30140  20  VAL   A C   
145  O O   . VAL   A 20  ? 0.83157 0.87976 0.83999 -0.04701 0.04783  0.28234  20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.70493 0.68820 0.76894 -0.02540 0.04092  0.27820  20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.66624 0.65723 0.74211 -0.01977 0.03303  0.30793  20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.69125 0.63775 0.77300 -0.01758 0.04501  0.25813  20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.74079 0.77954 0.77772 -0.05249 0.04201  0.33352  21  THR   A N   
150  C CA  . THR   A 21  ? 0.75135 0.82744 0.75960 -0.06087 0.04250  0.34845  21  THR   A CA  
151  C C   . THR   A 21  ? 0.80404 0.89261 0.81182 -0.05901 0.03105  0.37787  21  THR   A C   
152  O O   . THR   A 21  ? 0.82148 0.89168 0.85825 -0.05602 0.02668  0.40204  21  THR   A O   
153  C CB  . THR   A 21  ? 0.79112 0.87577 0.80217 -0.07354 0.05143  0.36369  21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.74785 0.82770 0.76136 -0.07549 0.06069  0.33784  21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.73035 0.85520 0.70910 -0.08139 0.05410  0.38154  21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.80940 0.92780 0.78436 -0.06089 0.02554  0.37594  22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.78404 0.92321 0.75338 -0.06215 0.01227  0.40554  22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.73464 0.90993 0.65670 -0.07390 0.01295  0.40962  22  CYS   A C   
159  O O   . CYS   A 22  ? 0.76327 0.94805 0.65242 -0.07525 0.01524  0.38160  22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.72812 0.86567 0.70674 -0.05250 0.00050  0.39737  22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.90648 1.07474 0.88555 -0.05405 -0.01906 0.43698  22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.81022 1.00162 0.72872 -0.08132 0.01188  0.43889  23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.82683 1.04924 0.69989 -0.09107 0.01564  0.43594  23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.85897 1.08316 0.71504 -0.09385 0.03543  0.41566  23  GLY   A C   
165  O O   . GLY   A 23  ? 0.92490 1.13793 0.80774 -0.09502 0.04589  0.42076  23  GLY   A O   
166  N N   . THR   A 24  ? 0.84935 1.08743 0.66184 -0.09499 0.04052  0.39159  24  THR   A N   
167  C CA  . THR   A 24  ? 0.83234 1.07214 0.63068 -0.09303 0.06001  0.36492  24  THR   A CA  
168  C C   . THR   A 24  ? 0.89511 1.10754 0.71127 -0.08271 0.06213  0.32921  24  THR   A C   
169  O O   . THR   A 24  ? 0.93664 1.14251 0.76966 -0.07944 0.07562  0.31641  24  THR   A O   
170  C CB  . THR   A 24  ? 0.92693 1.19298 0.66533 -0.09762 0.06698  0.35413  24  THR   A CB  
171  O OG1 . THR   A 24  ? 1.04101 1.32586 0.77277 -0.10332 0.07211  0.37271  24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.96379 1.22480 0.68620 -0.08993 0.08507  0.31708  24  THR   A CG2 
173  N N   . THR   A 25  ? 0.82473 1.02409 0.63901 -0.07846 0.04841  0.31532  25  THR   A N   
174  C CA  . THR   A 25  ? 0.78601 0.95982 0.61848 -0.06917 0.04932  0.28521  25  THR   A CA  
175  C C   . THR   A 25  ? 0.76193 0.91339 0.64303 -0.06467 0.05160  0.29121  25  THR   A C   
176  O O   . THR   A 25  ? 0.77118 0.91572 0.67881 -0.06556 0.04406  0.31664  25  THR   A O   
177  C CB  . THR   A 25  ? 0.82178 0.98920 0.64945 -0.06740 0.03288  0.27704  25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.89643 1.08507 0.67849 -0.07615 0.02575  0.27883  25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.78407 0.93014 0.61683 -0.05958 0.03599  0.24304  25  THR   A CG2 
180  N N   . THR   A 26  ? 0.76555 0.90410 0.65728 -0.05983 0.06163  0.26751  26  THR   A N   
181  C CA  . THR   A 26  ? 0.79336 0.90765 0.72495 -0.05713 0.06261  0.26662  26  THR   A CA  
182  C C   . THR   A 26  ? 0.76651 0.86339 0.70208 -0.04882 0.06383  0.23488  26  THR   A C   
183  O O   . THR   A 26  ? 0.84493 0.95054 0.75881 -0.04623 0.07088  0.21464  26  THR   A O   
184  C CB  . THR   A 26  ? 0.84617 0.96845 0.79132 -0.06460 0.07353  0.27848  26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.83998 0.93704 0.81716 -0.06378 0.07380  0.26916  26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.99937 1.14819 0.91836 -0.06496 0.08752  0.26655  26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.73891 0.81028 0.70117 -0.04378 0.05789  0.23110  27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.71596 0.77151 0.68184 -0.03635 0.05840  0.20380  27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.70230 0.73054 0.69869 -0.03447 0.05803  0.20185  27  LEU   A C   
190  O O   . LEU   A 27  ? 0.73497 0.75478 0.74873 -0.04017 0.05857  0.21877  27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.70962 0.76571 0.66304 -0.03117 0.04991  0.19576  27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.72740 0.78875 0.68685 -0.03107 0.03883  0.21769  27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.68614 0.72521 0.68069 -0.02388 0.03652  0.22646  27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.72532 0.79707 0.66506 -0.03083 0.03041  0.20793  27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.69094 0.70355 0.69152 -0.02740 0.05719  0.18079  28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.64745 0.63254 0.66896 -0.02550 0.05763  0.17296  28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.65498 0.62129 0.69029 -0.01653 0.05328  0.17754  28  ASN   A C   
198  O O   . ASN   A 28  ? 0.66191 0.63946 0.69175 -0.01068 0.04906  0.17981  28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.62742 0.60925 0.64364 -0.02312 0.06060  0.14795  28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.66979 0.67243 0.67760 -0.02879 0.06628  0.14432  28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.67235 0.67755 0.69180 -0.03738 0.06862  0.15244  28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.64006 0.65726 0.62934 -0.02389 0.06899  0.13254  28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.67067 0.60812 0.72448 -0.01564 0.05461  0.17874  29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.64489 0.56154 0.71438 -0.00401 0.05400  0.18226  29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.67594 0.55974 0.75126 -0.00040 0.05854  0.16233  29  GLY   A C   
206  O O   . GLY   A 29  ? 0.68998 0.56200 0.76198 -0.01031 0.05959  0.15199  29  GLY   A O   
207  N N   . LEU   A 30  ? 0.70553 0.57681 0.78916 0.01351  0.06122  0.15754  30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.69554 0.53514 0.77988 0.01925  0.06729  0.13717  30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.78731 0.59194 0.89055 0.02809  0.07170  0.14719  30  LEU   A C   
210  O O   . LEU   A 30  ? 0.76985 0.57905 0.88924 0.04237  0.07360  0.16167  30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.68830 0.54035 0.76633 0.02954  0.07016  0.12280  30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.75186 0.57657 0.82565 0.03695  0.07800  0.10139  30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.74280 0.56976 0.79630 0.02571  0.07585  0.08130  30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.67725 0.51523 0.75781 0.05236  0.08315  0.10095  30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.80748 0.57694 0.90994 0.01927  0.07292  0.14015  31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.78636 0.51389 0.90520 0.02464  0.07682  0.14952  31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.78622 0.47346 0.89840 0.03457  0.08599  0.12408  31  TRP   A C   
218  O O   . TRP   A 31  ? 0.79340 0.45668 0.88915 0.02216  0.08511  0.10310  31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.78724 0.49976 0.90832 0.00487  0.07121  0.15952  31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.86411 0.52733 1.00153 0.00712  0.07408  0.16987  31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.87165 0.51117 1.02702 0.02786  0.08103  0.18013  31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.91812 0.54797 1.05741 -0.01222 0.07018  0.17183  31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.87649 0.46524 1.04334 0.02396  0.08242  0.18743  31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.88802 0.46909 1.04448 -0.00220 0.07506  0.18229  31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.88492 0.52275 1.01563 -0.03730 0.06292  0.16735  31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 1.02671 0.56205 1.18932 -0.01832 0.07212  0.18704  31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.94433 0.54270 1.08306 -0.05447 0.05931  0.17332  31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 1.00985 0.55504 1.16306 -0.04591 0.06350  0.18244  31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.83364 0.51558 0.95812 0.05674  0.09493  0.12656  32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.89271 0.53660 1.01052 0.07025  0.10735  0.10371  32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.94403 0.55236 1.08626 0.08886  0.11647  0.11801  32  LEU   A C   
232  O O   . LEU   A 32  ? 0.96173 0.59525 1.12955 0.10203  0.11616  0.14477  32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.83046 0.50488 0.94164 0.08288  0.11345  0.09232  32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.78188 0.48803 0.86999 0.06738  0.10560  0.07836  32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.78271 0.51854 0.86921 0.08008  0.11143  0.07297  32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.80783 0.48325 0.87086 0.05248  0.10416  0.05336  32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.95507 0.50438 1.08915 0.08962  0.12391  0.10067  33  ASP   A N   
238  C CA  . ASP   A 33  ? 1.02084 0.52500 1.17766 0.10807  0.13406  0.11243  33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.99478 0.51232 1.17676 0.10073  0.12300  0.14926  33  ASP   A C   
240  O O   . ASP   A 33  ? 0.98865 0.51748 1.16152 0.07544  0.11005  0.15455  33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.95539 0.46857 1.12753 0.13975  0.15028  0.11271  33  ASP   A CB  
242  C CG  . ASP   A 33  ? 1.07957 0.57526 1.22290 0.14596  0.16309  0.07617  33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 1.12776 0.56915 1.24533 0.13663  0.16629  0.04992  33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.95908 0.49588 1.10411 0.15837  0.16920  0.07432  33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.99134 0.51218 1.20557 0.12231  0.12789  0.17702  34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.93110 0.46756 1.16865 0.11672  0.11728  0.21547  34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.93021 0.53998 1.17576 0.11668  0.10732  0.23858  34  ASP   A C   
248  O O   . ASP   A 34  ? 0.91214 0.54225 1.18185 0.12202  0.10129  0.27407  34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.95210 0.45260 1.21683 0.13735  0.12449  0.23218  34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.96179 0.48083 1.24434 0.16859  0.13675  0.23150  34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.99350 0.54059 1.27044 0.17612  0.14288  0.21950  34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.94688 0.45394 1.25075 0.18552  0.14062  0.24443  34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.90102 0.54925 1.12530 0.10983  0.10468  0.21944  35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.79897 0.51143 1.02524 0.10766  0.09499  0.23570  35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.79392 0.53164 0.98984 0.08298  0.08553  0.22134  35  VAL   A C   
256  O O   . VAL   A 35  ? 0.80213 0.52003 0.97661 0.07389  0.08874  0.19258  35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.78952 0.52728 1.02542 0.12771  0.10257  0.22955  35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.71603 0.51665 0.95636 0.12319  0.08999  0.24976  35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.72886 0.43882 0.99648 0.15581  0.11621  0.24047  35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.77616 0.55813 0.96965 0.07275  0.07410  0.24174  36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.73463 0.54543 0.90105 0.05323  0.06698  0.23031  36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.68865 0.54809 0.85049 0.05596  0.06076  0.23571  36  VAL   A C   
263  O O   . VAL   A 36  ? 0.71650 0.60086 0.89171 0.06002  0.05401  0.26279  36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.78539 0.59941 0.94707 0.03517  0.06040  0.24782  36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.66583 0.52083 0.80270 0.02017  0.05442  0.24252  36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.80903 0.57650 0.97113 0.02596  0.06458  0.23717  36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.66400 0.53608 0.80698 0.05257  0.06188  0.21105  37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.64479 0.55695 0.78045 0.05222  0.05567  0.21168  37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.66457 0.59875 0.77274 0.03475  0.04889  0.20609  37  TYR   A C   
270  O O   . TYR   A 37  ? 0.67750 0.59853 0.77130 0.02587  0.05219  0.19000  37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.64139 0.55128 0.77586 0.06129  0.06259  0.18964  37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.63812 0.52217 0.79534 0.08033  0.07398  0.18926  37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.69057 0.53059 0.84357 0.08275  0.08355  0.17252  37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.63566 0.53952 0.81842 0.09582  0.07551  0.20562  37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.70411 0.51546 0.87364 0.10152  0.09617  0.16939  37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.69805 0.57863 0.90276 0.11647  0.08911  0.20525  37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.73281 0.56450 0.92871 0.11997  0.10037  0.18568  37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.70472 0.50780 0.91798 0.14175  0.11607  0.18219  37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.64435 0.61257 0.74501 0.02996  0.03955  0.21924  38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.61862 0.60632 0.69026 0.01551  0.03501  0.21348  38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.62229 0.64141 0.68305 0.01225  0.02504  0.21822  38  CYS   A C   
282  O O   . CYS   A 38  ? 0.62583 0.65787 0.70582 0.01892  0.01921  0.23480  38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.62100 0.61071 0.68813 0.00648  0.03378  0.23186  38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.69331 0.71587 0.75809 0.00245  0.02154  0.26529  38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.61451 0.64599 0.64546 0.00191  0.02273  0.20417  39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.63500 0.69201 0.65021 -0.00492 0.01152  0.20726  39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.63662 0.71597 0.65151 -0.01001 0.00094  0.23612  39  PRO   A C   
288  O O   . PRO   A 39  ? 0.66532 0.74377 0.67624 -0.01305 0.00322  0.24955  39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.59232 0.64879 0.57263 -0.01387 0.01447  0.18515  39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.57267 0.60637 0.55945 -0.00844 0.02671  0.16798  39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.51741 0.53855 0.52900 -0.00323 0.03056  0.18333  39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.67088 0.77316 0.69071 -0.01230 -0.01169 0.24780  40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.66503 0.79231 0.68862 -0.01659 -0.02410 0.27918  40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.65716 0.79944 0.63748 -0.03261 -0.03021 0.28009  40  ARG   A C   
295  O O   . ARG   A 40  ? 0.69338 0.85379 0.67147 -0.03702 -0.03807 0.30717  40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.67705 0.83002 0.72178 -0.01555 -0.03756 0.29378  40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.67171 0.83792 0.69073 -0.02936 -0.04755 0.27626  40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.68170 0.88240 0.72239 -0.03307 -0.06498 0.29909  40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.69446 0.90439 0.71603 -0.04773 -0.07525 0.28240  40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.67852 0.92019 0.71725 -0.05548 -0.09200 0.29845  40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.63896 0.91009 0.71623 -0.04789 -0.10009 0.33279  40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.63090 0.87515 0.64982 -0.07150 -0.10124 0.28114  40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.66265 0.79726 0.60796 -0.04032 -0.02567 0.25205  41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.72422 0.87140 0.62408 -0.05386 -0.02876 0.24955  41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.77450 0.91713 0.66652 -0.05298 -0.01629 0.25630  41  HIS   A C   
306  O O   . HIS   A 41  ? 0.75572 0.90684 0.60861 -0.06170 -0.01304 0.25033  41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.81333 0.95075 0.67881 -0.06052 -0.02695 0.21679  41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.77720 0.88872 0.64648 -0.05152 -0.00977 0.19156  41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.79095 0.89620 0.63418 -0.05207 0.00325  0.17816  41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.72925 0.82284 0.62477 -0.04197 -0.00386 0.17846  41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.75363 0.83936 0.60997 -0.04340 0.01492  0.15943  41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.77318 0.85057 0.65883 -0.03786 0.01041  0.15882  41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.76191 0.89086 0.68979 -0.04318 -0.00877 0.26865  42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.76672 0.89521 0.69371 -0.04526 -0.00038 0.28372  42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.83067 0.98536 0.74722 -0.05313 -0.01123 0.31676  42  VAL   A C   
316  O O   . VAL   A 42  ? 0.79080 0.95398 0.69223 -0.05938 -0.00530 0.32959  42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.73272 0.83476 0.70079 -0.03506 0.00792  0.28837  42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.71076 0.81187 0.71348 -0.02699 -0.00084 0.31495  42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.72998 0.82764 0.69649 -0.04017 0.01831  0.29663  42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.78180 0.95324 0.70665 -0.05368 -0.02743 0.33300  43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.83662 1.03664 0.75289 -0.06150 -0.04066 0.36771  43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.82802 1.05177 0.68970 -0.07747 -0.04957 0.35795  43  ILE   A C   
323  O O   . ILE   A 43  ? 0.85752 1.10986 0.70253 -0.08733 -0.06453 0.38333  43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.80870 1.01878 0.76658 -0.05322 -0.05452 0.39479  43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.78152 1.00289 0.73748 -0.05542 -0.06593 0.37898  43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.77143 0.95107 0.77884 -0.03585 -0.04314 0.40033  43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.77800 1.00418 0.78619 -0.04164 -0.07244 0.39747  43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.82192 1.03250 0.65389 -0.08017 -0.04062 0.32133  44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.93279 1.15587 0.70999 -0.09430 -0.04736 0.30448  44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.90071 1.12785 0.63612 -0.09927 -0.03273 0.29908  44  CYS   A C   
331  O O   . CYS   A 44  ? 0.86449 1.07500 0.60710 -0.09110 -0.01328 0.28449  44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.93583 1.13848 0.70560 -0.09320 -0.04567 0.26768  44  CYS   A CB  
333  S SG  . CYS   A 44  ? 1.02210 1.23763 0.80381 -0.10111 -0.07029 0.27141  44  CYS   A SG  
334  N N   . THR   A 45  ? 0.87939 1.13144 0.57112 -0.11294 -0.04196 0.31169  45  THR   A N   
335  C CA  . THR   A 45  ? 1.06590 1.32350 0.70976 -0.11753 -0.02605 0.30190  45  THR   A CA  
336  C C   . THR   A 45  ? 1.22067 1.45866 0.82461 -0.11830 -0.01754 0.25804  45  THR   A C   
337  O O   . THR   A 45  ? 1.21472 1.44100 0.81502 -0.12215 -0.03028 0.24004  45  THR   A O   
338  C CB  . THR   A 45  ? 1.08869 1.37732 0.69568 -0.13129 -0.03739 0.32689  45  THR   A CB  
339  O OG1 . THR   A 45  ? 1.17515 1.46725 0.73321 -0.14446 -0.05148 0.30663  45  THR   A OG1 
340  C CG2 . THR   A 45  ? 0.94076 1.24308 0.59741 -0.12922 -0.05368 0.36473  45  THR   A CG2 
341  N N   . SER   A 46  ? 1.34917 1.58339 0.92593 -0.11395 0.00516  0.24207  46  SER   A N   
342  C CA  . SER   A 46  ? 1.32428 1.53505 0.86953 -0.10995 0.01746  0.20066  46  SER   A CA  
343  C C   . SER   A 46  ? 1.37171 1.58024 0.85762 -0.12466 0.00375  0.18261  46  SER   A C   
344  O O   . SER   A 46  ? 1.41006 1.59162 0.87369 -0.12279 0.00856  0.14774  46  SER   A O   
345  C CB  . SER   A 46  ? 1.30517 1.51845 0.83535 -0.10067 0.04594  0.19142  46  SER   A CB  
346  O OG  . SER   A 46  ? 1.22722 1.43343 0.81271 -0.08783 0.05790  0.19650  46  SER   A OG  
347  N N   . GLU   A 47  ? 1.38949 1.62435 0.84911 -0.14026 -0.01436 0.20606  47  GLU   A N   
348  C CA  . GLU   A 47  ? 1.34768 1.58179 0.75362 -0.15855 -0.03355 0.19164  47  GLU   A CA  
349  C C   . GLU   A 47  ? 1.30406 1.54344 0.74280 -0.16801 -0.06299 0.20473  47  GLU   A C   
350  O O   . GLU   A 47  ? 1.32488 1.55890 0.72763 -0.18451 -0.08091 0.18892  47  GLU   A O   
351  C CB  . GLU   A 47  ? 1.39464 1.64920 0.76117 -0.16709 -0.03665 0.20261  47  GLU   A CB  
352  C CG  . GLU   A 47  ? 1.36727 1.65286 0.77558 -0.16818 -0.04953 0.24714  47  GLU   A CG  
353  C CD  . GLU   A 47  ? 1.42188 1.71907 0.83808 -0.15816 -0.02774 0.26391  47  GLU   A CD  
354  O OE1 . GLU   A 47  ? 1.44965 1.73407 0.86258 -0.14671 -0.00197 0.24738  47  GLU   A OE1 
355  O OE2 . GLU   A 47  ? 1.25866 1.57905 0.68673 -0.16223 -0.03654 0.29446  47  GLU   A OE2 
356  N N   . ASP   A 48  ? 1.27798 1.52757 0.78374 -0.15836 -0.06807 0.23308  48  ASP   A N   
357  C CA  . ASP   A 48  ? 1.23985 1.49860 0.78254 -0.16417 -0.09295 0.24757  48  ASP   A CA  
358  C C   . ASP   A 48  ? 1.19015 1.41925 0.76375 -0.15608 -0.08960 0.22120  48  ASP   A C   
359  O O   . ASP   A 48  ? 1.12382 1.36054 0.72501 -0.16184 -0.10873 0.22917  48  ASP   A O   
360  C CB  . ASP   A 48  ? 1.16290 1.44587 0.76237 -0.15591 -0.09931 0.29165  48  ASP   A CB  
361  C CG  . ASP   A 48  ? 1.25612 1.57144 0.86562 -0.16915 -0.12906 0.32048  48  ASP   A CG  
362  O OD1 . ASP   A 48  ? 1.21642 1.54007 0.78225 -0.18670 -0.14286 0.30879  48  ASP   A OD1 
363  O OD2 . ASP   A 48  ? 1.37997 1.70796 1.04911 -0.15931 -0.13625 0.34973  48  ASP   A OD2 
364  N N   . MET   A 49  ? 1.23186 1.43079 0.80291 -0.14307 -0.06600 0.19241  49  MET   A N   
365  C CA  . MET   A 49  ? 1.13497 1.30601 0.73279 -0.13555 -0.06244 0.16879  49  MET   A CA  
366  C C   . MET   A 49  ? 1.13084 1.28747 0.69250 -0.15207 -0.07713 0.14434  49  MET   A C   
367  O O   . MET   A 49  ? 1.07810 1.21539 0.66406 -0.14932 -0.07878 0.12991  49  MET   A O   
368  C CB  . MET   A 49  ? 1.15111 1.29672 0.75320 -0.11826 -0.03483 0.14658  49  MET   A CB  
369  C CG  . MET   A 49  ? 1.13569 1.28675 0.78979 -0.10238 -0.02266 0.16652  49  MET   A CG  
370  S SD  . MET   A 49  ? 1.35432 1.49021 1.00418 -0.08737 0.00767  0.14846  49  MET   A SD  
371  C CE  . MET   A 49  ? 1.04906 1.18722 0.76551 -0.07492 0.01272  0.17199  49  MET   A CE  
372  N N   . LEU   A 50  ? 1.17423 1.33874 0.67711 -0.17051 -0.08828 0.13962  50  LEU   A N   
373  C CA  . LEU   A 50  ? 1.18358 1.32982 0.64759 -0.18967 -0.10398 0.11475  50  LEU   A CA  
374  C C   . LEU   A 50  ? 1.18813 1.35516 0.68881 -0.20328 -0.13227 0.13477  50  LEU   A C   
375  O O   . LEU   A 50  ? 1.12150 1.26848 0.63114 -0.20973 -0.13950 0.11760  50  LEU   A O   
376  C CB  . LEU   A 50  ? 1.25724 1.40579 0.64348 -0.20718 -0.10878 0.10363  50  LEU   A CB  
377  C CG  . LEU   A 50  ? 1.23794 1.34441 0.56735 -0.20335 -0.08761 0.06053  50  LEU   A CG  
378  C CD1 . LEU   A 50  ? 1.19029 1.25897 0.50630 -0.21520 -0.09840 0.03017  50  LEU   A CD1 
379  C CD2 . LEU   A 50  ? 1.15835 1.25168 0.51601 -0.17499 -0.05480 0.05372  50  LEU   A CD2 
380  N N   . ASN   A 51  ? 1.21958 1.42861 0.74407 -0.20760 -0.14829 0.17327  51  ASN   A N   
381  C CA  . ASN   A 51  ? 1.18058 1.41764 0.74823 -0.21761 -0.17387 0.19796  51  ASN   A CA  
382  C C   . ASN   A 51  ? 1.13364 1.40817 0.75177 -0.20510 -0.17651 0.24187  51  ASN   A C   
383  O O   . ASN   A 51  ? 1.24813 1.55777 0.85308 -0.21714 -0.19450 0.26995  51  ASN   A O   
384  C CB  . ASN   A 51  ? 1.19208 1.44368 0.71410 -0.24948 -0.20383 0.19622  51  ASN   A CB  
385  C CG  . ASN   A 51  ? 1.27313 1.55202 0.84346 -0.26090 -0.22915 0.21722  51  ASN   A CG  
386  O OD1 . ASN   A 51  ? 1.17328 1.45144 0.80528 -0.24429 -0.22092 0.22446  51  ASN   A OD1 
387  N ND2 . ASN   A 51  ? 1.51813 1.82268 1.06479 -0.28820 -0.25815 0.22716  51  ASN   A ND2 
388  N N   . PRO   A 52  ? 1.08851 1.35501 0.76419 -0.18108 -0.15933 0.24930  52  PRO   A N   
389  C CA  . PRO   A 52  ? 1.01019 1.30217 0.73110 -0.16667 -0.15780 0.28809  52  PRO   A CA  
390  C C   . PRO   A 52  ? 0.93404 1.25751 0.71251 -0.16515 -0.17586 0.31932  52  PRO   A C   
391  O O   . PRO   A 52  ? 0.97714 1.29285 0.79019 -0.15999 -0.17469 0.31003  52  PRO   A O   
392  C CB  . PRO   A 52  ? 0.96545 1.22643 0.71269 -0.14264 -0.12874 0.27511  52  PRO   A CB  
393  C CG  . PRO   A 52  ? 0.95389 1.18284 0.69592 -0.14168 -0.12036 0.23803  52  PRO   A CG  
394  C CD  . PRO   A 52  ? 1.05631 1.28612 0.75237 -0.16582 -0.13890 0.22121  52  PRO   A CD  
395  N N   . ASN   A 53  ? 0.92411 1.28569 0.71451 -0.16883 -0.19192 0.35859  53  ASN   A N   
396  C CA  . ASN   A 53  ? 0.93739 1.33355 0.79057 -0.16210 -0.20630 0.39505  53  ASN   A CA  
397  C C   . ASN   A 53  ? 0.89448 1.28056 0.79862 -0.13349 -0.18630 0.41437  53  ASN   A C   
398  O O   . ASN   A 53  ? 0.95570 1.35452 0.87071 -0.12791 -0.18596 0.44009  53  ASN   A O   
399  C CB  . ASN   A 53  ? 0.99574 1.43081 0.84587 -0.17901 -0.22862 0.41693  53  ASN   A CB  
400  C CG  . ASN   A 53  ? 0.99757 1.46858 0.91910 -0.17121 -0.23956 0.44937  53  ASN   A CG  
401  O OD1 . ASN   A 53  ? 0.99488 1.46921 0.96893 -0.14740 -0.22788 0.47307  53  ASN   A OD1 
402  N ND2 . ASN   A 53  ? 0.98686 1.48336 0.91115 -0.19142 -0.26072 0.44979  53  ASN   A ND2 
403  N N   . TYR   A 54  ? 0.83067 1.18815 0.76922 -0.11525 -0.16692 0.39558  54  TYR   A N   
404  C CA  . TYR   A 54  ? 0.83665 1.17168 0.81175 -0.09020 -0.14508 0.40331  54  TYR   A CA  
405  C C   . TYR   A 54  ? 0.87116 1.23306 0.89831 -0.07668 -0.15228 0.44875  54  TYR   A C   
406  O O   . TYR   A 54  ? 0.88042 1.22627 0.92584 -0.06146 -0.13929 0.46315  54  TYR   A O   
407  C CB  . TYR   A 54  ? 0.76468 1.06768 0.76526 -0.07506 -0.12597 0.37539  54  TYR   A CB  
408  C CG  . TYR   A 54  ? 0.75857 1.02658 0.71563 -0.08071 -0.11208 0.33371  54  TYR   A CG  
409  C CD1 . TYR   A 54  ? 0.77405 1.03854 0.70117 -0.09626 -0.11943 0.30769  54  TYR   A CD1 
410  C CD2 . TYR   A 54  ? 0.71612 0.95535 0.66321 -0.07116 -0.09234 0.32229  54  TYR   A CD2 
411  C CE1 . TYR   A 54  ? 0.75452 0.98607 0.64494 -0.09870 -0.10586 0.27151  54  TYR   A CE1 
412  C CE2 . TYR   A 54  ? 0.74513 0.95718 0.65713 -0.07456 -0.07951 0.28730  54  TYR   A CE2 
413  C CZ  . TYR   A 54  ? 0.76869 0.97641 0.65285 -0.08683 -0.08569 0.26220  54  TYR   A CZ  
414  O OH  . TYR   A 54  ? 0.81161 0.99121 0.66382 -0.08756 -0.07203 0.22916  54  TYR   A OH  
415  N N   . GLU   A 55  ? 0.82154 1.22354 0.87577 -0.08188 -0.17249 0.47226  55  GLU   A N   
416  C CA  . GLU   A 55  ? 0.94472 1.36663 1.05764 -0.06563 -0.17190 0.50394  55  GLU   A CA  
417  C C   . GLU   A 55  ? 0.93349 1.36836 1.03060 -0.07355 -0.17809 0.52188  55  GLU   A C   
418  O O   . GLU   A 55  ? 0.92688 1.35496 1.05868 -0.05641 -0.16821 0.54204  55  GLU   A O   
419  C CB  . GLU   A 55  ? 1.02829 1.49030 1.18187 -0.06856 -0.18644 0.51823  55  GLU   A CB  
420  C CG  . GLU   A 55  ? 1.08004 1.53394 1.28302 -0.04661 -0.17275 0.51559  55  GLU   A CG  
421  C CD  . GLU   A 55  ? 1.24734 1.67820 1.49939 -0.01421 -0.14982 0.52796  55  GLU   A CD  
422  O OE1 . GLU   A 55  ? 1.23411 1.66562 1.53159 0.00501  -0.13839 0.52960  55  GLU   A OE1 
423  O OE2 . GLU   A 55  ? 1.35137 1.76287 1.59696 -0.00823 -0.14255 0.53535  55  GLU   A OE2 
424  N N   . ASP   A 56  ? 0.93885 1.38972 0.98213 -0.09939 -0.19361 0.51388  56  ASP   A N   
425  C CA  . ASP   A 56  ? 1.02741 1.49135 1.04992 -0.10787 -0.19877 0.52989  56  ASP   A CA  
426  C C   . ASP   A 56  ? 1.01836 1.44880 1.00468 -0.10456 -0.18101 0.51726  56  ASP   A C   
427  O O   . ASP   A 56  ? 0.90198 1.34189 0.86543 -0.11239 -0.18331 0.52850  56  ASP   A O   
428  C CB  . ASP   A 56  ? 1.01485 1.50958 0.99299 -0.13704 -0.22187 0.52622  56  ASP   A CB  
429  C CG  . ASP   A 56  ? 0.98907 1.52828 1.01094 -0.14209 -0.24110 0.55388  56  ASP   A CG  
430  O OD1 . ASP   A 56  ? 0.97697 1.52336 1.05473 -0.12730 -0.23818 0.56337  56  ASP   A OD1 
431  O OD2 . ASP   A 56  ? 0.93127 1.49954 0.93168 -0.16080 -0.25816 0.56669  56  ASP   A OD2 
432  N N   . LEU   A 57  ? 1.00581 1.39985 0.98766 -0.09393 -0.16315 0.49562  57  LEU   A N   
433  C CA  . LEU   A 57  ? 0.95250 1.31527 0.91236 -0.08875 -0.14360 0.48628  57  LEU   A CA  
434  C C   . LEU   A 57  ? 0.95717 1.29536 0.97040 -0.06534 -0.12760 0.50130  57  LEU   A C   
435  O O   . LEU   A 57  ? 0.92317 1.24842 0.93438 -0.06273 -0.11775 0.51011  57  LEU   A O   
436  C CB  . LEU   A 57  ? 0.93853 1.27574 0.85599 -0.09407 -0.13293 0.45158  57  LEU   A CB  
437  C CG  . LEU   A 57  ? 1.00253 1.34374 0.84836 -0.11524 -0.13619 0.42787  57  LEU   A CG  
438  C CD1 . LEU   A 57  ? 1.02910 1.40290 0.85389 -0.13448 -0.16068 0.43141  57  LEU   A CD1 
439  C CD2 . LEU   A 57  ? 0.96753 1.27764 0.79120 -0.11465 -0.12228 0.38574  57  LEU   A CD2 
440  N N   . LEU   A 58  ? 0.93973 1.26970 0.99984 -0.04870 -0.12423 0.50321  58  LEU   A N   
441  C CA  . LEU   A 58  ? 0.90589 1.20623 1.01432 -0.02573 -0.10795 0.51309  58  LEU   A CA  
442  C C   . LEU   A 58  ? 0.89554 1.21182 1.04100 -0.01834 -0.11312 0.54519  58  LEU   A C   
443  O O   . LEU   A 58  ? 0.92085 1.20862 1.09267 -0.00446 -0.10011 0.55396  58  LEU   A O   
444  C CB  . LEU   A 58  ? 0.83588 1.12306 0.98075 -0.00876 -0.10083 0.50381  58  LEU   A CB  
445  C CG  . LEU   A 58  ? 0.79001 1.03577 0.97573 0.01504  -0.08064 0.50438  58  LEU   A CG  
446  C CD1 . LEU   A 58  ? 0.80926 1.01720 0.96797 0.01084  -0.06666 0.49079  58  LEU   A CD1 
447  C CD2 . LEU   A 58  ? 0.81745 1.05102 1.03103 0.03096  -0.07171 0.49004  58  LEU   A CD2 
448  N N   . ILE   A 59  ? 0.86159 1.22175 1.00980 -0.02840 -0.13222 0.56317  59  ILE   A N   
449  C CA  . ILE   A 59  ? 0.89000 1.26734 1.07473 -0.02125 -0.13694 0.59613  59  ILE   A CA  
450  C C   . ILE   A 59  ? 0.88178 1.25074 1.03966 -0.02971 -0.13431 0.60511  59  ILE   A C   
451  O O   . ILE   A 59  ? 0.88512 1.24184 1.07504 -0.01789 -0.12804 0.62615  59  ILE   A O   
452  C CB  . ILE   A 59  ? 0.92754 1.35749 1.12364 -0.03175 -0.15866 0.61547  59  ILE   A CB  
453  C CG1 . ILE   A 59  ? 0.94537 1.39893 1.08056 -0.06018 -0.17520 0.60021  59  ILE   A CG1 
454  C CG2 . ILE   A 59  ? 0.80826 1.24835 1.05471 -0.01641 -0.15723 0.61808  59  ILE   A CG2 
455  C CD1 . ILE   A 59  ? 0.89087 1.39518 1.03366 -0.07499 -0.19854 0.61847  59  ILE   A CD1 
456  N N   . ARG   A 60  ? 0.94174 1.31569 1.04078 -0.04968 -0.13760 0.58902  60  ARG   A N   
457  C CA  . ARG   A 60  ? 0.90426 1.27248 0.97469 -0.05824 -0.13257 0.59559  60  ARG   A CA  
458  C C   . ARG   A 60  ? 0.96422 1.28661 1.03991 -0.04842 -0.11102 0.58392  60  ARG   A C   
459  O O   . ARG   A 60  ? 0.99505 1.31158 1.04743 -0.05631 -0.10450 0.58723  60  ARG   A O   
460  C CB  . ARG   A 60  ? 0.84970 1.23882 0.85330 -0.08160 -0.14059 0.57962  60  ARG   A CB  
461  N N   . LYS   A 61  ? 1.01588 1.30708 1.12157 -0.03250 -0.09989 0.57065  61  LYS   A N   
462  C CA  . LYS   A 61  ? 0.98590 1.23144 1.09870 -0.02455 -0.08056 0.55788  61  LYS   A CA  
463  C C   . LYS   A 61  ? 0.94822 1.16654 1.11661 -0.00457 -0.07355 0.57408  61  LYS   A C   
464  O O   . LYS   A 61  ? 1.00255 1.22671 1.20731 0.00983  -0.07683 0.58072  61  LYS   A O   
465  C CB  . LYS   A 61  ? 0.93531 1.16083 1.03347 -0.02289 -0.07172 0.52642  61  LYS   A CB  
466  C CG  . LYS   A 61  ? 0.92603 1.16691 0.96562 -0.04152 -0.07329 0.50583  61  LYS   A CG  
467  C CD  . LYS   A 61  ? 0.91434 1.14634 0.92712 -0.05112 -0.06225 0.50434  61  LYS   A CD  
468  C CE  . LYS   A 61  ? 0.94463 1.20459 0.89854 -0.06930 -0.06660 0.49327  61  LYS   A CE  
469  N NZ  . LYS   A 61  ? 0.91032 1.18081 0.83781 -0.07445 -0.07426 0.47151  61  LYS   A NZ  
470  N N   . SER   A 62  ? 0.92374 1.11248 1.09836 -0.00406 -0.06332 0.58001  62  SER   A N   
471  C CA  . SER   A 62  ? 0.94925 1.09989 1.16963 0.01347  -0.05415 0.58968  62  SER   A CA  
472  C C   . SER   A 62  ? 0.94247 1.04249 1.16200 0.01669  -0.03744 0.56406  62  SER   A C   
473  O O   . SER   A 62  ? 0.91509 1.01397 1.10260 0.00617  -0.03307 0.54181  62  SER   A O   
474  C CB  . SER   A 62  ? 0.98369 1.13717 1.21456 0.00973  -0.05757 0.61917  62  SER   A CB  
475  O OG  . SER   A 62  ? 1.03685 1.23625 1.27427 0.00812  -0.07329 0.64492  62  SER   A OG  
476  N N   . ASN   A 63  ? 0.97261 1.02940 1.22699 0.03084  -0.02802 0.56702  63  ASN   A N   
477  C CA  . ASN   A 63  ? 0.97079 0.97586 1.22567 0.03269  -0.01336 0.54228  63  ASN   A CA  
478  C C   . ASN   A 63  ? 0.99723 0.99692 1.22243 0.01161  -0.01003 0.53759  63  ASN   A C   
479  O O   . ASN   A 63  ? 1.02439 1.00977 1.23138 0.00458  -0.00236 0.51344  63  ASN   A O   
480  C CB  . ASN   A 63  ? 0.88285 0.83984 1.17601 0.05006  -0.00485 0.54628  63  ASN   A CB  
481  C CG  . ASN   A 63  ? 0.89050 0.84850 1.21410 0.07368  -0.00247 0.54429  63  ASN   A CG  
482  O OD1 . ASN   A 63  ? 0.91478 0.88012 1.23297 0.07898  0.00040  0.52458  63  ASN   A OD1 
483  N ND2 . ASN   A 63  ? 0.86387 0.81571 1.22098 0.08841  -0.00267 0.56562  63  ASN   A ND2 
484  N N   . HIS   A 64  ? 0.93629 0.95104 1.15754 0.00125  -0.01522 0.56155  64  HIS   A N   
485  C CA  . HIS   A 64  ? 0.94744 0.95667 1.14805 -0.01743 -0.01008 0.56050  64  HIS   A CA  
486  C C   . HIS   A 64  ? 0.95340 1.00110 1.11101 -0.03276 -0.01036 0.54856  64  HIS   A C   
487  O O   . HIS   A 64  ? 0.96125 1.00854 1.10224 -0.04730 -0.00355 0.54489  64  HIS   A O   
488  C CB  . HIS   A 64  ? 1.06740 1.08257 1.27844 -0.02286 -0.01486 0.59189  64  HIS   A CB  
489  C CG  . HIS   A 64  ? 1.05698 1.12288 1.25948 -0.02361 -0.02786 0.61552  64  HIS   A CG  
490  N ND1 . HIS   A 64  ? 1.01148 1.11942 1.17802 -0.04032 -0.03217 0.62315  64  HIS   A ND1 
491  C CD2 . HIS   A 64  ? 1.07709 1.15983 1.30191 -0.01036 -0.03746 0.63265  64  HIS   A CD2 
492  C CE1 . HIS   A 64  ? 1.03297 1.17916 1.19741 -0.03881 -0.04519 0.64318  64  HIS   A CE1 
493  N NE2 . HIS   A 64  ? 1.11415 1.24796 1.31579 -0.02125 -0.04923 0.65056  64  HIS   A NE2 
494  N N   . ASN   A 65  ? 0.96397 1.04479 1.10317 -0.03026 -0.01753 0.54212  65  ASN   A N   
495  C CA  . ASN   A 65  ? 0.91851 1.02881 1.01343 -0.04343 -0.01606 0.52610  65  ASN   A CA  
496  C C   . ASN   A 65  ? 0.84975 0.93744 0.93794 -0.04296 -0.00498 0.49637  65  ASN   A C   
497  O O   . ASN   A 65  ? 0.80970 0.91759 0.86257 -0.05271 -0.00082 0.48098  65  ASN   A O   
498  C CB  . ASN   A 65  ? 0.92055 1.07195 0.99386 -0.04394 -0.02941 0.52861  65  ASN   A CB  
499  C CG  . ASN   A 65  ? 1.02015 1.19367 1.11016 -0.04127 -0.04267 0.55893  65  ASN   A CG  
500  O OD1 . ASN   A 65  ? 1.07899 1.23384 1.21099 -0.02751 -0.04422 0.57303  65  ASN   A OD1 
501  N ND2 . ASN   A 65  ? 1.04980 1.26321 1.10608 -0.05406 -0.05165 0.56845  65  ASN   A ND2 
502  N N   . PHE   A 66  ? 0.88645 0.93251 1.00628 -0.03146 0.00063  0.48729  66  PHE   A N   
503  C CA  . PHE   A 66  ? 0.90330 0.92625 1.02018 -0.03016 0.01030  0.45998  66  PHE   A CA  
504  C C   . PHE   A 66  ? 0.90295 0.88990 1.03289 -0.03768 0.02017  0.45444  66  PHE   A C   
505  O O   . PHE   A 66  ? 0.89153 0.84151 1.05064 -0.03129 0.02101  0.46074  66  PHE   A O   
506  C CB  . PHE   A 66  ? 0.89792 0.90133 1.03788 -0.01152 0.00946  0.44677  66  PHE   A CB  
507  C CG  . PHE   A 66  ? 0.90267 0.94352 1.03209 -0.00654 -0.00114 0.44826  66  PHE   A CG  
508  C CD1 . PHE   A 66  ? 0.85511 0.92339 0.94795 -0.01567 -0.00298 0.42422  66  PHE   A CD1 
509  C CD2 . PHE   A 66  ? 0.89059 0.93947 1.04793 0.00673  -0.00964 0.47140  66  PHE   A CD2 
510  C CE1 . PHE   A 66  ? 0.89989 0.99960 0.98234 -0.01448 -0.01456 0.42519  66  PHE   A CE1 
511  C CE2 . PHE   A 66  ? 0.91259 0.99935 1.06316 0.00838  -0.02152 0.47568  66  PHE   A CE2 
512  C CZ  . PHE   A 66  ? 0.92017 1.03121 1.03192 -0.00375 -0.02484 0.45294  66  PHE   A CZ  
513  N N   . LEU   A 67  ? 0.85820 0.85658 0.96625 -0.05099 0.02729  0.43795  67  LEU   A N   
514  C CA  . LEU   A 67  ? 0.83420 0.80709 0.95390 -0.06245 0.03497  0.43357  67  LEU   A CA  
515  C C   . LEU   A 67  ? 0.86814 0.81836 0.98816 -0.05849 0.04020  0.39226  67  LEU   A C   
516  O O   . LEU   A 67  ? 0.86120 0.83482 0.95896 -0.06156 0.04397  0.36870  67  LEU   A O   
517  C CB  . LEU   A 67  ? 0.82147 0.83042 0.92028 -0.07936 0.03953  0.44427  67  LEU   A CB  
518  C CG  . LEU   A 67  ? 0.88537 0.88565 0.99142 -0.09412 0.04813  0.43579  67  LEU   A CG  
519  C CD1 . LEU   A 67  ? 1.01307 0.97337 1.14900 -0.10005 0.04546  0.44680  67  LEU   A CD1 
520  C CD2 . LEU   A 67  ? 0.91541 0.96307 0.99687 -0.10536 0.05502  0.44046  67  LEU   A CD2 
521  N N   . VAL   A 68  ? 0.90380 0.80724 1.04768 -0.05099 0.04085  0.38372  68  VAL   A N   
522  C CA  . VAL   A 68  ? 0.88541 0.76466 1.02811 -0.04724 0.04501  0.34611  68  VAL   A CA  
523  C C   . VAL   A 68  ? 0.88391 0.74023 1.03386 -0.06450 0.04788  0.34069  68  VAL   A C   
524  O O   . VAL   A 68  ? 0.88228 0.70305 1.05225 -0.07013 0.04690  0.35723  68  VAL   A O   
525  C CB  . VAL   A 68  ? 0.90256 0.74490 1.06242 -0.02829 0.04548  0.33702  68  VAL   A CB  
526  C CG1 . VAL   A 68  ? 0.82759 0.64598 0.98126 -0.02591 0.05025  0.29836  68  VAL   A CG1 
527  C CG2 . VAL   A 68  ? 0.80014 0.67092 0.95877 -0.01295 0.04116  0.34701  68  VAL   A CG2 
528  N N   . GLN   A 69  ? 0.88291 0.75901 1.01844 -0.07342 0.05075  0.31877  69  GLN   A N   
529  C CA  . GLN   A 69  ? 0.88362 0.74695 1.02737 -0.09193 0.05169  0.31375  69  GLN   A CA  
530  C C   . GLN   A 69  ? 0.84487 0.68822 0.98366 -0.08978 0.05183  0.27745  69  GLN   A C   
531  O O   . GLN   A 69  ? 0.79174 0.65906 0.91424 -0.08120 0.05372  0.25721  69  GLN   A O   
532  C CB  . GLN   A 69  ? 0.88847 0.80021 1.02386 -0.10585 0.05535  0.32586  69  GLN   A CB  
533  C CG  . GLN   A 69  ? 0.94094 0.85313 1.09225 -0.12272 0.05503  0.36033  69  GLN   A CG  
534  C CD  . GLN   A 69  ? 0.99775 0.96549 1.13754 -0.13167 0.06156  0.37675  69  GLN   A CD  
535  O OE1 . GLN   A 69  ? 1.02168 1.02181 1.14018 -0.12214 0.06429  0.38256  69  GLN   A OE1 
536  N NE2 . GLN   A 69  ? 1.07023 1.05007 1.22343 -0.15071 0.06436  0.38460  69  GLN   A NE2 
537  N N   . ALA   A 70  ? 0.88191 0.67932 1.03282 -0.09816 0.04936  0.26963  70  ALA   A N   
538  C CA  . ALA   A 70  ? 0.90125 0.67841 1.04522 -0.10145 0.04794  0.23719  70  ALA   A CA  
539  C C   . ALA   A 70  ? 0.99048 0.77241 1.14330 -0.12752 0.04374  0.24156  70  ALA   A C   
540  O O   . ALA   A 70  ? 1.07356 0.81861 1.24049 -0.14212 0.03982  0.25185  70  ALA   A O   
541  C CB  . ALA   A 70  ? 0.91653 0.63512 1.06292 -0.09110 0.04839  0.22207  70  ALA   A CB  
542  N N   . GLY   A 71  ? 0.94964 0.77731 1.09634 -0.13347 0.04458  0.23525  71  GLY   A N   
543  C CA  . GLY   A 71  ? 1.02814 0.87571 1.18889 -0.15760 0.04165  0.24744  71  GLY   A CA  
544  C C   . GLY   A 71  ? 1.07129 0.93653 1.24485 -0.16573 0.04483  0.28363  71  GLY   A C   
545  O O   . GLY   A 71  ? 1.11990 1.00651 1.28512 -0.15193 0.05040  0.29778  71  GLY   A O   
546  N N   . ASN   A 72  ? 1.01522 0.87197 1.20843 -0.19019 0.04031  0.30012  72  ASN   A N   
547  C CA  . ASN   A 72  ? 1.14969 1.02178 1.35695 -0.20103 0.04318  0.33772  72  ASN   A CA  
548  C C   . ASN   A 72  ? 1.19421 1.00931 1.41116 -0.20120 0.03917  0.35308  72  ASN   A C   
549  O O   . ASN   A 72  ? 1.12094 0.93736 1.35032 -0.21340 0.03855  0.38032  72  ASN   A O   
550  C CB  . ASN   A 72  ? 1.32558 1.22681 1.55322 -0.22881 0.04138  0.35273  72  ASN   A CB  
551  C CG  . ASN   A 72  ? 1.34750 1.31757 1.57030 -0.22469 0.04995  0.34995  72  ASN   A CG  
552  O OD1 . ASN   A 72  ? 1.23018 1.21569 1.43285 -0.20370 0.05441  0.32763  72  ASN   A OD1 
553  N ND2 . ASN   A 72  ? 1.23252 1.24381 1.47537 -0.24430 0.05320  0.37362  72  ASN   A ND2 
554  N N   . VAL   A 73  ? 1.19089 0.95861 1.39939 -0.18402 0.03737  0.33169  73  VAL   A N   
555  C CA  . VAL   A 73  ? 1.12455 0.83669 1.34306 -0.17729 0.03594  0.34456  73  VAL   A CA  
556  C C   . VAL   A 73  ? 1.06147 0.78182 1.26893 -0.14726 0.04084  0.34343  73  VAL   A C   
557  O O   . VAL   A 73  ? 1.03189 0.75120 1.22453 -0.13096 0.04273  0.31401  73  VAL   A O   
558  C CB  . VAL   A 73  ? 1.12740 0.76941 1.34833 -0.18401 0.03065  0.32001  73  VAL   A CB  
559  C CG1 . VAL   A 73  ? 1.15265 0.73890 1.37845 -0.16518 0.03316  0.32477  73  VAL   A CG1 
560  C CG2 . VAL   A 73  ? 1.20496 0.83507 1.43766 -0.21639 0.02305  0.32595  73  VAL   A CG2 
561  N N   . GLN   A 74  ? 1.03744 0.76845 1.25215 -0.14097 0.04189  0.37615  74  GLN   A N   
562  C CA  . GLN   A 74  ? 1.05036 0.80319 1.25652 -0.11692 0.04432  0.38242  74  GLN   A CA  
563  C C   . GLN   A 74  ? 1.05220 0.75422 1.26932 -0.09676 0.04401  0.37983  74  GLN   A C   
564  O O   . GLN   A 74  ? 1.08180 0.73477 1.30976 -0.10044 0.04229  0.37915  74  GLN   A O   
565  C CB  . GLN   A 74  ? 1.05043 0.85359 1.25026 -0.11919 0.04392  0.41236  74  GLN   A CB  
566  C CG  . GLN   A 74  ? 1.02959 0.81194 1.24211 -0.11845 0.03989  0.43542  74  GLN   A CG  
567  C CD  . GLN   A 74  ? 1.11308 0.90919 1.32420 -0.09720 0.03749  0.45074  74  GLN   A CD  
568  O OE1 . GLN   A 74  ? 1.08433 0.92892 1.27859 -0.09197 0.03748  0.45627  74  GLN   A OE1 
569  N NE2 . GLN   A 74  ? 1.18858 0.94229 1.41689 -0.08494 0.03519  0.45692  74  GLN   A NE2 
570  N N   . LEU   A 75  ? 1.11850 0.83580 1.33002 -0.07423 0.04599  0.37489  75  LEU   A N   
571  C CA  . LEU   A 75  ? 1.05421 0.73269 1.27883 -0.05089 0.04823  0.37204  75  LEU   A CA  
572  C C   . LEU   A 75  ? 1.03421 0.74193 1.26518 -0.03687 0.04431  0.40033  75  LEU   A C   
573  O O   . LEU   A 75  ? 1.04309 0.80503 1.26195 -0.03852 0.04100  0.41425  75  LEU   A O   
574  C CB  . LEU   A 75  ? 0.98219 0.66396 1.19364 -0.03433 0.05242  0.33676  75  LEU   A CB  
575  C CG  . LEU   A 75  ? 0.97769 0.60343 1.18768 -0.03091 0.05751  0.30326  75  LEU   A CG  
576  C CD1 . LEU   A 75  ? 0.98959 0.59582 1.19307 -0.05799 0.05404  0.29154  75  LEU   A CD1 
577  C CD2 . LEU   A 75  ? 1.02079 0.66508 1.21411 -0.01662 0.06151  0.27218  75  LEU   A CD2 
578  N N   . ARG   A 76  ? 1.02396 0.69550 1.27257 -0.02310 0.04456  0.40770  76  ARG   A N   
579  C CA  . ARG   A 76  ? 1.02305 0.72094 1.28310 -0.00881 0.03996  0.43547  76  ARG   A CA  
580  C C   . ARG   A 76  ? 0.97910 0.68869 1.24641 0.01635  0.04243  0.42835  76  ARG   A C   
581  O O   . ARG   A 76  ? 0.97942 0.64841 1.25522 0.03135  0.05030  0.40688  76  ARG   A O   
582  C CB  . ARG   A 76  ? 1.00099 0.65721 1.27963 -0.00616 0.03931  0.45048  76  ARG   A CB  
583  N N   . VAL   A 77  ? 0.93797 0.70437 1.20027 0.01993  0.03573  0.44565  77  VAL   A N   
584  C CA  . VAL   A 77  ? 0.93907 0.72793 1.21012 0.04077  0.03549  0.44412  77  VAL   A CA  
585  C C   . VAL   A 77  ? 0.92658 0.71273 1.22612 0.05863  0.03327  0.46630  77  VAL   A C   
586  O O   . VAL   A 77  ? 1.00285 0.80214 1.30739 0.05190  0.02622  0.49283  77  VAL   A O   
587  C CB  . VAL   A 77  ? 0.96932 0.81992 1.21846 0.03268  0.02720  0.45137  77  VAL   A CB  
588  C CG1 . VAL   A 77  ? 0.94493 0.81785 1.20312 0.05098  0.02606  0.44746  77  VAL   A CG1 
589  C CG2 . VAL   A 77  ? 0.96213 0.81702 1.18322 0.01397  0.03046  0.43303  77  VAL   A CG2 
590  N N   . ILE   A 78  ? 0.90209 0.67369 1.22150 0.08209  0.04021  0.45645  78  ILE   A N   
591  C CA  . ILE   A 78  ? 0.94481 0.71133 1.29543 0.10147  0.04068  0.47646  78  ILE   A CA  
592  C C   . ILE   A 78  ? 0.86347 0.67961 1.22995 0.11767  0.03719  0.48628  78  ILE   A C   
593  O O   . ILE   A 78  ? 0.88273 0.72393 1.27308 0.12740  0.03149  0.51332  78  ILE   A O   
594  C CB  . ILE   A 78  ? 0.95992 0.65635 1.32380 0.11558  0.05428  0.45808  78  ILE   A CB  
595  C CG1 . ILE   A 78  ? 0.94357 0.61941 1.30826 0.13340  0.06764  0.42618  78  ILE   A CG1 
596  C CG2 . ILE   A 78  ? 0.96137 0.61124 1.30774 0.09450  0.05481  0.44826  78  ILE   A CG2 
597  C CD1 . ILE   A 78  ? 1.03679 0.73680 1.43048 0.16083  0.07276  0.43504  78  ILE   A CD1 
598  N N   . GLY   A 79  ? 0.89750 0.73078 1.25165 0.11882  0.03953  0.46637  79  GLY   A N   
599  C CA  . GLY   A 79  ? 0.81684 0.69912 1.18514 0.13081  0.03519  0.47462  79  GLY   A CA  
600  C C   . GLY   A 79  ? 0.81328 0.72417 1.15405 0.11870  0.03065  0.45947  79  GLY   A C   
601  O O   . GLY   A 79  ? 0.85233 0.73431 1.17109 0.11069  0.03770  0.43462  79  GLY   A O   
602  N N   . HIS   A 80  ? 0.79671 0.76449 1.13831 0.11609  0.01800  0.47484  80  HIS   A N   
603  C CA  . HIS   A 80  ? 0.78971 0.78681 1.10224 0.10284  0.01120  0.46297  80  HIS   A CA  
604  C C   . HIS   A 80  ? 0.80783 0.85235 1.13767 0.11095  0.00340  0.47205  80  HIS   A C   
605  O O   . HIS   A 80  ? 0.82389 0.90393 1.17304 0.11250  -0.00727 0.49775  80  HIS   A O   
606  C CB  . HIS   A 80  ? 0.81922 0.84092 1.09546 0.07743  -0.00168 0.47226  80  HIS   A CB  
607  C CG  . HIS   A 80  ? 0.91757 0.98117 1.19952 0.07173  -0.01688 0.50260  80  HIS   A CG  
608  N ND1 . HIS   A 80  ? 0.93399 0.99030 1.24866 0.08320  -0.01617 0.52428  80  HIS   A ND1 
609  C CD2 . HIS   A 80  ? 0.91125 1.02391 1.16891 0.05542  -0.03333 0.51411  80  HIS   A CD2 
610  C CE1 . HIS   A 80  ? 1.01239 1.11388 1.32481 0.07404  -0.03179 0.54977  80  HIS   A CE1 
611  N NE2 . HIS   A 80  ? 0.89258 1.02835 1.16917 0.05659  -0.04265 0.54299  80  HIS   A NE2 
612  N N   . SER   A 81  ? 0.77009 0.81726 1.09358 0.11430  0.00820  0.45115  81  SER   A N   
613  C CA  . SER   A 81  ? 0.72645 0.82078 1.06513 0.11824  0.00004  0.45800  81  SER   A CA  
614  C C   . SER   A 81  ? 0.82190 0.93142 1.12084 0.09854  -0.00431 0.42520  81  SER   A C   
615  O O   . SER   A 81  ? 0.81552 0.89555 1.08210 0.08839  0.00325  0.39471  81  SER   A O   
616  C CB  . SER   A 81  ? 0.73687 0.82088 1.11748 0.14574  0.01614  0.45488  81  SER   A CB  
617  O OG  . SER   A 81  ? 0.78703 0.82369 1.15608 0.15323  0.03541  0.41959  81  SER   A OG  
618  N N   . MET   A 82  ? 0.80882 0.96496 1.11228 0.09272  -0.01734 0.43317  82  MET   A N   
619  C CA  . MET   A 82  ? 0.81327 0.98353 1.08106 0.07363  -0.02324 0.40517  82  MET   A CA  
620  C C   . MET   A 82  ? 0.75884 0.94187 1.05009 0.08399  -0.01671 0.39443  82  MET   A C   
621  O O   . MET   A 82  ? 0.72699 0.93878 1.06049 0.09788  -0.01895 0.42012  82  MET   A O   
622  C CB  . MET   A 82  ? 0.83496 1.04708 1.07738 0.05066  -0.04678 0.42076  82  MET   A CB  
623  C CG  . MET   A 82  ? 0.89541 1.12837 1.11302 0.03348  -0.05586 0.39925  82  MET   A CG  
624  S SD  . MET   A 82  ? 0.87878 1.12516 1.03535 0.00310  -0.07343 0.39211  82  MET   A SD  
625  C CE  . MET   A 82  ? 0.87417 1.17853 1.04676 -0.00664 -0.10088 0.43468  82  MET   A CE  
626  N N   . GLN   A 83  ? 0.73422 0.89797 1.00008 0.07784  -0.00796 0.35861  83  GLN   A N   
627  C CA  . GLN   A 83  ? 0.74123 0.91702 1.02283 0.08422  -0.00121 0.34639  83  GLN   A CA  
628  C C   . GLN   A 83  ? 0.66984 0.85364 0.91344 0.06131  -0.01027 0.32258  83  GLN   A C   
629  O O   . GLN   A 83  ? 0.64716 0.79925 0.85985 0.05609  -0.00171 0.29310  83  GLN   A O   
630  C CB  . GLN   A 83  ? 0.71500 0.85142 1.00789 0.10485  0.02309  0.32640  83  GLN   A CB  
631  C CG  . GLN   A 83  ? 0.68926 0.84546 1.00842 0.11667  0.03230  0.32391  83  GLN   A CG  
632  C CD  . GLN   A 83  ? 0.74053 0.85758 1.06409 0.13665  0.05713  0.30233  83  GLN   A CD  
633  O OE1 . GLN   A 83  ? 0.79167 0.86398 1.09485 0.13822  0.06548  0.28544  83  GLN   A OE1 
634  N NE2 . GLN   A 83  ? 0.78344 0.91828 1.13346 0.15138  0.06919  0.30353  83  GLN   A NE2 
635  N N   . ASN   A 84  ? 0.66445 0.88998 0.91223 0.04772  -0.02792 0.33620  84  ASN   A N   
636  C CA  . ASN   A 84  ? 0.64716 0.87879 0.85937 0.02449  -0.03879 0.31591  84  ASN   A CA  
637  C C   . ASN   A 84  ? 0.69912 0.90791 0.86345 0.01030  -0.04273 0.30091  84  ASN   A C   
638  O O   . ASN   A 84  ? 0.70100 0.92235 0.85799 0.00452  -0.05370 0.32055  84  ASN   A O   
639  C CB  . ASN   A 84  ? 0.64024 0.85705 0.85528 0.02983  -0.02442 0.29161  84  ASN   A CB  
640  C CG  . ASN   A 84  ? 0.61483 0.85560 0.87909 0.04738  -0.01601 0.30835  84  ASN   A CG  
641  O OD1 . ASN   A 84  ? 0.60106 0.88501 0.89057 0.04124  -0.02946 0.33108  84  ASN   A OD1 
642  N ND2 . ASN   A 84  ? 0.64580 0.85991 0.92331 0.06884  0.00659  0.29701  84  ASN   A ND2 
643  N N   . CYS   A 85  ? 0.67256 0.85072 0.80547 0.00550  -0.03343 0.26922  85  CYS   A N   
644  C CA  . CYS   A 85  ? 0.67861 0.83859 0.76868 -0.00621 -0.03455 0.25467  85  CYS   A CA  
645  C C   . CYS   A 85  ? 0.73128 0.85947 0.82156 0.00580  -0.01851 0.24804  85  CYS   A C   
646  O O   . CYS   A 85  ? 0.71089 0.82274 0.76977 -0.00165 -0.01498 0.23282  85  CYS   A O   
647  C CB  . CYS   A 85  ? 0.67764 0.82632 0.73441 -0.01948 -0.03553 0.22599  85  CYS   A CB  
648  S SG  . CYS   A 85  ? 0.66084 0.84056 0.70948 -0.04032 -0.05743 0.23124  85  CYS   A SG  
649  N N   . VAL   A 86  ? 0.65995 0.77863 0.78537 0.02395  -0.00838 0.25906  86  VAL   A N   
650  C CA  . VAL   A 86  ? 0.67505 0.76001 0.80205 0.03316  0.00523  0.25309  86  VAL   A CA  
651  C C   . VAL   A 86  ? 0.68788 0.77691 0.83587 0.03966  0.00197  0.28366  86  VAL   A C   
652  O O   . VAL   A 86  ? 0.74402 0.85900 0.91876 0.04562  -0.00601 0.30953  86  VAL   A O   
653  C CB  . VAL   A 86  ? 0.68929 0.74808 0.83314 0.04848  0.02162  0.23600  86  VAL   A CB  
654  C CG1 . VAL   A 86  ? 0.72321 0.78348 0.90813 0.06812  0.02767  0.25615  86  VAL   A CG1 
655  C CG2 . VAL   A 86  ? 0.66562 0.68822 0.79307 0.04776  0.03205  0.21738  86  VAL   A CG2 
656  N N   . LEU   A 87  ? 0.70759 0.77240 0.84563 0.03799  0.00771  0.28291  87  LEU   A N   
657  C CA  . LEU   A 87  ? 0.73363 0.79416 0.89122 0.04378  0.00635  0.31180  87  LEU   A CA  
658  C C   . LEU   A 87  ? 0.70890 0.72591 0.88562 0.05772  0.02196  0.30390  87  LEU   A C   
659  O O   . LEU   A 87  ? 0.65365 0.64428 0.81321 0.05347  0.03077  0.27753  87  LEU   A O   
660  C CB  . LEU   A 87  ? 0.70154 0.77129 0.83048 0.02718  -0.00090 0.32135  87  LEU   A CB  
661  C CG  . LEU   A 87  ? 0.73137 0.79733 0.87368 0.02837  -0.00315 0.35313  87  LEU   A CG  
662  C CD1 . LEU   A 87  ? 0.77885 0.87946 0.94004 0.03151  -0.01755 0.38870  87  LEU   A CD1 
663  C CD2 . LEU   A 87  ? 0.71329 0.78193 0.82141 0.01124  -0.00364 0.35134  87  LEU   A CD2 
664  N N   . LYS   A 88  ? 0.72039 0.72934 0.93245 0.07435  0.02502  0.32655  88  LYS   A N   
665  C CA  . LYS   A 88  ? 0.71836 0.68039 0.94834 0.08892  0.04012  0.31911  88  LYS   A CA  
666  C C   . LYS   A 88  ? 0.77378 0.71823 1.01757 0.08963  0.03812  0.34679  88  LYS   A C   
667  O O   . LYS   A 88  ? 0.80846 0.77669 1.07389 0.09548  0.02958  0.38066  88  LYS   A O   
668  C CB  . LYS   A 88  ? 0.72988 0.68964 0.99194 0.11229  0.04998  0.31983  88  LYS   A CB  
669  C CG  . LYS   A 88  ? 0.72781 0.69728 0.97865 0.11292  0.05555  0.29197  88  LYS   A CG  
670  C CD  . LYS   A 88  ? 0.75590 0.75899 1.03964 0.12872  0.05602  0.30840  88  LYS   A CD  
671  C CE  . LYS   A 88  ? 0.77497 0.75047 1.07808 0.15208  0.07688  0.29455  88  LYS   A CE  
672  N NZ  . LYS   A 88  ? 0.81049 0.81977 1.15572 0.17189  0.08005  0.31805  88  LYS   A NZ  
673  N N   . LEU   A 89  ? 0.77513 0.67925 1.00805 0.08267  0.04496  0.33448  89  LEU   A N   
674  C CA  . LEU   A 89  ? 0.79694 0.67891 1.04173 0.08007  0.04357  0.35980  89  LEU   A CA  
675  C C   . LEU   A 89  ? 0.83058 0.65323 1.09396 0.09367  0.05735  0.34979  89  LEU   A C   
676  O O   . LEU   A 89  ? 0.85745 0.64985 1.10461 0.08965  0.06569  0.31677  89  LEU   A O   
677  C CB  . LEU   A 89  ? 0.80822 0.69585 1.02382 0.05573  0.03846  0.35753  89  LEU   A CB  
678  C CG  . LEU   A 89  ? 0.79185 0.72979 0.97816 0.04055  0.02808  0.35801  89  LEU   A CG  
679  C CD1 . LEU   A 89  ? 0.68835 0.62513 0.84691 0.02064  0.02961  0.34657  89  LEU   A CD1 
680  C CD2 . LEU   A 89  ? 0.82185 0.79639 1.01590 0.04061  0.01551  0.39593  89  LEU   A CD2 
681  N N   . LYS   A 90  ? 0.82100 0.62579 1.11698 0.10948  0.05930  0.37839  90  LYS   A N   
682  C CA  . LYS   A 90  ? 0.86374 0.60869 1.17419 0.12228  0.07226  0.36653  90  LYS   A CA  
683  C C   . LYS   A 90  ? 0.96115 0.67300 1.26159 0.10308  0.06884  0.37017  90  LYS   A C   
684  O O   . LYS   A 90  ? 0.97068 0.70252 1.27645 0.09495  0.05893  0.39774  90  LYS   A O   
685  C CB  . LYS   A 90  ? 0.91330 0.66431 1.25659 0.14579  0.07536  0.38313  90  LYS   A CB  
686  C CG  . LYS   A 90  ? 0.90648 0.62421 1.26169 0.16986  0.09323  0.35921  90  LYS   A CG  
687  C CD  . LYS   A 90  ? 0.91692 0.56714 1.27162 0.17344  0.10259  0.34593  90  LYS   A CD  
688  C CE  . LYS   A 90  ? 0.98616 0.60835 1.35371 0.20061  0.12066  0.32717  90  LYS   A CE  
689  N NZ  . LYS   A 90  ? 1.00235 0.55276 1.36303 0.20281  0.12888  0.31074  90  LYS   A NZ  
690  N N   . VAL   A 91  ? 0.97118 0.63459 1.25702 0.09445  0.07646  0.34290  91  VAL   A N   
691  C CA  . VAL   A 91  ? 1.00917 0.64119 1.28644 0.07302  0.07264  0.34465  91  VAL   A CA  
692  C C   . VAL   A 91  ? 1.03119 0.59873 1.31735 0.08264  0.08070  0.33181  91  VAL   A C   
693  O O   . VAL   A 91  ? 1.02452 0.56426 1.31288 0.10182  0.09225  0.30910  91  VAL   A O   
694  C CB  . VAL   A 91  ? 1.02327 0.65752 1.27290 0.04918  0.07102  0.32109  91  VAL   A CB  
695  C CG1 . VAL   A 91  ? 0.90650 0.60763 1.13976 0.03613  0.06129  0.33169  91  VAL   A CG1 
696  C CG2 . VAL   A 91  ? 0.93774 0.55458 1.17123 0.05660  0.07965  0.27935  91  VAL   A CG2 
697  N N   . ASP   A 92  ? 1.14813 0.69164 1.43712 0.06896  0.07504  0.34629  92  ASP   A N   
698  C CA  . ASP   A 92  ? 1.16189 0.64012 1.45686 0.07550  0.08057  0.33740  92  ASP   A CA  
699  C C   . ASP   A 92  ? 1.16807 0.58923 1.44109 0.06393  0.08611  0.29921  92  ASP   A C   
700  O O   . ASP   A 92  ? 1.14064 0.50095 1.41091 0.06437  0.08908  0.28774  92  ASP   A O   
701  C CB  . ASP   A 92  ? 1.21193 0.68499 1.51587 0.06205  0.07153  0.36753  92  ASP   A CB  
702  C CG  . ASP   A 92  ? 1.29066 0.74308 1.57751 0.02962  0.06556  0.36180  92  ASP   A CG  
703  O OD1 . ASP   A 92  ? 1.23582 0.73525 1.51361 0.01107  0.05927  0.37057  92  ASP   A OD1 
704  O OD2 . ASP   A 92  ? 1.34423 0.73502 1.62700 0.02215  0.06685  0.35005  92  ASP   A OD2 
705  N N   . THR   A 93  ? 1.20055 0.63884 1.45642 0.05322  0.08696  0.27887  93  THR   A N   
706  C CA  . THR   A 93  ? 1.18541 0.57680 1.41901 0.03875  0.09008  0.24315  93  THR   A CA  
707  C C   . THR   A 93  ? 1.09477 0.50136 1.31601 0.05012  0.09925  0.21678  93  THR   A C   
708  O O   . THR   A 93  ? 1.00125 0.47000 1.21909 0.04942  0.09494  0.22318  93  THR   A O   
709  C CB  . THR   A 93  ? 1.20088 0.59897 1.42592 0.00311  0.07881  0.24848  93  THR   A CB  
710  O OG1 . THR   A 93  ? 1.19271 0.56831 1.42639 -0.00830 0.07189  0.26984  93  THR   A OG1 
711  C CG2 . THR   A 93  ? 1.17309 0.53252 1.37607 -0.01432 0.07977  0.21155  93  THR   A CG2 
712  N N   . ALA   A 94  ? 1.12543 0.48400 1.33055 0.05939  0.10932  0.18240  94  ALA   A N   
713  C CA  . ALA   A 94  ? 1.08919 0.46375 1.27231 0.06578  0.11642  0.15137  94  ALA   A CA  
714  C C   . ALA   A 94  ? 1.07579 0.45689 1.22925 0.03416  0.10531  0.12858  94  ALA   A C   
715  O O   . ALA   A 94  ? 1.11461 0.44957 1.25999 0.01321  0.09998  0.12021  94  ALA   A O   
716  C CB  . ALA   A 94  ? 1.09550 0.41935 1.27029 0.08947  0.13312  0.12433  94  ALA   A CB  
717  N N   . ASN   A 95  ? 1.03854 0.47713 1.17789 0.03012  0.10107  0.12023  95  ASN   A N   
718  C CA  . ASN   A 95  ? 0.98990 0.44407 1.10586 0.00258  0.09027  0.10280  95  ASN   A CA  
719  C C   . ASN   A 95  ? 0.99837 0.39877 1.08728 -0.00458 0.09333  0.06650  95  ASN   A C   
720  O O   . ASN   A 95  ? 1.08020 0.47447 1.15220 0.01190  0.10355  0.04319  95  ASN   A O   
721  C CB  . ASN   A 95  ? 0.98031 0.50137 1.08742 0.00472  0.08741  0.10050  95  ASN   A CB  
722  C CG  . ASN   A 95  ? 0.93653 0.47608 1.02210 -0.01934 0.07768  0.08290  95  ASN   A CG  
723  O OD1 . ASN   A 95  ? 1.00371 0.52415 1.08743 -0.04269 0.06926  0.08242  95  ASN   A OD1 
724  N ND2 . ASN   A 95  ? 0.92381 0.50271 0.99567 -0.01415 0.07821  0.07067  95  ASN   A ND2 
725  N N   . PRO   A 96  ? 1.02235 0.38383 1.10502 -0.03039 0.08436  0.06113  96  PRO   A N   
726  C CA  . PRO   A 96  ? 1.06183 0.36943 1.11353 -0.04064 0.08501  0.02475  96  PRO   A CA  
727  C C   . PRO   A 96  ? 1.10849 0.45153 1.13120 -0.04872 0.08044  0.00009  96  PRO   A C   
728  O O   . PRO   A 96  ? 1.19585 0.50116 1.18765 -0.05031 0.08389  -0.03188 96  PRO   A O   
729  C CB  . PRO   A 96  ? 1.08143 0.35258 1.13767 -0.07262 0.07173  0.03126  96  PRO   A CB  
730  C CG  . PRO   A 96  ? 1.01764 0.34802 1.10038 -0.08430 0.06218  0.06671  96  PRO   A CG  
731  C CD  . PRO   A 96  ? 1.01948 0.38711 1.12138 -0.05391 0.07244  0.08827  96  PRO   A CD  
732  N N   . LYS   A 97  ? 0.99922 0.41162 1.02915 -0.05338 0.07322  0.01387  97  LYS   A N   
733  C CA  . LYS   A 97  ? 1.01621 0.46539 1.02288 -0.05799 0.06931  -0.00504 97  LYS   A CA  
734  C C   . LYS   A 97  ? 1.01582 0.49454 1.02001 -0.02960 0.08183  -0.00813 97  LYS   A C   
735  O O   . LYS   A 97  ? 1.02364 0.54475 1.01599 -0.03106 0.07853  -0.01481 97  LYS   A O   
736  C CB  . LYS   A 97  ? 0.97049 0.47498 0.98657 -0.07939 0.05503  0.01039  97  LYS   A CB  
737  C CG  . LYS   A 97  ? 1.09267 0.57920 1.10267 -0.11238 0.04030  0.00441  97  LYS   A CG  
738  C CD  . LYS   A 97  ? 1.12576 0.66416 1.15873 -0.13008 0.03006  0.03041  97  LYS   A CD  
739  C CE  . LYS   A 97  ? 1.23405 0.75203 1.26972 -0.16412 0.01563  0.03069  97  LYS   A CE  
740  N NZ  . LYS   A 97  ? 1.25815 0.83557 1.31487 -0.18203 0.00647  0.05319  97  LYS   A NZ  
741  N N   . THR   A 98  ? 0.99144 0.44966 1.00909 -0.00412 0.09586  -0.00157 98  THR   A N   
742  C CA  . THR   A 98  ? 0.97303 0.46245 0.99297 0.02155  0.10749  -0.00158 98  THR   A CA  
743  C C   . THR   A 98  ? 1.00310 0.48056 0.98931 0.02460  0.11407  -0.03344 98  THR   A C   
744  O O   . THR   A 98  ? 1.03175 0.45418 0.99706 0.02355  0.12002  -0.05603 98  THR   A O   
745  C CB  . THR   A 98  ? 0.99957 0.46952 1.04433 0.04859  0.12146  0.01317  98  THR   A CB  
746  O OG1 . THR   A 98  ? 0.98531 0.47101 1.05966 0.04515  0.11408  0.04570  98  THR   A OG1 
747  C CG2 . THR   A 98  ? 0.96093 0.46966 1.01140 0.07262  0.13235  0.01513  98  THR   A CG2 
748  N N   . PRO   A 99  ? 1.00305 0.52806 0.98061 0.02739  0.11313  -0.03634 99  PRO   A N   
749  C CA  . PRO   A 99  ? 1.00146 0.51852 0.94582 0.03040  0.11976  -0.06372 99  PRO   A CA  
750  C C   . PRO   A 99  ? 0.99391 0.50911 0.94144 0.06013  0.14020  -0.06701 99  PRO   A C   
751  O O   . PRO   A 99  ? 0.99120 0.51526 0.97010 0.07859  0.14777  -0.04648 99  PRO   A O   
752  C CB  . PRO   A 99  ? 0.99495 0.56635 0.93301 0.01776  0.10764  -0.06021 99  PRO   A CB  
753  C CG  . PRO   A 99  ? 0.92845 0.54134 0.89904 0.02248  0.10366  -0.03149 99  PRO   A CG  
754  C CD  . PRO   A 99  ? 0.90164 0.48716 0.89505 0.02356  0.10407  -0.01584 99  PRO   A CD  
755  N N   . LYS   A 100 ? 0.99448 0.50096 0.91041 0.06477  0.14932  -0.09105 100 LYS   A N   
756  C CA  . LYS   A 100 ? 1.01001 0.53351 0.93053 0.09148  0.16853  -0.09084 100 LYS   A CA  
757  C C   . LYS   A 100 ? 0.96702 0.55581 0.90792 0.09185  0.16130  -0.06921 100 LYS   A C   
758  O O   . LYS   A 100 ? 1.01228 0.62838 0.93709 0.07558  0.14932  -0.07288 100 LYS   A O   
759  C CB  . LYS   A 100 ? 1.11454 0.61757 0.99205 0.09379  0.17978  -0.12091 100 LYS   A CB  
760  C CG  . LYS   A 100 ? 1.23251 0.67289 1.07422 0.07915  0.17745  -0.14869 100 LYS   A CG  
761  C CD  . LYS   A 100 ? 1.32675 0.70994 1.16723 0.10220  0.19977  -0.16109 100 LYS   A CD  
762  C CE  . LYS   A 100 ? 1.38091 0.75512 1.18810 0.12047  0.22228  -0.18471 100 LYS   A CE  
763  N NZ  . LYS   A 100 ? 1.40820 0.77314 1.16134 0.09696  0.21258  -0.21200 100 LYS   A NZ  
764  N N   . TYR   A 101 ? 0.92740 0.54058 0.90408 0.10928  0.16719  -0.04583 101 TYR   A N   
765  C CA  . TYR   A 101 ? 0.90377 0.57336 0.89940 0.10605  0.15751  -0.02499 101 TYR   A CA  
766  C C   . TYR   A 101 ? 0.87527 0.57478 0.89292 0.12841  0.17114  -0.01241 101 TYR   A C   
767  O O   . TYR   A 101 ? 0.77043 0.45045 0.79634 0.14963  0.18926  -0.01519 101 TYR   A O   
768  C CB  . TYR   A 101 ? 0.88124 0.56199 0.90042 0.09582  0.14287  -0.00283 101 TYR   A CB  
769  C CG  . TYR   A 101 ? 0.85718 0.52777 0.90864 0.11218  0.14920  0.01716  101 TYR   A CG  
770  C CD1 . TYR   A 101 ? 0.81832 0.52832 0.89868 0.12583  0.15110  0.04009  101 TYR   A CD1 
771  C CD2 . TYR   A 101 ? 0.82581 0.44807 0.88021 0.11246  0.15152  0.01524  101 TYR   A CD2 
772  C CE1 . TYR   A 101 ? 0.74265 0.44789 0.85491 0.14093  0.15522  0.06183  101 TYR   A CE1 
773  C CE2 . TYR   A 101 ? 0.87742 0.49026 0.96357 0.12841  0.15684  0.03667  101 TYR   A CE2 
774  C CZ  . TYR   A 101 ? 0.84452 0.50099 0.96012 0.14332  0.15858  0.06072  101 TYR   A CZ  
775  O OH  . TYR   A 101 ? 0.94790 0.59883 1.09738 0.15959  0.16251  0.08518  101 TYR   A OH  
776  N N   . LYS   A 102 ? 0.79241 0.54000 0.82109 0.12305  0.16213  0.00237  102 LYS   A N   
777  C CA  . LYS   A 102 ? 0.76561 0.55070 0.81623 0.13800  0.17065  0.01673  102 LYS   A CA  
778  C C   . LYS   A 102 ? 0.75884 0.58615 0.82683 0.12687  0.15408  0.03767  102 LYS   A C   
779  O O   . LYS   A 102 ? 0.75958 0.59153 0.81273 0.10833  0.13944  0.03454  102 LYS   A O   
780  C CB  . LYS   A 102 ? 0.77728 0.57165 0.80546 0.14114  0.18155  0.00141  102 LYS   A CB  
781  C CG  . LYS   A 102 ? 0.78561 0.59623 0.83329 0.16458  0.20190  0.00852  102 LYS   A CG  
782  C CD  . LYS   A 102 ? 0.87809 0.70809 0.90420 0.16386  0.21043  -0.00153 102 LYS   A CD  
783  C CE  . LYS   A 102 ? 0.92274 0.72092 0.90203 0.15079  0.20812  -0.02867 102 LYS   A CE  
784  N NZ  . LYS   A 102 ? 1.05379 0.86505 1.00904 0.15455  0.22119  -0.03885 102 LYS   A NZ  
785  N N   . PHE   A 103 ? 0.70870 0.56712 0.80800 0.13839  0.15673  0.05895  103 PHE   A N   
786  C CA  . PHE   A 103 ? 0.68023 0.57929 0.79318 0.12748  0.14140  0.07756  103 PHE   A CA  
787  C C   . PHE   A 103 ? 0.69101 0.62344 0.80940 0.13049  0.14665  0.08060  103 PHE   A C   
788  O O   . PHE   A 103 ? 0.66016 0.60876 0.80323 0.14725  0.15919  0.09145  103 PHE   A O   
789  C CB  . PHE   A 103 ? 0.66559 0.57801 0.81053 0.13354  0.13568  0.10309  103 PHE   A CB  
790  C CG  . PHE   A 103 ? 0.68158 0.56576 0.82234 0.12739  0.12847  0.10491  103 PHE   A CG  
791  C CD1 . PHE   A 103 ? 0.72112 0.58079 0.83293 0.11202  0.12286  0.08699  103 PHE   A CD1 
792  C CD2 . PHE   A 103 ? 0.68232 0.56725 0.85079 0.13667  0.12705  0.12739  103 PHE   A CD2 
793  C CE1 . PHE   A 103 ? 0.75723 0.59409 0.86796 0.10474  0.11661  0.09106  103 PHE   A CE1 
794  C CE2 . PHE   A 103 ? 0.74155 0.60081 0.90706 0.12999  0.12076  0.13179  103 PHE   A CE2 
795  C CZ  . PHE   A 103 ? 0.75965 0.59507 0.89636 0.11337  0.11586  0.11342  103 PHE   A CZ  
796  N N   . VAL   A 104 ? 0.62396 0.56722 0.72166 0.11480  0.13781  0.07268  104 VAL   A N   
797  C CA  . VAL   A 104 ? 0.61919 0.59094 0.71921 0.11392  0.14134  0.07577  104 VAL   A CA  
798  C C   . VAL   A 104 ? 0.66290 0.65832 0.76342 0.09606  0.12306  0.08518  104 VAL   A C   
799  O O   . VAL   A 104 ? 0.65108 0.63413 0.73386 0.08331  0.11102  0.07843  104 VAL   A O   
800  C CB  . VAL   A 104 ? 0.65257 0.60815 0.72217 0.11348  0.15109  0.05504  104 VAL   A CB  
801  C CG1 . VAL   A 104 ? 0.66568 0.59710 0.70576 0.09881  0.13986  0.03934  104 VAL   A CG1 
802  C CG2 . VAL   A 104 ? 0.81852 0.80449 0.88972 0.10948  0.15292  0.06122  104 VAL   A CG2 
803  N N   . ARG   A 105 ? 0.61351 0.64277 0.73501 0.09504  0.12147  0.10097  105 ARG   A N   
804  C CA  . ARG   A 105 ? 0.58557 0.63310 0.70401 0.07686  0.10509  0.10724  105 ARG   A CA  
805  C C   . ARG   A 105 ? 0.56036 0.60598 0.65956 0.07023  0.10815  0.09678  105 ARG   A C   
806  O O   . ARG   A 105 ? 0.63464 0.69459 0.74235 0.07734  0.12044  0.10041  105 ARG   A O   
807  C CB  . ARG   A 105 ? 0.51680 0.60179 0.66795 0.07525  0.09897  0.13081  105 ARG   A CB  
808  C CG  . ARG   A 105 ? 0.55060 0.64986 0.69600 0.05402  0.08047  0.13592  105 ARG   A CG  
809  C CD  . ARG   A 105 ? 0.56815 0.70120 0.74261 0.04901  0.06881  0.15928  105 ARG   A CD  
810  N NE  . ARG   A 105 ? 0.61711 0.75610 0.77874 0.02625  0.04923  0.16044  105 ARG   A NE  
811  C CZ  . ARG   A 105 ? 0.61630 0.74845 0.76287 0.01583  0.03457  0.15968  105 ARG   A CZ  
812  N NH1 . ARG   A 105 ? 0.54675 0.66932 0.69239 0.02499  0.03608  0.16109  105 ARG   A NH1 
813  N NH2 . ARG   A 105 ? 0.59366 0.72664 0.72381 -0.00467 0.01862  0.15722  105 ARG   A NH2 
814  N N   . ILE   A 106 ? 0.62014 0.64948 0.69448 0.05781  0.09812  0.08542  106 ILE   A N   
815  C CA  . ILE   A 106 ? 0.65857 0.68458 0.71516 0.05174  0.09949  0.07783  106 ILE   A CA  
816  C C   . ILE   A 106 ? 0.67331 0.71931 0.73993 0.03913  0.09004  0.09002  106 ILE   A C   
817  O O   . ILE   A 106 ? 0.67062 0.73196 0.75400 0.03321  0.08062  0.10188  106 ILE   A O   
818  C CB  . ILE   A 106 ? 0.70232 0.70356 0.73175 0.04588  0.09363  0.06231  106 ILE   A CB  
819  C CG1 . ILE   A 106 ? 0.68355 0.67885 0.71154 0.03865  0.08123  0.06267  106 ILE   A CG1 
820  C CG2 . ILE   A 106 ? 0.76429 0.74658 0.77959 0.05474  0.10368  0.04900  106 ILE   A CG2 
821  C CD1 . ILE   A 106 ? 0.65945 0.65973 0.68335 0.02606  0.06965  0.06602  106 ILE   A CD1 
822  N N   . GLN   A 107 ? 0.67205 0.71704 0.72755 0.03346  0.09124  0.08794  107 GLN   A N   
823  C CA  . GLN   A 107 ? 0.65044 0.70954 0.71464 0.02003  0.08309  0.09935  107 GLN   A CA  
824  C C   . GLN   A 107 ? 0.68128 0.71779 0.72378 0.00878  0.07200  0.09055  107 GLN   A C   
825  O O   . GLN   A 107 ? 0.63812 0.65478 0.66074 0.01325  0.07380  0.07774  107 GLN   A O   
826  C CB  . GLN   A 107 ? 0.70709 0.78522 0.78009 0.02305  0.09536  0.10859  107 GLN   A CB  
827  C CG  . GLN   A 107 ? 0.77368 0.87822 0.87261 0.03604  0.10881  0.11945  107 GLN   A CG  
828  C CD  . GLN   A 107 ? 0.97193 1.10391 1.08486 0.03599  0.11998  0.13344  107 GLN   A CD  
829  O OE1 . GLN   A 107 ? 1.08270 1.22027 1.19195 0.05029  0.13883  0.13082  107 GLN   A OE1 
830  N NE2 . GLN   A 107 ? 0.99387 1.14238 1.12141 0.01888  0.10877  0.14829  107 GLN   A NE2 
831  N N   . PRO   A 108 ? 0.68410 0.72233 0.73059 -0.00600 0.06016  0.09725  108 PRO   A N   
832  C CA  . PRO   A 108 ? 0.65703 0.66961 0.68345 -0.01431 0.05205  0.08864  108 PRO   A CA  
833  C C   . PRO   A 108 ? 0.62973 0.63404 0.64501 -0.00904 0.05995  0.08622  108 PRO   A C   
834  O O   . PRO   A 108 ? 0.68221 0.70277 0.70560 -0.00726 0.06830  0.09569  108 PRO   A O   
835  C CB  . PRO   A 108 ? 0.61570 0.63238 0.65096 -0.03195 0.04041  0.09850  108 PRO   A CB  
836  C CG  . PRO   A 108 ? 0.66843 0.71397 0.72646 -0.03419 0.03770  0.11037  108 PRO   A CG  
837  C CD  . PRO   A 108 ? 0.64972 0.71277 0.71989 -0.01632 0.05329  0.11335  108 PRO   A CD  
838  N N   . GLY   A 109 ? 0.60729 0.58935 0.60415 -0.00600 0.05772  0.07482  109 GLY   A N   
839  C CA  . GLY   A 109 ? 0.60947 0.58474 0.59478 -0.00138 0.06231  0.07361  109 GLY   A CA  
840  C C   . GLY   A 109 ? 0.61685 0.59357 0.59246 0.00966  0.06956  0.06461  109 GLY   A C   
841  O O   . GLY   A 109 ? 0.67935 0.64746 0.64201 0.01251  0.06889  0.06041  109 GLY   A O   
842  N N   . GLN   A 110 ? 0.66532 0.65189 0.64767 0.01539  0.07562  0.06231  110 GLN   A N   
843  C CA  . GLN   A 110 ? 0.66113 0.64306 0.63265 0.02383  0.08173  0.05195  110 GLN   A CA  
844  C C   . GLN   A 110 ? 0.66863 0.63636 0.63289 0.02350  0.07466  0.04253  110 GLN   A C   
845  O O   . GLN   A 110 ? 0.61928 0.58245 0.58784 0.01959  0.06782  0.04287  110 GLN   A O   
846  C CB  . GLN   A 110 ? 0.66325 0.65395 0.64563 0.03133  0.09089  0.05223  110 GLN   A CB  
847  C CG  . GLN   A 110 ? 0.71998 0.73085 0.71503 0.03316  0.09982  0.06385  110 GLN   A CG  
848  C CD  . GLN   A 110 ? 0.76907 0.78588 0.77037 0.04571  0.11381  0.06168  110 GLN   A CD  
849  O OE1 . GLN   A 110 ? 0.81883 0.84318 0.84024 0.05010  0.11473  0.06720  110 GLN   A OE1 
850  N NE2 . GLN   A 110 ? 0.89597 0.90812 0.87858 0.05212  0.12495  0.05348  110 GLN   A NE2 
851  N N   . THR   A 111 ? 0.64699 0.60899 0.59893 0.02673  0.07654  0.03419  111 THR   A N   
852  C CA  . THR   A 111 ? 0.66916 0.62293 0.61677 0.02575  0.07057  0.02753  111 THR   A CA  
853  C C   . THR   A 111 ? 0.62658 0.57502 0.57413 0.02805  0.07366  0.02032  111 THR   A C   
854  O O   . THR   A 111 ? 0.69966 0.64664 0.64572 0.03212  0.08130  0.01778  111 THR   A O   
855  C CB  . THR   A 111 ? 0.69743 0.65096 0.63369 0.02461  0.06672  0.02663  111 THR   A CB  
856  O OG1 . THR   A 111 ? 0.71242 0.66856 0.63551 0.02524  0.07130  0.02365  111 THR   A OG1 
857  C CG2 . THR   A 111 ? 0.70075 0.65432 0.63930 0.02323  0.06324  0.03525  111 THR   A CG2 
858  N N   . PHE   A 112 ? 0.64447 0.58891 0.59410 0.02588  0.06877  0.01755  112 PHE   A N   
859  C CA  . PHE   A 112 ? 0.62703 0.56376 0.57800 0.02578  0.07020  0.01257  112 PHE   A CA  
860  C C   . PHE   A 112 ? 0.63953 0.57730 0.59152 0.02122  0.06412  0.01158  112 PHE   A C   
861  O O   . PHE   A 112 ? 0.62474 0.56919 0.57884 0.02103  0.06088  0.01496  112 PHE   A O   
862  C CB  . PHE   A 112 ? 0.59897 0.53516 0.56267 0.02923  0.07363  0.01769  112 PHE   A CB  
863  C CG  . PHE   A 112 ? 0.61050 0.55490 0.58145 0.02688  0.06873  0.02508  112 PHE   A CG  
864  C CD1 . PHE   A 112 ? 0.59332 0.53739 0.56534 0.02382  0.06493  0.02609  112 PHE   A CD1 
865  C CD2 . PHE   A 112 ? 0.63761 0.59012 0.61257 0.02630  0.06788  0.03103  112 PHE   A CD2 
866  C CE1 . PHE   A 112 ? 0.59996 0.54985 0.57224 0.02114  0.06099  0.03070  112 PHE   A CE1 
867  C CE2 . PHE   A 112 ? 0.60906 0.56561 0.58584 0.02167  0.06191  0.03551  112 PHE   A CE2 
868  C CZ  . PHE   A 112 ? 0.67515 0.62948 0.64824 0.01955  0.05876  0.03423  112 PHE   A CZ  
869  N N   . SER   A 113 ? 0.66413 0.59444 0.61520 0.01762  0.06347  0.00707  113 SER   A N   
870  C CA  . SER   A 113 ? 0.61778 0.55307 0.57402 0.01197  0.05848  0.00858  113 SER   A CA  
871  C C   . SER   A 113 ? 0.59751 0.53294 0.56400 0.01219  0.06001  0.01468  113 SER   A C   
872  O O   . SER   A 113 ? 0.55819 0.48475 0.52841 0.01478  0.06339  0.01649  113 SER   A O   
873  C CB  . SER   A 113 ? 0.61532 0.54278 0.56586 0.00408  0.05493  0.00213  113 SER   A CB  
874  O OG  . SER   A 113 ? 0.69893 0.63288 0.63869 0.00145  0.05045  -0.00114 113 SER   A OG  
875  N N   . VAL   A 114 ? 0.54330 0.49055 0.51450 0.01041  0.05823  0.01914  114 VAL   A N   
876  C CA  . VAL   A 114 ? 0.55869 0.50974 0.53550 0.00960  0.05977  0.02602  114 VAL   A CA  
877  C C   . VAL   A 114 ? 0.53314 0.49028 0.51748 0.00251  0.05845  0.02968  114 VAL   A C   
878  O O   . VAL   A 114 ? 0.53252 0.50233 0.51992 0.00074  0.05682  0.02949  114 VAL   A O   
879  C CB  . VAL   A 114 ? 0.61611 0.57592 0.58826 0.01362  0.06105  0.02777  114 VAL   A CB  
880  C CG1 . VAL   A 114 ? 0.55479 0.52265 0.52790 0.01137  0.06296  0.03445  114 VAL   A CG1 
881  C CG2 . VAL   A 114 ? 0.53666 0.49074 0.50443 0.01658  0.06057  0.02722  114 VAL   A CG2 
882  N N   . LEU   A 115 ? 0.59998 0.54983 0.59007 -0.00170 0.05894  0.03531  115 LEU   A N   
883  C CA  . LEU   A 115 ? 0.52250 0.47843 0.52203 -0.01077 0.05765  0.04197  115 LEU   A CA  
884  C C   . LEU   A 115 ? 0.55205 0.52260 0.55338 -0.00964 0.06153  0.05272  115 LEU   A C   
885  O O   . LEU   A 115 ? 0.59985 0.56382 0.60180 -0.00953 0.06226  0.06022  115 LEU   A O   
886  C CB  . LEU   A 115 ? 0.56976 0.50317 0.57341 -0.01751 0.05563  0.04186  115 LEU   A CB  
887  C CG  . LEU   A 115 ? 0.57857 0.51710 0.59387 -0.03021 0.05299  0.05061  115 LEU   A CG  
888  C CD1 . LEU   A 115 ? 0.55048 0.50761 0.56945 -0.03722 0.04842  0.04786  115 LEU   A CD1 
889  C CD2 . LEU   A 115 ? 0.65503 0.56354 0.67369 -0.03747 0.05097  0.05045  115 LEU   A CD2 
890  N N   . ALA   A 116 ? 0.54321 0.53434 0.54461 -0.00787 0.06462  0.05411  116 ALA   A N   
891  C CA  . ALA   A 116 ? 0.54662 0.55229 0.54349 -0.00588 0.07039  0.06174  116 ALA   A CA  
892  C C   . ALA   A 116 ? 0.62679 0.64130 0.63506 -0.01540 0.07151  0.07534  116 ALA   A C   
893  O O   . ALA   A 116 ? 0.59358 0.61981 0.61559 -0.02205 0.07101  0.07899  116 ALA   A O   
894  C CB  . ALA   A 116 ? 0.59912 0.62116 0.59205 0.00166  0.07624  0.05736  116 ALA   A CB  
895  N N   . CYS   A 117 ? 0.61509 0.62637 0.61912 -0.01720 0.07215  0.08510  117 CYS   A N   
896  C CA  . CYS   A 117 ? 0.68025 0.69646 0.69549 -0.02708 0.07269  0.10108  117 CYS   A CA  
897  C C   . CYS   A 117 ? 0.62865 0.66687 0.63401 -0.02656 0.07960  0.11254  117 CYS   A C   
898  O O   . CYS   A 117 ? 0.62665 0.66752 0.61286 -0.01965 0.08142  0.10817  117 CYS   A O   
899  C CB  . CYS   A 117 ? 0.69588 0.68632 0.71714 -0.03020 0.06719  0.10674  117 CYS   A CB  
900  S SG  . CYS   A 117 ? 0.69695 0.65840 0.72726 -0.03403 0.06143  0.09407  117 CYS   A SG  
901  N N   . TYR   A 118 ? 0.70431 0.75833 0.72141 -0.03555 0.08315  0.12759  118 TYR   A N   
902  C CA  . TYR   A 118 ? 0.68896 0.76591 0.69573 -0.03658 0.09109  0.14138  118 TYR   A CA  
903  C C   . TYR   A 118 ? 0.66573 0.74415 0.68876 -0.04976 0.08940  0.16346  118 TYR   A C   
904  O O   . TYR   A 118 ? 0.65633 0.73621 0.70114 -0.05960 0.08771  0.16828  118 TYR   A O   
905  C CB  . TYR   A 118 ? 0.62032 0.72594 0.62394 -0.03095 0.10284  0.13726  118 TYR   A CB  
906  C CG  . TYR   A 118 ? 0.67042 0.76902 0.65700 -0.01753 0.10476  0.11657  118 TYR   A CG  
907  C CD1 . TYR   A 118 ? 0.65413 0.74694 0.61198 -0.01149 0.10639  0.10982  118 TYR   A CD1 
908  C CD2 . TYR   A 118 ? 0.63867 0.73529 0.63744 -0.01256 0.10342  0.10494  118 TYR   A CD2 
909  C CE1 . TYR   A 118 ? 0.66123 0.74306 0.60383 -0.00137 0.10733  0.09126  118 TYR   A CE1 
910  C CE2 . TYR   A 118 ? 0.67149 0.75896 0.65613 -0.00069 0.10502  0.08840  118 TYR   A CE2 
911  C CZ  . TYR   A 118 ? 0.65748 0.73566 0.61451 0.00459  0.10723  0.08118  118 TYR   A CZ  
912  O OH  . TYR   A 118 ? 0.67768 0.74250 0.62105 0.01437  0.10808  0.06496  118 TYR   A OH  
913  N N   . ASN   A 119 ? 0.67630 0.75363 0.68912 -0.05126 0.08836  0.17801  119 ASN   A N   
914  C CA  . ASN   A 119 ? 0.65903 0.73374 0.68671 -0.06315 0.08613  0.20231  119 ASN   A CA  
915  C C   . ASN   A 119 ? 0.69809 0.73845 0.74801 -0.06923 0.07717  0.20079  119 ASN   A C   
916  O O   . ASN   A 119 ? 0.67007 0.70530 0.73882 -0.08245 0.07564  0.21583  119 ASN   A O   
917  C CB  . ASN   A 119 ? 0.65736 0.76476 0.69306 -0.07235 0.09573  0.21796  119 ASN   A CB  
918  C CG  . ASN   A 119 ? 0.72183 0.86055 0.73105 -0.06598 0.10707  0.22120  119 ASN   A CG  
919  O OD1 . ASN   A 119 ? 0.73674 0.87829 0.72802 -0.06648 0.10601  0.23388  119 ASN   A OD1 
920  N ND2 . ASN   A 119 ? 0.71092 0.87300 0.71625 -0.05936 0.11813  0.20964  119 ASN   A ND2 
921  N N   . GLY   A 120 ? 0.68704 0.70245 0.73357 -0.06029 0.07181  0.18221  120 GLY   A N   
922  C CA  . GLY   A 120 ? 0.67213 0.65142 0.73326 -0.06355 0.06537  0.17645  120 GLY   A CA  
923  C C   . GLY   A 120 ? 0.70935 0.68429 0.77959 -0.07166 0.06324  0.16273  120 GLY   A C   
924  O O   . GLY   A 120 ? 0.76875 0.71098 0.84373 -0.07387 0.05793  0.15194  120 GLY   A O   
925  N N   . SER   A 121 ? 0.66100 0.66870 0.73355 -0.07593 0.06736  0.16319  121 SER   A N   
926  C CA  . SER   A 121 ? 0.68012 0.68967 0.76307 -0.08391 0.06316  0.15222  121 SER   A CA  
927  C C   . SER   A 121 ? 0.69919 0.71666 0.76985 -0.07074 0.06423  0.13215  121 SER   A C   
928  O O   . SER   A 121 ? 0.67129 0.70725 0.72936 -0.05852 0.07125  0.13014  121 SER   A O   
929  C CB  . SER   A 121 ? 0.69351 0.73822 0.79407 -0.09676 0.06646  0.16807  121 SER   A CB  
930  O OG  . SER   A 121 ? 0.74486 0.78497 0.85689 -0.10983 0.06627  0.19010  121 SER   A OG  
931  N N   . PRO   A 122 ? 0.73097 0.73260 0.80270 -0.07363 0.05709  0.11717  122 PRO   A N   
932  C CA  . PRO   A 122 ? 0.67750 0.68622 0.73843 -0.06162 0.05757  0.10095  122 PRO   A CA  
933  C C   . PRO   A 122 ? 0.64366 0.69136 0.71384 -0.06020 0.06190  0.10521  122 PRO   A C   
934  O O   . PRO   A 122 ? 0.73641 0.80397 0.82543 -0.07281 0.05990  0.11586  122 PRO   A O   
935  C CB  . PRO   A 122 ? 0.69228 0.67425 0.75077 -0.06799 0.04833  0.08680  122 PRO   A CB  
936  C CG  . PRO   A 122 ? 0.75285 0.70350 0.81608 -0.07911 0.04474  0.09182  122 PRO   A CG  
937  C CD  . PRO   A 122 ? 0.77918 0.75035 0.85766 -0.08785 0.04802  0.11328  122 PRO   A CD  
938  N N   . SER   A 123 ? 0.67682 0.73523 0.73537 -0.04456 0.06820  0.09763  123 SER   A N   
939  C CA  . SER   A 123 ? 0.71224 0.80398 0.77906 -0.03775 0.07480  0.09999  123 SER   A CA  
940  C C   . SER   A 123 ? 0.66242 0.75424 0.72964 -0.03155 0.06965  0.08850  123 SER   A C   
941  O O   . SER   A 123 ? 0.62709 0.74737 0.71060 -0.02984 0.07103  0.09370  123 SER   A O   
942  C CB  . SER   A 123 ? 0.74512 0.84683 0.79660 -0.02397 0.08745  0.10019  123 SER   A CB  
943  O OG  . SER   A 123 ? 0.84765 0.97628 0.90551 -0.01320 0.09658  0.10003  123 SER   A OG  
944  N N   . GLY   A 124 ? 0.62083 0.68441 0.67247 -0.02797 0.06401  0.07542  124 GLY   A N   
945  C CA  . GLY   A 124 ? 0.64054 0.70398 0.69037 -0.02308 0.05877  0.06665  124 GLY   A CA  
946  C C   . GLY   A 124 ? 0.55581 0.58891 0.58630 -0.01836 0.05587  0.05412  124 GLY   A C   
947  O O   . GLY   A 124 ? 0.54703 0.56227 0.56776 -0.01661 0.05855  0.05257  124 GLY   A O   
948  N N   . VAL   A 125 ? 0.56223 0.59329 0.58882 -0.01621 0.05033  0.04738  125 VAL   A N   
949  C CA  . VAL   A 125 ? 0.57470 0.58181 0.58431 -0.01204 0.04847  0.03681  125 VAL   A CA  
950  C C   . VAL   A 125 ? 0.52055 0.53454 0.52620 -0.00143 0.04904  0.03457  125 VAL   A C   
951  O O   . VAL   A 125 ? 0.56550 0.59956 0.58169 -0.00043 0.04621  0.03962  125 VAL   A O   
952  C CB  . VAL   A 125 ? 0.56030 0.55026 0.56384 -0.02356 0.04057  0.03022  125 VAL   A CB  
953  C CG1 . VAL   A 125 ? 0.57940 0.58206 0.58292 -0.02879 0.03186  0.02892  125 VAL   A CG1 
954  C CG2 . VAL   A 125 ? 0.59437 0.55825 0.58227 -0.01814 0.04353  0.02114  125 VAL   A CG2 
955  N N   . TYR   A 126 ? 0.53924 0.53793 0.53243 0.00640  0.05250  0.02927  126 TYR   A N   
956  C CA  . TYR   A 126 ? 0.57137 0.57058 0.56011 0.01514  0.05274  0.02797  126 TYR   A CA  
957  C C   . TYR   A 126 ? 0.58572 0.56612 0.56106 0.01664  0.05294  0.02231  126 TYR   A C   
958  O O   . TYR   A 126 ? 0.54703 0.51640 0.51866 0.01446  0.05492  0.02014  126 TYR   A O   
959  C CB  . TYR   A 126 ? 0.54391 0.54972 0.53597 0.02534  0.05986  0.03046  126 TYR   A CB  
960  C CG  . TYR   A 126 ? 0.56236 0.56037 0.54676 0.02609  0.06574  0.02853  126 TYR   A CG  
961  C CD1 . TYR   A 126 ? 0.57966 0.56075 0.55125 0.02743  0.06586  0.02387  126 TYR   A CD1 
962  C CD2 . TYR   A 126 ? 0.55541 0.56620 0.54559 0.02407  0.07036  0.03330  126 TYR   A CD2 
963  C CE1 . TYR   A 126 ? 0.56200 0.53911 0.52532 0.02622  0.06866  0.02351  126 TYR   A CE1 
964  C CE2 . TYR   A 126 ? 0.58323 0.58916 0.56318 0.02380  0.07470  0.03306  126 TYR   A CE2 
965  C CZ  . TYR   A 126 ? 0.60681 0.59588 0.57259 0.02464  0.07298  0.02789  126 TYR   A CZ  
966  O OH  . TYR   A 126 ? 0.58607 0.57332 0.54043 0.02256  0.07492  0.02897  126 TYR   A OH  
967  N N   . GLN   A 127 ? 0.58657 0.56591 0.55728 0.02085  0.05121  0.02244  127 GLN   A N   
968  C CA  . GLN   A 127 ? 0.60494 0.57175 0.56528 0.02175  0.05202  0.01971  127 GLN   A CA  
969  C C   . GLN   A 127 ? 0.64287 0.60207 0.60174 0.02678  0.05537  0.02063  127 GLN   A C   
970  O O   . GLN   A 127 ? 0.70445 0.66428 0.66578 0.03203  0.05649  0.02232  127 GLN   A O   
971  C CB  . GLN   A 127 ? 0.58921 0.55989 0.54346 0.02120  0.04775  0.02145  127 GLN   A CB  
972  C CG  . GLN   A 127 ? 0.66706 0.62890 0.61022 0.02117  0.05025  0.01982  127 GLN   A CG  
973  C CD  . GLN   A 127 ? 0.69663 0.65140 0.63176 0.01700  0.05264  0.01248  127 GLN   A CD  
974  O OE1 . GLN   A 127 ? 0.70665 0.65868 0.64469 0.01289  0.05149  0.00849  127 GLN   A OE1 
975  N NE2 . GLN   A 127 ? 0.76575 0.71652 0.69105 0.01843  0.05704  0.01113  127 GLN   A NE2 
976  N N   . CYS   A 128 ? 0.64299 0.59450 0.59821 0.02503  0.05693  0.01958  128 CYS   A N   
977  C CA  . CYS   A 128 ? 0.67462 0.61930 0.62779 0.02547  0.05751  0.02053  128 CYS   A CA  
978  C C   . CYS   A 128 ? 0.75272 0.69495 0.70491 0.02364  0.05747  0.02354  128 CYS   A C   
979  O O   . CYS   A 128 ? 0.66451 0.61027 0.61626 0.02361  0.05949  0.02372  128 CYS   A O   
980  C CB  . CYS   A 128 ? 0.62294 0.56815 0.57673 0.02301  0.05816  0.02024  128 CYS   A CB  
981  S SG  . CYS   A 128 ? 0.88930 0.83461 0.83793 0.02520  0.06016  0.01762  128 CYS   A SG  
982  N N   . ALA   A 129 ? 0.71482 0.65056 0.66578 0.02144  0.05571  0.02568  129 ALA   A N   
983  C CA  . ALA   A 129 ? 0.69403 0.63133 0.64800 0.01759  0.05545  0.03143  129 ALA   A CA  
984  C C   . ALA   A 129 ? 0.66629 0.60336 0.62303 0.01135  0.05193  0.03338  129 ALA   A C   
985  O O   . ALA   A 129 ? 0.77454 0.70285 0.72417 0.00907  0.04873  0.02896  129 ALA   A O   
986  C CB  . ALA   A 129 ? 0.67755 0.60784 0.62900 0.01711  0.05406  0.03579  129 ALA   A CB  
987  N N   . MET   A 130 ? 0.59566 0.54425 0.56225 0.00871  0.05276  0.04037  130 MET   A N   
988  C CA  . MET   A 130 ? 0.60730 0.56195 0.58015 0.00084  0.04708  0.04590  130 MET   A CA  
989  C C   . MET   A 130 ? 0.66381 0.61029 0.63473 -0.00851 0.04156  0.04911  130 MET   A C   
990  O O   . MET   A 130 ? 0.67597 0.62952 0.65538 -0.01046 0.04374  0.05725  130 MET   A O   
991  C CB  . MET   A 130 ? 0.67917 0.65323 0.66892 0.00350  0.05098  0.05488  130 MET   A CB  
992  C CG  . MET   A 130 ? 0.68534 0.67354 0.68717 -0.00524 0.04355  0.06504  130 MET   A CG  
993  S SD  . MET   A 130 ? 0.74890 0.73208 0.73917 -0.01068 0.03435  0.06107  130 MET   A SD  
994  C CE  . MET   A 130 ? 0.63931 0.63089 0.63994 0.00149  0.04160  0.06414  130 MET   A CE  
995  N N   . ARG   A 131 ? 0.70791 0.63769 0.66617 -0.01473 0.03509  0.04259  131 ARG   A N   
996  C CA  . ARG   A 131 ? 0.73005 0.64320 0.68384 -0.02453 0.02938  0.04348  131 ARG   A CA  
997  C C   . ARG   A 131 ? 0.71709 0.64560 0.68464 -0.03821 0.02231  0.05532  131 ARG   A C   
998  O O   . ARG   A 131 ? 0.69673 0.64636 0.67391 -0.04040 0.01971  0.06086  131 ARG   A O   
999  C CB  . ARG   A 131 ? 0.76073 0.64798 0.69398 -0.02742 0.02540  0.03073  131 ARG   A CB  
1000 C CG  . ARG   A 131 ? 0.78161 0.66092 0.70530 -0.01331 0.03328  0.02096  131 ARG   A CG  
1001 C CD  . ARG   A 131 ? 0.80765 0.67609 0.73441 -0.00414 0.03848  0.02211  131 ARG   A CD  
1002 N NE  . ARG   A 131 ? 0.86509 0.71733 0.79360 -0.01196 0.03424  0.02760  131 ARG   A NE  
1003 C CZ  . ARG   A 131 ? 0.86347 0.71127 0.79839 -0.00694 0.03685  0.03503  131 ARG   A CZ  
1004 N NH1 . ARG   A 131 ? 0.80240 0.66223 0.74148 0.00523  0.04249  0.03707  131 ARG   A NH1 
1005 N NH2 . ARG   A 131 ? 0.83027 0.66179 0.76731 -0.01594 0.03251  0.04198  131 ARG   A NH2 
1006 N N   . PRO   A 132 ? 0.71753 0.63779 0.68915 -0.04781 0.01883  0.06184  132 PRO   A N   
1007 C CA  . PRO   A 132 ? 0.70592 0.64544 0.69488 -0.06300 0.01150  0.07586  132 PRO   A CA  
1008 C C   . PRO   A 132 ? 0.68935 0.63272 0.67436 -0.07658 -0.00124 0.07422  132 PRO   A C   
1009 O O   . PRO   A 132 ? 0.69359 0.66588 0.69900 -0.08590 -0.00696 0.08852  132 PRO   A O   
1010 C CB  . PRO   A 132 ? 0.70623 0.62580 0.69455 -0.07338 0.00830  0.08072  132 PRO   A CB  
1011 C CG  . PRO   A 132 ? 0.74183 0.64752 0.72203 -0.05768 0.01854  0.07627  132 PRO   A CG  
1012 C CD  . PRO   A 132 ? 0.73433 0.63246 0.69988 -0.04440 0.02221  0.06090  132 PRO   A CD  
1013 N N   . ASN   A 133 ? 0.67463 0.59292 0.63422 -0.07790 -0.00567 0.05848  133 ASN   A N   
1014 C CA  . ASN   A 133 ? 0.70896 0.63309 0.65914 -0.09075 -0.01795 0.05651  133 ASN   A CA  
1015 C C   . ASN   A 133 ? 0.68674 0.63318 0.63953 -0.07910 -0.01384 0.05788  133 ASN   A C   
1016 O O   . ASN   A 133 ? 0.71840 0.66801 0.65755 -0.08705 -0.02283 0.05523  133 ASN   A O   
1017 C CB  . ASN   A 133 ? 0.76286 0.64702 0.67924 -0.09961 -0.02424 0.03800  133 ASN   A CB  
1018 C CG  . ASN   A 133 ? 0.77968 0.64054 0.67809 -0.08090 -0.01137 0.02270  133 ASN   A CG  
1019 O OD1 . ASN   A 133 ? 0.76322 0.63733 0.67442 -0.06394 0.00004  0.02632  133 ASN   A OD1 
1020 N ND2 . ASN   A 133 ? 0.86216 0.68830 0.73064 -0.08403 -0.01283 0.00534  133 ASN   A ND2 
1021 N N   . PHE   A 134 ? 0.67428 0.63435 0.64227 -0.06162 -0.00102 0.06214  134 PHE   A N   
1022 C CA  . PHE   A 134 ? 0.67724 0.65691 0.65320 -0.05069 0.00352  0.06633  134 PHE   A CA  
1023 C C   . PHE   A 134 ? 0.68545 0.64986 0.63735 -0.04594 0.00499  0.05352  134 PHE   A C   
1024 O O   . PHE   A 134 ? 0.68679 0.66544 0.64116 -0.04237 0.00462  0.05839  134 PHE   A O   
1025 C CB  . PHE   A 134 ? 0.62262 0.63338 0.61833 -0.05902 -0.00585 0.08306  134 PHE   A CB  
1026 C CG  . PHE   A 134 ? 0.62901 0.66321 0.65471 -0.06028 -0.00371 0.09872  134 PHE   A CG  
1027 C CD1 . PHE   A 134 ? 0.62181 0.67472 0.67012 -0.04384 0.00938  0.10719  134 PHE   A CD1 
1028 C CD2 . PHE   A 134 ? 0.66671 0.70270 0.69714 -0.07805 -0.01357 0.10460  134 PHE   A CD2 
1029 C CE1 . PHE   A 134 ? 0.64431 0.72127 0.71949 -0.04301 0.01455  0.12166  134 PHE   A CE1 
1030 C CE2 . PHE   A 134 ? 0.58516 0.64740 0.64551 -0.07943 -0.01003 0.12143  134 PHE   A CE2 
1031 C CZ  . PHE   A 134 ? 0.57575 0.66037 0.65848 -0.06077 0.00510  0.13010  134 PHE   A CZ  
1032 N N   . THR   A 135 ? 0.73149 0.66813 0.66179 -0.04506 0.00760  0.03894  135 THR   A N   
1033 C CA  . THR   A 135 ? 0.73459 0.65947 0.64570 -0.03662 0.01379  0.02737  135 THR   A CA  
1034 C C   . THR   A 135 ? 0.72736 0.64826 0.64632 -0.02143 0.02579  0.02443  135 THR   A C   
1035 O O   . THR   A 135 ? 0.71985 0.64279 0.65281 -0.01838 0.02864  0.02923  135 THR   A O   
1036 C CB  . THR   A 135 ? 0.71560 0.61292 0.59717 -0.04379 0.01033  0.01267  135 THR   A CB  
1037 O OG1 . THR   A 135 ? 0.72650 0.59969 0.60637 -0.03809 0.01608  0.00543  135 THR   A OG1 
1038 C CG2 . THR   A 135 ? 0.73733 0.63445 0.61071 -0.06376 -0.00482 0.01508  135 THR   A CG2 
1039 N N   . ILE   A 136 ? 0.70814 0.62648 0.61780 -0.01299 0.03243  0.01788  136 ILE   A N   
1040 C CA  . ILE   A 136 ? 0.72042 0.63614 0.63600 -0.00091 0.04155  0.01493  136 ILE   A CA  
1041 C C   . ILE   A 136 ? 0.74404 0.64688 0.64306 0.00480  0.04717  0.00442  136 ILE   A C   
1042 O O   . ILE   A 136 ? 0.73514 0.63603 0.61724 0.00131  0.04664  -0.00038 136 ILE   A O   
1043 C CB  . ILE   A 136 ? 0.75818 0.69133 0.68860 0.00476  0.04556  0.02145  136 ILE   A CB  
1044 C CG1 . ILE   A 136 ? 0.76158 0.70127 0.68563 0.00612  0.04804  0.02091  136 ILE   A CG1 
1045 C CG2 . ILE   A 136 ? 0.64334 0.58924 0.58916 0.00152  0.04240  0.03146  136 ILE   A CG2 
1046 C CD1 . ILE   A 136 ? 0.69384 0.64238 0.63063 0.01165  0.05299  0.02455  136 ILE   A CD1 
1047 N N   . LYS   A 137 ? 0.75528 0.65097 0.65896 0.01424  0.05307  0.00180  137 LYS   A N   
1048 C CA  . LYS   A 137 ? 0.80812 0.69392 0.70187 0.02355  0.06099  -0.00645 137 LYS   A CA  
1049 C C   . LYS   A 137 ? 0.92886 0.83540 0.83534 0.03176  0.06749  -0.00210 137 LYS   A C   
1050 O O   . LYS   A 137 ? 1.05233 0.96243 0.97053 0.04033  0.07115  0.00024  137 LYS   A O   
1051 C CB  . LYS   A 137 ? 0.88398 0.74774 0.77783 0.02924  0.06251  -0.00952 137 LYS   A CB  
1052 C CG  . LYS   A 137 ? 0.90316 0.74603 0.78916 0.01784  0.05429  -0.01091 137 LYS   A CG  
1053 C CD  . LYS   A 137 ? 0.97730 0.79477 0.86465 0.02375  0.05618  -0.01191 137 LYS   A CD  
1054 C CE  . LYS   A 137 ? 1.07023 0.90228 0.97866 0.02933  0.05618  0.00094  137 LYS   A CE  
1055 N NZ  . LYS   A 137 ? 0.96181 0.77353 0.87348 0.02576  0.05217  0.00687  137 LYS   A NZ  
1056 N N   . GLY   A 138 ? 0.85989 0.78135 0.76512 0.02773  0.06771  0.00090  138 GLY   A N   
1057 C CA  . GLY   A 138 ? 0.74482 0.68552 0.66285 0.03148  0.07234  0.00650  138 GLY   A CA  
1058 C C   . GLY   A 138 ? 0.73624 0.68341 0.64683 0.03791  0.08208  0.00349  138 GLY   A C   
1059 O O   . GLY   A 138 ? 0.75182 0.68503 0.64651 0.04321  0.08747  -0.00546 138 GLY   A O   
1060 N N   . SER   A 139 ? 0.71498 0.68270 0.63714 0.03735  0.08531  0.01110  139 SER   A N   
1061 C CA  . SER   A 139 ? 0.69852 0.68041 0.61766 0.04287  0.09625  0.01196  139 SER   A CA  
1062 C C   . SER   A 139 ? 0.67997 0.67627 0.59832 0.03383  0.09520  0.02099  139 SER   A C   
1063 O O   . SER   A 139 ? 0.68697 0.69415 0.62401 0.02851  0.09136  0.03028  139 SER   A O   
1064 C CB  . SER   A 139 ? 0.67999 0.67875 0.62168 0.05132  0.10182  0.01696  139 SER   A CB  
1065 O OG  . SER   A 139 ? 0.66130 0.68081 0.60543 0.05594  0.11346  0.02123  139 SER   A OG  
1066 N N   . PHE   A 140 ? 0.67765 0.67245 0.57280 0.03139  0.09823  0.01856  140 PHE   A N   
1067 C CA  . PHE   A 140 ? 0.68671 0.69358 0.57873 0.02208  0.09534  0.02968  140 PHE   A CA  
1068 C C   . PHE   A 140 ? 0.73948 0.75637 0.60793 0.02345  0.10559  0.02884  140 PHE   A C   
1069 O O   . PHE   A 140 ? 0.81140 0.81497 0.65342 0.02733  0.10975  0.01551  140 PHE   A O   
1070 C CB  . PHE   A 140 ? 0.70816 0.70374 0.59373 0.01345  0.08259  0.03148  140 PHE   A CB  
1071 C CG  . PHE   A 140 ? 0.66054 0.65004 0.56871 0.01213  0.07486  0.03481  140 PHE   A CG  
1072 C CD1 . PHE   A 140 ? 0.61813 0.61516 0.54741 0.01021  0.07452  0.04430  140 PHE   A CD1 
1073 C CD2 . PHE   A 140 ? 0.65226 0.62734 0.55878 0.01195  0.06844  0.02822  140 PHE   A CD2 
1074 C CE1 . PHE   A 140 ? 0.69502 0.68322 0.63953 0.00966  0.06908  0.04453  140 PHE   A CE1 
1075 C CE2 . PHE   A 140 ? 0.66243 0.63375 0.58688 0.01177  0.06376  0.03109  140 PHE   A CE2 
1076 C CZ  . PHE   A 140 ? 0.61379 0.59059 0.55528 0.01140  0.06464  0.03794  140 PHE   A CZ  
1077 N N   . LEU   A 141 ? 0.68163 0.72015 0.55759 0.01936  0.10982  0.04298  141 LEU   A N   
1078 C CA  . LEU   A 141 ? 0.72777 0.78105 0.58074 0.01947  0.12058  0.04574  141 LEU   A CA  
1079 C C   . LEU   A 141 ? 0.73727 0.79862 0.58326 0.00700  0.11210  0.06128  141 LEU   A C   
1080 O O   . LEU   A 141 ? 0.73673 0.79034 0.59721 0.00044  0.09893  0.06869  141 LEU   A O   
1081 C CB  . LEU   A 141 ? 0.70363 0.78196 0.57428 0.02647  0.13576  0.05274  141 LEU   A CB  
1082 C CG  . LEU   A 141 ? 0.76410 0.84091 0.65095 0.04013  0.14349  0.04307  141 LEU   A CG  
1083 C CD1 . LEU   A 141 ? 0.75450 0.86294 0.67393 0.04159  0.15139  0.05781  141 LEU   A CD1 
1084 C CD2 . LEU   A 141 ? 0.75559 0.82040 0.61320 0.05334  0.15693  0.02567  141 LEU   A CD2 
1085 N N   . ASN   A 142 ? 0.77442 0.85233 0.59802 0.00494  0.12080  0.06731  142 ASN   A N   
1086 C CA  . ASN   A 142 ? 0.77500 0.86385 0.59131 -0.00663 0.11306  0.08578  142 ASN   A CA  
1087 C C   . ASN   A 142 ? 0.75849 0.85522 0.61293 -0.01194 0.10845  0.10591  142 ASN   A C   
1088 O O   . ASN   A 142 ? 0.77805 0.88526 0.65631 -0.00947 0.11654  0.10987  142 ASN   A O   
1089 C CB  . ASN   A 142 ? 0.72809 0.83689 0.51269 -0.00749 0.12583  0.08991  142 ASN   A CB  
1090 C CG  . ASN   A 142 ? 0.76699 0.86177 0.50656 -0.00421 0.12936  0.06785  142 ASN   A CG  
1091 O OD1 . ASN   A 142 ? 0.96892 1.04708 0.70533 0.00641  0.13653  0.04751  142 ASN   A OD1 
1092 N ND2 . ASN   A 142 ? 0.78399 0.88370 0.48725 -0.01399 0.12363  0.07203  142 ASN   A ND2 
1093 N N   . GLY   A 143 ? 0.77291 0.86369 0.63410 -0.01951 0.09492  0.11893  143 GLY   A N   
1094 C CA  . GLY   A 143 ? 0.77391 0.86272 0.66907 -0.02399 0.09014  0.13555  143 GLY   A CA  
1095 C C   . GLY   A 143 ? 0.69347 0.76133 0.61351 -0.02028 0.08401  0.12542  143 GLY   A C   
1096 O O   . GLY   A 143 ? 0.76890 0.82849 0.71369 -0.02402 0.07972  0.13595  143 GLY   A O   
1097 N N   . SER   A 144 ? 0.65474 0.71175 0.56726 -0.01340 0.08384  0.10539  144 SER   A N   
1098 C CA  . SER   A 144 ? 0.65248 0.69182 0.58483 -0.01017 0.07853  0.09656  144 SER   A CA  
1099 C C   . SER   A 144 ? 0.62397 0.64992 0.56162 -0.01105 0.06783  0.10034  144 SER   A C   
1100 O O   . SER   A 144 ? 0.55691 0.56867 0.51139 -0.00845 0.06486  0.09568  144 SER   A O   
1101 C CB  . SER   A 144 ? 0.65902 0.69240 0.58309 -0.00248 0.08215  0.07717  144 SER   A CB  
1102 O OG  . SER   A 144 ? 0.66988 0.69712 0.56901 -0.00155 0.07924  0.06855  144 SER   A OG  
1103 N N   . CYS   A 145 ? 0.64964 0.68207 0.57331 -0.01444 0.06226  0.10929  145 CYS   A N   
1104 C CA  . CYS   A 145 ? 0.60688 0.63276 0.54020 -0.01411 0.05224  0.11572  145 CYS   A CA  
1105 C C   . CYS   A 145 ? 0.58384 0.60007 0.54531 -0.01258 0.05152  0.12850  145 CYS   A C   
1106 O O   . CYS   A 145 ? 0.59919 0.61728 0.56829 -0.01631 0.05509  0.13993  145 CYS   A O   
1107 C CB  . CYS   A 145 ? 0.65762 0.69780 0.57210 -0.02001 0.04455  0.12701  145 CYS   A CB  
1108 S SG  . CYS   A 145 ? 0.81745 0.85850 0.69491 -0.02324 0.04316  0.10724  145 CYS   A SG  
1109 N N   . GLY   A 146 ? 0.56272 0.56720 0.53955 -0.00710 0.04778  0.12642  146 GLY   A N   
1110 C CA  . GLY   A 146 ? 0.53312 0.52063 0.53381 -0.00307 0.04938  0.13238  146 GLY   A CA  
1111 C C   . GLY   A 146 ? 0.54506 0.51566 0.55109 -0.00107 0.05463  0.11530  146 GLY   A C   
1112 O O   . GLY   A 146 ? 0.60313 0.55429 0.62410 0.00260  0.05628  0.11490  146 GLY   A O   
1113 N N   . SER   A 147 ? 0.48669 0.46353 0.48000 -0.00312 0.05735  0.10159  147 SER   A N   
1114 C CA  . SER   A 147 ? 0.51767 0.48277 0.51473 -0.00156 0.05992  0.08661  147 SER   A CA  
1115 C C   . SER   A 147 ? 0.57509 0.53079 0.57411 0.00555  0.05885  0.07839  147 SER   A C   
1116 O O   . SER   A 147 ? 0.53682 0.50099 0.53091 0.00796  0.05603  0.07995  147 SER   A O   
1117 C CB  . SER   A 147 ? 0.52002 0.49746 0.50616 -0.00291 0.06284  0.07712  147 SER   A CB  
1118 O OG  . SER   A 147 ? 0.61047 0.60131 0.59703 -0.00856 0.06617  0.08610  147 SER   A OG  
1119 N N   . VAL   A 148 ? 0.53841 0.47742 0.54373 0.00768  0.06101  0.07014  148 VAL   A N   
1120 C CA  . VAL   A 148 ? 0.62265 0.55378 0.63104 0.01549  0.06268  0.06469  148 VAL   A CA  
1121 C C   . VAL   A 148 ? 0.61035 0.54008 0.60909 0.01583  0.06380  0.04978  148 VAL   A C   
1122 O O   . VAL   A 148 ? 0.57508 0.50595 0.56849 0.01061  0.06286  0.04375  148 VAL   A O   
1123 C CB  . VAL   A 148 ? 0.56067 0.47083 0.58146 0.02056  0.06651  0.06752  148 VAL   A CB  
1124 C CG1 . VAL   A 148 ? 0.59342 0.50568 0.62627 0.02079  0.06459  0.08622  148 VAL   A CG1 
1125 C CG2 . VAL   A 148 ? 0.48452 0.37443 0.50124 0.01503  0.06794  0.05648  148 VAL   A CG2 
1126 N N   . GLY   A 149 ? 0.53984 0.47082 0.53835 0.02177  0.06545  0.04663  149 GLY   A N   
1127 C CA  . GLY   A 149 ? 0.60128 0.53014 0.59111 0.02293  0.06707  0.03532  149 GLY   A CA  
1128 C C   . GLY   A 149 ? 0.58849 0.50306 0.58026 0.02907  0.07344  0.03014  149 GLY   A C   
1129 O O   . GLY   A 149 ? 0.57937 0.49113 0.58277 0.03600  0.07755  0.03688  149 GLY   A O   
1130 N N   . PHE   A 150 ? 0.54509 0.45151 0.52486 0.02715  0.07461  0.01865  150 PHE   A N   
1131 C CA  . PHE   A 150 ? 0.65576 0.54334 0.63062 0.03189  0.08171  0.01016  150 PHE   A CA  
1132 C C   . PHE   A 150 ? 0.67181 0.55959 0.62866 0.03019  0.08254  -0.00074 150 PHE   A C   
1133 O O   . PHE   A 150 ? 0.69321 0.59226 0.64354 0.02374  0.07572  -0.00134 150 PHE   A O   
1134 C CB  . PHE   A 150 ? 0.64146 0.50680 0.61668 0.02683  0.08070  0.00663  150 PHE   A CB  
1135 C CG  . PHE   A 150 ? 0.62827 0.49540 0.59557 0.01375  0.07216  0.00213  150 PHE   A CG  
1136 C CD1 . PHE   A 150 ? 0.60890 0.49322 0.58502 0.00787  0.06625  0.01182  150 PHE   A CD1 
1137 C CD2 . PHE   A 150 ? 0.60284 0.45705 0.55362 0.00714  0.07019  -0.01113 150 PHE   A CD2 
1138 C CE1 . PHE   A 150 ? 0.57051 0.46239 0.54460 -0.00279 0.05961  0.01029  150 PHE   A CE1 
1139 C CE2 . PHE   A 150 ? 0.62757 0.48920 0.57531 -0.00596 0.06060  -0.01239 150 PHE   A CE2 
1140 C CZ  . PHE   A 150 ? 0.62585 0.50799 0.58809 -0.01018 0.05583  -0.00066 150 PHE   A CZ  
1141 N N   . ASN   A 151 ? 0.63639 0.51224 0.58515 0.03720  0.09187  -0.00832 151 ASN   A N   
1142 C CA  . ASN   A 151 ? 0.67298 0.54435 0.59863 0.03469  0.09357  -0.02025 151 ASN   A CA  
1143 C C   . ASN   A 151 ? 0.75828 0.59912 0.66919 0.03409  0.09843  -0.03488 151 ASN   A C   
1144 O O   . ASN   A 151 ? 0.80597 0.62869 0.72784 0.04072  0.10476  -0.03445 151 ASN   A O   
1145 C CB  . ASN   A 151 ? 0.70459 0.58994 0.62786 0.04339  0.10262  -0.01728 151 ASN   A CB  
1146 C CG  . ASN   A 151 ? 0.65710 0.56650 0.58832 0.04021  0.09598  -0.00575 151 ASN   A CG  
1147 O OD1 . ASN   A 151 ? 0.70945 0.62519 0.62935 0.03340  0.08886  -0.00680 151 ASN   A OD1 
1148 N ND2 . ASN   A 151 ? 0.67312 0.59516 0.62421 0.04472  0.09756  0.00598  151 ASN   A ND2 
1149 N N   . ILE   A 152 ? 0.78150 0.61491 0.66642 0.02569  0.09488  -0.04763 152 ILE   A N   
1150 C CA  . ILE   A 152 ? 0.90931 0.70917 0.77257 0.02231  0.09840  -0.06537 152 ILE   A CA  
1151 C C   . ILE   A 152 ? 0.95685 0.75376 0.78950 0.02602  0.10704  -0.07800 152 ILE   A C   
1152 O O   . ILE   A 152 ? 0.94130 0.75865 0.75989 0.01898  0.09991  -0.07629 152 ILE   A O   
1153 C CB  . ILE   A 152 ? 0.84605 0.63688 0.70246 0.00318  0.08282  -0.07035 152 ILE   A CB  
1154 C CG1 . ILE   A 152 ? 0.79557 0.58263 0.67957 0.00052  0.07851  -0.05920 152 ILE   A CG1 
1155 C CG2 . ILE   A 152 ? 0.96298 0.71874 0.78765 -0.00457 0.08384  -0.09187 152 ILE   A CG2 
1156 C CD1 . ILE   A 152 ? 0.74446 0.53955 0.63230 -0.01797 0.06292  -0.05595 152 ILE   A CD1 
1157 N N   . ASP   A 153 ? 0.99438 0.76607 0.81654 0.03812  0.12340  -0.08969 153 ASP   A N   
1158 C CA  . ASP   A 153 ? 1.07457 0.83872 0.86203 0.04264  0.13510  -0.10476 153 ASP   A CA  
1159 C C   . ASP   A 153 ? 1.07870 0.79647 0.83568 0.03709  0.13761  -0.12917 153 ASP   A C   
1160 O O   . ASP   A 153 ? 1.07822 0.76514 0.84210 0.04956  0.15098  -0.13602 153 ASP   A O   
1161 C CB  . ASP   A 153 ? 1.14610 0.92284 0.94601 0.06420  0.15616  -0.09804 153 ASP   A CB  
1162 C CG  . ASP   A 153 ? 1.25157 1.06588 1.08961 0.06865  0.15256  -0.07319 153 ASP   A CG  
1163 O OD1 . ASP   A 153 ? 1.34110 1.16313 1.20418 0.08445  0.16551  -0.06349 153 ASP   A OD1 
1164 O OD2 . ASP   A 153 ? 1.08519 0.92082 0.92824 0.05647  0.13683  -0.06334 153 ASP   A OD2 
1165 N N   . TYR   A 154 ? 1.11090 0.82300 0.83390 0.01825  0.12442  -0.14184 154 TYR   A N   
1166 C CA  . TYR   A 154 ? 1.19605 0.86316 0.88679 0.00549  0.12054  -0.16585 154 TYR   A CA  
1167 C C   . TYR   A 154 ? 1.25086 0.89177 0.96839 0.00027  0.11400  -0.16299 154 TYR   A C   
1168 O O   . TYR   A 154 ? 1.25749 0.90959 0.98785 -0.01844 0.09422  -0.15448 154 TYR   A O   
1169 C CB  . TYR   A 154 ? 1.23721 0.87051 0.89280 0.01973  0.14317  -0.18873 154 TYR   A CB  
1170 C CG  . TYR   A 154 ? 1.35574 0.93467 0.97058 0.00538  0.13955  -0.21780 154 TYR   A CG  
1171 C CD1 . TYR   A 154 ? 1.37525 0.94908 0.97798 -0.02379 0.11371  -0.22198 154 TYR   A CD1 
1172 C CD2 . TYR   A 154 ? 1.40525 0.93753 0.99406 0.02070  0.16218  -0.24109 154 TYR   A CD2 
1173 C CE1 . TYR   A 154 ? 1.33697 0.85947 0.90168 -0.04059 0.10809  -0.24878 154 TYR   A CE1 
1174 C CE2 . TYR   A 154 ? 1.44458 0.92039 0.99228 0.00633  0.15869  -0.27029 154 TYR   A CE2 
1175 C CZ  . TYR   A 154 ? 1.46983 0.94043 1.00485 -0.02604 0.13035  -0.27418 154 TYR   A CZ  
1176 O OH  . TYR   A 154 ? 1.53659 0.94958 1.02982 -0.04394 0.12460  -0.30347 154 TYR   A OH  
1177 N N   . ASP   A 155 ? 1.23176 0.83914 0.95929 0.01726  0.13119  -0.16828 155 ASP   A N   
1178 C CA  . ASP   A 155 ? 1.20242 0.77881 0.95270 0.01294  0.12655  -0.16519 155 ASP   A CA  
1179 C C   . ASP   A 155 ? 1.19445 0.78617 0.99134 0.03219  0.13537  -0.14199 155 ASP   A C   
1180 O O   . ASP   A 155 ? 1.17169 0.74245 0.99082 0.02941  0.13137  -0.13448 155 ASP   A O   
1181 C CB  . ASP   A 155 ? 1.38807 0.89965 1.10803 0.01330  0.13635  -0.19232 155 ASP   A CB  
1182 C CG  . ASP   A 155 ? 1.34110 0.83277 1.06018 0.04426  0.16523  -0.19950 155 ASP   A CG  
1183 O OD1 . ASP   A 155 ? 1.33189 0.86222 1.05752 0.06085  0.17715  -0.19013 155 ASP   A OD1 
1184 O OD2 . ASP   A 155 ? 1.25205 0.68901 0.96565 0.05218  0.17649  -0.21361 155 ASP   A OD2 
1185 N N   . CYS   A 156 ? 1.14677 0.77512 0.95902 0.04981  0.14604  -0.12898 156 CYS   A N   
1186 C CA  . CYS   A 156 ? 1.05774 0.70274 0.91213 0.06724  0.15349  -0.10696 156 CYS   A CA  
1187 C C   . CYS   A 156 ? 0.96074 0.65447 0.83967 0.05988  0.13941  -0.08438 156 CYS   A C   
1188 O O   . CYS   A 156 ? 0.98241 0.70705 0.85122 0.05532  0.13513  -0.08271 156 CYS   A O   
1189 C CB  . CYS   A 156 ? 0.99872 0.64979 0.85772 0.09299  0.17663  -0.10683 156 CYS   A CB  
1190 S SG  . CYS   A 156 ? 1.06591 0.75769 0.97866 0.10930  0.17953  -0.07414 156 CYS   A SG  
1191 N N   . VAL   A 157 ? 0.89668 0.59525 0.80632 0.05945  0.13317  -0.06688 157 VAL   A N   
1192 C CA  . VAL   A 157 ? 0.90900 0.64827 0.83914 0.05294  0.12104  -0.04731 157 VAL   A CA  
1193 C C   . VAL   A 157 ? 0.84271 0.60907 0.79794 0.06981  0.12948  -0.03049 157 VAL   A C   
1194 O O   . VAL   A 157 ? 0.90823 0.66381 0.88342 0.08369  0.13842  -0.02240 157 VAL   A O   
1195 C CB  . VAL   A 157 ? 0.81767 0.55036 0.76304 0.04060  0.10902  -0.03720 157 VAL   A CB  
1196 C CG1 . VAL   A 157 ? 0.77166 0.54465 0.73492 0.03675  0.09980  -0.01855 157 VAL   A CG1 
1197 C CG2 . VAL   A 157 ? 0.81157 0.52349 0.73593 0.02080  0.09865  -0.05141 157 VAL   A CG2 
1198 N N   . SER   A 158 ? 0.74835 0.54992 0.70438 0.06797  0.12575  -0.02372 158 SER   A N   
1199 C CA  . SER   A 158 ? 0.71733 0.54859 0.69706 0.07898  0.13019  -0.00676 158 SER   A CA  
1200 C C   . SER   A 158 ? 0.74575 0.59872 0.74095 0.06947  0.11594  0.00884  158 SER   A C   
1201 O O   . SER   A 158 ? 0.71517 0.58401 0.70139 0.05870  0.10653  0.00843  158 SER   A O   
1202 C CB  . SER   A 158 ? 0.70280 0.55506 0.67197 0.08196  0.13619  -0.00949 158 SER   A CB  
1203 O OG  . SER   A 158 ? 0.84972 0.68443 0.80490 0.09377  0.15284  -0.02243 158 SER   A OG  
1204 N N   . PHE   A 159 ? 0.72416 0.57652 0.74125 0.07415  0.11496  0.02275  159 PHE   A N   
1205 C CA  . PHE   A 159 ? 0.67552 0.54861 0.70366 0.06577  0.10277  0.03767  159 PHE   A CA  
1206 C C   . PHE   A 159 ? 0.70630 0.61157 0.74719 0.06910  0.10130  0.05009  159 PHE   A C   
1207 O O   . PHE   A 159 ? 0.69403 0.60869 0.75495 0.08090  0.10788  0.06098  159 PHE   A O   
1208 C CB  . PHE   A 159 ? 0.74128 0.60224 0.78556 0.06784  0.10115  0.04992  159 PHE   A CB  
1209 C CG  . PHE   A 159 ? 0.75615 0.58703 0.78980 0.05921  0.09910  0.04077  159 PHE   A CG  
1210 C CD1 . PHE   A 159 ? 0.68063 0.51843 0.70448 0.04368  0.08892  0.03949  159 PHE   A CD1 
1211 C CD2 . PHE   A 159 ? 0.77137 0.56666 0.80603 0.06646  0.10777  0.03386  159 PHE   A CD2 
1212 C CE1 . PHE   A 159 ? 0.77642 0.59097 0.79428 0.03339  0.08592  0.03361  159 PHE   A CE1 
1213 C CE2 . PHE   A 159 ? 0.77438 0.53987 0.79946 0.05518  0.10406  0.02572  159 PHE   A CE2 
1214 C CZ  . PHE   A 159 ? 0.79421 0.57174 0.81228 0.03751  0.09233  0.02673  159 PHE   A CZ  
1215 N N   . CYS   A 160 ? 0.65193 0.57388 0.68296 0.05855  0.09252  0.04930  160 CYS   A N   
1216 C CA  . CYS   A 160 ? 0.68143 0.62974 0.72130 0.05767  0.08921  0.05915  160 CYS   A CA  
1217 C C   . CYS   A 160 ? 0.72878 0.69154 0.76895 0.04741  0.07656  0.06834  160 CYS   A C   
1218 O O   . CYS   A 160 ? 0.78585 0.76922 0.83662 0.04539  0.07178  0.07940  160 CYS   A O   
1219 C CB  . CYS   A 160 ? 0.65567 0.60816 0.68158 0.05476  0.09140  0.04978  160 CYS   A CB  
1220 S SG  . CYS   A 160 ? 0.67191 0.61391 0.67351 0.04355  0.08396  0.03678  160 CYS   A SG  
1221 N N   . TYR   A 161 ? 0.65040 0.60431 0.67871 0.04020  0.07124  0.06439  161 TYR   A N   
1222 C CA  . TYR   A 161 ? 0.61533 0.58122 0.63642 0.03085  0.06160  0.06926  161 TYR   A CA  
1223 C C   . TYR   A 161 ? 0.65710 0.61898 0.67759 0.02796  0.05904  0.07542  161 TYR   A C   
1224 O O   . TYR   A 161 ? 0.67209 0.61839 0.69215 0.02894  0.06312  0.07092  161 TYR   A O   
1225 C CB  . TYR   A 161 ? 0.57538 0.53887 0.57837 0.02470  0.05948  0.05716  161 TYR   A CB  
1226 C CG  . TYR   A 161 ? 0.59352 0.56416 0.58467 0.01671  0.05213  0.05844  161 TYR   A CG  
1227 C CD1 . TYR   A 161 ? 0.59913 0.57922 0.58820 0.01137  0.04578  0.06193  161 TYR   A CD1 
1228 C CD2 . TYR   A 161 ? 0.59487 0.56264 0.57577 0.01375  0.05202  0.05584  161 TYR   A CD2 
1229 C CE1 . TYR   A 161 ? 0.64022 0.62157 0.61249 0.00337  0.03940  0.05979  161 TYR   A CE1 
1230 C CE2 . TYR   A 161 ? 0.58247 0.55523 0.54827 0.00807  0.04799  0.05492  161 TYR   A CE2 
1231 C CZ  . TYR   A 161 ? 0.62792 0.60493 0.58706 0.00295  0.04163  0.05544  161 TYR   A CZ  
1232 O OH  . TYR   A 161 ? 0.60339 0.58025 0.54183 -0.00339 0.03791  0.05137  161 TYR   A OH  
1233 N N   . MET   A 162 ? 0.61263 0.58910 0.63160 0.02255  0.05153  0.08639  162 MET   A N   
1234 C CA  . MET   A 162 ? 0.59919 0.57629 0.61287 0.01784  0.04903  0.09356  162 MET   A CA  
1235 C C   . MET   A 162 ? 0.60141 0.59143 0.59542 0.00893  0.04237  0.09267  162 MET   A C   
1236 O O   . MET   A 162 ? 0.59489 0.59671 0.58710 0.00538  0.03546  0.09669  162 MET   A O   
1237 C CB  . MET   A 162 ? 0.55871 0.53912 0.59082 0.02209  0.04757  0.11263  162 MET   A CB  
1238 C CG  . MET   A 162 ? 0.57456 0.55923 0.59998 0.01552  0.04419  0.12386  162 MET   A CG  
1239 S SD  . MET   A 162 ? 0.68194 0.66830 0.73078 0.02088  0.04190  0.15031  162 MET   A SD  
1240 C CE  . MET   A 162 ? 0.60198 0.55984 0.65508 0.02052  0.04977  0.14693  162 MET   A CE  
1241 N N   . HIS   A 163 ? 0.53648 0.52448 0.51558 0.00490  0.04476  0.08733  163 HIS   A N   
1242 C CA  . HIS   A 163 ? 0.55341 0.54836 0.50905 -0.00130 0.04201  0.08156  163 HIS   A CA  
1243 C C   . HIS   A 163 ? 0.56108 0.57055 0.50744 -0.00774 0.03507  0.09546  163 HIS   A C   
1244 O O   . HIS   A 163 ? 0.56365 0.57833 0.51845 -0.00773 0.03534  0.11011  163 HIS   A O   
1245 C CB  . HIS   A 163 ? 0.59314 0.58450 0.53826 -0.00075 0.04960  0.07195  163 HIS   A CB  
1246 C CG  . HIS   A 163 ? 0.65779 0.65124 0.57763 -0.00350 0.05036  0.06252  163 HIS   A CG  
1247 N ND1 . HIS   A 163 ? 0.61067 0.59682 0.51926 -0.00517 0.04612  0.05268  163 HIS   A ND1 
1248 C CD2 . HIS   A 163 ? 0.61899 0.61904 0.52147 -0.00470 0.05595  0.06103  163 HIS   A CD2 
1249 C CE1 . HIS   A 163 ? 0.65304 0.63644 0.53659 -0.00694 0.04883  0.04347  163 HIS   A CE1 
1250 N NE2 . HIS   A 163 ? 0.71150 0.70467 0.59036 -0.00560 0.05583  0.04803  163 HIS   A NE2 
1251 N N   . HIS   A 164 ? 0.58685 0.60159 0.51392 -0.01461 0.02805  0.09114  164 HIS   A N   
1252 C CA  . HIS   A 164 ? 0.61775 0.64815 0.53057 -0.02341 0.01853  0.10337  164 HIS   A CA  
1253 C C   . HIS   A 164 ? 0.72215 0.75049 0.59686 -0.03114 0.01807  0.09045  164 HIS   A C   
1254 O O   . HIS   A 164 ? 0.76419 0.80426 0.61961 -0.03697 0.01583  0.09857  164 HIS   A O   
1255 C CB  . HIS   A 164 ? 0.63348 0.67539 0.56079 -0.02729 0.00639  0.11395  164 HIS   A CB  
1256 C CG  . HIS   A 164 ? 0.61405 0.66715 0.57309 -0.02070 0.00474  0.13580  164 HIS   A CG  
1257 N ND1 . HIS   A 164 ? 0.59447 0.63596 0.57995 -0.00859 0.01424  0.13569  164 HIS   A ND1 
1258 C CD2 . HIS   A 164 ? 0.61396 0.68729 0.58218 -0.02371 -0.00509 0.15868  164 HIS   A CD2 
1259 C CE1 . HIS   A 164 ? 0.61278 0.66326 0.62286 -0.00287 0.01205  0.15624  164 HIS   A CE1 
1260 N NE2 . HIS   A 164 ? 0.63520 0.70680 0.63784 -0.01136 0.00005  0.17222  164 HIS   A NE2 
1261 N N   . MET   A 165 ? 0.70582 0.71802 0.56766 -0.03083 0.02091  0.07082  165 MET   A N   
1262 C CA  . MET   A 165 ? 0.72439 0.72949 0.54865 -0.03946 0.01763  0.05755  165 MET   A CA  
1263 C C   . MET   A 165 ? 0.74382 0.72520 0.55832 -0.03365 0.02653  0.03593  165 MET   A C   
1264 O O   . MET   A 165 ? 0.76453 0.73801 0.60223 -0.02640 0.03018  0.03325  165 MET   A O   
1265 C CB  . MET   A 165 ? 0.73937 0.75153 0.55828 -0.05322 0.00012  0.06330  165 MET   A CB  
1266 C CG  . MET   A 165 ? 0.83940 0.84908 0.61467 -0.06669 -0.00737 0.05482  165 MET   A CG  
1267 S SD  . MET   A 165 ? 0.98494 1.00912 0.76253 -0.08587 -0.03173 0.06616  165 MET   A SD  
1268 C CE  . MET   A 165 ? 0.76662 0.79025 0.59401 -0.07734 -0.03023 0.07194  165 MET   A CE  
1269 N N   . GLU   A 166 ? 0.78781 0.75708 0.56603 -0.03647 0.03025  0.02084  166 GLU   A N   
1270 C CA  . GLU   A 166 ? 0.85574 0.79839 0.62136 -0.03056 0.03825  0.00031  166 GLU   A CA  
1271 C C   . GLU   A 166 ? 0.84279 0.76564 0.57666 -0.04417 0.02754  -0.01278 166 GLU   A C   
1272 O O   . GLU   A 166 ? 0.89338 0.82144 0.59664 -0.05563 0.02057  -0.01341 166 GLU   A O   
1273 C CB  . GLU   A 166 ? 0.89601 0.83677 0.64765 -0.01834 0.05631  -0.00851 166 GLU   A CB  
1274 C CG  . GLU   A 166 ? 0.96356 0.87751 0.70803 -0.00777 0.06685  -0.02726 166 GLU   A CG  
1275 C CD  . GLU   A 166 ? 0.94165 0.86099 0.67975 0.00693  0.08645  -0.03242 166 GLU   A CD  
1276 O OE1 . GLU   A 166 ? 1.07111 1.00342 0.78583 0.00473  0.09200  -0.03116 166 GLU   A OE1 
1277 O OE2 . GLU   A 166 ? 0.99952 0.91359 0.75717 0.02065  0.09635  -0.03568 166 GLU   A OE2 
1278 N N   . LEU   A 167 ? 0.86950 0.76928 0.60930 -0.04457 0.02526  -0.02244 167 LEU   A N   
1279 C CA  . LEU   A 167 ? 0.89062 0.76849 0.60403 -0.06078 0.01271  -0.03384 167 LEU   A CA  
1280 C C   . LEU   A 167 ? 0.97214 0.81463 0.64697 -0.05610 0.02365  -0.05858 167 LEU   A C   
1281 O O   . LEU   A 167 ? 1.01575 0.85171 0.69445 -0.03745 0.04173  -0.06505 167 LEU   A O   
1282 C CB  . LEU   A 167 ? 0.86504 0.73590 0.60621 -0.06599 0.00377  -0.02882 167 LEU   A CB  
1283 C CG  . LEU   A 167 ? 0.84975 0.75327 0.62328 -0.07381 -0.00888 -0.00619 167 LEU   A CG  
1284 C CD1 . LEU   A 167 ? 0.84512 0.74734 0.65297 -0.06964 -0.00810 0.00032  167 LEU   A CD1 
1285 C CD2 . LEU   A 167 ? 0.88355 0.79477 0.64005 -0.09632 -0.02854 -0.00224 167 LEU   A CD2 
1286 N N   . PRO   A 168 ? 1.01646 0.83550 0.65337 -0.07283 0.01311  -0.07285 168 PRO   A N   
1287 C CA  . PRO   A 168 ? 1.04133 0.81983 0.63665 -0.06732 0.02523  -0.09959 168 PRO   A CA  
1288 C C   . PRO   A 168 ? 1.04946 0.79749 0.66171 -0.04997 0.03877  -0.10911 168 PRO   A C   
1289 O O   . PRO   A 168 ? 1.06061 0.78689 0.65294 -0.03367 0.05730  -0.12543 168 PRO   A O   
1290 C CB  . PRO   A 168 ? 1.01988 0.77488 0.57700 -0.09348 0.00601  -0.11182 168 PRO   A CB  
1291 C CG  . PRO   A 168 ? 1.02684 0.82245 0.59995 -0.11166 -0.01476 -0.08898 168 PRO   A CG  
1292 C CD  . PRO   A 168 ? 1.05612 0.89070 0.68111 -0.09705 -0.00921 -0.06420 168 PRO   A CD  
1293 N N   . THR   A 169 ? 0.97467 0.72203 0.62329 -0.05184 0.03110  -0.09811 169 THR   A N   
1294 C CA  . THR   A 169 ? 1.02685 0.74625 0.69088 -0.03600 0.04252  -0.10430 169 THR   A CA  
1295 C C   . THR   A 169 ? 0.98645 0.73037 0.68088 -0.01214 0.05922  -0.09432 169 THR   A C   
1296 O O   . THR   A 169 ? 1.01771 0.74790 0.73232 0.00166  0.06700  -0.09370 169 THR   A O   
1297 C CB  . THR   A 169 ? 0.89279 0.60276 0.58192 -0.04779 0.02863  -0.09493 169 THR   A CB  
1298 O OG1 . THR   A 169 ? 0.97278 0.72567 0.69825 -0.05096 0.02115  -0.07205 169 THR   A OG1 
1299 C CG2 . THR   A 169 ? 0.91525 0.59736 0.57547 -0.07363 0.01125  -0.10529 169 THR   A CG2 
1300 N N   . GLY   A 170 ? 0.91205 0.69205 0.61047 -0.00840 0.06370  -0.08511 170 GLY   A N   
1301 C CA  . GLY   A 170 ? 0.90631 0.71123 0.63248 0.01031  0.07763  -0.07526 170 GLY   A CA  
1302 C C   . GLY   A 170 ? 0.85162 0.68416 0.61827 0.00925  0.07041  -0.05550 170 GLY   A C   
1303 O O   . GLY   A 170 ? 0.83299 0.68764 0.62214 0.02104  0.07914  -0.04666 170 GLY   A O   
1304 N N   . VAL   A 171 ? 0.82745 0.65955 0.60358 -0.00486 0.05520  -0.04856 171 VAL   A N   
1305 C CA  . VAL   A 171 ? 0.80690 0.66247 0.61769 -0.00533 0.04986  -0.03168 171 VAL   A CA  
1306 C C   . VAL   A 171 ? 0.81761 0.70213 0.63290 -0.01255 0.04404  -0.01968 171 VAL   A C   
1307 O O   . VAL   A 171 ? 0.83727 0.72597 0.62914 -0.01766 0.04346  -0.02268 171 VAL   A O   
1308 C CB  . VAL   A 171 ? 0.80556 0.64903 0.62709 -0.01495 0.03920  -0.02827 171 VAL   A CB  
1309 C CG1 . VAL   A 171 ? 0.75460 0.56841 0.57532 -0.00673 0.04508  -0.03651 171 VAL   A CG1 
1310 C CG2 . VAL   A 171 ? 0.78065 0.61828 0.58349 -0.03437 0.02523  -0.03043 171 VAL   A CG2 
1311 N N   . HIS   A 172 ? 0.80174 0.70520 0.64560 -0.01254 0.04022  -0.00564 172 HIS   A N   
1312 C CA  . HIS   A 172 ? 0.74466 0.67298 0.59843 -0.01500 0.03740  0.00748  172 HIS   A CA  
1313 C C   . HIS   A 172 ? 0.74129 0.68194 0.61444 -0.02270 0.02674  0.02011  172 HIS   A C   
1314 O O   . HIS   A 172 ? 0.69188 0.62765 0.57914 -0.02283 0.02504  0.02105  172 HIS   A O   
1315 C CB  . HIS   A 172 ? 0.69444 0.63419 0.56585 -0.00365 0.04738  0.01240  172 HIS   A CB  
1316 C CG  . HIS   A 172 ? 0.79500 0.73124 0.65359 0.00456  0.05879  0.00396  172 HIS   A CG  
1317 N ND1 . HIS   A 172 ? 0.77600 0.70106 0.63865 0.01451  0.06643  -0.00391 172 HIS   A ND1 
1318 C CD2 . HIS   A 172 ? 0.77589 0.72088 0.61848 0.00505  0.06475  0.00377  172 HIS   A CD2 
1319 C CE1 . HIS   A 172 ? 0.75901 0.68741 0.61188 0.02210  0.07739  -0.00855 172 HIS   A CE1 
1320 N NE2 . HIS   A 172 ? 0.76610 0.70660 0.60545 0.01623  0.07728  -0.00457 172 HIS   A NE2 
1321 N N   . ALA   A 173 ? 0.70034 0.65947 0.57520 -0.02843 0.02026  0.03185  173 ALA   A N   
1322 C CA  . ALA   A 173 ? 0.64786 0.62430 0.54433 -0.03388 0.01087  0.04699  173 ALA   A CA  
1323 C C   . ALA   A 173 ? 0.64601 0.64010 0.56099 -0.02722 0.01355  0.06186  173 ALA   A C   
1324 O O   . ALA   A 173 ? 0.64218 0.63856 0.54643 -0.02523 0.01744  0.06297  173 ALA   A O   
1325 C CB  . ALA   A 173 ? 0.66202 0.64418 0.54319 -0.05043 -0.00415 0.04985  173 ALA   A CB  
1326 N N   . GLY   A 174 ? 0.64454 0.65026 0.58795 -0.02335 0.01256  0.07397  174 GLY   A N   
1327 C CA  . GLY   A 174 ? 0.61635 0.63313 0.57923 -0.01579 0.01557  0.08815  174 GLY   A CA  
1328 C C   . GLY   A 174 ? 0.63941 0.67130 0.63232 -0.01188 0.01341  0.10254  174 GLY   A C   
1329 O O   . GLY   A 174 ? 0.62130 0.66164 0.62047 -0.01784 0.00754  0.10446  174 GLY   A O   
1330 N N   . THR   A 175 ? 0.60614 0.64080 0.61907 -0.00146 0.01916  0.11330  175 THR   A N   
1331 C CA  . THR   A 175 ? 0.61467 0.66409 0.65898 0.00661  0.02029  0.12861  175 THR   A CA  
1332 C C   . THR   A 175 ? 0.62394 0.65727 0.68108 0.02076  0.03506  0.12113  175 THR   A C   
1333 O O   . THR   A 175 ? 0.57438 0.58681 0.61780 0.02280  0.04188  0.10713  175 THR   A O   
1334 C CB  . THR   A 175 ? 0.56453 0.62977 0.62307 0.00844  0.01424  0.15048  175 THR   A CB  
1335 O OG1 . THR   A 175 ? 0.57745 0.62477 0.63613 0.01642  0.02261  0.15009  175 THR   A OG1 
1336 C CG2 . THR   A 175 ? 0.59676 0.67686 0.63431 -0.00738 -0.00097 0.15632  175 THR   A CG2 
1337 N N   . ASP   A 176 ? 0.59599 0.64117 0.67930 0.03014  0.03998  0.13084  176 ASP   A N   
1338 C CA  . ASP   A 176 ? 0.62768 0.65706 0.72280 0.04560  0.05499  0.12598  176 ASP   A CA  
1339 C C   . ASP   A 176 ? 0.66712 0.68592 0.77216 0.05330  0.05722  0.13558  176 ASP   A C   
1340 O O   . ASP   A 176 ? 0.61753 0.64620 0.72206 0.04692  0.04716  0.14866  176 ASP   A O   
1341 C CB  . ASP   A 176 ? 0.67875 0.72573 0.79852 0.05519  0.06239  0.13383  176 ASP   A CB  
1342 C CG  . ASP   A 176 ? 0.70629 0.78483 0.85626 0.05762  0.05544  0.15935  176 ASP   A CG  
1343 O OD1 . ASP   A 176 ? 0.68810 0.77287 0.83805 0.05220  0.04439  0.17132  176 ASP   A OD1 
1344 O OD2 . ASP   A 176 ? 0.68864 0.78937 0.86342 0.06471  0.06092  0.16936  176 ASP   A OD2 
1345 N N   . LEU   A 177 ? 0.68000 0.67678 0.79242 0.06650  0.07043  0.12944  177 LEU   A N   
1346 C CA  . LEU   A 177 ? 0.64107 0.62033 0.76321 0.07340  0.07316  0.13790  177 LEU   A CA  
1347 C C   . LEU   A 177 ? 0.62016 0.61779 0.77485 0.08484  0.07256  0.16314  177 LEU   A C   
1348 O O   . LEU   A 177 ? 0.66529 0.64664 0.83294 0.09335  0.07594  0.17337  177 LEU   A O   
1349 C CB  . LEU   A 177 ? 0.67243 0.61558 0.78829 0.08195  0.08668  0.12065  177 LEU   A CB  
1350 C CG  . LEU   A 177 ? 0.67396 0.59551 0.76647 0.06947  0.08284  0.10778  177 LEU   A CG  
1351 C CD1 . LEU   A 177 ? 0.61964 0.54559 0.71693 0.06285  0.07395  0.12518  177 LEU   A CD1 
1352 C CD2 . LEU   A 177 ? 0.65013 0.58143 0.71982 0.05755  0.07784  0.09347  177 LEU   A CD2 
1353 N N   . GLU   A 178 ? 0.67001 0.70160 0.84038 0.08478  0.06777  0.17510  178 GLU   A N   
1354 C CA  . GLU   A 178 ? 0.70889 0.76838 0.91323 0.09324  0.06343  0.20344  178 GLU   A CA  
1355 C C   . GLU   A 178 ? 0.66666 0.75571 0.86511 0.07569  0.04269  0.21947  178 GLU   A C   
1356 O O   . GLU   A 178 ? 0.68546 0.80557 0.91090 0.07860  0.03445  0.24564  178 GLU   A O   
1357 C CB  . GLU   A 178 ? 0.69807 0.78098 0.92941 0.10537  0.07261  0.20923  178 GLU   A CB  
1358 C CG  . GLU   A 178 ? 0.78203 0.88197 1.05630 0.12538  0.07846  0.23528  178 GLU   A CG  
1359 C CD  . GLU   A 178 ? 0.87262 0.99903 1.17512 0.13872  0.09074  0.24088  178 GLU   A CD  
1360 O OE1 . GLU   A 178 ? 0.87336 0.97644 1.16818 0.15096  0.11018  0.22143  178 GLU   A OE1 
1361 O OE2 . GLU   A 178 ? 0.82371 0.99631 1.15514 0.13575  0.08064  0.26530  178 GLU   A OE2 
1362 N N   . GLY   A 179 ? 0.65690 0.73776 0.81995 0.05789  0.03432  0.20439  179 GLY   A N   
1363 C CA  . GLY   A 179 ? 0.64113 0.74379 0.78869 0.04033  0.01618  0.21432  179 GLY   A CA  
1364 C C   . GLY   A 179 ? 0.64395 0.77258 0.78762 0.02681  0.00482  0.21378  179 GLY   A C   
1365 O O   . GLY   A 179 ? 0.63649 0.78174 0.76337 0.01037  -0.01150 0.22027  179 GLY   A O   
1366 N N   . ASN   A 180 ? 0.61867 0.75049 0.77536 0.03183  0.01272  0.20642  180 ASN   A N   
1367 C CA  . ASN   A 180 ? 0.54085 0.69599 0.69751 0.01743  0.00202  0.20751  180 ASN   A CA  
1368 C C   . ASN   A 180 ? 0.55870 0.68970 0.67764 0.00439  0.00125  0.18129  180 ASN   A C   
1369 O O   . ASN   A 180 ? 0.54392 0.65034 0.65411 0.01226  0.01492  0.16342  180 ASN   A O   
1370 C CB  . ASN   A 180 ? 0.55217 0.72681 0.74458 0.02917  0.01195  0.21641  180 ASN   A CB  
1371 C CG  . ASN   A 180 ? 0.61431 0.82027 0.84913 0.04202  0.01120  0.24601  180 ASN   A CG  
1372 O OD1 . ASN   A 180 ? 0.61145 0.84796 0.85579 0.03075  -0.00697 0.26669  180 ASN   A OD1 
1373 N ND2 . ASN   A 180 ? 0.69033 0.88882 0.95033 0.06604  0.03086  0.24852  180 ASN   A ND2 
1374 N N   . PHE   A 181 ? 0.54146 0.67887 0.63752 -0.01529 -0.01496 0.17935  181 PHE   A N   
1375 C CA  . PHE   A 181 ? 0.62693 0.73892 0.68717 -0.02623 -0.01551 0.15533  181 PHE   A CA  
1376 C C   . PHE   A 181 ? 0.59454 0.70158 0.66204 -0.02638 -0.00933 0.14644  181 PHE   A C   
1377 O O   . PHE   A 181 ? 0.55916 0.69080 0.65318 -0.02861 -0.01244 0.16030  181 PHE   A O   
1378 C CB  . PHE   A 181 ? 0.64778 0.76576 0.68100 -0.04734 -0.03389 0.15470  181 PHE   A CB  
1379 C CG  . PHE   A 181 ? 0.60356 0.70218 0.60098 -0.04979 -0.03308 0.14248  181 PHE   A CG  
1380 C CD1 . PHE   A 181 ? 0.62522 0.69403 0.59449 -0.05020 -0.02518 0.11848  181 PHE   A CD1 
1381 C CD2 . PHE   A 181 ? 0.61084 0.72364 0.60425 -0.05104 -0.03955 0.15718  181 PHE   A CD2 
1382 C CE1 . PHE   A 181 ? 0.62697 0.68208 0.56600 -0.05080 -0.02197 0.10839  181 PHE   A CE1 
1383 C CE2 . PHE   A 181 ? 0.69108 0.78952 0.65142 -0.05336 -0.03692 0.14744  181 PHE   A CE2 
1384 C CZ  . PHE   A 181 ? 0.68296 0.75335 0.61653 -0.05286 -0.02729 0.12247  181 PHE   A CZ  
1385 N N   . TYR   A 182 ? 0.60375 0.68180 0.64937 -0.02407 -0.00050 0.12559  182 TYR   A N   
1386 C CA  . TYR   A 182 ? 0.56826 0.63838 0.61230 -0.02838 0.00225  0.11695  182 TYR   A CA  
1387 C C   . TYR   A 182 ? 0.63256 0.69751 0.65537 -0.04900 -0.01300 0.11179  182 TYR   A C   
1388 O O   . TYR   A 182 ? 0.75260 0.79541 0.74418 -0.05380 -0.01542 0.09706  182 TYR   A O   
1389 C CB  . TYR   A 182 ? 0.60323 0.64586 0.63219 -0.01845 0.01547  0.09909  182 TYR   A CB  
1390 C CG  . TYR   A 182 ? 0.61892 0.66160 0.66448 -0.00120 0.03019  0.10048  182 TYR   A CG  
1391 C CD1 . TYR   A 182 ? 0.59084 0.64322 0.65404 0.00480  0.03869  0.10492  182 TYR   A CD1 
1392 C CD2 . TYR   A 182 ? 0.61008 0.64130 0.65131 0.00813  0.03614  0.09662  182 TYR   A CD2 
1393 C CE1 . TYR   A 182 ? 0.61565 0.66387 0.68778 0.02065  0.05332  0.10287  182 TYR   A CE1 
1394 C CE2 . TYR   A 182 ? 0.62127 0.64618 0.67351 0.02208  0.04885  0.09511  182 TYR   A CE2 
1395 C CZ  . TYR   A 182 ? 0.66206 0.69411 0.72767 0.02884  0.05775  0.09683  182 TYR   A CZ  
1396 O OH  . TYR   A 182 ? 0.59655 0.61850 0.66737 0.04287  0.07151  0.09232  182 TYR   A OH  
1397 N N   . GLY   A 183 ? 0.64778 0.73255 0.68715 -0.06156 -0.02282 0.12367  183 GLY   A N   
1398 C CA  . GLY   A 183 ? 0.63364 0.70981 0.65236 -0.08407 -0.03887 0.11815  183 GLY   A CA  
1399 C C   . GLY   A 183 ? 0.66294 0.76001 0.67694 -0.09844 -0.05692 0.12917  183 GLY   A C   
1400 O O   . GLY   A 183 ? 0.70062 0.82090 0.73031 -0.08963 -0.05690 0.14386  183 GLY   A O   
1401 N N   . PRO   A 184 ? 0.70281 0.78988 0.69301 -0.12162 -0.07340 0.12233  184 PRO   A N   
1402 C CA  . PRO   A 184 ? 0.70559 0.81491 0.68750 -0.14012 -0.09430 0.13325  184 PRO   A CA  
1403 C C   . PRO   A 184 ? 0.75928 0.84990 0.69864 -0.13998 -0.09541 0.11932  184 PRO   A C   
1404 O O   . PRO   A 184 ? 0.77167 0.84675 0.67287 -0.15938 -0.10885 0.10707  184 PRO   A O   
1405 C CB  . PRO   A 184 ? 0.74536 0.84653 0.71804 -0.16716 -0.11087 0.12917  184 PRO   A CB  
1406 C CG  . PRO   A 184 ? 0.74795 0.80271 0.70061 -0.16168 -0.09741 0.10552  184 PRO   A CG  
1407 C CD  . PRO   A 184 ? 0.70839 0.75763 0.67270 -0.13219 -0.07390 0.10222  184 PRO   A CD  
1408 N N   . PHE   A 185 ? 0.73918 0.83017 0.68342 -0.11858 -0.08047 0.12075  185 PHE   A N   
1409 C CA  . PHE   A 185 ? 0.75089 0.82789 0.65903 -0.11613 -0.07785 0.11024  185 PHE   A CA  
1410 C C   . PHE   A 185 ? 0.73231 0.84179 0.65613 -0.11093 -0.08237 0.13371  185 PHE   A C   
1411 O O   . PHE   A 185 ? 0.70654 0.84182 0.67298 -0.10046 -0.08031 0.15483  185 PHE   A O   
1412 C CB  . PHE   A 185 ? 0.76616 0.81277 0.66401 -0.09756 -0.05660 0.09171  185 PHE   A CB  
1413 C CG  . PHE   A 185 ? 0.75322 0.77042 0.64446 -0.09836 -0.05065 0.07365  185 PHE   A CG  
1414 C CD1 . PHE   A 185 ? 0.78593 0.77830 0.64369 -0.11484 -0.05934 0.05709  185 PHE   A CD1 
1415 C CD2 . PHE   A 185 ? 0.68688 0.69908 0.60331 -0.08303 -0.03664 0.07339  185 PHE   A CD2 
1416 C CE1 . PHE   A 185 ? 0.79461 0.75699 0.64828 -0.11489 -0.05394 0.04276  185 PHE   A CE1 
1417 C CE2 . PHE   A 185 ? 0.70892 0.69576 0.61981 -0.08379 -0.03199 0.06015  185 PHE   A CE2 
1418 C CZ  . PHE   A 185 ? 0.74491 0.70646 0.62643 -0.09919 -0.04055 0.04591  185 PHE   A CZ  
1419 N N   . VAL   A 186 ? 0.76827 0.87576 0.65639 -0.11786 -0.08784 0.13051  186 VAL   A N   
1420 C CA  . VAL   A 186 ? 0.76562 0.90138 0.66173 -0.11480 -0.09324 0.15373  186 VAL   A CA  
1421 C C   . VAL   A 186 ? 0.75515 0.87282 0.61702 -0.10808 -0.08144 0.14216  186 VAL   A C   
1422 O O   . VAL   A 186 ? 0.78585 0.87502 0.61020 -0.11141 -0.07478 0.11674  186 VAL   A O   
1423 C CB  . VAL   A 186 ? 0.70806 0.87418 0.59506 -0.13762 -0.11919 0.17026  186 VAL   A CB  
1424 C CG1 . VAL   A 186 ? 0.67036 0.86241 0.59951 -0.14415 -0.13060 0.18660  186 VAL   A CG1 
1425 C CG2 . VAL   A 186 ? 0.71899 0.86230 0.54705 -0.15877 -0.12867 0.14627  186 VAL   A CG2 
1426 N N   . ASP   A 187 ? 0.77977 0.91430 0.65674 -0.09788 -0.07786 0.16230  187 ASP   A N   
1427 C CA  . ASP   A 187 ? 0.82265 0.94595 0.67271 -0.09213 -0.06616 0.15651  187 ASP   A CA  
1428 C C   . ASP   A 187 ? 0.82208 0.95639 0.62596 -0.11014 -0.07951 0.15773  187 ASP   A C   
1429 O O   . ASP   A 187 ? 0.81603 0.97896 0.62403 -0.11556 -0.09174 0.18339  187 ASP   A O   
1430 C CB  . ASP   A 187 ? 0.74759 0.88054 0.63172 -0.07602 -0.05722 0.17818  187 ASP   A CB  
1431 C CG  . ASP   A 187 ? 0.74386 0.90573 0.66881 -0.07367 -0.06897 0.20829  187 ASP   A CG  
1432 O OD1 . ASP   A 187 ? 0.80839 0.99370 0.73011 -0.08821 -0.08787 0.21890  187 ASP   A OD1 
1433 O OD2 . ASP   A 187 ? 0.75576 0.91674 0.71674 -0.05717 -0.05928 0.22185  187 ASP   A OD2 
1434 N N   . ARG   A 188 ? 0.81789 0.92811 0.57580 -0.11855 -0.07630 0.12990  188 ARG   A N   
1435 C CA  . ARG   A 188 ? 0.89605 1.01066 0.60179 -0.13843 -0.08983 0.12425  188 ARG   A CA  
1436 C C   . ARG   A 188 ? 0.94908 1.02690 0.60697 -0.13910 -0.07675 0.08895  188 ARG   A C   
1437 O O   . ARG   A 188 ? 0.89998 0.95044 0.56249 -0.13671 -0.07181 0.06871  188 ARG   A O   
1438 C CB  . ARG   A 188 ? 0.88573 1.01758 0.59639 -0.15894 -0.11574 0.13334  188 ARG   A CB  
1439 C CG  . ARG   A 188 ? 0.97573 1.10377 0.62702 -0.18426 -0.13270 0.12022  188 ARG   A CG  
1440 C CD  . ARG   A 188 ? 1.13221 1.30351 0.78183 -0.19921 -0.15577 0.15101  188 ARG   A CD  
1441 N NE  . ARG   A 188 ? 1.23006 1.39811 0.81423 -0.22463 -0.17197 0.13776  188 ARG   A NE  
1442 C CZ  . ARG   A 188 ? 1.18692 1.34737 0.74989 -0.24925 -0.19258 0.12534  188 ARG   A CZ  
1443 N NH1 . ARG   A 188 ? 1.14985 1.30842 0.75445 -0.25220 -0.19944 0.12661  188 ARG   A NH1 
1444 N NH2 . ARG   A 188 ? 1.19131 1.34536 0.68795 -0.27274 -0.20658 0.11117  188 ARG   A NH2 
1445 N N   . GLN   A 189 ? 0.95412 1.03106 0.56679 -0.14097 -0.06965 0.08240  189 GLN   A N   
1446 C CA  . GLN   A 189 ? 0.95596 0.99838 0.52268 -0.13864 -0.05445 0.04894  189 GLN   A CA  
1447 C C   . GLN   A 189 ? 0.96435 0.98553 0.48878 -0.16009 -0.07072 0.02796  189 GLN   A C   
1448 O O   . GLN   A 189 ? 0.96917 0.99409 0.44195 -0.17658 -0.08056 0.02308  189 GLN   A O   
1449 C CB  . GLN   A 189 ? 0.95583 1.00656 0.48625 -0.13347 -0.03960 0.04878  189 GLN   A CB  
1450 C CG  . GLN   A 189 ? 0.95258 0.96970 0.44226 -0.12488 -0.01826 0.01536  189 GLN   A CG  
1451 C CD  . GLN   A 189 ? 1.00238 1.03353 0.46390 -0.11666 0.00070  0.01806  189 GLN   A CD  
1452 O OE1 . GLN   A 189 ? 0.99080 1.04508 0.48666 -0.10534 0.01029  0.03989  189 GLN   A OE1 
1453 N NE2 . GLN   A 189 ? 0.94784 0.96411 0.34544 -0.12299 0.00680  -0.00433 189 GLN   A NE2 
1454 N N   . THR   A 190 ? 0.95187 0.94984 0.49647 -0.16153 -0.07428 0.01587  190 THR   A N   
1455 C CA  . THR   A 190 ? 1.00201 0.97240 0.51041 -0.18277 -0.08918 -0.00554 190 THR   A CA  
1456 C C   . THR   A 190 ? 0.97656 0.90998 0.50558 -0.17347 -0.07906 -0.02390 190 THR   A C   
1457 O O   . THR   A 190 ? 0.91593 0.85654 0.49513 -0.15578 -0.06849 -0.01296 190 THR   A O   
1458 C CB  . THR   A 190 ? 0.98969 0.99006 0.50929 -0.20807 -0.12049 0.01556  190 THR   A CB  
1459 O OG1 . THR   A 190 ? 1.01236 0.98268 0.49498 -0.23216 -0.13629 -0.00663 190 THR   A OG1 
1460 C CG2 . THR   A 190 ? 0.93079 0.95671 0.52201 -0.19980 -0.12447 0.04130  190 THR   A CG2 
1461 N N   . ALA   A 191 ? 1.00173 0.89301 0.48865 -0.18563 -0.08202 -0.05234 191 ALA   A N   
1462 C CA  . ALA   A 191 ? 1.05872 0.91074 0.56113 -0.17881 -0.07399 -0.06906 191 ALA   A CA  
1463 C C   . ALA   A 191 ? 1.04214 0.91274 0.59730 -0.18792 -0.09017 -0.04838 191 ALA   A C   
1464 O O   . ALA   A 191 ? 1.05277 0.93343 0.60353 -0.21395 -0.11472 -0.04142 191 ALA   A O   
1465 C CB  . ALA   A 191 ? 1.05766 0.85700 0.50215 -0.19299 -0.07655 -0.10263 191 ALA   A CB  
1466 N N   . GLN   A 192 ? 1.00307 0.88117 0.60782 -0.16744 -0.07672 -0.03760 192 GLN   A N   
1467 C CA  . GLN   A 192 ? 1.03742 0.93518 0.69330 -0.17196 -0.08702 -0.01771 192 GLN   A CA  
1468 C C   . GLN   A 192 ? 1.06704 0.92723 0.73377 -0.16538 -0.07756 -0.03177 192 GLN   A C   
1469 O O   . GLN   A 192 ? 1.02550 0.87436 0.70518 -0.14202 -0.05716 -0.03690 192 GLN   A O   
1470 C CB  . GLN   A 192 ? 0.96859 0.90813 0.67191 -0.15455 -0.08007 0.00857  192 GLN   A CB  
1471 C CG  . GLN   A 192 ? 0.94505 0.92178 0.64278 -0.15994 -0.08972 0.02700  192 GLN   A CG  
1472 C CD  . GLN   A 192 ? 0.87264 0.88881 0.62410 -0.14835 -0.08920 0.05647  192 GLN   A CD  
1473 O OE1 . GLN   A 192 ? 0.89885 0.92643 0.68943 -0.14874 -0.09340 0.06804  192 GLN   A OE1 
1474 N NE2 . GLN   A 192 ? 0.83267 0.86891 0.58601 -0.13781 -0.08312 0.06926  192 GLN   A NE2 
1475 N N   . ALA   A 193 ? 1.02801 0.87029 0.69045 -0.18734 -0.09361 -0.03601 193 ALA   A N   
1476 C CA  . ALA   A 193 ? 1.11795 0.92142 0.78845 -0.18436 -0.08692 -0.04743 193 ALA   A CA  
1477 C C   . ALA   A 193 ? 1.12922 0.95989 0.85663 -0.17120 -0.08049 -0.02538 193 ALA   A C   
1478 O O   . ALA   A 193 ? 1.13867 1.00345 0.89839 -0.18331 -0.09381 -0.00379 193 ALA   A O   
1479 C CB  . ALA   A 193 ? 1.30035 1.07605 0.94952 -0.21525 -0.10766 -0.05663 193 ALA   A CB  
1480 N N   . ALA   A 194 ? 1.13440 0.95258 0.87382 -0.14621 -0.05980 -0.03016 194 ALA   A N   
1481 C CA  . ALA   A 194 ? 1.05867 0.89331 0.84320 -0.13540 -0.05333 -0.01386 194 ALA   A CA  
1482 C C   . ALA   A 194 ? 1.05528 0.86566 0.84696 -0.15031 -0.06136 -0.01422 194 ALA   A C   
1483 O O   . ALA   A 194 ? 1.12116 0.88736 0.88204 -0.16042 -0.06488 -0.03269 194 ALA   A O   
1484 C CB  . ALA   A 194 ? 0.99994 0.82708 0.79177 -0.10778 -0.03175 -0.01909 194 ALA   A CB  
1485 N N   . GLY   A 195 ? 1.01259 0.85082 0.84466 -0.15170 -0.06340 0.00661  195 GLY   A N   
1486 C CA  . GLY   A 195 ? 1.06654 0.88664 0.91067 -0.16517 -0.06928 0.01080  195 GLY   A CA  
1487 C C   . GLY   A 195 ? 1.03008 0.81044 0.86835 -0.14929 -0.05449 -0.00047 195 GLY   A C   
1488 O O   . GLY   A 195 ? 1.00186 0.77478 0.83235 -0.12639 -0.03902 -0.00961 195 GLY   A O   
1489 N N   . THR   A 196 ? 1.05267 0.80875 0.89721 -0.16272 -0.06026 0.00268  196 THR   A N   
1490 C CA  . THR   A 196 ? 1.02596 0.74546 0.86973 -0.14866 -0.04801 -0.00293 196 THR   A CA  
1491 C C   . THR   A 196 ? 0.98088 0.73174 0.85467 -0.12636 -0.03355 0.01212  196 THR   A C   
1492 O O   . THR   A 196 ? 1.00034 0.79024 0.90348 -0.13015 -0.03527 0.03193  196 THR   A O   
1493 C CB  . THR   A 196 ? 1.01495 0.70426 0.86269 -0.17044 -0.05884 0.00191  196 THR   A CB  
1494 O OG1 . THR   A 196 ? 1.08311 0.74836 0.90324 -0.19678 -0.07609 -0.01099 196 THR   A OG1 
1495 C CG2 . THR   A 196 ? 1.02860 0.67040 0.86962 -0.15590 -0.04734 -0.00575 196 THR   A CG2 
1496 N N   . ASP   A 197 ? 0.91527 0.64980 0.78114 -0.10322 -0.01903 0.00264  197 ASP   A N   
1497 C CA  . ASP   A 197 ? 0.96968 0.73192 0.85786 -0.08310 -0.00664 0.01397  197 ASP   A CA  
1498 C C   . ASP   A 197 ? 1.13656 0.88494 1.03926 -0.08164 -0.00386 0.02545  197 ASP   A C   
1499 O O   . ASP   A 197 ? 1.23760 0.94887 1.13011 -0.07344 0.00073  0.01810  197 ASP   A O   
1500 C CB  . ASP   A 197 ? 0.99817 0.75664 0.87401 -0.06109 0.00570  0.00133  197 ASP   A CB  
1501 C CG  . ASP   A 197 ? 0.98975 0.78524 0.88559 -0.04596 0.01435  0.01166  197 ASP   A CG  
1502 O OD1 . ASP   A 197 ? 0.83081 0.65524 0.74636 -0.05142 0.01183  0.02610  197 ASP   A OD1 
1503 O OD2 . ASP   A 197 ? 1.07673 0.87215 0.96856 -0.02895 0.02400  0.00520  197 ASP   A OD2 
1504 N N   . THR   A 198 ? 1.04019 0.81939 0.96723 -0.08842 -0.00560 0.04489  198 THR   A N   
1505 C CA  . THR   A 198 ? 0.99151 0.76580 0.93236 -0.08600 -0.00155 0.05931  198 THR   A CA  
1506 C C   . THR   A 198 ? 0.93343 0.72361 0.87864 -0.06274 0.01111  0.06152  198 THR   A C   
1507 O O   . THR   A 198 ? 0.88616 0.69466 0.82792 -0.05069 0.01641  0.05363  198 THR   A O   
1508 C CB  . THR   A 198 ? 0.93625 0.74040 0.90015 -0.10266 -0.00665 0.08007  198 THR   A CB  
1509 O OG1 . THR   A 198 ? 0.93217 0.78200 0.91133 -0.09155 0.00193  0.08895  198 THR   A OG1 
1510 C CG2 . THR   A 198 ? 0.90659 0.71049 0.86927 -0.12653 -0.02129 0.07843  198 THR   A CG2 
1511 N N   . THR   A 199 ? 0.96003 0.74236 0.91227 -0.05799 0.01473  0.07342  199 THR   A N   
1512 C CA  . THR   A 199 ? 0.91118 0.70939 0.86636 -0.03914 0.02393  0.07765  199 THR   A CA  
1513 C C   . THR   A 199 ? 0.86454 0.70270 0.83273 -0.04079 0.02794  0.09289  199 THR   A C   
1514 O O   . THR   A 199 ? 0.88797 0.73352 0.86678 -0.05376 0.02562  0.10800  199 THR   A O   
1515 C CB  . THR   A 199 ? 0.89043 0.65909 0.84455 -0.03143 0.02525  0.08360  199 THR   A CB  
1516 O OG1 . THR   A 199 ? 0.93328 0.66012 0.87476 -0.02915 0.02363  0.06818  199 THR   A OG1 
1517 C CG2 . THR   A 199 ? 0.87176 0.65944 0.82796 -0.01286 0.03213  0.08768  199 THR   A CG2 
1518 N N   . ILE   A 200 ? 0.82658 0.68969 0.79333 -0.02814 0.03465  0.08865  200 ILE   A N   
1519 C CA  . ILE   A 200 ? 0.72730 0.62469 0.70145 -0.02726 0.04094  0.09898  200 ILE   A CA  
1520 C C   . ILE   A 200 ? 0.75564 0.65487 0.72893 -0.02484 0.04383  0.11376  200 ILE   A C   
1521 O O   . ILE   A 200 ? 0.68421 0.58499 0.64932 -0.01339 0.04627  0.11220  200 ILE   A O   
1522 C CB  . ILE   A 200 ? 0.71750 0.63389 0.68738 -0.01579 0.04676  0.08816  200 ILE   A CB  
1523 C CG1 . ILE   A 200 ? 0.76647 0.68266 0.73787 -0.01864 0.04342  0.07727  200 ILE   A CG1 
1524 C CG2 . ILE   A 200 ? 0.67144 0.61715 0.64535 -0.01366 0.05521  0.09621  200 ILE   A CG2 
1525 C CD1 . ILE   A 200 ? 0.72117 0.62878 0.68267 -0.00868 0.04404  0.06285  200 ILE   A CD1 
1526 N N   . THR   A 201 ? 0.76296 0.66479 0.74552 -0.03720 0.04260  0.13027  201 THR   A N   
1527 C CA  . THR   A 201 ? 0.69404 0.59346 0.67589 -0.03771 0.04375  0.14804  201 THR   A CA  
1528 C C   . THR   A 201 ? 0.66331 0.59176 0.63604 -0.02782 0.05224  0.15254  201 THR   A C   
1529 O O   . THR   A 201 ? 0.67782 0.60257 0.64216 -0.02138 0.05145  0.15985  201 THR   A O   
1530 C CB  . THR   A 201 ? 0.70785 0.61027 0.70353 -0.05534 0.04167  0.16666  201 THR   A CB  
1531 O OG1 . THR   A 201 ? 0.76122 0.63450 0.76194 -0.06779 0.03178  0.16008  201 THR   A OG1 
1532 C CG2 . THR   A 201 ? 0.75091 0.64774 0.74599 -0.05702 0.04217  0.18775  201 THR   A CG2 
1533 N N   . VAL   A 202 ? 0.68997 0.64695 0.66345 -0.02656 0.06027  0.14876  202 VAL   A N   
1534 C CA  . VAL   A 202 ? 0.67275 0.65360 0.63236 -0.01834 0.06946  0.15006  202 VAL   A CA  
1535 C C   . VAL   A 202 ? 0.68726 0.65995 0.63181 -0.00717 0.06639  0.13564  202 VAL   A C   
1536 O O   . VAL   A 202 ? 0.67701 0.65967 0.60599 -0.00285 0.06799  0.13943  202 VAL   A O   
1537 C CB  . VAL   A 202 ? 0.69467 0.70246 0.65954 -0.01705 0.08061  0.14674  202 VAL   A CB  
1538 C CG1 . VAL   A 202 ? 0.76833 0.76971 0.74199 -0.01455 0.07757  0.13035  202 VAL   A CG1 
1539 C CG2 . VAL   A 202 ? 0.66067 0.68705 0.60529 -0.00789 0.09167  0.14314  202 VAL   A CG2 
1540 N N   . ASN   A 203 ? 0.71580 0.67233 0.66442 -0.00374 0.06123  0.12040  203 ASN   A N   
1541 C CA  . ASN   A 203 ? 0.64376 0.59602 0.58284 0.00555  0.05825  0.10867  203 ASN   A CA  
1542 C C   . ASN   A 203 ? 0.66402 0.60387 0.60220 0.00905  0.05157  0.11823  203 ASN   A C   
1543 O O   . ASN   A 203 ? 0.67581 0.62499 0.60512 0.01480  0.04928  0.11854  203 ASN   A O   
1544 C CB  . ASN   A 203 ? 0.69489 0.63629 0.63966 0.00799  0.05614  0.09251  203 ASN   A CB  
1545 C CG  . ASN   A 203 ? 0.69135 0.64704 0.63583 0.00893  0.06220  0.08265  203 ASN   A CG  
1546 O OD1 . ASN   A 203 ? 0.69629 0.66839 0.63787 0.00848  0.06961  0.08662  203 ASN   A OD1 
1547 N ND2 . ASN   A 203 ? 0.68658 0.63558 0.63423 0.01124  0.06022  0.07058  203 ASN   A ND2 
1548 N N   . VAL   A 204 ? 0.64186 0.55969 0.58998 0.00549  0.04767  0.12642  204 VAL   A N   
1549 C CA  . VAL   A 204 ? 0.68732 0.59031 0.63796 0.01124  0.04252  0.13787  204 VAL   A CA  
1550 C C   . VAL   A 204 ? 0.70122 0.62382 0.64391 0.01032  0.04237  0.15669  204 VAL   A C   
1551 O O   . VAL   A 204 ? 0.68650 0.61500 0.62619 0.01791  0.03786  0.16365  204 VAL   A O   
1552 C CB  . VAL   A 204 ? 0.70139 0.57064 0.66216 0.00639  0.03939  0.14279  204 VAL   A CB  
1553 C CG1 . VAL   A 204 ? 0.69212 0.54479 0.65774 0.01356  0.03557  0.15899  204 VAL   A CG1 
1554 C CG2 . VAL   A 204 ? 0.70687 0.55515 0.66905 0.00875  0.03889  0.12282  204 VAL   A CG2 
1555 N N   . LEU   A 205 ? 0.64073 0.57724 0.58003 0.00081  0.04737  0.16661  205 LEU   A N   
1556 C CA  . LEU   A 205 ? 0.67131 0.62869 0.59842 -0.00104 0.04879  0.18493  205 LEU   A CA  
1557 C C   . LEU   A 205 ? 0.64054 0.62068 0.54781 0.00459  0.04941  0.17525  205 LEU   A C   
1558 O O   . LEU   A 205 ? 0.71300 0.70376 0.60956 0.00683  0.04396  0.18724  205 LEU   A O   
1559 C CB  . LEU   A 205 ? 0.71965 0.69160 0.64760 -0.01177 0.05707  0.19618  205 LEU   A CB  
1560 C CG  . LEU   A 205 ? 0.63526 0.58599 0.58239 -0.02197 0.05395  0.21067  205 LEU   A CG  
1561 C CD1 . LEU   A 205 ? 0.64598 0.61529 0.60146 -0.03335 0.06206  0.21624  205 LEU   A CD1 
1562 C CD2 . LEU   A 205 ? 0.71041 0.65264 0.65779 -0.02332 0.04886  0.23614  205 LEU   A CD2 
1563 N N   . ALA   A 206 ? 0.68897 0.67580 0.59091 0.00593  0.05481  0.15437  206 ALA   A N   
1564 C CA  . ALA   A 206 ? 0.71213 0.71390 0.59423 0.00918  0.05433  0.14227  206 ALA   A CA  
1565 C C   . ALA   A 206 ? 0.74116 0.73887 0.62723 0.01474  0.04287  0.14137  206 ALA   A C   
1566 O O   . ALA   A 206 ? 0.70967 0.72305 0.57988 0.01428  0.03704  0.14417  206 ALA   A O   
1567 C CB  . ALA   A 206 ? 0.64816 0.65053 0.52846 0.01031  0.06211  0.12070  206 ALA   A CB  
1568 N N   . TRP   A 207 ? 0.68368 0.66234 0.59050 0.01976  0.03966  0.13788  207 TRP   A N   
1569 C CA  . TRP   A 207 ? 0.66323 0.64085 0.57940 0.02749  0.03118  0.14009  207 TRP   A CA  
1570 C C   . TRP   A 207 ? 0.69694 0.67996 0.61485 0.02988  0.02418  0.16447  207 TRP   A C   
1571 O O   . TRP   A 207 ? 0.72388 0.72382 0.64060 0.03328  0.01580  0.17117  207 TRP   A O   
1572 C CB  . TRP   A 207 ? 0.68806 0.64237 0.62337 0.03378  0.03267  0.13121  207 TRP   A CB  
1573 C CG  . TRP   A 207 ? 0.72084 0.67534 0.66981 0.04458  0.02761  0.13329  207 TRP   A CG  
1574 C CD1 . TRP   A 207 ? 0.70726 0.67945 0.65776 0.04723  0.02439  0.12525  207 TRP   A CD1 
1575 C CD2 . TRP   A 207 ? 0.73635 0.67265 0.70205 0.05483  0.02635  0.14488  207 TRP   A CD2 
1576 N NE1 . TRP   A 207 ? 0.70258 0.67443 0.67206 0.05904  0.02173  0.13273  207 TRP   A NE1 
1577 C CE2 . TRP   A 207 ? 0.72985 0.67814 0.70836 0.06546  0.02376  0.14402  207 TRP   A CE2 
1578 C CE3 . TRP   A 207 ? 0.75574 0.66528 0.72787 0.05597  0.02756  0.15640  207 TRP   A CE3 
1579 C CZ2 . TRP   A 207 ? 0.82549 0.76124 0.82360 0.08023  0.02430  0.15401  207 TRP   A CZ2 
1580 C CZ3 . TRP   A 207 ? 0.78281 0.67371 0.77172 0.06960  0.02718  0.16477  207 TRP   A CZ3 
1581 C CH2 . TRP   A 207 ? 0.83455 0.73916 0.83658 0.08310  0.02652  0.16340  207 TRP   A CH2 
1582 N N   . LEU   A 208 ? 0.65313 0.62331 0.57554 0.02715  0.02641  0.18020  208 LEU   A N   
1583 C CA  . LEU   A 208 ? 0.70031 0.67543 0.62421 0.02900  0.01982  0.20689  208 LEU   A CA  
1584 C C   . LEU   A 208 ? 0.74759 0.75494 0.64608 0.02267  0.01652  0.21518  208 LEU   A C   
1585 O O   . LEU   A 208 ? 0.74589 0.76749 0.64281 0.02520  0.00706  0.23480  208 LEU   A O   
1586 C CB  . LEU   A 208 ? 0.70471 0.65818 0.63740 0.02428  0.02311  0.22300  208 LEU   A CB  
1587 C CG  . LEU   A 208 ? 0.73434 0.64944 0.68925 0.03057  0.02308  0.22075  208 LEU   A CG  
1588 C CD1 . LEU   A 208 ? 0.66205 0.55554 0.62161 0.01929  0.02643  0.23006  208 LEU   A CD1 
1589 C CD2 . LEU   A 208 ? 0.75750 0.66434 0.72731 0.04445  0.01639  0.23690  208 LEU   A CD2 
1590 N N   . TYR   A 209 ? 0.75192 0.77091 0.62934 0.01490  0.02440  0.20083  209 TYR   A N   
1591 C CA  . TYR   A 209 ? 0.74980 0.79570 0.59597 0.00870  0.02294  0.20324  209 TYR   A CA  
1592 C C   . TYR   A 209 ? 0.81515 0.87426 0.65353 0.00981  0.01229  0.19238  209 TYR   A C   
1593 O O   . TYR   A 209 ? 0.78805 0.86850 0.60917 0.00601  0.00222  0.20472  209 TYR   A O   
1594 C CB  . TYR   A 209 ? 0.72565 0.77651 0.55259 0.00297  0.03722  0.18853  209 TYR   A CB  
1595 C CG  . TYR   A 209 ? 0.75599 0.81345 0.57810 -0.00232 0.04624  0.20772  209 TYR   A CG  
1596 C CD1 . TYR   A 209 ? 0.75985 0.83859 0.55694 -0.00720 0.04483  0.22656  209 TYR   A CD1 
1597 C CD2 . TYR   A 209 ? 0.72455 0.76977 0.56707 -0.00401 0.05553  0.20859  209 TYR   A CD2 
1598 C CE1 . TYR   A 209 ? 0.76230 0.85014 0.55583 -0.01270 0.05432  0.24641  209 TYR   A CE1 
1599 C CE2 . TYR   A 209 ? 0.73932 0.79428 0.58113 -0.01068 0.06370  0.22854  209 TYR   A CE2 
1600 C CZ  . TYR   A 209 ? 0.74767 0.82402 0.56546 -0.01454 0.06398  0.24778  209 TYR   A CZ  
1601 O OH  . TYR   A 209 ? 0.81271 0.90175 0.63034 -0.02177 0.07321  0.27009  209 TYR   A OH  
1602 N N   . ALA   A 210 ? 0.86139 0.91004 0.71246 0.01335  0.01333  0.17098  210 ALA   A N   
1603 C CA  . ALA   A 210 ? 0.79369 0.85515 0.64398 0.01296  0.00259  0.16275  210 ALA   A CA  
1604 C C   . ALA   A 210 ? 0.79770 0.87076 0.66791 0.01935  -0.01047 0.18520  210 ALA   A C   
1605 O O   . ALA   A 210 ? 0.82143 0.91695 0.68704 0.01572  -0.02290 0.18782  210 ALA   A O   
1606 C CB  . ALA   A 210 ? 0.70481 0.75214 0.57052 0.01625  0.00727  0.14027  210 ALA   A CB  
1607 N N   . ALA   A 211 ? 0.76205 0.81974 0.65562 0.02864  -0.00824 0.20195  211 ALA   A N   
1608 C CA  . ALA   A 211 ? 0.73706 0.80379 0.65264 0.03811  -0.01876 0.22596  211 ALA   A CA  
1609 C C   . ALA   A 211 ? 0.81216 0.90409 0.70901 0.03167  -0.02927 0.25053  211 ALA   A C   
1610 O O   . ALA   A 211 ? 0.83246 0.95127 0.73343 0.03230  -0.04337 0.26415  211 ALA   A O   
1611 C CB  . ALA   A 211 ? 0.70469 0.74001 0.64739 0.05018  -0.01201 0.23508  211 ALA   A CB  
1612 N N   . VAL   A 212 ? 0.83085 0.91784 0.70741 0.02463  -0.02289 0.25827  212 VAL   A N   
1613 C CA  . VAL   A 212 ? 0.81776 0.92978 0.67098 0.01729  -0.03142 0.28236  212 VAL   A CA  
1614 C C   . VAL   A 212 ? 0.80784 0.94919 0.62903 0.00607  -0.04105 0.27064  212 VAL   A C   
1615 O O   . VAL   A 212 ? 0.81558 0.98490 0.62705 0.00204  -0.05654 0.29057  212 VAL   A O   
1616 C CB  . VAL   A 212 ? 0.83095 0.93440 0.66655 0.01051  -0.01938 0.28980  212 VAL   A CB  
1617 C CG1 . VAL   A 212 ? 0.75416 0.88727 0.55571 0.00078  -0.02583 0.31071  212 VAL   A CG1 
1618 C CG2 . VAL   A 212 ? 0.84200 0.91639 0.70953 0.01834  -0.01465 0.30702  212 VAL   A CG2 
1619 N N   . ILE   A 213 ? 0.77283 0.90695 0.57724 0.00018  -0.03313 0.23862  213 ILE   A N   
1620 C CA  . ILE   A 213 ? 0.80018 0.95373 0.57446 -0.01161 -0.04250 0.22298  213 ILE   A CA  
1621 C C   . ILE   A 213 ? 0.87618 1.04912 0.67423 -0.00990 -0.06073 0.23157  213 ILE   A C   
1622 O O   . ILE   A 213 ? 0.95720 1.15719 0.73425 -0.02138 -0.07689 0.23607  213 ILE   A O   
1623 C CB  . ILE   A 213 ? 0.87467 1.00922 0.63506 -0.01527 -0.02941 0.18746  213 ILE   A CB  
1624 C CG1 . ILE   A 213 ? 0.89028 1.01292 0.62966 -0.01599 -0.01079 0.18176  213 ILE   A CG1 
1625 C CG2 . ILE   A 213 ? 0.91337 1.06026 0.64379 -0.02846 -0.03982 0.16921  213 ILE   A CG2 
1626 C CD1 . ILE   A 213 ? 0.88446 0.99301 0.60378 -0.01920 0.00198  0.14939  213 ILE   A CD1 
1627 N N   . ASN   A 214 ? 0.81452 0.97591 0.65643 0.00406  -0.05843 0.23485  214 ASN   A N   
1628 C CA  . ASN   A 214 ? 0.77255 0.95353 0.64340 0.00800  -0.07140 0.24045  214 ASN   A CA  
1629 C C   . ASN   A 214 ? 0.84149 1.04038 0.74247 0.01996  -0.08196 0.27636  214 ASN   A C   
1630 O O   . ASN   A 214 ? 0.89434 1.10417 0.83289 0.03093  -0.08660 0.28406  214 ASN   A O   
1631 C CB  . ASN   A 214 ? 0.82593 0.98547 0.72462 0.01712  -0.06006 0.21998  214 ASN   A CB  
1632 C CG  . ASN   A 214 ? 0.90087 1.06517 0.78585 0.00451  -0.06266 0.19406  214 ASN   A CG  
1633 O OD1 . ASN   A 214 ? 0.89074 1.07654 0.79449 0.00245  -0.07349 0.19633  214 ASN   A OD1 
1634 N ND2 . ASN   A 214 ? 0.87342 1.01812 0.72709 -0.00414 -0.05248 0.17066  214 ASN   A ND2 
1635 N N   . GLY   A 215 ? 0.78128 0.98442 0.66824 0.01910  -0.08486 0.30015  215 GLY   A N   
1636 C CA  . GLY   A 215 ? 0.74336 0.96354 0.65729 0.03028  -0.09591 0.33772  215 GLY   A CA  
1637 C C   . GLY   A 215 ? 0.81524 1.00233 0.76591 0.05062  -0.08357 0.34973  215 GLY   A C   
1638 O O   . GLY   A 215 ? 0.81033 1.00021 0.77566 0.05926  -0.08888 0.38245  215 GLY   A O   
1639 N N   . ASP   A 216 ? 0.86555 1.01959 0.82990 0.05785  -0.06785 0.32439  216 ASP   A N   
1640 C CA  . ASP   A 216 ? 0.88253 0.99912 0.87670 0.07533  -0.05605 0.33073  216 ASP   A CA  
1641 C C   . ASP   A 216 ? 0.88523 0.97559 0.86058 0.06862  -0.04825 0.33696  216 ASP   A C   
1642 O O   . ASP   A 216 ? 0.92860 1.00190 0.88365 0.05862  -0.03754 0.31374  216 ASP   A O   
1643 C CB  . ASP   A 216 ? 0.82436 0.91682 0.83308 0.08237  -0.04306 0.30058  216 ASP   A CB  
1644 C CG  . ASP   A 216 ? 0.92067 0.99330 0.96916 0.10534  -0.03697 0.30939  216 ASP   A CG  
1645 O OD1 . ASP   A 216 ? 0.93894 1.00380 1.00413 0.11650  -0.03987 0.33742  216 ASP   A OD1 
1646 O OD2 . ASP   A 216 ? 0.95537 1.01842 1.01733 0.11286  -0.02813 0.28839  216 ASP   A OD2 
1647 N N   . ARG   A 217 ? 0.92027 1.00882 0.90531 0.07415  -0.05353 0.37078  217 ARG   A N   
1648 C CA  . ARG   A 217 ? 0.93385 1.00499 0.90042 0.06447  -0.04783 0.38198  217 ARG   A CA  
1649 C C   . ARG   A 217 ? 0.90492 0.94737 0.89898 0.07674  -0.04733 0.41221  217 ARG   A C   
1650 O O   . ARG   A 217 ? 0.85141 0.89365 0.83394 0.06884  -0.04906 0.43706  217 ARG   A O   
1651 C CB  . ARG   A 217 ? 0.91014 1.01953 0.83870 0.04797  -0.05665 0.39467  217 ARG   A CB  
1652 N N   . TRP   A 218 ? 0.93475 0.95086 0.96416 0.09612  -0.04374 0.41063  218 TRP   A N   
1653 C CA  . TRP   A 218 ? 0.89156 0.87164 0.94761 0.10964  -0.04196 0.43681  218 TRP   A CA  
1654 C C   . TRP   A 218 ? 0.96543 0.89559 1.01588 0.10112  -0.03024 0.42692  218 TRP   A C   
1655 O O   . TRP   A 218 ? 1.00423 0.90029 1.07105 0.10684  -0.02954 0.45014  218 TRP   A O   
1656 C CB  . TRP   A 218 ? 0.91499 0.88123 1.00940 0.13551  -0.03941 0.43618  218 TRP   A CB  
1657 C CG  . TRP   A 218 ? 0.95600 0.89489 1.05330 0.14001  -0.02595 0.39656  218 TRP   A CG  
1658 C CD1 . TRP   A 218 ? 0.91685 0.88208 1.01171 0.14006  -0.02482 0.37143  218 TRP   A CD1 
1659 C CD2 . TRP   A 218 ? 0.95159 0.83176 1.05249 0.14309  -0.01275 0.37851  218 TRP   A CD2 
1660 N NE1 . TRP   A 218 ? 0.91709 0.84586 1.01354 0.14420  -0.01103 0.34035  218 TRP   A NE1 
1661 C CE2 . TRP   A 218 ? 0.95054 0.82697 1.04910 0.14573  -0.00396 0.34301  218 TRP   A CE2 
1662 C CE3 . TRP   A 218 ? 0.91251 0.74220 1.01722 0.14198  -0.00855 0.38941  218 TRP   A CE3 
1663 C CZ2 . TRP   A 218 ? 0.95207 0.77819 1.04893 0.14744  0.00831  0.31770  218 TRP   A CZ2 
1664 C CZ3 . TRP   A 218 ? 0.94420 0.72150 1.04798 0.14239  0.00292  0.36281  218 TRP   A CZ3 
1665 C CH2 . TRP   A 218 ? 0.96081 0.73757 1.05927 0.14525  0.01101  0.32705  218 TRP   A CH2 
1666 N N   . PHE   A 219 ? 0.95205 0.87749 0.98148 0.08686  -0.02204 0.39502  219 PHE   A N   
1667 C CA  . PHE   A 219 ? 0.96739 0.84913 0.99487 0.07741  -0.01235 0.38357  219 PHE   A CA  
1668 C C   . PHE   A 219 ? 0.97290 0.86457 0.98046 0.05713  -0.01209 0.40017  219 PHE   A C   
1669 O O   . PHE   A 219 ? 0.99381 0.85099 1.00533 0.04771  -0.00660 0.40087  219 PHE   A O   
1670 C CB  . PHE   A 219 ? 0.94133 0.81462 0.96091 0.07355  -0.00379 0.34278  219 PHE   A CB  
1671 C CG  . PHE   A 219 ? 0.91025 0.82828 0.90704 0.06478  -0.00503 0.32621  219 PHE   A CG  
1672 C CD1 . PHE   A 219 ? 0.90414 0.84901 0.90478 0.07439  -0.00969 0.31740  219 PHE   A CD1 
1673 C CD2 . PHE   A 219 ? 0.88297 0.81567 0.85565 0.04698  -0.00099 0.32019  219 PHE   A CD2 
1674 C CE1 . PHE   A 219 ? 0.87659 0.85645 0.85491 0.06463  -0.01161 0.30140  219 PHE   A CE1 
1675 C CE2 . PHE   A 219 ? 0.88061 0.84805 0.83075 0.04039  -0.00078 0.30339  219 PHE   A CE2 
1676 C CZ  . PHE   A 219 ? 0.88108 0.86923 0.83276 0.04833  -0.00675 0.29322  219 PHE   A CZ  
1677 N N   . LEU   A 220 ? 0.93424 0.87264 0.91942 0.04908  -0.01755 0.41310  220 LEU   A N   
1678 C CA  . LEU   A 220 ? 0.93592 0.88797 0.90082 0.03134  -0.01483 0.43066  220 LEU   A CA  
1679 C C   . LEU   A 220 ? 0.98887 0.91746 0.97106 0.03222  -0.01884 0.46964  220 LEU   A C   
1680 O O   . LEU   A 220 ? 1.02959 0.96759 1.02162 0.04270  -0.02832 0.48709  220 LEU   A O   
1681 C CB  . LEU   A 220 ? 0.92278 0.92805 0.85493 0.02405  -0.01938 0.43523  220 LEU   A CB  
1682 C CG  . LEU   A 220 ? 0.93384 0.96141 0.84890 0.02423  -0.01818 0.39965  220 LEU   A CG  
1683 C CD1 . LEU   A 220 ? 0.86585 0.93961 0.75205 0.01997  -0.02828 0.40809  220 LEU   A CD1 
1684 C CD2 . LEU   A 220 ? 0.96460 0.98686 0.86563 0.01326  -0.00421 0.37229  220 LEU   A CD2 
1685 N N   . ASN   A 221 ? 1.02958 0.92875 1.01678 0.01967  -0.01188 0.47114  221 ASN   A N   
1686 C CA  . ASN   A 221 ? 1.05844 0.93238 1.05989 0.01670  -0.01481 0.49253  221 ASN   A CA  
1687 C C   . ASN   A 221 ? 1.07564 0.98202 1.05687 -0.00166 -0.01239 0.50913  221 ASN   A C   
1688 O O   . ASN   A 221 ? 1.10927 1.05552 1.06457 -0.01072 -0.00718 0.50185  221 ASN   A O   
1689 C CB  . ASN   A 221 ? 1.05970 0.87281 1.08227 0.01437  -0.01042 0.48264  221 ASN   A CB  
1690 C CG  . ASN   A 221 ? 1.11471 0.92488 1.12935 -0.00405 -0.00197 0.46622  221 ASN   A CG  
1691 O OD1 . ASN   A 221 ? 1.11397 0.96755 1.10843 -0.01476 0.00285  0.46477  221 ASN   A OD1 
1692 N ND2 . ASN   A 221 ? 1.12481 0.88351 1.15478 -0.00801 0.00001  0.45298  221 ASN   A ND2 
1693 N N   . ARG   A 222 ? 1.09303 0.98065 1.08588 -0.00634 -0.01492 0.53123  222 ARG   A N   
1694 C CA  . ARG   A 222 ? 1.13481 1.05062 1.11273 -0.02274 -0.01196 0.55034  222 ARG   A CA  
1695 C C   . ARG   A 222 ? 1.13196 1.02824 1.11655 -0.04118 -0.00298 0.54696  222 ARG   A C   
1696 O O   . ARG   A 222 ? 1.26132 1.16356 1.24651 -0.05380 -0.00125 0.56730  222 ARG   A O   
1697 C CB  . ARG   A 222 ? 1.11768 1.03048 1.10489 -0.01795 -0.02069 0.58040  222 ARG   A CB  
1698 N N   . PHE   A 223 ? 1.16457 1.03998 1.15560 -0.04383 0.00210  0.52283  223 PHE   A N   
1699 C CA  . PHE   A 223 ? 1.12191 0.97907 1.12316 -0.06246 0.00835  0.51829  223 PHE   A CA  
1700 C C   . PHE   A 223 ? 1.10078 1.00133 1.08585 -0.07217 0.01920  0.50484  223 PHE   A C   
1701 O O   . PHE   A 223 ? 1.12198 1.05763 1.08590 -0.06368 0.02224  0.49494  223 PHE   A O   
1702 C CB  . PHE   A 223 ? 1.14964 0.94675 1.17126 -0.06009 0.00522  0.50055  223 PHE   A CB  
1703 C CG  . PHE   A 223 ? 1.18786 0.93377 1.22598 -0.05098 -0.00241 0.51156  223 PHE   A CG  
1704 C CD1 . PHE   A 223 ? 1.22009 0.90637 1.27176 -0.04562 -0.00439 0.49330  223 PHE   A CD1 
1705 C CD2 . PHE   A 223 ? 1.20903 0.96473 1.24777 -0.04764 -0.00677 0.53940  223 PHE   A CD2 
1706 C CE1 . PHE   A 223 ? 1.22891 0.86444 1.29345 -0.03522 -0.00913 0.50096  223 PHE   A CE1 
1707 C CE2 . PHE   A 223 ? 1.19332 0.90042 1.24835 -0.03778 -0.01268 0.54994  223 PHE   A CE2 
1708 C CZ  . PHE   A 223 ? 1.17788 0.82379 1.24537 -0.03090 -0.01314 0.53004  223 PHE   A CZ  
1709 N N   . THR   A 224 ? 1.07380 0.97179 1.06969 -0.09021 0.02507  0.50435  224 THR   A N   
1710 C CA  . THR   A 224 ? 1.06714 1.00533 1.05398 -0.09857 0.03697  0.49233  224 THR   A CA  
1711 C C   . THR   A 224 ? 1.05167 0.96696 1.06202 -0.11512 0.03773  0.48436  224 THR   A C   
1712 O O   . THR   A 224 ? 1.08571 0.95840 1.11461 -0.12411 0.02980  0.49155  224 THR   A O   
1713 C CB  . THR   A 224 ? 1.07091 1.06061 1.04033 -0.10422 0.04635  0.50866  224 THR   A CB  
1714 O OG1 . THR   A 224 ? 1.04647 1.07786 0.99431 -0.09975 0.05837  0.49169  224 THR   A OG1 
1715 C CG2 . THR   A 224 ? 0.92180 0.91422 0.91057 -0.12354 0.05028  0.52476  224 THR   A CG2 
1716 N N   . THR   A 225 ? 0.97625 0.91940 0.98522 -0.11932 0.04679  0.46870  225 THR   A N   
1717 C CA  . THR   A 225 ? 1.06317 0.99347 1.09513 -0.13649 0.04611  0.46140  225 THR   A CA  
1718 C C   . THR   A 225 ? 1.07792 1.06396 1.10936 -0.14203 0.06040  0.45852  225 THR   A C   
1719 O O   . THR   A 225 ? 1.07994 1.10724 1.08965 -0.13098 0.07190  0.45755  225 THR   A O   
1720 C CB  . THR   A 225 ? 1.05826 0.94554 1.09724 -0.13310 0.03818  0.43826  225 THR   A CB  
1721 O OG1 . THR   A 225 ? 1.18338 1.03058 1.21638 -0.11735 0.02986  0.43691  225 THR   A OG1 
1722 C CG2 . THR   A 225 ? 1.02449 0.87841 1.08630 -0.15427 0.03020  0.43477  225 THR   A CG2 
1723 N N   . THR   A 226 ? 1.06011 1.04647 1.11553 -0.15905 0.05944  0.45646  226 THR   A N   
1724 C CA  . THR   A 226 ? 0.98899 1.02504 1.05237 -0.16285 0.07219  0.45175  226 THR   A CA  
1725 C C   . THR   A 226 ? 0.95121 0.97676 1.02112 -0.16109 0.06955  0.42835  226 THR   A C   
1726 O O   . THR   A 226 ? 0.89531 0.87181 0.96838 -0.16342 0.05613  0.41734  226 THR   A O   
1727 C CB  . THR   A 226 ? 1.05153 1.10423 1.14183 -0.18382 0.07185  0.46928  226 THR   A CB  
1728 O OG1 . THR   A 226 ? 1.26067 1.31006 1.34677 -0.18756 0.07068  0.49247  226 THR   A OG1 
1729 C CG2 . THR   A 226 ? 1.08211 1.19697 1.18046 -0.18241 0.08878  0.46979  226 THR   A CG2 
1730 N N   . LEU   A 227 ? 0.94969 1.02134 1.02087 -0.15554 0.08347  0.42037  227 LEU   A N   
1731 C CA  . LEU   A 227 ? 0.84415 0.91140 0.92130 -0.15052 0.08065  0.39189  227 LEU   A CA  
1732 C C   . LEU   A 227 ? 0.86095 0.90170 0.96515 -0.17249 0.06515  0.39179  227 LEU   A C   
1733 O O   . LEU   A 227 ? 0.85730 0.86961 0.95916 -0.16918 0.05495  0.36484  227 LEU   A O   
1734 C CB  . LEU   A 227 ? 0.77010 0.89286 0.84925 -0.14076 0.09926  0.38661  227 LEU   A CB  
1735 C CG  . LEU   A 227 ? 0.76944 0.89322 0.84599 -0.12635 0.09993  0.35345  227 LEU   A CG  
1736 C CD1 . LEU   A 227 ? 0.72782 0.80847 0.77960 -0.11208 0.08956  0.32648  227 LEU   A CD1 
1737 C CD2 . LEU   A 227 ? 0.77851 0.95123 0.84825 -0.11056 0.12206  0.34988  227 LEU   A CD2 
1738 N N   . ASN   A 228 ? 0.93638 0.98571 1.06294 -0.19391 0.06190  0.41589  228 ASN   A N   
1739 C CA  . ASN   A 228 ? 0.92774 0.95212 1.07718 -0.21733 0.04506  0.41334  228 ASN   A CA  
1740 C C   . ASN   A 228 ? 0.93555 0.88717 1.07428 -0.22333 0.02820  0.40570  228 ASN   A C   
1741 O O   . ASN   A 228 ? 0.93497 0.85023 1.07453 -0.23176 0.01521  0.38779  228 ASN   A O   
1742 C CB  . ASN   A 228 ? 0.84313 0.89991 1.01826 -0.23551 0.04541  0.43465  228 ASN   A CB  
1743 C CG  . ASN   A 228 ? 0.85252 0.98000 1.04221 -0.22790 0.06267  0.44083  228 ASN   A CG  
1744 O OD1 . ASN   A 228 ? 0.80338 0.95504 1.01479 -0.23449 0.05998  0.43557  228 ASN   A OD1 
1745 N ND2 . ASN   A 228 ? 0.83261 0.99334 1.00972 -0.21313 0.08051  0.45177  228 ASN   A ND2 
1746 N N   . ASP   A 229 ? 0.92151 0.85037 1.04907 -0.21791 0.02855  0.41833  229 ASP   A N   
1747 C CA  . ASP   A 229 ? 1.04942 0.90748 1.16896 -0.21997 0.01481  0.41160  229 ASP   A CA  
1748 C C   . ASP   A 229 ? 1.06521 0.89253 1.16557 -0.20003 0.01315  0.38756  229 ASP   A C   
1749 O O   . ASP   A 229 ? 1.04427 0.81722 1.14001 -0.20245 0.00164  0.36712  229 ASP   A O   
1750 C CB  . ASP   A 229 ? 1.08979 0.93495 1.20425 -0.21588 0.01636  0.43272  229 ASP   A CB  
1751 C CG  . ASP   A 229 ? 1.23981 1.01541 1.35700 -0.22635 0.00255  0.43106  229 ASP   A CG  
1752 O OD1 . ASP   A 229 ? 1.38374 1.12524 1.50630 -0.24097 -0.00825 0.41366  229 ASP   A OD1 
1753 O OD2 . ASP   A 229 ? 1.30895 1.06276 1.42136 -0.21986 0.00247  0.44619  229 ASP   A OD2 
1754 N N   . PHE   A 230 ? 1.00014 0.86310 1.08404 -0.17575 0.02513  0.37914  230 PHE   A N   
1755 C CA  . PHE   A 230 ? 0.97919 0.82229 1.04381 -0.15266 0.02409  0.34669  230 PHE   A CA  
1756 C C   . PHE   A 230 ? 0.97423 0.81001 1.04173 -0.15775 0.01838  0.31819  230 PHE   A C   
1757 O O   . PHE   A 230 ? 0.99997 0.79383 1.05674 -0.15002 0.01143  0.29400  230 PHE   A O   
1758 C CB  . PHE   A 230 ? 0.93509 0.82185 0.98238 -0.13068 0.03676  0.34311  230 PHE   A CB  
1759 C CG  . PHE   A 230 ? 0.89729 0.78296 0.93081 -0.11228 0.03764  0.30904  230 PHE   A CG  
1760 C CD1 . PHE   A 230 ? 0.88062 0.73053 0.90257 -0.09637 0.03223  0.29422  230 PHE   A CD1 
1761 C CD2 . PHE   A 230 ? 0.91889 0.84026 0.95355 -0.11026 0.04454  0.29392  230 PHE   A CD2 
1762 C CE1 . PHE   A 230 ? 0.82908 0.68033 0.84015 -0.08102 0.03338  0.26537  230 PHE   A CE1 
1763 C CE2 . PHE   A 230 ? 0.85149 0.77004 0.87437 -0.09466 0.04493  0.26492  230 PHE   A CE2 
1764 C CZ  . PHE   A 230 ? 0.82495 0.70926 0.83564 -0.08111 0.03922  0.25087  230 PHE   A CZ  
1765 N N   . ASN   A 231 ? 0.93438 0.81280 1.01685 -0.17024 0.02170  0.32227  231 ASN   A N   
1766 C CA  . ASN   A 231 ? 0.95653 0.83404 1.04313 -0.17635 0.01480  0.29926  231 ASN   A CA  
1767 C C   . ASN   A 231 ? 1.05780 0.88016 1.14664 -0.19697 -0.00234 0.29245  231 ASN   A C   
1768 O O   . ASN   A 231 ? 1.08354 0.88108 1.16103 -0.19524 -0.00984 0.26550  231 ASN   A O   
1769 C CB  . ASN   A 231 ? 0.90268 0.83955 1.01133 -0.18652 0.02114  0.31158  231 ASN   A CB  
1770 C CG  . ASN   A 231 ? 0.83045 0.81228 0.93116 -0.16276 0.03739  0.30250  231 ASN   A CG  
1771 O OD1 . ASN   A 231 ? 0.79611 0.76566 0.87864 -0.14439 0.03817  0.27707  231 ASN   A OD1 
1772 N ND2 . ASN   A 231 ? 0.85040 0.88358 0.96425 -0.16319 0.05140  0.32339  231 ASN   A ND2 
1773 N N   . LEU   A 232 ? 1.06625 0.86701 1.16737 -0.21738 -0.00853 0.31647  232 LEU   A N   
1774 C CA  . LEU   A 232 ? 1.10527 0.84880 1.20722 -0.24070 -0.02545 0.31015  232 LEU   A CA  
1775 C C   . LEU   A 232 ? 1.14054 0.81998 1.21671 -0.22363 -0.02887 0.28248  232 LEU   A C   
1776 O O   . LEU   A 232 ? 1.16684 0.81007 1.23094 -0.23155 -0.03904 0.25738  232 LEU   A O   
1777 C CB  . LEU   A 232 ? 1.07866 0.80833 1.19885 -0.26424 -0.03003 0.34386  232 LEU   A CB  
1778 C CG  . LEU   A 232 ? 1.16522 0.93058 1.30963 -0.29217 -0.03677 0.35520  232 LEU   A CG  
1779 C CD1 . LEU   A 232 ? 1.12346 0.96729 1.28445 -0.28833 -0.02654 0.36320  232 LEU   A CD1 
1780 C CD2 . LEU   A 232 ? 1.06667 0.83210 1.22381 -0.30256 -0.03570 0.37986  232 LEU   A CD2 
1781 N N   . VAL   A 233 ? 1.15046 0.81780 1.21761 -0.19965 -0.02007 0.28738  233 VAL   A N   
1782 C CA  . VAL   A 233 ? 1.18653 0.80065 1.23377 -0.17936 -0.02050 0.26339  233 VAL   A CA  
1783 C C   . VAL   A 233 ? 1.17926 0.81491 1.21129 -0.15916 -0.01512 0.23367  233 VAL   A C   
1784 O O   . VAL   A 233 ? 1.22105 0.81587 1.23650 -0.14661 -0.01608 0.20877  233 VAL   A O   
1785 C CB  . VAL   A 233 ? 1.17417 0.77376 1.22171 -0.16034 -0.01418 0.28250  233 VAL   A CB  
1786 C CG1 . VAL   A 233 ? 1.13816 0.68376 1.19522 -0.17765 -0.02213 0.30266  233 VAL   A CG1 
1787 C CG2 . VAL   A 233 ? 1.12341 0.78822 1.17747 -0.15294 -0.00427 0.30592  233 VAL   A CG2 
1788 N N   . ALA   A 234 ? 1.11701 0.81473 1.15443 -0.15549 -0.00843 0.23595  234 ALA   A N   
1789 C CA  . ALA   A 234 ? 1.09193 0.80933 1.11653 -0.13733 -0.00349 0.21026  234 ALA   A CA  
1790 C C   . ALA   A 234 ? 1.11117 0.81191 1.12900 -0.15059 -0.01301 0.18747  234 ALA   A C   
1791 O O   . ALA   A 234 ? 1.08868 0.77715 1.08982 -0.13648 -0.01162 0.16247  234 ALA   A O   
1792 C CB  . ALA   A 234 ? 0.99147 0.77378 1.02306 -0.12956 0.00688  0.21910  234 ALA   A CB  
1793 N N   . MET   A 235 ? 1.07538 0.77814 1.10576 -0.17896 -0.02337 0.19707  235 MET   A N   
1794 C CA  . MET   A 235 ? 1.13122 0.82007 1.15291 -0.19477 -0.03526 0.17691  235 MET   A CA  
1795 C C   . MET   A 235 ? 1.18011 0.79527 1.17884 -0.19898 -0.04324 0.15648  235 MET   A C   
1796 O O   . MET   A 235 ? 1.20012 0.79683 1.17854 -0.20063 -0.04873 0.13082  235 MET   A O   
1797 C CB  . MET   A 235 ? 1.16396 0.88470 1.20897 -0.22535 -0.04546 0.19559  235 MET   A CB  
1798 C CG  . MET   A 235 ? 1.24047 1.02693 1.31169 -0.22126 -0.03413 0.22252  235 MET   A CG  
1799 S SD  . MET   A 235 ? 1.94924 1.77857 2.05576 -0.25651 -0.04403 0.25060  235 MET   A SD  
1800 C CE  . MET   A 235 ? 1.30265 1.21223 1.43095 -0.23685 -0.02292 0.27064  235 MET   A CE  
1801 N N   . LYS   A 236 ? 1.15552 0.72667 1.15560 -0.19982 -0.04309 0.16740  236 LYS   A N   
1802 C CA  . LYS   A 236 ? 1.22185 0.71773 1.19904 -0.19807 -0.04702 0.14606  236 LYS   A CA  
1803 C C   . LYS   A 236 ? 1.21751 0.70303 1.17547 -0.16444 -0.03494 0.12287  236 LYS   A C   
1804 O O   . LYS   A 236 ? 1.22959 0.66503 1.16318 -0.16059 -0.03600 0.09645  236 LYS   A O   
1805 C CB  . LYS   A 236 ? 1.30650 0.75649 1.29309 -0.20375 -0.04838 0.16602  236 LYS   A CB  
1806 C CG  . LYS   A 236 ? 1.37676 0.74015 1.34136 -0.20848 -0.05410 0.14489  236 LYS   A CG  
1807 C CD  . LYS   A 236 ? 1.44267 0.78669 1.38388 -0.23012 -0.06637 0.11612  236 LYS   A CD  
1808 C CE  . LYS   A 236 ? 1.45438 0.71351 1.37830 -0.25212 -0.07773 0.10401  236 LYS   A CE  
1809 N NZ  . LYS   A 236 ? 1.49671 0.74809 1.40279 -0.28608 -0.09568 0.08571  236 LYS   A NZ  
1810 N N   . TYR   A 237 ? 1.20838 0.74117 1.17594 -0.14090 -0.02320 0.13210  237 TYR   A N   
1811 C CA  . TYR   A 237 ? 1.13926 0.67309 1.09414 -0.11058 -0.01221 0.11434  237 TYR   A CA  
1812 C C   . TYR   A 237 ? 1.10809 0.68864 1.05728 -0.10633 -0.01004 0.10022  237 TYR   A C   
1813 O O   . TYR   A 237 ? 1.04758 0.64650 0.99269 -0.08276 -0.00045 0.09212  237 TYR   A O   
1814 C CB  . TYR   A 237 ? 1.08660 0.63791 1.05458 -0.08838 -0.00269 0.13407  237 TYR   A CB  
1815 C CG  . TYR   A 237 ? 1.15471 0.65038 1.12101 -0.07438 0.00024  0.13596  237 TYR   A CG  
1816 C CD1 . TYR   A 237 ? 1.15835 0.63489 1.13897 -0.08112 -0.00265 0.16267  237 TYR   A CD1 
1817 C CD2 . TYR   A 237 ? 1.22402 0.68702 1.17590 -0.05319 0.00711  0.11266  237 TYR   A CD2 
1818 C CE1 . TYR   A 237 ? 1.22004 0.64369 1.20192 -0.06628 0.00034  0.16649  237 TYR   A CE1 
1819 C CE2 . TYR   A 237 ? 1.14240 0.55450 1.09586 -0.03695 0.01179  0.11509  237 TYR   A CE2 
1820 C CZ  . TYR   A 237 ? 1.22836 0.61953 1.19746 -0.04318 0.00793  0.14220  237 TYR   A CZ  
1821 O OH  . TYR   A 237 ? 1.37472 0.71333 1.34822 -0.02525 0.01278  0.14691  237 TYR   A OH  
1822 N N   . ASN   A 238 ? 1.08202 0.68294 1.03312 -0.12933 -0.01950 0.09920  238 ASN   A N   
1823 C CA  . ASN   A 238 ? 1.10897 0.75160 1.05639 -0.12685 -0.01889 0.08809  238 ASN   A CA  
1824 C C   . ASN   A 238 ? 1.05792 0.75201 1.01831 -0.10716 -0.00737 0.09839  238 ASN   A C   
1825 O O   . ASN   A 238 ? 1.08202 0.79238 1.03417 -0.09087 -0.00117 0.08496  238 ASN   A O   
1826 C CB  . ASN   A 238 ? 1.20856 0.82172 1.12837 -0.11830 -0.01821 0.05889  238 ASN   A CB  
1827 C CG  . ASN   A 238 ? 1.43224 1.02038 1.33549 -0.14447 -0.03264 0.04575  238 ASN   A CG  
1828 O OD1 . ASN   A 238 ? 1.42938 1.05005 1.34457 -0.16554 -0.04312 0.05586  238 ASN   A OD1 
1829 N ND2 . ASN   A 238 ? 1.54849 1.07924 1.42382 -0.14337 -0.03326 0.02335  238 ASN   A ND2 
1830 N N   . TYR   A 239 ? 1.05788 0.77631 1.03676 -0.10981 -0.00442 0.12230  239 TYR   A N   
1831 C CA  . TYR   A 239 ? 0.96759 0.73410 0.95529 -0.09509 0.00589  0.13183  239 TYR   A CA  
1832 C C   . TYR   A 239 ? 0.93261 0.74494 0.93706 -0.10833 0.00524  0.14360  239 TYR   A C   
1833 O O   . TYR   A 239 ? 0.88544 0.69779 0.90197 -0.13050 -0.00306 0.15499  239 TYR   A O   
1834 C CB  . TYR   A 239 ? 0.95304 0.71875 0.94587 -0.08638 0.01164  0.15067  239 TYR   A CB  
1835 C CG  . TYR   A 239 ? 0.90053 0.64841 0.88259 -0.06339 0.01680  0.14211  239 TYR   A CG  
1836 C CD1 . TYR   A 239 ? 0.93597 0.64123 0.90650 -0.05643 0.01487  0.12382  239 TYR   A CD1 
1837 C CD2 . TYR   A 239 ? 0.85023 0.62593 0.83347 -0.04892 0.02376  0.15280  239 TYR   A CD2 
1838 C CE1 . TYR   A 239 ? 0.97158 0.66648 0.93770 -0.03409 0.02072  0.11876  239 TYR   A CE1 
1839 C CE2 . TYR   A 239 ? 0.88142 0.64695 0.85900 -0.02942 0.02665  0.14797  239 TYR   A CE2 
1840 C CZ  . TYR   A 239 ? 0.95064 0.67784 0.92251 -0.02128 0.02559  0.13214  239 TYR   A CZ  
1841 O OH  . TYR   A 239 ? 0.90379 0.62679 0.87520 -0.00051 0.02958  0.12997  239 TYR   A OH  
1842 N N   . GLU   A 240 ? 0.88648 0.73748 0.89303 -0.09457 0.01413  0.14112  240 GLU   A N   
1843 C CA  . GLU   A 240 ? 0.89579 0.79254 0.92071 -0.10141 0.01728  0.15323  240 GLU   A CA  
1844 C C   . GLU   A 240 ? 0.83045 0.74574 0.87037 -0.10968 0.02190  0.17879  240 GLU   A C   
1845 O O   . GLU   A 240 ? 0.82621 0.73480 0.85876 -0.10065 0.02796  0.18614  240 GLU   A O   
1846 C CB  . GLU   A 240 ? 0.86297 0.78959 0.88485 -0.08210 0.02818  0.14476  240 GLU   A CB  
1847 C CG  . GLU   A 240 ? 0.92310 0.84698 0.93867 -0.07879 0.02368  0.12648  240 GLU   A CG  
1848 C CD  . GLU   A 240 ? 1.01191 0.95472 1.04361 -0.09552 0.01513  0.13275  240 GLU   A CD  
1849 O OE1 . GLU   A 240 ? 1.02040 1.00183 1.07363 -0.09747 0.02070  0.14860  240 GLU   A OE1 
1850 O OE2 . GLU   A 240 ? 1.09031 1.01081 1.11283 -0.10672 0.00298  0.12235  240 GLU   A OE2 
1851 N N   . PRO   A 241 ? 0.81234 0.75380 0.87419 -0.12741 0.01888  0.19491  241 PRO   A N   
1852 C CA  . PRO   A 241 ? 0.82131 0.78789 0.89894 -0.13469 0.02599  0.22157  241 PRO   A CA  
1853 C C   . PRO   A 241 ? 0.81042 0.81301 0.88383 -0.11409 0.04412  0.22470  241 PRO   A C   
1854 O O   . PRO   A 241 ? 0.84921 0.87747 0.92454 -0.10205 0.05147  0.21493  241 PRO   A O   
1855 C CB  . PRO   A 241 ? 0.79556 0.79131 0.90136 -0.15663 0.01934  0.23650  241 PRO   A CB  
1856 C CG  . PRO   A 241 ? 0.85978 0.85973 0.96438 -0.15427 0.01260  0.21807  241 PRO   A CG  
1857 C CD  . PRO   A 241 ? 0.88781 0.84137 0.96227 -0.14234 0.00842  0.19188  241 PRO   A CD  
1858 N N   . LEU   A 242 ? 0.79739 0.79903 0.86278 -0.11026 0.05095  0.23816  242 LEU   A N   
1859 C CA  . LEU   A 242 ? 0.74622 0.77906 0.80095 -0.09319 0.06758  0.24065  242 LEU   A CA  
1860 C C   . LEU   A 242 ? 0.72157 0.80310 0.79677 -0.09858 0.08029  0.26100  242 LEU   A C   
1861 O O   . LEU   A 242 ? 0.63357 0.72437 0.72593 -0.11594 0.07850  0.28512  242 LEU   A O   
1862 C CB  . LEU   A 242 ? 0.74298 0.75923 0.77873 -0.08785 0.06870  0.24894  242 LEU   A CB  
1863 C CG  . LEU   A 242 ? 0.75724 0.78886 0.76882 -0.06825 0.07983  0.23947  242 LEU   A CG  
1864 C CD1 . LEU   A 242 ? 0.70273 0.71310 0.70118 -0.05498 0.07462  0.21184  242 LEU   A CD1 
1865 C CD2 . LEU   A 242 ? 0.69495 0.72337 0.69161 -0.06742 0.08075  0.25700  242 LEU   A CD2 
1866 N N   . THR   A 243 ? 0.69514 0.80729 0.76975 -0.08327 0.09411  0.25213  243 THR   A N   
1867 C CA  . THR   A 243 ? 0.71376 0.87509 0.80786 -0.08261 0.11061  0.26959  243 THR   A CA  
1868 C C   . THR   A 243 ? 0.64228 0.82138 0.71282 -0.06899 0.12932  0.27372  243 THR   A C   
1869 O O   . THR   A 243 ? 0.64099 0.79686 0.68032 -0.05958 0.12798  0.26108  243 THR   A O   
1870 C CB  . THR   A 243 ? 0.66802 0.85196 0.77888 -0.07264 0.11598  0.25868  243 THR   A CB  
1871 O OG1 . THR   A 243 ? 0.70104 0.87275 0.78584 -0.05107 0.12361  0.23422  243 THR   A OG1 
1872 C CG2 . THR   A 243 ? 0.56417 0.73213 0.69312 -0.08722 0.09575  0.25420  243 THR   A CG2 
1873 N N   . GLN   A 244 ? 0.63891 0.86250 0.72454 -0.06861 0.14701  0.29264  244 GLN   A N   
1874 C CA  . GLN   A 244 ? 0.68925 0.93282 0.74802 -0.05442 0.16772  0.29383  244 GLN   A CA  
1875 C C   . GLN   A 244 ? 0.70258 0.93787 0.73657 -0.03200 0.17682  0.26395  244 GLN   A C   
1876 O O   . GLN   A 244 ? 0.71306 0.94283 0.71033 -0.02194 0.18502  0.25447  244 GLN   A O   
1877 C CB  . GLN   A 244 ? 0.63645 0.93228 0.71800 -0.05664 0.18799  0.31947  244 GLN   A CB  
1878 C CG  . GLN   A 244 ? 0.76218 1.06915 0.83703 -0.07006 0.19095  0.34749  244 GLN   A CG  
1879 C CD  . GLN   A 244 ? 0.80615 1.09869 0.83241 -0.05944 0.19642  0.33859  244 GLN   A CD  
1880 O OE1 . GLN   A 244 ? 0.81739 1.11549 0.81618 -0.04038 0.21111  0.31808  244 GLN   A OE1 
1881 N NE2 . GLN   A 244 ? 0.85045 1.12298 0.86562 -0.07234 0.18362  0.35442  244 GLN   A NE2 
1882 N N   . ASP   A 245 ? 0.69788 0.93117 0.75059 -0.02562 0.17408  0.24978  245 ASP   A N   
1883 C CA  . ASP   A 245 ? 0.66355 0.88234 0.69534 -0.00628 0.18030  0.22179  245 ASP   A CA  
1884 C C   . ASP   A 245 ? 0.66007 0.83800 0.65857 -0.00598 0.16577  0.20336  245 ASP   A C   
1885 O O   . ASP   A 245 ? 0.67992 0.84998 0.64542 0.00537  0.17349  0.18785  245 ASP   A O   
1886 C CB  . ASP   A 245 ? 0.72716 0.94900 0.78884 -0.00254 0.17584  0.21488  245 ASP   A CB  
1887 C CG  . ASP   A 245 ? 0.80214 1.06313 0.88579 0.01161  0.19828  0.22160  245 ASP   A CG  
1888 O OD1 . ASP   A 245 ? 0.90147 1.16935 1.01134 0.01708  0.19605  0.21875  245 ASP   A OD1 
1889 O OD2 . ASP   A 245 ? 0.91308 1.19926 0.98802 0.01810  0.21884  0.23094  245 ASP   A OD2 
1890 N N   . HIS   A 246 ? 0.61489 0.76681 0.62168 -0.01867 0.14473  0.20482  246 HIS   A N   
1891 C CA  . HIS   A 246 ? 0.70056 0.81811 0.68175 -0.01753 0.13167  0.19123  246 HIS   A CA  
1892 C C   . HIS   A 246 ? 0.69252 0.81363 0.64571 -0.01705 0.13615  0.19981  246 HIS   A C   
1893 O O   . HIS   A 246 ? 0.72564 0.83401 0.65047 -0.00936 0.13421  0.18525  246 HIS   A O   
1894 C CB  . HIS   A 246 ? 0.71673 0.80703 0.71241 -0.03050 0.11191  0.19472  246 HIS   A CB  
1895 C CG  . HIS   A 246 ? 0.72950 0.81286 0.74451 -0.03213 0.10438  0.18382  246 HIS   A CG  
1896 N ND1 . HIS   A 246 ? 0.73368 0.80256 0.76653 -0.04725 0.09006  0.18995  246 HIS   A ND1 
1897 C CD2 . HIS   A 246 ? 0.63499 0.72248 0.65211 -0.02137 0.10844  0.16770  246 HIS   A CD2 
1898 C CE1 . HIS   A 246 ? 0.68280 0.75097 0.72634 -0.04616 0.08527  0.17850  246 HIS   A CE1 
1899 N NE2 . HIS   A 246 ? 0.74049 0.82046 0.77667 -0.03002 0.09636  0.16634  246 HIS   A NE2 
1900 N N   . VAL   A 247 ? 0.61811 0.75818 0.57911 -0.02684 0.14091  0.22526  247 VAL   A N   
1901 C CA  . VAL   A 247 ? 0.67077 0.81742 0.60427 -0.02748 0.14472  0.23738  247 VAL   A CA  
1902 C C   . VAL   A 247 ? 0.74882 0.91059 0.64916 -0.01355 0.16103  0.22176  247 VAL   A C   
1903 O O   . VAL   A 247 ? 0.75770 0.91093 0.62460 -0.01064 0.15706  0.21536  247 VAL   A O   
1904 C CB  . VAL   A 247 ? 0.72541 0.89488 0.67540 -0.04086 0.15000  0.26991  247 VAL   A CB  
1905 C CG1 . VAL   A 247 ? 0.71806 0.91061 0.63680 -0.03831 0.16306  0.28291  247 VAL   A CG1 
1906 C CG2 . VAL   A 247 ? 0.71687 0.85828 0.68554 -0.05597 0.13050  0.28474  247 VAL   A CG2 
1907 N N   . ASP   A 248 ? 0.70118 0.88408 0.61021 -0.00458 0.17899  0.21464  248 ASP   A N   
1908 C CA  . ASP   A 248 ? 0.67838 0.87099 0.55392 0.00950  0.19736  0.19778  248 ASP   A CA  
1909 C C   . ASP   A 248 ? 0.73170 0.89377 0.58516 0.01743  0.18860  0.16759  248 ASP   A C   
1910 O O   . ASP   A 248 ? 0.79954 0.95818 0.61371 0.02374  0.19565  0.15242  248 ASP   A O   
1911 C CB  . ASP   A 248 ? 0.73970 0.96109 0.63545 0.01980  0.22056  0.19915  248 ASP   A CB  
1912 C CG  . ASP   A 248 ? 0.71780 0.97749 0.63274 0.01214  0.23299  0.23048  248 ASP   A CG  
1913 O OD1 . ASP   A 248 ? 0.75582 1.02171 0.65124 0.00275  0.23105  0.24740  248 ASP   A OD1 
1914 O OD2 . ASP   A 248 ? 0.67494 0.96094 0.62666 0.01497  0.24419  0.24052  248 ASP   A OD2 
1915 N N   . ILE   A 249 ? 0.70073 0.84076 0.57705 0.01583  0.17317  0.15867  249 ILE   A N   
1916 C CA  . ILE   A 249 ? 0.73374 0.84699 0.59253 0.02145  0.16423  0.13319  249 ILE   A CA  
1917 C C   . ILE   A 249 ? 0.73661 0.83685 0.56974 0.01494  0.14879  0.13400  249 ILE   A C   
1918 O O   . ILE   A 249 ? 0.76302 0.85332 0.56587 0.01806  0.14661  0.11674  249 ILE   A O   
1919 C CB  . ILE   A 249 ? 0.68278 0.78024 0.57298 0.02139  0.15341  0.12608  249 ILE   A CB  
1920 C CG1 . ILE   A 249 ? 0.74048 0.85054 0.65027 0.03141  0.16861  0.12100  249 ILE   A CG1 
1921 C CG2 . ILE   A 249 ? 0.73251 0.80352 0.60808 0.02332  0.14073  0.10610  249 ILE   A CG2 
1922 C CD1 . ILE   A 249 ? 0.72847 0.83825 0.67642 0.02690  0.15913  0.12732  249 ILE   A CD1 
1923 N N   . LEU   A 250 ? 0.71228 0.81250 0.55806 0.00537  0.13740  0.15528  250 LEU   A N   
1924 C CA  . LEU   A 250 ? 0.71948 0.81062 0.54687 0.00095  0.12269  0.16108  250 LEU   A CA  
1925 C C   . LEU   A 250 ? 0.74197 0.85190 0.53212 -0.00022 0.12979  0.16832  250 LEU   A C   
1926 O O   . LEU   A 250 ? 0.70231 0.80904 0.47272 -0.00334 0.11706  0.17206  250 LEU   A O   
1927 C CB  . LEU   A 250 ? 0.67167 0.75323 0.52468 -0.00712 0.11022  0.18277  250 LEU   A CB  
1928 C CG  . LEU   A 250 ? 0.61294 0.67071 0.49432 -0.00715 0.09991  0.17364  250 LEU   A CG  
1929 C CD1 . LEU   A 250 ? 0.61164 0.65817 0.51686 -0.01641 0.09226  0.19402  250 LEU   A CD1 
1930 C CD2 . LEU   A 250 ? 0.65148 0.69175 0.52395 -0.00181 0.08783  0.15811  250 LEU   A CD2 
1931 N N   . GLY   A 251 ? 0.75031 0.88191 0.53034 0.00259  0.15000  0.17099  251 GLY   A N   
1932 C CA  . GLY   A 251 ? 0.77630 0.92868 0.51853 0.00093  0.15970  0.17977  251 GLY   A CA  
1933 C C   . GLY   A 251 ? 0.81616 0.96094 0.51332 0.00151  0.15300  0.16125  251 GLY   A C   
1934 O O   . GLY   A 251 ? 0.82000 0.97323 0.49235 -0.00546 0.14328  0.17495  251 GLY   A O   
1935 N N   . PRO   A 252 ? 0.87031 0.99973 0.55546 0.00867  0.15762  0.13109  252 PRO   A N   
1936 C CA  . PRO   A 252 ? 0.98072 1.09787 0.62725 0.00547  0.14608  0.11186  252 PRO   A CA  
1937 C C   . PRO   A 252 ? 0.92043 1.03387 0.57368 -0.00311 0.11996  0.12485  252 PRO   A C   
1938 O O   . PRO   A 252 ? 0.88184 1.00440 0.50067 -0.01019 0.11012  0.12900  252 PRO   A O   
1939 C CB  . PRO   A 252 ? 0.90307 0.99664 0.55764 0.01317  0.15025  0.08236  252 PRO   A CB  
1940 C CG  . PRO   A 252 ? 0.92104 1.02383 0.59379 0.02382  0.17454  0.08299  252 PRO   A CG  
1941 C CD  . PRO   A 252 ? 0.82339 0.94810 0.52682 0.01950  0.17488  0.11493  252 PRO   A CD  
1942 N N   . LEU   A 253 ? 0.83015 0.93178 0.52653 -0.00218 0.10891  0.13224  253 LEU   A N   
1943 C CA  . LEU   A 253 ? 0.80819 0.90685 0.51647 -0.00679 0.08723  0.14697  253 LEU   A CA  
1944 C C   . LEU   A 253 ? 0.83483 0.95114 0.53736 -0.01207 0.08408  0.17853  253 LEU   A C   
1945 O O   . LEU   A 253 ? 0.85470 0.97935 0.54180 -0.01655 0.06914  0.19034  253 LEU   A O   
1946 C CB  . LEU   A 253 ? 0.76867 0.84875 0.52169 -0.00295 0.08061  0.14703  253 LEU   A CB  
1947 C CG  . LEU   A 253 ? 0.69701 0.76035 0.45769 0.00055  0.07569  0.12187  253 LEU   A CG  
1948 C CD1 . LEU   A 253 ? 0.70015 0.74762 0.50048 0.00395  0.07008  0.12456  253 LEU   A CD1 
1949 C CD2 . LEU   A 253 ? 0.76302 0.82943 0.50230 -0.00376 0.06076  0.11547  253 LEU   A CD2 
1950 N N   . SER   A 254 ? 0.85144 0.97560 0.56846 -0.01242 0.09718  0.19502  254 SER   A N   
1951 C CA  . SER   A 254 ? 0.82111 0.96211 0.53231 -0.01865 0.09578  0.22736  254 SER   A CA  
1952 C C   . SER   A 254 ? 0.84651 1.00939 0.50672 -0.02283 0.09711  0.22929  254 SER   A C   
1953 O O   . SER   A 254 ? 0.87145 1.04599 0.52095 -0.02839 0.08518  0.25400  254 SER   A O   
1954 C CB  . SER   A 254 ? 0.76655 0.91656 0.49908 -0.02052 0.11216  0.24298  254 SER   A CB  
1955 O OG  . SER   A 254 ? 0.84446 1.00956 0.57414 -0.02805 0.11083  0.27710  254 SER   A OG  
1956 N N   . ALA   A 255 ? 0.84947 1.01637 0.47617 -0.02016 0.11093  0.20331  255 ALA   A N   
1957 C CA  . ALA   A 255 ? 0.84587 1.03142 0.41663 -0.02532 0.11378  0.20193  255 ALA   A CA  
1958 C C   . ALA   A 255 ? 0.93319 1.11612 0.48269 -0.03190 0.08918  0.19740  255 ALA   A C   
1959 O O   . ALA   A 255 ? 0.97827 1.18102 0.49251 -0.03997 0.08079  0.21288  255 ALA   A O   
1960 C CB  . ALA   A 255 ? 0.93644 1.12078 0.47582 -0.01926 0.13699  0.17220  255 ALA   A CB  
1961 N N   . GLN   A 256 ? 0.88368 1.04588 0.45508 -0.02945 0.07679  0.17860  256 GLN   A N   
1962 C CA  . GLN   A 256 ? 0.96329 1.12742 0.51875 -0.03666 0.05344  0.17459  256 GLN   A CA  
1963 C C   . GLN   A 256 ? 0.99265 1.16849 0.57396 -0.03846 0.03342  0.20897  256 GLN   A C   
1964 O O   . GLN   A 256 ? 0.99652 1.18797 0.55824 -0.04602 0.01426  0.21779  256 GLN   A O   
1965 C CB  . GLN   A 256 ? 1.04690 1.18783 0.62023 -0.03385 0.04808  0.14571  256 GLN   A CB  
1966 C CG  . GLN   A 256 ? 1.19037 1.33404 0.73386 -0.04442 0.02933  0.13151  256 GLN   A CG  
1967 C CD  . GLN   A 256 ? 1.34757 1.48288 0.93062 -0.04341 0.01196  0.12935  256 GLN   A CD  
1968 O OE1 . GLN   A 256 ? 1.43826 1.58423 1.05294 -0.04092 -0.00152 0.15454  256 GLN   A OE1 
1969 N NE2 . GLN   A 256 ? 1.49532 1.61101 1.07797 -0.04438 0.01352  0.10022  256 GLN   A NE2 
1970 N N   . THR   A 257 ? 1.06208 1.22997 0.68731 -0.03188 0.03688  0.22912  257 THR   A N   
1971 C CA  . THR   A 257 ? 0.96099 1.13284 0.61435 -0.03067 0.02031  0.26146  257 THR   A CA  
1972 C C   . THR   A 257 ? 0.91456 1.10347 0.55838 -0.03483 0.02357  0.29651  257 THR   A C   
1973 O O   . THR   A 257 ? 0.92550 1.11994 0.58549 -0.03430 0.00868  0.32661  257 THR   A O   
1974 C CB  . THR   A 257 ? 0.87931 1.02473 0.58615 -0.02134 0.02015  0.26136  257 THR   A CB  
1975 O OG1 . THR   A 257 ? 0.89387 1.02662 0.61186 -0.01956 0.03935  0.25136  257 THR   A OG1 
1976 C CG2 . THR   A 257 ? 0.86796 1.00244 0.58934 -0.01720 0.01029  0.23819  257 THR   A CG2 
1977 N N   . GLY   A 258 ? 0.95162 1.14992 0.57204 -0.03810 0.04339  0.29540  258 GLY   A N   
1978 C CA  . GLY   A 258 ? 0.89004 1.10639 0.50323 -0.04320 0.04854  0.33068  258 GLY   A CA  
1979 C C   . GLY   A 258 ? 0.83490 1.03474 0.49761 -0.04080 0.04900  0.35642  258 GLY   A C   
1980 O O   . GLY   A 258 ? 0.90532 1.11337 0.57168 -0.04541 0.04783  0.38697  258 GLY   A O   
1981 N N   . ILE   A 259 ? 0.89904 1.07050 0.60147 -0.03433 0.04950  0.34016  259 ILE   A N   
1982 C CA  . ILE   A 259 ? 0.84958 0.99832 0.59643 -0.03364 0.04957  0.35857  259 ILE   A CA  
1983 C C   . ILE   A 259 ? 0.82469 0.97024 0.58310 -0.03591 0.06873  0.34513  259 ILE   A C   
1984 O O   . ILE   A 259 ? 0.76844 0.90360 0.53292 -0.03085 0.07379  0.31405  259 ILE   A O   
1985 C CB  . ILE   A 259 ? 0.90586 1.02454 0.68747 -0.02487 0.03524  0.35060  259 ILE   A CB  
1986 C CG1 . ILE   A 259 ? 0.86020 0.98960 0.63260 -0.02074 0.01676  0.36060  259 ILE   A CG1 
1987 C CG2 . ILE   A 259 ? 0.86555 0.95517 0.68671 -0.02517 0.03432  0.36987  259 ILE   A CG2 
1988 C CD1 . ILE   A 259 ? 0.88170 0.98952 0.68374 -0.01010 0.00629  0.34629  259 ILE   A CD1 
1989 N N   . ALA   A 260 ? 0.85582 1.01296 0.61944 -0.04394 0.07894  0.37092  260 ALA   A N   
1990 C CA  . ALA   A 260 ? 0.80496 0.96479 0.58660 -0.04726 0.09603  0.36413  260 ALA   A CA  
1991 C C   . ALA   A 260 ? 0.81087 0.93750 0.63057 -0.04421 0.08995  0.34600  260 ALA   A C   
1992 O O   . ALA   A 260 ? 0.81537 0.91329 0.65513 -0.04217 0.07468  0.35054  260 ALA   A O   
1993 C CB  . ALA   A 260 ? 0.79153 0.96427 0.58529 -0.05856 0.10298  0.39917  260 ALA   A CB  
1994 N N   . VAL   A 261 ? 0.79955 0.93096 0.62776 -0.04274 0.10269  0.32508  261 VAL   A N   
1995 C CA  . VAL   A 261 ? 0.76276 0.86642 0.62256 -0.04102 0.09703  0.30717  261 VAL   A CA  
1996 C C   . VAL   A 261 ? 0.80366 0.88419 0.69607 -0.05122 0.08854  0.32940  261 VAL   A C   
1997 O O   . VAL   A 261 ? 0.78651 0.83280 0.69667 -0.04912 0.07614  0.32113  261 VAL   A O   
1998 C CB  . VAL   A 261 ? 0.71010 0.82868 0.57522 -0.03840 0.11247  0.28717  261 VAL   A CB  
1999 C CG1 . VAL   A 261 ? 0.70080 0.79618 0.60063 -0.04114 0.10622  0.27715  261 VAL   A CG1 
2000 C CG2 . VAL   A 261 ? 0.70590 0.83093 0.54129 -0.02702 0.11751  0.25869  261 VAL   A CG2 
2001 N N   . LEU   A 262 ? 0.79072 0.88801 0.69011 -0.06288 0.09556  0.35802  262 LEU   A N   
2002 C CA  . LEU   A 262 ? 0.77835 0.84996 0.70856 -0.07569 0.08697  0.37935  262 LEU   A CA  
2003 C C   . LEU   A 262 ? 0.86946 0.90915 0.80017 -0.07273 0.07134  0.39364  262 LEU   A C   
2004 O O   . LEU   A 262 ? 0.91011 0.91045 0.86461 -0.07749 0.06117  0.39718  262 LEU   A O   
2005 C CB  . LEU   A 262 ? 0.87180 0.97221 0.81103 -0.09055 0.09822  0.40990  262 LEU   A CB  
2006 C CG  . LEU   A 262 ? 0.89646 1.03594 0.84107 -0.09267 0.11667  0.40348  262 LEU   A CG  
2007 C CD1 . LEU   A 262 ? 0.87516 1.05247 0.78300 -0.08050 0.13350  0.39498  262 LEU   A CD1 
2008 C CD2 . LEU   A 262 ? 0.80788 0.95931 0.78023 -0.10946 0.11892  0.42566  262 LEU   A CD2 
2009 N N   . ASP   A 263 ? 0.86359 0.91884 0.76813 -0.06469 0.06903  0.40202  263 ASP   A N   
2010 C CA  . ASP   A 263 ? 0.86661 0.89587 0.77539 -0.05884 0.05398  0.41725  263 ASP   A CA  
2011 C C   . ASP   A 263 ? 0.89883 0.89819 0.81676 -0.04561 0.04465  0.38900  263 ASP   A C   
2012 O O   . ASP   A 263 ? 0.89083 0.85431 0.82741 -0.04090 0.03445  0.39661  263 ASP   A O   
2013 C CB  . ASP   A 263 ? 0.85243 0.91289 0.73071 -0.05518 0.05220  0.43584  263 ASP   A CB  
2014 C CG  . ASP   A 263 ? 0.99469 1.07573 0.86830 -0.06620 0.05807  0.45800  263 ASP   A CG  
2015 O OD1 . ASP   A 263 ? 1.00321 1.06989 0.90244 -0.07713 0.06069  0.46807  263 ASP   A OD1 
2016 O OD2 . ASP   A 263 ? 1.06642 1.17786 0.91021 -0.06481 0.05941  0.46368  263 ASP   A OD2 
2017 N N   . MET   A 264 ? 0.87465 0.88740 0.78010 -0.03887 0.04925  0.35707  264 MET   A N   
2018 C CA  . MET   A 264 ? 0.85358 0.84135 0.76897 -0.02784 0.04239  0.33044  264 MET   A CA  
2019 C C   . MET   A 264 ? 0.86359 0.81486 0.80532 -0.03275 0.04142  0.32158  264 MET   A C   
2020 O O   . MET   A 264 ? 0.88266 0.80038 0.83736 -0.02482 0.03398  0.31319  264 MET   A O   
2021 C CB  . MET   A 264 ? 0.81327 0.82330 0.70944 -0.02209 0.04791  0.30068  264 MET   A CB  
2022 C CG  . MET   A 264 ? 0.80413 0.79688 0.70685 -0.01063 0.04059  0.27684  264 MET   A CG  
2023 S SD  . MET   A 264 ? 0.86634 0.86401 0.76437 0.00007  0.02690  0.29032  264 MET   A SD  
2024 C CE  . MET   A 264 ? 0.87424 0.82640 0.80622 0.00752  0.02061  0.29880  264 MET   A CE  
2025 N N   . CYS   A 265 ? 0.86903 0.82752 0.81848 -0.04614 0.04897  0.32374  265 CYS   A N   
2026 C CA  . CYS   A 265 ? 0.87529 0.79980 0.84769 -0.05537 0.04523  0.31840  265 CYS   A CA  
2027 C C   . CYS   A 265 ? 0.93362 0.81855 0.91990 -0.05913 0.03622  0.34003  265 CYS   A C   
2028 O O   . CYS   A 265 ? 0.94916 0.79121 0.94768 -0.05926 0.02996  0.32822  265 CYS   A O   
2029 C CB  . CYS   A 265 ? 0.78676 0.73382 0.76853 -0.07126 0.05342  0.32350  265 CYS   A CB  
2030 S SG  . CYS   A 265 ? 0.84747 0.83918 0.81590 -0.06444 0.06692  0.30146  265 CYS   A SG  
2031 N N   . ALA   A 266 ? 0.90980 0.80638 0.89258 -0.06188 0.03588  0.37168  266 ALA   A N   
2032 C CA  . ALA   A 266 ? 0.96092 0.81753 0.95813 -0.06367 0.02744  0.39537  266 ALA   A CA  
2033 C C   . ALA   A 266 ? 1.02590 0.85245 1.02534 -0.04341 0.02027  0.38445  266 ALA   A C   
2034 O O   . ALA   A 266 ? 1.08253 0.85873 1.09713 -0.04143 0.01521  0.38236  266 ALA   A O   
2035 C CB  . ALA   A 266 ? 1.02368 0.90475 1.01528 -0.06975 0.02861  0.43435  266 ALA   A CB  
2036 N N   . SER   A 267 ? 1.00629 0.86285 0.99100 -0.02842 0.02014  0.37735  267 SER   A N   
2037 C CA  . SER   A 267 ? 1.02126 0.85758 1.01253 -0.00859 0.01416  0.36865  267 SER   A CA  
2038 C C   . SER   A 267 ? 1.00314 0.80856 1.00165 -0.00363 0.01591  0.33433  267 SER   A C   
2039 O O   . SER   A 267 ? 1.08204 0.84919 1.09325 0.00896  0.01320  0.32975  267 SER   A O   
2040 C CB  . SER   A 267 ? 1.01057 0.89082 0.98507 0.00225  0.01200  0.36801  267 SER   A CB  
2041 O OG  . SER   A 267 ? 1.03059 0.94052 0.99285 -0.00343 0.00981  0.39955  267 SER   A OG  
2042 N N   . LEU   A 268 ? 0.95851 0.77992 0.94879 -0.01258 0.02126  0.31092  268 LEU   A N   
2043 C CA  . LEU   A 268 ? 0.92424 0.71832 0.91881 -0.01048 0.02220  0.28050  268 LEU   A CA  
2044 C C   . LEU   A 268 ? 0.99838 0.74301 1.00480 -0.02204 0.01933  0.28232  268 LEU   A C   
2045 O O   . LEU   A 268 ? 1.02902 0.73501 1.03815 -0.01555 0.01831  0.26266  268 LEU   A O   
2046 C CB  . LEU   A 268 ? 0.87003 0.69556 0.85452 -0.01723 0.02766  0.25905  268 LEU   A CB  
2047 C CG  . LEU   A 268 ? 0.88980 0.69266 0.87705 -0.01987 0.02789  0.23109  268 LEU   A CG  
2048 C CD1 . LEU   A 268 ? 0.87303 0.65378 0.86036 -0.00202 0.02682  0.21332  268 LEU   A CD1 
2049 C CD2 . LEU   A 268 ? 0.79871 0.63666 0.77920 -0.02562 0.03316  0.21627  268 LEU   A CD2 
2050 N N   . LYS   A 269 ? 1.00670 0.75131 1.01881 -0.04020 0.01821  0.30536  269 LYS   A N   
2051 C CA  . LYS   A 269 ? 1.01545 0.71019 1.03891 -0.05491 0.01333  0.30952  269 LYS   A CA  
2052 C C   . LYS   A 269 ? 1.06626 0.70794 1.09660 -0.04010 0.00989  0.31361  269 LYS   A C   
2053 O O   . LYS   A 269 ? 1.06920 0.66348 1.09932 -0.03745 0.00866  0.29182  269 LYS   A O   
2054 C CB  . LYS   A 269 ? 1.04614 0.75574 1.07766 -0.07675 0.01272  0.34041  269 LYS   A CB  
2055 C CG  . LYS   A 269 ? 1.07304 0.73706 1.11695 -0.09934 0.00616  0.34419  269 LYS   A CG  
2056 C CD  . LYS   A 269 ? 1.03080 0.71985 1.08591 -0.12284 0.00651  0.37674  269 LYS   A CD  
2057 C CE  . LYS   A 269 ? 1.08533 0.73282 1.14998 -0.12911 0.00100  0.40188  269 LYS   A CE  
2058 N NZ  . LYS   A 269 ? 1.01991 0.71283 1.08538 -0.13573 0.00558  0.43003  269 LYS   A NZ  
2059 N N   . GLU   A 270 ? 1.06457 0.71425 1.10012 -0.02911 0.00889  0.34180  270 GLU   A N   
2060 C CA  . GLU   A 270 ? 1.08954 0.69173 1.13634 -0.01167 0.00665  0.35039  270 GLU   A CA  
2061 C C   . GLU   A 270 ? 1.13219 0.72578 1.17689 0.01251  0.01044  0.32228  270 GLU   A C   
2062 O O   . GLU   A 270 ? 1.18088 0.72194 1.23314 0.02557  0.01184  0.31479  270 GLU   A O   
2063 C CB  . GLU   A 270 ? 1.12078 0.74430 1.17461 -0.00406 0.00374  0.38965  270 GLU   A CB  
2064 N N   . LEU   A 271 ? 1.10382 0.74702 1.13835 0.01886  0.01319  0.30663  271 LEU   A N   
2065 C CA  . LEU   A 271 ? 1.07149 0.71165 1.10511 0.03902  0.01738  0.28038  271 LEU   A CA  
2066 C C   . LEU   A 271 ? 1.10119 0.69950 1.12786 0.03334  0.02052  0.24872  271 LEU   A C   
2067 O O   . LEU   A 271 ? 1.14441 0.71015 1.17313 0.05064  0.02520  0.23221  271 LEU   A O   
2068 C CB  . LEU   A 271 ? 0.98734 0.68772 1.01092 0.04230  0.01845  0.27121  271 LEU   A CB  
2069 C CG  . LEU   A 271 ? 0.96188 0.69527 0.99193 0.06154  0.01618  0.28472  271 LEU   A CG  
2070 C CD1 . LEU   A 271 ? 0.95203 0.66567 0.99433 0.08440  0.02035  0.27005  271 LEU   A CD1 
2071 C CD2 . LEU   A 271 ? 1.05594 0.79182 1.09496 0.06294  0.01025  0.32307  271 LEU   A CD2 
2072 N N   . LEU   A 272 ? 1.04940 0.65027 1.06743 0.00932  0.01826  0.24056  272 LEU   A N   
2073 C CA  . LEU   A 272 ? 1.11291 0.67656 1.12151 0.00055  0.01852  0.21183  272 LEU   A CA  
2074 C C   . LEU   A 272 ? 1.18766 0.68058 1.19942 -0.00132 0.01658  0.21311  272 LEU   A C   
2075 O O   . LEU   A 272 ? 1.20931 0.65976 1.21137 0.00583  0.01989  0.18744  272 LEU   A O   
2076 C CB  . LEU   A 272 ? 1.04684 0.63577 1.04968 -0.02546 0.01478  0.20722  272 LEU   A CB  
2077 C CG  . LEU   A 272 ? 1.04991 0.68255 1.04342 -0.02240 0.01829  0.18638  272 LEU   A CG  
2078 C CD1 . LEU   A 272 ? 0.99650 0.67264 0.99188 -0.04151 0.01698  0.19537  272 LEU   A CD1 
2079 C CD2 . LEU   A 272 ? 1.07789 0.68011 1.05932 -0.02188 0.01867  0.15542  272 LEU   A CD2 
2080 N N   . GLN   A 273 ? 1.16222 0.63941 1.18577 -0.01068 0.01194  0.24271  273 GLN   A N   
2081 C CA  . GLN   A 273 ? 1.28129 0.68603 1.30792 -0.01718 0.00889  0.24536  273 GLN   A CA  
2082 C C   . GLN   A 273 ? 1.30446 0.66820 1.34038 0.01246  0.01482  0.25025  273 GLN   A C   
2083 O O   . GLN   A 273 ? 1.24569 0.53885 1.28049 0.01245  0.01509  0.24373  273 GLN   A O   
2084 C CB  . GLN   A 273 ? 1.29292 0.69708 1.33083 -0.04199 0.00128  0.27810  273 GLN   A CB  
2085 C CG  . GLN   A 273 ? 1.28131 0.72960 1.31579 -0.07029 -0.00309 0.27786  273 GLN   A CG  
2086 C CD  . GLN   A 273 ? 1.30793 0.73403 1.35297 -0.10033 -0.01113 0.30132  273 GLN   A CD  
2087 O OE1 . GLN   A 273 ? 1.39578 0.77280 1.43674 -0.11969 -0.01791 0.28744  273 GLN   A OE1 
2088 N NE2 . GLN   A 273 ? 1.22507 0.68758 1.28249 -0.10587 -0.01081 0.33771  273 GLN   A NE2 
2089 N N   . ASN   A 274 ? 1.28707 0.69243 1.33280 0.03750  0.01941  0.26171  274 ASN   A N   
2090 C CA  . ASN   A 274 ? 1.27292 0.64993 1.33452 0.06754  0.02483  0.27313  274 ASN   A CA  
2091 C C   . ASN   A 274 ? 1.25642 0.65949 1.31948 0.09601  0.03387  0.25475  274 ASN   A C   
2092 O O   . ASN   A 274 ? 1.24631 0.62657 1.32527 0.12385  0.04044  0.26152  274 ASN   A O   
2093 C CB  . ASN   A 274 ? 1.27688 0.67987 1.35736 0.07107  0.01916  0.31786  274 ASN   A CB  
2094 C CG  . ASN   A 274 ? 1.34048 0.73731 1.41627 0.04030  0.01028  0.33654  274 ASN   A CG  
2095 O OD1 . ASN   A 274 ? 1.35835 0.80803 1.43500 0.02901  0.00595  0.36072  274 ASN   A OD1 
2096 N ND2 . ASN   A 274 ? 1.34647 0.67955 1.41500 0.02650  0.00826  0.32479  274 ASN   A ND2 
2097 N N   . GLY   A 275 ? 1.22849 0.67908 1.27825 0.09042  0.03487  0.23389  275 GLY   A N   
2098 C CA  . GLY   A 275 ? 1.30517 0.78175 1.35676 0.11383  0.04320  0.21679  275 GLY   A CA  
2099 C C   . GLY   A 275 ? 1.31218 0.84279 1.38344 0.13149  0.04118  0.24299  275 GLY   A C   
2100 O O   . GLY   A 275 ? 1.30101 0.84421 1.38391 0.12939  0.03389  0.27573  275 GLY   A O   
2101 N N   . MET   A 276 ? 1.28835 0.85325 1.36289 0.14791  0.04697  0.22923  276 MET   A N   
2102 C CA  . MET   A 276 ? 1.19045 0.81053 1.28371 0.16287  0.04336  0.25161  276 MET   A CA  
2103 C C   . MET   A 276 ? 1.22857 0.83076 1.35068 0.19293  0.04815  0.27152  276 MET   A C   
2104 O O   . MET   A 276 ? 1.15830 0.80713 1.29987 0.20472  0.04254  0.29618  276 MET   A O   
2105 C CB  . MET   A 276 ? 1.12143 0.78873 1.20929 0.16514  0.04626  0.23118  276 MET   A CB  
2106 C CG  . MET   A 276 ? 1.05967 0.77622 1.13159 0.14257  0.03700  0.23216  276 MET   A CG  
2107 S SD  . MET   A 276 ? 1.17186 0.90061 1.22235 0.13032  0.04220  0.19455  276 MET   A SD  
2108 C CE  . MET   A 276 ? 1.10676 0.77425 1.14039 0.11462  0.04503  0.17786  276 MET   A CE  
2109 N N   . ASN   A 277 ? 1.30902 0.84509 1.43425 0.20559  0.05809  0.26162  277 ASN   A N   
2110 C CA  . ASN   A 277 ? 1.24324 0.75814 1.39555 0.23432  0.06329  0.27829  277 ASN   A CA  
2111 C C   . ASN   A 277 ? 1.21327 0.77874 1.38843 0.26011  0.06943  0.28024  277 ASN   A C   
2112 O O   . ASN   A 277 ? 1.15103 0.74518 1.35218 0.27548  0.06478  0.30433  277 ASN   A O   
2113 C CB  . ASN   A 277 ? 1.24905 0.77127 1.41212 0.22712  0.04927  0.31365  277 ASN   A CB  
2114 C CG  . ASN   A 277 ? 1.37486 0.82622 1.52980 0.21982  0.04854  0.31054  277 ASN   A CG  
2115 O OD1 . ASN   A 277 ? 1.37205 0.77005 1.52235 0.23128  0.05854  0.28577  277 ASN   A OD1 
2116 N ND2 . ASN   A 277 ? 1.44145 0.89245 1.59260 0.19987  0.03652  0.33543  277 ASN   A ND2 
2117 N N   . GLY   A 278 ? 1.14797 0.72949 1.31253 0.26169  0.07860  0.25369  278 GLY   A N   
2118 C CA  . GLY   A 278 ? 1.13086 0.76318 1.31769 0.28317  0.08496  0.25522  278 GLY   A CA  
2119 C C   . GLY   A 278 ? 1.10340 0.81374 1.29928 0.27223  0.06951  0.27579  278 GLY   A C   
2120 O O   . GLY   A 278 ? 1.04872 0.80705 1.26398 0.28549  0.07227  0.27800  278 GLY   A O   
2121 N N   . ARG   A 279 ? 1.11504 0.83970 1.29675 0.24793  0.05371  0.29092  279 ARG   A N   
2122 C CA  . ARG   A 279 ? 1.02751 0.82079 1.20808 0.23403  0.03909  0.30491  279 ARG   A CA  
2123 C C   . ARG   A 279 ? 0.98340 0.79811 1.13797 0.21448  0.04008  0.27336  279 ARG   A C   
2124 O O   . ARG   A 279 ? 0.98822 0.76793 1.12559 0.21033  0.05053  0.24373  279 ARG   A O   
2125 C CB  . ARG   A 279 ? 1.04172 0.84131 1.21240 0.21629  0.02436  0.33167  279 ARG   A CB  
2126 C CG  . ARG   A 279 ? 1.01270 0.81151 1.21263 0.23451  0.01863  0.37217  279 ARG   A CG  
2127 C CD  . ARG   A 279 ? 1.02865 0.76832 1.22111 0.22807  0.01969  0.37915  279 ARG   A CD  
2128 N NE  . ARG   A 279 ? 1.16039 0.90692 1.37107 0.23577  0.01147  0.40781  279 ARG   A NE  
2129 C CZ  . ARG   A 279 ? 1.13345 0.86701 1.37105 0.26042  0.01736  0.41165  279 ARG   A CZ  
2130 N NH1 . ARG   A 279 ? 1.05552 0.76842 1.30371 0.28027  0.03263  0.38729  279 ARG   A NH1 
2131 N NH2 . ARG   A 279 ? 1.02811 0.77081 1.28159 0.26562  0.00869  0.44091  279 ARG   A NH2 
2132 N N   . THR   A 280 ? 0.95383 0.82576 1.10466 0.20195  0.02833  0.28039  280 THR   A N   
2133 C CA  . THR   A 280 ? 0.93665 0.83070 1.06570 0.18435  0.02838  0.25394  280 THR   A CA  
2134 C C   . THR   A 280 ? 0.87853 0.80677 0.98670 0.16089  0.01402  0.26225  280 THR   A C   
2135 O O   . THR   A 280 ? 0.89648 0.85231 1.01154 0.16062  0.00220  0.28984  280 THR   A O   
2136 C CB  . THR   A 280 ? 0.86633 0.79675 1.01443 0.19649  0.03258  0.24718  280 THR   A CB  
2137 O OG1 . THR   A 280 ? 0.81695 0.78848 0.99448 0.20887  0.02336  0.27782  280 THR   A OG1 
2138 C CG2 . THR   A 280 ? 0.91048 0.80512 1.06761 0.21624  0.05127  0.22852  280 THR   A CG2 
2139 N N   . ILE   A 281 ? 0.79866 0.72512 0.88024 0.14194  0.01566  0.23836  281 ILE   A N   
2140 C CA  . ILE   A 281 ? 0.79435 0.74883 0.85185 0.12076  0.00607  0.23989  281 ILE   A CA  
2141 C C   . ILE   A 281 ? 0.79497 0.77822 0.84479 0.11315  0.00550  0.21937  281 ILE   A C   
2142 O O   . ILE   A 281 ? 0.73842 0.70477 0.78327 0.11187  0.01478  0.19524  281 ILE   A O   
2143 C CB  . ILE   A 281 ? 0.80557 0.73144 0.84052 0.10528  0.00963  0.23257  281 ILE   A CB  
2144 C CG1 . ILE   A 281 ? 0.80720 0.70260 0.85086 0.11008  0.00921  0.25520  281 ILE   A CG1 
2145 C CG2 . ILE   A 281 ? 0.75847 0.71455 0.76783 0.08649  0.00355  0.23161  281 ILE   A CG2 
2146 C CD1 . ILE   A 281 ? 0.77529 0.64322 0.80218 0.09370  0.01262  0.25051  281 ILE   A CD1 
2147 N N   . LEU   A 282 ? 0.75516 0.78076 0.80283 0.10666  -0.00637 0.22966  282 LEU   A N   
2148 C CA  . LEU   A 282 ? 0.73091 0.78287 0.77193 0.09719  -0.00900 0.21238  282 LEU   A CA  
2149 C C   . LEU   A 282 ? 0.73925 0.78954 0.80413 0.11068  0.00000  0.20134  282 LEU   A C   
2150 O O   . LEU   A 282 ? 0.71874 0.76854 0.77580 0.10377  0.00510  0.17981  282 LEU   A O   
2151 C CB  . LEU   A 282 ? 0.73293 0.77349 0.74256 0.07960  -0.00525 0.19004  282 LEU   A CB  
2152 C CG  . LEU   A 282 ? 0.74106 0.79742 0.72155 0.06334  -0.01332 0.19464  282 LEU   A CG  
2153 C CD1 . LEU   A 282 ? 0.66832 0.71003 0.62442 0.05141  -0.00507 0.17131  282 LEU   A CD1 
2154 C CD2 . LEU   A 282 ? 0.77072 0.86634 0.74807 0.05616  -0.02773 0.20184  282 LEU   A CD2 
2155 N N   . GLY   A 283 ? 0.73188 0.78076 0.82620 0.13121  0.00335  0.21719  283 GLY   A N   
2156 C CA  . GLY   A 283 ? 0.74384 0.79555 0.86216 0.14707  0.01414  0.20961  283 GLY   A CA  
2157 C C   . GLY   A 283 ? 0.82159 0.82945 0.93080 0.15297  0.03076  0.18611  283 GLY   A C   
2158 O O   . GLY   A 283 ? 0.97063 0.98249 1.09145 0.16261  0.04119  0.17503  283 GLY   A O   
2159 N N   . SER   A 284 ? 0.78680 0.75536 0.87497 0.14611  0.03311  0.17899  284 SER   A N   
2160 C CA  . SER   A 284 ? 0.83909 0.76401 0.91638 0.14930  0.04609  0.15791  284 SER   A CA  
2161 C C   . SER   A 284 ? 0.87745 0.75991 0.95674 0.15772  0.04882  0.16733  284 SER   A C   
2162 O O   . SER   A 284 ? 0.90476 0.78845 0.98282 0.15176  0.03965  0.18634  284 SER   A O   
2163 C CB  . SER   A 284 ? 0.87262 0.79027 0.92208 0.12809  0.04509  0.13790  284 SER   A CB  
2164 O OG  . SER   A 284 ? 0.88414 0.75753 0.92000 0.12583  0.05197  0.12448  284 SER   A OG  
2165 N N   . ALA   A 285 ? 0.86210 0.70560 0.94288 0.17108  0.06164  0.15430  285 ALA   A N   
2166 C CA  . ALA   A 285 ? 0.90653 0.69923 0.98612 0.17699  0.06477  0.15898  285 ALA   A CA  
2167 C C   . ALA   A 285 ? 0.91624 0.67163 0.96801 0.15700  0.06438  0.14068  285 ALA   A C   
2168 O O   . ALA   A 285 ? 0.96349 0.67165 1.01129 0.15726  0.06605  0.14163  285 ALA   A O   
2169 C CB  . ALA   A 285 ? 0.91805 0.68326 1.01379 0.20428  0.07955  0.15498  285 ALA   A CB  
2170 N N   . LEU   A 286 ? 0.91332 0.68907 0.94786 0.13931  0.06152  0.12568  286 LEU   A N   
2171 C CA  . LEU   A 286 ? 0.95116 0.70400 0.96348 0.11868  0.05902  0.11219  286 LEU   A CA  
2172 C C   . LEU   A 286 ? 0.91154 0.69510 0.91789 0.10042  0.04919  0.12295  286 LEU   A C   
2173 O O   . LEU   A 286 ? 0.87180 0.69495 0.88413 0.10153  0.04457  0.13364  286 LEU   A O   
2174 C CB  . LEU   A 286 ? 0.91386 0.66357 0.91103 0.11477  0.06540  0.08591  286 LEU   A CB  
2175 C CG  . LEU   A 286 ? 1.00822 0.72177 1.00025 0.12909  0.07725  0.06887  286 LEU   A CG  
2176 C CD1 . LEU   A 286 ? 0.98352 0.68234 0.95038 0.11433  0.07839  0.04532  286 LEU   A CD1 
2177 C CD2 . LEU   A 286 ? 1.08045 0.74486 1.07591 0.13676  0.07895  0.07557  286 LEU   A CD2 
2178 N N   . LEU   A 287 ? 0.90123 0.66636 0.89506 0.08307  0.04627  0.11990  287 LEU   A N   
2179 C CA  . LEU   A 287 ? 0.83645 0.63017 0.82293 0.06662  0.04072  0.12662  287 LEU   A CA  
2180 C C   . LEU   A 287 ? 0.83857 0.65368 0.81545 0.06004  0.04273  0.10769  287 LEU   A C   
2181 O O   . LEU   A 287 ? 0.83568 0.63252 0.80491 0.05436  0.04513  0.09154  287 LEU   A O   
2182 C CB  . LEU   A 287 ? 0.81021 0.58036 0.79260 0.05119  0.03771  0.13441  287 LEU   A CB  
2183 C CG  . LEU   A 287 ? 0.85870 0.60702 0.85138 0.05610  0.03506  0.15710  287 LEU   A CG  
2184 C CD1 . LEU   A 287 ? 0.89550 0.62235 0.88569 0.03757  0.03165  0.16635  287 LEU   A CD1 
2185 C CD2 . LEU   A 287 ? 0.85432 0.63920 0.85291 0.06289  0.03133  0.17843  287 LEU   A CD2 
2186 N N   . GLU   A 288 ? 0.77329 0.62541 0.74957 0.06022  0.04095  0.11008  288 GLU   A N   
2187 C CA  . GLU   A 288 ? 0.81046 0.68182 0.77962 0.05512  0.04280  0.09447  288 GLU   A CA  
2188 C C   . GLU   A 288 ? 0.76047 0.63983 0.72029 0.04054  0.04230  0.09366  288 GLU   A C   
2189 O O   . GLU   A 288 ? 0.79872 0.68894 0.75569 0.03545  0.04043  0.10699  288 GLU   A O   
2190 C CB  . GLU   A 288 ? 0.82921 0.73245 0.80173 0.06033  0.04047  0.09694  288 GLU   A CB  
2191 C CG  . GLU   A 288 ? 0.86550 0.77093 0.85288 0.07549  0.04187  0.09935  288 GLU   A CG  
2192 C CD  . GLU   A 288 ? 1.13126 1.03539 1.11960 0.07921  0.04824  0.08241  288 GLU   A CD  
2193 O OE1 . GLU   A 288 ? 1.16267 1.03961 1.14500 0.07961  0.05359  0.07149  288 GLU   A OE1 
2194 O OE2 . GLU   A 288 ? 1.29228 1.22267 1.28608 0.08021  0.04732  0.08061  288 GLU   A OE2 
2195 N N   . ASP   A 289 ? 0.72966 0.60684 0.68532 0.03465  0.04466  0.07948  289 ASP   A N   
2196 C CA  . ASP   A 289 ? 0.71171 0.59857 0.66377 0.02297  0.04534  0.08007  289 ASP   A CA  
2197 C C   . ASP   A 289 ? 0.76946 0.67463 0.71837 0.02213  0.04809  0.06872  289 ASP   A C   
2198 O O   . ASP   A 289 ? 0.73526 0.64712 0.68482 0.01498  0.04983  0.06764  289 ASP   A O   
2199 C CB  . ASP   A 289 ? 0.76815 0.63295 0.72194 0.01333  0.04346  0.07940  289 ASP   A CB  
2200 C CG  . ASP   A 289 ? 0.83617 0.68787 0.78596 0.01305  0.04326  0.06333  289 ASP   A CG  
2201 O OD1 . ASP   A 289 ? 0.86468 0.71427 0.81237 0.02360  0.04579  0.05483  289 ASP   A OD1 
2202 O OD2 . ASP   A 289 ? 0.80129 0.64734 0.75014 0.00150  0.04029  0.06067  289 ASP   A OD2 
2203 N N   . GLU   A 290 ? 0.77985 0.69391 0.72795 0.02911  0.04844  0.06207  290 GLU   A N   
2204 C CA  . GLU   A 290 ? 0.70362 0.63115 0.64925 0.02790  0.05066  0.05259  290 GLU   A CA  
2205 C C   . GLU   A 290 ? 0.71652 0.66108 0.65565 0.02812  0.05032  0.05428  290 GLU   A C   
2206 O O   . GLU   A 290 ? 0.70050 0.65277 0.63855 0.02920  0.04943  0.04759  290 GLU   A O   
2207 C CB  . GLU   A 290 ? 0.66842 0.59247 0.61708 0.03237  0.05116  0.04335  290 GLU   A CB  
2208 C CG  . GLU   A 290 ? 0.84224 0.74604 0.79083 0.03325  0.05158  0.03983  290 GLU   A CG  
2209 C CD  . GLU   A 290 ? 1.00072 0.90367 0.94603 0.03069  0.05309  0.03009  290 GLU   A CD  
2210 O OE1 . GLU   A 290 ? 1.02391 0.93980 0.97114 0.03325  0.05491  0.02659  290 GLU   A OE1 
2211 O OE2 . GLU   A 290 ? 0.90490 0.79481 0.84532 0.02458  0.05141  0.02716  290 GLU   A OE2 
2212 N N   . PHE   A 291 ? 0.70978 0.65982 0.64269 0.02557  0.05064  0.06356  291 PHE   A N   
2213 C CA  . PHE   A 291 ? 0.68889 0.65355 0.60827 0.02389  0.05087  0.06377  291 PHE   A CA  
2214 C C   . PHE   A 291 ? 0.67539 0.64491 0.58821 0.02026  0.05786  0.06843  291 PHE   A C   
2215 O O   . PHE   A 291 ? 0.65056 0.62103 0.56377 0.01823  0.05765  0.08191  291 PHE   A O   
2216 C CB  . PHE   A 291 ? 0.73922 0.71172 0.65527 0.02563  0.04366  0.07427  291 PHE   A CB  
2217 C CG  . PHE   A 291 ? 0.72911 0.70489 0.65500 0.03004  0.03782  0.07178  291 PHE   A CG  
2218 C CD1 . PHE   A 291 ? 0.71672 0.70260 0.63781 0.02672  0.03512  0.06237  291 PHE   A CD1 
2219 C CD2 . PHE   A 291 ? 0.69198 0.66065 0.63288 0.03760  0.03574  0.07967  291 PHE   A CD2 
2220 C CE1 . PHE   A 291 ? 0.72912 0.72354 0.66310 0.02956  0.02997  0.06296  291 PHE   A CE1 
2221 C CE2 . PHE   A 291 ? 0.71496 0.69160 0.66813 0.04358  0.03272  0.07921  291 PHE   A CE2 
2222 C CZ  . PHE   A 291 ? 0.72367 0.71616 0.67477 0.03891  0.02956  0.07198  291 PHE   A CZ  
2223 N N   . THR   A 292 ? 0.70282 0.67579 0.61196 0.02015  0.06498  0.05899  292 THR   A N   
2224 C CA  . THR   A 292 ? 0.66349 0.64588 0.56814 0.01917  0.07444  0.06380  292 THR   A CA  
2225 C C   . THR   A 292 ? 0.68662 0.67921 0.56866 0.01820  0.07628  0.06722  292 THR   A C   
2226 O O   . THR   A 292 ? 0.69284 0.68532 0.56111 0.01749  0.06992  0.06140  292 THR   A O   
2227 C CB  . THR   A 292 ? 0.65475 0.63806 0.56261 0.02262  0.08323  0.05330  292 THR   A CB  
2228 O OG1 . THR   A 292 ? 0.74731 0.72606 0.63884 0.02456  0.08393  0.03968  292 THR   A OG1 
2229 C CG2 . THR   A 292 ? 0.64279 0.61907 0.57023 0.02246  0.07980  0.05129  292 THR   A CG2 
2230 N N   . PRO   A 293 ? 0.61748 0.62155 0.49478 0.01689  0.08443  0.07783  293 PRO   A N   
2231 C CA  . PRO   A 293 ? 0.63876 0.65423 0.48840 0.01585  0.08825  0.07967  293 PRO   A CA  
2232 C C   . PRO   A 293 ? 0.72517 0.73622 0.55236 0.01788  0.09129  0.05968  293 PRO   A C   
2233 O O   . PRO   A 293 ? 0.75614 0.77034 0.55839 0.01400  0.08537  0.05697  293 PRO   A O   
2234 C CB  . PRO   A 293 ? 0.67431 0.70452 0.52655 0.01583  0.10175  0.09141  293 PRO   A CB  
2235 C CG  . PRO   A 293 ? 0.63045 0.65662 0.51316 0.01240  0.09749  0.10346  293 PRO   A CG  
2236 C CD  . PRO   A 293 ? 0.64444 0.65412 0.54067 0.01466  0.09006  0.08994  293 PRO   A CD  
2237 N N   . PHE   A 294 ? 0.75348 0.75593 0.58905 0.02289  0.09906  0.04627  294 PHE   A N   
2238 C CA  . PHE   A 294 ? 0.79337 0.78386 0.60930 0.02409  0.10122  0.02630  294 PHE   A CA  
2239 C C   . PHE   A 294 ? 0.82923 0.81236 0.64245 0.01762  0.08472  0.02106  294 PHE   A C   
2240 O O   . PHE   A 294 ? 0.87395 0.85492 0.66098 0.01203  0.07981  0.01194  294 PHE   A O   
2241 C CB  . PHE   A 294 ? 0.81308 0.79388 0.64545 0.03182  0.11159  0.01702  294 PHE   A CB  
2242 C CG  . PHE   A 294 ? 1.06059 1.02542 0.87058 0.03552  0.12031  -0.00290 294 PHE   A CG  
2243 C CD1 . PHE   A 294 ? 1.09399 1.05224 0.86837 0.02905  0.11632  -0.01427 294 PHE   A CD1 
2244 C CD2 . PHE   A 294 ? 1.11373 1.06842 0.93793 0.04511  0.13189  -0.00991 294 PHE   A CD2 
2245 C CE1 . PHE   A 294 ? 1.18436 1.12120 0.93455 0.03098  0.12410  -0.03531 294 PHE   A CE1 
2246 C CE2 . PHE   A 294 ? 1.12592 1.05913 0.92969 0.04970  0.14100  -0.02905 294 PHE   A CE2 
2247 C CZ  . PHE   A 294 ? 1.13153 1.05330 0.89661 0.04210  0.13736  -0.04328 294 PHE   A CZ  
2248 N N   . ASP   A 295 ? 0.75456 0.73552 0.59397 0.01762  0.07606  0.02713  295 ASP   A N   
2249 C CA  . ASP   A 295 ? 0.78053 0.75952 0.62309 0.01308  0.06252  0.02444  295 ASP   A CA  
2250 C C   . ASP   A 295 ? 0.83277 0.82473 0.65966 0.00755  0.05215  0.03291  295 ASP   A C   
2251 O O   . ASP   A 295 ? 0.84957 0.84402 0.66658 0.00096  0.04221  0.02714  295 ASP   A O   
2252 C CB  . ASP   A 295 ? 0.72825 0.70512 0.59921 0.01610  0.05798  0.03138  295 ASP   A CB  
2253 C CG  . ASP   A 295 ? 0.78386 0.75068 0.66921 0.01950  0.06451  0.02422  295 ASP   A CG  
2254 O OD1 . ASP   A 295 ? 0.86848 0.82760 0.74633 0.01979  0.06990  0.01276  295 ASP   A OD1 
2255 O OD2 . ASP   A 295 ? 0.75934 0.72448 0.66247 0.02169  0.06382  0.03034  295 ASP   A OD2 
2256 N N   . VAL   A 296 ? 0.80800 0.80977 0.63432 0.00894  0.05294  0.04889  296 VAL   A N   
2257 C CA  . VAL   A 296 ? 0.75681 0.77309 0.57082 0.00449  0.04195  0.06142  296 VAL   A CA  
2258 C C   . VAL   A 296 ? 0.82746 0.84896 0.60399 -0.00296 0.04149  0.05152  296 VAL   A C   
2259 O O   . VAL   A 296 ? 0.90846 0.93965 0.67264 -0.01056 0.02785  0.05235  296 VAL   A O   
2260 C CB  . VAL   A 296 ? 0.70650 0.72901 0.52841 0.00729  0.04363  0.08277  296 VAL   A CB  
2261 C CG1 . VAL   A 296 ? 0.75407 0.79380 0.55741 0.00261  0.03405  0.09781  296 VAL   A CG1 
2262 C CG2 . VAL   A 296 ? 0.62330 0.63632 0.47759 0.01301  0.04025  0.09119  296 VAL   A CG2 
2263 N N   . VAL   A 297 ? 0.81799 0.83357 0.57558 -0.00101 0.05654  0.04152  297 VAL   A N   
2264 C CA  . VAL   A 297 ? 0.87143 0.88792 0.58669 -0.00704 0.05933  0.02943  297 VAL   A CA  
2265 C C   . VAL   A 297 ? 0.93439 0.93630 0.63730 -0.01431 0.05158  0.00842  297 VAL   A C   
2266 O O   . VAL   A 297 ? 0.94919 0.95637 0.62401 -0.02566 0.03951  0.00405  297 VAL   A O   
2267 C CB  . VAL   A 297 ? 0.82748 0.84047 0.52908 0.00024  0.08122  0.02317  297 VAL   A CB  
2268 C CG1 . VAL   A 297 ? 0.70855 0.72014 0.36063 -0.00479 0.08642  0.00885  297 VAL   A CG1 
2269 C CG2 . VAL   A 297 ? 0.76856 0.79796 0.48611 0.00432  0.08750  0.04641  297 VAL   A CG2 
2270 N N   . ARG   A 298 ? 0.93909 0.92270 0.66215 -0.00951 0.05744  -0.00373 298 ARG   A N   
2271 C CA  . ARG   A 298 ? 0.96256 0.92876 0.67626 -0.01749 0.05084  -0.02256 298 ARG   A CA  
2272 C C   . ARG   A 298 ? 0.96174 0.94150 0.68586 -0.02860 0.02936  -0.01474 298 ARG   A C   
2273 O O   . ARG   A 298 ? 1.00721 0.98079 0.71234 -0.04164 0.01873  -0.02684 298 ARG   A O   
2274 C CB  . ARG   A 298 ? 0.96207 0.90829 0.70027 -0.00936 0.06101  -0.03164 298 ARG   A CB  
2275 C CG  . ARG   A 298 ? 0.98178 0.93536 0.76034 -0.00634 0.05434  -0.01894 298 ARG   A CG  
2276 C CD  . ARG   A 298 ? 1.15501 1.09172 0.95422 0.00142  0.06459  -0.02551 298 ARG   A CD  
2277 N NE  . ARG   A 298 ? 1.17144 1.10966 0.99849 -0.00045 0.05600  -0.02044 298 ARG   A NE  
2278 C CZ  . ARG   A 298 ? 1.04956 0.98977 0.87836 -0.01058 0.04328  -0.02237 298 ARG   A CZ  
2279 N NH1 . ARG   A 298 ? 0.98468 0.92296 0.78832 -0.02212 0.03495  -0.03076 298 ARG   A NH1 
2280 N NH2 . ARG   A 298 ? 0.86929 0.81511 0.72504 -0.01013 0.03874  -0.01542 298 ARG   A NH2 
2281 N N   . GLN   A 299 ? 0.95401 0.95215 0.70843 -0.02388 0.02287  0.00560  299 GLN   A N   
2282 C CA  . GLN   A 299 ? 0.94448 0.96100 0.71329 -0.03135 0.00437  0.01628  299 GLN   A CA  
2283 C C   . GLN   A 299 ? 0.98230 1.01894 0.72415 -0.04126 -0.00873 0.02498  299 GLN   A C   
2284 O O   . GLN   A 299 ? 1.00318 1.05250 0.74119 -0.05398 -0.02565 0.02551  299 GLN   A O   
2285 C CB  . GLN   A 299 ? 0.88430 0.91074 0.69298 -0.02022 0.00423  0.03408  299 GLN   A CB  
2286 C CG  . GLN   A 299 ? 0.82819 0.87995 0.65479 -0.02270 -0.01196 0.05145  299 GLN   A CG  
2287 C CD  . GLN   A 299 ? 0.74700 0.80158 0.61307 -0.01324 -0.01075 0.05867  299 GLN   A CD  
2288 O OE1 . GLN   A 299 ? 0.69557 0.77145 0.58154 -0.01343 -0.02144 0.07116  299 GLN   A OE1 
2289 N NE2 . GLN   A 299 ? 0.76422 0.79956 0.64131 -0.00473 0.00255  0.05152  299 GLN   A NE2 
2290 N N   . CYS   A 300 ? 1.02104 1.06338 0.74394 -0.03717 -0.00201 0.03339  300 CYS   A N   
2291 C CA  . CYS   A 300 ? 1.02015 1.08247 0.71200 -0.04693 -0.01369 0.04291  300 CYS   A CA  
2292 C C   . CYS   A 300 ? 1.09600 1.14559 0.73608 -0.05827 -0.01074 0.02015  300 CYS   A C   
2293 O O   . CYS   A 300 ? 1.05318 1.11774 0.65766 -0.06698 -0.01792 0.02554  300 CYS   A O   
2294 C CB  . CYS   A 300 ? 1.00800 1.08334 0.70334 -0.03805 -0.00788 0.06583  300 CYS   A CB  
2295 S SG  . CYS   A 300 ? 1.00718 1.08877 0.75833 -0.02428 -0.01039 0.09048  300 CYS   A SG  
2296 N N   . SER   A 301 ? 1.08124 1.10196 0.71483 -0.05803 -0.00012 -0.00503 301 SER   A N   
2297 C CA  . SER   A 301 ? 1.01410 1.01394 0.59812 -0.06718 0.00477  -0.03078 301 SER   A CA  
2298 C C   . SER   A 301 ? 1.12457 1.10207 0.70530 -0.07999 -0.00473 -0.05169 301 SER   A C   
2299 O O   . SER   A 301 ? 1.23099 1.18622 0.76713 -0.09034 -0.00355 -0.07513 301 SER   A O   
2300 C CB  . SER   A 301 ? 1.02652 1.00607 0.59940 -0.05222 0.03225  -0.04308 301 SER   A CB  
2301 O OG  . SER   A 301 ? 1.17824 1.17681 0.73291 -0.04698 0.04110  -0.02928 301 SER   A OG  
2302 N N   . GLY   A 302 ? 1.03900 1.01991 0.66339 -0.08010 -0.01314 -0.04443 302 GLY   A N   
2303 C CA  . GLY   A 302 ? 0.97682 0.93770 0.60256 -0.09359 -0.02205 -0.06095 302 GLY   A CA  
2304 C C   . GLY   A 302 ? 1.08588 1.00417 0.70091 -0.08720 -0.00344 -0.08543 302 GLY   A C   
2305 O O   . GLY   A 302 ? 1.05078 0.94116 0.63773 -0.10118 -0.00787 -0.10727 302 GLY   A O   
2306 N N   . VAL   A 303 ? 1.06994 0.98178 0.70763 -0.06677 0.01662  -0.08154 303 VAL   A N   
2307 C CA  . VAL   A 303 ? 1.14045 1.01555 0.77289 -0.05718 0.03563  -0.10085 303 VAL   A CA  
2308 C C   . VAL   A 303 ? 1.16847 1.02447 0.82605 -0.06394 0.02881  -0.10620 303 VAL   A C   
2309 O O   . VAL   A 303 ? 1.16685 1.04147 0.86481 -0.06259 0.02173  -0.08934 303 VAL   A O   
2310 C CB  . VAL   A 303 ? 1.09289 0.97452 0.74795 -0.03503 0.05616  -0.09048 303 VAL   A CB  
2311 C CG1 . VAL   A 303 ? 1.06329 0.91527 0.73471 -0.02368 0.07155  -0.10154 303 VAL   A CG1 
2312 C CG2 . VAL   A 303 ? 1.09895 0.98917 0.72082 -0.02879 0.06878  -0.09136 303 VAL   A CG2 
2313 N N   . THR   A 304 ? 1.14711 0.96419 0.77963 -0.07129 0.03177  -0.12963 304 THR   A N   
2314 C CA  . THR   A 304 ? 1.10004 0.89552 0.75426 -0.08021 0.02488  -0.13397 304 THR   A CA  
2315 C C   . THR   A 304 ? 1.13172 0.88880 0.79266 -0.06459 0.04545  -0.14570 304 THR   A C   
2316 O O   . THR   A 304 ? 1.14682 0.88745 0.83350 -0.06700 0.04348  -0.14400 304 THR   A O   
2317 C CB  . THR   A 304 ? 1.03029 0.80896 0.65467 -0.10749 0.00554  -0.14931 304 THR   A CB  
2318 O OG1 . THR   A 304 ? 1.08561 0.83319 0.65516 -0.11013 0.01332  -0.17471 304 THR   A OG1 
2319 C CG2 . THR   A 304 ? 0.96002 0.78368 0.59092 -0.12346 -0.01800 -0.13163 304 THR   A CG2 
2320 C C13 . A1ALH B .   ? 0.83894 0.85109 0.62363 -0.01789 0.06464  0.04262  401 A1ALH A C13 
2321 C C17 . A1ALH B .   ? 0.84179 0.86173 0.59120 -0.01729 0.07647  0.03758  401 A1ALH A C17 
2322 C C22 . A1ALH B .   ? 0.86540 0.84447 0.51517 -0.06838 0.01857  0.00931  401 A1ALH A C22 
2323 C C24 . A1ALH B .   ? 0.92623 0.84866 0.50969 -0.06527 0.03402  -0.03935 401 A1ALH A C24 
2324 C C26 . A1ALH B .   ? 0.94618 0.81887 0.44893 -0.09684 0.01159  -0.07429 401 A1ALH A C26 
2325 C C28 . A1ALH B .   ? 1.02464 0.81000 0.47679 -0.09093 0.02648  -0.12693 401 A1ALH A C28 
2326 C C02 . A1ALH B .   ? 0.84020 0.84447 0.53588 -0.06000 0.02087  0.03416  401 A1ALH A C02 
2327 C C04 . A1ALH B .   ? 0.77736 0.82733 0.52530 -0.06003 0.01117  0.08367  401 A1ALH A C04 
2328 C C05 . A1ALH B .   ? 0.76655 0.84379 0.50851 -0.06952 -0.00030 0.10972  401 A1ALH A C05 
2329 C C06 . A1ALH B .   ? 0.83541 0.92620 0.59553 -0.07865 -0.02138 0.12586  401 A1ALH A C06 
2330 C C07 . A1ALH B .   ? 0.85331 0.97317 0.60534 -0.08830 -0.03453 0.15328  401 A1ALH A C07 
2331 C C08 . A1ALH B .   ? 0.82175 0.91006 0.63422 -0.06759 -0.02042 0.13470  401 A1ALH A C08 
2332 C C09 . A1ALH B .   ? 0.75219 0.79938 0.50958 -0.04686 0.03140  0.08018  401 A1ALH A C09 
2333 C C11 . A1ALH B .   ? 0.75334 0.79859 0.56470 -0.02773 0.05319  0.08503  401 A1ALH A C11 
2334 C C12 . A1ALH B .   ? 0.76205 0.78972 0.58021 -0.01826 0.06203  0.06441  401 A1ALH A C12 
2335 C C14 . A1ALH B .   ? 0.83495 0.83116 0.63240 -0.00655 0.07376  0.02746  401 A1ALH A C14 
2336 C C16 . A1ALH B .   ? 0.87248 0.88732 0.62765 -0.00293 0.09466  0.02502  401 A1ALH A C16 
2337 C C19 . A1ALH B .   ? 0.70607 0.75857 0.55359 -0.02599 0.05259  0.10548  401 A1ALH A C19 
2338 C C23 . A1ALH B .   ? 0.88340 0.83671 0.51077 -0.05803 0.03555  -0.01460 401 A1ALH A C23 
2339 C C25 . A1ALH B .   ? 0.95964 0.87432 0.51426 -0.08713 0.01329  -0.04381 401 A1ALH A C25 
2340 C C27 . A1ALH B .   ? 0.97284 0.80486 0.47130 -0.08371 0.02642  -0.09770 401 A1ALH A C27 
2341 C C29 . A1ALH B .   ? 1.00783 0.78481 0.40873 -0.11589 0.00914  -0.13677 401 A1ALH A C29 
2342 C C31 . A1ALH B .   ? 1.16644 0.86211 0.52746 -0.14174 -0.00976 -0.17361 401 A1ALH A C31 
2343 C C32 . A1ALH B .   ? 1.01995 0.84214 0.42382 -0.13062 -0.00753 -0.11264 401 A1ALH A C32 
2344 C C33 . A1ALH B .   ? 0.94170 0.80919 0.39596 -0.12030 -0.00573 -0.08197 401 A1ALH A C33 
2345 C C35 . A1ALH B .   ? 1.02818 0.78642 0.51809 -0.04696 0.06515  -0.13939 401 A1ALH A C35 
2346 C C36 . A1ALH B .   ? 0.92093 0.86901 0.50202 -0.09830 -0.00512 -0.01688 401 A1ALH A C36 
2347 C C37 . A1ALH B .   ? 0.86777 0.84539 0.49425 -0.08784 -0.00157 0.00823  401 A1ALH A C37 
2348 N N03 . A1ALH B .   ? 0.87785 0.90989 0.58294 -0.06763 0.00946  0.05961  401 A1ALH A N03 
2349 N N10 . A1ALH B .   ? 0.73932 0.78382 0.53861 -0.03697 0.03693  0.08649  401 A1ALH A N10 
2350 N N15 . A1ALH B .   ? 0.87877 0.87733 0.66065 0.00183  0.08974  0.01884  401 A1ALH A N15 
2351 N N20 . A1ALH B .   ? 0.73657 0.79910 0.59289 -0.02576 0.06014  0.11751  401 A1ALH A N20 
2352 O O01 . A1ALH B .   ? 0.77327 0.77194 0.49833 -0.04695 0.03176  0.03259  401 A1ALH A O01 
2353 O O18 . A1ALH B .   ? 0.75510 0.74046 0.57320 -0.00417 0.06902  0.02461  401 A1ALH A O18 
2354 O O21 . A1ALH B .   ? 0.86065 0.90889 0.58874 -0.04568 0.04252  0.07177  401 A1ALH A O21 
2355 O O30 . A1ALH B .   ? 1.08003 0.80687 0.43049 -0.12598 0.00760  -0.16735 401 A1ALH A O30 
2356 O O34 . A1ALH B .   ? 1.04942 0.79504 0.50452 -0.07446 0.04252  -0.14599 401 A1ALH A O34 
2357 O O   . HOH   C .   ? 1.09652 1.03925 0.87729 -0.04767 0.01123  -0.03894 501 HOH   A O   
2358 O O   . HOH   C .   ? 0.80941 0.74300 0.67017 -0.02678 0.02774  -0.02573 502 HOH   A O   
2359 O O   . HOH   C .   ? 1.06969 0.77825 0.75968 -0.14644 -0.04920 -0.07347 503 HOH   A O   
2360 O O   . HOH   C .   ? 0.77924 0.44278 0.74231 0.02258  0.03538  0.10248  504 HOH   A O   
2361 O O   . HOH   C .   ? 0.64253 0.61051 0.74043 0.08076  0.09598  0.09591  505 HOH   A O   
2362 O O   . HOH   C .   ? 0.69542 0.76667 0.67297 0.02378  0.10778  0.05835  506 HOH   A O   
2363 O O   . HOH   C .   ? 0.92646 0.72583 0.69098 -0.03994 0.05153  -0.10086 507 HOH   A O   
2364 O O   . HOH   C .   ? 0.67928 0.96779 0.84514 -0.10199 0.14578  0.34216  508 HOH   A O   
2365 O O   . HOH   C .   ? 0.91000 1.06518 0.74579 -0.08475 0.07644  0.50010  509 HOH   A O   
2366 O O   . HOH   C .   ? 0.92726 0.95376 0.55887 -0.04714 0.06070  0.02960  510 HOH   A O   
2367 O O   . HOH   C .   ? 0.62380 0.78463 0.66564 0.05963  -0.03606 0.18557  511 HOH   A O   
2368 O O   . HOH   C .   ? 0.54901 0.81930 0.92541 0.10949  0.03087  0.33197  512 HOH   A O   
2369 O O   . HOH   C .   ? 0.54640 0.71283 0.70301 -0.02551 0.01595  0.17042  513 HOH   A O   
2370 O O   . HOH   C .   ? 0.79120 0.69857 1.15831 0.16670  0.06337  0.39928  514 HOH   A O   
2371 O O   . HOH   C .   ? 1.01467 0.64895 0.50505 -0.01814 0.08812  -0.18586 515 HOH   A O   
2372 O O   . HOH   C .   ? 0.56343 0.69405 0.70094 0.00205  0.05052  0.14624  516 HOH   A O   
2373 O O   . HOH   C .   ? 0.83275 1.12184 1.00694 -0.04426 0.15340  0.27146  517 HOH   A O   
2374 O O   . HOH   C .   ? 0.82981 0.98629 0.86465 -0.08293 -0.00096 0.54547  518 HOH   A O   
2375 O O   . HOH   C .   ? 0.74357 0.75612 0.77050 -0.03764 0.06108  0.12941  519 HOH   A O   
2376 O O   . HOH   C .   ? 0.48071 0.72203 0.74081 0.03307  0.03125  0.23171  520 HOH   A O   
2377 O O   . HOH   C .   ? 0.83100 0.76426 1.25962 0.18861  0.05860  0.45058  521 HOH   A O   
2378 O O   . HOH   C .   ? 0.65346 0.94371 0.60362 -0.14789 -0.16551 0.26835  522 HOH   A O   
# 
